data_9BMS
# 
_entry.id   9BMS 
# 
_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   9BMS         pdb_00009bms 10.2210/pdb9bms/pdb 
WWPDB D_1000283536 ?            ?                   
EMDB  EMD-44709    ?            ?                   
# 
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                        9BMS 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-2 of motor domain from full-length human dynein-1 in 5 mM ADP' 
_pdbx_database_related.db_id          EMD-44709 
_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                   9BMS 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BMS 
_struct.title                        'State-2 of motor domain from full-length human 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        9BMS 
_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              9BMS 
_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 ? TYR A 1473 ? MET A 1457 TYR A 1473 1 ? 17 
HELX_P HELX_P2   AA2 GLY A 1489 ? SER A 1510 ? GLY A 1489 SER A 1510 1 ? 22 
HELX_P HELX_P3   AA3 TYR A 1512 ? SER A 1554 ? TYR A 1512 SER A 1554 1 ? 43 
HELX_P HELX_P4   AA4 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P5   AA5 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P6   AA6 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P7   AA7 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P8   AA8 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P9   AA9 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P10  AB1 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P11  AB2 ASN A 1646 ? GLN A 1651 ? ASN A 1646 GLN A 1651 5 ? 6  
HELX_P HELX_P12  AB3 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P13  AB4 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P14  AB5 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P15  AB6 GLN A 1746 ? GLY A 1770 ? GLN A 1746 GLY A 1770 1 ? 25 
HELX_P HELX_P16  AB7 PRO A 1777 ? LEU A 1797 ? PRO A 1777 LEU A 1797 1 ? 21 
HELX_P HELX_P17  AB8 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P18  AB9 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P19  AC1 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P20  AC2 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P21  AC3 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P22  AC4 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P23  AC5 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P24  AC6 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P25  AC7 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P26  AC8 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P27  AC9 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P28  AD1 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P29  AD2 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P30  AD3 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P31  AD4 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P32  AD5 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P33  AD6 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P34  AD7 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P35  AD8 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P36  AD9 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P37  AE1 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P38  AE2 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P39  AE3 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P40  AE4 ASN A 2314 ? ASN A 2316 ? ASN A 2314 ASN A 2316 5 ? 3  
HELX_P HELX_P41  AE5 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P42  AE6 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P43  AE7 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P44  AE8 GLY A 2431 ? PHE A 2441 ? GLY A 2431 PHE A 2441 1 ? 11 
HELX_P HELX_P45  AE9 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P46  AF1 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P47  AF2 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P48  AF3 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P49  AF4 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P50  AF5 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P51  AF6 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P52  AF7 GLY A 2600 ? ARG A 2610 ? GLY A 2600 ARG A 2610 1 ? 11 
HELX_P HELX_P53  AF8 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P54  AF9 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P55  AG1 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P56  AG2 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P57  AG3 ARG A 2757 ? THR A 2764 ? ARG A 2757 THR A 2764 5 ? 8  
HELX_P HELX_P58  AG4 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P59  AG5 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P60  AG6 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P61  AG7 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P62  AG8 ASP A 2862 ? MET A 2867 ? ASP A 2862 MET A 2867 1 ? 6  
HELX_P HELX_P63  AG9 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P64  AH1 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P65  AH2 GLY A 2942 ? GLY A 2955 ? GLY A 2942 GLY A 2955 1 ? 14 
HELX_P HELX_P66  AH3 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P67  AH4 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P68  AH5 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P69  AH6 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P70  AH7 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P71  AH8 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P72  AH9 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P73  AI1 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P74  AI2 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P75  AI3 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P76  AI4 GLU A 3450 ? ALA A 3517 ? GLU A 3450 ALA A 3517 1 ? 68 
HELX_P HELX_P77  AI5 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P78  AI6 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P79  AI7 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P80  AI8 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P81  AI9 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P82  AJ1 LYS A 3605 ? LYS A 3608 ? LYS A 3605 LYS A 3608 5 ? 4  
HELX_P HELX_P83  AJ2 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P84  AJ3 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P85  AJ4 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P86  AJ5 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P87  AJ6 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P88  AJ7 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P89  AJ8 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P90  AJ9 ASP A 3763 ? LEU A 3818 ? ASP A 3763 LEU A 3818 1 ? 56 
HELX_P HELX_P91  AK1 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P92  AK2 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P93  AK3 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P94  AK4 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P95  AK5 LEU A 3876 ? GLY A 3894 ? LEU A 3876 GLY A 3894 1 ? 19 
HELX_P HELX_P96  AK6 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P97  AK7 ASN A 3912 ? ILE A 3914 ? ASN A 3912 ILE A 3914 5 ? 3  
HELX_P HELX_P98  AK8 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P99  AK9 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P100 AL1 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P101 AL2 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P102 AL3 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P103 AL4 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P104 AL5 ARG A 4000 ? LEU A 4013 ? ARG A 4000 LEU A 4013 1 ? 14 
HELX_P HELX_P105 AL6 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P106 AL7 ASP A 4026 ? THR A 4033 ? ASP A 4026 THR A 4033 1 ? 8  
HELX_P HELX_P107 AL8 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P108 AL9 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P109 AM1 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P110 AM2 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P111 AM3 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P112 AM4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P113 AM5 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P114 AM6 ASN A 4174 ? LEU A 4194 ? ASN A 4174 LEU A 4194 1 ? 21 
HELX_P HELX_P115 AM7 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P116 AM8 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P117 AM9 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P118 AN1 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P119 AN2 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P120 AN3 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P121 AN4 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P122 AN5 GLU A 4328 ? MET A 4346 ? GLU A 4328 MET A 4346 1 ? 19 
HELX_P HELX_P123 AN6 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P124 AN7 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P125 AN8 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P126 AN9 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P127 AO1 GLY A 4500 ? ILE A 4507 ? GLY A 4500 ILE A 4507 1 ? 8  
HELX_P HELX_P128 AO2 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P129 AO3 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P130 AO4 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 GLU 2344 OE2 ? ? ? 1_555 G MG . MG ? ? A GLU 2344 A MG 4706 1_555 ? ? ? ? ? ? ? 1.918 ? ? 
metalc2 metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG . MG ? ? A ADP 4701 A MG 4705 1_555 ? ? ? ? ? ? ? 1.762 ? ? 
metalc3 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.615 ? ? 
metalc4 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
# 
_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 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 87.8 ? 
2 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 95.6 ? 
3 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP . ? A ATP 4702 ? 1_555 63.4 ? 
# 
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 ? 7 ? 
# 
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 
AC2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 1476 ? TYR A 1480 ? ASP A 1476 TYR A 1480 
AA1 2 CYS A 1484 ? ARG A 1488 ? CYS A 1484 ARG A 1488 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA5 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA5 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2253 ? GLY A 2249 ILE A 2253 
AA7 2 ARG A 2298 ? VAL A 2302 ? ARG A 2298 VAL A 2302 
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 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB6 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB7 1 ARG A 3654 ? THR A 3656 ? ARG A 3654 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 ALA A 4568 ? ASN A 4571 ? ALA A 4568 ASN A 4571 
AC2 2 LYS A 4574 ? LEU A 4577 ? LYS A 4574 LEU A 4577 
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 ? GLN A 4566 ? LYS A 4564 GLN A 4566 
AC2 7 THR A 4583 ? ALA A 4584 ? THR A 4583 ALA A 4584 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 1476 ? N ASP A 1476 O ARG A 1488 ? O ARG A 1488 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA5 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N VAL A 2250 ? N VAL A 2250 O TRP A 2300 ? O TRP A 2300 
AA7 2 3 N ILE A 2301 ? N ILE A 2301 O MET A 2342 ? O MET A 2342 
AA7 3 4 O ILE A 2341 ? O ILE A 2341 N LEU A 2220 ? N LEU A 2220 
AA7 4 5 N MET A 2221 ? N MET A 2221 O VAL A 2362 ? O VAL A 2362 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N VAL A 2618 ? N VAL A 2618 O VAL A 2660 ? O VAL A 2660 
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 ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB3 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O THR A 2699 ? O THR A 2699 N ARG A 2694 ? N ARG A 2694 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N TYR A 2959 ? N TYR A 2959 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N MET A 2994 ? N MET A 2994 O VAL A 3065 ? O VAL A 3065 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 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 SER A 3680 ? O SER A 3680 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N ILE A 3590 ? N ILE A 3590 O VAL A 3699 ? O VAL A 3699 
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 PHE A 4125 ? O PHE A 4125 
AB8 3 4 O LEU A 4126 ? O LEU A 4126 N VAL A 4041 ? N VAL A 4041 
AB8 4 5 N LEU A 4042 ? N LEU A 4042 O PHE A 4145 ? O PHE A 4145 
AB9 1 2 N LEU A 4284 ? N LEU A 4284 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AC1 3 4 O VAL A 4593 ? O VAL A 4593 N CYS A 4540 ? N CYS A 4540 
AC2 1 2 N ASN A 4571 ? N ASN A 4571 O LYS A 4574 ? O LYS A 4574 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O PHE A 4624 ? O PHE A 4624 N VAL A 4605 ? N VAL A 4605 
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 
AC2 6 7 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
# 
_pdbx_entry_details.entry_id                   9BMS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 2231 ? ? MG  A MG  4706 ? ? 1.33 
2 1 OG1 A THR 1913 ? ? MG  A MG  4705 ? ? 1.42 
3 1 OD1 A ASP 1958 ? ? OG1 A THR 2017 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 1614 ? ? -96.81  32.96   
2  1 ASN A 1643 ? ? -95.07  32.43   
3  1 ALA A 1862 ? ? 58.32   -121.21 
4  1 PRO A 1907 ? ? -61.66  -172.59 
5  1 THR A 2061 ? ? -103.30 40.20   
6  1 ASP A 2320 ? ? -97.21  -137.91 
7  1 ASP A 2505 ? ? -97.64  32.61   
8  1 SER A 3640 ? ? -108.93 41.00   
9  1 LYS A 4171 ? ? -101.53 -169.97 
10 1 ASN A 4597 ? ? 38.44   48.88   
11 1 GLU A 4599 ? ? 60.99   -142.09 
12 1 PHE A 4620 ? ? -162.43 -165.49 
13 1 THR A 4628 ? ? 54.89   -135.86 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 2091 ? ? 0.079 'SIDE CHAIN' 
2 1 ARG A 2358 ? ? 0.085 'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMS 
_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                    9BMS 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.04 
_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               38237 
_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-2 of motor domain from full-length human dynein-1 in 5 mM 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                        9BMS 
_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              9BMS 
_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                9BMS 
_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           9BMS 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-2 of motor domain from full-length human dynein-1 in 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                    9BMS 
_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 ? 144.931 234.177 162.391 1.00 63.24 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 143.539 233.751 162.476 1.00 65.95 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 143.209 232.718 161.406 1.00 66.19 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 142.046 232.356 161.223 1.00 63.31 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 142.600 234.952 162.352 1.00 64.69 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 142.782 236.003 163.436 1.00 64.38 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 141.802 235.665 164.912 1.00 69.47 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 143.033 234.920 165.979 1.00 64.83 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 144.239 232.245 160.699 1.00 61.10 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 144.027 231.238 159.664 1.00 59.51 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 143.475 229.944 160.248 1.00 60.78 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 142.753 229.209 159.562 1.00 60.58 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 145.332 230.970 158.913 1.00 57.71 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 143.803 229.650 161.508 1.00 59.97 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 143.236 228.481 162.168 1.00 60.38 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 141.719 228.582 162.247 1.00 62.10 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 141.007 227.610 161.968 1.00 61.61 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 143.831 228.329 163.569 1.00 59.80 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 145.251 227.779 163.692 1.00 60.63 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 146.288 228.869 163.462 1.00 59.55 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 145.441 227.147 165.056 1.00 59.69 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 141.207 229.758 162.620 1.00 63.02 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 139.763 229.960 162.673 1.00 62.59 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 139.138 229.830 161.290 1.00 63.14 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 138.058 229.247 161.141 1.00 62.39 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 139.454 231.329 163.278 1.00 61.76 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 137.974 231.629 163.426 1.00 63.29 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 137.716 233.049 163.888 1.00 64.59 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 138.028 233.988 163.126 1.00 63.38 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 137.205 233.227 165.014 1.00 64.00 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 139.805 230.369 160.265 1.00 64.18 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 139.281 230.263 158.906 1.00 63.81 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 139.182 228.808 158.469 1.00 63.82 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 138.173 228.393 157.887 1.00 64.11 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 140.161 231.052 157.935 1.00 63.89 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 140.543 232.453 158.399 1.00 64.28 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 139.409 233.177 159.097 1.00 66.87 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 138.346 233.373 158.469 1.00 66.46 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 139.581 233.555 160.275 1.00 65.35 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 140.215 228.010 158.752 1.00 62.29 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 140.181 226.605 158.359 1.00 61.66 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 139.161 225.819 159.174 1.00 61.62 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 138.527 224.892 158.655 1.00 60.74 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 141.564 225.983 158.506 1.00 59.99 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 142.478 226.232 157.341 1.00 63.27 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 142.800 227.522 156.952 1.00 62.96 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 143.030 225.172 156.643 1.00 62.07 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 143.648 227.748 155.885 1.00 61.33 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 143.878 225.391 155.573 1.00 61.42 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 144.187 226.680 155.194 1.00 61.13 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 139.000 226.157 160.458 1.00 56.94 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 137.964 225.505 161.253 1.00 56.79 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 136.582 225.807 160.691 1.00 57.03 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 135.723 224.921 160.624 1.00 57.52 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 138.059 225.941 162.716 1.00 57.22 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 139.258 225.441 163.524 1.00 57.99 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 138.938 225.435 165.011 1.00 55.87 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 139.699 224.059 163.061 1.00 56.21 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 136.353 227.052 160.273 1.00 55.67 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 135.085 227.396 159.635 1.00 57.19 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 134.916 226.658 158.312 1.00 57.96 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 133.806 226.242 157.965 1.00 56.68 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 134.991 228.907 159.428 1.00 57.83 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 133.614 229.383 158.994 1.00 56.70 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 132.523 228.768 159.859 1.00 57.53 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 131.141 229.098 159.320 1.00 57.79 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 130.071 228.351 160.038 1.00 57.49 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 136.007 226.495 157.557 1.00 56.75 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 135.945 225.724 156.318 1.00 57.72 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 135.513 224.289 156.589 1.00 57.13 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 134.632 223.751 155.909 1.00 55.19 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 137.305 225.741 155.617 1.00 55.50 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 137.710 227.082 155.045 1.00 56.55 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 139.196 227.155 154.748 1.00 57.36 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 139.890 228.058 155.212 1.00 58.06 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 139.691 226.195 153.975 1.00 56.23 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 136.128 223.656 157.590 1.00 53.25 ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 135.779 222.284 157.946 1.00 52.13 ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 134.325 222.207 158.395 1.00 52.88 ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 133.590 221.279 158.029 1.00 53.43 ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 136.739 221.756 159.029 1.00 51.67 ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 138.146 221.572 158.456 1.00 51.59 ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 136.222 220.457 159.626 1.00 50.31 ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 139.234 221.548 159.505 1.00 50.49 ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 133.893 223.180 159.198 1.00 54.73 ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 132.513 223.205 159.670 1.00 55.57 ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 131.538 223.300 158.503 1.00 56.00 ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 130.533 222.585 158.461 1.00 54.07 ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 132.321 224.371 160.639 1.00 55.45 ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 130.888 224.592 161.092 1.00 55.70 ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 130.712 225.620 162.233 1.00 53.98 ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 131.585 225.440 163.393 1.00 55.89 ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 132.848 225.840 163.483 1.00 56.61 ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 133.421 226.550 162.524 1.00 54.60 ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 133.544 225.547 164.578 1.00 56.12 ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 131.831 224.172 157.537 1.00 55.66 ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 130.954 224.311 156.378 1.00 56.44 ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 130.940 223.044 155.532 1.00 56.15 ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 129.880 222.619 155.054 1.00 54.15 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 131.378 225.515 155.536 1.00 55.69 ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 131.051 226.853 156.175 1.00 58.31 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 129.566 227.171 156.143 1.00 59.17 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 128.818 226.467 155.431 1.00 58.23 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 129.146 228.122 156.833 1.00 57.79 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 132.107 222.422 155.335 1.00 54.10 ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 132.169 221.197 154.542 1.00 53.63 ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 131.334 220.102 155.188 1.00 51.00 ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 130.570 219.400 154.514 1.00 51.72 ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 133.627 220.751 154.337 1.00 51.83 ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 133.671 219.419 153.608 1.00 49.58 ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 134.384 221.788 153.532 1.00 52.45 ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 131.453 219.945 156.507 1.00 48.32 ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 130.693 218.889 157.165 1.00 48.92 ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 129.213 219.228 157.286 1.00 49.78 ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 128.377 218.319 157.327 1.00 50.32 ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 131.289 218.583 158.532 1.00 47.19 ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 132.553 217.798 158.459 1.00 50.00 ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 133.759 218.137 158.992 1.00 51.55 ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 132.738 216.530 157.818 1.00 49.18 ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 134.685 217.159 158.723 1.00 48.72 ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 134.083 216.163 158.003 1.00 48.19 ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 131.896 215.671 157.106 1.00 49.37 ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 134.606 214.976 157.501 1.00 49.79 ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 132.417 214.494 156.608 1.00 47.75 ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 133.758 214.157 156.807 1.00 48.64 ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 128.863 220.514 157.347 1.00 53.61 ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 127.452 220.883 157.340 1.00 53.96 ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 126.834 220.685 155.963 1.00 52.73 ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 125.623 220.465 155.856 1.00 52.38 ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 127.280 222.331 157.799 1.00 54.75 ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 127.642 222.526 159.261 1.00 55.08 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 128.110 221.600 159.924 1.00 54.41 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 127.432 223.735 159.765 1.00 53.74 ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 127.641 220.759 154.904 1.00 50.46 ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 127.147 220.541 153.551 1.00 51.64 ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 127.367 219.122 153.046 1.00 50.68 ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 126.758 218.740 152.040 1.00 50.06 ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 127.807 221.523 152.575 1.00 51.80 ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 129.234 221.413 152.671 1.00 51.34 ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 127.391 222.950 152.893 1.00 50.54 ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 128.209 218.335 153.710 1.00 49.05 ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 128.487 216.979 153.254 1.00 47.43 ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 127.296 216.072 153.533 1.00 50.22 ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 126.755 216.058 154.643 1.00 49.74 ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 129.738 216.431 153.937 1.00 45.52 ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 130.434 215.331 153.166 1.00 46.25 ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 129.868 214.069 153.055 1.00 47.45 ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 131.657 215.556 152.550 1.00 47.96 ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 130.499 213.062 152.351 1.00 48.08 ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 132.297 214.554 151.844 1.00 47.97 ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 131.713 213.310 151.748 1.00 47.81 ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 132.342 212.307 151.047 1.00 45.13 ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 126.890 215.308 152.520 1.00 50.62 ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 125.812 214.343 152.645 1.00 47.90 ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 126.276 212.994 152.115 1.00 47.26 ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 127.103 212.920 151.202 1.00 45.26 ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 124.554 214.793 151.890 1.00 45.76 ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 123.747 215.861 152.608 1.00 47.91 ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 122.425 216.145 151.924 1.00 49.81 ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 122.192 215.594 150.828 1.00 48.66 ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 121.618 216.916 152.483 1.00 49.12 ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 125.737 211.929 152.701 1.00 43.80 ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 126.080 210.580 152.272 1.00 41.31 ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 125.509 210.323 150.884 1.00 41.86 ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 124.299 210.446 150.671 1.00 42.88 ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 125.548 209.559 153.272 1.00 39.35 ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 126.332 209.411 154.574 1.00 38.96 ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 125.535 208.610 155.589 1.00 40.55 ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 127.683 208.764 154.320 1.00 39.52 ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 126.377 209.970 149.939 1.00 37.25 ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 125.933 209.678 148.582 1.00 38.56 ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 125.225 208.332 148.558 1.00 38.07 ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 125.849 207.289 148.774 1.00 38.80 ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 127.120 209.685 147.624 1.00 39.23 ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 126.699 209.836 146.175 1.00 40.94 ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 125.512 210.135 145.927 1.00 40.95 ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 127.554 209.657 145.285 1.00 39.45 ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 123.923 208.352 148.293 1.00 35.46 ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 123.091 207.159 148.334 1.00 37.92 ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 122.673 206.766 146.925 1.00 40.28 ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 122.338 207.625 146.103 1.00 40.42 ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 121.848 207.381 149.203 1.00 36.23 ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 122.081 207.746 150.669 1.00 38.14 ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 120.791 207.625 151.461 1.00 40.01 ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 123.160 206.868 151.275 1.00 38.40 ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 122.697 205.465 146.652 1.00 39.58 ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 122.255 204.915 145.376 1.00 38.36 ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 121.318 203.747 145.654 1.00 39.67 ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 121.550 202.957 146.575 1.00 42.24 ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 123.448 204.489 144.492 1.00 37.64 ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 124.180 203.292 145.086 1.00 36.49 ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 122.979 204.187 143.075 1.00 38.67 ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 120.241 203.659 144.879 1.00 40.36 ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 119.249 202.617 145.103 1.00 42.20 ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 119.834 201.232 144.836 1.00 41.59 ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 120.735 201.058 144.011 1.00 39.94 ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 118.006 202.860 144.241 1.00 41.16 ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 118.231 202.554 142.769 1.00 44.09 ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 119.359 202.573 142.277 1.00 41.69 ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 117.148 202.266 142.059 1.00 43.21 ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 119.328 200.244 145.571 1.00 38.07 ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 119.796 198.861 145.470 1.00 38.07 ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 118.584 197.966 145.225 1.00 40.76 ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 117.979 197.458 146.173 1.00 39.71 ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 120.562 198.454 146.724 1.00 36.68 ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 120.976 196.999 146.759 1.00 36.90 ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 121.981 196.523 145.929 1.00 32.34 ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 120.366 196.106 147.628 1.00 38.43 ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 122.362 195.196 145.961 1.00 33.00 ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 120.741 194.778 147.667 1.00 39.03 ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 121.740 194.328 146.832 1.00 38.01 ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 122.115 193.005 146.869 1.00 37.14 ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 118.234 197.790 143.950 1.00 41.87 ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 117.159 196.885 143.535 1.00 42.21 ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 115.838 197.229 144.217 1.00 43.27 ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 115.053 196.345 144.568 1.00 43.13 ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 117.541 195.426 143.793 1.00 42.53 ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 118.908 195.042 143.251 1.00 41.44 ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 119.370 193.685 143.740 1.00 42.20 ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 118.671 193.017 144.501 1.00 41.49 ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 120.555 193.273 143.308 1.00 41.90 ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 115.593 198.528 144.408 1.00 42.81 ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 114.359 199.032 145.012 1.00 44.67 ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 114.137 198.472 146.415 1.00 43.58 ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 113.000 198.382 146.888 1.00 41.91 ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 113.145 198.744 144.123 1.00 43.88 ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 113.403 199.071 142.666 1.00 45.17 ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 113.994 200.100 142.344 1.00 44.24 ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 112.957 198.193 141.775 1.00 44.67 ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 115.216 198.089 147.094 1.00 42.03 ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 115.145 197.590 148.461 1.00 41.30 ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 115.578 198.628 149.487 1.00 42.14 ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 114.992 198.703 150.571 1.00 42.84 ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 116.008 196.335 148.614 1.00 39.32 ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 115.624 195.200 147.679 1.00 40.42 ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 116.761 194.203 147.529 1.00 41.14 ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 116.318 192.970 146.760 1.00 40.69 ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 115.439 192.088 147.579 1.00 40.08 ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 116.586 199.432 149.163 1.00 40.35 ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 117.072 200.483 150.046 1.00 38.55 ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 117.977 201.402 149.237 1.00 39.55 ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 118.118 201.255 148.020 1.00 39.39 ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 117.803 199.899 151.258 1.00 39.89 ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 118.970 198.579 150.864 1.00 47.56 ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 118.589 202.361 149.926 1.00 39.56 ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 119.541 203.293 149.325 1.00 38.44 ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 120.886 203.085 150.012 1.00 40.40 ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 121.125 203.615 151.102 1.00 43.57 ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 119.061 204.735 149.454 1.00 38.89 ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 117.745 205.014 148.750 1.00 39.67 ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 117.953 205.873 147.514 1.00 39.87 ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 118.613 207.135 147.825 1.00 43.00 ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 118.015 208.175 148.390 1.00 40.82 ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 116.733 208.143 148.716 1.00 39.96 ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 118.720 209.276 148.632 1.00 37.42 ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 121.760 202.318 149.370 1.00 35.67 ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 123.062 202.018 149.944 1.00 33.48 ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 124.007 203.205 149.799 1.00 32.41 ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 123.935 203.976 148.838 1.00 32.86 ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 123.667 200.786 149.275 1.00 33.68 ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 122.872 199.489 149.413 1.00 32.99 ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 123.626 198.342 148.769 1.00 32.23 ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 122.583 199.191 150.875 1.00 33.28 ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 124.904 203.341 150.776 1.00 33.00 ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 125.884 204.417 150.763 1.00 32.10 ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 126.910 204.163 149.668 1.00 34.44 ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 127.356 203.028 149.457 1.00 34.67 ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 126.555 204.543 152.142 1.00 30.27 ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 125.501 204.729 153.234 1.00 32.09 ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 127.545 205.695 152.156 1.00 30.52 ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 126.081 204.938 154.611 1.00 34.14 ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 127.287 205.225 148.962 1.00 36.90 ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 128.265 205.154 147.890 1.00 35.76 ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 129.294 206.260 148.077 1.00 37.53 ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 128.994 207.317 148.636 1.00 39.59 ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 127.589 205.276 146.514 1.00 36.27 ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 128.515 205.083 145.326 1.00 37.17 ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 127.754 205.179 144.016 1.00 37.71 ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 126.992 206.418 143.919 1.00 40.40 ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 126.105 206.677 142.966 1.00 41.73 ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 125.848 205.806 142.006 1.00 40.38 ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 125.461 207.841 142.980 1.00 39.49 ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 130.515 206.002 147.617 1.00 36.55 ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 131.576 206.984 147.723 1.00 36.16 ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 132.296 206.933 149.054 1.00 37.27 ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 132.488 207.961 149.709 1.00 38.92 ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 132.697 205.728 149.465 1.00 31.62 ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 133.406 205.566 150.729 1.00 29.78 ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 134.772 206.237 150.690 1.00 30.54 ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 135.221 206.808 151.692 1.00 32.87 ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 133.555 204.080 151.050 1.00 30.84 ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 132.258 203.382 151.302 1.00 33.04 ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 131.643 202.481 150.485 1.00 31.07 ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 131.423 203.513 152.456 1.00 32.19 ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 130.472 202.049 151.054 1.00 30.19 ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 130.315 202.667 152.266 1.00 29.36 ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 131.503 204.267 153.629 1.00 30.03 ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 129.295 202.553 153.206 1.00 27.87 ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 130.491 204.152 154.560 1.00 32.00 ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 129.401 203.303 154.343 1.00 31.67 ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 135.451 206.165 149.541 1.00 32.76 ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 136.807 206.697 149.441 1.00 34.23 ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 136.843 208.201 149.674 1.00 36.13 ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 137.725 208.703 150.381 1.00 36.74 ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 137.408 206.329 148.081 1.00 35.38 ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 136.647 206.937 146.910 1.00 36.79 ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 135.622 207.614 147.134 1.00 35.71 ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 137.076 206.730 145.756 1.00 35.86 ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 135.892 208.940 149.094 1.00 35.99 ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 135.864 210.387 149.288 1.00 36.88 ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 135.648 210.741 150.751 1.00 35.96 ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 136.326 211.624 151.290 1.00 37.57 ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 134.771 211.013 148.420 1.00 36.72 ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 134.936 210.689 146.950 1.00 38.68 ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 136.001 211.016 146.384 1.00 39.55 ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 133.999 210.114 146.359 1.00 37.54 ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 134.711 210.060 151.412 1.00 33.41 ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 134.433 210.335 152.817 1.00 34.96 ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 135.644 210.030 153.689 1.00 36.68 ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 136.012 210.825 154.566 1.00 39.70 ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 133.218 209.523 153.264 1.00 32.49 ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 132.803 209.564 154.732 1.00 32.94 ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 132.075 210.856 155.052 1.00 36.55 ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 131.929 208.367 155.042 1.00 32.59 ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 136.286 208.881 153.456 1.00 34.84 ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 137.453 208.517 154.251 1.00 35.34 ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 138.598 209.497 154.036 1.00 36.76 ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 139.270 209.901 154.992 1.00 38.37 ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 137.895 207.094 153.913 1.00 35.93 ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 136.955 206.034 154.410 1.00 34.43 ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 136.263 206.204 155.593 1.00 32.31 ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 136.769 204.867 153.692 1.00 34.36 ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 135.400 205.230 156.051 1.00 30.93 ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 135.907 203.891 154.145 1.00 33.98 ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 135.223 204.072 155.325 1.00 32.51 ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 138.837 209.890 152.781 1.00 37.31 ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 139.897 210.850 152.494 1.00 39.09 ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 139.608 212.197 153.140 1.00 37.74 ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 140.518 212.845 153.665 1.00 38.02 ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 140.070 211.000 150.984 1.00 37.07 ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 140.610 209.742 150.332 1.00 39.11 ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 141.009 208.799 151.014 1.00 37.21 ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 140.621 209.722 149.005 1.00 38.24 ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 138.347 212.636 153.107 1.00 37.04 ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 137.991 213.900 153.741 1.00 39.38 ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 138.220 213.847 155.246 1.00 38.95 ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 138.769 214.789 155.832 1.00 41.46 ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 136.535 214.247 153.429 1.00 37.21 ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 136.079 215.582 153.988 1.00 38.42 ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 136.858 216.728 153.368 1.00 40.22 ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 136.554 216.869 151.887 1.00 39.92 ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 137.343 217.969 151.267 1.00 39.11 ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 137.818 212.745 155.887 1.00 35.15 ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 138.027 212.613 157.326 1.00 36.63 ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 139.515 212.621 157.655 1.00 40.37 ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 139.953 213.300 158.595 1.00 39.68 ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 137.335 211.343 157.857 1.00 36.33 ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 137.652 211.146 159.329 1.00 38.20 ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 135.837 211.432 157.655 1.00 37.00 ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 140.314 211.877 156.887 1.00 40.14 ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 141.753 211.839 157.138 1.00 39.28 ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 142.386 213.213 156.957 1.00 41.18 ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 143.205 213.642 157.779 1.00 42.28 ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 142.420 210.822 156.212 1.00 39.82 ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 142.152 209.376 156.579 1.00 42.30 ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 142.804 208.423 155.593 1.00 41.95 ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 142.643 206.981 156.039 1.00 41.80 ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 141.213 206.573 156.084 1.00 40.04 ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 142.014 213.917 155.884 1.00 42.23 ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 142.584 215.235 155.627 1.00 43.15 ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 142.218 216.217 156.729 1.00 44.11 ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 143.060 217.007 157.169 1.00 44.69 ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 142.112 215.747 154.266 1.00 42.78 ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 142.719 217.077 153.855 1.00 43.24 ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 141.906 217.780 152.787 1.00 44.85 ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 140.879 217.216 152.352 1.00 43.90 ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 142.288 218.898 152.385 1.00 45.30 ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 140.968 216.177 157.198 1.00 42.19 ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 140.563 217.100 158.251 1.00 42.88 ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 141.237 216.767 159.578 1.00 43.19 ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 141.601 217.672 160.337 1.00 45.13 ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 139.042 217.102 158.385 1.00 41.67 ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 138.351 217.880 157.311 1.00 41.64 ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 136.998 218.135 157.324 1.00 41.80 ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 138.831 218.463 156.185 1.00 42.26 ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 136.673 218.840 156.256 1.00 43.56 ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 137.768 219.053 155.549 1.00 44.22 ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 141.433 215.478 159.871 1.00 39.90 ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 142.155 215.100 161.085 1.00 41.94 ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 143.596 215.598 161.024 1.00 40.27 ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 144.125 216.149 162.002 1.00 39.27 ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 142.087 213.576 161.292 1.00 40.00 ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 140.690 213.165 161.762 1.00 38.13 ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 143.138 213.122 162.292 1.00 39.02 ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 140.479 211.668 161.812 1.00 40.26 ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 144.250 215.417 159.874 1.00 40.83 ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 145.620 215.903 159.720 1.00 43.24 ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 145.683 217.420 159.847 1.00 44.08 ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 146.617 217.962 160.452 1.00 44.24 ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 146.190 215.450 158.376 1.00 41.40 ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 146.222 213.941 158.236 1.00 43.72 ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 146.143 213.214 159.225 1.00 44.08 ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 146.337 213.464 157.004 1.00 43.14 ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 144.697 218.123 159.286 1.00 41.91 ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 144.660 219.576 159.421 1.00 41.88 ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 144.511 219.988 160.879 1.00 45.71 ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 145.187 220.916 161.340 1.00 45.86 ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 143.521 220.155 158.583 1.00 40.80 ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 142.269 219.924 159.203 1.00 44.97 ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 143.636 219.308 161.623 1.00 46.52 ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 143.441 219.638 163.033 1.00 45.88 ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 144.732 219.420 163.813 1.00 46.38 ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 145.094 220.223 164.683 1.00 46.80 ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 142.273 218.820 163.617 1.00 45.13 ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 142.233 218.947 165.128 1.00 46.15 ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 140.954 219.279 163.016 1.00 43.61 ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 145.456 218.340 163.507 1.00 46.77 ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 146.759 218.134 164.138 1.00 48.20 ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 147.726 219.262 163.791 1.00 48.18 ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 148.450 219.769 164.662 1.00 46.25 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 147.337 216.782 163.716 1.00 45.74 ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 146.484 215.720 164.102 1.00 45.75 ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 147.745 219.673 162.520 1.00 48.57 ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 148.624 220.761 162.102 1.00 49.65 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 148.319 222.040 162.867 1.00 51.63 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 149.227 222.818 163.181 1.00 51.13 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 148.495 220.991 160.597 1.00 46.10 ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 147.043 222.286 163.163 1.00 55.31 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 146.707 223.449 163.981 1.00 54.98 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 147.131 223.247 165.429 1.00 54.38 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 147.568 224.197 166.086 1.00 54.62 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 145.218 223.763 163.885 1.00 54.24 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 144.730 223.554 162.496 1.00 55.83 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 145.286 224.873 161.416 1.00 65.07 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 144.162 224.630 160.065 1.00 55.56 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 147.021 222.016 165.939 1.00 54.75 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 147.565 221.726 167.263 1.00 54.53 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 149.045 222.067 167.340 1.00 54.69 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 149.550 222.409 168.416 1.00 52.84 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 147.367 220.256 167.630 1.00 53.78 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 145.932 219.797 167.713 1.00 52.42 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 145.885 218.290 167.842 1.00 53.35 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 144.476 217.778 167.669 1.00 54.22 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 144.434 216.292 167.584 1.00 53.58 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 149.756 221.972 166.214 1.00 54.89 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 151.173 222.327 166.200 1.00 55.07 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 151.391 223.791 166.575 1.00 54.27 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 152.321 224.115 167.325 1.00 52.15 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 151.773 222.036 164.826 1.00 52.75 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 151.740 220.583 164.353 1.00 52.64 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 152.598 220.408 163.112 1.00 51.92 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 152.201 219.649 165.462 1.00 51.97 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 150.552 224.691 166.062 1.00 56.85 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 150.751 226.120 166.260 1.00 56.99 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 150.426 226.533 167.697 1.00 58.02 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 149.682 225.845 168.399 1.00 53.94 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 149.881 226.912 165.287 1.00 55.20 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 148.593 227.139 165.828 1.00 54.91 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 150.992 227.652 168.164 1.00 62.67 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 150.630 228.132 169.509 1.00 60.22 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 149.249 228.761 169.572 1.00 59.31 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 148.495 228.493 170.519 1.00 57.95 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 151.737 229.147 169.825 1.00 57.84 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 152.185 229.634 168.491 1.00 56.95 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 152.065 228.460 167.557 1.00 57.92 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 148.888 229.582 168.576 1.00 62.92 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 147.575 230.221 168.551 1.00 62.49 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 146.445 229.218 168.727 1.00 62.28 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 145.349 229.600 169.155 1.00 60.59 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 147.379 230.984 167.239 1.00 62.59 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 148.271 232.195 167.073 1.00 63.40 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 148.964 232.730 168.153 1.00 62.53 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 148.416 232.807 165.835 1.00 61.41 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 149.778 233.836 168.003 1.00 62.87 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 149.228 233.915 165.675 1.00 63.36 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 149.906 234.425 166.761 1.00 64.58 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 150.715 235.526 166.607 1.00 61.01 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 146.703 227.943 168.432 1.00 60.95 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 145.782 226.839 168.665 1.00 61.18 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 145.062 226.969 169.997 1.00 61.83 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 143.873 226.648 170.095 1.00 61.48 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 146.550 225.518 168.616 1.00 60.00 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 145.777 224.311 169.086 1.00 61.77 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 144.669 223.853 168.388 1.00 60.94 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 146.163 223.622 170.227 1.00 60.50 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 143.965 222.745 168.817 1.00 60.22 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 145.467 222.515 170.663 1.00 60.25 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 144.370 222.081 169.956 1.00 60.90 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 143.674 220.977 170.390 1.00 60.54 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 145.765 227.473 171.016 1.00 59.19 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 145.182 227.547 172.352 1.00 58.22 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 143.857 228.301 172.347 1.00 58.04 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 142.875 227.839 172.941 1.00 56.28 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 146.166 228.201 173.322 1.00 56.78 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 145.666 228.249 174.757 1.00 57.19 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 145.163 226.888 175.212 1.00 57.42 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 144.457 226.978 176.554 1.00 58.84 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 143.905 225.660 176.979 1.00 57.93 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 143.796 229.442 171.653 1.00 57.08 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 142.587 230.261 171.703 1.00 57.51 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 141.392 229.517 171.121 1.00 57.67 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 140.245 229.823 171.464 1.00 57.12 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 142.806 231.616 170.989 1.00 58.41 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 142.944 231.430 169.490 1.00 56.32 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 141.682 232.594 171.319 1.00 57.24 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 141.629 228.530 170.256 1.00 59.10 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 140.565 227.691 169.728 1.00 59.68 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 140.657 226.250 170.210 1.00 60.43 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 139.824 225.427 169.806 1.00 60.37 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 140.574 227.715 168.194 1.00 59.06 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 140.728 229.089 167.606 1.00 60.48 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 139.852 230.105 167.942 1.00 58.87 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 141.746 229.358 166.707 1.00 60.99 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 139.992 231.369 167.399 1.00 59.05 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 141.892 230.619 166.160 1.00 61.53 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 141.013 231.626 166.506 1.00 60.14 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 141.622 225.939 171.084 1.00 58.67 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 141.968 224.556 171.405 1.00 56.98 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 140.732 223.707 171.670 1.00 58.09 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 140.449 222.754 170.932 1.00 58.53 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 142.907 224.523 172.612 1.00 56.10 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 143.097 223.138 173.209 1.00 57.95 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 144.073 223.128 174.366 1.00 60.05 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 143.802 223.806 175.379 1.00 59.70 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 145.112 222.443 174.263 1.00 60.02 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 139.960 224.073 172.697 1.00 54.62 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 138.789 223.288 173.074 1.00 55.82 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 137.895 223.030 171.873 1.00 55.71 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 137.552 221.879 171.575 1.00 54.51 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 138.008 224.003 174.177 1.00 53.98 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 136.588 223.490 174.353 1.00 54.67 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 135.697 224.473 175.085 1.00 56.18 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 135.513 225.601 174.579 1.00 55.76 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 135.180 224.119 176.165 1.00 55.94 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 137.551 224.092 171.136 1.00 50.26 ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 136.712 223.923 169.956 1.00 50.66 ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 137.334 222.918 169.001 1.00 51.89 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 136.708 221.913 168.643 1.00 50.20 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 136.495 225.269 169.265 1.00 52.68 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 135.641 225.150 168.016 1.00 55.34 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 134.482 224.695 168.128 1.00 52.42 ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 136.128 225.508 166.924 1.00 55.17 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 138.604 223.136 168.644 1.00 51.87 ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 139.289 222.184 167.778 1.00 50.93 ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 139.298 220.803 168.408 1.00 50.57 ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 139.029 219.801 167.731 1.00 51.65 ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 140.712 222.660 167.491 1.00 48.05 ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 139.555 220.735 169.718 1.00 48.17 ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 139.473 219.462 170.420 1.00 47.47 ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 138.123 218.810 170.175 1.00 47.91 ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 138.048 217.673 169.695 1.00 48.52 ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 139.706 219.670 171.917 1.00 48.76 ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 141.165 219.745 172.361 1.00 51.20 ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 141.261 219.761 173.877 1.00 48.88 ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 141.941 218.569 171.792 1.00 49.41 ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 137.043 219.556 170.421 1.00 48.35 ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 135.715 219.008 170.191 1.00 50.50 ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 135.625 218.439 168.786 1.00 49.80 ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 135.199 217.291 168.588 1.00 49.45 ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 134.654 220.088 170.414 1.00 51.02 ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 134.631 221.006 169.335 1.00 51.24 ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 136.130 219.195 167.808 1.00 49.35 ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 136.030 218.773 166.419 1.00 49.65 ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 136.634 217.391 166.224 1.00 50.11 ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 135.972 216.492 165.683 1.00 49.14 ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 136.694 219.802 165.504 1.00 49.51 ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 135.697 220.711 164.857 1.00 51.86 ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 135.581 222.059 165.028 1.00 50.68 ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 134.665 220.334 163.938 1.00 51.25 ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 134.542 222.545 164.272 1.00 50.42 ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 133.965 221.505 163.593 1.00 50.74 ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 134.269 219.119 163.372 1.00 48.85 ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 132.890 221.497 162.708 1.00 49.84 ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 133.203 219.113 162.495 1.00 49.79 ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 132.526 220.294 162.170 1.00 50.99 ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 137.859 217.170 166.725 1.00 47.41 ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 138.494 215.887 166.442 1.00 45.07 ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 137.624 214.755 166.954 1.00 45.98 ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 137.441 213.745 166.264 1.00 48.92 ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 139.900 215.780 167.041 1.00 45.11 ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 139.982 215.779 168.555 1.00 47.85 ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 141.404 215.722 169.063 1.00 50.75 ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 142.324 215.705 168.224 1.00 51.63 ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 141.599 215.684 170.295 1.00 49.75 ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 137.019 214.943 168.132 1.00 42.48 ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 136.179 213.895 168.691 1.00 43.20 ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 135.103 213.502 167.693 1.00 42.59 ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 135.021 212.338 167.278 1.00 44.13 ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 135.569 214.367 170.012 1.00 43.40 ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 134.474 213.451 170.509 1.00 46.31 ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 134.755 212.254 170.731 1.00 48.51 ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 133.333 213.928 170.686 1.00 44.94 ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 134.350 214.491 167.202 1.00 41.22 ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 133.331 214.206 166.203 1.00 40.91 ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 133.951 213.510 165.005 1.00 39.56 ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 133.491 212.440 164.586 1.00 40.06 ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 132.628 215.498 165.783 1.00 42.73 ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 131.780 216.126 166.875 1.00 42.65 ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 130.855 217.191 166.311 1.00 42.57 ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 131.635 218.420 165.876 1.00 43.08 ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 130.738 219.523 165.434 1.00 41.47 ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 135.059 214.063 164.500 1.00 37.46 ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 135.741 213.450 163.370 1.00 38.68 ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 136.048 211.995 163.670 1.00 38.94 ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 135.664 211.096 162.909 1.00 37.39 ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 137.020 214.224 163.046 1.00 37.95 ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 136.865 215.431 162.122 1.00 40.19 ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 138.214 216.073 161.854 1.00 40.87 ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 136.202 215.018 160.819 1.00 39.97 ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 136.666 211.738 164.828 1.00 38.23 ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 136.995 210.367 165.188 1.00 35.27 ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 135.746 209.503 165.157 1.00 35.83 ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 135.714 208.462 164.488 1.00 39.24 ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 137.654 210.326 166.567 1.00 36.61 ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 139.037 210.944 166.570 1.00 37.61 ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 139.728 210.950 165.552 1.00 35.60 ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 139.450 211.466 167.718 1.00 36.17 ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 134.674 209.977 165.799 1.00 35.20 ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 133.435 209.214 165.819 1.00 33.87 ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 132.994 208.885 164.405 1.00 35.20 ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 132.725 207.720 164.083 1.00 39.45 ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 132.349 209.991 166.565 1.00 36.48 ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 132.632 210.173 168.046 1.00 37.07 ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 131.748 211.249 168.648 1.00 36.49 ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 130.340 211.026 168.348 1.00 37.99 ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 129.457 211.992 168.138 1.00 39.34 ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 129.804 213.266 168.186 1.00 39.46 ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 128.194 211.670 167.875 1.00 37.51 ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 132.995 209.894 163.524 1.00 34.05 ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 132.624 209.665 162.130 1.00 34.53 ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 133.420 208.494 161.580 1.00 35.11 ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 132.857 207.465 161.181 1.00 34.87 ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 132.841 210.938 161.294 1.00 35.50 ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 131.751 211.967 161.595 1.00 37.25 ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 132.861 210.609 159.810 1.00 32.36 ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 131.974 213.303 160.925 1.00 35.38 ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 134.750 208.601 161.652 1.00 37.46 ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 135.605 207.538 161.142 1.00 32.28 ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 135.198 206.205 161.742 1.00 29.60 ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 134.903 205.248 161.014 1.00 32.73 ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 137.070 207.850 161.450 1.00 32.61 ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 138.054 206.940 160.743 1.00 32.93 ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 138.219 207.327 158.993 1.00 46.96 ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 139.843 208.075 158.977 1.00 34.67 ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 135.075 206.162 163.072 1.00 26.92 ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 134.733 204.916 163.743 1.00 30.15 ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 133.473 204.320 163.140 1.00 31.46 ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 133.468 203.164 162.698 1.00 32.84 ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 134.560 205.153 165.243 1.00 30.64 ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 132.418 205.132 163.033 1.00 31.79 ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 131.164 204.624 162.494 1.00 29.43 ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 131.379 204.067 161.097 1.00 31.77 ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 131.030 202.914 160.808 1.00 37.01 ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 130.111 205.732 162.485 1.00 31.58 ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 128.705 205.337 162.032 1.00 33.09 ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 128.118 204.301 162.972 1.00 31.98 ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 127.809 206.559 161.948 1.00 33.42 ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 132.036 204.838 160.241 1.00 31.68 ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 132.208 204.408 158.866 1.00 28.59 ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 133.349 203.420 158.710 1.00 29.43 ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 133.550 202.903 157.608 1.00 32.38 ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 132.397 205.626 157.964 1.00 29.75 ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 131.183 206.509 157.901 1.00 32.35 ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 130.004 206.045 157.342 1.00 32.97 ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 131.212 207.793 158.417 1.00 34.49 ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 128.883 206.848 157.286 1.00 31.27 ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 130.091 208.599 158.363 1.00 34.10 ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 128.925 208.126 157.799 1.00 31.73 ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 134.095 203.134 159.781 1.00 32.09 ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 134.988 201.988 159.741 1.00 29.61 ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 134.237 200.679 159.916 1.00 30.60 ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 134.785 199.617 159.604 1.00 32.35 ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 136.077 202.110 160.809 1.00 32.36 ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 137.064 203.221 160.510 1.00 35.69 ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 137.277 203.522 159.317 1.00 33.68 ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 137.628 203.789 161.467 1.00 39.31 ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 133.000 200.732 160.401 1.00 28.52 ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 132.173 199.543 160.557 1.00 29.43 ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 131.117 199.458 159.467 1.00 29.31 ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 130.977 198.429 158.805 1.00 29.81 ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 131.532 199.522 161.961 1.00 26.49 ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 130.919 198.160 162.242 1.00 29.77 ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 132.560 199.878 163.019 1.00 27.86 ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 130.400 200.565 159.244 1.00 27.55 ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 129.233 200.564 158.368 1.00 27.40 ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 129.548 199.941 157.017 1.00 26.44 ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 128.843 199.031 156.563 1.00 28.14 ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 128.728 201.994 158.190 1.00 28.40 ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 127.292 202.091 157.801 1.00 30.48 ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 126.641 201.341 156.867 1.00 29.37 ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 126.325 202.997 158.334 1.00 32.76 ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 125.326 201.724 156.787 1.00 29.93 ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 125.107 202.742 157.679 1.00 32.15 ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 126.371 204.003 159.305 1.00 31.90 ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 123.946 203.452 157.963 1.00 30.61 ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 125.219 204.705 159.584 1.00 30.88 ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 124.024 204.427 158.917 1.00 30.72 ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 130.629 200.401 156.379 1.00 26.15 ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 131.012 199.872 155.071 1.00 26.19 ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 131.022 198.351 155.107 1.00 26.71 ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 130.275 197.691 154.372 1.00 31.24 ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 132.368 200.451 154.625 1.00 25.84 ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 132.839 199.788 153.329 1.00 28.26 ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 133.419 200.351 155.724 1.00 24.30 ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 133.972 200.525 152.650 1.00 27.05 ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 131.801 197.776 156.030 1.00 21.46 ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 131.856 196.325 156.144 1.00 21.96 ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 130.456 195.759 156.296 1.00 21.99 ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 130.018 194.929 155.489 1.00 25.90 ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 132.732 195.920 157.331 1.00 22.61 ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 134.196 196.229 157.109 1.00 29.99 ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 134.636 196.223 155.940 1.00 32.61 ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 134.909 196.479 158.103 1.00 27.71 ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 129.708 196.284 157.271 1.00 22.36 ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 128.327 195.858 157.481 1.00 21.06 ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 127.585 195.862 156.156 1.00 21.59 ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 127.114 194.821 155.681 1.00 26.49 ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 127.631 196.762 158.513 1.00 20.86 ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 126.159 196.404 158.622 1.00 21.93 ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 128.315 196.654 159.863 1.00 22.59 ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 127.565 197.024 155.496 1.00 19.56 ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 126.828 197.143 154.248 1.00 17.58 ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 127.267 196.062 153.279 1.00 20.16 ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 126.450 195.249 152.827 1.00 23.69 ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 127.033 198.530 153.642 1.00 19.74 ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 126.359 198.722 152.296 1.00 20.77 ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 126.399 200.162 151.829 1.00 23.42 ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 125.791 201.041 152.438 1.00 28.05 ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 127.118 200.412 150.742 1.00 22.52 ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 128.580 195.965 153.049 1.00 23.11 ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 129.087 194.983 152.100 1.00 19.57 ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 128.582 193.602 152.468 1.00 19.46 ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 127.948 192.920 151.650 1.00 23.45 ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 130.614 195.015 152.070 1.00 16.85 ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 131.233 193.928 151.211 1.00 21.84 ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 132.737 194.095 151.108 1.00 23.02 ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 133.348 194.359 152.405 1.00 22.61 ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 133.561 193.439 153.335 1.00 23.12 ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 133.228 192.173 153.146 1.00 21.29 ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 134.126 193.798 154.486 1.00 20.88 ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 128.762 193.222 153.735 1.00 17.57 ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 128.322 191.907 154.178 1.00 15.77 ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 126.855 191.715 153.838 1.00 18.26 ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 126.489 190.814 153.067 1.00 24.99 ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 128.561 191.763 155.681 1.00 16.66 ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 128.978 190.379 156.128 1.00 19.02 ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 129.712 190.442 157.455 1.00 20.97 ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 130.948 191.207 157.355 1.00 22.83 ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 132.149 190.670 157.183 1.00 24.26 ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 132.314 189.360 157.099 1.00 22.68 ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 133.210 191.467 157.094 1.00 25.66 ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 126.022 192.656 154.298 1.00 17.98 ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 124.588 192.523 154.096 1.00 18.33 ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 124.288 192.286 152.633 1.00 16.49 ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 123.554 191.349 152.287 1.00 23.82 ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 123.861 193.768 154.603 1.00 22.37 ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 122.377 193.706 154.418 1.00 21.99 ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 121.472 193.120 155.253 1.00 22.37 ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 121.625 194.245 153.325 1.00 22.23 ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 120.202 193.263 154.749 1.00 20.61 ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 120.269 193.949 153.566 1.00 20.71 ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 121.965 194.949 152.167 1.00 23.84 ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 119.256 194.334 152.694 1.00 20.99 ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 120.958 195.330 151.302 1.00 22.48 ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 119.620 195.022 151.569 1.00 21.85 ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 124.941 193.056 151.756 1.00 15.29 ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 124.666 192.956 150.327 1.00 15.25 ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 124.729 191.502 149.891 1.00 18.98 ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 123.717 190.907 149.499 1.00 23.55 ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 125.641 193.830 149.520 1.00 19.02 ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 125.532 193.511 148.040 1.00 20.25 ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 125.361 195.299 149.767 1.00 20.63 ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 125.895 190.872 150.062 1.00 17.92 ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 125.996 189.524 149.524 1.00 15.60 ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 125.136 188.566 150.329 1.00 12.71 ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 124.509 187.668 149.752 1.00 18.69 ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 127.457 189.066 149.426 1.00 18.72 ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 128.238 188.864 150.707 1.00 15.89 ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 127.997 187.774 151.532 1.00 17.64 ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 129.263 189.731 151.052 1.00 12.65 ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 128.726 187.579 152.686 1.00 17.88 ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 130.001 189.541 152.202 1.00 15.02 ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 129.726 188.464 153.015 1.00 15.97 ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 130.457 188.272 154.164 1.00 19.67 ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 125.015 188.796 151.638 1.00 16.25 ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 124.140 187.943 152.431 1.00 17.74 ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 122.713 188.040 151.921 1.00 19.63 ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 122.016 187.024 151.806 1.00 20.91 ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 124.231 188.316 153.908 1.00 17.53 ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 125.415 187.690 154.648 1.00 20.17 ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 125.362 188.006 156.129 1.00 23.23 ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 125.455 186.188 154.421 1.00 18.53 ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 122.282 189.249 151.546 1.00 20.71 ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 120.960 189.395 150.955 1.00 18.26 ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 120.838 188.514 149.721 1.00 22.05 ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 119.906 187.706 149.609 1.00 25.54 ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 120.697 190.862 150.613 1.00 18.98 ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 119.234 191.258 150.664 1.00 23.65 ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 118.542 191.106 149.327 1.00 28.65 ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 119.244 191.037 148.298 1.00 27.82 ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 117.294 191.058 149.305 1.00 29.28 ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 121.828 188.590 148.827 1.00 19.77 ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 121.783 187.806 147.608 1.00 17.30 ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 121.793 186.317 147.854 1.00 18.94 ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 121.472 185.542 146.946 1.00 22.04 ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 122.147 185.895 149.066 1.00 17.76 ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 122.129 184.478 149.387 1.00 17.65 ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 120.781 184.055 149.961 1.00 23.38 ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 120.328 182.931 149.713 1.00 28.68 ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 123.283 184.153 150.349 1.00 17.36 ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 124.618 184.340 149.632 1.00 16.90 ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 123.172 182.737 150.886 1.00 19.44 ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 125.783 184.486 150.561 1.00 18.94 ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 120.107 184.938 150.694 1.00 28.04 ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 118.867 184.579 151.365 1.00 26.84 ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 117.628 184.957 150.568 1.00 25.42 ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 116.510 184.745 151.047 1.00 25.01 ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 118.816 185.219 152.754 1.00 23.16 ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 119.717 184.555 153.754 1.00 21.94 ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 119.404 183.309 154.266 1.00 23.64 ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 120.884 185.170 154.171 1.00 24.27 ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 120.233 182.695 155.182 1.00 27.64 ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 121.716 184.560 155.087 1.00 23.15 ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 121.390 183.321 155.593 1.00 26.39 ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 117.796 185.511 149.370 1.00 25.65 ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 116.676 185.857 148.504 1.00 29.27 ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 116.732 185.136 147.168 1.00 32.08 ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 115.722 184.576 146.727 1.00 33.43 ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 116.636 187.376 148.275 1.00 30.54 ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 116.712 188.052 149.536 1.00 26.70 ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 115.349 187.772 147.570 1.00 29.39 ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 117.890 185.136 146.504 1.00 34.35 ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 117.996 184.478 145.213 1.00 34.64 ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 117.852 182.971 145.298 1.00 35.07 ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 117.298 182.340 144.392 1.00 35.29 ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 118.343 182.374 146.379 1.00 37.14 ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 118.351 180.926 146.541 1.00 39.79 ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 117.134 180.484 147.342 1.00 42.87 ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 116.854 181.031 148.414 1.00 43.06 ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 119.631 180.466 147.237 1.00 39.74 ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 119.711 180.985 148.553 1.00 42.45 ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 116.413 179.492 146.816 1.00 48.38 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 115.223 178.978 147.478 1.00 48.66 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 115.494 177.750 148.337 1.00 48.36 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 114.702 177.460 149.238 1.00 48.14 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 114.148 178.637 146.440 1.00 46.45 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 116.584 177.024 148.083 1.00 50.05 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 116.871 175.818 148.852 1.00 50.69 ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 117.376 176.126 150.254 1.00 51.90 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 117.254 175.275 151.143 1.00 49.76 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 117.894 174.955 148.112 1.00 50.73 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 117.280 174.176 146.966 1.00 52.75 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 116.283 174.657 146.387 1.00 51.45 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 117.795 173.085 146.644 1.00 51.29 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 117.937 177.318 150.473 1.00 49.98 ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 118.504 177.642 151.777 1.00 49.00 ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 117.412 177.778 152.831 1.00 48.17 ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 117.658 177.529 154.018 1.00 46.90 ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 119.374 178.911 151.682 1.00 44.51 ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 120.291 179.022 152.901 1.00 43.73 ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 118.514 180.158 151.532 1.00 41.98 ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 121.259 180.178 152.832 1.00 41.05 ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 116.200 178.172 152.434 1.00 49.31 ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 115.124 178.311 153.410 1.00 49.82 ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 114.714 176.957 153.981 1.00 50.62 ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 114.436 176.843 155.179 1.00 46.22 ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 113.927 179.038 152.789 1.00 49.78 ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 113.093 178.218 151.817 1.00 49.85 ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 112.131 179.094 151.035 1.00 50.12 ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 110.910 179.448 151.867 1.00 50.18 ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 109.687 179.577 151.030 1.00 48.52 ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 114.673 175.917 153.142 1.00 53.80 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 114.378 174.582 153.649 1.00 54.00 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 115.586 173.985 154.360 1.00 53.21 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 115.441 173.314 155.388 1.00 54.10 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 113.920 173.667 152.513 1.00 52.95 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 113.060 174.347 151.495 1.00 56.29 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 113.579 175.027 150.416 1.00 57.44 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 111.714 174.467 151.403 1.00 55.36 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 112.591 175.526 149.695 1.00 55.47 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 111.448 175.200 150.273 1.00 56.09 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 116.787 174.215 153.825 1.00 48.86 ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 117.986 173.649 154.435 1.00 50.44 ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 118.314 174.335 155.756 1.00 49.43 ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 118.654 173.675 156.744 1.00 48.14 ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 119.166 173.756 153.469 1.00 49.17 ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 120.262 172.699 153.613 1.00 49.95 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 119.701 171.300 153.405 1.00 48.33 ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 121.401 172.977 152.646 1.00 47.60 ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 118.220 175.663 155.791 1.00 46.99 ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 118.696 176.465 156.917 1.00 46.77 ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 117.653 177.519 157.276 1.00 46.65 ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 117.806 178.702 156.949 1.00 46.51 ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 120.039 177.106 156.572 1.00 45.79 ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 121.196 176.120 156.378 1.00 47.57 ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 122.459 176.818 155.900 1.00 45.05 ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 121.460 175.351 157.664 1.00 47.65 ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 116.571 177.121 157.954 1.00 50.23 ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 115.487 178.086 158.213 1.00 49.20 ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 115.779 179.059 159.345 1.00 47.45 ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 115.365 180.225 159.273 1.00 46.92 ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 114.290 177.179 158.548 1.00 48.90 ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 114.726 175.770 158.192 1.00 48.11 ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 116.204 175.763 158.379 1.00 48.69 ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 116.470 178.610 160.397 1.00 44.76 ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 116.566 179.411 161.617 1.00 48.20 ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 117.366 180.688 161.375 1.00 48.40 ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 116.912 181.793 161.702 1.00 45.83 ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 117.146 178.567 162.770 1.00 46.59 ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 118.489 177.951 162.392 1.00 45.14 ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 117.276 179.411 164.028 1.00 42.89 ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 118.551 180.574 160.769 1.00 45.85 ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 119.302 181.800 160.529 1.00 45.92 ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 118.765 182.542 159.317 1.00 44.32 ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 119.082 183.718 159.132 1.00 43.25 ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 120.801 181.525 160.390 1.00 43.15 ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 121.291 181.140 159.011 1.00 42.55 ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 121.096 179.679 158.694 1.00 46.85 ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 120.189 179.043 159.270 1.00 47.03 ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 121.883 179.162 157.878 1.00 46.65 ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 117.923 181.900 158.505 1.00 39.56 ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 117.167 182.653 157.508 1.00 40.66 ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 116.206 183.627 158.180 1.00 43.01 ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 116.116 184.795 157.784 1.00 44.27 ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 116.410 181.705 156.579 1.00 41.19 ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 117.295 180.677 156.120 1.00 44.71 ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 115.860 182.461 155.383 1.00 37.82 ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 115.497 183.173 159.218 1.00 41.75 ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 114.653 184.091 159.983 1.00 42.96 ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 115.493 185.129 160.720 1.00 43.08 ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 115.110 186.306 160.810 1.00 40.51 ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 113.782 183.312 160.968 1.00 43.30 ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 112.764 182.396 160.311 1.00 44.94 ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 111.752 183.151 159.470 1.00 44.88 ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 111.767 183.077 158.242 1.00 43.01 ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 110.858 183.878 160.132 1.00 44.30 ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 116.636 184.705 161.265 1.00 41.65 ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 117.537 185.649 161.922 1.00 40.36 ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 117.957 186.756 160.964 1.00 39.71 ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 117.889 187.947 161.297 1.00 39.93 ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 118.767 184.913 162.457 1.00 39.72 ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 118.477 183.926 163.574 1.00 41.63 ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 119.720 183.666 164.414 1.00 41.33 ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 119.569 182.508 165.290 1.00 44.96 ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 118.796 182.472 166.367 1.00 44.84 ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 118.079 183.518 166.742 1.00 41.99 ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 118.744 181.356 167.089 1.00 43.22 ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 118.375 186.378 159.754 1.00 34.94 ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 118.778 187.363 158.763 1.00 35.02 ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 117.599 188.192 158.288 1.00 34.91 ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 117.781 189.347 157.912 1.00 35.77 ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 119.450 186.693 157.567 1.00 32.01 ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 119.869 187.662 156.501 1.00 32.46 ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 121.006 188.433 156.661 1.00 30.23 ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 119.113 187.824 155.354 1.00 30.02 ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 121.391 189.333 155.692 1.00 28.87 ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 119.494 188.722 154.379 1.00 29.61 ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 120.633 189.477 154.550 1.00 30.29 ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 116.390 187.630 158.287 1.00 34.92 ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 115.224 188.451 157.981 1.00 37.07 ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 115.064 189.563 159.008 1.00 38.00 ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 114.821 190.721 158.650 1.00 37.26 ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 113.967 187.585 157.924 1.00 38.35 ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 112.718 188.355 157.538 1.00 38.58 ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 112.817 188.957 156.151 1.00 39.75 ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 113.015 190.163 155.997 1.00 38.22 ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 112.680 188.118 155.130 1.00 37.87 ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 115.229 189.231 160.290 1.00 40.59 ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 115.138 190.248 161.337 1.00 39.67 ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 116.240 191.296 161.192 1.00 39.46 ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 115.983 192.508 161.260 1.00 38.52 ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 115.203 189.585 162.713 1.00 40.35 ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 114.370 188.439 162.767 1.00 43.30 ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 117.481 190.849 160.994 1.00 35.82 ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 118.591 191.794 160.878 1.00 33.60 ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 118.470 192.630 159.608 1.00 32.85 ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 118.842 193.808 159.590 1.00 35.82 ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 119.944 191.065 160.975 1.00 31.53 ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 119.983 190.204 162.238 1.00 35.70 ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 121.093 192.045 160.968 1.00 32.93 ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 120.725 188.923 162.082 1.00 35.05 ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 117.945 192.047 158.532 1.00 28.10 ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 117.703 192.810 157.316 1.00 29.29 ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 116.614 193.848 157.534 1.00 33.52 ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 116.697 194.957 157.000 1.00 33.97 ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 117.331 191.866 156.175 1.00 31.27 ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 117.244 192.564 154.946 1.00 33.18 ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 115.585 193.512 158.317 1.00 35.45 ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 114.579 194.508 158.669 1.00 34.17 ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 115.207 195.668 159.433 1.00 35.21 ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 114.926 196.838 159.146 1.00 34.36 ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 113.468 193.863 159.497 1.00 34.17 ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 112.845 192.822 158.734 1.00 36.37 ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 112.423 194.897 159.884 1.00 34.15 ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 116.075 195.356 160.398 1.00 32.48 ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 116.764 196.413 161.138 1.00 32.80 ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 117.631 197.262 160.214 1.00 35.12 ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 117.646 198.497 160.320 1.00 36.39 ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 117.612 195.808 162.256 1.00 31.76 ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 116.856 194.887 163.193 1.00 34.40 ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 117.654 194.539 164.434 1.00 38.79 ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 118.891 194.720 164.418 1.00 38.29 ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 117.046 194.083 165.425 1.00 39.12 ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 118.363 196.615 159.303 1.00 32.31 ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 119.244 197.339 158.393 1.00 29.35 ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 118.454 198.237 157.449 1.00 31.44 ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 118.864 199.370 157.180 1.00 35.82 ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 120.105 196.355 157.602 1.00 26.41 ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 121.140 197.015 156.739 1.00 28.97 ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 122.331 197.462 157.283 1.00 31.50 ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 120.921 197.190 155.383 1.00 29.43 ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 123.285 198.071 156.492 1.00 29.47 ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 121.871 197.798 154.588 1.00 30.05 ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 123.053 198.239 155.144 1.00 30.07 ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 117.324 197.751 156.929 1.00 31.77 ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 116.500 198.589 156.065 1.00 33.34 ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 115.863 199.736 156.835 1.00 34.33 ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 115.714 200.831 156.286 1.00 34.69 ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 115.423 197.760 155.364 1.00 34.70 ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 115.879 196.576 154.514 1.00 32.30 ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 114.764 195.553 154.386 1.00 32.82 ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 116.339 197.047 153.144 1.00 32.42 ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 115.480 199.516 158.095 1.00 34.37 ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 114.981 200.626 158.903 1.00 35.96 ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 116.055 201.688 159.094 1.00 37.28 ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 115.789 202.890 158.957 1.00 35.48 ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 114.485 200.112 160.254 1.00 33.28 ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 117.286 201.261 159.391 1.00 35.42 ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 118.385 202.212 159.538 1.00 33.47 ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 118.661 202.945 158.230 1.00 33.51 ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 118.912 204.156 158.228 1.00 36.82 ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 119.638 201.486 160.023 1.00 33.79 ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 120.854 202.350 160.358 1.00 34.45 ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 120.459 203.534 161.223 1.00 34.48 ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 121.917 201.513 161.044 1.00 35.27 ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 118.622 202.228 157.107 1.00 33.99 ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 118.874 202.856 155.815 1.00 35.46 ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 117.772 203.846 155.458 1.00 37.24 ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 118.042 204.892 154.863 1.00 39.91 ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 119.015 201.791 154.729 1.00 35.97 ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 120.357 201.069 154.730 1.00 39.07 ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 121.712 202.011 155.460 1.00 45.95 ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 122.044 203.214 154.175 1.00 36.37 ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 116.524 203.529 155.806 1.00 36.65 ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 115.435 204.480 155.611 1.00 38.03 ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 115.640 205.726 156.461 1.00 39.81 ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 115.420 206.851 155.993 1.00 35.34 ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 114.097 203.818 155.939 1.00 37.06 ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 112.884 204.676 155.629 1.00 40.20 ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 112.778 204.969 154.142 1.00 41.23 ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 112.351 203.733 153.366 1.00 39.80 ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 112.120 204.031 151.926 1.00 39.49 ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 116.065 205.544 157.715 1.00 40.46 ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 116.355 206.693 158.569 1.00 39.02 ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 117.454 207.558 157.965 1.00 37.15 ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 117.381 208.791 158.010 1.00 36.92 ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 116.756 206.226 159.967 1.00 35.80 ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 115.642 205.562 160.756 1.00 35.41 ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 115.990 205.496 162.234 1.00 37.41 ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 117.028 204.420 162.507 1.00 37.46 ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 116.837 203.782 163.837 1.00 36.65 ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 118.485 206.924 157.405 1.00 37.19 ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 119.562 207.672 156.762 1.00 36.89 ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 119.051 208.392 155.518 1.00 38.67 ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 119.439 209.532 155.240 1.00 41.02 ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 120.737 206.734 156.434 1.00 34.50 ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 121.791 207.460 155.616 1.00 36.00 ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 121.336 206.190 157.711 1.00 33.23 ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 118.177 207.741 154.750 1.00 39.12 ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 117.654 208.349 153.532 1.00 39.50 ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 116.754 209.538 153.834 1.00 43.24 ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 116.683 210.476 153.033 1.00 41.33 ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 116.899 207.308 152.707 1.00 40.29 ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 116.284 207.900 151.577 1.00 41.63 ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 116.052 209.515 154.971 1.00 45.53 ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 115.245 210.669 155.356 1.00 43.14 ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 116.113 211.907 155.547 1.00 40.84 ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 115.772 212.996 155.070 1.00 43.34 ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 114.461 210.368 156.636 1.00 42.36 ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 113.456 209.237 156.511 1.00 44.36 ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 112.277 209.627 155.637 1.00 44.76 ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 111.270 208.493 155.536 1.00 43.23 ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 110.891 207.968 156.876 1.00 42.43 ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 117.243 211.758 156.237 1.00 38.39 ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 118.185 212.849 156.477 1.00 40.92 ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 119.582 212.359 156.121 1.00 40.39 ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 120.275 211.764 156.957 1.00 37.83 ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 118.116 213.331 157.924 1.00 42.20 ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 118.338 212.262 158.826 1.00 42.83 ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 120.028 212.585 154.885 1.00 41.38 ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 121.339 212.086 154.453 1.00 42.47 ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 122.530 212.872 154.981 1.00 44.41 ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 123.649 212.634 154.521 1.00 42.18 ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 121.250 212.199 152.923 1.00 40.98 ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 120.328 213.340 152.693 1.00 39.74 ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 119.316 213.289 153.805 1.00 39.12 ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 122.328 213.796 155.916 1.00 49.57 ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 123.442 214.540 156.489 1.00 47.64 ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 124.327 213.619 157.320 1.00 47.89 ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 123.838 212.744 158.040 1.00 48.35 ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 122.924 215.692 157.348 1.00 47.67 ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 123.818 216.929 157.432 1.00 49.11 ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 124.134 217.461 156.043 1.00 47.41 ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 123.167 218.003 158.289 1.00 47.63 ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 125.642 213.817 157.210 1.00 46.38 ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 126.582 212.960 157.927 1.00 47.21 ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 126.473 213.175 159.433 1.00 47.81 ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 126.473 212.215 160.210 1.00 44.30 ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 128.016 213.195 157.418 1.00 45.59 ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 129.007 212.373 158.225 1.00 43.95 ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 128.108 212.841 155.947 1.00 46.09 ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 126.385 214.434 159.872 1.00 48.20 ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 126.205 214.700 161.297 1.00 48.18 ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 124.854 214.208 161.801 1.00 49.21 ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 124.754 213.703 162.926 1.00 50.88 ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 126.381 216.186 161.603 1.00 48.18 ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 127.632 216.803 161.020 1.00 49.84 ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 129.030 216.245 162.011 1.00 54.75 ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 130.281 217.433 161.570 1.00 48.05 ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 123.800 214.354 160.996 1.00 45.50 ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 122.496 213.855 161.417 1.00 45.73 ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 122.528 212.346 161.613 1.00 46.74 ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 121.937 211.822 162.564 1.00 45.38 ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 121.422 214.246 160.402 1.00 45.30 ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 120.124 214.664 161.064 1.00 48.38 ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 119.885 214.249 162.217 1.00 47.45 ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 119.346 215.412 160.436 1.00 48.90 ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 123.213 211.629 160.720 1.00 44.41 ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 123.406 210.194 160.905 1.00 42.39 ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 124.231 209.924 162.158 1.00 42.30 ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 123.914 209.026 162.948 1.00 43.39 ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 124.057 209.581 159.652 1.00 39.42 ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 124.549 208.172 159.940 1.00 39.59 ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 123.075 209.579 158.494 1.00 40.31 ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 125.296 210.702 162.364 1.00 39.70 ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 126.154 210.506 163.528 1.00 40.43 ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 125.420 210.792 164.831 1.00 43.50 ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 125.781 210.245 165.879 1.00 40.86 ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 127.396 211.388 163.416 1.00 36.86 ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 128.578 210.994 164.305 1.00 39.36 ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 129.377 209.879 163.660 1.00 40.05 ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 129.463 212.199 164.582 1.00 39.89 ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 124.395 211.639 164.791 1.00 45.68 ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 123.650 212.010 165.985 1.00 44.45 ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 122.519 211.041 166.304 1.00 44.06 ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 121.799 211.257 167.286 1.00 45.16 ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 123.090 213.427 165.838 1.00 43.89 ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 124.177 214.483 165.842 1.00 45.06 ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 125.366 214.165 165.887 1.00 42.86 ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 123.777 215.748 165.792 1.00 45.36 ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 122.337 209.989 165.502 1.00 40.23 ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 121.334 208.980 165.812 1.00 42.34 ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 121.718 208.277 167.103 1.00 41.97 ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 122.881 207.904 167.304 1.00 40.43 ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 121.197 207.989 164.646 1.00 41.75 ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 120.666 208.699 163.401 1.00 40.39 ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 120.287 206.831 165.027 1.00 39.46 ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 120.482 207.786 162.211 1.00 39.72 ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 120.746 208.106 167.996 1.00 40.84 ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 121.023 207.505 169.294 1.00 41.11 ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 121.457 206.053 169.129 1.00 41.53 ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 120.837 205.282 168.389 1.00 39.85 ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 119.795 207.615 170.202 1.00 39.41 ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 118.629 206.701 169.848 1.00 42.68 ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 117.705 207.308 168.810 1.00 44.20 ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 118.123 207.618 167.694 1.00 41.87 ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 116.439 207.477 169.173 1.00 42.13 ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 122.553 205.693 169.797 1.00 40.79 ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 123.057 204.330 169.751 1.00 39.23 ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 123.394 203.834 168.363 1.00 40.77 ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 123.271 202.634 168.096 1.00 41.31 ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 123.815 204.728 167.465 1.00 39.26 ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 124.099 204.311 166.095 1.00 35.86 ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 125.359 203.453 166.044 1.00 34.49 ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 125.407 202.442 165.333 1.00 37.80 ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 124.196 205.539 165.167 1.00 35.33 ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 125.266 206.514 165.647 1.00 35.57 ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 124.457 205.108 163.732 1.00 33.25 ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 126.392 203.827 166.802 1.00 33.92 ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 127.618 203.040 166.822 1.00 35.14 ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 127.357 201.637 167.353 1.00 37.93 ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 127.785 200.641 166.754 1.00 35.22 ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 128.678 203.750 167.665 1.00 35.28 ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 130.040 203.079 167.654 1.00 36.97 ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 130.821 203.365 166.388 1.00 39.64 ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 131.162 204.513 166.102 1.00 37.91 ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 131.113 202.319 165.625 1.00 39.84 ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 126.639 201.540 168.474 1.00 39.14 ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 126.316 200.235 169.040 1.00 36.80 ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 125.453 199.423 168.084 1.00 38.37 ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 125.625 198.205 167.960 1.00 40.27 ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 125.617 200.406 170.387 1.00 37.41 ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 125.563 199.140 171.225 1.00 39.01 ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 124.298 199.090 172.064 1.00 38.82 ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 123.207 198.425 171.364 1.00 42.30 ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 122.218 199.056 170.744 1.00 43.69 ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 122.149 200.377 170.721 1.00 42.95 ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 121.276 198.344 170.132 1.00 40.68 ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 124.516 200.085 167.397 1.00 34.87 ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 123.682 199.388 166.425 1.00 35.04 ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 124.519 198.805 165.296 1.00 36.57 ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 124.322 197.650 164.902 1.00 38.24 ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 122.619 200.339 165.873 1.00 35.52 ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 121.816 199.698 164.898 1.00 36.75 ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 125.465 199.586 164.766 1.00 34.29 ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 126.318 199.077 163.694 1.00 33.16 ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 127.194 197.923 164.170 1.00 35.75 ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 127.363 196.933 163.448 1.00 35.35 ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 127.179 200.201 163.112 1.00 31.63 ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 126.603 201.016 161.950 1.00 31.99 ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 126.398 200.124 160.737 1.00 32.21 ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 125.308 201.715 162.313 1.00 34.32 ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 127.761 198.026 165.375 1.00 36.70 ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 128.581 196.925 165.881 1.00 34.67 ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 127.752 195.660 166.085 1.00 35.99 ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 128.206 194.553 165.765 1.00 38.76 ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 129.285 197.326 167.179 1.00 36.09 ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 130.000 198.662 167.112 1.00 36.35 ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 131.285 198.682 167.914 1.00 40.09 ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 131.303 198.117 169.028 1.00 40.44 ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 132.277 199.265 167.432 1.00 38.05 ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 126.534 195.801 166.613 1.00 32.04 ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 125.675 194.635 166.801 1.00 33.54 ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 125.288 194.014 165.464 1.00 36.99 ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 125.263 192.784 165.326 1.00 36.82 ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 124.430 195.024 167.596 1.00 34.83 ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 123.659 193.838 168.152 1.00 34.41 ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 122.392 194.287 168.858 1.00 35.51 ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 121.620 195.218 168.044 1.00 38.47 ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 120.681 194.854 167.181 1.00 36.95 ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 120.368 193.583 166.994 1.00 34.17 ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 120.041 195.791 166.487 1.00 35.80 ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 124.980 194.849 164.467 1.00 34.43 ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 124.674 194.329 163.139 1.00 32.59 ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 125.868 193.588 162.557 1.00 33.39 ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 125.711 192.522 161.954 1.00 34.25 ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 124.248 195.461 162.206 1.00 30.19 ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 122.931 196.174 162.505 1.00 34.20 ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 122.738 197.352 161.562 1.00 33.52 ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 121.760 195.218 162.424 1.00 32.22 ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 127.072 194.142 162.727 1.00 29.03 ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 128.270 193.472 162.232 1.00 27.34 ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 128.461 192.121 162.904 1.00 30.03 ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 128.782 191.129 162.240 1.00 32.33 ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 129.496 194.358 162.449 1.00 25.34 ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 128.255 192.059 164.221 1.00 30.05 ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 128.415 190.797 164.937 1.00 31.57 ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 127.404 189.758 164.463 1.00 33.82 ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 127.756 188.598 164.214 1.00 36.56 ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 128.286 191.031 166.442 1.00 31.61 ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 129.589 191.479 167.076 1.00 36.88 ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 130.597 191.590 166.346 1.00 39.08 ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 129.606 191.720 168.300 1.00 36.81 ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 126.137 190.159 164.325 1.00 29.13 ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 125.111 189.211 163.895 1.00 28.79 ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 125.353 188.738 162.466 1.00 29.94 ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 125.187 187.548 162.160 1.00 30.92 ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 123.724 189.843 164.024 1.00 30.55 ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 123.282 190.239 165.435 1.00 30.41 ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 121.789 190.511 165.475 1.00 29.69 ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 123.662 189.172 166.445 1.00 28.80 ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 125.749 189.655 161.578 1.00 29.65 ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 126.066 189.272 160.209 1.00 27.84 ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 127.248 188.318 160.172 1.00 27.28 ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 127.257 187.360 159.391 1.00 30.18 ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 126.354 190.519 159.370 1.00 22.80 ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 125.150 191.385 158.995 1.00 22.99 ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 125.574 192.524 158.084 1.00 21.12 ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 124.052 190.556 158.351 1.00 27.17 ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 128.256 188.558 161.014 1.00 22.90 ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 129.382 187.643 161.083 1.00 27.22 ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 128.979 186.260 161.552 1.00 29.81 ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 129.455 185.253 161.023 1.00 31.17 ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 128.096 186.189 162.551 1.00 27.95 ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 127.637 184.880 163.016 1.00 28.30 ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 126.867 184.139 161.926 1.00 28.71 ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 127.094 182.942 161.702 1.00 31.86 ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 126.784 185.025 164.276 1.00 27.80 ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 127.482 185.744 165.416 1.00 28.25 ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 126.732 185.581 166.730 1.00 30.10 ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 125.226 185.645 166.541 1.00 30.69 ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 124.553 186.256 167.719 1.00 30.08 ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 125.965 184.833 161.226 1.00 23.87 ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 125.235 184.177 160.140 1.00 24.20 ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 126.191 183.721 159.049 1.00 25.84 ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 126.073 182.605 158.525 1.00 26.92 ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 124.143 185.101 159.575 1.00 23.58 ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 123.178 185.528 160.670 1.00 29.73 ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 123.399 184.417 158.440 1.00 25.94 ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 122.114 186.435 160.155 1.00 30.68 ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 127.149 184.572 158.690 1.00 24.58 ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 128.113 184.233 157.651 1.00 21.64 ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 128.942 183.014 158.043 1.00 25.24 ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 129.223 182.146 157.209 1.00 27.47 ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 128.997 185.448 157.380 1.00 22.39 ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 130.352 185.143 156.813 1.00 24.50 ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 131.119 186.404 156.512 1.00 25.32 ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 130.558 187.498 156.505 1.00 26.90 ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 132.413 186.266 156.288 1.00 24.30 ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 129.344 182.933 159.313 1.00 26.35 ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 130.035 181.745 159.796 1.00 25.25 ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 129.113 180.537 159.882 1.00 25.16 ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 129.600 179.406 159.970 1.00 27.50 ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 130.663 182.017 161.164 1.00 25.27 ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 132.134 182.394 161.103 1.00 26.77 ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 132.314 183.815 160.600 1.00 27.37 ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 133.770 184.247 160.658 1.00 26.11 ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 133.962 185.601 160.069 1.00 26.46 ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 127.796 180.750 159.858 1.00 25.27 ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 126.826 179.662 159.909 1.00 26.25 ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 126.323 179.257 158.525 1.00 25.39 ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 125.165 178.852 158.383 1.00 23.73 ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 125.651 180.045 160.808 1.00 24.22 ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 127.173 179.355 157.497 1.00 26.57 ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 126.774 179.029 156.131 1.00 25.64 ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 127.745 178.066 155.455 1.00 27.14 ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 127.848 178.063 154.225 1.00 30.89 ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 126.638 180.301 155.290 1.00 22.91 ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 125.377 181.147 155.466 1.00 21.50 ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 125.232 182.124 154.314 1.00 19.88 ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 124.145 180.267 155.576 1.00 26.26 ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 128.463 177.248 156.229 1.00 26.23 ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 129.465 176.373 155.638 1.00 25.97 ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 128.880 175.287 154.752 1.00 27.75 ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 129.395 175.021 153.661 1.00 31.29 ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 127.809 174.634 155.212 1.00 29.58 ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 127.245 173.510 154.466 1.00 31.24 ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 126.677 173.959 153.125 1.00 30.37 ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 126.840 173.267 152.109 1.00 32.97 ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 126.171 172.818 155.303 1.00 31.88 ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 126.703 172.152 156.563 1.00 30.88 ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 125.657 171.305 157.262 1.00 34.17 ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 124.474 171.375 156.869 1.00 34.88 ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 126.018 170.571 158.205 1.00 32.70 ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 126.002 175.109 153.104 1.00 23.12 ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 125.503 175.650 151.846 1.00 27.04 ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 126.645 175.938 150.882 1.00 29.06 ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 126.539 175.669 149.679 1.00 29.93 ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 124.688 176.916 152.108 1.00 25.47 ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 124.098 177.520 150.858 1.00 26.73 ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 123.007 176.935 150.230 1.00 26.80 ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 124.636 178.672 150.303 1.00 24.90 ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 122.469 177.484 149.083 1.00 29.16 ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 124.104 179.228 149.160 1.00 25.03 ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 123.022 178.631 148.555 1.00 29.95 ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 122.493 179.184 147.412 1.00 31.56 ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 127.750 176.483 151.393 1.00 23.93 ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 128.899 176.761 150.542 1.00 18.38 ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 129.502 175.478 149.989 1.00 22.92 ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 129.913 175.431 148.826 1.00 26.58 ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 129.944 177.559 151.316 1.00 18.15 ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 129.563 179.017 151.560 1.00 20.81 ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 130.745 179.787 152.109 1.00 22.68 ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 129.051 179.649 150.278 1.00 19.62 ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 129.571 174.426 150.809 1.00 21.08 ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 130.085 173.149 150.321 1.00 18.54 ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 129.191 172.576 149.227 1.00 19.51 ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 129.683 172.062 148.212 1.00 22.76 ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 130.222 172.161 151.478 1.00 20.71 ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 131.577 172.202 152.167 1.00 22.60 ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 132.707 171.738 151.267 1.00 24.67 ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 132.583 170.651 150.667 1.00 26.98 ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 133.717 172.462 151.159 1.00 21.82 ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 127.872 172.660 149.410 1.00 18.15 ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 126.959 172.188 148.374 1.00 20.90 ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 127.118 172.992 147.087 1.00 22.50 ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 127.109 172.429 145.984 1.00 21.70 ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 125.516 172.253 148.872 1.00 23.56 ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 125.194 171.257 149.974 1.00 24.51 ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 123.724 171.299 150.380 1.00 25.45 ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 122.814 171.150 149.248 1.00 29.26 ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 122.224 172.156 148.616 1.00 30.96 ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 122.416 173.412 148.984 1.00 29.23 ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 121.421 171.894 147.588 1.00 28.11 ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 127.269 174.313 147.208 1.00 20.68 ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 127.464 175.145 146.024 1.00 17.40 ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 128.780 174.817 145.329 1.00 18.10 ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 128.857 174.840 144.096 1.00 19.57 ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 127.402 176.623 146.404 1.00 20.90 ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 125.998 177.118 146.707 1.00 20.86 ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 125.247 177.538 145.459 1.00 26.00 ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 125.879 177.634 144.386 1.00 28.38 ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 124.023 177.771 145.549 1.00 23.72 ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 129.828 174.517 146.102 1.00 15.07 ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 131.077 174.055 145.508 1.00 9.68  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 130.860 172.767 144.732 1.00 12.71 ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 131.409 172.588 143.640 1.00 15.38 ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 132.139 173.841 146.584 1.00 11.23 ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 132.646 175.099 147.252 1.00 11.01 ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 133.356 174.755 148.546 1.00 9.97  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 133.432 175.887 149.460 1.00 9.08  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 134.279 176.898 149.335 1.00 13.54 ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 135.145 176.953 148.337 1.00 13.71 ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 134.258 177.878 150.233 1.00 17.76 ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 130.074 171.847 145.293 1.00 18.87 ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 129.730 170.633 144.561 1.00 15.73 ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 128.984 170.954 143.271 1.00 15.42 ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 129.136 170.241 142.274 1.00 11.98 ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 128.898 169.700 145.439 1.00 16.81 ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 129.636 169.269 146.568 1.00 19.81 ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 128.175 172.016 143.273 1.00 20.16 ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 127.449 172.395 142.062 1.00 16.47 ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 128.398 172.869 140.965 1.00 14.38 ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 128.320 172.407 139.822 1.00 17.04 ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 126.419 173.477 142.386 1.00 16.87 ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 127.053 174.700 142.716 1.00 20.55 ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 129.295 173.793 141.291 1.00 15.72 ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 130.282 174.311 140.340 1.00 13.12 ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 131.675 173.976 140.851 1.00 11.50 ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 132.139 174.603 141.823 1.00 11.36 ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 130.121 175.819 140.152 1.00 14.13 ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 130.972 176.395 139.055 1.00 13.15 ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 130.807 175.990 137.743 1.00 15.18 ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 131.931 177.354 139.337 1.00 11.89 ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 131.586 176.523 136.734 1.00 12.26 ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 132.712 177.890 138.332 1.00 6.93  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 132.540 177.474 137.030 1.00 7.81  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 132.377 173.019 140.241 1.00 12.10 ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 133.600 172.486 140.866 1.00 10.65 ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 134.696 173.514 141.093 1.00 11.36 ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 135.433 173.401 142.080 1.00 11.33 ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 134.046 171.398 139.878 1.00 9.25  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 133.400 171.760 138.584 1.00 8.76  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 132.095 172.391 138.940 1.00 10.13 ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 134.830 174.515 140.220 1.00 7.52  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 135.898 175.497 140.382 1.00 4.65  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 135.749 176.302 141.666 1.00 9.52  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 136.738 176.862 142.155 1.00 9.32  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 135.947 176.425 139.170 1.00 5.44  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 136.260 175.705 137.874 1.00 4.00  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 136.511 176.674 136.737 1.00 4.41  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 136.846 175.979 135.499 1.00 3.63  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 138.035 176.019 134.916 1.00 5.25  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 139.035 176.717 135.432 1.00 9.72  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 138.228 175.345 133.788 1.00 4.96  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 134.546 176.338 142.245 1.00 9.86  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 134.350 177.009 143.523 1.00 4.90  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 135.157 176.356 144.634 1.00 7.47  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 135.317 176.955 145.702 1.00 11.51 ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 132.868 177.017 143.894 1.00 5.76  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 132.056 178.020 143.129 1.00 9.56  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 132.651 179.148 142.593 1.00 7.88  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 130.696 177.837 142.954 1.00 9.51  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 131.905 180.072 141.890 1.00 8.00  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 129.945 178.757 142.252 1.00 9.67  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 130.550 179.876 141.719 1.00 10.63 ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 135.658 175.138 144.413 1.00 7.07  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 136.543 174.508 145.381 1.00 5.17  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 137.839 175.283 145.565 1.00 8.74  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 138.520 175.096 146.579 1.00 11.15 ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 136.853 173.074 144.955 1.00 3.97  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 135.844 172.062 145.438 1.00 9.23  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 135.844 171.628 146.754 1.00 6.22  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 134.887 171.542 144.578 1.00 10.23 ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 134.923 170.704 147.201 1.00 10.59 ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 133.963 170.618 145.016 1.00 11.32 ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 133.984 170.204 146.328 1.00 14.63 ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 133.064 169.284 146.769 1.00 14.79 ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 138.197 176.150 144.616 1.00 8.80  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 139.417 176.941 144.707 1.00 4.62  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 139.152 178.353 145.213 1.00 8.56  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 140.035 179.213 145.129 1.00 11.28 ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 140.121 176.981 143.352 1.00 3.50  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 140.234 175.640 142.692 1.00 9.07  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 140.643 174.532 143.414 1.00 9.08  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 139.929 175.486 141.352 1.00 8.14  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 140.743 173.296 142.812 1.00 9.15  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 140.031 174.252 140.745 1.00 7.96  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 140.438 173.157 141.477 1.00 12.45 ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 137.959 178.602 145.740 1.00 10.86 ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 137.555 179.911 146.236 1.00 7.13  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 137.191 179.768 147.707 1.00 11.15 ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 136.441 178.858 148.079 1.00 14.13 ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 136.373 180.476 145.428 1.00 5.33  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 135.862 181.749 146.051 1.00 12.59 ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 136.791 180.722 143.993 1.00 5.97  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 137.722 180.661 148.537 1.00 10.21 ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 137.448 180.615 149.957 1.00 10.18 ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 136.003 180.944 150.276 1.00 16.26 ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 135.225 181.389 149.433 1.00 20.26 ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 135.638 180.708 151.540 1.00 15.65 ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 134.258 180.922 151.967 1.00 14.47 ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 133.848 182.383 151.829 1.00 15.91 ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 132.733 182.680 151.388 1.00 20.10 ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 134.075 180.445 153.406 1.00 19.18 ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 134.173 178.938 153.539 1.00 22.75 ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 133.836 178.231 152.567 1.00 19.37 ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 134.584 178.460 154.616 1.00 26.66 ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 134.738 183.308 152.199 1.00 18.84 ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 134.438 184.731 152.068 1.00 17.84 ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 134.120 185.089 150.623 1.00 19.86 ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 133.065 185.664 150.318 1.00 18.96 ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 135.634 185.553 152.555 1.00 21.36 ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 136.010 185.350 154.007 1.00 24.59 ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 134.981 185.908 154.956 1.00 29.14 ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 134.352 186.932 154.616 1.00 27.04 ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 134.793 185.322 156.042 1.00 27.07 ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 135.023 184.729 149.711 1.00 18.49 ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 134.853 185.091 148.314 1.00 15.02 ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 133.739 184.291 147.660 1.00 14.96 ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 133.077 184.793 146.748 1.00 21.96 ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 136.170 184.900 147.570 1.00 15.34 ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 137.348 185.478 148.325 1.00 21.39 ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 137.299 186.674 148.681 1.00 23.38 ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 138.322 184.736 148.567 1.00 18.13 ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 133.508 183.055 148.104 1.00 13.42 ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 132.379 182.297 147.576 1.00 14.17 ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 131.054 182.938 147.969 1.00 13.60 ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 130.134 183.026 147.148 1.00 17.65 ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 132.433 180.847 148.055 1.00 12.44 ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 131.400 179.939 147.388 1.00 11.14 ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 131.456 180.095 145.881 1.00 12.18 ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 131.614 178.498 147.786 1.00 12.66 ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 130.936 183.391 149.221 1.00 14.61 ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 129.740 184.122 149.628 1.00 11.86 ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 129.586 185.402 148.820 1.00 13.05 ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 128.475 185.757 148.410 1.00 16.55 ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 129.796 184.445 151.122 1.00 16.47 ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 129.717 183.293 152.125 1.00 18.22 ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 130.062 183.785 153.515 1.00 18.34 ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 128.348 182.650 152.122 1.00 18.32 ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 130.694 186.106 148.577 1.00 13.66 ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 130.629 187.322 147.770 1.00 11.17 ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 130.160 187.023 146.348 1.00 14.81 ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 129.366 187.780 145.778 1.00 20.36 ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 131.991 188.013 147.752 1.00 13.47 ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 132.053 189.227 146.841 1.00 19.14 ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 132.909 190.340 147.411 1.00 24.20 ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 133.356 190.212 148.571 1.00 22.44 ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 133.133 191.343 146.701 1.00 21.78 ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 130.643 185.928 145.759 1.00 15.17 ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 130.251 185.569 144.398 1.00 14.25 ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 128.777 185.190 144.347 1.00 17.41 ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 128.033 185.647 143.472 1.00 18.65 ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 131.138 184.429 143.865 1.00 13.83 ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 132.569 184.911 143.640 1.00 14.94 ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 130.568 183.868 142.573 1.00 14.67 ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 133.550 183.787 143.424 1.00 13.25 ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 128.333 184.343 145.279 1.00 13.99 ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 126.950 183.875 145.262 1.00 13.15 ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 125.990 185.031 145.505 1.00 17.95 ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 124.970 185.167 144.819 1.00 20.68 ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 126.750 182.750 146.293 1.00 14.55 ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 127.657 181.559 145.977 1.00 14.73 ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 125.298 182.307 146.321 1.00 17.54 ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 127.375 180.912 144.649 1.00 12.63 ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 126.298 185.882 146.486 1.00 14.95 ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 125.404 186.985 146.797 1.00 12.95 ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 125.331 188.025 145.695 1.00 14.71 ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 124.258 188.558 145.404 1.00 19.49 ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 126.469 188.327 145.066 1.00 15.80 ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 126.547 189.361 144.042 1.00 20.82 ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 126.409 188.806 142.631 1.00 24.01 ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 127.021 189.339 141.695 1.00 24.92 ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 127.857 190.138 144.183 1.00 20.35 ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 127.858 191.060 145.384 1.00 18.72 ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 128.586 190.838 146.350 1.00 19.27 ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 127.041 192.103 145.329 1.00 21.02 ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 125.630 187.737 142.452 1.00 24.78 ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 125.428 187.183 141.117 1.00 27.20 ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 124.698 188.171 140.214 1.00 29.00 ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 125.005 188.275 139.021 1.00 30.50 ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 124.659 185.866 141.206 1.00 26.64 ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 123.344 186.074 141.690 1.00 28.06 ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 123.720 188.896 140.763 1.00 26.50 ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 122.986 189.873 139.965 1.00 27.55 ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 123.893 191.002 139.493 1.00 29.94 ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 123.808 191.434 138.337 1.00 30.38 ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 121.813 190.435 140.769 1.00 28.57 ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 120.689 189.445 141.011 1.00 31.67 ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 119.539 190.094 141.762 1.00 31.65 ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 118.423 189.101 142.033 1.00 29.32 ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 117.293 189.723 142.775 1.00 29.88 ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 124.766 191.492 140.367 1.00 28.14 ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 125.673 192.592 140.042 1.00 27.21 ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 127.012 191.978 139.640 1.00 28.25 ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 127.892 191.756 140.472 1.00 26.89 ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 125.804 193.552 141.220 1.00 25.03 ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 126.793 194.666 140.958 1.00 30.31 ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 127.021 195.055 139.812 1.00 31.13 ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 127.370 195.205 142.023 1.00 29.05 ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 127.156 191.709 138.341 1.00 27.91 ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 128.314 190.987 137.826 1.00 24.04 ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 129.607 191.782 137.984 1.00 24.42 ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 130.689 191.187 138.060 1.00 27.79 ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 128.069 190.608 136.353 1.00 23.04 ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 129.214 189.774 135.801 1.00 24.67 ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 126.749 189.866 136.213 1.00 23.18 ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 129.525 193.112 138.055 1.00 24.42 ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 130.728 193.938 138.107 1.00 25.34 ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 131.598 193.641 139.322 1.00 24.35 ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 132.801 193.920 139.288 1.00 21.93 ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 130.348 195.418 138.092 1.00 27.94 ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 131.025 193.088 140.392 1.00 23.98 ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 131.803 192.751 141.578 1.00 26.59 ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 132.492 191.397 141.480 1.00 26.40 ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 133.353 191.099 142.314 1.00 27.73 ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 130.910 192.775 142.821 1.00 26.11 ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 130.176 194.085 143.031 1.00 26.50 ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 131.052 195.112 143.728 1.00 25.88 ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 131.505 194.616 145.091 1.00 28.40 ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 131.611 195.726 146.077 1.00 27.38 ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 132.138 190.575 140.494 1.00 19.09 ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 132.731 189.253 140.342 1.00 15.42 ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 134.032 189.267 139.556 1.00 19.32 ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 134.698 188.229 139.480 1.00 23.30 ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 131.744 188.306 139.654 1.00 14.94 ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 130.298 188.325 140.146 1.00 20.47 ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 129.444 187.398 139.303 1.00 19.88 ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 130.229 187.939 141.610 1.00 20.53 ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 134.413 190.408 138.977 1.00 16.04 ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 135.565 190.442 138.084 1.00 14.14 ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 136.865 190.125 138.811 1.00 15.15 ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 137.797 189.590 138.200 1.00 17.46 ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 135.657 191.805 137.400 1.00 14.45 ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 134.369 192.242 136.727 1.00 17.73 ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 134.216 191.674 135.332 1.00 16.25 ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 134.987 190.814 134.914 1.00 20.02 ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 133.215 192.152 134.606 1.00 14.20 ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 136.953 190.435 140.101 1.00 13.79 ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 138.175 190.182 140.852 1.00 15.31 ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 138.276 188.751 141.359 1.00 14.89 ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 139.289 188.400 141.971 1.00 15.26 ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 138.286 191.158 142.026 1.00 13.99 ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 137.193 191.020 143.068 1.00 12.62 ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 137.421 191.985 144.219 1.00 12.75 ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 136.343 191.855 145.280 1.00 13.64 ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 136.562 192.799 146.409 1.00 14.64 ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 137.262 187.920 141.122 1.00 10.50 ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 137.265 186.542 141.586 1.00 12.04 ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 137.525 185.530 140.480 1.00 11.59 ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 137.752 184.354 140.783 1.00 12.10 ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 135.930 186.211 142.265 1.00 13.24 ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 135.598 187.105 143.417 1.00 15.93 ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 136.257 187.038 144.626 1.00 14.09 ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 134.675 188.086 143.549 1.00 16.73 ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 135.756 187.939 145.451 1.00 13.71 ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 134.793 188.588 144.822 1.00 14.87 ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 137.496 185.946 139.212 1.00 13.67 ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 137.718 185.009 138.117 1.00 7.92  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 139.158 184.524 138.048 1.00 10.92 ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 139.413 183.464 137.470 1.00 13.24 ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 137.324 185.646 136.785 1.00 6.98  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 135.846 185.831 136.618 1.00 11.79 ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 135.016 184.741 136.429 1.00 12.56 ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 135.284 187.093 136.651 1.00 12.32 ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 133.654 184.906 136.277 1.00 10.49 ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 133.924 187.266 136.501 1.00 13.62 ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 133.110 186.171 136.313 1.00 15.61 ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 140.106 185.274 138.618 1.00 13.23 ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 141.500 184.851 138.594 1.00 9.99  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 141.761 183.661 139.504 1.00 8.39  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 142.779 182.983 139.340 1.00 13.72 ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 142.411 186.015 138.983 1.00 11.04 ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 142.295 186.437 140.437 1.00 14.19 ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 143.499 187.256 140.873 1.00 11.65 ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 143.575 188.571 140.116 1.00 12.86 ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 142.385 189.429 140.369 1.00 15.01 ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 140.870 183.391 140.459 1.00 5.71  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 141.047 182.261 141.361 1.00 5.87  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 140.439 180.975 140.820 1.00 8.67  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 140.804 179.891 141.286 1.00 9.99  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 140.436 182.582 142.726 1.00 4.66  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 140.623 184.024 143.151 1.00 11.38 ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 139.802 184.359 144.382 1.00 9.03  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 139.828 185.851 144.650 1.00 10.42 ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 138.975 186.228 145.806 1.00 9.98  ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 139.530 181.068 139.847 1.00 8.96  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 138.870 179.896 139.296 1.00 5.80  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 139.376 179.495 137.918 1.00 8.83  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 139.123 178.364 137.496 1.00 13.00 ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 137.354 180.125 139.214 1.00 5.70  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 136.777 180.881 140.395 1.00 6.96  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 134.979 181.000 140.340 1.00 14.26 ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 134.764 182.390 139.236 1.00 12.91 ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 140.079 180.379 137.215 1.00 8.58  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 140.545 180.105 135.867 1.00 6.06  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 142.043 180.361 135.778 1.00 10.93 ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 142.617 181.111 136.570 1.00 10.18 ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 139.802 180.959 134.833 1.00 4.78  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 138.334 180.657 134.737 1.00 7.79  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 137.432 181.256 135.598 1.00 10.14 ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 137.856 179.775 133.782 1.00 10.17 ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 136.081 180.981 135.510 1.00 5.74  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 136.508 179.497 133.691 1.00 8.13  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 135.620 180.100 134.555 1.00 6.70  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 142.675 179.717 134.794 1.00 10.39 ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 144.120 179.839 134.633 1.00 4.25  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 144.506 181.209 134.092 1.00 9.55  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 145.445 181.842 134.589 1.00 16.48 ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 144.642 178.735 133.716 1.00 4.23  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 143.795 181.687 133.075 1.00 7.73  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 144.163 182.933 132.435 1.00 7.26  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 143.021 183.908 132.258 1.00 7.20  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 143.200 184.976 131.667 1.00 13.35 ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 141.841 183.558 132.762 1.00 8.37  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 140.671 184.426 132.684 1.00 8.48  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 140.666 185.282 133.945 1.00 9.38  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 140.327 184.811 135.031 1.00 15.14 ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 139.377 183.628 132.535 1.00 7.96  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 138.187 184.563 132.422 1.00 5.98  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 139.456 182.708 131.333 1.00 12.20 ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 141.050 186.549 133.802 1.00 7.99  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 141.025 187.478 134.922 1.00 13.36 ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 139.744 188.296 134.980 1.00 16.68 ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 139.398 188.805 136.052 1.00 17.36 ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 142.227 188.425 134.853 1.00 10.99 ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 142.040 189.414 133.857 1.00 14.45 ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 139.036 188.429 133.862 1.00 11.06 ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 137.783 189.167 133.824 1.00 7.25  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 136.968 188.674 132.640 1.00 12.04 ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 137.493 188.031 131.728 1.00 20.58 ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 138.021 190.677 133.728 1.00 13.03 ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 138.445 191.041 132.426 1.00 14.97 ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 135.677 188.984 132.667 1.00 14.03 ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 134.768 188.620 131.591 1.00 13.09 ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 134.188 189.891 130.986 1.00 14.66 ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 134.079 190.934 131.639 1.00 19.37 ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 133.648 187.673 132.070 1.00 12.90 ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 132.899 188.279 133.257 1.00 13.68 ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 134.219 186.315 132.437 1.00 14.77 ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 131.522 187.695 133.465 1.00 14.57 ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 133.813 189.796 129.714 1.00 13.52 ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 133.310 190.927 128.943 1.00 14.78 ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 131.799 190.790 128.821 1.00 20.10 ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 131.296 189.730 128.435 1.00 20.54 ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 133.967 190.999 127.554 1.00 15.48 ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 135.490 191.028 127.685 1.00 18.67 ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 133.472 192.214 126.792 1.00 18.98 ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 136.215 190.746 126.391 1.00 16.44 ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 131.080 191.859 129.144 1.00 23.82 ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 129.629 191.879 129.071 1.00 23.13 ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 129.177 193.037 128.193 1.00 26.77 ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 129.957 193.924 127.837 1.00 26.54 ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 128.999 191.996 130.466 1.00 23.07 ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 129.148 190.811 131.424 1.00 22.39 ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 130.490 190.862 132.132 1.00 22.83 ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 128.014 190.768 132.427 1.00 25.52 ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 127.895 193.021 127.840 1.00 31.12 ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 127.310 194.088 127.038 1.00 29.64 ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 126.937 195.255 127.950 1.00 34.81 ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 127.278 195.285 129.135 1.00 35.13 ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 126.114 193.563 126.250 1.00 29.66 ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 125.078 192.902 127.135 1.00 33.64 ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 125.296 192.709 128.330 1.00 35.31 ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 123.941 192.548 126.550 1.00 35.13 ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 126.226 196.242 127.400 1.00 43.61 ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 125.845 197.410 128.186 1.00 44.97 ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 124.818 197.078 129.262 1.00 45.26 ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 124.765 197.768 130.284 1.00 46.77 ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 125.317 198.513 127.264 1.00 44.08 ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 123.812 198.498 127.021 1.00 46.24 ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 123.340 197.257 126.284 1.00 48.37 ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 122.136 196.938 126.365 1.00 48.92 ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 124.169 196.606 125.611 1.00 47.30 ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 124.006 196.040 129.057 1.00 40.04 ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 123.011 195.630 130.036 1.00 39.15 ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 123.632 194.769 131.132 1.00 40.17 ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 123.073 194.683 132.231 1.00 41.77 ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 121.881 194.884 129.293 1.00 38.38 ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 120.827 194.260 130.212 1.00 44.41 ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 120.750 194.573 131.415 1.00 44.43 ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 119.981 193.508 129.680 1.00 45.49 ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 124.815 194.204 130.882 1.00 35.85 ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 125.429 193.207 131.764 1.00 34.89 ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 124.527 191.986 131.915 1.00 33.06 ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 124.385 191.423 133.002 1.00 34.77 ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 125.784 193.795 133.134 1.00 34.88 ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 126.895 194.819 133.059 1.00 36.13 ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 127.331 195.201 131.974 1.00 35.82 ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 127.368 195.267 134.215 1.00 36.06 ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 123.915 191.573 130.807 1.00 30.19 ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 123.072 190.390 130.779 1.00 32.45 ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 123.568 189.319 129.822 1.00 33.10 ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 123.047 188.198 129.856 1.00 32.57 ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 121.632 190.766 130.398 1.00 31.45 ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 121.597 191.452 129.161 1.00 31.04 ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 124.539 189.627 128.968 1.00 25.95 ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 125.091 188.676 128.011 1.00 23.18 ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 126.606 188.695 128.141 1.00 23.79 ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 127.219 189.769 128.119 1.00 28.53 ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 124.665 189.009 126.567 1.00 22.18 ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 125.360 188.089 125.586 1.00 22.55 ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 123.157 188.905 126.420 1.00 22.59 ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 127.204 187.517 128.279 1.00 18.00 ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 128.654 187.388 128.379 1.00 16.71 ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 129.204 187.209 126.969 1.00 16.49 ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 129.071 186.140 126.370 1.00 18.53 ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 129.057 186.220 129.287 1.00 14.31 ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 130.566 186.065 129.311 1.00 12.47 ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 128.522 186.437 130.692 1.00 14.58 ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 129.822 188.263 126.437 1.00 14.99 ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 130.335 188.237 125.075 1.00 15.28 ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 131.682 187.534 124.960 1.00 15.56 ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 132.033 187.078 123.869 1.00 16.19 ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 130.460 189.663 124.536 1.00 19.00 ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 129.181 190.497 124.496 1.00 18.93 ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 129.451 191.849 123.863 1.00 16.08 ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 128.090 189.759 123.741 1.00 16.09 ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 132.437 187.440 126.046 1.00 14.28 ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 133.740 186.812 125.978 1.00 7.80  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 134.474 186.924 127.291 1.00 11.11 ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 133.880 187.208 128.333 1.00 18.02 ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 135.786 186.697 127.230 1.00 12.02 ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 136.647 186.712 128.403 1.00 10.49 ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 137.876 187.560 128.107 1.00 9.65  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 138.201 187.848 126.954 1.00 17.13 ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 137.070 185.294 128.837 1.00 10.92 ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 137.671 184.538 127.652 1.00 12.32 ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 135.888 184.539 129.421 1.00 13.02 ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 138.062 183.115 127.965 1.00 10.80 ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 138.562 187.959 129.175 1.00 10.69 ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 139.767 188.767 129.062 1.00 12.18 ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 140.814 188.250 130.038 1.00 10.68 ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 140.494 187.627 131.053 1.00 14.43 ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 139.480 190.250 129.328 1.00 14.86 ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 140.673 191.013 129.298 1.00 20.20 ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 142.075 188.513 129.717 1.00 8.85  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 143.196 188.130 130.561 1.00 15.53 ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 143.755 189.351 131.284 1.00 19.88 ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 143.354 190.490 131.041 1.00 22.88 ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 144.289 187.451 129.730 1.00 16.38 ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 144.829 188.343 128.773 1.00 18.34 ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 144.699 189.093 132.194 1.00 16.61 ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 145.294 190.177 132.968 1.00 20.78 ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 146.141 191.108 132.112 1.00 22.29 ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 146.433 192.230 132.542 1.00 23.72 ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 146.137 189.608 134.112 1.00 20.48 ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 147.142 188.556 133.683 1.00 21.69 ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 147.245 187.439 134.711 1.00 23.78 ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 146.023 186.651 134.795 1.00 28.74 ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 145.683 185.906 135.839 1.00 29.64 ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 146.451 185.828 136.913 1.00 26.59 ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 144.543 185.221 135.805 1.00 22.14 ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 146.539 190.677 130.919 1.00 21.46 ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 147.309 191.504 130.004 1.00 21.08 ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 146.436 192.255 129.007 1.00 23.37 ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 146.972 192.926 128.118 1.00 25.10 ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 148.330 190.648 129.247 1.00 20.47 ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 149.350 189.968 130.144 1.00 23.53 ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 148.913 188.584 130.577 1.00 26.97 ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 147.893 188.090 130.050 1.00 27.44 ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 149.584 187.988 131.444 1.00 25.58 ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 145.115 192.157 129.128 1.00 21.42 ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 144.206 192.817 128.219 1.00 23.59 ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 143.819 192.011 126.999 1.00 19.79 ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 142.969 192.463 126.223 1.00 21.12 ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 144.416 190.839 126.800 1.00 12.25 ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 144.045 189.994 125.675 1.00 15.50 ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 142.629 189.465 125.858 1.00 16.70 ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 142.252 189.014 126.941 1.00 19.24 ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 145.029 188.834 125.537 1.00 14.45 ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 144.907 188.068 124.239 1.00 10.21 ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 145.798 186.846 124.208 1.00 13.26 ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 145.492 185.871 124.925 1.00 19.09 ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 146.805 186.862 123.473 1.00 16.88 ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 141.842 189.520 124.787 1.00 10.56 ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 140.429 189.180 124.839 1.00 10.69 ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 140.126 188.019 123.906 1.00 12.92 ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 140.669 187.936 122.802 1.00 17.74 ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 139.557 190.381 124.463 1.00 12.93 ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 139.732 191.587 125.366 1.00 16.76 ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 139.221 192.864 124.734 1.00 21.65 ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 137.991 193.083 124.745 1.00 21.29 ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 140.048 193.650 124.226 1.00 21.20 ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 139.253 187.125 124.363 1.00 11.74 ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 138.717 186.040 123.553 1.00 10.98 ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 137.219 186.266 123.429 1.00 12.30 ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 136.504 186.287 124.438 1.00 15.54 ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 139.014 184.663 124.165 1.00 9.83  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 138.445 183.561 123.289 1.00 11.76 ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 140.506 184.481 124.351 1.00 9.07  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 136.745 186.432 122.198 1.00 10.27 ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 135.346 186.741 121.936 1.00 10.35 ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 134.593 185.451 121.644 1.00 12.47 ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 134.965 184.701 120.733 1.00 17.37 ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 135.225 187.716 120.767 1.00 13.52 ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 135.601 189.149 121.110 1.00 16.85 ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 134.750 189.776 122.571 1.00 26.87 ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 133.057 189.768 121.994 1.00 13.19 ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 133.540 185.192 122.413 1.00 12.44 ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 132.778 183.960 122.253 1.00 10.99 ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 132.045 183.947 120.917 1.00 13.01 ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 131.483 184.958 120.487 1.00 13.13 ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 131.773 183.804 123.394 1.00 9.57  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 132.398 183.486 124.722 1.00 8.29  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 133.741 183.161 124.816 1.00 13.89 ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 131.640 183.507 125.880 1.00 9.12  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 134.313 182.870 126.037 1.00 14.08 ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 132.207 183.216 127.103 1.00 9.57  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 133.545 182.896 127.181 1.00 11.20 ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 132.056 182.787 120.256 1.00 9.21  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 131.276 182.631 119.032 1.00 10.15 ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 129.784 182.592 119.339 1.00 15.18 ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 128.973 183.123 118.572 1.00 17.56 ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 131.707 181.368 118.288 1.00 9.02  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 133.165 180.997 118.487 1.00 11.51 ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 134.087 181.927 117.718 1.00 9.88  ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 134.416 181.371 116.344 1.00 12.16 ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 135.505 182.147 115.690 1.00 12.43 ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 129.406 181.967 120.449 1.00 13.00 ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 128.024 181.953 120.925 1.00 12.23 ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 127.981 182.608 122.297 1.00 13.20 ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 128.291 181.954 123.308 1.00 13.84 ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 127.475 180.529 120.992 1.00 12.98 ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 127.706 179.866 119.744 1.00 17.62 ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 125.983 180.546 121.282 1.00 13.23 ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 127.617 183.887 122.387 1.00 16.14 ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 127.650 184.575 123.681 1.00 14.60 ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 126.712 183.936 124.693 1.00 13.43 ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 125.630 183.453 124.357 1.00 17.87 ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 127.210 186.002 123.334 1.00 16.98 ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 127.442 186.135 121.865 1.00 16.86 ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 127.194 184.779 121.295 1.00 14.47 ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 127.145 183.943 125.950 1.00 14.38 ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 126.381 183.357 127.046 1.00 15.78 ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 125.420 184.404 127.591 1.00 19.23 ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 125.831 185.516 127.939 1.00 23.30 ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 127.317 182.841 128.151 1.00 14.79 ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 126.515 182.387 129.358 1.00 15.08 ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 128.182 181.710 127.623 1.00 16.21 ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 124.142 184.049 127.669 1.00 22.10 ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 123.101 184.948 128.152 1.00 24.76 ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 122.860 184.687 129.633 1.00 27.26 ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 122.589 183.550 130.030 1.00 30.12 ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 121.811 184.761 127.355 1.00 26.39 ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 120.769 185.566 127.875 1.00 28.65 ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 122.959 185.741 130.445 1.00 26.05 ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 122.734 185.587 131.877 1.00 25.36 ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 121.245 185.625 132.207 1.00 29.30 ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 120.810 185.017 133.192 1.00 31.39 ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 123.509 186.659 132.660 1.00 26.26 ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 124.932 186.793 132.114 1.00 25.21 ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 123.539 186.322 134.141 1.00 27.00 ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 125.820 187.699 132.934 1.00 24.35 ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 120.444 186.333 131.407 1.00 31.30 ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 119.003 186.355 131.643 1.00 31.03 ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 118.394 184.970 131.468 1.00 32.68 ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 117.525 184.563 132.248 1.00 34.26 ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 118.328 187.355 130.705 1.00 30.55 ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 118.712 187.082 129.352 1.00 33.56 ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 118.723 188.775 131.066 1.00 31.16 ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 118.833 184.232 130.447 1.00 30.12 ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 118.320 182.884 130.232 1.00 31.46 ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 118.744 181.934 131.345 1.00 33.33 ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 118.016 180.985 131.658 1.00 34.12 ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 118.787 182.352 128.878 1.00 34.09 ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 117.852 182.678 127.725 1.00 36.23 ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 117.947 181.670 126.598 1.00 37.48 ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 119.076 181.378 126.149 1.00 33.69 ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 116.890 181.166 126.161 1.00 36.27 ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 119.907 182.169 131.948 1.00 29.39 ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 120.457 181.301 132.989 1.00 27.30 ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 120.830 182.152 134.195 1.00 30.91 ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 122.009 182.438 134.434 1.00 35.69 ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 121.665 180.528 132.460 1.00 22.41 ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 121.456 179.947 131.097 1.00 30.39 ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 120.965 178.675 130.896 1.00 30.90 ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 121.662 180.468 129.864 1.00 30.65 ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 120.884 178.436 129.599 1.00 31.47 ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 121.302 179.508 128.951 1.00 30.50 ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 119.835 182.584 134.975 1.00 28.12 ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 120.123 183.502 136.090 1.00 26.83 ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 121.053 182.926 137.142 1.00 29.59 ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 121.792 183.689 137.777 1.00 32.45 ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 118.731 183.793 136.670 1.00 30.99 ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 117.762 183.391 135.596 1.00 30.27 ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 118.406 182.247 134.891 1.00 28.06 ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 121.035 181.612 137.358 1.00 26.46 ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 121.868 181.012 138.390 1.00 24.24 ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 123.345 181.216 138.076 1.00 25.76 ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 123.785 181.038 136.939 1.00 26.50 ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 121.556 179.523 138.523 1.00 25.61 ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 120.202 179.227 139.146 1.00 28.10 ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 120.098 177.775 139.586 1.00 30.43 ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 121.111 177.451 140.670 1.00 26.93 ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 121.181 178.515 141.708 1.00 27.88 ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 124.110 181.585 139.107 1.00 23.56 ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 125.520 181.929 138.921 1.00 20.19 ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 126.304 180.737 138.384 1.00 21.42 ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 127.073 180.859 137.421 1.00 26.47 ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 126.114 182.465 140.241 1.00 23.80 ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 127.556 182.935 140.049 1.00 20.05 ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 125.979 181.454 141.376 1.00 24.73 ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 127.689 184.133 139.162 1.00 22.63 ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 126.104 179.558 138.978 1.00 18.73 ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 126.879 178.390 138.579 1.00 18.20 ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 126.510 177.929 137.176 1.00 20.21 ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 127.376 177.478 136.417 1.00 24.55 ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 126.687 177.266 139.599 1.00 20.27 ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 125.235 176.858 139.761 1.00 26.84 ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 124.360 177.318 139.031 1.00 30.76 ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 124.976 175.988 140.729 1.00 25.08 ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 125.234 178.054 136.804 1.00 20.48 ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 124.797 177.601 135.486 1.00 21.81 ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 125.464 178.406 134.376 1.00 22.29 ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 126.076 177.837 133.459 1.00 25.39 ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 123.276 177.690 135.389 1.00 23.19 ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 122.717 177.412 134.008 1.00 29.70 ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 121.203 177.347 133.998 1.00 32.37 ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 120.595 177.487 135.079 1.00 29.18 ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 120.622 177.157 132.909 1.00 28.86 ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 125.380 179.737 134.444 1.00 15.87 ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 125.992 180.518 133.379 1.00 15.85 ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 127.508 180.564 133.512 1.00 16.28 ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 128.188 180.784 132.510 1.00 20.65 ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 125.404 181.934 133.308 1.00 17.25 ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 125.783 182.896 134.396 1.00 17.15 ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 125.032 183.246 135.477 1.00 16.84 ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 126.972 183.692 134.462 1.00 19.94 ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 125.696 184.180 136.233 1.00 18.91 ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 126.889 184.472 135.631 1.00 18.55 ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 128.110 183.807 133.657 1.00 19.99 ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 127.896 185.355 136.010 1.00 15.47 ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 129.107 184.682 134.039 1.00 14.94 ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 128.995 185.444 135.205 1.00 13.52 ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 128.058 180.320 134.704 1.00 11.85 ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 129.506 180.156 134.809 1.00 11.45 ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 129.975 178.905 134.071 1.00 16.23 ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 130.986 178.938 133.355 1.00 23.27 ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 129.921 180.105 136.278 1.00 12.28 ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 130.360 181.439 136.882 1.00 10.79 ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 130.707 181.275 138.350 1.00 14.15 ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 131.534 182.004 136.110 1.00 12.17 ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 129.250 177.795 134.229 1.00 10.95 ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 129.576 176.582 133.484 1.00 11.12 ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 129.417 176.805 131.986 1.00 11.76 ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 130.237 176.332 131.187 1.00 17.54 ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 128.689 175.426 133.948 1.00 12.03 ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 128.718 175.343 135.376 1.00 14.98 ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 129.177 174.114 133.361 1.00 11.83 ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 128.364 177.522 131.588 1.00 9.88  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 128.190 177.841 130.175 1.00 8.98  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 129.339 178.697 129.656 1.00 7.55  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 129.802 178.503 128.527 1.00 10.79 ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 126.852 178.544 129.958 1.00 11.80 ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 125.648 177.614 129.832 1.00 14.14 ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 124.373 178.368 130.134 1.00 15.33 ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 125.594 177.001 128.445 1.00 14.88 ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 129.810 179.646 130.466 1.00 8.29  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 130.936 180.489 130.070 1.00 9.77  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 132.190 179.650 129.879 1.00 10.57 ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 132.935 179.837 128.914 1.00 14.32 ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 131.152 181.609 131.105 1.00 7.61  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 132.561 182.165 131.009 1.00 6.89  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 130.136 182.715 130.901 1.00 12.89 ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 132.448 178.713 130.794 1.00 10.45 ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 133.627 177.857 130.664 1.00 5.26  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 133.547 176.985 129.411 1.00 7.90  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 134.525 176.860 128.654 1.00 13.62 ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 133.778 176.999 131.920 1.00 4.13  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 134.674 175.790 131.756 1.00 9.65  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 134.732 174.948 133.014 1.00 16.94 ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 133.670 174.727 133.633 1.00 15.52 ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 135.840 174.507 133.385 1.00 14.64 ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 132.380 176.381 129.170 1.00 7.10  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 132.213 175.545 127.984 1.00 2.80  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 132.380 176.360 126.709 1.00 6.14  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 133.030 175.910 125.754 1.00 8.86  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 130.847 174.863 128.009 1.00 6.03  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 130.704 173.793 129.075 1.00 13.02 ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 129.335 173.134 129.013 1.00 11.02 ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 129.211 172.013 130.029 1.00 9.38  ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 130.216 170.940 129.795 1.00 8.68  ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 131.803 177.562 126.673 1.00 7.81  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 131.954 178.420 125.506 1.00 4.10  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 133.394 178.875 125.331 1.00 6.73  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 133.853 179.030 124.198 1.00 8.75  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 131.025 179.626 125.611 1.00 4.83  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 130.878 180.395 124.314 1.00 11.70 ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 130.656 179.490 123.120 1.00 16.43 ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 129.688 178.701 123.142 1.00 18.25 ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 131.448 179.566 122.158 1.00 13.67 ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 134.117 179.096 126.430 1.00 6.20  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 135.538 179.407 126.342 1.00 3.33  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 136.289 178.297 125.626 1.00 4.77  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 137.051 178.548 124.683 1.00 11.14 ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 136.112 179.618 127.743 1.00 6.16  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 137.624 179.492 127.821 1.00 7.17  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 138.249 179.580 129.510 1.00 16.27 ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 138.153 177.861 130.001 1.00 4.33  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 136.073 177.052 126.054 1.00 6.15  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 136.751 175.933 125.405 1.00 2.83  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 136.364 175.822 123.933 1.00 3.84  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 137.229 175.641 123.064 1.00 6.28  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 136.447 174.631 126.143 1.00 0.43  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 137.049 174.564 127.530 1.00 2.16  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 136.837 173.203 128.156 1.00 4.00  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 137.593 173.056 129.394 1.00 11.47 ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 137.049 172.800 130.576 1.00 13.81 ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 135.742 172.657 130.720 1.00 10.59 ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 137.838 172.683 131.640 1.00 12.36 ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 135.070 175.950 123.629 1.00 4.16  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 134.608 175.786 122.252 1.00 3.15  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 135.167 176.886 121.353 1.00 7.00  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 135.621 176.618 120.233 1.00 13.40 ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 133.071 175.741 122.208 1.00 5.65  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 132.582 175.784 120.772 1.00 6.88  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 132.562 174.493 122.902 1.00 5.50  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 135.136 178.140 121.817 1.00 4.97  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 135.644 179.231 120.997 1.00 3.95  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 137.153 179.153 120.838 1.00 5.83  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 137.674 179.506 119.776 1.00 9.82  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 135.228 180.590 121.574 1.00 6.94  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 135.531 181.623 120.628 1.00 14.46 ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 135.955 180.896 122.871 1.00 6.89  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 137.874 178.673 121.856 1.00 4.69  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 139.307 178.472 121.688 1.00 2.63  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 139.585 177.401 120.642 1.00 6.03  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 140.486 177.558 119.812 1.00 7.01  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 139.953 178.111 123.023 1.00 3.87  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 140.367 179.305 123.882 1.00 1.17  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 141.129 178.840 125.103 1.00 5.58  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 141.200 180.281 123.072 1.00 2.43  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 138.807 176.315 120.651 1.00 8.20  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 138.989 175.277 119.641 1.00 2.67  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 138.706 175.805 118.237 1.00 2.81  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 139.459 175.528 117.294 1.00 8.07  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 138.094 174.080 119.953 1.00 4.02  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 137.624 176.571 118.079 1.00 4.87  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 137.281 177.095 116.759 1.00 5.81  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 138.315 178.103 116.272 1.00 6.83  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 138.695 178.100 115.090 1.00 8.84  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 135.886 177.714 116.789 1.00 6.80  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 134.774 176.701 116.997 1.00 6.43  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 133.409 177.366 117.005 1.00 9.76  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 132.296 176.335 117.105 1.00 11.24 ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 130.951 176.972 117.149 1.00 6.31  ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 138.787 178.976 117.164 1.00 7.88  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 139.824 179.927 116.791 1.00 5.81  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 141.123 179.212 116.450 1.00 5.95  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 141.858 179.646 115.559 1.00 8.07  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 140.039 180.937 117.916 1.00 4.79  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 138.971 182.014 118.093 1.00 7.98  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 139.171 182.744 119.409 1.00 5.13  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 138.993 182.987 116.930 1.00 8.96  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 141.426 178.112 117.145 1.00 7.65  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 142.601 177.322 116.795 1.00 6.56  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 142.457 176.712 115.410 1.00 8.39  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 143.425 176.661 114.644 1.00 14.85 ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 142.837 176.230 117.838 1.00 5.76  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 143.890 175.185 117.459 1.00 2.98  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 145.288 175.762 117.580 1.00 2.89  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 143.747 173.933 118.305 1.00 4.73  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 141.259 176.231 115.072 1.00 5.09  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 141.035 175.695 113.732 1.00 2.26  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 141.262 176.764 112.669 1.00 4.83  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 141.946 176.527 111.662 1.00 8.30  ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 139.622 175.122 113.627 1.00 4.50  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 140.701 177.957 112.884 1.00 9.66  ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 140.900 179.046 111.931 1.00 7.20  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 142.369 179.440 111.836 1.00 8.99  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 142.887 179.690 110.741 1.00 12.81 ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 140.047 180.252 112.318 1.00 5.76  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 138.568 179.948 112.472 1.00 10.47 ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 137.782 181.134 112.988 1.00 15.02 ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 138.406 182.168 113.307 1.00 15.88 ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 136.541 181.033 113.078 1.00 15.49 ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 143.060 179.497 112.977 1.00 10.10 ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 144.468 179.869 112.984 1.00 5.55  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 145.316 178.838 112.257 1.00 7.53  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 146.276 179.194 111.569 1.00 8.87  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 144.957 180.046 114.420 1.00 6.60  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 146.329 180.395 114.447 1.00 8.51  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 144.994 177.554 112.414 1.00 10.28 ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 145.722 176.510 111.696 1.00 10.44 ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 145.500 176.653 110.197 1.00 12.78 ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 146.443 176.577 109.398 1.00 15.28 ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 145.305 175.119 112.202 1.00 4.17  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 145.739 174.045 111.221 1.00 9.66  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 145.897 174.858 113.571 1.00 7.92  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 144.243 176.871 109.794 1.00 12.71 ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 143.953 177.068 108.377 1.00 12.76 ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 144.716 178.265 107.822 1.00 13.07 ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 145.175 178.243 106.674 1.00 19.55 ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 142.449 177.247 108.170 1.00 13.24 ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 141.753 176.122 108.722 1.00 16.87 ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 142.121 177.356 106.692 1.00 11.62 ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 144.874 179.314 108.628 1.00 13.69 ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 145.594 180.498 108.169 1.00 16.27 ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 147.101 180.258 108.112 1.00 18.65 ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 147.768 180.701 107.169 1.00 18.99 ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 145.276 181.685 109.077 1.00 14.12 ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 145.292 183.026 108.375 1.00 14.62 ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 144.647 184.116 109.204 1.00 21.30 ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 143.678 183.813 109.931 1.00 15.20 ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 145.107 185.274 109.129 1.00 26.44 ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 147.654 179.561 109.109 1.00 18.42 ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 149.102 179.373 109.196 1.00 17.55 ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 149.602 178.297 108.247 1.00 20.28 ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 150.809 178.222 107.993 1.00 21.56 ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 149.517 179.037 110.643 1.00 15.20 ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 149.048 177.646 111.028 1.00 14.08 ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 151.020 179.204 110.851 1.00 12.84 ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 148.707 177.467 107.701 1.00 23.19 ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 149.132 176.540 106.658 1.00 22.70 ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 149.712 177.262 105.449 1.00 24.04 ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 150.459 176.653 104.676 1.00 27.46 ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 147.967 175.653 106.213 1.00 20.88 ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 147.500 174.651 107.255 1.00 20.90 ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 148.302 173.367 107.230 1.00 26.48 ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 148.654 172.904 106.125 1.00 30.37 ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 148.578 172.818 108.317 1.00 24.51 ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 149.381 178.542 105.262 1.00 26.64 ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 149.967 179.318 104.173 1.00 27.61 ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 151.438 179.607 104.451 1.00 24.93 ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 152.292 179.464 103.568 1.00 25.96 ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 149.172 180.617 103.952 1.00 28.21 ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 147.688 180.304 103.749 1.00 27.79 ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 149.729 181.389 102.769 1.00 23.96 ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 147.418 179.341 102.616 1.00 24.66 ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 151.757 180.025 105.679 1.00 23.17 ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 153.145 180.320 106.023 1.00 24.89 ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 154.007 179.067 105.959 1.00 28.56 ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 155.153 179.115 105.499 1.00 33.63 ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 153.224 180.965 107.405 1.00 25.82 ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 152.300 182.132 107.578 1.00 27.07 ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 152.246 183.132 106.623 1.00 24.66 ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 151.486 182.231 108.691 1.00 22.96 ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 151.398 184.206 106.776 1.00 23.10 ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 150.636 183.303 108.848 1.00 24.17 ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 150.591 184.292 107.890 1.00 24.27 ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 153.479 177.939 106.426 1.00 29.01 ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 154.130 176.674 106.167 1.00 29.27 ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 154.088 176.334 104.691 1.00 35.03 ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 153.210 176.779 103.951 1.00 36.19 ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 155.070 175.546 104.253 1.00 43.73 ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 155.212 175.168 102.847 1.00 47.17 ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 155.406 176.391 101.954 1.00 46.96 ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 155.044 176.377 100.776 1.00 47.65 ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 154.013 174.340 102.370 1.00 44.10 ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 153.772 173.076 103.174 1.00 42.84 ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 152.380 172.515 102.923 1.00 45.68 ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 152.283 171.840 101.566 1.00 47.55 ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 150.982 171.136 101.388 1.00 45.33 ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 155.975 177.460 102.509 1.00 37.83 ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 156.217 178.697 101.780 1.00 37.52 ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 157.690 179.052 101.879 1.00 38.86 ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 158.267 179.028 102.971 1.00 37.81 ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 155.356 179.842 102.321 1.00 35.94 ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 158.299 179.381 100.737 1.00 40.04 ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 159.723 179.694 100.717 1.00 39.11 ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 160.002 181.047 101.360 1.00 39.32 ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 160.937 181.188 102.157 1.00 39.96 ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 160.247 179.662 99.282  1.00 39.94 ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 159.662 180.737 98.536  1.00 39.30 ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 159.891 178.340 98.618  1.00 38.81 ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 159.202 182.057 101.027 1.00 41.31 ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 159.358 183.399 101.568 1.00 40.11 ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 158.060 183.836 102.229 1.00 41.28 ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 156.971 183.612 101.692 1.00 41.77 ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 159.749 184.398 100.474 1.00 39.69 ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 158.694 184.579 99.547  1.00 39.62 ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 158.181 184.462 103.397 1.00 34.79 ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 157.037 184.912 104.180 1.00 35.99 ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 157.093 186.428 104.291 1.00 35.23 ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 158.118 186.987 104.697 1.00 34.21 ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 157.013 184.264 105.576 1.00 35.85 ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 157.297 182.765 105.473 1.00 33.04 ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 155.677 184.515 106.258 1.00 35.10 ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 157.307 182.062 106.803 1.00 30.01 ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 155.999 187.083 103.930 1.00 31.46 ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 155.901 188.528 104.088 1.00 30.06 ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 155.816 188.867 105.569 1.00 28.39 ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 154.943 188.332 106.265 1.00 30.23 ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 154.677 189.059 103.346 1.00 29.86 ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 154.719 190.563 103.150 1.00 31.78 ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 155.828 191.136 103.158 1.00 32.49 ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 153.642 191.173 102.987 1.00 29.59 ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 156.698 189.716 106.097 1.00 28.48 ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 156.614 190.058 107.527 1.00 27.31 ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 155.290 190.682 107.926 1.00 25.07 ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 154.810 190.432 109.038 1.00 25.37 ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 157.780 191.036 107.722 1.00 24.30 ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 158.731 190.720 106.616 1.00 24.26 ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 157.879 190.316 105.452 1.00 26.32 ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 154.681 191.487 107.052 1.00 21.47 ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 153.421 192.136 107.398 1.00 21.41 ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 152.296 191.122 107.560 1.00 23.76 ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 151.492 191.224 108.493 1.00 23.47 ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 153.062 193.176 106.339 1.00 24.66 ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 154.137 194.231 106.174 1.00 25.38 ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 154.563 194.854 107.145 1.00 25.59 ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 154.584 194.431 104.940 1.00 23.02 ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 152.223 190.134 106.663 1.00 22.41 ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 151.193 189.107 106.777 1.00 21.18 ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 151.375 188.278 108.043 1.00 17.03 ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 150.402 187.968 108.740 1.00 19.06 ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 151.210 188.206 105.543 1.00 19.18 ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 151.237 189.016 104.360 1.00 23.17 ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 149.976 187.321 105.513 1.00 17.10 ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 152.620 187.913 108.356 1.00 15.41 ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 152.883 187.151 109.572 1.00 13.79 ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 152.529 187.958 110.815 1.00 15.77 ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 151.968 187.418 111.773 1.00 20.30 ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 154.348 186.715 109.609 1.00 13.64 ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 154.591 185.465 110.421 1.00 16.56 ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 154.075 184.243 110.018 1.00 18.94 ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 155.337 185.507 111.590 1.00 14.29 ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 154.292 183.098 110.756 1.00 19.00 ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 155.558 184.368 112.335 1.00 14.16 ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 155.034 183.167 111.915 1.00 16.67 ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 155.254 182.028 112.655 1.00 14.20 ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 152.850 189.254 110.817 1.00 15.21 ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 152.519 190.101 111.958 1.00 13.25 ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 151.008 190.237 112.107 1.00 16.03 ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 150.478 190.222 113.226 1.00 16.37 ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 153.206 191.471 111.816 1.00 15.63 ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 154.702 191.346 112.112 1.00 12.84 ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 152.568 192.497 112.735 1.00 16.41 ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 155.007 190.831 113.496 1.00 13.24 ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 150.291 190.369 110.989 1.00 16.21 ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 148.834 190.433 111.049 1.00 14.78 ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 148.249 189.143 111.610 1.00 14.96 ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 147.335 189.177 112.443 1.00 16.22 ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 148.265 190.717 109.658 1.00 13.95 ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 148.830 191.931 109.148 1.00 18.22 ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 146.753 190.858 109.720 1.00 13.53 ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 148.770 187.995 111.171 1.00 11.97 ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 148.302 186.722 111.708 1.00 10.56 ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 148.597 186.607 113.199 1.00 9.71  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 147.768 186.106 113.966 1.00 11.79 ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 148.939 185.561 110.948 1.00 10.50 ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 148.746 184.238 111.618 1.00 14.97 ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 147.625 183.462 111.591 1.00 12.94 ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 149.699 183.537 112.423 1.00 13.63 ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 147.822 182.320 112.326 1.00 13.11 ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 149.089 182.343 112.849 1.00 10.13 ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 151.011 183.801 112.824 1.00 10.61 ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 149.742 181.417 113.655 1.00 7.97  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 151.658 182.882 113.626 1.00 9.83  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 151.024 181.705 114.033 1.00 9.46  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 149.777 187.060 113.623 1.00 8.59  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 150.138 187.008 115.038 1.00 8.71  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 149.184 187.866 115.859 1.00 12.60 ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 148.695 187.447 116.916 1.00 14.79 ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 151.600 187.451 115.231 1.00 9.08  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 152.557 186.343 114.794 1.00 8.37  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 151.862 187.839 116.677 1.00 10.59 ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 153.978 186.813 114.622 1.00 13.89 ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 148.902 189.079 115.380 1.00 13.70 ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 148.019 189.978 116.115 1.00 11.26 ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 146.578 189.491 116.111 1.00 10.73 ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 145.818 189.805 117.035 1.00 8.58  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 148.100 191.386 115.527 1.00 8.99  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 149.217 192.206 116.133 1.00 13.99 ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 149.593 191.934 117.292 1.00 15.69 ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 149.717 193.125 115.452 1.00 16.21 ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 146.180 188.731 115.090 1.00 9.01  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 144.788 188.302 114.989 1.00 10.15 ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 144.425 187.298 116.079 1.00 9.96  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 143.309 187.330 116.609 1.00 11.73 ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 144.523 187.713 113.606 1.00 11.89 ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 143.103 187.213 113.403 1.00 10.22 ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 142.842 186.873 111.945 1.00 10.63 ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 141.518 186.150 111.777 1.00 11.63 ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 140.382 186.935 112.331 1.00 11.72 ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 145.346 186.409 116.432 1.00 10.46 ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 145.050 185.296 117.323 1.00 5.03  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 145.803 185.434 118.640 1.00 6.40  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 146.725 186.241 118.784 1.00 12.35 ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 145.390 183.963 116.648 1.00 2.08  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 144.520 183.664 115.452 1.00 5.44  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 143.258 183.113 115.607 1.00 7.95  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 144.957 183.946 114.167 1.00 7.66  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 142.458 182.844 114.517 1.00 7.28  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 144.166 183.680 113.072 1.00 9.71  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 142.919 183.130 113.251 1.00 10.55 ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 142.127 182.863 112.159 1.00 14.39 ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 145.392 184.621 119.609 1.00 3.65  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 145.962 184.661 120.945 1.00 1.56  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 147.364 184.055 120.955 1.00 4.96  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 147.778 183.365 120.021 1.00 15.48 ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 145.060 183.915 121.930 1.00 4.71  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 143.796 184.670 122.318 1.00 10.58 ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 142.755 184.689 121.216 1.00 9.44  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 142.855 183.951 120.237 1.00 8.32  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 141.749 185.541 121.368 1.00 8.87  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 148.098 184.328 122.036 1.00 0.00  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 149.480 183.866 122.134 1.00 4.20  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 149.556 182.344 122.144 1.00 8.16  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 150.308 181.739 121.364 1.00 12.61 ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 150.135 184.447 123.386 1.00 1.43  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 148.783 181.703 123.022 1.00 7.38  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 148.780 180.248 123.049 1.00 3.10  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 148.293 179.679 121.725 1.00 2.69  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 148.800 178.650 121.270 1.00 10.41 ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 147.932 179.737 124.218 1.00 0.00  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 146.438 179.666 123.963 1.00 0.68  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 145.664 179.188 125.172 1.00 4.95  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 145.529 179.906 126.159 1.00 10.75 ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 145.147 177.967 125.100 1.00 3.78  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 147.357 180.365 121.065 1.00 2.98  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 146.834 179.866 119.800 1.00 2.53  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 147.862 179.982 118.682 1.00 2.92  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 147.990 179.068 117.863 1.00 7.01  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 145.550 180.604 119.434 1.00 2.96  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 144.339 180.208 120.276 1.00 3.57  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 143.076 180.741 119.651 1.00 6.67  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 144.262 178.698 120.438 1.00 2.47  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 148.608 181.088 118.625 1.00 2.85  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 149.611 181.218 117.571 1.00 4.75  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 150.758 180.239 117.801 1.00 4.05  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 151.274 179.636 116.851 1.00 7.64  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 150.106 182.674 117.441 1.00 3.90  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 148.962 183.591 117.050 1.00 5.43  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 150.768 183.163 118.711 1.00 1.67  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 151.162 180.042 119.061 1.00 2.94  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 152.206 179.058 119.341 1.00 1.20  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 151.731 177.655 118.975 1.00 2.56  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 152.468 176.872 118.361 1.00 13.18 ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 152.649 179.144 120.812 1.00 2.10  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 153.653 178.055 121.124 1.00 3.19  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 153.248 180.509 121.099 1.00 4.35  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 150.489 177.321 119.334 1.00 1.06  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 149.940 176.010 119.010 1.00 0.33  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 149.834 175.807 117.505 1.00 4.14  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 150.110 174.714 116.999 1.00 9.36  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 148.574 175.853 119.673 1.00 1.49  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 148.063 174.459 120.015 1.00 2.21  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 149.105 173.676 120.791 1.00 2.37  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 146.786 174.591 120.815 1.00 6.02  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 149.421 176.844 116.773 1.00 2.93  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 149.323 176.740 115.322 1.00 0.00  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 150.690 176.536 114.688 1.00 2.46  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 150.834 175.736 113.757 1.00 7.85  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 148.649 177.989 114.755 1.00 4.86  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 147.517 178.345 115.525 1.00 10.03 ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 151.706 177.255 115.177 1.00 2.74  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 153.059 177.046 114.671 1.00 2.26  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 153.526 175.621 114.937 1.00 4.43  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 154.125 174.981 114.063 1.00 8.97  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 154.017 178.053 115.303 1.00 3.73  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 153.252 175.106 116.139 1.00 2.58  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 153.642 173.737 116.462 1.00 0.00  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 152.935 172.730 115.564 1.00 0.42  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 153.557 171.780 115.077 1.00 3.92  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 153.350 173.443 117.932 1.00 0.00  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 154.200 174.248 118.889 1.00 1.64  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 153.880 173.971 120.339 1.00 1.13  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 154.769 173.674 121.135 1.00 5.86  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 152.607 174.067 120.693 1.00 6.84  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 151.635 172.924 115.333 1.00 2.73  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 150.879 172.010 114.479 1.00 3.23  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 151.422 172.037 113.057 1.00 3.40  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 151.606 170.989 112.426 1.00 8.22  ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 149.380 172.359 114.514 1.00 1.88  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 148.785 172.048 115.886 1.00 2.80  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 148.629 171.608 113.431 1.00 2.90  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 147.485 172.764 116.156 1.00 2.58  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 151.683 173.237 112.531 1.00 2.25  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 152.197 173.351 111.171 1.00 2.51  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 153.553 172.676 111.036 1.00 4.08  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 153.793 171.937 110.074 1.00 8.03  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 152.284 174.821 110.764 1.00 5.40  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 154.452 172.906 111.998 1.00 4.14  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 155.768 172.282 111.928 1.00 3.36  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 155.674 170.766 112.038 1.00 2.28  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 156.361 170.040 111.311 1.00 7.67  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 156.679 172.838 113.018 1.00 5.05  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 157.963 172.084 113.144 1.00 2.94  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 159.078 172.233 112.375 1.00 3.41  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 158.262 171.054 114.091 1.00 3.14  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 160.056 171.363 112.787 1.00 1.18  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 159.578 170.627 113.840 1.00 0.12  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 157.544 170.453 115.128 1.00 6.85  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 160.191 169.628 114.587 1.00 3.07  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 158.154 169.461 115.868 1.00 4.78  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 159.464 169.058 115.595 1.00 6.04  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 154.834 170.267 112.949 1.00 3.68  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 154.698 168.824 113.113 1.00 2.17  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 154.146 168.177 111.850 1.00 5.08  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 154.629 167.122 111.422 1.00 11.83 ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 153.801 168.514 114.308 1.00 2.19  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 154.316 169.095 115.493 1.00 4.99  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 153.137 168.798 111.235 1.00 6.29  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 152.582 168.244 110.006 1.00 3.38  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 153.589 168.303 108.865 1.00 7.07  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 153.669 167.374 108.054 1.00 12.09 ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 151.293 168.975 109.636 1.00 4.31  ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 150.114 168.605 110.524 1.00 10.71 ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 148.816 169.243 110.074 1.00 19.37 ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 148.857 170.109 109.176 1.00 16.89 ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 147.754 168.878 110.618 1.00 16.37 ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 154.374 169.382 108.787 1.00 7.24  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 155.404 169.471 107.755 1.00 5.08  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 156.452 168.380 107.927 1.00 7.70  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 156.870 167.749 106.949 1.00 11.33 ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 156.058 170.850 107.784 1.00 1.24  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 155.190 171.920 107.158 1.00 9.54  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 154.030 171.679 106.825 1.00 13.98 ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 155.747 173.113 106.994 1.00 14.01 ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 156.892 168.144 109.166 1.00 9.53  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 157.887 167.105 109.411 1.00 4.90  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 157.312 165.729 109.105 1.00 7.12  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 157.997 164.867 108.546 1.00 13.68 ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 158.412 167.191 110.855 1.00 1.59  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 159.339 166.027 111.148 1.00 6.29  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 159.138 168.501 111.073 1.00 3.81  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 156.048 165.495 109.467 1.00 8.13  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 155.420 164.215 109.159 1.00 6.75  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 155.327 163.995 107.654 1.00 11.36 ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 155.591 162.893 107.163 1.00 17.73 ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 154.035 164.140 109.802 1.00 4.46  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 153.528 162.728 110.019 1.00 9.64  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 153.900 162.177 111.379 1.00 14.98 ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 154.595 162.883 112.138 1.00 12.92 ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 153.497 161.038 111.692 1.00 15.32 ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 154.954 165.036 106.903 1.00 6.66  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 154.894 164.920 105.449 1.00 7.06  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 156.271 164.643 104.859 1.00 11.56 ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 156.417 163.796 103.968 1.00 13.39 ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 154.304 166.194 104.847 1.00 11.49 ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 153.019 166.450 105.430 1.00 16.61 ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 154.152 166.053 103.342 1.00 9.66  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 157.297 165.343 105.350 1.00 13.98 ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 158.650 165.119 104.850 1.00 12.30 ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 159.119 163.698 105.139 1.00 15.33 ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 159.722 163.049 104.277 1.00 20.85 ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 159.610 166.136 105.465 1.00 13.07 ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 158.847 163.198 106.345 1.00 13.74 ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 159.260 161.843 106.690 1.00 14.06 ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 158.494 160.806 105.877 1.00 17.36 ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 159.057 159.780 105.483 1.00 22.18 ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 159.081 161.604 108.188 1.00 13.50 ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 160.064 162.366 109.080 1.00 12.10 ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 160.001 161.866 110.510 1.00 10.71 ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 161.478 162.261 108.535 1.00 12.34 ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 157.210 161.055 105.610 1.00 16.72 ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 156.458 160.157 104.741 1.00 18.51 ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 157.038 160.150 103.332 1.00 22.15 ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 157.081 159.102 102.675 1.00 24.05 ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 154.984 160.560 104.715 1.00 17.33 ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 154.401 160.431 105.999 1.00 22.44 ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 157.478 161.313 102.847 1.00 22.88 ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 158.119 161.369 101.535 1.00 22.76 ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 159.435 160.598 101.524 1.00 24.16 ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 159.740 159.891 100.557 1.00 27.71 ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 158.346 162.824 101.125 1.00 23.81 ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 157.127 163.446 100.759 1.00 24.35 ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 160.229 160.722 102.590 1.00 26.14 ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 161.518 160.040 102.659 1.00 27.38 ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 161.410 158.576 103.067 1.00 31.82 ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 162.429 157.880 103.065 1.00 32.33 ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 162.459 160.753 103.634 1.00 24.57 ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 162.575 162.242 103.418 1.00 27.36 ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 163.348 163.088 104.805 1.00 36.13 ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 164.919 162.236 104.877 1.00 27.73 ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 160.213 158.106 103.431 1.00 35.37 ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 160.047 156.717 103.836 1.00 36.27 ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 160.639 155.706 102.875 1.00 41.34 ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 160.945 154.577 103.268 1.00 39.76 ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 160.810 156.085 101.607 1.00 44.01 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 161.440 155.194 100.649 1.00 44.50 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 162.920 154.978 100.889 1.00 47.05 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 163.493 154.029 100.342 1.00 45.79 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 163.551 155.830 101.694 1.00 45.20 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 164.965 155.695 101.980 1.00 44.63 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 165.848 156.322 100.921 1.00 48.08 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 166.611 157.251 101.207 1.00 44.92 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 165.746 155.824 99.689  1.00 48.86 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 166.522 156.363 98.589  1.00 46.27 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 165.972 157.628 97.974  1.00 47.85 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 166.576 158.160 97.036  1.00 46.51 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 164.841 158.119 98.472  1.00 49.29 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 164.242 159.333 97.944  1.00 50.34 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 165.041 160.560 98.381  1.00 48.23 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 166.028 160.471 99.118  1.00 45.14 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 162.789 159.457 98.404  1.00 47.48 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 161.910 158.347 97.866  1.00 48.46 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 162.210 157.830 96.769  1.00 48.33 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 160.920 157.992 98.539  1.00 46.85 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 164.596 161.725 97.916  1.00 43.59 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 165.226 162.980 98.288  1.00 43.43 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 164.942 163.295 99.756  1.00 43.77 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 164.299 162.527 100.477 1.00 43.07 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 164.739 164.107 97.379  1.00 39.06 ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 165.434 164.449 100.208 1.00 36.37 ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 165.295 164.880 101.598 1.00 31.58 ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 164.538 166.200 101.647 1.00 32.81 ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 165.148 167.280 101.599 1.00 30.07 ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 166.661 165.009 102.269 1.00 28.10 ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 163.206 166.165 101.729 1.00 32.37 ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 162.440 167.389 101.990 1.00 27.51 ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 162.497 167.862 103.434 1.00 21.75 ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 161.862 168.873 103.758 1.00 25.40 ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 161.008 166.990 101.600 1.00 27.13 ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 160.974 165.515 101.742 1.00 25.88 ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 162.337 165.038 101.353 1.00 27.33 ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 163.218 167.162 104.313 1.00 15.23 ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 163.459 167.687 105.653 1.00 17.36 ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 164.263 168.977 105.600 1.00 23.30 ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 164.103 169.849 106.464 1.00 24.11 ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 164.185 166.648 106.507 1.00 17.44 ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 163.328 165.760 107.410 1.00 17.34 ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 164.212 164.844 108.236 1.00 15.35 ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 162.442 166.603 108.306 1.00 14.72 ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 165.133 169.115 104.596 1.00 20.43 ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 165.844 170.372 104.404 1.00 15.53 ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 164.874 171.506 104.099 1.00 16.62 ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 165.101 172.648 104.509 1.00 19.57 ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 166.874 170.230 103.284 1.00 18.40 ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 168.131 169.533 103.705 1.00 22.29 ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 168.528 168.328 103.167 1.00 22.90 ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 169.077 169.872 104.610 1.00 18.92 ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 169.667 167.955 103.723 1.00 21.07 ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 170.021 168.874 104.603 1.00 18.99 ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 163.788 171.210 103.383 1.00 17.97 ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 162.765 172.224 103.145 1.00 16.16 ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 162.112 172.664 104.450 1.00 15.11 ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 161.860 173.857 104.657 1.00 21.71 ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 161.712 171.693 102.173 1.00 17.81 ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 162.283 171.421 100.905 1.00 24.59 ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 161.830 171.711 105.344 1.00 12.12 ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 161.250 172.053 106.640 1.00 13.14 ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 162.215 172.914 107.443 1.00 15.89 ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 161.818 173.915 108.053 1.00 19.62 ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 160.864 170.774 107.406 1.00 9.78  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 160.270 171.126 108.755 1.00 8.44  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 159.890 169.943 106.590 1.00 16.24 ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 163.497 172.540 107.455 1.00 15.26 ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 164.488 173.333 108.178 1.00 11.47 ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 164.609 174.732 107.592 1.00 13.96 ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 164.734 175.713 108.332 1.00 17.25 ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 165.842 172.627 108.163 1.00 11.28 ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 166.953 173.336 108.936 1.00 9.53  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 166.607 173.415 110.413 1.00 7.71  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 168.285 172.635 108.733 1.00 14.31 ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 164.580 174.846 106.262 1.00 11.83 ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 164.673 176.152 105.623 1.00 11.89 ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 163.467 177.018 105.955 1.00 15.77 ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 163.609 178.220 106.203 1.00 20.78 ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 164.815 175.986 104.110 1.00 13.57 ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 166.099 175.491 103.771 1.00 17.79 ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 162.267 176.432 105.954 1.00 14.11 ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 161.077 177.193 106.324 1.00 13.28 ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 161.154 177.656 107.773 1.00 12.30 ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 160.817 178.806 108.088 1.00 16.25 ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 159.824 176.351 106.092 1.00 14.38 ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 158.550 177.174 106.125 1.00 25.03 ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 158.281 177.892 107.087 1.00 23.24 ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 157.757 177.076 105.065 1.00 26.01 ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 161.602 176.774 108.671 1.00 13.25 ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 161.745 177.147 110.075 1.00 12.66 ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 162.745 178.285 110.220 1.00 13.87 ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 162.512 179.243 110.963 1.00 15.43 ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 162.151 175.924 110.917 1.00 11.39 ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 162.610 176.357 112.296 1.00 7.03  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 160.992 174.948 111.028 1.00 9.25  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 163.869 178.204 109.502 1.00 12.69 ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 164.887 179.245 109.592 1.00 9.34  ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 164.387 180.567 109.024 1.00 13.10 ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 164.692 181.633 109.569 1.00 16.44 ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 166.160 178.798 108.875 1.00 7.96  ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 167.144 178.070 109.772 1.00 11.57 ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 168.270 177.417 108.996 1.00 19.99 ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 168.124 177.244 107.768 1.00 18.54 ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 169.303 177.080 109.613 1.00 17.65 ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 163.628 180.524 107.929 1.00 13.84 ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 163.079 181.750 107.349 1.00 10.81 ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 162.109 182.410 108.321 1.00 11.78 ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 162.155 183.627 108.548 1.00 16.25 ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 162.409 181.449 105.998 1.00 8.73  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 161.515 182.602 105.577 1.00 14.05 ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 163.460 181.179 104.936 1.00 13.61 ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 161.218 181.613 108.917 1.00 11.18 ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 160.269 182.174 109.872 1.00 10.34 ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 160.984 182.710 111.107 1.00 9.62  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 160.598 183.749 111.655 1.00 12.22 ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 159.230 181.126 110.260 1.00 9.89  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 158.807 180.415 109.092 1.00 15.43 ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 158.024 181.794 110.887 1.00 9.82  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 162.032 182.017 111.556 1.00 8.45  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 162.807 182.489 112.698 1.00 5.60  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 163.522 183.795 112.379 1.00 8.86  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 163.620 184.679 113.236 1.00 12.14 ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 163.805 181.414 113.126 1.00 2.56  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 164.339 181.495 114.555 1.00 2.24  ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 163.199 181.629 115.545 1.00 1.71  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 165.175 180.269 114.866 1.00 6.96  ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 164.038 183.931 111.156 1.00 8.89  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 164.651 185.188 110.744 1.00 8.78  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 163.627 186.315 110.726 1.00 11.32 ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 163.921 187.439 111.146 1.00 14.77 ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 165.298 185.032 109.367 1.00 10.00 ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 166.570 184.213 109.413 1.00 15.72 ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 167.209 184.094 110.458 1.00 15.05 ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 166.946 183.639 108.275 1.00 16.45 ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 162.415 186.030 110.243 1.00 10.12 ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 161.356 187.037 110.255 1.00 9.86  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 161.040 187.462 111.684 1.00 12.75 ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 160.909 188.657 111.979 1.00 9.35  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 160.105 186.506 109.530 1.00 8.50  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 158.919 187.426 109.771 1.00 8.05  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 160.375 186.356 108.044 1.00 12.70 ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 160.921 186.492 112.593 1.00 13.87 ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 160.628 186.812 113.989 1.00 8.93  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 161.752 187.624 114.624 1.00 9.78  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 161.495 188.582 115.365 1.00 15.50 ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 160.387 185.529 114.782 1.00 8.35  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 159.181 184.672 114.406 1.00 6.74  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 159.291 183.307 115.053 1.00 7.34  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 157.894 185.350 114.818 1.00 7.40  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 163.005 187.248 114.356 1.00 8.77  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 164.141 187.970 114.921 1.00 8.67  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 164.214 189.392 114.387 1.00 12.09 ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 164.571 190.319 115.122 1.00 16.76 ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 165.438 187.217 114.631 1.00 9.07  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 163.898 189.583 113.105 1.00 12.01 ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 163.809 190.933 112.564 1.00 12.33 ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 162.691 191.716 113.239 1.00 17.40 ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 162.844 192.909 113.529 1.00 21.54 ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 163.590 190.880 111.052 1.00 12.76 ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 164.823 190.422 110.301 1.00 18.50 ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 165.818 190.056 110.959 1.00 19.99 ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 164.795 190.426 109.053 1.00 17.33 ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 161.556 191.061 113.491 1.00 15.47 ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 160.425 191.743 114.116 1.00 15.04 ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 160.756 192.194 115.534 1.00 13.63 ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 160.378 193.296 115.944 1.00 20.83 ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 159.199 190.832 114.115 1.00 14.66 ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 158.802 190.520 112.791 1.00 18.10 ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 161.452 191.353 116.305 1.00 12.16 ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 161.786 191.725 117.679 1.00 14.74 ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 162.940 192.709 117.766 1.00 17.97 ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 163.248 193.190 118.863 1.00 17.64 ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 162.129 190.500 118.546 1.00 13.85 ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 160.968 189.531 118.565 1.00 11.17 ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 163.393 189.826 118.047 1.00 12.52 ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 163.593 193.019 116.645 1.00 17.68 ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 164.655 194.015 116.636 1.00 18.17 ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 164.126 195.438 116.535 1.00 22.97 ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 164.921 196.382 116.588 1.00 24.71 ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 165.621 193.742 115.483 1.00 17.72 ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 166.758 192.765 115.777 1.00 21.04 ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 167.533 192.446 114.510 1.00 22.98 ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 167.681 193.329 116.842 1.00 19.53 ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 162.816 195.614 116.390 1.00 26.73 ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 162.193 196.924 116.298 1.00 26.12 ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 161.076 197.023 117.328 1.00 26.41 ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 160.670 196.029 117.935 1.00 26.39 ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 161.656 197.190 114.885 1.00 24.28 ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 160.973 195.996 114.244 1.00 25.61 ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 160.496 196.308 112.535 1.00 39.41 ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 159.300 195.001 112.276 1.00 26.79 ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 160.587 198.245 117.526 1.00 31.18 ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 159.583 198.497 118.553 1.00 30.74 ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 158.271 197.806 118.201 1.00 32.39 ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 157.773 197.927 117.079 1.00 36.08 ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 159.366 199.999 118.715 1.00 32.19 ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 158.190 200.368 119.600 1.00 33.75 ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 158.607 200.663 121.025 1.00 37.22 ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 159.816 200.564 121.322 1.00 38.09 ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 157.729 200.996 121.849 1.00 34.20 ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 157.715 197.084 119.165 1.00 23.57 ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 156.468 196.352 119.024 1.00 23.88 ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 155.597 196.597 120.245 1.00 21.06 ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 156.103 196.941 121.318 1.00 20.55 ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 156.716 194.844 118.862 1.00 19.02 ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 157.748 194.473 117.811 1.00 18.90 ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 157.175 194.457 116.409 1.00 18.75 ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 155.996 194.744 116.204 1.00 19.64 ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 158.008 194.117 115.435 1.00 19.88 ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 154.281 196.443 120.111 1.00 17.56 ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 153.423 196.498 121.289 1.00 12.80 ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 153.757 195.372 122.242 1.00 18.08 ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 154.217 194.292 121.820 1.00 19.02 ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 152.010 196.345 120.704 1.00 13.90 ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 152.136 196.789 119.293 1.00 17.59 ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 153.505 196.368 118.863 1.00 17.32 ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 153.558 195.577 123.549 1.00 18.36 ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 153.989 194.557 124.522 1.00 15.37 ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 153.359 193.192 124.309 1.00 11.97 ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 154.046 192.174 124.451 1.00 13.67 ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 153.577 195.170 125.869 1.00 12.28 ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 153.478 196.637 125.609 1.00 12.23 ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 152.982 196.762 124.205 1.00 12.99 ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 152.072 193.135 123.958 1.00 8.00  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 151.426 191.846 123.738 1.00 11.12 ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 152.010 191.147 122.518 1.00 12.76 ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 152.338 189.953 122.566 1.00 15.87 ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 149.918 192.036 123.584 1.00 15.62 ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 149.070 190.763 123.562 1.00 12.28 ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 149.123 190.072 124.910 1.00 11.66 ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 147.637 191.082 123.179 1.00 11.29 ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 152.158 191.879 121.413 1.00 9.38  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 152.794 191.306 120.234 1.00 7.78  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 154.254 190.972 120.503 1.00 10.86 ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 154.774 190.002 119.950 1.00 17.21 ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 152.675 192.261 119.048 1.00 10.26 ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 153.136 191.661 117.732 1.00 11.01 ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 153.520 192.737 116.738 1.00 12.06 ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 152.358 193.470 116.253 1.00 11.99 ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 152.421 194.595 115.555 1.00 13.33 ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 153.579 195.157 115.253 1.00 17.01 ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 151.293 195.170 115.150 1.00 13.07 ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 154.925 191.758 121.346 1.00 7.59  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 156.307 191.445 121.700 1.00 5.98  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 156.402 190.116 122.438 1.00 10.54 ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 157.284 189.298 122.151 1.00 15.20 ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 156.897 192.575 122.542 1.00 9.56  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 158.407 192.528 122.674 1.00 9.95  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 158.870 193.324 123.882 1.00 14.36 ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 158.607 192.617 125.130 1.00 17.85 ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 157.961 193.140 126.163 1.00 15.22 ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 157.495 194.379 126.131 1.00 15.01 ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 157.776 192.402 127.253 1.00 9.20  ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 155.496 189.875 123.390 1.00 12.36 ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 155.499 188.597 124.098 1.00 6.37  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 155.131 187.449 123.165 1.00 4.47  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 155.698 186.353 123.267 1.00 11.57 ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 154.548 188.651 125.293 1.00 6.67  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 154.858 189.773 126.267 1.00 9.49  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 155.565 189.266 127.512 1.00 12.06 ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 154.774 188.287 128.248 1.00 13.86 ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 153.815 188.599 129.109 1.00 16.03 ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 153.485 189.857 129.350 1.00 12.72 ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 153.175 187.623 129.748 1.00 15.11 ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 154.186 187.679 122.249 1.00 2.11  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 153.860 186.654 121.262 1.00 4.73  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 155.071 186.315 120.403 1.00 10.07 ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 155.344 185.139 120.131 1.00 14.34 ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 152.699 187.116 120.384 1.00 5.83  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 151.349 187.135 121.075 1.00 5.75  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 150.249 187.504 120.096 1.00 3.94  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 148.933 187.742 120.807 1.00 6.57  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 147.879 188.208 119.868 1.00 8.26  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 155.812 187.337 119.970 1.00 5.84  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 157.005 187.111 119.165 1.00 2.61  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 158.075 186.370 119.956 1.00 5.96  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 158.778 185.518 119.408 1.00 11.56 ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 157.551 188.443 118.648 1.00 5.45  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 156.740 189.183 117.583 1.00 7.02  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 157.238 190.608 117.442 1.00 11.91 ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 156.814 188.462 116.256 1.00 5.45  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 158.225 186.693 121.242 1.00 5.72  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 159.196 185.980 122.069 1.00 1.53  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 158.830 184.506 122.209 1.00 3.87  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 159.697 183.626 122.104 1.00 7.52  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 159.299 186.638 123.444 1.00 1.68  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 159.944 188.010 123.427 1.00 6.59  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 159.850 188.712 124.767 1.00 14.05 ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 159.298 188.115 125.713 1.00 15.17 ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 160.329 189.860 124.873 1.00 14.24 ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 157.547 184.217 122.445 1.00 3.54  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 157.108 182.827 122.534 1.00 2.27  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 157.335 182.096 121.218 1.00 4.84  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 157.786 180.942 121.205 1.00 9.42  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 155.633 182.764 122.925 1.00 2.15  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 155.328 183.393 124.248 1.00 3.88  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 154.049 183.471 124.753 1.00 4.06  ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 156.132 183.970 125.170 1.00 7.52  ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 154.078 184.074 125.927 1.00 7.54  ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 155.332 184.386 126.206 1.00 6.86  ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 157.025 182.755 120.100 1.00 3.42  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 157.235 182.140 118.797 1.00 5.04  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 158.713 181.889 118.536 1.00 5.34  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 159.084 180.856 117.971 1.00 9.64  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 156.633 183.016 117.702 1.00 4.00  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 155.159 182.751 117.407 1.00 1.05  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 154.654 183.703 116.347 1.00 4.84  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 154.958 181.310 116.974 1.00 1.77  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 159.577 182.823 118.941 1.00 1.99  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 161.012 182.627 118.773 1.00 0.48  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 161.482 181.427 119.579 1.00 4.75  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 162.249 180.597 119.084 1.00 12.25 ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 161.786 183.901 119.162 1.00 3.18  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 161.668 184.953 118.065 1.00 2.48  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 163.248 183.582 119.419 1.00 4.89  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 162.328 186.252 118.414 1.00 4.35  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 161.033 181.313 120.830 1.00 5.02  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 161.423 180.164 121.645 1.00 2.14  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 160.985 178.856 120.993 1.00 1.52  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 161.785 177.918 120.836 1.00 6.12  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 160.828 180.290 123.047 1.00 2.90  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 161.169 181.566 123.601 1.00 5.05  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 161.361 179.193 123.952 1.00 6.23  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 159.716 178.789 120.581 1.00 1.64  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 159.201 177.559 119.990 1.00 1.36  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 159.926 177.212 118.698 1.00 3.52  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 160.255 176.046 118.459 1.00 10.19 ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 157.698 177.675 119.743 1.00 3.78  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 157.001 176.360 119.379 1.00 7.03  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 157.431 175.149 120.213 1.00 13.69 ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 157.879 175.309 121.370 1.00 15.21 ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 157.324 174.019 119.694 1.00 9.70  ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 160.197 178.208 117.854 1.00 4.61  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 160.847 177.927 116.581 1.00 1.52  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 162.334 177.636 116.733 1.00 0.06  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 162.892 176.910 115.910 1.00 7.54  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 160.623 179.081 115.607 1.00 2.48  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 159.371 178.947 114.738 1.00 1.70  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 158.091 179.110 115.537 1.00 6.77  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 159.423 179.951 113.618 1.00 4.80  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 162.992 178.167 117.764 1.00 0.43  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 164.355 177.729 118.057 1.00 3.09  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 164.355 176.261 118.457 1.00 5.29  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 165.208 175.479 118.012 1.00 5.80  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 164.993 178.617 119.140 1.00 1.08  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 166.325 178.042 119.571 1.00 5.76  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 165.210 180.016 118.605 1.00 1.33  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 163.390 175.856 119.289 1.00 3.60  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 163.279 174.437 119.619 1.00 0.00  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 163.016 173.598 118.372 1.00 2.47  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 163.612 172.527 118.197 1.00 10.97 ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 162.176 174.213 120.650 1.00 0.00  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 161.895 172.769 120.921 1.00 3.09  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 162.872 171.886 121.329 1.00 2.88  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 160.752 172.050 120.835 1.00 4.43  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 162.341 170.687 121.484 1.00 1.86  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 161.055 170.760 121.192 1.00 5.61  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 162.127 174.070 117.497 1.00 1.99  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 161.810 173.332 116.277 1.00 0.00  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 163.021 173.227 115.358 1.00 0.86  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 163.249 172.183 114.740 1.00 4.80  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 160.646 174.001 115.550 1.00 0.46  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 159.343 173.972 116.318 1.00 3.40  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 158.203 174.600 115.553 1.00 4.66  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 158.415 175.298 114.564 1.00 5.60  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 156.982 174.363 116.012 1.00 7.99  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 163.798 174.305 115.244 1.00 4.68  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 165.004 174.275 114.425 1.00 2.21  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 166.020 173.292 114.983 1.00 4.05  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 166.644 172.540 114.226 1.00 7.55  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 165.605 175.677 114.331 1.00 1.65  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 166.915 175.745 113.571 1.00 5.00  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 167.641 177.047 113.856 1.00 7.62  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 168.007 177.170 115.261 1.00 8.95  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 168.428 178.291 115.829 1.00 10.36 ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 168.552 179.412 115.140 1.00 7.43  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 168.737 178.287 117.123 1.00 7.11  ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 166.202 173.281 116.307 1.00 3.46  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 167.114 172.315 116.910 1.00 0.00  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 166.653 170.886 116.652 1.00 4.19  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 167.461 170.015 116.308 1.00 10.95 ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 167.239 172.579 118.410 1.00 3.32  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 167.919 173.899 118.717 1.00 13.02 ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 168.395 174.558 117.769 1.00 13.25 ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 167.976 174.278 119.905 1.00 9.22  ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 165.349 170.629 116.798 1.00 7.67  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 164.825 169.282 116.583 1.00 4.18  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 164.996 168.864 115.128 1.00 3.01  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 165.369 167.722 114.836 1.00 7.67  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 163.353 169.203 117.028 1.00 0.00  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 162.703 167.942 116.490 1.00 3.54  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 163.262 169.241 118.537 1.00 0.29  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 164.720 169.772 114.191 1.00 0.09  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 164.856 169.445 112.776 1.00 0.00  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 166.314 169.204 112.402 1.00 4.46  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 166.616 168.303 111.610 1.00 9.94  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 164.258 170.558 111.918 1.00 5.56  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 162.907 170.800 112.324 1.00 7.31  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 164.264 170.158 110.454 1.00 7.14  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 167.230 169.999 112.958 1.00 3.50  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 168.651 169.767 112.719 1.00 0.96  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 169.082 168.414 113.266 1.00 6.71  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 169.868 167.702 112.632 1.00 11.43 ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 169.479 170.886 113.345 1.00 2.65  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 169.508 172.168 112.535 1.00 6.32  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 170.250 173.262 113.276 1.00 5.38  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 170.373 174.476 112.480 1.00 8.41  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 170.831 175.631 112.941 1.00 13.58 ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 171.228 175.764 114.196 1.00 7.79  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 170.895 176.677 112.123 1.00 13.70 ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 168.581 168.047 114.448 1.00 6.60  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 168.887 166.731 115.001 1.00 3.05  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 168.338 165.618 114.117 1.00 6.59  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 169.000 164.595 113.909 1.00 15.59 ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 168.327 166.615 116.418 1.00 5.61  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 168.422 165.286 116.895 1.00 13.34 ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 167.122 165.796 113.595 1.00 5.24  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 166.529 164.783 112.726 1.00 5.07  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 167.328 164.622 111.439 1.00 9.27  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 167.548 163.498 110.972 1.00 14.73 ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 165.078 165.144 112.408 1.00 5.41  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 164.032 164.926 113.500 1.00 4.71  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 162.638 165.113 112.933 1.00 3.56  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 164.180 163.550 114.120 1.00 8.60  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 167.757 165.736 110.845 1.00 9.86  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 168.562 165.668 109.628 1.00 10.84 ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 169.909 165.018 109.914 1.00 10.85 ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 170.387 164.179 109.139 1.00 14.66 ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 168.724 167.071 109.018 1.00 9.37  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 167.372 167.604 108.544 1.00 10.41 ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 169.715 167.042 107.867 1.00 8.04  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 167.408 169.049 108.113 1.00 9.83  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 170.541 165.388 111.030 1.00 8.73  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 171.849 164.837 111.370 1.00 12.18 ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 171.783 163.339 111.632 1.00 14.11 ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 172.761 162.623 111.388 1.00 15.93 ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 172.419 165.568 112.585 1.00 11.94 ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 173.850 165.199 112.931 1.00 14.72 ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 174.313 165.911 114.191 1.00 15.18 ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 175.791 165.671 114.451 1.00 13.68 ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 176.642 166.226 113.363 1.00 12.72 ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 170.646 162.845 112.120 1.00 14.28 ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 170.480 161.424 112.398 1.00 15.15 ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 170.049 160.625 111.178 1.00 15.60 ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 169.840 159.413 111.300 1.00 17.61 ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 169.465 161.227 113.527 1.00 14.78 ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 169.949 161.756 114.748 1.00 15.36 ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 169.913 161.267 110.015 1.00 15.15 ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 169.512 160.598 108.777 1.00 19.48 ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 168.176 159.879 108.944 1.00 19.59 ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 168.031 158.706 108.598 1.00 19.63 ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 170.596 159.630 108.294 1.00 18.90 ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 171.968 160.263 108.141 1.00 19.88 ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 172.106 160.981 106.810 1.00 22.89 ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 172.271 159.998 105.665 1.00 22.69 ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 171.697 160.526 104.396 1.00 20.05 ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 167.192 160.591 109.483 1.00 18.60 ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 165.882 160.011 109.759 1.00 17.34 ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 165.042 160.060 108.492 1.00 21.59 ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 164.855 161.127 107.898 1.00 25.27 ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 165.190 160.758 110.909 1.00 18.71 ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 166.053 160.695 112.165 1.00 18.29 ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 163.820 160.165 111.181 1.00 15.27 ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 166.292 159.302 112.646 1.00 16.63 ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 164.527 158.903 108.077 1.00 22.57 ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 163.711 158.821 106.876 1.00 21.54 ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 162.338 158.212 107.111 1.00 20.15 ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 161.504 158.243 106.202 1.00 25.78 ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 164.437 158.013 105.789 1.00 23.25 ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 164.906 156.660 106.285 1.00 25.06 ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 164.788 156.395 107.500 1.00 25.34 ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 165.392 155.861 105.460 1.00 28.44 ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 162.072 157.669 108.297 1.00 14.02 ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 160.808 157.012 108.598 1.00 12.71 ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 160.068 157.802 109.666 1.00 12.97 ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 160.664 158.209 110.668 1.00 16.48 ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 161.035 155.573 109.063 1.00 12.97 ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 159.780 154.729 108.979 1.00 16.59 ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 158.953 154.915 108.088 1.00 18.78 ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 159.633 153.797 109.913 1.00 14.81 ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 158.768 158.016 109.449 1.00 9.25  ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 157.954 158.726 110.428 1.00 8.07  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 157.708 157.901 111.683 1.00 11.76 ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 157.264 158.452 112.695 1.00 15.19 ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 156.620 159.137 109.807 1.00 9.94  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 157.978 156.599 111.638 1.00 10.20 ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 157.824 155.725 112.792 1.00 6.25  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 159.118 155.536 113.569 1.00 5.32  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 159.146 154.742 114.513 1.00 8.45  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 157.283 154.362 112.353 1.00 9.04  ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 156.059 154.447 111.459 1.00 12.67 ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 154.901 155.109 112.184 1.00 11.38 ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 154.385 154.233 113.312 1.00 11.73 ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 153.198 154.834 113.981 1.00 14.78 ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 160.189 156.223 113.186 1.00 5.10  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 161.426 156.162 113.951 1.00 7.87  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 161.237 156.827 115.308 1.00 6.35  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 160.613 157.884 115.416 1.00 10.20 ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 162.557 156.842 113.183 1.00 10.48 ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 163.728 156.935 113.975 1.00 12.72 ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 161.779 156.195 116.354 1.00 10.37 ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 161.634 156.741 117.698 1.00 5.88  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 162.337 158.079 117.865 1.00 6.26  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 161.979 158.842 118.767 1.00 11.16 ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 162.162 155.757 118.740 1.00 3.24  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 161.706 156.063 120.136 1.00 1.75  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 160.409 155.788 120.530 1.00 2.19  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 162.569 156.643 121.048 1.00 2.81  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 159.986 156.076 121.811 1.00 3.65  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 162.150 156.931 122.329 1.00 3.82  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 160.859 156.647 122.711 1.00 8.13  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 163.326 158.379 117.025 1.00 6.27  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 163.937 159.702 117.055 1.00 6.83  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 162.936 160.785 116.676 1.00 10.78 ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 163.092 161.943 117.078 1.00 10.41 ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 165.157 159.718 116.136 1.00 4.12  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 166.312 158.882 116.672 1.00 8.99  ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 166.336 157.467 116.121 1.00 17.91 ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 166.063 157.279 114.920 1.00 18.51 ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 166.631 156.534 116.898 1.00 17.92 ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 161.903 160.429 115.913 1.00 9.27  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 160.783 161.327 115.667 1.00 2.41  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 159.616 161.081 116.612 1.00 7.03  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 158.912 162.031 116.973 1.00 18.64 ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 160.309 161.196 114.216 1.00 5.51  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 159.043 161.945 113.911 1.00 7.05  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 157.896 161.427 113.384 1.00 5.22  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 158.793 163.343 114.115 1.00 6.86  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 156.952 162.413 113.245 1.00 3.59  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 157.477 163.597 113.686 1.00 5.25  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 159.555 164.401 114.618 1.00 6.85  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 156.905 164.864 113.748 1.00 9.01  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 158.985 165.658 114.676 1.00 6.27  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 157.673 165.879 114.244 1.00 9.91  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 159.395 159.832 117.030 1.00 6.20  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 158.282 159.543 117.929 1.00 3.04  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 158.522 160.085 119.331 1.00 4.33  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 157.563 160.421 120.032 1.00 11.50 ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 158.017 158.040 117.992 1.00 1.36  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 157.521 157.371 116.715 1.00 3.89  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 157.445 155.872 116.920 1.00 11.21 ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 156.171 157.929 116.311 1.00 6.01  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 159.782 160.175 119.762 1.00 3.21  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 160.067 160.694 121.092 1.00 2.71  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 159.817 162.190 121.207 1.00 8.76  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 159.807 162.714 122.326 1.00 14.15 ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 161.513 160.385 121.483 1.00 6.66  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 162.412 160.799 120.471 1.00 9.63  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 159.624 162.885 120.092 1.00 12.32 ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 159.323 164.305 120.122 1.00 11.42 ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 157.849 164.529 120.446 1.00 9.88  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 157.027 163.612 120.397 1.00 14.62 ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 159.667 164.959 118.784 1.00 10.76 ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 161.050 164.623 118.259 1.00 12.25 ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 162.153 165.084 119.186 1.00 16.20 ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 162.090 166.174 119.751 1.00 17.52 ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 163.177 164.254 119.346 1.00 16.00 ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 157.522 165.774 120.781 1.00 9.41  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 156.141 166.178 121.009 1.00 9.66  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 155.563 166.643 119.678 1.00 13.14 ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 155.979 167.672 119.137 1.00 16.17 ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 156.064 167.273 122.067 1.00 10.55 ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 154.665 167.532 122.585 1.00 10.09 ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 154.670 168.353 124.186 1.00 19.17 ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 154.230 166.992 125.261 1.00 18.82 ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 154.605 165.885 119.151 1.00 7.37  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 154.061 166.106 117.823 1.00 5.42  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 152.580 166.440 117.922 1.00 4.17  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 151.838 165.809 118.679 1.00 1.91  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 154.274 164.873 116.942 1.00 4.79  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 155.569 164.138 117.257 1.00 3.99  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 155.682 162.824 116.509 1.00 7.22  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 154.634 161.877 116.867 1.00 7.86  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 154.632 161.144 117.972 1.00 5.05  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 155.590 161.252 118.875 1.00 3.59  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 153.641 160.281 118.175 1.00 5.42  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 152.157 167.437 117.152 1.00 8.36  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 150.793 167.949 117.192 1.00 4.20  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 150.097 167.594 115.886 1.00 5.78  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 150.581 167.948 114.806 1.00 10.22 ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 150.784 169.460 117.419 1.00 4.53  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 151.485 169.890 118.676 1.00 3.89  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 152.867 169.930 118.740 1.00 2.94  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 150.760 170.252 119.795 1.00 3.25  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 153.509 170.320 119.894 1.00 2.97  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 151.397 170.645 120.951 1.00 5.32  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 152.774 170.678 121.000 1.00 7.01  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 148.967 166.902 115.988 1.00 2.56  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 148.200 166.466 114.831 1.00 6.49  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 146.828 167.121 114.864 1.00 8.61  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 146.121 167.039 115.873 1.00 14.32 ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 148.063 164.944 114.808 1.00 6.12  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 149.390 164.223 114.782 1.00 9.08  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 150.352 164.536 113.833 1.00 11.76 ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 149.683 163.235 115.712 1.00 6.00  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 151.568 163.885 113.807 1.00 9.33  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 150.896 162.579 115.694 1.00 8.85  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 151.833 162.906 114.739 1.00 12.04 ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 153.042 162.254 114.716 1.00 10.87 ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 146.457 167.764 113.765 1.00 7.33  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 145.175 168.443 113.643 1.00 8.68  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 144.299 167.697 112.648 1.00 15.66 ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 144.750 167.359 111.549 1.00 18.38 ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 145.362 169.894 113.201 1.00 9.60  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 144.208 170.781 113.552 1.00 8.57  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 143.918 171.066 114.874 1.00 9.67  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 143.408 171.323 112.564 1.00 10.07 ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 142.857 171.877 115.202 1.00 12.99 ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 142.344 172.134 112.886 1.00 13.25 ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 142.068 172.410 114.208 1.00 15.67 ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 143.050 167.442 113.038 1.00 18.26 ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 142.070 166.762 112.194 1.00 16.68 ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 140.881 167.690 111.997 1.00 20.76 ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 139.949 167.703 112.816 1.00 25.89 ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 141.637 165.435 112.813 1.00 16.74 ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 140.904 164.547 111.830 1.00 24.40 ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 140.859 164.894 110.632 1.00 24.91 ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 140.372 163.499 112.256 1.00 25.59 ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 140.869 168.491 110.929 1.00 21.34 ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 139.720 169.377 110.687 1.00 23.69 ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 138.426 168.634 110.408 1.00 26.41 ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 137.349 169.225 110.547 1.00 24.97 ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 140.164 170.205 109.473 1.00 23.48 ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 141.190 169.361 108.797 1.00 20.29 ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 141.906 168.630 109.892 1.00 20.78 ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 138.493 167.361 110.018 1.00 28.02 ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 137.294 166.589 109.725 1.00 27.46 ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 136.588 166.087 110.976 1.00 28.02 ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 135.476 165.560 110.869 1.00 32.65 ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 137.639 165.401 108.821 1.00 26.23 ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 138.590 165.735 107.682 1.00 27.85 ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 138.070 166.890 106.840 1.00 30.61 ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 137.175 166.396 105.715 1.00 30.71 ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 136.505 167.524 105.008 1.00 30.86 ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 137.199 166.230 112.148 1.00 24.22 ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 136.561 165.799 113.383 1.00 25.51 ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 135.376 166.701 113.703 1.00 28.45 ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 135.503 167.929 113.713 1.00 27.98 ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 137.568 165.817 114.532 1.00 25.83 ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 137.003 165.370 115.866 1.00 25.42 ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 137.187 163.887 116.108 1.00 29.71 ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 138.237 163.323 115.798 1.00 29.68 ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 136.167 163.246 116.666 1.00 29.37 ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 134.218 166.089 113.959 1.00 31.60 ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 133.025 166.867 114.278 1.00 32.97 ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 133.185 167.612 115.596 1.00 32.76 ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 132.803 168.783 115.705 1.00 30.63 ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 131.798 165.956 114.323 1.00 31.56 ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 132.002 164.928 115.301 1.00 32.57 ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 131.561 165.316 112.965 1.00 28.55 ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 133.746 166.954 116.606 1.00 26.91 ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 133.954 167.578 117.906 1.00 23.39 ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 135.182 168.477 117.840 1.00 24.47 ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 136.301 167.990 117.650 1.00 30.48 ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 134.116 166.513 118.988 1.00 21.54 ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 133.968 167.076 120.386 1.00 25.91 ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 133.637 168.271 120.517 1.00 29.35 ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 134.184 166.319 121.357 1.00 27.54 ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 134.972 169.785 117.993 1.00 19.46 ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 136.078 170.734 117.903 1.00 18.27 ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 137.090 170.499 119.015 1.00 18.72 ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 138.290 170.734 118.834 1.00 21.35 ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 135.548 172.180 117.915 1.00 16.50 ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 134.799 172.477 116.629 1.00 18.86 ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 134.647 172.406 119.117 1.00 17.69 ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 136.632 170.031 120.177 1.00 13.67 ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 137.529 169.781 121.298 1.00 13.92 ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 138.427 168.570 121.080 1.00 15.04 ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 139.361 168.367 121.862 1.00 16.39 ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 136.719 169.602 122.582 1.00 14.67 ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 135.901 170.809 123.045 1.00 12.24 ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 135.464 170.637 124.489 1.00 12.59 ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 136.688 172.095 122.873 1.00 9.52  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 138.171 167.768 120.048 1.00 14.94 ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 138.963 166.579 119.760 1.00 13.15 ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 139.736 166.689 118.453 1.00 15.86 ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 140.334 165.703 118.014 1.00 18.46 ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 138.063 165.343 119.730 1.00 16.14 ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 137.359 165.054 121.041 1.00 18.43 ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 138.167 164.152 121.948 1.00 19.60 ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 138.666 164.583 122.986 1.00 18.02 ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 138.302 162.890 121.559 1.00 18.83 ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 139.740 167.863 117.820 1.00 14.60 ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 140.414 168.004 116.534 1.00 14.04 ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 141.929 167.991 116.679 1.00 12.37 ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 142.636 167.635 115.731 1.00 15.16 ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 139.964 169.290 115.841 1.00 13.33 ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 138.492 169.316 115.475 1.00 14.90 ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 138.170 170.379 114.445 1.00 20.05 ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 138.638 171.512 114.539 1.00 21.25 ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 137.365 170.016 113.454 1.00 19.28 ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 142.446 168.369 117.843 1.00 9.86  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 143.879 168.455 118.080 1.00 7.28  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 144.319 167.342 119.022 1.00 9.50  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 143.685 167.111 120.055 1.00 9.99  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 144.256 169.816 118.665 1.00 7.17  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 145.685 169.937 119.192 1.00 3.02  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 146.689 169.768 118.068 1.00 5.89  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 145.882 171.266 119.884 1.00 3.35  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 145.401 166.660 118.657 1.00 7.35  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 145.997 165.621 119.484 1.00 3.27  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 147.480 165.911 119.651 1.00 6.89  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 148.152 166.324 118.702 1.00 13.78 ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 145.800 164.234 118.864 1.00 5.93  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 146.326 163.222 119.702 1.00 11.20 ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 147.988 165.707 120.863 1.00 6.38  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 149.396 165.917 121.175 1.00 3.78  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 149.981 164.578 121.593 1.00 4.55  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 149.510 163.967 122.559 1.00 11.84 ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 149.584 166.970 122.277 1.00 0.57  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 148.724 168.200 121.983 1.00 0.00  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 151.044 167.355 122.397 1.00 8.07  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 148.594 169.140 123.149 1.00 6.53  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 151.002 164.124 120.877 1.00 2.38  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 151.561 162.798 121.085 1.00 3.98  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 153.044 162.888 121.406 1.00 3.82  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 153.784 163.650 120.780 1.00 12.94 ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 151.345 161.915 119.856 1.00 5.49  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 149.920 161.915 119.340 1.00 4.33  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 149.659 160.796 118.356 1.00 10.66 ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 150.532 159.971 118.092 1.00 11.15 ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 148.451 160.759 117.807 1.00 12.33 ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 153.468 162.102 122.391 1.00 1.37  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 154.879 161.945 122.720 1.00 0.38  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 155.126 160.476 123.023 1.00 6.18  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 154.566 159.942 123.984 1.00 13.05 ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 155.284 162.821 123.907 1.00 1.20  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 156.736 163.257 123.875 1.00 4.22  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 157.167 164.386 125.208 1.00 12.74 ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 158.814 164.875 124.709 1.00 1.96  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 155.960 159.833 122.204 1.00 6.87  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 156.196 158.387 122.254 1.00 2.83  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 154.849 157.705 122.048 1.00 6.05  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 154.218 157.937 121.003 1.00 9.63  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 156.941 158.027 123.540 1.00 0.44  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 154.371 156.883 122.976 1.00 3.15  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 153.062 156.257 122.850 1.00 3.52  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 151.965 157.031 123.569 1.00 5.54  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 150.805 156.610 123.531 1.00 9.29  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 153.111 154.823 123.383 1.00 5.84  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 153.384 154.766 124.870 1.00 10.15 ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 154.447 155.173 125.334 1.00 10.21 ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 152.419 154.261 125.629 1.00 8.94  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 152.298 158.144 124.214 1.00 3.51  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 151.322 158.899 124.986 1.00 2.15  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 150.558 159.859 124.086 1.00 4.34  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 151.159 160.623 123.327 1.00 4.11  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 152.014 159.666 126.110 1.00 2.31  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 149.231 159.818 124.173 1.00 6.03  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 148.352 160.691 123.409 1.00 3.63  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 147.496 161.510 124.365 1.00 5.04  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 146.952 160.975 125.336 1.00 11.53 ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 147.452 159.890 122.466 1.00 5.21  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 148.201 159.085 121.423 1.00 8.08  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 147.263 158.159 120.670 1.00 9.22  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 148.011 157.348 119.625 1.00 7.58  ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 149.050 156.479 120.243 1.00 6.81  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 147.374 162.804 124.084 1.00 2.83  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 146.605 163.710 124.921 1.00 3.74  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 145.744 164.601 124.042 1.00 5.04  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 146.074 164.868 122.884 1.00 8.93  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 147.510 164.583 125.798 1.00 1.46  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 148.561 163.816 126.542 1.00 4.26  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 148.272 163.228 127.761 1.00 3.92  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 149.836 163.686 126.027 1.00 4.44  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 149.235 162.524 128.448 1.00 3.14  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 150.802 162.983 126.710 1.00 4.73  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 150.501 162.401 127.923 1.00 3.74  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 144.637 165.061 124.611 1.00 5.22  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 143.777 166.046 123.978 1.00 5.83  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 144.016 167.402 124.624 1.00 9.74  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 144.178 167.498 125.843 1.00 15.65 ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 142.303 165.657 124.109 1.00 7.77  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 141.899 164.565 123.140 1.00 15.19 ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 142.479 164.428 122.062 1.00 17.95 ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 140.900 163.777 123.519 1.00 11.20 ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 144.055 168.447 123.803 1.00 4.75  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 144.224 169.791 124.335 1.00 1.42  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 143.024 170.162 125.194 1.00 5.36  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 141.875 170.057 124.757 1.00 9.96  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 144.397 170.795 123.198 1.00 3.37  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 145.160 172.042 123.585 1.00 3.29  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 146.532 172.006 123.773 1.00 4.42  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 144.508 173.251 123.763 1.00 3.71  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 147.232 173.141 124.127 1.00 7.82  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 145.198 174.393 124.117 1.00 0.90  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 146.561 174.331 124.298 1.00 4.77  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 147.260 175.461 124.650 1.00 8.00  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 143.293 170.592 126.427 1.00 4.41  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 142.218 170.958 127.330 1.00 6.38  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 141.512 172.240 126.951 1.00 8.34  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 140.379 172.464 127.392 1.00 11.85 ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 142.157 173.086 126.148 1.00 9.51  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 141.582 174.342 125.668 1.00 6.95  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 141.209 175.275 126.814 1.00 7.39  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 140.321 176.117 126.682 1.00 12.15 ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 140.378 174.087 124.757 1.00 3.78  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 140.757 173.577 123.400 1.00 5.62  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 141.498 174.363 122.536 1.00 5.00  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 140.390 172.308 122.993 1.00 7.59  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 141.857 173.898 121.292 1.00 5.01  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 140.746 171.837 121.748 1.00 7.57  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 141.481 172.633 120.896 1.00 5.04  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 141.883 175.123 127.950 1.00 4.72  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 141.777 176.104 129.019 1.00 3.73  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 142.507 177.374 128.606 1.00 8.67  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 143.647 177.319 128.137 1.00 17.95 ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 142.369 175.542 130.310 1.00 4.77  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 142.694 176.581 131.367 1.00 5.18  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 141.472 177.036 132.135 1.00 14.10 ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 141.516 178.133 132.729 1.00 16.00 ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 140.468 176.294 132.151 1.00 17.00 ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 141.852 178.521 128.769 1.00 6.53  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 142.463 179.790 128.390 1.00 2.12  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 143.554 180.140 129.392 1.00 6.68  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 143.270 180.416 130.561 1.00 11.57 ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 141.414 180.894 128.320 1.00 4.52  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 141.983 182.218 127.869 1.00 5.11  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 142.741 182.307 126.712 1.00 11.58 ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 141.771 183.374 128.604 1.00 3.79  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 143.270 183.508 126.295 1.00 7.33  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 142.295 184.582 128.193 1.00 7.83  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 143.042 184.642 127.037 1.00 9.58  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 143.569 185.842 126.623 1.00 18.01 ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 144.802 180.125 128.936 1.00 5.89  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 145.953 180.367 129.793 1.00 4.28  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 146.446 181.807 129.741 1.00 6.64  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 147.408 182.139 130.439 1.00 13.87 ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 147.093 179.419 129.412 1.00 5.61  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 146.703 177.945 129.307 1.00 4.10  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 147.706 177.186 128.465 1.00 7.54  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 146.577 177.327 130.686 1.00 9.43  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 145.816 182.662 128.947 1.00 8.10  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 146.288 184.032 128.843 1.00 9.50  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 147.605 184.085 128.096 1.00 11.17 ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 147.765 183.478 127.032 1.00 12.43 ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 148.563 184.816 128.651 1.00 11.59 ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 149.903 184.929 128.081 1.00 13.40 ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 150.869 184.471 129.166 1.00 14.46 ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 151.266 185.242 130.042 1.00 17.78 ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 150.218 186.349 127.604 1.00 10.96 ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 151.651 186.437 127.101 1.00 6.77  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 149.243 186.772 126.520 1.00 12.90 ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 151.249 183.198 129.118 1.00 12.79 ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 152.144 182.621 130.108 1.00 15.46 ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 153.588 182.697 129.632 1.00 19.62 ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 153.882 182.513 128.448 1.00 21.51 ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 151.770 181.166 130.393 1.00 15.40 ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 150.409 180.986 131.040 1.00 12.42 ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 150.322 181.641 132.401 1.00 16.36 ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 149.641 182.651 132.573 1.00 17.91 ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 151.017 181.071 133.376 1.00 18.86 ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 154.491 182.963 130.571 1.00 19.33 ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 155.913 183.065 130.259 1.00 19.21 ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 156.431 181.706 129.805 1.00 18.65 ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 156.544 180.775 130.609 1.00 19.04 ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 156.686 183.569 131.472 1.00 20.48 ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 156.783 185.082 131.514 1.00 25.68 ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 157.194 185.679 130.496 1.00 25.74 ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 156.448 185.674 132.560 1.00 24.59 ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 156.650 181.536 128.503 1.00 14.13 ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 157.070 180.220 127.962 1.00 12.82 ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 158.513 179.886 128.358 1.00 13.45 ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 159.336 180.801 128.390 1.00 12.49 ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 156.906 180.237 126.443 1.00 9.54  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 155.487 180.052 125.940 1.00 8.77  ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 155.355 178.759 125.148 1.00 13.41 ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 156.533 178.556 124.254 1.00 10.78 ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 156.446 177.282 123.538 1.00 8.27  ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 158.802 178.610 128.616 1.00 10.54 ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 160.137 178.164 129.066 1.00 7.25  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 160.943 177.679 127.866 1.00 9.49  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 160.380 176.968 127.037 1.00 10.64 ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 159.902 177.018 130.043 1.00 7.80  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 160.144 177.307 131.523 1.00 9.39  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 159.006 178.139 132.068 1.00 12.46 ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 160.223 175.975 132.233 1.00 7.37  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 162.216 178.053 127.781 1.00 7.82  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 163.073 177.533 126.695 1.00 3.31  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 163.006 176.015 126.814 1.00 6.39  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 163.148 175.541 127.929 1.00 9.25  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 164.484 178.080 126.904 1.00 0.78  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 165.424 177.623 125.803 1.00 1.87  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 164.481 179.595 127.029 1.00 0.94  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 162.761 175.297 125.724 1.00 5.68  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 162.588 173.827 125.814 1.00 2.86  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 163.969 173.197 125.659 1.00 4.28  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 164.359 172.873 124.545 1.00 7.91  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 161.488 173.420 124.844 1.00 4.83  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 161.331 171.920 124.652 1.00 3.06  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 160.214 171.363 125.493 1.00 6.04  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 159.671 172.055 126.358 1.00 10.00 ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 159.871 170.108 125.255 1.00 6.04  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 164.661 173.019 126.770 1.00 4.58  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 166.034 172.532 126.737 1.00 2.91  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 166.005 171.045 126.665 1.00 3.56  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 164.916 170.511 126.485 1.00 6.64  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 166.653 173.032 128.032 1.00 5.52  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 165.663 172.798 129.022 1.00 8.41  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 166.927 174.522 128.004 1.00 2.90  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 167.148 170.338 126.712 1.00 2.55  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 167.134 168.891 126.799 1.00 1.93  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 166.511 168.269 128.059 1.00 3.80  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 165.954 167.178 127.934 1.00 4.79  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 168.622 168.673 126.750 1.00 1.03  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 169.129 169.759 125.859 1.00 4.03  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 168.468 170.907 126.565 1.00 6.13  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 166.584 168.918 129.220 1.00 4.53  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 166.016 168.395 130.487 1.00 3.13  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 164.529 168.710 130.589 1.00 2.97  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 163.905 168.143 131.472 1.00 7.35  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 166.768 168.996 131.667 1.00 5.06  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 166.266 168.641 133.066 1.00 4.09  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 166.660 167.228 133.438 1.00 7.11  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 166.829 169.636 134.057 1.00 1.14  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 163.999 169.613 129.773 1.00 2.57  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 162.557 169.901 129.747 1.00 3.13  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 162.005 168.996 128.717 1.00 4.11  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 160.806 168.824 128.697 1.00 13.84 ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 162.291 171.342 129.355 1.00 2.04  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 163.012 172.114 130.307 1.00 6.24  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 160.821 171.707 129.416 1.00 3.18  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 162.844 168.440 127.865 1.00 0.00  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 162.405 167.426 126.892 1.00 0.00  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 162.454 166.104 127.629 1.00 0.38  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 161.500 165.340 127.503 1.00 8.00  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 163.323 167.391 125.696 1.00 4.36  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 162.951 168.283 124.525 1.00 11.15 ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 161.893 168.930 124.601 1.00 12.77 ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 163.728 168.321 123.553 1.00 8.02  ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 163.520 165.848 128.383 1.00 3.08  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 163.507 164.634 129.195 1.00 0.87  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 162.384 164.672 130.220 1.00 1.70  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 161.725 163.655 130.474 1.00 6.69  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 164.860 164.458 129.884 1.00 1.67  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 165.093 163.085 130.486 1.00 0.40  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 166.320 163.105 131.379 1.00 7.50  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 166.599 161.804 131.975 1.00 10.00 ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 167.788 161.221 131.970 1.00 7.87  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 168.833 161.790 131.395 1.00 8.33  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 167.932 160.035 132.555 1.00 6.78  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 162.157 165.838 130.825 1.00 1.69  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 161.044 165.990 131.756 1.00 0.00  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 159.715 165.749 131.061 1.00 1.10  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 158.848 165.050 131.593 1.00 4.96  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 161.074 167.379 132.391 1.00 0.00  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 159.816 167.647 133.662 1.00 6.86  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 159.538 166.314 129.866 1.00 4.45  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 158.305 166.096 129.119 1.00 0.00  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 158.107 164.621 128.818 1.00 0.00  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 157.009 164.086 129.003 1.00 5.71  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 158.322 166.900 127.820 1.00 0.00  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 157.966 168.360 127.968 1.00 0.23  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 158.154 169.027 129.170 1.00 2.09  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 157.443 169.071 126.902 1.00 1.86  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 157.831 170.360 129.301 1.00 3.45  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 157.116 170.403 127.023 1.00 5.14  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 157.313 171.043 128.223 1.00 6.77  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 156.986 172.371 128.345 1.00 11.25 ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 159.164 163.942 128.370 1.00 1.73  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 159.051 162.524 128.040 1.00 0.41  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 158.671 161.702 129.266 1.00 1.60  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 157.729 160.904 129.224 1.00 8.69  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 160.362 162.022 127.438 1.00 1.31  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 160.360 160.583 126.918 1.00 0.38  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 159.475 160.454 125.690 1.00 2.44  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 161.775 160.126 126.612 1.00 1.62  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 159.386 161.899 130.377 1.00 2.29  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 159.114 161.110 131.576 1.00 0.53  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 157.725 161.399 132.132 1.00 3.85  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 157.001 160.476 132.525 1.00 10.72 ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 160.181 161.381 132.637 1.00 0.69  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 161.481 161.227 132.057 1.00 2.68  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 160.035 160.410 133.795 1.00 0.00  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 157.327 162.673 132.164 1.00 3.48  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 156.034 163.022 132.739 1.00 0.17  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 154.889 162.544 131.856 1.00 1.26  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 153.854 162.103 132.365 1.00 11.73 ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 155.948 164.529 132.966 1.00 0.00  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 156.925 165.081 133.998 1.00 3.75  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 156.727 164.436 135.666 1.00 25.91 ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 158.072 163.257 135.744 1.00 2.42  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 155.049 162.613 130.533 1.00 0.00  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 154.020 162.082 129.646 1.00 0.00  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 153.942 160.564 129.727 1.00 1.57  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 152.852 159.996 129.607 1.00 7.17  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 154.276 162.525 128.206 1.00 1.05  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 155.648 162.297 127.870 1.00 8.49  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 153.956 164.000 128.037 1.00 2.91  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 155.078 159.892 129.921 1.00 3.37  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 155.048 158.451 130.151 1.00 3.21  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 154.308 158.122 131.441 1.00 3.01  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 153.553 157.145 131.502 1.00 9.89  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 156.469 157.895 130.187 1.00 3.69  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 157.125 157.779 128.824 1.00 2.28  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 156.516 156.682 127.979 1.00 6.20  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 156.662 155.498 128.281 1.00 6.82  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 155.827 157.068 126.912 1.00 5.51  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 154.521 158.923 132.486 1.00 1.46  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 153.775 158.737 133.727 1.00 0.00  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 152.285 158.969 133.516 1.00 0.00  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 151.451 158.231 134.054 1.00 6.74  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 154.314 159.674 134.807 1.00 0.14  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 151.930 159.997 132.743 1.00 0.00  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 150.523 160.291 132.485 1.00 0.00  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 149.854 159.169 131.701 1.00 0.87  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 148.705 158.810 131.977 1.00 3.32  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 150.394 161.613 131.732 1.00 0.89  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 150.761 162.888 132.487 1.00 1.54  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 150.858 164.056 131.527 1.00 3.76  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 149.751 163.170 133.578 1.00 4.19  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 150.554 158.614 130.709 1.00 2.42  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 149.990 157.513 129.934 1.00 3.15  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 149.779 156.274 130.793 1.00 6.57  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 148.810 155.536 130.585 1.00 8.74  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 150.893 157.192 128.744 1.00 3.91  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 150.315 156.166 127.781 1.00 7.04  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 149.135 156.697 126.985 1.00 15.70 ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 148.904 157.924 126.995 1.00 16.22 ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 148.437 155.883 126.348 1.00 15.67 ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 150.662 156.033 131.757 1.00 2.73  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 150.497 154.945 132.709 1.00 0.00  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 149.509 155.280 133.814 1.00 5.18  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 149.353 154.482 134.746 1.00 12.17 ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 151.849 154.567 133.318 1.00 1.22  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 148.848 156.436 133.726 1.00 2.24  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 147.912 156.906 134.747 1.00 0.00  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 148.581 156.975 136.117 1.00 2.12  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 147.986 156.636 137.140 1.00 8.48  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 146.651 156.040 134.788 1.00 5.49  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 145.761 156.202 133.565 1.00 7.71  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 145.808 157.630 133.046 1.00 7.20  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 144.911 157.858 131.921 1.00 10.83 ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 145.191 157.546 130.663 1.00 13.72 ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 146.328 156.960 130.333 1.00 11.24 ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 144.308 157.836 129.712 1.00 15.07 ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 149.832 157.417 136.127 1.00 3.22  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 150.597 157.653 137.340 1.00 2.50  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 150.857 159.144 137.496 1.00 1.69  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 150.585 159.945 136.600 1.00 7.88  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 151.923 156.888 137.312 1.00 0.39  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 151.881 155.363 137.399 1.00 3.31  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 153.288 154.802 137.343 1.00 6.44  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 151.174 154.916 138.662 1.00 4.61  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 151.384 159.511 138.657 1.00 2.16  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 151.811 160.874 138.879 1.00 3.50  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 153.254 161.091 138.470 1.00 2.53  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 153.981 160.159 138.141 1.00 12.32 ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 153.670 162.352 138.505 1.00 0.00  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 155.031 162.731 138.185 1.00 0.00  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 155.746 163.267 139.410 1.00 2.22  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 155.145 163.946 140.243 1.00 13.23 ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 157.035 162.957 139.516 1.00 0.00  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 157.853 163.376 140.654 1.00 0.00  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 159.213 163.841 140.163 1.00 5.11  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 160.194 163.087 140.180 1.00 12.75 ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 157.997 162.241 141.671 1.00 0.71  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 158.870 162.607 142.722 1.00 13.77 ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 159.310 165.080 139.678 1.00 1.83  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 160.635 165.647 139.389 1.00 2.35  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 161.296 166.114 140.677 1.00 2.92  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 160.789 167.003 141.362 1.00 9.78  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 160.325 166.820 138.451 1.00 0.65  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 158.922 167.175 138.733 1.00 2.33  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 158.218 165.931 139.176 1.00 3.53  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 162.428 165.502 141.011 1.00 0.98  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 163.154 165.806 142.231 1.00 2.88  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 164.526 166.375 141.896 1.00 4.16  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 165.038 166.213 140.786 1.00 9.39  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 163.299 164.562 143.122 1.00 2.78  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 164.117 163.460 142.509 1.00 1.15  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 163.522 162.504 141.709 1.00 2.93  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 165.477 163.373 142.748 1.00 1.70  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 164.269 161.490 141.148 1.00 4.05  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 166.228 162.361 142.189 1.00 3.08  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 165.622 161.418 141.389 1.00 4.24  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 165.075 167.095 142.852 1.00 2.58  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 166.412 167.633 142.627 1.00 2.17  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 166.631 168.871 143.423 1.00 7.17  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 165.746 169.253 144.173 1.00 12.22 ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 167.809 169.492 143.327 1.00 3.17  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 168.080 170.653 144.138 1.00 4.64  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 167.069 171.702 143.748 1.00 4.23  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 166.155 171.376 142.980 1.00 9.07  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 169.487 170.947 143.686 1.00 6.77  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 169.582 170.385 142.300 1.00 3.51  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 168.893 169.063 142.484 1.00 1.37  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 167.191 172.929 144.244 1.00 4.50  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 166.151 173.943 143.964 1.00 9.20  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 166.671 174.933 142.941 1.00 9.17  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 167.814 175.346 143.075 1.00 10.76 ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 165.788 174.665 145.207 1.00 5.75  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 165.840 175.327 141.988 1.00 8.52  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 166.330 176.191 140.911 1.00 4.75  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 166.697 175.334 139.735 1.00 5.75  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 167.678 175.678 139.066 1.00 14.67 ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 165.936 174.266 139.486 1.00 3.15  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 166.248 173.312 138.418 1.00 3.95  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 165.140 173.302 137.409 1.00 7.87  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 165.410 172.974 136.269 1.00 13.28 ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 166.489 171.940 139.032 1.00 3.91  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 165.431 171.712 139.950 1.00 9.31  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 167.808 171.872 139.773 1.00 4.16  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 163.929 173.652 137.775 1.00 9.73  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 162.883 173.754 136.749 1.00 6.85  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 161.747 172.832 137.080 1.00 8.52  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 160.800 172.767 136.296 1.00 14.96 ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 161.806 172.184 138.232 1.00 7.40  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 160.815 171.163 138.611 1.00 2.37  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 159.404 171.738 138.581 1.00 9.65  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 158.566 171.128 137.938 1.00 20.04 ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 161.298 170.645 139.970 1.00 4.16  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 162.648 169.984 140.074 1.00 7.92  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 162.930 169.783 141.553 1.00 3.81  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 162.798 171.076 142.269 1.00 5.51  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 162.798 170.902 143.720 1.00 14.28 ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 159.164 172.898 139.153 1.00 7.13  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 157.788 173.406 139.306 1.00 5.84  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 157.309 174.065 138.065 1.00 12.63 ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 156.104 174.091 137.867 1.00 17.78 ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 157.743 174.403 140.459 1.00 8.31  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 158.296 173.810 141.630 1.00 11.65 ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 156.328 174.877 140.739 1.00 13.55 ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 158.213 174.635 137.282 1.00 14.85 ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 157.834 175.377 136.066 1.00 8.75  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 157.734 174.383 134.920 1.00 11.69 ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 156.817 174.518 134.114 1.00 20.93 ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 158.872 176.453 135.781 1.00 14.46 ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 158.885 177.586 136.804 1.00 20.82 ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 157.592 178.358 137.019 1.00 24.02 ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 157.032 178.845 136.017 1.00 23.64 ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 157.156 178.509 138.182 1.00 21.21 ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 158.623 173.402 134.874 1.00 12.62 ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 158.596 172.391 133.809 1.00 6.39  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 157.271 171.665 133.917 1.00 9.70  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 156.721 171.299 132.886 1.00 17.67 ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 159.712 171.466 133.958 1.00 8.97  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 160.916 172.069 133.515 1.00 10.88 ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 156.801 171.440 135.127 1.00 14.46 ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 155.465 170.863 135.270 1.00 12.77 ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 154.413 171.826 134.734 1.00 13.85 ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 153.501 171.435 133.994 1.00 16.37 ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 155.197 170.490 136.739 1.00 10.50 ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 153.725 170.189 136.948 1.00 14.50 ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 156.052 169.306 137.146 1.00 15.60 ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 154.533 173.108 135.091 1.00 14.20 ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 153.585 174.103 134.602 1.00 9.78  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 153.658 174.247 133.088 1.00 12.76 ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 152.629 174.397 132.421 1.00 21.04 ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 153.838 175.449 135.278 1.00 13.68 ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 153.482 175.483 136.749 1.00 16.69 ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 153.172 176.898 137.201 1.00 15.66 ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 154.327 177.835 136.911 1.00 14.90 ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 154.001 179.240 137.273 1.00 13.69 ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 154.867 174.213 132.526 1.00 14.32 ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 155.027 174.347 131.084 1.00 7.75  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 154.438 173.154 130.348 1.00 11.46 ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 153.834 173.315 129.282 1.00 18.11 ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 156.504 174.519 130.736 1.00 12.39 ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 154.614 171.946 130.888 1.00 12.93 ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 153.989 170.779 130.276 1.00 8.83  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 152.470 170.859 130.365 1.00 12.72 ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 151.768 170.498 129.414 1.00 17.30 ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 154.492 169.495 130.931 1.00 9.02  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 153.835 168.227 130.383 1.00 6.76  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 154.124 168.068 128.901 1.00 9.82  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 154.287 167.007 131.148 1.00 6.08  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 151.947 171.324 131.500 1.00 17.46 ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 150.507 171.477 131.624 1.00 10.46 ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 149.941 172.496 130.656 1.00 9.93  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 148.874 172.289 130.073 1.00 19.86 ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 150.644 173.616 130.475 1.00 14.57 ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 150.194 174.634 129.533 1.00 13.46 ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 150.343 174.168 128.091 1.00 15.53 ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 149.538 174.546 127.233 1.00 18.50 ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 150.968 175.932 129.757 1.00 11.21 ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 150.765 176.528 131.115 1.00 16.10 ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 149.741 176.141 131.953 1.00 18.41 ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 151.457 177.481 131.782 1.00 16.72 ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 149.809 176.831 133.077 1.00 16.99 ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 150.841 177.653 132.999 1.00 18.85 ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 151.365 173.359 127.804 1.00 12.39 ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 151.530 172.809 126.465 1.00 9.14  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 150.363 171.909 126.088 1.00 15.04 ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 149.969 171.858 124.917 1.00 20.30 ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 152.847 172.042 126.378 1.00 13.23 ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 153.105 171.398 125.034 1.00 14.01 ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 153.665 172.375 124.027 1.00 17.20 ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 152.936 172.907 123.190 1.00 19.20 ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 154.967 172.621 124.103 1.00 14.51 ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 149.804 171.196 127.058 1.00 17.00 ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 148.615 170.383 126.855 1.00 8.05  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 147.330 171.167 127.077 1.00 7.86  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 146.244 170.585 126.997 1.00 12.79 ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 148.643 169.168 127.785 1.00 9.29  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 149.897 168.295 127.719 1.00 5.85  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 149.787 167.135 128.687 1.00 7.44  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 150.120 167.793 126.305 1.00 11.01 ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 147.427 172.464 127.352 1.00 7.19  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 146.253 173.287 127.576 1.00 7.28  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 145.480 172.934 128.826 1.00 10.06 ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 144.244 172.923 128.804 1.00 13.46 ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 146.178 172.648 129.918 1.00 14.67 ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 145.557 172.226 131.161 1.00 10.33 ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 145.596 173.350 132.186 1.00 13.05 ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 146.383 174.295 132.083 1.00 16.90 ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 146.254 170.984 131.729 1.00 5.54  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 146.252 169.792 130.794 1.00 7.86  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 144.901 169.108 130.785 1.00 10.52 ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 144.982 167.746 130.271 1.00 11.02 ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 145.008 167.431 128.984 1.00 10.15 ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 144.974 168.360 128.044 1.00 11.26 ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 145.072 166.151 128.632 1.00 8.48  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 144.723 173.233 133.181 1.00 14.41 ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 144.705 174.141 134.322 1.00 11.22 ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 145.593 173.538 135.403 1.00 9.12  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 145.212 172.565 136.060 1.00 14.40 ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 143.275 174.346 134.817 1.00 11.26 ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 143.138 175.385 135.897 1.00 11.03 ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 144.164 176.274 136.169 1.00 12.73 ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 141.972 175.475 136.637 1.00 8.50  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 144.032 177.223 137.159 1.00 10.85 ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 141.835 176.423 137.626 1.00 9.33  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 142.866 177.299 137.888 1.00 12.60 ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 146.779 174.107 135.585 1.00 11.43 ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 147.748 173.610 136.553 1.00 12.49 ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 147.658 174.471 137.803 1.00 14.35 ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 147.899 175.683 137.752 1.00 22.35 ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 149.172 173.618 135.980 1.00 12.04 ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 150.140 172.978 136.959 1.00 11.72 ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 149.204 172.899 134.648 1.00 13.76 ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 147.312 173.850 138.924 1.00 8.43  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 147.275 174.527 140.211 1.00 9.05  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 148.512 174.155 141.013 1.00 10.49 ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 148.809 172.972 141.198 1.00 16.46 ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 146.013 174.169 141.000 1.00 9.37  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 144.712 174.858 140.585 1.00 4.40  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 144.133 174.247 139.327 1.00 11.63 ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 143.711 174.817 141.717 1.00 10.36 ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 149.226 175.169 141.483 1.00 10.37 ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 150.454 174.991 142.247 1.00 9.98  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 150.118 175.118 143.723 1.00 12.46 ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 149.537 176.121 144.154 1.00 19.01 ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 151.521 176.013 141.828 1.00 11.55 ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 152.693 175.971 142.776 1.00 12.06 ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 151.982 175.729 140.413 1.00 13.12 ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 150.481 174.101 144.501 1.00 5.67  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 150.251 174.084 145.938 1.00 2.90  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 151.588 174.012 146.656 1.00 5.43  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 152.405 173.130 146.369 1.00 14.52 ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 149.364 172.904 146.343 1.00 1.01  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 147.999 172.931 145.721 1.00 3.98  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 146.993 173.711 146.261 1.00 5.45  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 147.723 172.174 144.597 1.00 9.75  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 145.739 173.739 145.691 1.00 3.67  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 146.469 172.198 144.023 1.00 8.97  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 145.477 172.981 144.571 1.00 4.42  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 151.811 174.940 147.582 1.00 3.90  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 153.020 174.951 148.402 1.00 4.86  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 152.715 174.176 149.675 1.00 5.56  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 152.152 174.717 150.629 1.00 13.21 ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 153.458 176.380 148.701 1.00 8.81  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 154.863 176.452 149.259 1.00 9.69  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 155.571 175.449 149.319 1.00 10.67 ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 155.273 177.642 149.672 1.00 13.72 ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 153.092 172.902 149.688 1.00 1.77  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 152.724 172.010 150.775 1.00 3.87  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 153.540 172.297 152.029 1.00 7.42  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 154.664 172.800 151.967 1.00 11.27 ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 152.920 170.556 150.351 1.00 0.78  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 151.733 169.975 149.126 1.00 12.09 ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 152.952 171.973 153.176 1.00 4.85  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 153.636 172.049 154.459 1.00 2.99  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 153.028 170.995 155.376 1.00 3.28  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 152.188 170.194 154.955 1.00 8.77  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 153.556 173.466 155.045 1.00 6.63  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 152.200 173.786 155.631 1.00 11.74 ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 151.180 173.387 155.037 1.00 13.04 ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 152.152 174.445 156.692 1.00 13.53 ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 153.455 170.994 156.641 1.00 1.35  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 153.014 169.961 157.571 1.00 4.35  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 151.523 170.038 157.875 1.00 9.35  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 150.959 169.066 158.390 1.00 13.32 ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 153.814 170.045 158.872 1.00 5.61  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 153.318 171.100 159.845 1.00 12.05 ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 154.056 172.416 159.705 1.00 15.61 ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 155.080 172.454 158.993 1.00 12.71 ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 153.610 173.413 160.311 1.00 11.53 ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 150.870 171.160 157.571 1.00 4.96  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 149.450 171.316 157.854 1.00 3.36  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 148.554 170.751 156.760 1.00 4.77  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 147.330 170.758 156.920 1.00 6.68  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 149.114 172.792 158.076 1.00 3.64  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 149.347 173.524 156.866 1.00 8.27  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 149.979 173.368 159.181 1.00 3.16  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 149.126 170.272 155.654 1.00 4.21  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 148.355 169.604 154.603 1.00 6.13  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 148.096 168.169 155.054 1.00 8.82  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 148.789 167.224 154.674 1.00 13.82 ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 149.101 169.648 153.275 1.00 3.83  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 148.916 170.928 152.507 1.00 5.65  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 149.336 172.134 153.032 1.00 5.53  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 148.340 170.919 151.250 1.00 7.76  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 149.176 173.310 152.325 1.00 4.36  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 148.177 172.091 150.538 1.00 9.81  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 148.596 173.288 151.077 1.00 3.76  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 147.070 168.008 155.882 1.00 4.97  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 146.751 166.710 156.457 1.00 2.87  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 145.937 165.887 155.460 1.00 4.92  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 145.828 166.228 154.280 1.00 8.84  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 146.030 166.885 157.793 1.00 3.71  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 144.877 167.860 157.712 1.00 11.44 ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 144.591 168.358 156.606 1.00 16.31 ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 144.254 168.128 158.759 1.00 12.32 ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 145.369 164.773 155.928 1.00 6.47  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 144.617 163.890 155.041 1.00 4.24  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 143.380 164.587 154.491 1.00 5.26  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 143.060 164.456 153.305 1.00 8.40  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 144.213 162.621 155.790 1.00 4.46  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 143.403 161.651 154.971 1.00 6.86  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 144.019 160.822 154.056 1.00 6.46  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 142.027 161.595 155.089 1.00 6.65  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 143.284 159.926 153.313 1.00 7.97  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 141.285 160.708 154.344 1.00 4.05  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 141.916 159.875 153.450 1.00 8.49  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 142.669 165.332 155.340 1.00 4.05  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 141.395 165.911 154.928 1.00 5.66  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 141.591 167.067 153.954 1.00 7.91  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 140.854 167.185 152.968 1.00 9.80  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 140.611 166.368 156.154 1.00 7.55  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 140.331 165.254 157.145 1.00 10.70 ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 138.961 165.375 157.775 1.00 16.39 ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 138.835 165.699 158.956 1.00 19.73 ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 137.926 165.115 156.989 1.00 11.44 ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 142.567 167.937 154.219 1.00 5.46  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 142.829 169.051 153.313 1.00 0.00  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 143.268 168.549 151.944 1.00 5.49  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 142.788 169.026 150.908 1.00 14.98 ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 143.887 169.974 153.915 1.00 1.43  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 144.175 167.571 151.925 1.00 3.23  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 144.621 167.000 150.661 1.00 0.00  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 143.481 166.284 149.952 1.00 3.17  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 143.380 166.334 148.723 1.00 9.81  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 145.792 166.049 150.897 1.00 0.30  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 147.085 166.747 151.281 1.00 6.54  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 147.863 167.580 149.888 1.00 18.70 ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 148.240 166.185 148.834 1.00 7.59  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 142.609 165.615 150.708 1.00 3.87  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 141.470 164.952 150.097 1.00 2.69  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 140.496 165.924 149.462 1.00 5.64  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 139.969 165.670 148.380 1.00 14.06 ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 140.243 167.052 150.129 1.00 1.45  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 139.361 168.063 149.553 1.00 0.74  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 139.991 168.711 148.325 1.00 4.25  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 139.299 168.992 147.335 1.00 9.90  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 139.014 169.112 150.605 1.00 2.81  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 137.913 170.061 150.187 1.00 7.99  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 137.559 171.014 151.310 1.00 7.21  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 136.719 172.107 150.841 1.00 7.47  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 137.181 173.209 150.269 1.00 11.32 ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 138.477 173.397 150.079 1.00 7.84  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 136.323 174.146 149.876 1.00 16.80 ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 141.304 168.953 148.367 1.00 2.58  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 142.004 169.464 147.191 1.00 2.67  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 141.897 168.471 146.040 1.00 2.77  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 141.685 168.855 144.882 1.00 8.47  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 143.470 169.780 147.541 1.00 0.00  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 143.552 171.025 148.426 1.00 1.63  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 144.294 169.972 146.282 1.00 1.45  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 144.934 171.293 148.975 1.00 0.00  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 142.040 167.179 146.341 1.00 2.51  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 141.890 166.147 145.323 1.00 0.88  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 140.478 166.126 144.761 1.00 1.74  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 140.288 165.919 143.561 1.00 4.77  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 142.251 164.780 145.899 1.00 2.78  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 143.721 164.574 146.099 1.00 5.34  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 144.643 165.361 145.433 1.00 4.67  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 144.183 163.585 146.949 1.00 5.11  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 145.994 165.167 145.615 1.00 4.84  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 145.532 163.389 147.134 1.00 3.70  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 146.440 164.182 146.466 1.00 4.43  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 139.473 166.312 145.618 1.00 6.57  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 138.091 166.371 145.148 1.00 5.10  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 137.924 167.514 144.158 1.00 7.19  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 137.342 167.351 143.076 1.00 14.90 ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 137.124 166.519 146.337 1.00 4.60  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 135.745 166.927 145.853 1.00 5.43  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 137.054 165.231 147.129 1.00 7.17  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 138.443 168.689 144.514 1.00 5.00  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 138.344 169.831 143.618 1.00 5.53  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 139.042 169.591 142.292 1.00 5.05  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 138.494 169.882 141.227 1.00 4.65  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 140.259 169.045 142.343 1.00 8.82  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 141.005 168.785 141.113 1.00 5.00  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 140.317 167.733 140.252 1.00 5.98  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 140.265 167.867 139.024 1.00 11.06 ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 142.432 168.354 141.447 1.00 4.52  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 143.327 169.397 142.116 1.00 2.77  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 144.646 168.775 142.526 1.00 5.46  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 143.554 170.581 141.196 1.00 3.95  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 139.794 166.676 140.873 1.00 6.34  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 139.122 165.619 140.125 1.00 3.58  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 137.866 166.138 139.447 1.00 6.59  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 137.601 165.812 138.285 1.00 15.00 ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 138.778 164.455 141.054 1.00 4.32  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 140.186 163.486 141.625 1.00 10.72 ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 137.073 166.945 140.155 1.00 5.99  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 135.838 167.442 139.561 1.00 4.25  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 136.116 168.489 138.489 1.00 7.61  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 135.454 168.504 137.444 1.00 8.37  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 134.920 168.000 140.645 1.00 5.69  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 134.108 166.935 141.356 1.00 8.19  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 133.117 167.518 142.335 1.00 14.36 ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 133.126 168.717 142.604 1.00 23.04 ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 132.250 166.669 142.875 1.00 11.78 ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 137.087 169.374 138.724 1.00 7.03  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 137.414 170.387 137.724 1.00 4.72  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 138.092 169.754 136.515 1.00 10.48 ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 137.763 170.069 135.365 1.00 13.21 ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 138.287 171.491 138.346 1.00 1.00  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 138.867 172.382 137.263 1.00 0.78  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 137.476 172.312 139.323 1.00 6.86  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 139.037 168.849 136.752 1.00 9.78  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 139.844 168.306 135.679 1.00 2.84  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 141.124 169.093 135.516 1.00 5.64  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 141.526 169.430 134.398 1.00 9.60  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 141.773 169.389 136.637 1.00 9.07  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 142.926 170.271 136.675 1.00 9.18  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 144.153 169.516 137.165 1.00 9.34  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 144.052 168.495 137.849 1.00 16.35 ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 142.657 171.479 137.581 1.00 8.80  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 145.322 170.035 136.803 1.00 8.68  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 146.589 169.461 137.228 1.00 6.62  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 146.978 170.026 138.585 1.00 6.35  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 146.968 171.246 138.783 1.00 17.16 ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 147.688 169.752 136.208 1.00 11.83 ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 147.688 168.832 135.038 1.00 9.41  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 146.636 168.111 134.562 1.00 10.35 ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 148.800 168.530 134.191 1.00 8.15  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 147.023 167.377 133.469 1.00 10.10 ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 148.348 167.618 133.220 1.00 9.78  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 150.134 168.943 134.157 1.00 6.77  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 149.181 167.113 132.229 1.00 8.61  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 150.959 168.439 133.175 1.00 7.91  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 150.480 167.535 132.223 1.00 8.84  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 147.320 169.142 139.515 1.00 4.74  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 147.764 169.574 140.822 1.00 7.02  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 149.244 169.347 141.036 1.00 10.35 ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 149.686 168.206 141.194 1.00 20.28 ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 150.021 170.425 141.042 1.00 9.11  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 151.456 170.354 141.282 1.00 10.02 ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 151.702 170.679 142.750 1.00 8.60  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 151.627 171.842 143.157 1.00 17.93 ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 152.210 171.315 140.364 1.00 14.04 ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 154.006 171.185 140.462 1.00 12.09 ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 151.989 169.650 143.544 1.00 4.98  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 152.202 169.797 144.982 1.00 2.77  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 153.704 169.889 145.231 1.00 5.13  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 154.387 168.881 145.412 1.00 14.14 ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 151.574 168.641 145.752 1.00 3.58  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 150.089 168.526 145.571 1.00 7.27  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 149.556 167.895 144.461 1.00 7.81  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 149.223 169.045 146.516 1.00 6.02  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 148.193 167.790 144.295 1.00 5.40  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 147.858 168.941 146.355 1.00 4.93  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 147.343 168.313 145.243 1.00 4.75  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 154.219 171.113 145.228 1.00 1.93  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 155.627 171.353 145.499 1.00 1.54  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 155.916 171.243 146.993 1.00 8.39  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 155.042 171.451 147.837 1.00 14.95 ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 156.043 172.726 144.981 1.00 7.79  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 155.638 172.951 143.547 1.00 16.09 ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 156.054 172.161 142.673 1.00 19.42 ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 154.906 173.921 143.289 1.00 15.98 ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 157.176 170.936 147.310 1.00 9.48  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 157.591 170.629 148.681 1.00 7.34  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 156.695 169.558 149.297 1.00 6.07  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 156.209 169.694 150.420 1.00 10.34 ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 157.636 171.878 149.570 1.00 10.55 ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 158.713 172.911 149.227 1.00 12.35 ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 158.328 173.867 148.118 1.00 17.47 ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 157.186 173.791 147.633 1.00 18.97 ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 159.175 174.701 147.733 1.00 18.02 ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 156.472 168.476 148.547 1.00 3.58  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 155.567 167.430 149.010 1.00 3.50  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 156.143 166.679 150.204 1.00 3.71  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 155.392 166.123 151.013 1.00 5.19  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 155.250 166.461 147.875 1.00 3.39  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 154.048 165.601 148.133 1.00 3.51  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 152.810 166.173 148.357 1.00 3.57  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 154.157 164.221 148.161 1.00 5.59  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 151.703 165.389 148.599 1.00 4.39  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 153.051 163.431 148.401 1.00 6.37  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 151.823 164.016 148.621 1.00 7.12  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 157.468 166.653 150.338 1.00 5.20  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 158.093 165.912 151.426 1.00 1.05  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 158.021 166.693 152.733 1.00 4.98  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 158.512 166.226 153.765 1.00 11.69 ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 159.545 165.570 151.086 1.00 3.72  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 160.320 166.756 150.558 1.00 9.86  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 159.753 167.806 150.270 1.00 13.00 ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 161.632 166.595 150.435 1.00 12.15 ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 157.418 167.882 152.703 1.00 3.60  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 157.199 168.642 153.925 1.00 3.18  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 155.979 168.170 154.703 1.00 6.58  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 155.803 168.584 155.853 1.00 10.08 ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 157.070 170.133 153.604 1.00 1.75  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 158.404 170.854 153.597 1.00 5.36  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 158.319 172.247 153.001 1.00 8.38  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 157.315 173.084 153.642 1.00 7.74  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 157.541 173.836 154.709 1.00 5.78  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 158.714 173.830 155.321 1.00 10.24 ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 156.569 174.610 155.178 1.00 4.50  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 155.144 167.321 154.113 1.00 4.40  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 154.060 166.696 154.852 1.00 0.82  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 154.617 165.723 155.884 1.00 6.01  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 155.748 165.244 155.779 1.00 10.59 ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 153.121 165.947 153.908 1.00 0.00  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 151.935 166.679 153.282 1.00 1.86  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 152.411 167.588 152.177 1.00 7.13  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 150.931 165.676 152.749 1.00 2.94  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 153.808 165.436 156.898 1.00 5.01  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 154.175 164.410 157.860 1.00 1.77  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 154.129 163.034 157.203 1.00 6.50  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 153.334 162.784 156.295 1.00 11.04 ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 153.247 164.456 159.071 1.00 6.21  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 153.331 165.754 159.855 1.00 9.08  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 152.148 165.961 160.777 1.00 15.58 ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 151.160 165.207 160.657 1.00 14.02 ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 152.205 166.877 161.622 1.00 13.33 ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 155.003 162.140 157.671 1.00 4.52  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 155.098 160.811 157.071 1.00 4.47  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 153.781 160.056 157.192 1.00 6.50  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 153.358 159.372 156.251 1.00 9.73  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 156.229 160.022 157.724 1.00 4.24  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 157.608 160.365 157.198 1.00 7.95  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 158.636 159.301 157.520 1.00 14.51 ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 158.373 158.114 157.236 1.00 13.40 ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 159.707 159.653 158.057 1.00 13.81 ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 153.119 160.170 158.344 1.00 3.17  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 151.808 159.554 158.507 1.00 2.96  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 150.801 160.151 157.533 1.00 6.40  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 149.967 159.432 156.969 1.00 10.59 ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 151.332 159.716 159.950 1.00 4.25  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 151.413 161.136 160.482 1.00 5.13  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 151.096 161.182 161.964 1.00 7.34  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 150.670 162.509 162.387 1.00 12.69 ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 149.410 162.851 162.620 1.00 13.96 ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 148.422 161.985 162.478 1.00 12.79 ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 149.136 164.095 163.003 1.00 10.82 ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 150.870 161.466 157.312 1.00 6.44  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 149.965 162.101 156.362 1.00 3.19  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 150.264 161.667 154.933 1.00 3.02  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 149.341 161.482 154.136 1.00 6.74  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 150.039 163.618 156.498 1.00 3.74  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 149.251 164.151 157.679 1.00 8.74  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 147.625 163.385 157.797 1.00 19.92 ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 147.380 163.377 159.569 1.00 3.69  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 151.542 161.495 154.588 1.00 1.50  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 151.877 160.972 153.266 1.00 0.00  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 151.325 159.564 153.082 1.00 0.89  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 150.749 159.240 152.032 1.00 7.72  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 153.392 160.983 153.063 1.00 2.08  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 154.090 162.342 153.063 1.00 2.33  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 155.592 162.174 153.208 1.00 2.77  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 153.762 163.096 151.796 1.00 3.71  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 151.473 158.718 154.103 1.00 0.00  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 150.930 157.367 154.031 1.00 1.78  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 149.418 157.390 153.860 1.00 3.72  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 148.864 156.623 153.065 1.00 7.14  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 151.318 156.581 155.283 1.00 3.70  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 150.681 155.318 155.311 1.00 9.36  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 148.733 158.268 154.597 1.00 1.90  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 147.282 158.365 154.475 1.00 0.48  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 146.861 158.855 153.092 1.00 4.22  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 145.912 158.325 152.503 1.00 8.30  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 146.732 159.282 155.563 1.00 4.36  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 147.554 159.864 152.558 1.00 5.32  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 147.204 160.426 151.256 1.00 1.94  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 147.510 159.439 150.131 1.00 0.20  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 146.947 159.543 149.029 1.00 4.50  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 147.928 161.775 151.064 1.00 1.31  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 147.694 162.343 149.680 1.00 6.19  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 147.446 162.774 152.100 1.00 5.33  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 148.402 158.477 150.381 1.00 0.00  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 148.655 157.439 149.384 1.00 0.00  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 147.376 156.708 148.990 1.00 3.25  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 147.217 156.329 147.826 1.00 6.81  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 149.694 156.448 149.906 1.00 2.35  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 149.168 155.665 150.961 1.00 6.02  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 146.449 156.516 149.933 1.00 3.96  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 145.188 155.848 149.620 1.00 4.37  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 144.380 156.639 148.597 1.00 6.21  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 143.872 156.080 147.615 1.00 7.53  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 144.370 155.651 150.896 1.00 4.16  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 144.542 154.302 151.566 1.00 9.91  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 143.787 154.213 152.876 1.00 15.82 ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 143.039 153.264 153.113 1.00 14.67 ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 143.984 155.201 153.741 1.00 10.50 ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 144.233 157.948 148.825 1.00 5.61  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 143.480 158.780 147.894 1.00 0.93  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 144.159 158.840 146.536 1.00 1.47  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 143.491 158.789 145.497 1.00 5.82  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 143.307 160.188 148.460 1.00 1.01  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 143.008 160.220 149.937 1.00 4.22  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 143.002 161.624 150.496 1.00 4.27  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 142.034 162.049 151.124 1.00 5.46  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 144.086 162.355 150.272 1.00 5.79  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 145.488 158.953 146.522 1.00 2.39  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 146.198 158.983 145.248 1.00 1.89  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 145.976 157.680 144.488 1.00 4.90  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 145.732 157.684 143.276 1.00 5.55  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 147.695 159.269 145.468 1.00 0.43  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 148.438 159.233 144.148 1.00 3.94  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 147.878 160.619 146.139 1.00 0.00  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 146.036 156.548 145.194 1.00 5.44  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 145.850 155.255 144.547 1.00 2.08  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 144.440 155.100 143.991 1.00 4.51  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 144.261 154.617 142.869 1.00 7.04  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 146.166 154.131 145.532 1.00 1.26  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 145.892 152.740 145.001 1.00 6.46  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 146.664 151.674 145.749 1.00 10.33 ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 147.103 151.889 146.879 1.00 13.54 ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 146.838 150.519 145.120 1.00 11.67 ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 143.421 155.502 144.759 1.00 4.29  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 142.053 155.351 144.263 1.00 2.32  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 141.786 156.293 143.095 1.00 5.44  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 141.088 155.928 142.138 1.00 9.70  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 141.041 155.581 145.386 1.00 4.64  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 140.873 157.281 145.951 1.00 27.13 ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 142.347 157.505 143.144 1.00 7.92  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 142.232 158.433 142.024 1.00 5.07  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 142.874 157.846 140.773 1.00 3.60  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 142.309 157.915 139.674 1.00 7.44  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 142.864 159.786 142.399 1.00 1.05  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 141.902 160.612 143.252 1.00 4.94  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 143.292 160.540 141.166 1.00 1.59  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 142.546 161.818 143.878 1.00 3.68  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 144.065 157.261 140.920 1.00 4.92  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 144.742 156.678 139.768 1.00 1.80  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 143.982 155.474 139.229 1.00 6.90  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 143.961 155.243 138.018 1.00 13.91 ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 146.173 156.294 140.139 1.00 3.12  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 147.101 157.479 140.307 1.00 1.79  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 148.476 157.070 140.774 1.00 5.56  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 148.786 155.882 140.849 1.00 8.99  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 149.311 158.049 141.092 1.00 2.63  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 143.359 154.689 140.112 1.00 7.66  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 142.541 153.570 139.649 1.00 9.08  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 141.334 154.059 138.859 1.00 7.93  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 140.978 153.477 137.824 1.00 11.69 ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 142.097 152.716 140.835 1.00 7.34  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 143.206 151.874 141.438 1.00 10.34 ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 142.792 151.216 142.737 1.00 13.62 ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 141.619 151.370 143.138 1.00 11.38 ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 143.640 150.544 143.361 1.00 11.57 ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 140.685 155.125 139.332 1.00 5.00  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 139.576 155.704 138.580 1.00 9.35  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 140.041 156.213 137.220 1.00 13.12 ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 139.366 156.004 136.204 1.00 18.23 ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 138.925 156.828 139.382 1.00 12.11 ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 141.197 156.879 137.181 1.00 12.61 ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 141.731 157.357 135.909 1.00 7.59  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 142.046 156.199 134.970 1.00 11.56 ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 141.793 156.278 133.764 1.00 17.02 ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 142.980 158.204 136.147 1.00 7.28  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 142.760 159.634 136.641 1.00 7.94  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 144.085 160.269 137.018 1.00 8.52  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 142.050 160.460 135.585 1.00 10.04 ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 142.613 155.115 135.509 1.00 10.24 ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 142.949 153.958 134.687 1.00 9.81  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 141.700 153.311 134.107 1.00 16.42 ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 141.676 152.940 132.928 1.00 19.55 ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 143.744 152.949 135.512 1.00 9.57  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 144.662 152.064 134.694 1.00 11.97 ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 145.816 151.548 135.531 1.00 14.91 ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 146.613 152.630 136.095 1.00 11.05 ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 146.887 152.763 137.387 1.00 14.84 ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 146.431 151.902 138.282 1.00 15.51 ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 147.638 153.785 137.787 1.00 12.94 ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 140.649 153.161 134.918 1.00 24.38 ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 139.394 152.637 134.391 1.00 24.14 ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 138.728 153.618 133.436 1.00 20.54 ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 137.891 153.208 132.627 1.00 23.22 ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 138.440 152.274 135.530 1.00 20.68 ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 137.562 153.415 136.008 1.00 21.53 ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 136.638 153.005 137.138 1.00 26.96 ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 137.142 152.620 138.213 1.00 23.39 ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 135.405 153.073 136.952 1.00 30.78 ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 139.081 154.903 133.516 1.00 23.81 ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 138.600 155.872 132.539 1.00 26.04 ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 139.304 155.709 131.197 1.00 28.44 ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 138.727 156.027 130.151 1.00 28.53 ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 138.804 157.290 133.076 1.00 25.48 ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 137.854 158.299 132.512 1.00 28.28 ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 137.494 158.324 131.183 1.00 31.86 ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 137.196 159.325 133.101 1.00 26.97 ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 136.653 159.322 130.976 1.00 30.32 ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 136.454 159.945 132.124 1.00 31.75 ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 140.547 155.223 131.207 1.00 32.93 ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 141.333 155.110 129.983 1.00 32.57 ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 140.924 153.917 129.129 1.00 33.48 ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 141.157 153.927 127.915 1.00 36.62 ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 142.819 155.011 130.323 1.00 29.96 ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 143.174 153.686 130.677 1.00 32.02 ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 140.336 152.892 129.733 1.00 34.81 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 140.012 151.680 128.993 1.00 41.21 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 138.963 151.977 127.926 1.00 45.77 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 137.964 152.652 128.216 1.00 43.75 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 139.509 150.591 129.939 1.00 42.51 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 140.527 150.230 131.003 1.00 42.09 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 140.200 150.144 132.187 1.00 42.59 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 141.770 150.020 130.587 1.00 41.60 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 139.149 151.504 126.691 1.00 53.58 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 138.153 151.777 125.641 1.00 50.61 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 136.797 151.148 125.905 1.00 50.59 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 135.805 151.586 125.310 1.00 49.76 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 138.804 151.191 124.380 1.00 50.12 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 139.738 150.142 124.895 1.00 50.43 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 140.259 150.670 126.202 1.00 51.21 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 136.723 150.135 126.770 1.00 52.66 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 135.437 149.517 127.080 1.00 54.39 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 134.483 150.504 127.735 1.00 54.76 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 133.263 150.397 127.562 1.00 53.93 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 135.645 148.299 127.980 1.00 54.52 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 136.650 148.558 129.086 1.00 54.97 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 136.450 149.432 129.930 1.00 50.96 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 137.739 147.799 129.084 1.00 53.71 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 135.012 151.464 128.488 1.00 52.71 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 134.174 152.489 129.093 1.00 53.35 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 133.575 153.396 128.024 1.00 51.95 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 134.243 153.770 127.055 1.00 49.26 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 134.982 153.321 130.089 1.00 50.91 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 134.347 154.653 130.422 1.00 51.69 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 133.185 154.721 131.180 1.00 51.28 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 134.904 155.841 129.971 1.00 50.28 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 132.599 155.937 131.482 1.00 52.81 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 134.326 157.060 130.268 1.00 48.03 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 133.176 157.102 131.024 1.00 51.27 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 132.597 158.314 131.322 1.00 49.69 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 132.306 153.747 128.208 1.00 54.05 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 131.602 154.674 127.335 1.00 54.82 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 131.071 155.829 128.171 1.00 55.81 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 130.482 155.607 129.234 1.00 54.29 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 130.455 153.975 126.599 1.00 54.03 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 129.554 153.193 127.532 1.00 55.11 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 130.059 152.287 128.228 1.00 55.30 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 128.340 153.484 127.572 1.00 53.62 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 131.282 157.057 127.692 1.00 55.91 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 130.833 158.231 128.432 1.00 56.46 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 129.317 158.285 128.569 1.00 56.08 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 128.810 159.022 129.421 1.00 54.47 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 131.342 159.507 127.760 1.00 54.86 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 132.857 159.650 127.763 1.00 53.94 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 133.296 160.922 127.055 1.00 54.47 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 132.795 160.957 125.621 1.00 55.14 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 133.195 162.212 124.926 1.00 55.05 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 128.587 157.525 127.750 1.00 52.75 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 127.135 157.473 127.890 1.00 51.59 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 126.719 156.799 129.191 1.00 50.72 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 125.619 157.049 129.697 1.00 51.07 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 126.520 156.742 126.696 1.00 51.42 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 127.120 155.447 126.567 1.00 52.43 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 126.750 157.528 125.415 1.00 49.39 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 127.578 155.948 129.747 1.00 49.24 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 127.279 155.251 130.991 1.00 50.46 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 127.542 156.182 132.174 1.00 51.36 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 127.736 157.391 132.017 1.00 48.60 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 128.092 153.963 131.083 1.00 47.41 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 129.478 154.240 131.198 1.00 46.77 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 127.540 155.623 133.379 1.00 46.35 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 127.779 156.420 134.573 1.00 44.68 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 129.190 156.998 134.543 1.00 47.07 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 130.137 156.287 134.176 1.00 45.02 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 127.583 155.574 135.830 1.00 40.93 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 129.373 158.265 134.906 1.00 42.75 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 130.719 158.851 134.886 1.00 40.09 ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 131.632 158.170 135.892 1.00 37.51 ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 131.189 157.657 136.922 1.00 37.29 ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 130.475 160.321 135.253 1.00 39.22 ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 129.016 160.550 134.998 1.00 37.02 ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 128.353 159.246 135.307 1.00 37.75 ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 132.927 158.165 135.576 1.00 32.24 ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 133.910 157.561 136.468 1.00 31.99 ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 133.959 158.350 137.767 1.00 30.23 ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 134.202 159.563 137.768 1.00 30.38 ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 135.286 157.495 135.800 1.00 30.30 ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 135.210 156.759 134.459 1.00 31.98 ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 136.288 156.823 136.719 1.00 28.01 ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 134.334 155.523 134.481 1.00 32.48 ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 133.729 157.662 138.881 1.00 23.07 ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 133.753 158.260 140.205 1.00 21.66 ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 134.719 157.489 141.093 1.00 23.36 ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 135.013 156.313 140.864 1.00 25.91 ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 132.355 158.278 140.837 1.00 26.33 ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 131.850 156.940 140.922 1.00 31.57 ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 131.400 159.122 140.008 1.00 22.82 ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 135.217 158.174 142.117 1.00 19.36 ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 136.145 157.582 143.065 1.00 18.22 ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 135.711 157.931 144.480 1.00 17.47 ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 134.901 158.835 144.702 1.00 21.40 ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 137.588 158.043 142.813 1.00 18.69 ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 137.952 159.713 143.373 1.00 32.40 ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 136.261 157.191 145.438 1.00 17.33 ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 135.897 157.317 146.846 1.00 18.54 ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 136.854 158.305 147.503 1.00 21.49 ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 137.980 157.953 147.861 1.00 25.17 ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 135.949 155.951 147.523 1.00 23.15 ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 135.697 155.960 149.016 1.00 24.07 ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 134.223 156.019 149.349 1.00 26.48 ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 133.879 156.505 150.445 1.00 26.64 ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 133.407 155.577 148.516 1.00 26.01 ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 136.410 159.551 147.659 1.00 15.93 ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 137.214 160.602 148.271 1.00 13.23 ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 136.441 161.203 149.434 1.00 17.48 ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 135.321 161.689 149.250 1.00 21.27 ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 137.574 161.685 147.252 1.00 12.40 ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 138.828 161.464 146.407 1.00 11.52 ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 138.927 162.528 145.331 1.00 12.21 ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 140.068 161.466 147.278 1.00 14.24 ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 137.049 161.178 150.622 1.00 17.59 ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 136.449 161.736 151.835 1.00 14.48 ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 135.048 161.180 152.069 1.00 16.90 ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 134.109 161.912 152.387 1.00 18.25 ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 136.429 163.264 151.784 1.00 15.81 ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 137.790 163.957 151.853 1.00 12.97 ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 137.615 165.449 152.062 1.00 14.22 ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 138.643 163.354 152.954 1.00 10.17 ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 134.911 159.863 151.899 1.00 16.69 ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 133.643 159.157 152.083 1.00 18.26 ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 132.554 159.686 151.151 1.00 20.37 ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 131.367 159.649 151.483 1.00 24.30 ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 133.177 159.218 153.540 1.00 21.28 ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 134.174 158.596 154.495 1.00 23.15 ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 134.733 159.275 155.356 1.00 22.45 ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 134.400 157.297 154.349 1.00 21.84 ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 132.948 160.173 149.978 1.00 19.41 ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 132.013 160.673 148.982 1.00 17.38 ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 132.379 160.114 147.615 1.00 22.46 ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 133.542 159.812 147.338 1.00 27.42 ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 132.008 162.207 148.922 1.00 19.11 ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 131.616 162.889 150.222 1.00 21.18 ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 130.178 162.582 150.598 1.00 22.72 ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 129.798 163.251 151.907 1.00 23.62 ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 128.487 162.766 152.418 1.00 23.29 ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 131.369 159.974 146.761 1.00 20.47 ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 131.574 159.560 145.374 1.00 19.43 ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 131.818 160.817 144.553 1.00 18.81 ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 130.889 161.577 144.269 1.00 24.22 ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 130.374 158.772 144.859 1.00 19.04 ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 130.337 157.323 145.313 1.00 22.32 ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 131.520 156.523 144.810 1.00 21.29 ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 131.760 156.439 143.606 1.00 18.92 ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 132.265 155.924 145.731 1.00 21.36 ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 133.071 161.042 144.170 1.00 15.79 ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 133.481 162.248 143.461 1.00 16.85 ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 133.812 161.875 142.026 1.00 18.25 ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 134.626 160.975 141.787 1.00 19.40 ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 134.681 162.921 144.148 1.00 17.06 ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 135.319 163.944 143.225 1.00 17.28 ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 134.243 163.570 145.450 1.00 20.37 ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 133.175 162.553 141.076 1.00 17.76 ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 133.436 162.292 139.667 1.00 16.63 ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 134.856 162.711 139.305 1.00 16.01 ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 135.341 163.760 139.735 1.00 16.85 ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 132.426 163.037 138.795 1.00 12.96 ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 132.545 162.738 137.312 1.00 17.86 ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 132.220 163.965 136.477 1.00 21.88 ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 133.299 165.027 136.614 1.00 20.96 ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 133.374 165.903 135.413 1.00 17.17 ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 135.522 161.881 138.508 1.00 15.66 ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 136.910 162.098 138.112 1.00 11.08 ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 136.942 162.458 136.634 1.00 13.27 ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 136.391 161.730 135.799 1.00 21.20 ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 137.777 160.860 138.393 1.00 10.27 ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 139.179 161.063 137.851 1.00 12.49 ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 137.817 160.572 139.881 1.00 11.22 ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 137.581 163.579 136.315 1.00 12.22 ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 137.737 164.053 134.946 1.00 7.35  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 139.034 163.518 134.343 1.00 11.33 ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 140.060 163.468 135.026 1.00 15.58 ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 137.739 165.574 134.900 1.00 4.71  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 137.941 166.050 133.581 1.00 12.67 ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 139.009 163.110 133.071 1.00 11.40 ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 140.215 162.527 132.462 1.00 9.87  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 141.380 163.495 132.333 1.00 11.10 ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 142.519 163.042 132.170 1.00 14.60 ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 139.723 162.064 131.083 1.00 11.06 ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 138.532 162.915 130.804 1.00 10.02 ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 137.878 163.155 132.129 1.00 10.35 ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 141.138 164.805 132.399 1.00 3.92  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 142.210 165.783 132.261 1.00 4.19  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 142.980 166.010 133.554 1.00 9.42  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 143.947 166.777 133.552 1.00 15.46 ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 141.641 167.116 131.769 1.00 7.95  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 141.195 167.062 130.324 1.00 16.46 ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 141.027 165.944 129.793 1.00 18.11 ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 141.014 168.138 129.717 1.00 17.45 ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 142.577 165.369 134.645 1.00 6.22  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 143.194 165.592 135.939 1.00 4.21  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 144.497 164.812 136.072 1.00 8.00  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 144.658 163.727 135.509 1.00 15.43 ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 142.224 165.195 137.050 1.00 7.68  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 142.630 165.616 138.446 1.00 14.89 ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 143.466 164.257 139.265 1.00 19.64 ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 142.310 162.951 138.876 1.00 11.69 ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 145.435 165.384 136.827 1.00 9.11  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 146.721 164.755 137.075 1.00 5.99  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 147.287 165.276 138.386 1.00 8.98  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 146.904 166.342 138.870 1.00 15.92 ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 147.706 165.013 135.932 1.00 7.64  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 148.208 164.505 138.959 1.00 8.28  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 148.874 164.853 140.209 1.00 8.47  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 150.376 164.832 139.973 1.00 8.58  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 150.914 163.850 139.450 1.00 11.08 ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 148.494 163.892 141.351 1.00 7.89  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 146.975 163.762 141.466 1.00 10.42 ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 149.084 164.369 142.667 1.00 6.35  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 146.530 162.687 142.427 1.00 7.24  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 151.048 165.916 140.352 1.00 7.59  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 152.497 166.018 140.274 1.00 7.62  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 153.027 166.514 141.608 1.00 10.44 ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 152.413 167.375 142.244 1.00 18.04 ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 152.942 166.964 139.153 1.00 12.05 ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 152.645 166.457 137.775 1.00 9.95  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 151.379 166.585 137.232 1.00 11.73 ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 153.629 165.850 137.019 1.00 9.25  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 151.104 166.116 135.968 1.00 12.72 ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 153.358 165.379 135.753 1.00 9.79  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 152.096 165.512 135.227 1.00 9.39  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 154.161 165.967 142.036 1.00 6.77  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 154.793 166.351 143.293 1.00 5.32  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 156.248 166.687 142.986 1.00 6.71  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 156.980 165.865 142.427 1.00 15.47 ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 154.682 165.260 144.366 1.00 5.69  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 155.209 163.918 143.857 1.00 5.71  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 153.236 165.101 144.805 1.00 6.49  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 155.370 162.878 144.940 1.00 4.01  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 156.668 167.903 143.321 1.00 7.71  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 158.061 168.291 143.173 1.00 6.25  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 158.681 168.474 144.549 1.00 9.76  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 158.149 169.198 145.395 1.00 16.17 ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 158.197 169.582 142.362 1.00 7.32  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 157.608 170.667 143.081 1.00 14.93 ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 157.487 169.444 141.029 1.00 5.49  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 159.809 167.808 144.773 1.00 7.32  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 160.430 167.787 146.085 1.00 8.82  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 161.940 167.775 145.928 1.00 2.83  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 162.473 167.404 144.880 1.00 6.12  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 159.971 166.569 146.897 1.00 8.74  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 160.449 165.248 146.317 1.00 8.03  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 159.775 163.808 147.153 1.00 9.41  ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 158.040 164.229 147.145 1.00 6.59  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 162.624 168.194 146.988 1.00 6.11  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 164.078 168.119 147.064 1.00 8.49  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 164.449 167.134 148.163 1.00 11.59 ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 164.385 167.480 149.353 1.00 14.20 ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 164.686 169.494 147.339 1.00 9.03  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 166.204 169.474 147.322 1.00 14.37 ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 166.823 168.470 146.975 1.00 16.75 ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 166.807 170.601 147.667 1.00 11.36 ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 164.828 165.900 147.823 1.00 11.47 ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 165.163 164.918 148.865 1.00 15.71 ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 166.476 165.200 149.571 1.00 20.00 ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 166.808 164.483 150.522 1.00 15.96 ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 165.214 163.598 148.088 1.00 13.79 ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 165.608 163.999 146.708 1.00 11.27 ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 164.997 165.354 146.465 1.00 10.49 ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 167.229 166.214 149.146 1.00 21.22 ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 168.504 166.505 149.768 1.00 18.03 ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 168.442 167.340 151.028 1.00 20.10 ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 169.470 167.494 151.694 1.00 24.13 ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 167.276 167.878 151.379 1.00 17.28 ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 167.138 168.623 152.622 1.00 16.79 ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 167.015 167.667 153.799 1.00 24.47 ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 166.169 166.768 153.797 1.00 24.75 ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 165.927 169.556 152.575 1.00 14.14 ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 166.058 170.716 151.616 1.00 22.79 ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 167.290 171.069 151.084 1.00 22.20 ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 164.950 171.465 151.248 1.00 21.96 ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 167.416 172.139 150.218 1.00 19.56 ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 165.064 172.531 150.377 1.00 21.41 ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 166.297 172.863 149.863 1.00 22.77 ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 166.422 173.923 148.995 1.00 20.69 ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 167.870 167.861 154.798 1.00 27.93 ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 167.772 167.099 156.031 1.00 26.44 ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 166.536 167.520 156.816 1.00 26.69 ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 166.120 168.681 156.788 1.00 23.66 ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 169.026 167.294 156.881 1.00 25.55 ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 165.946 166.559 157.518 1.00 23.57 ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 164.750 166.813 158.289 1.00 24.44 ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 163.458 166.738 157.509 1.00 24.22 ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 162.397 167.022 158.077 1.00 25.92 ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 163.508 166.375 156.233 1.00 19.05 ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 162.307 166.211 155.431 1.00 13.45 ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 161.785 164.787 155.553 1.00 12.23 ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 162.538 163.848 155.826 1.00 15.03 ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 162.580 166.544 153.964 1.00 13.34 ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 162.826 168.016 153.705 1.00 14.59 ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 161.524 168.762 153.493 1.00 10.50 ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 161.710 170.206 153.556 1.00 16.93 ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 161.767 171.001 152.497 1.00 15.60 ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 161.648 170.525 151.269 1.00 11.92 ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 161.946 172.306 152.676 1.00 13.49 ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 160.480 164.636 155.350 1.00 7.09  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 159.845 163.337 155.494 1.00 4.27  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 160.273 162.391 154.379 1.00 7.11  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 160.573 162.807 153.257 1.00 11.76 ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 158.326 163.484 155.491 1.00 4.99  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 157.903 164.395 156.489 1.00 14.29 ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 160.305 161.103 154.703 1.00 9.70  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 160.571 160.059 153.725 1.00 8.05  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 159.242 159.504 153.233 1.00 8.25  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 158.426 159.035 154.032 1.00 11.85 ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 161.427 158.948 154.331 1.00 8.74  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 162.808 159.425 154.724 1.00 15.15 ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 163.623 159.774 153.870 1.00 12.67 ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 163.080 159.444 156.023 1.00 12.96 ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 159.023 159.567 151.928 1.00 4.10  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 157.779 159.067 151.365 1.00 4.04  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 157.723 157.549 151.494 1.00 5.09  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 158.705 156.869 151.180 1.00 7.29  ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 157.646 159.476 149.900 1.00 3.66  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 157.071 160.863 149.613 1.00 5.58  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 158.065 161.957 149.961 1.00 3.51  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 156.648 160.957 148.158 1.00 8.67  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 156.611 156.987 151.962 1.00 3.20  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 156.496 155.526 152.021 1.00 5.63  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 156.551 154.918 150.627 1.00 5.69  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 156.173 155.545 149.636 1.00 7.16  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 155.132 155.300 152.684 1.00 4.21  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 154.404 156.590 152.539 1.00 2.95  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 155.441 157.660 152.550 1.00 2.09  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 157.040 153.678 150.564 1.00 3.90  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 157.251 153.026 149.275 1.00 4.81  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 155.938 152.836 148.524 1.00 8.27  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 155.905 152.918 147.291 1.00 12.18 ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 157.956 151.686 149.475 1.00 9.76  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 159.198 151.807 150.334 1.00 17.79 ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 160.057 152.658 150.021 1.00 17.62 ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 159.315 151.053 151.323 1.00 18.02 ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 154.846 152.578 149.247 1.00 8.64  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 153.554 152.435 148.584 1.00 4.52  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 153.074 153.758 148.004 1.00 4.35  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 152.227 153.767 147.103 1.00 7.21  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 152.519 151.865 149.555 1.00 4.27  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 152.096 152.861 150.611 1.00 5.81  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 152.931 153.477 151.268 1.00 7.79  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 150.790 153.024 150.781 1.00 7.11  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 153.596 154.879 148.502 1.00 0.09  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 153.304 156.173 147.898 1.00 1.57  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 154.278 156.491 146.771 1.00 1.28  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 153.887 157.074 145.753 1.00 6.20  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 153.344 157.273 148.960 1.00 5.21  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 153.159 158.711 148.474 1.00 2.04  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 151.766 158.918 147.907 1.00 3.93  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 153.434 159.692 149.597 1.00 0.84  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 155.548 156.112 146.934 1.00 2.43  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 156.539 156.365 145.895 1.00 0.00  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 156.256 155.556 144.637 1.00 0.80  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 156.583 156.000 143.532 1.00 6.23  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 157.939 156.051 146.417 1.00 2.22  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 158.567 157.171 147.220 1.00 1.78  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 160.035 156.896 147.489 1.00 1.12  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 160.206 155.763 148.481 1.00 6.37  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 161.619 155.621 148.919 1.00 9.60  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 155.661 154.372 144.781 1.00 1.27  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 155.352 153.539 143.625 1.00 1.95  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 154.233 154.114 142.765 1.00 2.60  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 154.042 153.644 141.639 1.00 6.97  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 154.985 152.128 144.082 1.00 4.01  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 153.496 151.900 144.274 1.00 5.74  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 153.224 150.559 144.926 1.00 7.70  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 151.732 150.309 145.058 1.00 10.63 ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 151.053 151.407 145.797 1.00 9.66  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 153.499 155.106 143.260 1.00 1.57  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 152.422 155.732 142.509 1.00 0.85  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 152.904 156.864 141.612 1.00 2.99  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 152.102 157.419 140.856 1.00 5.84  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 151.352 156.266 143.465 1.00 1.39  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 150.660 155.249 144.372 1.00 3.17  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 149.829 155.962 145.423 1.00 3.05  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 149.797 154.304 143.558 1.00 5.78  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 154.185 157.217 141.677 1.00 4.95  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 154.740 158.325 140.916 1.00 0.00  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 155.956 157.853 140.136 1.00 1.86  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 156.733 157.025 140.620 1.00 5.90  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 155.143 159.486 141.836 1.00 0.00  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 153.988 160.129 142.547 1.00 0.41  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 153.551 159.644 143.767 1.00 0.68  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 153.345 161.227 142.002 1.00 1.64  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 152.490 160.235 144.422 1.00 2.47  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 152.285 161.821 142.652 1.00 1.24  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 151.857 161.324 143.864 1.00 2.09  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 156.115 158.379 138.926 1.00 1.35  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 157.331 158.191 138.148 1.00 0.00  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 158.266 159.358 138.437 1.00 1.67  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 157.898 160.518 138.230 1.00 9.15  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 157.020 158.103 136.656 1.00 0.00  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 156.530 156.743 136.206 1.00 3.76  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 157.694 155.826 135.874 1.00 2.67  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 158.139 155.985 134.496 1.00 5.60  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 157.515 155.475 133.443 1.00 10.23 ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 156.409 154.760 133.573 1.00 9.06  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 158.015 155.685 132.229 1.00 8.58  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 159.461 159.053 138.929 1.00 0.00  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 160.395 160.070 139.381 1.00 0.00  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 161.412 160.396 138.296 1.00 3.15  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 161.755 159.555 137.461 1.00 8.58  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 161.120 159.617 140.649 1.00 6.22  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 162.032 158.572 140.369 1.00 10.12 ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 161.883 161.640 138.313 1.00 0.00  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 162.907 162.103 137.387 1.00 0.72  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 163.863 163.037 138.107 1.00 0.80  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 163.426 163.965 138.790 1.00 7.49  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 162.297 162.829 136.188 1.00 3.39  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 163.350 163.321 135.195 1.00 6.84  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 164.011 162.160 134.466 1.00 4.34  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 162.757 164.302 134.227 1.00 3.05  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 165.161 162.813 137.930 1.00 0.47  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 166.171 163.663 138.543 1.00 0.08  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 166.395 164.899 137.682 1.00 2.20  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 166.877 164.795 136.550 1.00 7.60  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 167.474 162.894 138.731 1.00 4.85  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 166.045 166.064 138.216 1.00 2.16  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 166.280 167.351 137.566 1.00 5.62  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 167.337 168.079 138.392 1.00 8.06  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 167.021 168.767 139.363 1.00 11.02 ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 164.992 168.159 137.458 1.00 2.79  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 163.981 167.589 136.483 1.00 5.06  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 162.595 168.702 136.207 1.00 11.32 ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 163.220 169.676 134.844 1.00 6.10  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 168.599 167.923 138.001 1.00 4.99  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 169.723 168.415 138.788 1.00 4.72  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 170.520 169.515 138.106 1.00 6.08  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 170.885 170.495 138.759 1.00 6.09  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 170.668 167.260 139.136 1.00 6.29  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 170.980 166.522 137.950 1.00 9.70  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 170.017 166.330 140.146 1.00 6.61  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 170.808 169.386 136.810 1.00 9.29  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 171.651 170.336 136.086 1.00 4.24  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 170.862 170.939 134.930 1.00 4.92  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 170.805 170.356 133.836 1.00 8.26  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 172.924 169.663 135.581 1.00 4.40  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 173.800 169.078 136.674 1.00 6.35  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 174.381 170.166 137.559 1.00 7.26  ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 175.448 169.610 138.486 1.00 8.73  ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 174.878 168.681 139.498 1.00 10.52 ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 170.235 172.095 135.126 1.00 5.68  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 169.599 172.784 134.000 1.00 3.93  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 170.631 173.272 132.998 1.00 6.94  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 171.777 173.571 133.342 1.00 11.81 ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 168.870 173.956 134.665 1.00 1.35  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 169.574 174.156 135.964 1.00 5.88  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 170.018 172.796 136.402 1.00 8.80  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 170.208 173.348 131.736 1.00 4.48  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 171.074 173.813 130.653 1.00 2.07  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 171.009 175.336 130.605 1.00 5.66  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 170.317 175.941 129.784 1.00 14.64 ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 170.657 173.188 129.328 1.00 5.56  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 170.748 171.675 129.343 1.00 14.60 ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 171.875 171.146 129.442 1.00 17.64 ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 169.693 171.012 129.264 1.00 9.22  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 171.760 175.967 131.513 1.00 5.59  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 171.712 177.420 131.637 1.00 5.21  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 172.231 178.118 130.388 1.00 5.24  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 171.776 179.221 130.064 1.00 8.35  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 172.516 177.874 132.856 1.00 4.88  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 172.200 177.125 134.134 1.00 4.40  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 173.401 177.119 135.059 1.00 6.97  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 173.065 176.651 136.397 1.00 13.82 ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 173.435 177.259 137.514 1.00 15.20 ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 174.149 178.374 137.490 1.00 12.66 ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 173.082 176.739 138.686 1.00 10.47 ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 173.183 177.505 129.685 1.00 7.43  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 173.731 178.122 128.481 1.00 7.54  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 172.657 178.296 127.414 1.00 8.61  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 172.500 179.382 126.843 1.00 15.28 ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 174.890 177.280 127.948 1.00 11.19 ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 175.270 177.576 126.510 1.00 13.71 ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 176.384 178.593 126.401 1.00 19.02 ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 176.366 179.460 125.528 1.00 21.50 ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 177.361 178.497 127.292 1.00 17.82 ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 171.770 177.328 127.237 1.00 5.26  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 170.735 177.413 126.169 1.00 3.31  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 169.602 178.336 126.601 1.00 5.54  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 169.107 179.056 125.752 1.00 10.51 ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 170.158 176.060 125.761 1.00 4.89  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 169.003 176.087 124.760 1.00 9.21  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 169.503 176.623 123.441 1.00 8.53  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 168.463 174.687 124.589 1.00 10.52 ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 169.198 178.294 127.862 1.00 3.47  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 168.096 179.149 128.392 1.00 0.00  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 168.496 180.609 128.220 1.00 3.17  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 167.631 181.401 127.888 1.00 12.33 ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 167.813 178.825 129.864 1.00 2.58  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 167.321 177.398 130.034 1.00 3.92  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 166.843 179.837 130.467 1.00 3.21  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 167.310 176.923 131.472 1.00 2.86  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 169.756 180.951 128.454 1.00 2.65  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 170.242 182.319 128.216 1.00 0.00  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 170.231 182.535 126.723 1.00 4.26  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 169.421 183.313 126.227 1.00 10.08 ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 171.637 182.461 128.722 1.00 1.56  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 171.036 181.769 126.012 1.00 5.71  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 171.145 182.070 124.589 1.00 5.31  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 169.776 182.330 123.973 1.00 5.84  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 169.584 183.323 123.264 1.00 11.39 ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 171.854 180.923 123.871 1.00 6.86  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 171.633 180.895 122.372 1.00 11.58 ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 172.015 179.565 121.759 1.00 18.07 ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 172.994 178.940 122.165 1.00 16.61 ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 171.239 179.122 120.777 1.00 15.24 ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 168.802 181.463 124.256 1.00 5.99  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 167.477 181.627 123.664 1.00 2.67  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 166.780 182.854 124.236 1.00 3.11  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 166.090 183.582 123.511 1.00 10.93 ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 166.639 180.350 123.861 1.00 3.56  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 165.229 180.555 123.336 1.00 4.11  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 167.297 179.179 123.157 1.00 5.52  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 166.942 183.110 125.537 1.00 0.62  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 166.307 184.277 126.139 1.00 0.10  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 166.858 185.573 125.559 1.00 6.34  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 166.098 186.506 125.281 1.00 14.72 ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 166.496 184.252 127.654 1.00 0.70  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 165.556 183.316 128.378 1.00 2.37  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 165.524 183.655 130.141 1.00 15.31 ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 164.740 185.264 130.158 1.00 9.71  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 168.177 185.651 125.374 1.00 2.97  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 168.756 186.858 124.795 1.00 3.84  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 168.447 186.970 123.308 1.00 6.06  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 168.340 188.083 122.781 1.00 13.34 ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 170.262 186.877 125.042 1.00 9.01  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 170.634 187.085 126.511 1.00 6.70  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 172.130 187.014 126.708 1.00 5.82  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 170.090 188.410 127.020 1.00 7.84  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 168.299 185.837 122.616 1.00 6.33  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 167.901 185.868 121.213 1.00 2.79  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 166.479 186.390 121.052 1.00 4.54  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 166.204 187.194 120.154 1.00 6.44  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 168.036 184.468 120.614 1.00 2.39  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 167.774 184.388 119.129 1.00 6.50  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 168.415 185.241 118.245 1.00 8.25  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 166.897 183.447 118.612 1.00 7.98  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 168.181 185.165 116.887 1.00 9.26  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 166.657 183.364 117.257 1.00 7.39  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 167.301 184.224 116.399 1.00 8.39  ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 167.065 184.144 115.048 1.00 11.03 ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 165.563 185.947 121.915 1.00 4.81  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 164.170 186.363 121.808 1.00 2.17  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 163.947 187.787 122.292 1.00 4.47  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 162.947 188.405 121.916 1.00 9.33  ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 163.273 185.406 122.593 1.00 2.57  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 163.599 185.418 123.970 1.00 2.70  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 164.848 188.321 123.117 1.00 8.22  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 164.697 189.676 123.625 1.00 8.61  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 165.244 190.735 122.678 1.00 11.00 ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 165.055 191.927 122.938 1.00 15.95 ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 165.374 189.808 124.991 1.00 5.29  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 164.504 189.361 126.152 1.00 4.73  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 165.292 189.157 127.431 1.00 10.80 ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 166.490 189.430 127.485 1.00 13.32 ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 164.621 188.672 128.467 1.00 10.22 ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 165.904 190.337 121.595 1.00 9.38  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 166.393 191.273 120.606 1.00 8.45  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 167.884 191.533 120.615 1.00 11.00 ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 168.333 192.451 119.919 1.00 19.31 ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 168.664 190.769 121.371 1.00 10.65 ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 170.108 190.955 121.391 1.00 12.40 ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 170.733 190.304 120.164 1.00 18.54 ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 170.524 189.114 119.908 1.00 20.69 ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 170.708 190.369 122.669 1.00 9.99  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 170.368 191.142 123.912 1.00 10.22 ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 169.134 190.997 124.520 1.00 11.59 ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 171.284 192.014 124.472 1.00 12.93 ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 168.821 191.705 125.661 1.00 11.79 ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 170.978 192.723 125.616 1.00 14.87 ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 169.744 192.569 126.209 1.00 13.95 ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 171.500 191.089 119.404 1.00 24.11 ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 172.128 190.563 118.195 1.00 26.72 ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 173.254 189.591 118.518 1.00 28.68 ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 173.510 188.662 117.743 1.00 29.07 ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 172.660 191.709 117.336 1.00 26.85 ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 171.620 192.748 116.956 1.00 28.58 ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 172.219 193.993 116.284 1.00 34.45 ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 173.483 194.443 116.862 1.00 36.93 ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 174.685 194.053 116.455 1.00 34.65 ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 174.834 193.215 115.442 1.00 31.72 ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 175.763 194.521 117.076 1.00 33.07 ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 173.931 189.784 119.647 1.00 24.85 ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 175.076 188.972 120.052 1.00 21.87 ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 174.703 187.970 121.134 1.00 25.19 ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 175.468 187.746 122.075 1.00 29.65 ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 176.218 189.868 120.521 1.00 22.98 ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 175.751 190.731 121.565 1.00 24.00 ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 176.732 190.716 119.371 1.00 25.67 ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 173.523 187.356 121.016 1.00 21.20 ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 172.989 186.530 122.095 1.00 16.71 ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 173.903 185.356 122.423 1.00 20.05 ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 174.081 185.013 123.597 1.00 20.94 ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 171.592 186.032 121.727 1.00 14.95 ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 174.478 184.713 121.404 1.00 19.87 ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 175.343 183.562 121.654 1.00 22.43 ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 176.594 183.970 122.424 1.00 25.06 ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 176.974 183.320 123.407 1.00 28.10 ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 175.720 182.892 120.333 1.00 24.98 ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 174.561 182.204 119.634 1.00 27.35 ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 175.001 181.417 118.416 1.00 31.15 ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 176.209 181.430 118.101 1.00 30.05 ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 174.138 180.787 117.771 1.00 27.20 ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 177.246 185.051 121.990 1.00 21.03 ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 178.434 185.539 122.687 1.00 20.77 ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 178.076 185.975 124.100 1.00 20.71 ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 178.803 185.687 125.060 1.00 24.77 ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 179.086 186.684 121.890 1.00 20.69 ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 180.222 187.304 122.682 1.00 20.31 ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 179.582 186.177 120.548 1.00 23.63 ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 176.947 186.668 124.250 1.00 18.17 ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 176.523 187.128 125.568 1.00 15.37 ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 176.277 185.958 126.513 1.00 17.88 ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 176.669 186.007 127.682 1.00 18.89 ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 175.270 187.988 125.435 1.00 15.05 ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 175.459 189.391 124.865 1.00 12.64 ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 174.117 190.029 124.604 1.00 16.95 ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 176.258 190.237 125.827 1.00 18.12 ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 175.629 184.896 126.028 1.00 14.40 ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 175.379 183.730 126.872 1.00 13.23 ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 176.679 183.022 127.234 1.00 18.64 ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 176.896 182.649 128.398 1.00 26.25 ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 174.422 182.771 126.168 1.00 12.66 ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 177.556 182.826 126.243 1.00 17.65 ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 178.840 182.180 126.489 1.00 19.20 ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 179.725 182.999 127.412 1.00 20.56 ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 180.659 182.453 128.006 1.00 21.39 ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 179.563 181.928 125.166 1.00 17.91 ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 178.886 180.868 124.323 1.00 21.00 ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 178.836 179.698 124.698 1.00 22.64 ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 178.359 181.274 123.175 1.00 21.18 ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 179.469 184.300 127.526 1.00 16.16 ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 180.187 185.137 128.475 1.00 13.99 ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 179.509 185.216 129.835 1.00 16.09 ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 180.194 185.444 130.838 1.00 21.95 ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 180.345 186.552 127.914 1.00 13.50 ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 181.451 186.708 126.892 1.00 12.49 ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 181.475 188.121 126.335 1.00 16.07 ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 182.799 188.428 125.657 1.00 18.74 ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 183.947 188.267 126.592 1.00 15.53 ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 178.193 185.031 129.896 1.00 13.72 ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 177.469 185.293 131.134 1.00 11.83 ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 177.270 184.038 131.984 1.00 11.25 ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 177.189 184.139 133.211 1.00 17.46 ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 176.124 185.975 130.829 1.00 11.68 ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 175.606 186.709 132.067 1.00 12.91 ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 175.091 184.971 130.344 1.00 11.08 ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 176.598 187.685 132.648 1.00 11.68 ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 177.191 182.857 131.380 1.00 10.07 ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 177.017 181.650 132.192 1.00 13.17 ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 178.338 181.295 132.878 1.00 18.26 ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 178.353 181.079 134.105 1.00 15.78 ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 176.459 180.484 131.358 1.00 13.61 ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 176.340 179.233 132.212 1.00 12.68 ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 175.113 180.860 130.768 1.00 11.03 ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 179.465 181.226 132.156 1.00 17.35 ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 180.744 181.049 132.857 1.00 12.16 ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 181.045 182.161 133.837 1.00 15.18 ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 181.741 181.921 134.827 1.00 19.18 ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 181.769 181.008 131.716 1.00 15.53 ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 180.999 180.524 130.557 1.00 18.89 ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 179.662 181.177 130.694 1.00 13.58 ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 180.547 183.377 133.596 1.00 14.65 ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 180.720 184.443 134.575 1.00 8.29  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 180.012 184.114 135.881 1.00 10.95 ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 180.551 184.358 136.967 1.00 19.49 ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 180.208 185.770 134.020 1.00 9.73  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 180.083 186.841 135.059 1.00 13.18 ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 181.205 187.501 135.531 1.00 14.15 ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 178.846 187.179 135.579 1.00 14.14 ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 181.092 188.482 136.493 1.00 12.60 ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 178.730 188.157 136.541 1.00 11.73 ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 179.852 188.813 136.996 1.00 11.51 ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 178.793 183.579 135.800 1.00 13.72 ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 178.088 183.182 137.013 1.00 14.22 ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 178.811 182.046 137.722 1.00 15.56 ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 178.902 182.034 138.956 1.00 16.69 ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 176.648 182.793 136.684 1.00 11.86 ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 175.679 183.935 136.773 1.00 10.23 ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 175.605 184.878 135.764 1.00 9.44  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 174.849 184.071 137.870 1.00 12.46 ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 174.719 185.931 135.842 1.00 8.98  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 173.960 185.124 137.956 1.00 14.61 ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 173.896 186.054 136.939 1.00 13.59 ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 179.346 181.087 136.959 1.00 16.39 ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 180.132 180.026 137.585 1.00 12.95 ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 181.373 180.588 138.274 1.00 17.45 ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 181.733 180.160 139.379 1.00 23.81 ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 180.520 178.980 136.542 1.00 14.28 ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 180.804 177.604 137.121 1.00 16.00 ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 181.238 176.635 136.036 1.00 19.27 ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 182.367 177.214 135.198 1.00 22.81 ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 182.442 176.582 133.853 1.00 20.24 ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 182.042 181.550 137.632 1.00 15.91 ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 183.221 182.177 138.221 1.00 15.56 ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 182.870 182.925 139.498 1.00 16.80 ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 183.624 182.885 140.474 1.00 22.87 ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 183.864 183.130 137.213 1.00 14.76 ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 184.774 182.528 136.143 1.00 18.23 ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 185.101 183.574 135.092 1.00 18.07 ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 186.043 181.988 136.771 1.00 22.43 ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 181.743 183.638 139.499 1.00 17.11 ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 181.309 184.325 140.711 1.00 14.42 ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 181.010 183.329 141.822 1.00 16.63 ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 181.334 183.574 142.989 1.00 18.90 ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 180.081 185.186 140.421 1.00 10.30 ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 180.451 186.731 139.584 1.00 30.25 ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 180.389 182.201 141.478 1.00 14.97 ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 180.103 181.184 142.482 1.00 9.94  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 181.385 180.610 143.072 1.00 18.17 ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 181.471 180.386 144.286 1.00 23.22 ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 179.249 180.075 141.871 1.00 15.81 ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 178.935 178.972 142.858 1.00 23.57 ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 178.215 179.241 143.842 1.00 23.05 ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 179.409 177.835 142.652 1.00 26.11 ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 182.393 180.370 142.236 1.00 24.65 ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 183.584 179.642 142.658 1.00 24.70 ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 184.769 180.534 143.013 1.00 24.87 ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 185.833 180.007 143.355 1.00 29.57 ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 184.001 178.652 141.566 1.00 22.06 ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 182.918 177.651 141.203 1.00 25.01 ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 183.363 176.665 140.144 1.00 29.09 ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 184.264 177.010 139.353 1.00 27.39 ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 182.811 175.546 140.101 1.00 30.64 ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 184.628 181.856 142.953 1.00 22.45 ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 185.768 182.731 143.207 1.00 17.77 ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 185.475 183.758 144.292 1.00 21.51 ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 186.394 184.231 144.968 1.00 25.54 ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 186.196 183.437 141.919 1.00 15.62 ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 186.845 182.519 140.900 1.00 20.25 ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 188.083 183.126 140.276 1.00 26.67 ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 188.191 184.343 140.143 1.00 28.13 ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 189.028 182.277 139.889 1.00 29.27 ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 184.209 184.124 144.459 1.00 21.10 ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 183.841 185.027 145.535 1.00 16.39 ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 183.817 184.284 146.866 1.00 18.96 ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 183.711 183.057 146.921 1.00 25.71 ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 182.482 185.672 145.263 1.00 15.76 ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 182.353 186.497 143.983 1.00 16.74 ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 181.024 187.226 143.954 1.00 14.08 ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 183.503 187.480 143.855 1.00 16.12 ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 183.923 185.050 147.951 1.00 13.21 ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 183.919 184.461 149.283 1.00 12.27 ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 182.588 183.770 149.557 1.00 10.10 ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 181.527 184.242 149.144 1.00 16.65 ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 184.181 185.535 150.337 1.00 12.12 ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 183.034 186.340 150.541 1.00 13.29 ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 182.651 182.642 150.257 1.00 6.67  ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 181.457 181.854 150.535 1.00 10.37 ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 180.629 182.543 151.612 1.00 9.95  ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 181.073 182.675 152.757 1.00 10.04 ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 181.840 180.442 150.970 1.00 14.14 ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 180.697 179.704 151.367 1.00 11.56 ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 179.427 182.978 151.245 1.00 8.40  ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 178.509 183.627 152.165 1.00 4.20  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 177.163 182.921 152.116 1.00 5.89  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 176.768 182.375 151.083 1.00 9.96  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 178.331 185.115 151.834 1.00 1.83  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 179.636 185.861 151.620 1.00 4.88  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 180.319 186.224 152.921 1.00 8.42  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 179.702 186.211 153.984 1.00 9.83  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 181.603 186.550 152.843 1.00 11.65 ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 176.461 182.935 153.250 1.00 7.58  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 175.183 182.239 153.345 1.00 6.83  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 174.088 182.912 152.528 1.00 9.50  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 173.092 182.260 152.200 1.00 11.33 ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 174.751 182.134 154.807 1.00 6.36  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 174.766 183.404 155.435 1.00 12.96 ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 174.245 184.192 152.196 1.00 5.09  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 173.249 184.928 151.430 1.00 3.61  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 173.614 185.052 149.956 1.00 7.13  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 172.968 185.814 149.231 1.00 13.83 ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 173.034 186.315 152.038 1.00 6.36  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 174.239 187.200 151.977 1.00 6.66  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 175.331 187.029 152.800 1.00 8.85  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 174.518 188.272 151.199 1.00 5.56  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 176.234 187.953 152.526 1.00 7.50  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 175.766 188.720 151.559 1.00 4.89  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 174.627 184.323 149.498 1.00 5.37  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 175.035 184.354 148.100 1.00 4.97  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 174.265 183.305 147.310 1.00 9.28  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 174.154 182.153 147.740 1.00 10.88 ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 176.537 184.102 147.968 1.00 6.23  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 177.397 185.325 148.163 1.00 6.61  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 176.850 186.523 148.597 1.00 4.43  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 178.757 185.283 147.905 1.00 9.38  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 177.638 187.640 148.773 1.00 5.80  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 179.549 186.394 148.077 1.00 9.01  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 178.986 187.570 148.512 1.00 5.56  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 179.780 188.678 148.684 1.00 8.99  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 173.739 183.708 146.156 1.00 7.36  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 173.063 182.789 145.249 1.00 3.14  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 173.425 183.166 143.822 1.00 6.59  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 173.155 184.288 143.388 1.00 5.20  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 171.545 182.824 145.440 1.00 7.75  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 170.812 182.018 144.386 1.00 14.85 ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 171.033 180.791 144.314 1.00 13.41 ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 170.018 182.612 143.627 1.00 11.54 ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 174.030 182.228 143.100 1.00 8.21  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 174.424 182.415 141.710 1.00 7.23  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 173.876 181.287 140.852 1.00 6.56  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 174.541 180.793 139.938 1.00 13.02 ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 175.942 182.510 141.583 1.00 9.23  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 176.549 183.608 142.406 1.00 10.31 ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 176.349 184.936 142.071 1.00 7.89  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 177.311 183.315 143.524 1.00 9.53  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 176.903 185.947 142.829 1.00 7.44  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 177.868 184.323 144.285 1.00 6.80  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 177.662 185.640 143.938 1.00 9.46  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 172.586 180.992 140.998 1.00 2.93  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 171.992 179.843 140.298 1.00 6.97  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 171.110 180.224 139.143 1.00 8.26  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 171.414 181.238 138.527 1.00 10.99 ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 170.046 179.469 138.867 1.00 6.89  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 169.229 179.713 137.651 1.00 4.61  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 168.224 180.831 137.919 1.00 4.34  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 167.950 181.590 136.990 1.00 5.78  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 168.531 178.456 137.138 1.00 4.81  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 167.670 178.615 135.885 1.00 5.65  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 168.491 179.141 134.732 1.00 8.72  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 167.064 177.274 135.534 1.00 7.61  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 167.685 180.918 139.131 1.00 7.43  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 166.672 181.951 139.457 1.00 3.96  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 167.405 183.287 139.501 1.00 7.23  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 166.745 184.318 139.372 1.00 13.31 ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 165.975 181.648 140.781 1.00 1.11  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 164.484 181.938 140.748 1.00 4.45  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 163.863 181.508 142.054 1.00 9.40  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 164.417 180.214 142.457 1.00 10.34 ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 163.676 179.153 142.691 1.00 7.88  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 162.425 179.135 142.282 1.00 7.84  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 164.181 178.125 143.339 1.00 2.45  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 168.728 183.251 139.622 1.00 7.29  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 169.535 184.488 139.608 1.00 5.97  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 170.027 184.802 138.207 1.00 5.62  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 170.395 185.950 138.008 1.00 9.74  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 170.705 184.363 140.514 1.00 6.56  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 170.087 183.839 137.294 1.00 3.19  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 170.454 184.151 135.897 1.00 3.47  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 169.179 184.670 135.256 1.00 5.74  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 169.247 185.701 134.606 1.00 12.50 ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 171.035 182.968 135.137 1.00 4.71  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 171.474 183.227 133.697 1.00 3.60  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 172.439 184.389 133.673 1.00 5.61  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 172.145 181.973 133.187 1.00 6.23  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 168.049 184.029 135.504 1.00 3.46  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 166.808 184.461 134.826 1.00 2.87  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 166.428 185.840 135.353 1.00 6.72  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 165.662 186.521 134.682 1.00 12.20 ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 165.671 183.455 134.987 1.00 4.34  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 164.528 183.634 134.010 1.00 4.16  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 163.659 182.390 133.919 1.00 5.73  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 162.453 182.623 133.075 1.00 7.36  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 161.651 183.711 133.634 1.00 8.26  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 166.947 186.233 136.509 1.00 4.06  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 166.601 187.543 137.110 1.00 5.41  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 167.445 188.583 136.407 1.00 6.81  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 167.011 189.731 136.298 1.00 10.60 ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 166.929 187.561 138.542 1.00 7.02  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 167.043 188.898 139.003 1.00 8.41  ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 168.615 188.173 135.980 1.00 5.06  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 169.567 189.034 135.281 1.00 4.11  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 169.174 189.192 133.819 1.00 5.66  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 169.241 190.286 133.255 1.00 10.71 ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 170.997 188.481 135.427 1.00 3.21  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 171.908 189.080 134.373 1.00 3.99  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 171.533 188.776 136.815 1.00 9.57  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 168.763 188.096 133.178 1.00 5.03  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 168.374 188.165 131.771 1.00 3.44  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 167.110 188.995 131.579 1.00 5.44  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 167.013 189.790 130.633 1.00 10.94 ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 168.181 186.757 131.210 1.00 4.47  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 169.425 185.869 131.190 1.00 1.88  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 169.047 184.442 130.849 1.00 1.84  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 170.458 186.402 130.214 1.00 6.90  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 166.123 188.822 132.464 1.00 5.62  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 164.907 189.629 132.373 1.00 7.93  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 165.236 191.105 132.566 1.00 7.93  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 164.736 191.976 131.836 1.00 10.00 ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 163.862 189.139 133.391 1.00 5.56  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 162.673 190.083 133.430 1.00 7.46  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 163.414 187.728 133.048 1.00 5.18  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 166.089 191.409 133.547 1.00 3.66  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 166.514 192.785 133.762 1.00 2.75  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 167.286 193.325 132.569 1.00 6.46  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 167.180 194.511 132.254 1.00 10.99 ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 167.362 192.877 135.030 1.00 6.68  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 166.601 192.536 136.174 1.00 12.15 ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 168.073 192.478 131.902 1.00 9.18  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 168.797 192.913 130.713 1.00 6.91  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 167.838 193.288 129.596 1.00 10.71 ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 168.030 194.300 128.914 1.00 16.03 ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 169.758 191.818 130.252 1.00 6.81  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 166.795 192.482 129.394 1.00 8.65  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 165.784 192.840 128.410 1.00 9.03  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 165.100 194.153 128.743 1.00 12.06 ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 164.920 195.019 127.877 1.00 15.13 ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 164.725 194.326 130.014 1.00 11.60 ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 164.072 195.565 130.432 1.00 9.70  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 164.991 196.768 130.245 1.00 13.39 ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 164.553 197.830 129.784 1.00 19.17 ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 163.623 195.457 131.888 1.00 11.03 ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 162.471 194.491 132.072 1.00 15.86 ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 161.793 194.127 131.112 1.00 16.09 ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 162.241 194.073 133.310 1.00 11.48 ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 166.269 196.621 130.596 1.00 14.20 ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 167.220 197.722 130.478 1.00 13.03 ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 167.470 198.057 129.016 1.00 14.30 ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 167.620 199.228 128.655 1.00 22.12 ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 168.525 197.378 131.220 1.00 11.61 ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 169.641 198.321 130.814 1.00 12.46 ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 168.309 197.438 132.721 1.00 11.65 ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 167.524 197.043 128.148 1.00 12.47 ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 167.674 197.313 126.723 1.00 13.69 ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 166.475 198.077 126.181 1.00 14.08 ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 166.634 199.019 125.397 1.00 17.64 ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 167.869 196.009 125.951 1.00 14.76 ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 168.241 196.222 124.495 1.00 14.44 ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 168.483 194.908 123.782 1.00 12.94 ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 167.176 194.281 123.343 1.00 10.71 ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 166.500 195.091 122.293 1.00 12.93 ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 165.264 197.686 126.591 1.00 14.47 ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 164.078 198.426 126.164 1.00 14.02 ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 164.125 199.869 126.655 1.00 19.67 ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 163.812 200.802 125.903 1.00 25.45 ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 162.816 197.730 126.668 1.00 13.48 ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 162.180 196.794 125.658 1.00 16.33 ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 160.959 196.099 126.241 1.00 16.22 ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 161.315 195.033 127.169 1.00 14.72 ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 161.851 193.872 126.815 1.00 19.64 ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 162.106 193.585 125.549 1.00 18.35 ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 162.133 192.977 127.756 1.00 19.99 ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 164.519 200.071 127.913 1.00 21.57 ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 164.598 201.421 128.464 1.00 18.94 ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 165.640 202.259 127.734 1.00 24.02 ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 165.412 203.442 127.456 1.00 27.94 ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 164.910 201.359 129.958 1.00 16.72 ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 164.842 202.702 130.661 1.00 24.24 ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 165.179 202.605 132.135 1.00 29.39 ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 165.534 201.500 132.594 1.00 27.59 ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 165.088 203.635 132.835 1.00 27.05 ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 166.793 201.667 127.417 1.00 23.42 ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 167.833 202.395 126.698 1.00 22.24 ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 167.389 202.743 125.285 1.00 26.78 ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 167.696 203.830 124.784 1.00 29.63 ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 169.123 201.577 126.664 1.00 21.75 ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 169.866 201.534 127.989 1.00 24.73 ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 171.363 201.391 127.774 1.00 24.90 ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 172.075 201.182 129.029 1.00 24.91 ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 173.395 201.145 129.141 1.00 27.39 ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 174.184 201.301 128.091 1.00 25.58 ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 173.938 200.948 130.339 1.00 25.01 ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 166.675 201.831 124.621 1.00 29.90 ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 166.152 202.128 123.291 1.00 27.10 ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 165.163 203.284 123.356 1.00 29.18 ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 165.197 204.200 122.525 1.00 32.84 ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 165.521 200.867 122.673 1.00 26.52 ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 166.610 199.963 122.092 1.00 25.61 ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 164.512 201.238 121.601 1.00 31.48 ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 166.261 198.498 122.111 1.00 25.55 ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 164.274 203.268 124.356 1.00 31.88 ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 163.332 204.371 124.524 1.00 33.59 ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 164.059 205.686 124.787 1.00 35.08 ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 163.689 206.731 124.239 1.00 39.42 ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 162.359 204.062 125.660 1.00 31.47 ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 161.351 202.975 125.335 1.00 32.02 ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 160.398 203.383 124.231 1.00 37.91 ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 160.443 202.844 123.126 1.00 38.29 ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 159.528 204.341 124.526 1.00 37.33 ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 165.096 205.649 125.625 1.00 36.27 ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 165.863 206.857 125.921 1.00 39.24 ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 166.550 207.399 124.674 1.00 40.63 ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 166.551 208.613 124.434 1.00 41.20 ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 166.887 206.561 127.016 1.00 39.33 ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 167.921 207.652 127.216 1.00 41.15 ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 168.880 207.302 128.342 1.00 41.58 ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 169.766 206.128 127.962 1.00 41.77 ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 170.695 206.466 126.848 1.00 39.37 ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 167.144 206.515 123.870 1.00 38.71 ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 167.820 206.950 122.650 1.00 38.96 ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 166.819 207.548 121.672 1.00 41.68 ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 167.090 208.570 121.027 1.00 43.32 ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 168.599 205.778 122.027 1.00 37.59 ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 169.846 205.468 122.856 1.00 40.79 ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 168.986 206.089 120.591 1.00 37.03 ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 170.678 204.329 122.310 1.00 41.48 ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 165.644 206.924 121.545 1.00 43.15 ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 164.611 207.476 120.674 1.00 41.28 ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 164.160 208.849 121.157 1.00 43.49 ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 163.942 209.757 120.347 1.00 44.60 ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 163.423 206.519 120.588 1.00 40.77 ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 163.740 205.196 119.914 1.00 43.22 ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 162.503 204.320 119.812 1.00 45.59 ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 161.895 204.388 118.422 1.00 44.15 ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 162.787 203.777 117.401 1.00 44.10 ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 164.013 209.022 122.473 1.00 48.95 ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 163.615 210.323 122.999 1.00 50.40 ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 164.684 211.378 122.734 1.00 52.60 ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 164.365 212.517 122.370 1.00 52.05 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 163.312 210.218 124.495 1.00 48.88 ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 163.721 211.436 125.307 1.00 50.27 ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 163.192 211.362 126.733 1.00 50.68 ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 163.865 210.348 127.537 1.00 52.85 ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 165.117 210.431 127.966 1.00 52.90 ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 165.876 211.478 127.688 1.00 51.68 ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 165.616 209.441 128.700 1.00 52.61 ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 165.961 211.019 122.904 1.00 51.37 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 167.033 211.964 122.606 1.00 50.14 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 167.036 212.350 121.133 1.00 51.00 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 167.223 213.523 120.791 1.00 51.57 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 168.394 211.389 122.999 1.00 49.78 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 168.549 211.033 124.462 1.00 52.26 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 169.814 210.240 124.725 1.00 54.33 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 169.925 209.630 125.809 1.00 53.24 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 170.700 210.224 123.845 1.00 51.09 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 166.843 211.373 120.243 1.00 51.00 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 166.784 211.682 118.817 1.00 51.02 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 165.597 212.582 118.497 1.00 51.37 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 165.701 213.489 117.664 1.00 50.58 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 166.718 210.392 118.000 1.00 50.35 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 168.057 209.690 117.845 1.00 50.00 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 167.902 208.352 117.142 1.00 50.01 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 169.233 207.856 116.602 1.00 49.39 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 170.271 207.787 117.667 1.00 49.31 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 164.455 212.340 119.146 1.00 53.82 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 163.278 213.169 118.914 1.00 55.53 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 163.498 214.603 119.384 1.00 56.94 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 163.112 215.552 118.694 1.00 57.31 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 162.062 212.557 119.607 1.00 54.72 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 160.732 213.160 119.182 1.00 55.08 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 160.296 214.299 120.083 1.00 55.59 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 160.652 214.282 121.281 1.00 56.22 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 159.597 215.212 119.594 1.00 54.21 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 164.115 214.783 120.553 1.00 59.72 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 164.305 216.126 121.088 1.00 60.62 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 165.527 216.832 120.514 1.00 59.88 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 165.716 218.022 120.785 1.00 59.20 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 164.400 216.082 122.617 1.00 59.52 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 165.600 215.327 123.166 1.00 59.84 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 166.774 216.235 123.473 1.00 60.72 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 166.573 217.466 123.543 1.00 60.10 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 167.897 215.718 123.653 1.00 60.43 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 166.355 216.138 119.737 1.00 61.26 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 167.511 216.727 119.066 1.00 62.07 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 167.380 216.407 117.580 1.00 62.96 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 167.892 215.390 117.102 1.00 62.44 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 168.822 216.201 119.644 1.00 60.49 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 169.224 216.854 120.956 1.00 61.70 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 169.446 218.348 120.783 1.00 61.64 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 170.480 218.635 119.796 1.00 65.22 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 170.270 219.280 118.657 1.00 64.01 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 169.067 219.719 118.321 1.00 61.54 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 171.291 219.491 117.832 1.00 62.19 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 166.696 217.280 116.849 1.00 56.50 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 166.406 217.026 115.456 1.00 55.64 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 165.273 216.030 115.291 1.00 55.18 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 164.522 215.725 116.221 1.00 52.93 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 165.153 215.517 114.066 1.00 55.98 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 164.132 214.520 113.731 1.00 56.29 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 164.790 213.458 112.851 1.00 56.36 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 164.825 213.585 111.623 1.00 56.51 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 162.933 215.161 113.045 1.00 54.85 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 162.040 215.962 113.982 1.00 55.47 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 160.999 216.779 113.243 1.00 57.00 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 160.219 216.186 112.467 1.00 57.29 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 160.959 218.011 113.438 1.00 55.07 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 165.310 212.411 113.490 1.00 50.23 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 165.927 211.302 112.765 1.00 50.24 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 165.883 210.076 113.668 1.00 50.31 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 166.653 209.992 114.629 1.00 50.14 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 167.357 211.642 112.363 1.00 47.12 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 164.993 209.137 113.358 1.00 47.82 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 164.820 207.921 114.144 1.00 47.88 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 164.846 206.727 113.200 1.00 48.54 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 164.086 206.685 112.227 1.00 47.73 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 163.510 207.944 114.953 1.00 47.17 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 163.127 206.538 115.395 1.00 46.17 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 163.643 208.868 116.154 1.00 46.27 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 165.716 205.763 113.490 1.00 52.62 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 165.825 204.542 112.699 1.00 52.77 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 166.062 203.376 113.644 1.00 52.91 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 167.043 203.376 114.394 1.00 52.60 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 166.955 204.643 111.672 1.00 51.40 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 167.080 203.397 110.818 1.00 50.80 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 166.048 202.938 110.283 1.00 50.59 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 168.206 202.878 110.682 1.00 50.85 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 165.164 202.388 113.610 1.00 49.12 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 165.285 201.247 114.513 1.00 46.97 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 166.543 200.439 114.224 1.00 48.09 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 167.226 199.988 115.151 1.00 48.77 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 164.043 200.362 114.409 1.00 44.20 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 162.835 200.898 115.158 1.00 45.21 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 162.933 200.684 116.656 1.00 49.23 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 163.829 199.931 117.094 1.00 49.46 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 162.117 201.271 117.395 1.00 48.18 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 166.864 200.239 112.944 1.00 44.77 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 168.046 199.466 112.600 1.00 44.65 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 169.331 200.120 113.067 1.00 45.61 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 170.242 199.443 113.556 1.00 43.70 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 169.428 201.443 112.919 1.00 49.87 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 170.623 202.155 113.361 1.00 50.37 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 170.801 202.051 114.870 1.00 50.53 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 171.921 201.864 115.359 1.00 50.10 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 170.549 203.617 112.926 1.00 50.26 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 171.856 204.377 113.075 1.00 51.12 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 171.718 205.843 112.717 1.00 53.04 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 170.575 206.302 112.511 1.00 51.69 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 172.754 206.538 112.638 1.00 51.99 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 169.707 202.177 115.626 1.00 45.13 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 169.788 202.042 117.077 1.00 44.44 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 170.181 200.621 117.461 1.00 43.38 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 171.023 200.411 118.344 1.00 41.60 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 168.455 202.455 117.729 1.00 40.93 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 168.129 203.913 117.400 1.00 43.91 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 168.508 202.249 119.233 1.00 42.14 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 166.749 204.342 117.839 1.00 44.43 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 169.582 199.625 116.805 1.00 43.11 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 169.882 198.235 117.131 1.00 43.34 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 171.339 197.896 116.842 1.00 43.30 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 171.988 197.194 117.625 1.00 42.36 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 168.951 197.302 116.358 1.00 41.04 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 171.869 198.380 115.716 1.00 48.55 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 173.264 198.104 115.383 1.00 48.83 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 174.215 198.811 116.340 1.00 47.09 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 175.198 198.217 116.800 1.00 46.92 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 173.550 198.518 113.940 1.00 49.44 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 173.267 197.432 112.914 1.00 49.38 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 173.475 197.908 111.490 1.00 49.84 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 172.776 197.405 110.585 1.00 48.81 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 174.336 198.786 111.275 1.00 48.54 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 173.945 200.077 116.651 1.00 45.12 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 174.815 200.869 117.520 1.00 44.27 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 174.256 200.883 118.941 1.00 45.35 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 173.819 201.908 119.468 1.00 47.39 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 174.971 202.281 116.963 1.00 44.25 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 175.415 202.288 115.515 1.00 45.81 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 176.366 201.604 115.142 1.00 44.65 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 174.726 203.067 114.689 1.00 46.01 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 174.278 199.709 119.564 1.00 38.97 ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 173.776 199.573 120.925 1.00 36.01 ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 174.711 198.702 121.755 1.00 37.75 ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 175.008 197.563 121.369 1.00 40.72 ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 172.363 198.987 120.921 1.00 36.72 ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 171.597 199.063 122.240 1.00 37.10 ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 170.969 200.434 122.416 1.00 35.55 ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 170.538 197.978 122.293 1.00 36.16 ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 175.190 199.194 122.899 1.00 32.59 ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 176.115 198.417 123.755 1.00 30.25 ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 175.414 197.324 124.559 1.00 27.64 ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 175.041 197.479 125.722 1.00 29.43 ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 176.720 199.495 124.655 1.00 29.66 ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 175.652 200.529 124.761 1.00 29.17 ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 174.925 200.537 123.444 1.00 29.37 ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 175.222 196.174 123.909 1.00 21.60 ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 174.592 195.038 124.573 1.00 22.15 ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 175.456 194.526 125.719 1.00 26.08 ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 174.937 194.111 126.765 1.00 29.86 ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 174.329 193.932 123.553 1.00 22.00 ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 173.285 194.310 122.516 1.00 26.04 ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 173.049 193.218 121.497 1.00 29.82 ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 173.788 192.212 121.522 1.00 32.46 ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 172.133 193.372 120.663 1.00 27.37 ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 176.778 194.544 125.535 1.00 23.42 ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 177.696 194.229 126.623 1.00 18.55 ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 177.423 195.103 127.840 1.00 18.47 ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 177.311 194.602 128.964 1.00 20.20 ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 179.138 194.419 126.152 1.00 22.42 ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 179.612 193.441 125.089 1.00 22.76 ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 180.160 192.158 125.676 1.00 23.13 ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 179.401 191.267 126.058 1.00 23.41 ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 181.477 192.053 125.746 1.00 22.98 ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 177.303 196.416 127.628 1.00 20.37 ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 177.086 197.335 128.739 1.00 17.98 ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 175.732 197.103 129.394 1.00 19.78 ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 175.601 197.224 130.615 1.00 21.67 ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 177.210 198.780 128.258 1.00 19.30 ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 178.642 199.228 128.022 1.00 22.86 ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 178.778 200.735 127.958 1.00 28.65 ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 178.943 201.365 129.023 1.00 29.17 ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 178.722 201.291 126.841 1.00 28.16 ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 174.711 196.775 128.600 1.00 18.89 ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 173.390 196.493 129.159 1.00 16.11 ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 173.449 195.268 130.066 1.00 11.10 ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 172.917 195.269 131.186 1.00 15.67 ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 172.363 196.308 128.026 1.00 17.65 ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 172.156 197.625 127.278 1.00 18.92 ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 171.050 195.780 128.572 1.00 15.41 ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 171.451 197.468 125.952 1.00 18.57 ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 174.099 194.203 129.591 1.00 10.40 ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 174.215 192.993 130.397 1.00 11.02 ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 175.012 193.251 131.669 1.00 14.82 ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 174.648 192.764 132.746 1.00 16.13 ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 174.855 191.875 129.573 1.00 11.24 ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 174.717 190.459 130.130 1.00 14.73 ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 173.293 189.956 129.968 1.00 15.90 ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 175.697 189.523 129.449 1.00 16.28 ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 176.100 194.021 131.569 1.00 17.14 ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 176.893 194.338 132.756 1.00 11.07 ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 176.087 195.182 133.735 1.00 12.05 ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 176.175 194.991 134.952 1.00 19.97 ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 178.208 195.032 132.360 1.00 12.79 ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 179.019 194.125 131.443 1.00 16.15 ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 179.017 195.397 133.593 1.00 12.30 ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 179.394 192.828 132.093 1.00 16.73 ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 175.301 196.132 133.228 1.00 13.28 ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 174.480 196.959 134.102 1.00 12.52 ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 173.468 196.115 134.860 1.00 9.87  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 173.278 196.297 136.068 1.00 14.75 ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 173.770 198.037 133.287 1.00 14.68 ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 172.940 198.995 134.116 1.00 14.35 ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 171.848 199.660 133.307 1.00 16.35 ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 172.088 200.150 132.205 1.00 18.96 ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 170.638 199.683 133.853 1.00 15.07 ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 172.810 195.182 134.170 1.00 10.98 ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 171.857 194.309 134.849 1.00 6.50  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 172.551 193.416 135.870 1.00 10.09 ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 172.060 193.240 136.994 1.00 13.48 ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 171.097 193.473 133.825 1.00 6.54  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 170.519 194.313 132.848 1.00 13.11 ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 173.707 192.855 135.502 1.00 10.75 ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 174.447 191.992 136.418 1.00 7.88  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 174.826 192.759 137.677 1.00 10.10 ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 174.677 192.260 138.797 1.00 15.55 ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 175.691 191.415 135.720 1.00 7.44  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 176.709 190.958 136.747 1.00 8.78  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 175.302 190.270 134.812 1.00 10.04 ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 175.320 193.985 137.510 1.00 9.85  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 175.699 194.792 138.662 1.00 7.54  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 174.486 195.128 139.515 1.00 6.11  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 174.484 194.882 140.725 1.00 10.89 ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 176.412 196.061 138.199 1.00 11.00 ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 178.047 195.772 137.490 1.00 22.47 ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 173.422 195.642 138.890 1.00 5.90  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 172.226 196.023 139.635 1.00 6.04  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 171.638 194.847 140.402 1.00 9.66  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 170.976 195.046 141.426 1.00 12.87 ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 171.179 196.599 138.683 1.00 5.23  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 171.439 198.032 138.258 1.00 12.34 ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 170.362 198.565 137.334 1.00 14.03 ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 169.405 197.818 137.044 1.00 14.08 ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 170.473 199.729 136.897 1.00 15.68 ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 171.857 193.622 139.927 1.00 11.28 ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 171.309 192.463 140.621 1.00 6.01  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 172.253 191.878 141.668 1.00 8.73  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 171.782 191.394 142.704 1.00 14.12 ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 170.933 191.377 139.609 1.00 7.67  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 170.196 191.966 138.531 1.00 9.11  ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 170.076 190.311 140.266 1.00 8.33  ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 173.567 191.919 141.446 1.00 7.03  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 174.499 191.191 142.299 1.00 3.51  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 175.294 192.070 143.255 1.00 4.04  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 175.682 191.592 144.325 1.00 10.44 ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 175.482 190.384 141.443 1.00 6.26  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 174.829 189.508 140.382 1.00 9.34  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 174.435 187.846 140.955 1.00 30.21 ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 172.752 188.064 141.524 1.00 11.38 ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 175.567 193.329 142.900 1.00 6.75  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 176.380 194.185 143.770 1.00 9.18  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 175.761 194.370 145.149 1.00 13.71 ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 176.500 194.299 146.143 1.00 16.19 ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 176.688 195.514 143.065 1.00 5.14  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 177.198 196.545 144.058 1.00 5.75  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 177.699 195.295 141.955 1.00 7.00  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 174.451 194.614 145.303 1.00 9.81  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 173.911 194.816 146.659 1.00 7.35  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 174.166 193.662 147.613 1.00 7.30  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 174.375 193.901 148.809 1.00 14.80 ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 172.413 195.012 146.406 1.00 7.37  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 172.348 195.596 145.058 1.00 7.77  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 173.436 194.923 144.277 1.00 9.44  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 174.159 192.420 147.132 1.00 4.15  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 174.377 191.276 148.007 1.00 3.77  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 175.835 191.090 148.401 1.00 6.08  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 176.111 190.348 149.349 1.00 10.98 ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 173.872 189.995 147.338 1.00 4.14  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 174.898 189.321 146.447 1.00 5.67  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 174.525 187.882 146.152 1.00 4.55  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 173.424 187.801 145.117 1.00 8.57  ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 173.251 186.414 144.609 1.00 12.64 ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 176.767 191.742 147.710 1.00 8.68  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 178.184 191.487 147.915 1.00 8.06  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 178.687 192.112 149.209 1.00 7.78  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 178.249 193.195 149.606 1.00 12.08 ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 178.997 192.026 146.741 1.00 8.40  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 178.839 191.312 145.402 1.00 6.33  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 179.894 191.811 144.441 1.00 9.38  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 178.931 189.808 145.577 1.00 2.99  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 179.617 191.417 149.859 1.00 9.51  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 180.340 191.959 151.002 1.00 13.71 ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 181.402 192.913 150.479 1.00 14.33 ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 181.654 192.972 149.271 1.00 15.09 ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 180.956 190.841 151.863 1.00 10.25 ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 179.867 189.942 152.418 1.00 9.15  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 181.946 190.038 151.053 1.00 9.78  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 182.025 193.675 151.382 1.00 15.73 ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 182.940 194.732 150.961 1.00 13.95 ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 184.127 194.175 150.185 1.00 14.04 ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 184.577 194.784 149.207 1.00 13.95 ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 183.422 195.522 152.177 1.00 14.68 ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 184.656 193.026 150.605 1.00 14.18 ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 185.841 192.478 149.954 1.00 16.71 ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 185.529 191.854 148.600 1.00 19.22 ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 186.426 191.744 147.757 1.00 22.62 ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 186.510 191.445 150.863 1.00 17.04 ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 185.573 190.371 151.384 1.00 19.07 ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 185.167 190.601 152.827 1.00 22.69 ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 185.329 191.737 153.318 1.00 22.09 ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 184.685 189.645 153.469 1.00 20.35 ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 184.280 191.445 148.366 1.00 14.89 ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 183.939 190.754 147.129 1.00 8.94  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 183.634 191.698 145.975 1.00 11.22 ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 183.627 191.255 144.821 1.00 15.29 ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 182.743 189.830 147.355 1.00 9.64  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 183.116 188.571 148.106 1.00 16.97 ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 184.324 188.271 148.200 1.00 18.06 ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 182.202 187.883 148.604 1.00 16.21 ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 183.372 192.977 146.252 1.00 12.25 ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 183.082 193.922 145.171 1.00 14.54 ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 184.268 194.097 144.228 1.00 19.64 ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 184.075 193.994 143.005 1.00 22.15 ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 182.580 195.256 145.757 1.00 12.98 ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 181.399 195.012 146.694 1.00 13.95 ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 182.192 196.213 144.646 1.00 11.55 ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 180.959 196.241 147.449 1.00 13.98 ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 185.496 194.362 144.701 1.00 16.98 ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 186.623 194.420 143.756 1.00 11.82 ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 186.846 193.115 143.018 1.00 16.80 ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 187.212 193.130 141.837 1.00 21.96 ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 187.817 194.781 144.652 1.00 15.25 ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 187.219 195.392 145.861 1.00 16.38 ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 185.937 194.661 146.076 1.00 15.73 ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 186.623 191.978 143.681 1.00 13.34 ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 186.774 190.690 143.012 1.00 13.56 ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 185.773 190.537 141.875 1.00 19.31 ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 186.132 190.098 140.777 1.00 26.14 ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 186.613 189.552 144.018 1.00 14.91 ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 187.607 189.506 145.177 1.00 21.00 ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 187.442 188.214 145.959 1.00 20.90 ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 189.029 189.649 144.670 1.00 23.94 ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 184.512 190.903 142.117 1.00 15.41 ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 183.505 190.767 141.071 1.00 14.42 ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 183.751 191.748 139.935 1.00 13.38 ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 183.512 191.423 138.768 1.00 18.06 ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 182.102 190.941 141.653 1.00 17.30 ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 180.929 190.724 140.691 1.00 17.59 ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 179.802 189.976 141.374 1.00 14.89 ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 180.416 192.054 140.159 1.00 16.86 ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 184.241 192.950 140.244 1.00 14.18 ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 184.543 193.883 139.160 1.00 15.38 ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 185.761 193.438 138.355 1.00 17.20 ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 185.803 193.642 137.137 1.00 21.94 ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 184.727 195.293 139.713 1.00 13.89 ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 183.438 196.049 139.855 1.00 17.76 ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 182.811 196.582 138.741 1.00 18.84 ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 182.842 196.211 141.092 1.00 18.35 ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 181.620 197.272 138.862 1.00 16.30 ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 181.652 196.901 141.218 1.00 18.04 ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 181.041 197.431 140.102 1.00 15.96 ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 186.745 192.812 139.004 1.00 16.02 ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 187.857 192.228 138.260 1.00 18.54 ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 187.386 191.074 137.384 1.00 18.99 ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 187.858 190.912 136.255 1.00 20.20 ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 188.947 191.768 139.225 1.00 21.00 ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 189.608 192.883 139.795 1.00 27.17 ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 186.456 190.260 137.889 1.00 17.18 ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 185.871 189.206 137.065 1.00 14.99 ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 185.127 189.792 135.872 1.00 17.92 ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 185.196 189.255 134.761 1.00 25.44 ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 184.937 188.340 137.907 1.00 14.70 ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 185.603 187.416 138.925 1.00 17.99 ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 184.561 186.671 139.740 1.00 18.71 ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 186.529 186.442 138.223 1.00 23.24 ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 184.401 190.890 136.089 1.00 15.82 ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 183.712 191.563 134.992 1.00 14.72 ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 184.700 192.059 133.946 1.00 15.20 ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 184.462 191.920 132.742 1.00 19.97 ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 182.883 192.729 135.531 1.00 15.11 ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 181.574 192.397 136.244 1.00 15.08 ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 180.965 193.654 136.833 1.00 17.63 ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 180.609 191.740 135.284 1.00 15.13 ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 185.813 192.645 134.388 1.00 16.52 ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 186.824 193.107 133.445 1.00 18.28 ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 187.487 191.944 132.716 1.00 19.45 ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 187.895 192.091 131.559 1.00 21.04 ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 187.874 193.949 134.169 1.00 20.27 ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 188.852 193.128 134.784 1.00 22.24 ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 187.612 190.791 133.376 1.00 19.72 ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 188.232 189.633 132.738 1.00 20.64 ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 187.317 189.024 131.682 1.00 21.34 ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 187.762 188.694 130.577 1.00 27.44 ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 188.602 188.592 133.793 1.00 23.07 ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 189.905 188.914 134.498 1.00 29.75 ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 190.268 190.107 134.562 1.00 29.32 ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 190.566 187.976 134.990 1.00 29.21 ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 186.035 188.866 132.001 1.00 17.36 ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 185.110 188.225 131.072 1.00 15.91 ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 184.508 189.220 130.082 1.00 18.07 ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 184.219 188.853 128.938 1.00 19.14 ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 184.007 187.482 131.845 1.00 12.51 ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 183.220 186.582 130.910 1.00 14.87 ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 184.608 186.670 132.976 1.00 18.55 ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 184.324 190.474 130.487 1.00 18.48 ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 183.748 191.515 129.635 1.00 15.29 ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 184.717 192.688 129.610 1.00 19.67 ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 184.487 193.713 130.268 1.00 23.37 ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 182.375 191.961 130.140 1.00 14.15 ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 181.365 190.854 130.249 1.00 16.81 ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 181.375 189.989 131.332 1.00 19.63 ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 180.384 190.697 129.287 1.00 20.39 ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 180.439 188.980 131.439 1.00 20.03 ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 179.446 189.689 129.390 1.00 18.55 ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 179.475 188.829 130.467 1.00 17.05 ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 185.816 192.574 128.868 1.00 21.98 ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 186.811 193.651 128.869 1.00 19.94 ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 186.336 194.856 128.074 1.00 20.10 ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 185.745 194.724 126.998 1.00 21.65 ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 188.035 193.001 128.216 1.00 18.19 ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 187.463 191.950 127.333 1.00 18.40 ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 186.223 191.443 128.017 1.00 20.66 ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 186.601 196.042 128.618 1.00 21.96 ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 186.345 197.289 127.929 1.00 23.90 ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 185.034 197.965 128.266 1.00 25.40 ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 184.840 199.124 127.875 1.00 24.69 ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 184.130 197.293 128.971 1.00 28.46 ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 182.827 197.853 129.311 1.00 30.15 ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 182.815 198.228 130.785 1.00 29.97 ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 183.280 197.466 131.641 1.00 26.16 ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 181.689 196.872 128.968 1.00 28.28 ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 181.571 196.717 127.464 1.00 26.23 ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 181.924 195.524 129.617 1.00 24.91 ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 182.295 199.416 131.080 1.00 35.22 ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 182.265 199.953 132.430 1.00 36.79 ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 180.826 200.148 132.886 1.00 36.73 ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 179.944 200.472 132.086 1.00 36.97 ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 183.021 201.286 132.515 1.00 37.08 ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 184.450 201.160 133.006 1.00 38.02 ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 185.415 200.799 131.895 1.00 38.81 ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 185.422 201.424 130.835 1.00 37.09 ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 186.236 199.783 132.131 1.00 37.87 ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 180.599 199.950 134.182 1.00 33.87 ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 179.285 200.120 134.788 1.00 35.30 ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 179.253 201.458 135.518 1.00 37.95 ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 179.846 201.601 136.592 1.00 36.41 ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 178.974 198.971 135.745 1.00 31.81 ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 177.760 199.215 136.612 1.00 32.52 ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 176.505 199.394 136.047 1.00 32.56 ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 177.870 199.275 137.994 1.00 32.97 ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 175.392 199.621 136.835 1.00 34.44 ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 176.764 199.502 138.789 1.00 34.07 ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 175.528 199.673 138.205 1.00 36.68 ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 174.423 199.898 138.993 1.00 35.11 ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 178.560 202.432 134.936 1.00 47.35 ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 178.356 203.739 135.554 1.00 46.61 ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 176.926 203.790 136.074 1.00 44.71 ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 175.977 203.879 135.287 1.00 44.17 ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 178.622 204.868 134.560 1.00 47.69 ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 179.974 204.805 133.922 1.00 49.21 ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 180.149 204.593 132.572 1.00 48.51 ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 181.216 204.927 134.449 1.00 47.47 ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 181.442 204.587 132.294 1.00 49.16 ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 182.110 204.788 133.415 1.00 48.92 ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 176.773 203.731 137.392 1.00 31.32 ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 175.447 203.737 137.990 1.00 30.81 ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 174.794 205.107 137.834 1.00 32.78 ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 175.461 206.145 137.823 1.00 31.74 ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 175.525 203.341 139.465 1.00 27.97 ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 175.627 204.502 140.438 1.00 29.81 ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 175.237 204.079 141.845 1.00 31.02 ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 173.873 203.570 141.905 1.00 33.16 ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 173.401 202.808 142.881 1.00 31.60 ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 174.161 202.438 143.900 1.00 28.13 ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 172.134 202.405 142.836 1.00 28.35 ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 173.473 205.097 137.684 1.00 32.01 ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 172.744 206.337 137.517 1.00 29.71 ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 172.769 207.185 138.774 1.00 33.99 ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 172.870 206.685 139.894 1.00 34.69 ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 172.678 208.496 138.577 1.00 37.98 ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 172.647 209.458 139.677 1.00 37.49 ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 171.191 209.869 139.871 1.00 38.39 ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 170.695 210.795 139.228 1.00 40.76 ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 173.547 210.653 139.387 1.00 35.12 ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 174.136 211.304 140.630 1.00 38.24 ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 173.305 212.466 141.136 1.00 41.30 ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 172.636 213.124 140.313 1.00 40.41 ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 173.323 212.722 142.359 1.00 40.91 ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 170.502 209.164 140.767 1.00 28.35 ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 169.081 209.398 141.024 1.00 28.43 ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 168.940 210.662 141.866 1.00 26.10 ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 168.759 210.627 143.085 1.00 30.23 ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 168.461 208.183 141.703 1.00 28.08 ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 168.422 206.949 140.812 1.00 30.79 ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 167.638 205.518 141.574 1.00 44.73 ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 168.909 205.016 142.730 1.00 26.66 ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 169.012 211.806 141.181 1.00 23.48 ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 169.077 213.093 141.869 1.00 23.67 ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 167.812 213.364 142.677 1.00 23.77 ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 167.883 213.791 143.834 1.00 24.73 ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 169.317 214.212 140.857 1.00 26.22 ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 170.537 213.964 140.150 1.00 25.10 ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 169.412 215.557 141.562 1.00 27.60 ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 166.640 213.127 142.081 1.00 18.89 ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 165.390 213.406 142.782 1.00 18.22 ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 165.232 212.515 144.007 1.00 19.27 ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 164.846 212.986 145.087 1.00 21.98 ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 164.205 213.229 141.833 1.00 16.03 ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 165.534 211.225 143.861 1.00 15.88 ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 165.442 210.321 144.999 1.00 14.36 ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 166.455 210.685 146.075 1.00 15.44 ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 166.157 210.585 147.266 1.00 20.30 ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 165.632 208.875 144.550 1.00 14.47 ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 165.391 207.852 145.663 1.00 14.59 ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 163.926 207.832 146.069 1.00 14.36 ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 165.850 206.479 145.236 1.00 13.62 ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 167.659 211.108 145.678 1.00 14.40 ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 168.649 211.512 146.673 1.00 11.29 ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 168.209 212.767 147.416 1.00 14.71 ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 168.448 212.891 148.622 1.00 20.94 ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 170.015 211.720 146.021 1.00 12.90 ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 170.661 210.446 145.504 1.00 16.46 ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 172.029 210.730 144.911 1.00 15.03 ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 173.044 210.859 145.947 1.00 20.09 ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 173.877 209.892 146.303 1.00 23.17 ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 173.885 208.724 145.683 1.00 18.53 ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 174.731 210.103 147.300 1.00 20.81 ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 167.571 213.712 146.721 1.00 12.98 ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 167.042 214.891 147.403 1.00 12.15 ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 165.943 214.512 148.387 1.00 14.10 ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 165.895 215.030 149.514 1.00 17.45 ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 166.522 215.902 146.383 1.00 13.73 ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 167.596 216.481 145.479 1.00 19.44 ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 167.151 217.754 144.789 1.00 24.09 ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 166.379 217.663 143.811 1.00 25.11 ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 167.575 218.846 145.221 1.00 19.18 ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 165.048 213.609 147.981 1.00 13.25 ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 164.008 213.144 148.895 1.00 9.97  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 164.615 212.445 150.106 1.00 13.65 ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 164.168 212.648 151.241 1.00 18.98 ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 163.045 212.212 148.161 1.00 11.92 ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 162.185 212.901 147.119 1.00 14.62 ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 161.478 214.126 147.663 1.00 20.50 ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 160.852 214.024 148.738 1.00 20.82 ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 161.547 215.191 147.014 1.00 20.00 ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 165.636 211.614 149.879 1.00 10.51 ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 166.311 210.938 150.981 1.00 8.66  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 166.973 211.938 151.914 1.00 11.25 ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 166.948 211.765 153.135 1.00 18.68 ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 167.348 209.954 150.443 1.00 10.89 ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 166.867 208.720 149.680 1.00 12.29 ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 168.051 207.964 149.111 1.00 12.27 ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 166.038 207.818 150.566 1.00 13.68 ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 167.586 212.984 151.357 1.00 13.17 ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 168.213 214.005 152.189 1.00 13.00 ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 167.184 214.713 153.056 1.00 10.76 ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 167.415 214.934 154.250 1.00 14.32 ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 168.962 215.010 151.315 1.00 9.67  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 169.877 215.936 152.095 1.00 16.02 ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 170.821 216.692 151.177 1.00 17.73 ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 171.820 217.516 151.976 1.00 17.18 ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 172.853 218.141 151.106 1.00 17.41 ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 166.032 215.065 152.477 1.00 8.83  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 164.985 215.709 153.267 1.00 8.35  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 164.478 214.788 154.373 1.00 11.82 ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 164.314 215.214 155.525 1.00 16.47 ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 163.835 216.141 152.360 1.00 10.50 ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 164.122 217.383 151.537 1.00 12.87 ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 162.850 217.932 150.910 1.00 15.28 ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 162.703 217.475 149.470 1.00 18.08 ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 163.574 218.253 148.549 1.00 18.11 ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 164.235 213.518 154.041 1.00 11.08 ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 163.719 212.572 155.029 1.00 7.27  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 164.733 212.354 156.143 1.00 7.08  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 164.377 212.298 157.326 1.00 11.60 ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 163.326 211.250 154.344 1.00 9.57  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 163.061 210.171 155.377 1.00 10.18 ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 162.105 211.455 153.466 1.00 10.09 ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 166.012 212.224 155.788 1.00 8.53  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 167.053 212.055 156.795 1.00 5.00  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 167.169 213.291 157.675 1.00 6.38  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 167.415 213.182 158.881 1.00 12.18 ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 168.388 211.752 156.117 1.00 5.64  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 168.520 210.087 155.441 1.00 6.53  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 167.010 214.478 157.087 1.00 9.87  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 167.052 215.701 157.879 1.00 9.29  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 165.911 215.742 158.886 1.00 11.02 ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 166.117 216.107 160.050 1.00 12.22 ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 167.008 216.921 156.962 1.00 8.33  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 166.606 218.207 157.660 1.00 10.88 ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 167.686 218.727 158.588 1.00 16.97 ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 168.875 218.493 158.368 1.00 14.78 ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 167.278 219.436 159.633 1.00 14.86 ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 164.702 215.362 158.468 1.00 11.80 ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 163.586 215.397 159.407 1.00 9.63  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 163.592 214.220 160.377 1.00 9.16  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 162.884 214.268 161.388 1.00 10.78 ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 162.248 215.430 158.666 1.00 7.97  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 161.939 214.184 157.868 1.00 13.49 ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 160.638 214.294 157.105 1.00 17.49 ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 159.990 215.358 157.183 1.00 16.81 ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 160.258 213.314 156.431 1.00 18.73 ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 164.366 213.171 160.097 1.00 9.88  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 164.449 212.004 160.963 1.00 7.15  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 165.742 211.955 161.766 1.00 9.58  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 166.056 210.913 162.351 1.00 12.56 ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 164.301 210.720 160.144 1.00 7.41  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 162.870 210.244 159.981 1.00 10.58 ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 162.723 208.907 158.782 1.00 22.38 ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 162.949 207.476 159.836 1.00 9.80  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 166.503 213.050 161.798 1.00 9.78  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 167.754 213.158 162.546 1.00 7.47  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 168.808 212.169 162.063 1.00 9.85  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 169.691 211.776 162.831 1.00 11.64 ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 167.521 212.982 164.051 1.00 6.15  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 166.409 213.842 164.595 1.00 8.86  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 166.469 215.224 164.508 1.00 11.72 ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 165.296 213.271 165.195 1.00 6.80  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 165.452 216.012 165.000 1.00 9.34  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 164.276 214.053 165.692 1.00 8.36  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 164.359 215.423 165.593 1.00 11.20 ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 163.343 216.207 166.087 1.00 13.31 ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 168.736 211.761 160.800 1.00 12.28 ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 169.668 210.790 160.247 1.00 8.58  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 170.728 211.488 159.409 1.00 10.87 ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 170.458 212.500 158.757 1.00 13.28 ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 168.929 209.754 159.402 1.00 9.01  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 167.911 208.869 160.124 1.00 7.21  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 167.653 207.610 159.324 1.00 12.01 ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 168.386 208.521 161.523 1.00 11.79 ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 171.940 210.943 159.436 1.00 12.90 ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 173.044 211.522 158.684 1.00 9.36  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 172.978 211.089 157.226 1.00 11.48 ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 172.868 209.898 156.922 1.00 13.70 ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 174.379 211.104 159.299 1.00 10.54 ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 174.444 211.563 160.655 1.00 17.04 ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 175.537 211.698 158.518 1.00 9.64  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 173.047 212.063 156.324 1.00 13.10 ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 173.034 211.824 154.889 1.00 10.75 ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 174.374 212.246 154.303 1.00 15.79 ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 174.920 213.291 154.669 1.00 17.34 ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 171.889 212.591 154.216 1.00 11.64 ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 171.904 212.550 152.704 1.00 17.59 ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 171.225 211.558 152.012 1.00 16.98 ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 172.581 213.514 151.969 1.00 16.89 ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 171.233 211.519 150.633 1.00 14.92 ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 172.595 213.482 150.592 1.00 14.58 ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 171.919 212.482 149.930 1.00 15.96 ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 171.931 212.450 148.556 1.00 20.81 ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 174.896 211.435 153.396 1.00 12.93 ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 176.172 211.728 152.769 1.00 16.46 ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 176.201 211.228 151.345 1.00 18.93 ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 175.525 210.254 150.996 1.00 19.97 ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 176.996 211.899 150.516 1.00 22.05 ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 177.140 211.561 149.107 1.00 22.60 ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 178.539 211.010 148.867 1.00 23.60 ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 179.533 211.681 149.167 1.00 23.21 ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 176.886 212.781 148.222 1.00 18.99 ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 175.412 213.082 148.051 1.00 23.06 ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 174.584 212.211 148.385 1.00 22.83 ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 175.079 214.192 147.582 1.00 27.65 ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 178.615 209.799 148.326 1.00 25.64 ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 179.889 209.201 147.984 1.00 26.75 ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 180.736 208.824 149.183 1.00 28.60 ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 180.402 207.896 149.921 1.00 30.08 ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 181.842 209.539 149.379 1.00 33.44 ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 182.777 209.250 150.456 1.00 34.77 ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 182.494 210.042 151.726 1.00 33.59 ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 183.243 209.908 152.698 1.00 34.49 ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 184.212 209.518 149.992 1.00 35.99 ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 184.886 208.316 149.352 1.00 36.57 ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 184.651 207.036 150.127 1.00 38.13 ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 185.233 206.889 151.223 1.00 36.94 ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 183.884 206.179 149.643 1.00 36.20 ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 181.447 210.860 151.742 1.00 25.83 ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 181.094 211.590 152.947 1.00 22.57 ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 180.538 210.635 154.001 1.00 22.49 ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 180.218 209.474 153.727 1.00 23.72 ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 180.075 212.684 152.637 1.00 20.66 ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 180.496 213.634 151.532 1.00 25.84 ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 179.394 214.599 151.148 1.00 28.14 ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 178.378 214.657 151.872 1.00 25.79 ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 179.541 215.298 150.125 1.00 28.47 ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 180.431 211.139 155.229 1.00 19.72 ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 179.904 210.355 156.340 1.00 16.19 ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 178.451 210.011 156.050 1.00 16.03 ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 177.590 210.896 155.991 1.00 16.55 ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 180.044 211.108 157.673 1.00 14.26 ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 179.622 210.221 158.830 1.00 15.23 ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 181.471 211.590 157.860 1.00 14.24 ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 178.168 208.724 155.870 1.00 11.92 ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 176.848 208.268 155.500 1.00 11.21 ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 176.671 207.942 154.036 1.00 16.31 ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 175.564 207.568 153.635 1.00 19.96 ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 177.722 208.074 153.224 1.00 15.59 ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 177.596 207.766 151.810 1.00 10.07 ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 177.339 206.296 151.549 1.00 13.61 ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 176.569 205.941 150.652 1.00 20.49 ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 177.984 205.419 152.322 1.00 9.96  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 177.755 203.986 152.172 1.00 8.12  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 176.310 203.629 152.500 1.00 9.40  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 175.689 202.807 151.818 1.00 18.72 ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 178.718 203.207 153.067 1.00 9.86  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 180.177 203.326 152.662 1.00 13.46 ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 181.281 202.461 153.795 1.00 32.03 ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 180.886 200.756 153.419 1.00 14.85 ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 175.759 204.243 153.547 1.00 8.06  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 174.373 203.978 153.921 1.00 6.44  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 173.408 204.442 152.837 1.00 10.94 ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 172.435 203.752 152.516 1.00 17.38 ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 174.056 204.655 155.252 1.00 10.06 ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 172.699 204.329 155.767 1.00 11.92 ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 172.291 203.152 156.314 1.00 8.27  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 171.558 205.188 155.762 1.00 11.20 ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 170.965 203.229 156.663 1.00 7.47  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 170.492 204.471 156.332 1.00 8.32  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 171.335 206.499 155.334 1.00 9.12  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 169.226 205.019 156.488 1.00 12.00 ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 170.079 207.039 155.488 1.00 8.15  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 169.038 206.301 156.059 1.00 12.23 ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 173.659 205.620 152.261 1.00 11.57 ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 172.783 206.132 151.208 1.00 8.08  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 172.889 205.259 149.965 1.00 9.35  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 171.899 205.007 149.268 1.00 18.45 ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 173.113 207.603 150.902 1.00 10.29 ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 172.281 208.106 149.736 1.00 12.22 ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 172.869 208.454 152.132 1.00 10.89 ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 174.098 204.775 149.672 1.00 6.99  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 174.265 203.844 148.562 1.00 8.50  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 173.495 202.555 148.811 1.00 13.04 ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 172.889 201.997 147.889 1.00 20.33 ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 175.749 203.552 148.338 1.00 11.09 ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 176.445 204.554 147.433 1.00 18.27 ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 175.947 204.492 146.003 1.00 25.75 ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 175.536 203.398 145.562 1.00 27.81 ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 175.966 205.536 145.318 1.00 20.44 ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 173.507 202.066 150.052 1.00 14.84 ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 172.729 200.877 150.390 1.00 7.32  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 171.235 201.132 150.227 1.00 8.84  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 170.494 200.255 149.772 1.00 13.98 ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 173.046 200.434 151.817 1.00 4.05  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 174.286 199.572 151.932 1.00 5.41  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 174.130 198.273 151.169 1.00 4.51  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 175.450 197.837 150.562 1.00 4.41  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 175.397 196.434 150.076 1.00 4.03  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 170.775 202.326 150.603 1.00 11.50 ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 169.366 202.677 150.424 1.00 12.14 ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 169.000 202.691 148.944 1.00 12.78 ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 167.938 202.199 148.544 1.00 17.00 ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 169.063 204.030 151.094 1.00 8.87  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 167.653 204.482 150.764 1.00 11.31 ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 169.246 203.930 152.594 1.00 7.95  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 169.871 203.262 148.109 1.00 12.00 ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 169.614 203.282 146.672 1.00 10.69 ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 169.610 201.873 146.091 1.00 9.49  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 168.807 201.557 145.205 1.00 12.34 ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 170.652 204.147 145.963 1.00 13.28 ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 170.695 205.623 146.351 1.00 10.21 ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 171.770 206.328 145.559 1.00 14.74 ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 169.350 206.284 146.140 1.00 9.61  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 170.514 201.013 146.566 1.00 7.57  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 170.518 199.623 146.126 1.00 2.95  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 169.233 198.914 146.532 1.00 7.20  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 168.688 198.112 145.767 1.00 14.70 ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 171.736 198.901 146.695 1.00 2.97  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 173.054 199.374 146.114 1.00 9.40  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 174.244 198.737 146.789 1.00 7.84  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 174.094 197.884 147.658 1.00 11.35 ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 175.441 199.149 146.391 1.00 11.55 ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 168.740 199.196 147.740 1.00 9.56  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 167.463 198.635 148.171 1.00 6.61  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 166.329 199.106 147.271 1.00 7.49  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 165.444 198.320 146.909 1.00 12.99 ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 167.196 199.019 149.626 1.00 4.25  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 165.954 198.429 150.290 1.00 6.81  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 166.171 196.964 150.596 1.00 11.94 ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 165.621 199.195 151.553 1.00 8.35  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 166.339 200.387 146.900 1.00 5.38  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 165.334 200.899 145.973 1.00 1.76  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 165.407 200.186 144.633 1.00 5.91  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 164.376 199.849 144.041 1.00 13.79 ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 165.508 202.402 145.775 1.00 7.81  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 164.620 202.965 144.691 1.00 10.64 ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 163.239 202.878 144.783 1.00 6.44  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 165.163 203.568 143.566 1.00 9.60  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 162.425 203.386 143.794 1.00 6.04  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 164.356 204.082 142.572 1.00 9.21  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 162.987 203.988 142.691 1.00 9.84  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 162.178 204.497 141.702 1.00 12.04 ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 166.622 199.962 144.128 1.00 9.36  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 166.777 199.243 142.867 1.00 4.41  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 166.245 197.821 142.974 1.00 2.56  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 165.596 197.322 142.050 1.00 10.94 ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 168.245 199.233 142.444 1.00 7.26  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 168.732 200.541 141.853 1.00 10.80 ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 170.080 200.406 141.179 1.00 15.08 ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 171.070 200.043 141.815 1.00 17.08 ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 170.127 200.695 139.885 1.00 10.55 ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 166.516 197.151 144.097 1.00 2.18  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 166.049 195.780 144.276 1.00 2.99  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 164.528 195.728 144.377 1.00 5.05  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 163.905 194.767 143.910 1.00 10.87 ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 166.728 195.138 145.500 1.00 3.17  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 168.239 195.055 145.289 1.00 5.79  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 166.191 193.744 145.745 1.00 5.82  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 168.651 194.065 144.228 1.00 5.89  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 163.904 196.745 144.980 1.00 6.22  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 162.446 196.754 145.092 1.00 2.01  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 161.781 196.710 143.723 1.00 5.22  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 160.725 196.088 143.558 1.00 9.50  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 161.969 197.987 145.859 1.00 1.11  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 162.598 199.158 145.328 1.00 13.32 ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 162.287 197.868 147.333 1.00 0.97  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 162.376 197.371 142.730 1.00 5.15  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 161.777 197.421 141.402 1.00 4.94  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 161.922 196.110 140.642 1.00 5.69  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 161.113 195.837 139.749 1.00 6.45  ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 162.395 198.558 140.592 1.00 2.86  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 162.323 199.909 141.271 1.00 1.42  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 162.875 201.019 140.404 1.00 9.60  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 164.085 201.238 140.354 1.00 12.83 ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 161.989 201.727 139.713 1.00 12.24 ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 162.923 195.299 140.968 1.00 3.65  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 163.166 194.045 140.270 1.00 4.48  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 162.488 192.871 140.962 1.00 6.04  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 161.885 192.025 140.304 1.00 11.23 ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 164.683 193.799 140.125 1.00 4.63  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 165.406 195.089 139.743 1.00 3.03  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 164.951 192.712 139.099 1.00 7.56  ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 166.910 194.961 139.742 1.00 2.66  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 162.577 192.805 142.287 1.00 2.50  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 162.083 191.671 143.055 1.00 2.76  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 160.905 192.091 143.917 1.00 3.97  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 160.892 193.191 144.476 1.00 10.07 ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 163.185 191.090 143.947 1.00 2.24  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 164.334 190.510 143.154 1.00 5.48  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 165.403 191.110 143.060 1.00 9.42  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 164.122 189.333 142.579 1.00 8.30  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 159.913 191.210 144.020 1.00 5.64  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 158.842 191.370 144.992 1.00 6.27  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 159.181 190.735 146.333 1.00 6.41  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 158.385 190.834 147.271 1.00 10.51 ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 157.533 190.785 144.450 1.00 1.95  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 157.614 189.332 144.101 1.00 2.27  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 158.143 188.881 142.912 1.00 4.77  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 157.224 188.229 144.782 1.00 3.83  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 158.079 187.562 142.876 1.00 6.51  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 157.525 187.142 143.999 1.00 5.56  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 160.339 190.088 146.442 1.00 3.79  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 160.822 189.553 147.698 1.00 2.41  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 162.236 190.009 147.981 1.00 6.54  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 163.142 189.783 147.173 1.00 16.91 ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 162.446 190.656 149.125 1.00 6.12  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 163.727 191.261 149.452 1.00 5.25  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 164.227 190.745 150.790 1.00 10.64 ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 163.446 190.307 151.638 1.00 20.68 ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 163.635 192.787 149.519 1.00 7.12  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 163.558 193.568 148.211 1.00 8.79  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 162.156 193.538 147.626 1.00 8.81  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 164.022 194.987 148.448 1.00 10.26 ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 165.543 190.813 150.974 1.00 5.24  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 166.166 190.496 152.253 1.00 4.41  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 167.265 191.507 152.528 1.00 7.68  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 168.238 191.583 151.774 1.00 13.61 ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 166.740 189.077 152.264 1.00 5.59  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 165.705 187.979 152.330 1.00 9.35  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 166.257 186.612 153.363 1.00 17.84 ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 165.138 185.323 152.836 1.00 12.52 ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 167.114 192.267 153.608 1.00 11.08 ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 168.188 193.113 154.121 1.00 9.29  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 168.947 192.289 155.152 1.00 11.00 ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 168.493 192.121 156.285 1.00 16.07 ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 167.642 194.398 154.728 1.00 10.85 ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 166.833 195.250 153.774 1.00 8.58  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 165.481 196.087 154.616 1.00 11.78 ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 164.101 195.061 154.128 1.00 15.12 ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 170.103 191.768 154.758 1.00 14.04 ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 170.893 190.883 155.606 1.00 8.20  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 172.079 191.672 156.137 1.00 10.64 ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 172.818 192.291 155.366 1.00 21.02 ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 171.361 189.639 154.837 1.00 6.38  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 172.006 188.645 155.784 1.00 13.25 ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 170.197 189.004 154.101 1.00 11.53 ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 172.262 191.660 157.453 1.00 7.12  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 173.389 192.327 158.053 1.00 5.92  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 173.358 192.281 159.563 1.00 10.21 ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 172.306 192.094 160.179 1.00 21.40 ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 174.516 192.475 160.192 1.00 7.54  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 174.583 192.408 161.655 1.00 7.47  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 173.693 193.456 162.303 1.00 10.74 ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 173.301 194.450 161.686 1.00 12.90 ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 176.062 192.675 161.956 1.00 8.10  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 176.773 192.316 160.697 1.00 10.34 ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 175.841 192.690 159.589 1.00 10.81 ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 173.354 193.206 163.565 1.00 8.77  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 172.510 194.126 164.314 1.00 9.11  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 173.143 195.510 164.359 1.00 8.87  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 174.347 195.655 164.578 1.00 13.28 ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 172.284 193.601 165.733 1.00 6.74  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 171.497 194.503 166.488 1.00 11.86 ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 172.317 196.529 164.145 1.00 5.42  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 172.810 197.889 164.106 1.00 2.94  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 173.604 198.247 162.875 1.00 9.83  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 174.608 198.959 162.980 1.00 15.00 ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 173.190 197.769 161.705 1.00 11.88 ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 173.829 198.120 160.446 1.00 6.91  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 172.994 199.087 159.616 1.00 8.85  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 173.372 199.401 158.484 1.00 17.10 ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 174.130 196.856 159.639 1.00 6.76  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 172.983 196.035 159.533 1.00 12.95 ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 171.875 199.567 160.152 1.00 12.15 ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 171.073 200.562 159.472 1.00 9.71  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 170.005 200.031 158.544 1.00 10.83 ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 169.520 200.788 157.700 1.00 18.88 ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 169.622 198.759 158.669 1.00 11.70 ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 168.629 198.185 157.763 1.00 6.13  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 167.257 198.819 157.962 1.00 10.18 ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 166.610 199.251 156.996 1.00 20.03 ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 168.554 196.673 157.974 1.00 7.59  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 169.827 195.936 157.630 1.00 12.06 ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 169.851 194.549 158.236 1.00 9.41  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 169.790 194.606 159.749 1.00 8.17  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 169.245 193.351 160.325 1.00 14.78 ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 166.794 198.872 159.213 1.00 16.28 ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 165.464 199.402 159.497 1.00 8.45  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 165.357 200.856 159.068 1.00 11.00 ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 164.387 201.253 158.413 1.00 21.49 ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 165.150 199.263 160.985 1.00 14.89 ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 165.145 197.907 161.387 1.00 19.39 ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 166.353 201.665 159.429 1.00 15.17 ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 166.348 203.064 159.023 1.00 13.86 ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 166.415 203.186 157.510 1.00 13.21 ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 165.764 204.057 156.923 1.00 19.00 ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 167.510 203.806 159.679 1.00 11.08 ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 167.208 204.356 161.066 1.00 16.26 ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 165.601 205.159 161.215 1.00 26.96 ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 164.673 203.905 162.097 1.00 20.82 ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 167.181 202.308 156.858 1.00 14.10 ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 167.278 202.340 155.404 1.00 8.38  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 165.916 202.159 154.756 1.00 12.66 ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 165.495 202.979 153.930 1.00 19.59 ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 168.246 201.264 154.912 1.00 10.42 ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 165.192 201.104 155.134 1.00 18.10 ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 163.923 200.874 154.449 1.00 12.52 ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 162.842 201.854 154.895 1.00 16.05 ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 161.981 202.212 154.087 1.00 22.06 ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 163.467 199.417 154.606 1.00 14.86 ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 162.957 198.991 155.949 1.00 15.98 ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 163.617 198.232 156.865 1.00 17.12 ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 161.655 199.237 156.498 1.00 18.45 ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 162.825 198.017 157.964 1.00 17.10 ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 161.615 198.625 157.763 1.00 16.14 ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 160.528 199.931 156.050 1.00 21.39 ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 160.495 198.684 158.584 1.00 20.54 ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 159.421 199.991 156.866 1.00 18.77 ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 159.410 199.371 158.117 1.00 20.55 ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 162.883 202.339 156.140 1.00 15.36 ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 161.925 203.358 156.560 1.00 8.86  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 162.126 204.656 155.785 1.00 15.04 ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 161.160 205.265 155.298 1.00 20.72 ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 162.052 203.613 158.061 1.00 11.12 ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 161.553 202.483 158.935 1.00 13.76 ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 161.531 202.903 160.390 1.00 16.06 ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 161.310 201.773 161.284 1.00 20.66 ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 160.126 201.237 161.539 1.00 21.55 ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 159.021 201.699 160.977 1.00 16.17 ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 160.048 200.212 162.382 1.00 20.33 ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 163.379 205.097 155.663 1.00 16.94 ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 163.679 206.317 154.925 1.00 13.91 ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 163.345 206.140 153.451 1.00 14.66 ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 162.834 207.061 152.808 1.00 17.73 ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 165.152 206.711 155.141 1.00 12.03 ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 165.602 207.715 154.103 1.00 12.98 ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 165.341 207.275 156.536 1.00 15.51 ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 163.613 204.955 152.894 1.00 15.21 ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 163.246 204.704 151.506 1.00 10.76 ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 161.738 204.776 151.309 1.00 10.40 ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 161.264 205.353 150.326 1.00 18.76 ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 163.776 203.343 151.059 1.00 12.47 ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 163.416 202.967 149.624 1.00 12.32 ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 164.023 203.967 148.658 1.00 13.08 ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 163.873 201.557 149.305 1.00 11.90 ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 160.969 204.200 152.235 1.00 9.81  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 159.515 204.245 152.126 1.00 8.94  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 159.004 205.679 152.182 1.00 12.08 ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 158.166 206.084 151.368 1.00 17.39 ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 158.890 203.401 153.237 1.00 11.40 ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 157.400 203.075 153.150 1.00 11.91 ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 157.067 202.406 151.831 1.00 11.79 ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 156.997 202.191 154.311 1.00 9.86  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 159.511 206.469 153.133 1.00 14.17 ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 159.066 207.856 153.240 1.00 11.16 ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 159.468 208.673 152.016 1.00 9.01  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 158.679 209.488 151.520 1.00 13.13 ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 159.615 208.493 154.514 1.00 14.08 ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 159.032 207.916 155.790 1.00 17.46 ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 159.593 208.610 157.016 1.00 16.71 ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 159.023 208.015 158.293 1.00 16.69 ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 159.572 208.678 159.505 1.00 18.54 ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 160.689 208.472 151.515 1.00 10.94 ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 161.138 209.208 150.338 1.00 6.75  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 160.320 208.839 149.109 1.00 8.62  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 159.978 209.710 148.305 1.00 15.21 ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 162.623 208.948 150.092 1.00 8.61  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 160.002 207.554 148.942 1.00 13.01 ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 159.163 207.145 147.822 1.00 9.81  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 157.764 207.730 147.944 1.00 9.64  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 157.166 208.141 146.943 1.00 9.88  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 159.106 205.620 147.743 1.00 5.84  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 160.370 204.960 147.197 1.00 5.30  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 160.163 203.469 147.012 1.00 10.72 ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 160.780 205.617 145.894 1.00 9.61  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 157.225 207.777 149.164 1.00 12.29 ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 155.921 208.397 149.370 1.00 9.23  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 155.945 209.872 148.992 1.00 10.02 ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 155.009 210.375 148.362 1.00 11.91 ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 155.485 208.224 150.825 1.00 9.98  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 154.220 208.973 151.193 1.00 7.99  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 153.721 208.614 152.577 1.00 19.13 ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 154.412 207.845 153.277 1.00 19.01 ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 152.639 209.100 152.966 1.00 22.08 ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 157.011 210.580 149.368 1.00 14.49 ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 157.083 212.008 149.066 1.00 11.32 ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 157.384 212.269 147.595 1.00 11.43 ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 156.999 213.317 147.065 1.00 16.10 ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 158.135 212.679 149.947 1.00 8.28  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 157.628 213.064 151.323 1.00 10.20 ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 158.770 213.225 152.307 1.00 12.36 ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 159.445 214.505 152.138 1.00 18.41 ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 159.748 215.328 153.134 1.00 17.17 ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 159.436 215.040 154.386 1.00 11.00 ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 160.373 216.470 152.865 1.00 15.72 ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 158.066 211.343 146.923 1.00 12.35 ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 158.479 211.545 145.537 1.00 8.59  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 157.396 211.116 144.550 1.00 14.97 ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 156.930 211.926 143.742 1.00 18.66 ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 159.785 210.785 145.273 1.00 9.25  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 160.274 210.698 143.828 1.00 11.69 ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 161.031 211.956 143.447 1.00 16.29 ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 161.146 209.470 143.638 1.00 9.82  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 156.988 209.848 144.604 1.00 13.61 ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 155.984 209.341 143.680 1.00 10.88 ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 154.565 209.740 144.060 1.00 12.97 ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 153.663 209.619 143.226 1.00 14.99 ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 156.070 207.815 143.593 1.00 12.23 ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 157.445 207.284 143.235 1.00 12.53 ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 157.519 205.773 143.319 1.00 17.20 ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 156.577 205.164 143.865 1.00 15.44 ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 158.516 205.195 142.839 1.00 17.50 ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 154.345 210.211 145.285 1.00 10.40 ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 153.012 210.558 145.726 1.00 11.55 ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 152.149 209.386 146.131 1.00 13.17 ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 150.951 209.575 146.368 1.00 14.66 ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 152.715 208.187 146.220 1.00 10.69 ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 151.977 206.987 146.598 1.00 11.64 ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 152.228 206.725 148.075 1.00 13.32 ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 153.381 206.586 148.501 1.00 14.35 ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 152.394 205.779 145.744 1.00 9.18  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 151.599 204.549 146.143 1.00 9.97  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 152.208 206.085 144.269 1.00 8.16  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 151.153 206.657 148.856 1.00 10.61 ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 151.281 206.439 150.291 1.00 7.81  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 151.918 205.083 150.572 1.00 10.35 ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 151.529 204.068 149.987 1.00 15.89 ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 149.913 206.531 150.963 1.00 8.95  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 149.877 205.957 152.369 1.00 13.89 ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 148.545 206.172 153.057 1.00 18.51 ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 147.671 206.836 152.465 1.00 15.89 ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 148.374 205.673 154.187 1.00 15.64 ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 152.897 205.070 151.473 1.00 7.86  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 153.596 203.861 151.835 1.00 8.41  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 153.156 203.353 153.191 1.00 10.16 ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 153.249 204.066 154.193 1.00 14.29 ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 152.673 202.115 153.217 1.00 5.17  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 152.234 201.452 154.437 1.00 7.17  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 153.117 200.234 154.654 1.00 9.12  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 153.301 199.426 153.736 1.00 14.28 ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 150.751 201.046 154.363 1.00 8.35  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 150.323 200.365 155.649 1.00 12.89 ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 149.885 202.260 154.079 1.00 8.70  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 153.661 200.105 155.860 1.00 8.50  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 154.548 199.007 156.215 1.00 4.14  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 153.931 198.199 157.344 1.00 9.17  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 153.548 198.757 158.378 1.00 17.60 ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 155.927 199.522 156.627 1.00 7.51  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 153.835 196.890 157.141 1.00 6.40  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 153.371 195.952 158.156 1.00 5.73  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 154.574 195.139 158.611 1.00 8.50  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 155.086 194.307 157.858 1.00 15.06 ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 152.272 195.045 157.607 1.00 7.13  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 151.246 195.765 156.792 1.00 9.45  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 150.032 196.164 157.308 1.00 11.32 ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 151.252 196.160 155.497 1.00 10.51 ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 149.336 196.775 156.366 1.00 11.65 ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 150.053 196.784 155.257 1.00 13.48 ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 155.026 195.384 159.835 1.00 12.97 ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 156.191 194.707 160.388 1.00 13.16 ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 155.705 193.529 161.218 1.00 14.11 ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 154.969 193.706 162.196 1.00 18.31 ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 157.051 195.664 161.225 1.00 9.28  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 157.177 197.009 160.514 1.00 11.06 ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 158.422 195.067 161.468 1.00 14.51 ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 157.866 198.059 161.329 1.00 17.20 ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 156.115 192.328 160.826 1.00 8.29  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 155.698 191.091 161.472 1.00 7.55  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 156.936 190.393 162.010 1.00 13.22 ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 157.920 190.218 161.283 1.00 17.11 ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 154.939 190.173 160.496 1.00 7.47  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 153.674 190.864 159.983 1.00 10.07 ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 154.601 188.849 161.159 1.00 10.63 ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 152.997 190.126 158.857 1.00 9.31  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 156.894 190.008 163.282 1.00 16.57 ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 157.932 189.155 163.841 1.00 9.52  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 157.500 187.704 163.664 1.00 11.57 ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 156.661 187.206 164.425 1.00 14.20 ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 158.182 189.476 165.313 1.00 8.71  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 159.586 189.116 165.756 1.00 13.11 ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 160.062 188.020 165.397 1.00 9.98  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 160.215 189.929 166.465 1.00 19.81 ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 158.042 187.003 162.665 1.00 6.63  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 157.542 185.656 162.358 1.00 2.08  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 157.804 184.634 163.447 1.00 4.42  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 157.086 183.629 163.511 1.00 4.35  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 158.292 185.297 161.072 1.00 7.74  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 159.561 186.076 161.174 1.00 5.74  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 159.197 187.369 161.830 1.00 5.16  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 158.803 184.848 164.298 1.00 5.02  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 159.154 183.885 165.330 1.00 3.10  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 158.689 184.298 166.719 1.00 7.82  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 158.849 183.518 167.662 1.00 10.27 ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 160.668 183.654 165.341 1.00 7.54  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 161.223 183.213 164.000 1.00 3.82  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 161.302 181.702 163.911 1.00 2.50  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 162.625 181.198 164.446 1.00 4.50  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 162.772 179.729 164.288 1.00 6.50  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 158.124 185.497 166.872 1.00 5.19  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 157.505 185.879 168.134 1.00 0.54  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 156.154 185.213 168.337 1.00 2.12  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 155.613 185.271 169.446 1.00 11.15 ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 157.350 187.396 168.209 1.00 0.79  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 155.601 184.590 167.297 1.00 3.50  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 154.327 183.892 167.363 1.00 6.17  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 154.502 182.520 166.729 1.00 5.29  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 155.448 182.271 165.980 1.00 9.82  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 153.198 184.668 166.657 1.00 3.67  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 153.591 184.971 165.210 1.00 0.00  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 152.881 185.952 167.405 1.00 7.27  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 152.629 185.882 164.497 1.00 3.22  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 153.571 181.625 167.041 1.00 2.31  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 153.598 180.301 166.446 1.00 3.20  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 153.237 180.376 164.966 1.00 4.90  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 152.607 181.329 164.499 1.00 8.58  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 152.640 179.362 167.177 1.00 6.74  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 151.294 179.762 166.994 1.00 13.78 ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 153.661 179.354 164.219 1.00 5.15  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 153.373 179.308 162.790 1.00 3.09  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 151.875 179.247 162.522 1.00 5.98  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 151.401 179.774 161.508 1.00 8.55  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 154.085 178.112 162.160 1.00 3.15  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 154.056 178.083 160.646 1.00 3.46  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 154.832 176.891 160.119 1.00 4.58  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 154.400 176.530 158.711 1.00 8.12  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 155.030 175.263 158.251 1.00 5.18  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 151.115 178.613 163.420 1.00 2.44  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 149.662 178.614 163.296 1.00 1.06  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 149.102 180.024 163.423 1.00 4.50  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 148.163 180.395 162.709 1.00 11.92 ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 149.047 177.696 164.351 1.00 4.01  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 149.020 176.246 163.915 1.00 14.36 ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 149.762 175.894 162.975 1.00 17.63 ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 148.259 175.457 164.514 1.00 10.68 ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 149.660 180.825 164.332 1.00 3.29  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 149.243 182.212 164.476 1.00 2.16  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 149.799 183.107 163.379 1.00 1.59  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 149.325 184.235 163.217 1.00 5.39  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 149.671 182.754 165.839 1.00 4.51  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 148.883 182.201 166.985 1.00 7.06  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 147.534 181.931 166.898 1.00 9.23  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 149.253 181.868 168.244 1.00 5.60  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 147.108 181.455 168.054 1.00 5.38  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 148.131 181.407 168.887 1.00 5.96  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 150.791 182.633 162.626 1.00 2.37  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 151.399 183.425 161.565 1.00 2.32  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 150.720 183.211 160.218 1.00 3.95  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 150.545 184.168 159.458 1.00 6.83  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 152.890 183.096 161.450 1.00 4.74  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 153.647 183.726 160.281 1.00 2.75  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 153.743 185.232 160.449 1.00 3.27  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 155.028 183.110 160.142 1.00 2.40  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 150.331 181.977 159.905 1.00 4.62  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 149.726 181.673 158.616 1.00 2.39  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 148.250 181.323 158.691 1.00 5.61  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 147.516 181.603 157.743 1.00 7.57  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 150.471 180.517 157.938 1.00 1.02  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 151.836 180.901 157.428 1.00 1.36  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 151.983 181.850 156.428 1.00 2.93  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 152.981 180.321 157.952 1.00 4.82  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 153.229 182.207 155.961 1.00 3.59  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 154.228 180.672 157.494 1.00 5.27  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 154.348 181.614 156.497 1.00 3.20  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 155.595 181.964 156.038 1.00 8.12  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 147.797 180.723 159.783 1.00 4.17  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 146.411 180.332 159.931 1.00 1.77  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 146.278 178.901 160.414 1.00 5.66  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 147.225 178.118 160.420 1.00 9.39  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 145.054 178.576 160.819 1.00 7.31  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 144.744 177.281 161.409 1.00 6.38  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 143.491 176.705 160.768 1.00 7.20  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 142.481 177.403 160.633 1.00 9.24  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 144.557 177.402 162.929 1.00 9.77  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 145.834 177.569 163.556 1.00 6.92  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 143.884 176.163 163.496 1.00 11.84 ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 143.556 175.436 160.380 1.00 8.74  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 142.396 174.694 159.910 1.00 9.48  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 141.894 173.821 161.052 1.00 13.73 ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 142.634 172.972 161.558 1.00 20.46 ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 142.747 173.846 158.688 1.00 14.54 ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 141.622 173.500 157.712 1.00 16.16 ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 140.756 174.710 157.428 1.00 15.01 ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 142.199 172.947 156.421 1.00 12.10 ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 140.649 174.033 161.455 1.00 21.63 ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 140.089 173.306 162.588 1.00 24.23 ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 139.899 171.840 162.221 1.00 30.32 ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 139.192 171.544 161.252 1.00 32.01 ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 138.759 173.930 163.000 1.00 25.86 ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 138.453 173.741 164.473 1.00 32.20 ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 139.112 172.905 165.122 1.00 31.80 ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 137.548 174.433 164.984 1.00 34.30 ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 140.507 170.899 162.946 1.00 32.47 ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 140.349 169.481 162.587 1.00 34.05 ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 138.921 168.975 162.690 1.00 34.37 ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 138.584 167.983 162.030 1.00 33.00 ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 141.273 168.761 163.579 1.00 32.61 ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 141.465 169.725 164.703 1.00 29.84 ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 141.429 171.083 164.080 1.00 28.79 ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 138.068 169.620 163.487 1.00 36.83 ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 136.703 169.141 163.688 1.00 34.82 ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 135.736 169.724 162.660 1.00 35.64 ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 135.103 168.980 161.905 1.00 37.32 ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 136.239 169.471 165.110 1.00 36.73 ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 137.273 169.110 166.158 1.00 37.50 ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 137.770 167.985 166.195 1.00 36.30 ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 137.602 170.066 167.020 1.00 34.75 ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 135.610 171.047 162.624 1.00 30.75 ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 134.650 171.707 161.750 1.00 32.30 ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 135.239 172.116 160.407 1.00 32.78 ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 134.501 172.629 159.558 1.00 32.73 ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 134.061 172.939 162.446 1.00 33.15 ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 133.087 173.554 161.593 1.00 38.03 ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 135.152 173.943 162.766 1.00 31.46 ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 136.540 171.900 160.193 1.00 25.59 ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 137.209 172.229 158.933 1.00 21.61 ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 137.015 173.699 158.562 1.00 23.10 ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 136.812 174.043 157.396 1.00 25.38 ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 136.738 171.315 157.800 1.00 24.51 ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 136.819 169.831 158.124 1.00 26.36 ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 138.184 169.455 158.676 1.00 24.33 ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 139.244 169.645 157.696 1.00 22.66 ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 140.537 169.504 157.955 1.00 21.35 ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 140.968 169.167 159.159 1.00 22.11 ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 141.420 169.702 156.980 1.00 20.43 ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 137.081 174.570 159.563 1.00 26.25 ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 136.945 176.005 159.364 1.00 23.34 ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 138.316 176.666 159.426 1.00 19.53 ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 139.137 176.337 160.286 1.00 21.23 ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 136.019 176.620 160.414 1.00 20.39 ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 135.685 178.081 160.163 1.00 23.42 ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 134.281 178.444 160.600 1.00 29.13 ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 133.922 178.150 161.759 1.00 30.15 ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 133.536 179.025 159.784 1.00 27.31 ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 138.554 177.599 158.510 1.00 9.60  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 139.847 178.255 158.390 1.00 6.00  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 139.853 179.561 159.172 1.00 8.68  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 138.984 180.415 158.977 1.00 9.64  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 140.178 178.522 156.921 1.00 4.36  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 141.412 179.338 156.727 1.00 5.11  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 141.477 180.672 156.457 1.00 8.29  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 142.766 178.877 156.787 1.00 3.78  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 142.787 181.071 156.347 1.00 6.37  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 143.597 179.985 156.546 1.00 3.75  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 143.353 177.631 157.022 1.00 1.56  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 144.984 179.888 156.533 1.00 1.99  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 144.730 177.537 157.009 1.00 4.66  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 145.530 178.658 156.765 1.00 5.53  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 140.836 179.710 160.056 1.00 7.95  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 141.072 180.944 160.791 1.00 3.32  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 142.359 181.562 160.266 1.00 4.90  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 143.410 180.913 160.277 1.00 10.12 ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 141.175 180.684 162.294 1.00 4.29  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 139.953 180.101 162.764 1.00 16.54 ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 141.432 181.980 163.042 1.00 4.34  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 142.273 182.808 159.807 1.00 4.45  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 143.416 183.464 159.191 1.00 1.38  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 144.505 183.749 160.216 1.00 5.95  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 144.225 184.089 161.368 1.00 12.51 ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 142.981 184.767 158.525 1.00 2.86  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 142.728 184.608 157.043 1.00 8.94  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 142.910 183.487 156.525 1.00 7.48  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 142.345 185.604 156.395 1.00 10.57 ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 145.754 183.608 159.787 1.00 3.89  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 146.890 183.985 160.598 1.00 1.79  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 147.195 185.462 160.458 1.00 5.08  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 146.394 186.251 159.960 1.00 10.36 ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 148.391 185.838 160.909 1.00 9.72  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 148.785 187.242 160.861 1.00 9.17  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 149.110 187.675 159.436 1.00 10.76 ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 148.493 188.603 158.896 1.00 15.26 ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 149.976 187.477 161.789 1.00 7.13  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 150.455 188.919 161.926 1.00 8.87  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 149.279 189.853 162.149 1.00 14.46 ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 151.450 189.029 163.063 1.00 12.59 ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 150.084 187.010 158.813 1.00 7.85  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 150.457 187.353 157.444 1.00 3.06  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 149.296 187.122 156.489 1.00 7.41  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 149.072 187.918 155.568 1.00 11.60 ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 151.676 186.541 157.012 1.00 4.38  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 152.007 186.677 155.555 1.00 7.27  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 152.484 187.872 155.049 1.00 6.84  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 151.835 185.613 154.689 1.00 6.06  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 152.788 188.002 153.711 1.00 5.78  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 152.136 185.737 153.349 1.00 5.20  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 152.613 186.933 152.860 1.00 6.72  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 148.549 186.033 156.686 1.00 6.84  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 147.394 185.767 155.836 1.00 0.11  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 146.347 186.863 155.970 1.00 3.74  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 145.782 187.315 154.969 1.00 7.63  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 146.788 184.408 156.179 1.00 0.00  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 147.834 183.442 156.328 1.00 5.33  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 145.846 183.957 155.078 1.00 0.96  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 146.073 187.308 157.201 1.00 3.97  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 145.101 188.380 157.397 1.00 2.41  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 145.562 189.669 156.735 1.00 5.15  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 144.773 190.346 156.069 1.00 10.10 ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 144.852 188.606 158.886 1.00 5.24  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 144.210 189.920 159.202 1.00 11.00 ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 142.862 190.150 159.039 1.00 15.64 ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 144.733 191.075 159.678 1.00 10.24 ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 142.581 191.390 159.397 1.00 11.60 ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 143.700 191.973 159.788 1.00 10.68 ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 146.840 190.019 156.898 1.00 7.78  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 147.351 191.250 156.301 1.00 2.42  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 147.253 191.186 154.780 1.00 3.25  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 146.770 192.121 154.127 1.00 8.59  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 148.798 191.508 156.762 1.00 2.89  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 149.433 192.605 155.930 1.00 7.54  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 148.829 191.864 158.239 1.00 6.84  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 147.694 190.070 154.194 1.00 2.11  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 147.678 189.936 152.743 1.00 0.00  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 146.255 189.931 152.200 1.00 3.60  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 145.983 190.543 151.164 1.00 8.85  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 148.418 188.667 152.325 1.00 2.84  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 148.654 188.494 150.824 1.00 4.82  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 149.507 189.630 150.286 1.00 3.86  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 149.301 187.154 150.533 1.00 4.00  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 145.336 189.241 152.878 1.00 2.29  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 143.951 189.205 152.424 1.00 0.00  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 143.296 190.575 152.534 1.00 3.42  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 142.511 190.964 151.664 1.00 7.81  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 143.169 188.166 153.223 1.00 1.25  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 141.775 187.898 152.697 1.00 4.97  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 140.977 187.080 153.688 1.00 5.29  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 141.654 185.834 154.028 1.00 1.30  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 141.641 184.746 153.272 1.00 2.99  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 140.994 184.714 152.120 1.00 8.09  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 142.293 183.664 153.681 1.00 3.85  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 143.600 191.319 153.600 1.00 4.30  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 143.076 192.672 153.731 1.00 1.20  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 143.601 193.571 152.619 1.00 4.40  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 142.862 194.403 152.084 1.00 9.80  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 143.436 193.238 155.104 1.00 3.47  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 143.287 194.742 155.225 1.00 9.33  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 143.623 195.212 156.629 1.00 10.53 ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 142.440 195.046 157.564 1.00 8.56  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 141.332 195.979 157.226 1.00 9.19  ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 144.877 193.417 152.259 1.00 4.91  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 145.427 194.190 151.148 1.00 1.42  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 144.750 193.807 149.836 1.00 3.22  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 144.392 194.675 149.031 1.00 8.30  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 146.952 194.009 151.072 1.00 1.32  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 147.626 194.626 152.297 1.00 3.12  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 147.498 194.634 149.802 1.00 2.93  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 149.075 194.234 152.454 1.00 2.26  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 144.567 192.507 149.599 1.00 6.07  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 143.989 192.041 148.341 1.00 3.90  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 142.546 192.510 148.199 1.00 3.86  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 142.125 192.945 147.121 1.00 8.04  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 144.096 190.508 148.242 1.00 2.45  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 145.549 190.082 148.039 1.00 0.30  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 143.232 189.981 147.111 1.00 4.78  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 145.801 188.632 148.368 1.00 0.20  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 141.766 192.423 149.278 1.00 0.74  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 140.361 192.815 149.214 1.00 2.23  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 140.214 194.294 148.884 1.00 8.26  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 139.317 194.680 148.123 1.00 10.78 ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 139.663 192.483 150.531 1.00 6.20  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 139.550 190.990 150.768 1.00 14.14 ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 139.861 190.214 149.839 1.00 10.53 ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 139.148 190.592 151.881 1.00 11.94 ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 141.083 195.134 149.446 1.00 6.03  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 141.105 196.570 149.162 1.00 3.19  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 139.756 197.217 149.462 1.00 6.05  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 139.213 197.979 148.660 1.00 13.59 ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 141.531 196.837 147.718 1.00 6.93  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 141.711 198.222 147.489 1.00 14.33 ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 139.208 196.898 150.634 1.00 9.06  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 137.962 197.527 151.058 1.00 12.50 ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 138.175 199.016 151.293 1.00 15.48 ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 137.306 199.839 150.983 1.00 18.38 ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 137.413 196.820 152.313 1.00 12.15 ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 136.150 197.507 152.804 1.00 9.85  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 137.146 195.355 152.018 1.00 14.75 ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 139.335 199.387 151.826 1.00 12.22 ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 139.667 200.773 152.128 1.00 9.25  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 140.822 201.276 151.264 1.00 12.20 ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 141.675 202.039 151.719 1.00 15.28 ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 139.995 200.933 153.610 1.00 10.58 ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 138.842 200.566 154.527 1.00 11.73 ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 139.326 200.240 155.929 1.00 14.29 ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 138.234 199.814 156.793 1.00 19.62 ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 137.712 198.595 156.797 1.00 16.09 ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 138.164 197.647 155.992 1.00 13.44 ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 136.713 198.319 157.629 1.00 16.42 ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 140.854 200.853 150.005 1.00 9.28  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 141.846 201.340 149.062 1.00 10.65 ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 143.280 200.967 149.372 1.00 11.46 ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 144.171 201.816 149.265 1.00 10.69 ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 143.526 199.713 149.757 1.00 9.19  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 144.886 199.270 150.033 1.00 3.52  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 145.667 198.926 148.773 1.00 6.51  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 146.895 198.811 148.835 1.00 13.65 ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 144.872 198.064 150.973 1.00 0.41  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 144.650 198.423 152.431 1.00 9.89  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 143.259 198.080 152.913 1.00 15.19 ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 143.019 198.146 154.136 1.00 16.48 ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 142.404 197.740 152.069 1.00 14.50 ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 144.992 198.756 147.636 1.00 3.73  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 145.681 198.449 146.390 1.00 4.41  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 146.262 199.681 145.713 1.00 6.94  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 147.080 199.535 144.797 1.00 8.10  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 144.735 197.733 145.423 1.00 5.28  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 144.440 196.266 145.731 1.00 3.48  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 143.395 195.716 144.777 1.00 6.69  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 145.710 195.444 145.671 1.00 4.68  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 145.864 200.880 146.129 1.00 8.34  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 146.409 202.115 145.589 1.00 7.02  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 147.605 202.621 146.381 1.00 10.08 ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 148.150 203.678 146.047 1.00 15.45 ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 145.327 203.199 145.546 1.00 6.13  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 143.929 202.683 145.254 1.00 8.19  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 143.852 201.889 143.965 1.00 9.40  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 143.253 200.815 143.918 1.00 8.89  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 144.461 202.416 142.910 1.00 9.75  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 148.017 201.899 147.415 1.00 6.35  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 149.133 202.279 148.265 1.00 3.93  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 150.279 201.294 148.086 1.00 6.79  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 150.096 200.169 147.617 1.00 12.83 ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 148.704 202.326 149.734 1.00 4.93  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 147.602 203.328 150.023 1.00 7.26  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 147.234 203.342 151.496 1.00 8.00  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 146.387 202.137 151.864 1.00 11.04 ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 145.925 202.185 153.278 1.00 13.03 ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 151.475 201.734 148.470 1.00 7.27  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 152.670 200.894 148.415 1.00 6.89  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 152.739 200.103 149.714 1.00 8.74  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 153.074 200.646 150.768 1.00 15.55 ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 153.915 201.744 148.202 1.00 8.53  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 155.220 201.036 148.512 1.00 10.08 ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 156.407 201.942 148.251 1.00 12.48 ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 156.767 201.977 146.839 1.00 12.47 ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 156.535 203.004 146.034 1.00 10.55 ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 155.938 204.101 146.469 1.00 9.55  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 156.914 202.929 144.762 1.00 8.09  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 152.415 198.816 149.644 1.00 4.89  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 152.358 197.957 150.820 1.00 3.03  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 153.652 197.161 150.925 1.00 7.09  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 154.013 196.432 149.997 1.00 9.97  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 151.156 197.016 150.747 1.00 3.40  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 149.864 197.688 150.324 1.00 5.32  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 149.150 198.357 151.477 1.00 9.30  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 148.677 199.485 151.358 1.00 13.96 ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 149.065 197.663 152.601 1.00 10.87 ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 154.344 197.303 152.053 1.00 8.39  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 155.576 196.575 152.322 1.00 7.15  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 155.373 195.728 153.568 1.00 8.52  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 155.152 196.266 154.655 1.00 16.77 ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 156.753 197.532 152.519 1.00 7.46  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 157.291 198.113 151.253 1.00 6.01  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 156.792 197.948 149.997 1.00 6.67  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 158.441 198.955 151.121 1.00 11.42 ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 157.559 198.634 149.089 1.00 4.72  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 158.577 199.261 149.754 1.00 10.27 ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 159.368 199.480 152.025 1.00 11.23 ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 159.602 200.070 149.271 1.00 8.42  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 160.384 200.280 151.544 1.00 8.84  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 160.492 200.568 150.179 1.00 6.90  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 155.460 194.412 153.412 1.00 7.25  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 155.346 193.484 154.531 1.00 8.56  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 156.757 193.070 154.920 1.00 13.28 ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 157.413 192.311 154.198 1.00 20.62 ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 154.476 192.271 154.176 1.00 10.10 ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 153.113 192.733 153.660 1.00 10.92 ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 154.310 191.372 155.386 1.00 11.67 ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 152.206 191.607 153.235 1.00 10.53 ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 157.226 193.565 156.060 1.00 14.05 ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 158.599 193.374 156.507 1.00 11.80 ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 158.608 192.293 157.577 1.00 11.18 ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 158.028 192.471 158.655 1.00 18.16 ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 159.206 194.680 157.040 1.00 7.59  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 160.698 194.513 157.271 1.00 13.75 ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 158.933 195.823 156.079 1.00 9.68  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 159.278 191.182 157.284 1.00 10.45 ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 159.400 190.071 158.227 1.00 5.86  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 160.640 190.252 159.104 1.00 12.56 ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 161.650 189.564 158.968 1.00 20.28 ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 159.442 188.748 157.475 1.00 8.76  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 158.088 188.221 157.102 1.00 10.20 ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 157.220 187.758 158.072 1.00 10.65 ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 157.686 188.189 155.779 1.00 9.96  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 155.977 187.272 157.732 1.00 10.09 ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 156.443 187.704 155.434 1.00 10.27 ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 155.588 187.245 156.412 1.00 12.42 ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 160.542 191.209 160.024 1.00 10.96 ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 161.655 191.509 160.914 1.00 5.09  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 161.760 190.446 162.001 1.00 10.45 ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 160.916 190.372 162.897 1.00 18.35 ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 161.464 192.894 161.534 1.00 6.85  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 162.703 193.396 162.252 1.00 16.58 ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 163.643 192.605 162.470 1.00 19.35 ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 162.734 194.593 162.605 1.00 14.75 ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 162.803 189.632 161.925 1.00 4.15  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 163.029 188.568 162.875 1.00 6.55  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 163.900 187.493 162.267 1.00 8.76  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 164.512 187.691 161.220 1.00 10.25 ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 163.949 186.346 162.936 1.00 8.28  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 164.767 185.227 162.497 1.00 0.86  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 164.072 184.461 161.380 1.00 3.81  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 162.844 184.378 161.325 1.00 14.85 ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 165.066 184.280 163.661 1.00 8.38  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 165.564 185.005 164.893 1.00 13.81 ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 166.772 185.316 164.956 1.00 13.41 ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 164.748 185.259 165.803 1.00 14.39 ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 164.877 183.891 160.487 1.00 5.39  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 164.384 183.107 159.362 1.00 8.78  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 164.862 181.673 159.536 1.00 11.73 ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 166.070 181.423 159.644 1.00 13.43 ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 164.853 183.679 158.014 1.00 4.48  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 164.774 182.622 156.930 1.00 5.38  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 164.009 184.878 157.629 1.00 6.39  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 163.921 180.741 159.569 1.00 9.99  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 164.195 179.315 159.547 1.00 5.89  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 163.291 178.670 158.511 1.00 8.64  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 162.245 179.227 158.164 1.00 10.84 ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 164.003 178.672 160.933 1.00 7.34  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 162.552 178.646 161.405 1.00 11.99 ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 161.650 179.144 160.713 1.00 12.58 ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 162.305 178.113 162.505 1.00 15.63 ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 163.674 177.508 157.976 1.00 5.94  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 162.863 176.906 156.906 1.00 7.16  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 161.420 176.643 157.301 1.00 8.09  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 160.534 176.741 156.444 1.00 13.83 ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 163.610 175.600 156.589 1.00 8.83  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 164.540 175.382 157.739 1.00 7.69  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 164.902 176.739 158.228 1.00 5.25  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 161.151 176.367 158.579 1.00 8.91  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 159.817 175.930 158.983 1.00 7.09  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 158.754 176.973 158.657 1.00 11.15 ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 157.669 176.626 158.177 1.00 13.61 ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 159.806 175.598 160.474 1.00 6.23  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 160.458 174.268 160.813 1.00 12.12 ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 160.041 173.746 162.173 1.00 19.32 ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 159.051 174.265 162.730 1.00 19.82 ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 160.701 172.817 162.685 1.00 17.52 ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 159.034 178.252 158.910 1.00 12.54 ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 158.043 179.287 158.640 1.00 5.36  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 158.201 179.943 157.277 1.00 8.91  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 157.195 180.331 156.676 1.00 13.67 ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 158.067 180.366 159.738 1.00 10.71 ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 159.104 181.454 159.578 1.00 11.93 ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 160.302 181.539 160.216 1.00 6.90  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 159.005 182.630 158.763 1.00 14.95 ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 160.972 182.672 159.832 1.00 4.98  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 160.194 183.361 158.940 1.00 8.78  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 158.034 183.128 157.890 1.00 13.16 ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 160.438 184.558 158.277 1.00 9.92  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 158.277 184.315 157.236 1.00 7.60  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 159.468 185.019 157.436 1.00 12.17 ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 159.424 180.079 156.760 1.00 11.46 ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 159.612 180.823 155.520 1.00 6.25  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 159.453 179.944 154.282 1.00 5.89  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 159.180 180.468 153.193 1.00 14.21 ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 160.983 181.528 155.495 1.00 1.16  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 162.113 180.520 155.434 1.00 4.77  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 161.063 182.545 154.366 1.00 5.09  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 159.593 178.620 154.413 1.00 5.38  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 159.383 177.746 153.269 1.00 3.20  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 157.930 177.720 152.815 1.00 6.41  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 157.656 177.258 151.704 1.00 11.68 ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 159.850 176.329 153.598 1.00 6.94  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 161.356 176.130 153.519 1.00 7.97  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 161.808 175.598 152.178 1.00 15.25 ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 163.002 175.754 151.848 1.00 16.47 ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 160.974 175.012 151.456 1.00 17.17 ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 157.000 178.196 153.646 1.00 7.87  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 155.623 178.380 153.210 1.00 5.25  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 155.483 179.523 152.217 1.00 6.66  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 154.446 179.634 151.555 1.00 10.39 ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 154.717 178.640 154.413 1.00 3.00  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 154.460 177.398 155.226 1.00 7.34  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 155.366 176.602 155.466 1.00 14.75 ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 153.218 177.221 155.659 1.00 7.27  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 156.498 180.374 152.103 1.00 4.37  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 156.465 181.535 151.228 1.00 0.67  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 157.151 181.282 149.897 1.00 1.84  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 157.423 182.236 149.165 1.00 10.32 ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 157.112 182.735 151.921 1.00 4.15  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 156.413 183.290 153.161 1.00 2.94  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 157.205 184.446 153.735 1.00 5.39  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 155.001 183.724 152.825 1.00 4.25  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 157.450 180.024 149.570 1.00 1.79  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 158.151 179.732 148.324 1.00 0.93  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 157.324 180.145 147.115 1.00 2.61  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 157.839 180.761 146.177 1.00 8.91  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 158.502 178.246 148.254 1.00 4.06  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 159.781 177.917 148.990 1.00 11.13 ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 160.439 178.797 149.543 1.00 12.65 ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 160.150 176.642 148.992 1.00 7.28  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 156.028 179.821 147.122 1.00 3.20  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 155.172 180.171 145.994 1.00 1.99  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 154.938 181.675 145.929 1.00 2.53  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 154.742 182.239 144.847 1.00 8.02  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 153.847 179.417 146.093 1.00 4.18  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 153.284 179.553 147.385 1.00 5.19  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 154.948 182.343 147.084 1.00 1.73  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 154.817 183.799 147.105 1.00 0.00  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 156.053 184.448 146.495 1.00 0.87  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 155.958 185.395 145.705 1.00 3.96  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 154.576 184.295 148.542 1.00 0.00  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 154.362 185.798 148.556 1.00 1.90  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 153.393 183.579 149.161 1.00 5.08  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 157.216 184.077 147.009 1.00 3.36  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 158.451 184.776 146.596 1.00 3.13  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 158.964 184.194 145.282 1.00 4.41  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 160.062 184.573 144.871 1.00 7.32  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 159.450 184.608 147.735 1.00 4.85  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 158.987 185.024 149.127 1.00 1.33  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 160.071 184.583 150.083 1.00 0.12  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 158.836 186.525 149.150 1.00 1.46  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 158.181 183.335 144.645 1.00 4.96  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 158.577 182.758 143.344 1.00 0.77  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 157.904 183.572 142.269 1.00 6.16  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 157.859 184.797 142.402 1.00 10.06 ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 158.063 181.359 143.119 1.00 2.76  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 158.700 180.285 143.983 1.00 10.73 ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 159.556 180.650 144.806 1.00 18.44 ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 158.341 179.102 143.810 1.00 6.44  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 157.384 182.896 141.260 1.00 8.03  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 156.736 183.600 140.135 1.00 7.46  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 155.301 183.135 140.127 1.00 12.74 ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 154.567 183.483 139.205 1.00 15.37 ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 157.424 183.294 138.829 1.00 10.26 ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 158.912 183.612 138.809 1.00 13.96 ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 159.268 184.769 139.121 1.00 12.90 ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 159.701 182.705 138.474 1.00 14.30 ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 154.965 182.307 141.098 1.00 6.26  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 153.552 181.903 141.229 1.00 1.51  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 152.910 183.069 141.973 1.00 6.92  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 151.761 183.377 141.674 1.00 12.20 ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 153.437 180.524 141.868 1.00 1.14  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 154.212 179.448 141.158 1.00 8.10  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 153.871 179.082 140.033 1.00 13.65 ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 155.219 178.894 141.815 1.00 9.15  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 153.661 183.749 142.833 1.00 3.77  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 153.142 184.836 143.664 1.00 2.27  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 151.806 184.462 144.298 1.00 5.09  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 150.854 185.244 144.305 1.00 10.71 ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 153.026 186.132 142.862 1.00 0.00  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 154.362 186.769 142.540 1.00 3.08  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 154.185 188.072 141.788 1.00 4.65  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 153.745 187.814 140.361 1.00 9.14  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 154.792 187.080 139.598 1.00 7.79  ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 151.737 183.249 144.837 1.00 1.54  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 150.524 182.715 145.441 1.00 0.00  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 150.811 182.272 146.866 1.00 1.52  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 151.787 181.561 147.114 1.00 12.42 ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 149.984 181.533 144.634 1.00 2.05  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 149.392 181.827 143.257 1.00 0.54  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 148.879 180.549 142.638 1.00 2.76  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 148.275 182.843 143.369 1.00 0.48  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 149.960 182.697 147.798 1.00 0.00  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 149.975 182.171 149.162 1.00 0.08  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 148.991 181.008 149.220 1.00 4.55  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 147.776 181.175 149.344 1.00 6.73  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 149.630 183.258 150.171 1.00 1.80  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 149.576 182.804 151.631 1.00 0.49  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 150.922 182.260 152.075 1.00 0.34  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 149.127 183.940 152.533 1.00 5.28  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 149.536 179.801 149.112 1.00 6.78  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 148.717 178.594 149.108 1.00 5.95  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 148.415 178.175 150.541 1.00 4.34  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 149.330 178.012 151.355 1.00 5.66  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 149.423 177.473 148.353 1.00 6.81  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 149.849 177.954 147.072 1.00 2.01  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 148.482 176.304 148.162 1.00 11.58 ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 147.141 178.001 150.848 1.00 3.90  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 146.676 177.582 152.157 1.00 3.34  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 146.136 176.163 152.101 1.00 5.49  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 145.702 175.693 151.045 1.00 8.07  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 145.589 178.536 152.661 1.00 3.55  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 145.914 180.029 152.599 1.00 1.42  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 144.691 180.848 152.960 1.00 5.42  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 147.077 180.366 153.514 1.00 0.07  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 146.160 175.437 153.223 1.00 3.30  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 145.709 174.035 153.198 1.00 2.42  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 144.248 173.856 152.825 1.00 4.71  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 143.874 172.766 152.378 1.00 13.13 ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 145.984 173.548 154.628 1.00 4.09  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 146.180 174.779 155.440 1.00 2.84  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 146.747 175.803 154.521 1.00 1.37  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 143.408 174.877 152.984 1.00 3.54  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 141.994 174.754 152.647 1.00 2.28  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 141.718 174.942 151.161 1.00 3.79  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 140.561 175.157 150.782 1.00 10.83 ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 141.166 175.753 153.460 1.00 3.41  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 141.544 177.188 153.178 1.00 6.55  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 142.687 177.589 153.374 1.00 9.29  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 140.582 177.974 152.715 1.00 5.73  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 142.741 174.866 150.314 1.00 2.91  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 142.567 175.022 148.887 1.00 2.41  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 142.522 176.450 148.396 1.00 7.88  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 142.378 176.667 147.187 1.00 10.90 ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 142.644 177.430 149.287 1.00 8.33  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 142.604 178.828 148.892 1.00 3.87  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 143.980 179.293 148.436 1.00 6.72  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 145.004 178.900 149.002 1.00 8.94  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 142.119 179.692 150.053 1.00 3.38  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 141.330 180.913 149.631 1.00 7.66  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 140.956 181.793 150.805 1.00 12.06 ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 140.863 181.270 151.934 1.00 8.70  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 140.757 183.007 150.596 1.00 14.13 ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 143.998 180.131 147.403 1.00 8.62  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 145.230 180.693 146.863 1.00 6.72  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 145.065 182.201 146.750 1.00 4.77  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 144.133 182.677 146.091 1.00 6.56  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 145.564 180.077 145.501 1.00 9.23  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 145.687 178.559 145.532 1.00 11.75 ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 145.284 177.937 144.209 1.00 4.61  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 146.426 177.730 143.328 1.00 6.86  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 146.455 178.076 142.050 1.00 14.12 ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 145.421 178.661 141.470 1.00 12.45 ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 147.549 177.831 141.334 1.00 12.34 ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 145.962 182.945 147.388 1.00 4.50  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 145.910 184.402 147.427 1.00 0.49  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 147.003 184.958 146.527 1.00 0.00  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 148.189 184.729 146.780 1.00 4.52  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 146.084 184.918 148.856 1.00 3.01  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 144.895 184.831 149.814 1.00 4.47  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 144.752 183.430 150.375 1.00 4.71  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 145.057 185.836 150.938 1.00 2.93  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 146.606 185.686 145.488 1.00 0.00  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 147.562 186.246 144.543 1.00 0.91  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 148.206 187.498 145.123 1.00 3.59  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 147.515 188.375 145.648 1.00 11.03 ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 146.877 186.570 143.218 1.00 3.43  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 146.332 185.403 142.629 1.00 7.61  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 149.524 187.583 145.021 1.00 0.00  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 150.244 188.744 145.527 1.00 0.00  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 150.002 189.941 144.617 1.00 5.90  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 150.306 189.865 143.420 1.00 12.62 ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 151.735 188.441 145.624 1.00 1.25  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 152.570 189.363 146.515 1.00 3.46  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 152.342 189.039 147.978 1.00 5.23  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 154.042 189.253 146.164 1.00 7.33  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 149.458 191.047 145.126 1.00 1.30  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 149.233 192.207 144.268 1.00 0.00  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 150.548 192.805 143.807 1.00 4.11  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 151.581 192.664 144.483 1.00 12.35 ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 148.462 193.178 145.181 1.00 0.08  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 147.902 192.326 146.267 1.00 4.73  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 148.899 191.238 146.473 1.00 3.84  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 150.563 193.477 142.652 1.00 2.90  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 151.825 194.044 142.147 1.00 4.58  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 152.408 195.138 143.023 1.00 5.37  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 153.600 195.436 142.894 1.00 7.37  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 151.438 194.587 140.764 1.00 4.84  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 149.964 194.797 140.837 1.00 4.81  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 149.440 193.717 141.730 1.00 5.82  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 151.619 195.752 143.901 1.00 2.87  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 152.099 196.836 144.748 1.00 3.06  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 152.637 196.354 146.087 1.00 3.33  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 153.018 197.185 146.918 1.00 7.04  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 150.982 197.855 144.986 1.00 5.35  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 149.863 197.303 145.844 1.00 7.21  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 149.227 196.312 145.492 1.00 10.10 ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 149.618 197.944 146.979 1.00 5.08  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 152.684 195.046 146.317 1.00 1.70  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 153.081 194.482 147.603 1.00 3.32  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 154.495 193.934 147.490 1.00 7.87  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 154.810 193.187 146.554 1.00 8.67  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 152.102 193.386 148.056 1.00 0.00  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 152.536 192.808 149.389 1.00 5.90  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 150.700 193.947 148.152 1.00 0.00  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 155.346 194.306 148.440 1.00 6.28  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 156.700 193.781 148.553 1.00 7.82  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 156.816 192.988 149.845 1.00 9.64  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 156.378 193.451 150.902 1.00 10.46 ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 157.735 194.907 148.538 1.00 7.93  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 157.814 195.679 147.236 1.00 5.56  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 158.350 194.813 146.115 1.00 1.59  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 158.492 195.561 144.872 1.00 7.28  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 157.490 195.864 144.060 1.00 7.80  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 156.249 195.495 144.326 1.00 8.08  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 157.739 196.557 142.953 1.00 9.55  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 157.402 191.799 149.760 1.00 9.88  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 157.663 190.965 150.927 1.00 11.05 ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 159.122 191.156 151.312 1.00 13.26 ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 160.026 190.827 150.536 1.00 20.69 ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 157.349 189.487 150.649 1.00 11.90 ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 155.920 189.337 150.126 1.00 12.64 ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 157.544 188.660 151.906 1.00 13.08 ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 154.864 189.804 151.097 1.00 13.31 ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 159.353 191.684 152.509 1.00 12.15 ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 160.684 192.057 152.959 1.00 8.87  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 161.075 191.229 154.175 1.00 12.97 ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 160.246 190.938 155.040 1.00 21.72 ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 160.744 193.548 153.303 1.00 17.00 ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 160.459 194.461 152.125 1.00 16.00 ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 161.277 196.057 152.264 1.00 17.65 ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 161.273 196.577 150.555 1.00 15.46 ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 162.350 190.847 154.229 1.00 11.52 ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 162.914 190.094 155.349 1.00 11.46 ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 164.091 190.898 155.890 1.00 13.55 ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 165.144 190.969 155.252 1.00 23.21 ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 163.349 188.690 154.931 1.00 11.18 ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 162.262 187.867 154.302 1.00 12.85 ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 161.958 188.003 152.960 1.00 14.27 ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 161.564 186.936 155.048 1.00 12.79 ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 160.968 187.244 152.381 1.00 12.42 ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 160.572 186.173 154.470 1.00 10.74 ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 160.275 186.328 153.137 1.00 10.13 ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 163.918 191.502 157.061 1.00 9.73  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 165.031 192.161 157.731 1.00 8.53  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 165.633 191.198 158.746 1.00 12.78 ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 165.037 190.938 159.796 1.00 18.73 ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 164.566 193.446 158.405 1.00 13.19 ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 165.687 194.224 159.057 1.00 11.79 ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 165.187 195.422 159.822 1.00 11.06 ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 164.397 196.200 159.252 1.00 17.46 ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 165.586 195.594 160.991 1.00 7.47  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 166.815 190.670 158.440 1.00 10.66 ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 167.426 189.613 159.233 1.00 8.21  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 168.853 190.009 159.582 1.00 11.97 ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 169.439 190.903 158.965 1.00 15.11 ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 167.412 188.263 158.486 1.00 8.21  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 165.990 187.784 158.294 1.00 13.78 ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 168.113 188.393 157.149 1.00 8.00  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 169.410 189.337 160.588 1.00 10.92 ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 170.803 189.534 160.952 1.00 5.39  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 171.714 188.438 160.422 1.00 9.57  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 172.925 188.657 160.307 1.00 15.46 ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 170.952 189.633 162.473 1.00 5.50  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 170.562 188.380 163.228 1.00 11.31 ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 171.011 188.414 164.674 1.00 13.79 ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 171.870 189.211 165.049 1.00 12.64 ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 170.431 187.547 165.494 1.00 10.90 ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 171.165 187.271 160.096 1.00 8.21  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 171.945 186.189 159.514 1.00 5.04  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 171.013 185.262 158.747 1.00 8.17  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 169.794 185.283 158.932 1.00 11.60 ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 172.753 185.437 160.586 1.00 6.04  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 171.883 184.752 161.641 1.00 13.42 ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 170.727 184.371 161.364 1.00 19.63 ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 172.374 184.587 162.776 1.00 10.75 ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 171.609 184.458 157.869 1.00 5.53  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 170.872 183.469 157.092 1.00 5.95  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 171.476 182.083 157.271 1.00 9.10  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 171.436 181.257 156.355 1.00 13.46 ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 170.836 183.851 155.613 1.00 3.72  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 169.838 184.939 155.217 1.00 6.87  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 169.973 185.267 153.742 1.00 6.80  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 168.418 184.511 155.544 1.00 7.67  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 172.040 181.813 158.449 1.00 4.75  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 172.734 180.555 158.692 1.00 5.86  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 171.796 179.360 158.767 1.00 6.51  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 172.270 178.222 158.716 1.00 13.46 ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 173.550 180.654 159.981 1.00 7.99  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 172.734 181.012 161.208 1.00 8.13  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 173.632 181.318 162.393 1.00 8.35  ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 174.318 180.065 162.906 1.00 8.17  ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 175.098 180.333 164.145 1.00 8.48  ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 170.487 179.584 158.885 1.00 3.69  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 169.525 178.495 158.928 1.00 5.52  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 168.591 178.457 157.730 1.00 8.17  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 167.918 177.439 157.530 1.00 10.56 ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 168.694 178.566 160.217 1.00 4.53  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 169.505 178.301 161.464 1.00 7.48  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 170.013 177.037 161.727 1.00 8.13  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 169.775 179.314 162.369 1.00 5.59  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 170.759 176.791 162.858 1.00 7.57  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 170.521 179.078 163.504 1.00 3.24  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 171.011 177.813 163.744 1.00 7.22  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 171.756 177.573 164.874 1.00 12.21 ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 168.528 179.520 156.933 1.00 9.04  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 167.741 179.490 155.711 1.00 6.11  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 168.397 178.585 154.677 1.00 5.61  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 169.624 178.472 154.603 1.00 4.77  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 167.576 180.900 155.145 1.00 2.96  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 167.565 177.935 153.870 1.00 4.38  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 168.044 176.998 152.871 1.00 4.00  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 168.262 177.707 151.536 1.00 3.09  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 168.027 178.909 151.394 1.00 4.25  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 167.064 175.835 152.720 1.00 10.33 ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 165.788 176.336 152.308 1.00 12.73 ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 166.909 175.102 154.042 1.00 9.16  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 168.726 176.949 150.540 1.00 6.36  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 168.980 177.523 149.224 1.00 4.27  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 167.695 177.971 148.544 1.00 4.64  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 167.701 178.957 147.797 1.00 6.10  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 169.718 176.513 148.344 1.00 6.65  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 170.113 176.993 146.947 1.00 9.79  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 171.090 178.154 147.042 1.00 6.95  ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 170.700 175.853 146.132 1.00 8.73  ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 166.589 177.263 148.788 1.00 3.07  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 165.323 177.623 148.160 1.00 4.35  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 164.879 179.020 148.572 1.00 4.14  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 164.375 179.788 147.747 1.00 7.07  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 164.251 176.593 148.515 1.00 7.10  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 165.053 179.364 149.849 1.00 4.39  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 164.672 180.693 150.316 1.00 3.02  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 165.622 181.760 149.785 1.00 2.21  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 165.184 182.822 149.329 1.00 8.40  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 164.641 180.720 151.843 1.00 5.75  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 163.950 179.564 152.332 1.00 9.60  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 163.940 181.969 152.331 1.00 4.96  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 166.927 181.495 149.840 1.00 1.82  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 167.914 182.500 149.453 1.00 3.21  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 167.809 182.814 147.966 1.00 6.10  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 167.923 183.974 147.552 1.00 7.99  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 169.329 182.032 149.836 1.00 3.86  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 170.373 183.014 149.331 1.00 5.64  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 169.440 181.866 151.340 1.00 2.23  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 167.484 181.801 147.184 1.00 4.13  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 167.456 181.952 145.715 1.00 2.34  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 166.247 182.750 145.254 1.00 5.53  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 166.383 183.449 144.253 1.00 5.73  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 167.431 180.599 145.120 1.00 0.35  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 166.409 179.807 145.700 1.00 1.95  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 165.132 182.668 145.959 1.00 3.40  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 163.867 183.292 145.525 1.00 1.30  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 163.825 184.787 145.839 1.00 6.18  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 162.854 185.424 145.408 1.00 10.10 ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 162.771 182.550 146.291 1.00 2.63  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 162.447 181.149 145.805 1.00 0.01  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 161.662 180.428 146.872 1.00 1.20  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 160.776 179.404 146.314 1.00 4.27  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 161.167 178.372 145.591 1.00 8.77  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 162.431 178.000 145.607 1.00 12.06 ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 160.290 177.712 144.861 1.00 9.82  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 164.831 185.345 146.520 1.00 6.10  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 164.738 186.759 146.960 1.00 3.05  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 165.963 187.612 146.617 1.00 6.44  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 167.059 187.061 146.618 1.00 12.87 ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 164.670 186.807 148.477 1.00 3.46  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 163.484 185.673 149.237 1.00 16.05 ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 165.790 188.905 146.349 1.00 3.61  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 166.867 189.852 146.149 1.00 3.60  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 167.540 190.114 147.478 1.00 3.15  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 166.878 190.076 148.516 1.00 13.83 ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 168.844 190.364 147.475 1.00 4.07  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 169.611 190.502 148.704 1.00 4.37  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 170.298 191.857 148.733 1.00 7.15  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 170.884 192.280 147.732 1.00 14.97 ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 170.655 189.392 148.831 1.00 3.78  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 170.085 187.995 148.977 1.00 3.90  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 169.691 187.554 150.676 1.00 15.80 ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 168.370 186.378 150.408 1.00 11.05 ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 170.221 192.532 149.876 1.00 5.60  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 170.998 193.735 150.142 1.00 7.88  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 171.777 193.491 151.426 1.00 9.06  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 171.180 193.238 152.479 1.00 14.24 ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 170.116 194.988 150.270 1.00 6.74  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 170.977 196.237 150.306 1.00 6.76  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 169.125 195.057 149.122 1.00 4.71  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 173.101 193.567 151.342 1.00 9.96  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 173.975 193.265 152.466 1.00 6.52  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 174.400 194.562 153.140 1.00 14.86 ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 175.073 195.395 152.527 1.00 17.63 ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 175.199 192.475 152.008 1.00 9.28  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 176.285 192.413 153.035 1.00 15.81 ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 177.445 193.129 153.044 1.00 15.88 ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 176.314 191.586 154.204 1.00 17.32 ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 178.193 192.801 154.148 1.00 13.34 ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 177.520 191.856 154.876 1.00 14.32 ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 175.435 190.646 154.747 1.00 14.99 ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 177.870 191.221 156.062 1.00 13.96 ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 175.785 190.017 155.925 1.00 14.08 ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 176.992 190.306 156.569 1.00 14.44 ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 174.009 194.722 154.400 1.00 15.74 ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 174.438 195.840 155.229 1.00 12.05 ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 175.547 195.352 156.150 1.00 14.34 ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 175.360 194.382 156.888 1.00 20.60 ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 173.279 196.398 156.054 1.00 9.18  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 172.219 197.086 155.243 1.00 7.49  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 171.318 196.356 154.489 1.00 7.71  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 172.113 198.464 155.251 1.00 10.21 ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 170.339 196.989 153.753 1.00 8.14  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 171.137 199.101 154.516 1.00 10.29 ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 170.249 198.363 153.766 1.00 8.94  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 176.693 196.015 156.107 1.00 12.69 ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 177.785 195.708 157.017 1.00 11.78 ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 177.793 196.704 158.168 1.00 17.04 ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 177.165 197.764 158.108 1.00 21.94 ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 179.129 195.732 156.286 1.00 17.37 ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 179.390 197.010 155.735 1.00 20.76 ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 178.508 196.345 159.234 1.00 15.75 ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 178.655 197.272 160.350 1.00 13.73 ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 179.462 198.503 159.962 1.00 13.90 ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 179.387 199.521 160.657 1.00 15.15 ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 179.303 196.566 161.540 1.00 16.66 ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 178.526 195.359 162.028 1.00 17.65 ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 178.578 195.197 163.533 1.00 20.61 ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 178.884 194.081 164.002 1.00 18.37 ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 178.313 196.188 164.247 1.00 22.11 ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 180.227 198.431 158.872 1.00 13.47 ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 180.924 199.598 158.351 1.00 11.86 ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 179.998 200.542 157.601 1.00 12.30 ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 180.353 201.709 157.403 1.00 13.78 ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 182.064 199.159 157.432 1.00 14.35 ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 182.856 197.998 157.999 1.00 20.07 ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 183.418 198.142 159.105 1.00 20.03 ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 182.916 196.939 157.341 1.00 20.04 ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 178.827 200.064 157.174 1.00 12.93 ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 177.866 200.931 156.497 1.00 9.19  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 177.400 202.034 157.436 1.00 10.01 ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 177.340 203.212 157.061 1.00 12.30 ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 176.682 200.102 155.964 1.00 5.59  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 175.490 200.992 155.679 1.00 9.30  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 177.088 199.342 154.715 1.00 13.29 ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 177.075 201.672 158.674 1.00 9.44  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 176.677 202.637 159.691 1.00 8.22  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 177.872 202.897 160.599 1.00 5.46  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 178.162 202.105 161.500 1.00 11.45 ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 175.479 202.123 160.482 1.00 7.98  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 175.073 202.940 161.708 1.00 9.44  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 174.422 204.243 161.285 1.00 15.53 ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 174.144 202.140 162.599 1.00 8.62  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 178.573 204.001 160.356 1.00 2.99  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 179.735 204.348 161.156 1.00 4.15  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 179.306 204.909 162.506 1.00 6.88  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 178.161 205.328 162.695 1.00 9.22  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 180.609 205.362 160.418 1.00 9.43  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 179.919 206.580 160.216 1.00 9.37  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 180.244 204.905 163.453 1.00 10.12 ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 179.942 205.389 164.796 1.00 3.90  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 179.713 206.896 164.807 1.00 4.75  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 178.941 207.403 165.630 1.00 13.15 ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 181.074 205.006 165.750 1.00 6.12  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 181.315 203.596 165.656 1.00 7.69  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 180.699 205.331 167.179 1.00 7.44  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 180.368 207.624 163.898 1.00 3.48  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 180.120 209.059 163.776 1.00 4.30  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 178.661 209.333 163.447 1.00 8.76  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 178.081 210.314 163.924 1.00 12.29 ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 181.025 209.658 162.701 1.00 6.67  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 182.482 209.326 162.915 1.00 18.48 ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 183.028 209.688 163.979 1.00 21.58 ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 183.087 208.702 162.019 1.00 16.14 ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 178.054 208.474 162.628 1.00 7.12  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 176.646 208.626 162.286 1.00 4.27  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 175.764 208.492 163.522 1.00 5.72  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 174.825 209.272 163.714 1.00 11.14 ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 176.271 207.583 161.235 1.00 5.89  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 176.959 207.797 159.898 1.00 6.19  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 176.591 206.517 158.684 1.00 18.15 ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 174.885 206.876 158.316 1.00 13.27 ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 176.064 207.513 164.378 1.00 4.53  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 175.279 207.308 165.593 1.00 1.74  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 175.463 208.480 166.549 1.00 8.16  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 174.510 208.939 167.191 1.00 14.71 ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 175.658 205.973 166.255 1.00 0.00  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 175.644 204.850 165.218 1.00 5.93  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 174.706 205.658 167.391 1.00 7.63  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 176.091 203.516 165.756 1.00 6.99  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 176.698 208.977 166.664 1.00 5.21  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 176.948 210.145 167.506 1.00 1.84  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 176.179 211.359 167.003 1.00 6.26  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 175.597 212.109 167.796 1.00 10.12 ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 178.444 210.446 167.555 1.00 3.12  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 179.245 209.443 168.335 1.00 6.75  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 178.618 208.458 169.078 1.00 5.74  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 180.627 209.486 168.322 1.00 9.03  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 179.355 207.538 169.793 1.00 4.86  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 181.367 208.570 169.034 1.00 9.23  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 180.731 207.596 169.771 1.00 5.25  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 176.170 211.571 165.686 1.00 6.94  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 175.427 212.687 165.111 1.00 2.54  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 173.935 212.541 165.371 1.00 6.89  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 173.250 213.519 165.685 1.00 10.94 ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 175.704 212.786 163.611 1.00 4.12  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 177.130 213.182 163.309 1.00 10.46 ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 177.879 213.577 164.202 1.00 18.18 ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 177.519 213.073 162.046 1.00 7.52  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 173.411 211.321 165.235 1.00 4.70  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 171.996 211.091 165.510 1.00 5.16  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 171.662 211.411 166.962 1.00 8.49  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 170.665 212.084 167.250 1.00 10.03 ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 171.630 209.645 165.175 1.00 3.42  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 170.186 209.319 165.496 1.00 5.19  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 169.904 208.433 166.300 1.00 10.30 ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 169.263 210.034 164.869 1.00 5.80  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 172.502 210.947 167.892 1.00 9.79  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 172.269 211.215 169.307 1.00 3.80  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 172.303 212.709 169.598 1.00 5.62  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 171.438 213.236 170.305 1.00 8.82  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 173.305 210.481 170.157 1.00 2.81  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 173.408 210.995 171.565 1.00 7.61  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 172.316 210.953 172.417 1.00 7.90  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 174.595 211.529 172.037 1.00 7.08  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 172.410 211.428 173.711 1.00 5.82  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 174.692 212.006 173.328 1.00 4.63  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 173.598 211.955 174.165 1.00 4.45  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 173.301 213.411 169.055 1.00 4.59  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 173.430 214.837 169.333 1.00 6.59  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 172.279 215.628 168.718 1.00 9.16  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 171.770 216.574 169.333 1.00 12.88 ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 174.776 215.351 168.827 1.00 6.09  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 175.985 214.882 169.639 1.00 3.22  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 177.272 215.400 169.031 1.00 12.26 ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 175.862 215.321 171.086 1.00 4.31  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 171.854 215.257 167.508 1.00 4.04  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 170.723 215.936 166.884 1.00 6.58  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 169.442 215.716 167.677 1.00 9.24  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 168.667 216.658 167.890 1.00 13.83 ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 170.554 215.456 165.444 1.00 5.26  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 169.204 214.482 168.129 1.00 9.42  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 168.019 214.223 168.941 1.00 7.13  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 168.072 214.991 170.254 1.00 8.69  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 167.049 215.505 170.721 1.00 14.75 ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 167.871 212.726 169.201 1.00 5.50  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 167.541 211.908 167.971 1.00 3.87  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 167.422 210.437 168.320 1.00 4.00  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 166.395 210.210 169.330 1.00 5.43  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 165.097 210.127 169.076 1.00 9.92  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 164.627 210.234 167.844 1.00 10.60 ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 164.250 209.932 170.082 1.00 10.05 ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 169.252 215.070 170.874 1.00 5.69  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 169.377 215.817 172.120 1.00 10.37 ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 169.103 217.299 171.907 1.00 13.63 ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 168.398 217.928 172.703 1.00 16.75 ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 170.767 215.612 172.720 1.00 8.68  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 170.930 216.091 174.163 1.00 7.20  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 169.998 215.326 175.085 1.00 10.63 ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 172.370 215.945 174.609 1.00 8.74  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 169.646 217.872 170.831 1.00 10.91 ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 169.446 219.293 170.567 1.00 7.27  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 168.033 219.608 170.098 1.00 10.38 ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 167.603 220.759 170.206 1.00 14.81 ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 170.448 219.787 169.522 1.00 3.74  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 171.871 219.908 170.027 1.00 9.16  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 172.822 220.247 168.895 1.00 9.80  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 174.132 220.657 169.386 1.00 13.39 ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 175.271 220.059 169.068 1.00 16.26 ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 175.299 219.014 168.258 1.00 12.50 ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 176.409 220.523 169.572 1.00 14.06 ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 167.302 218.619 169.582 1.00 11.69 ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 165.975 218.861 169.030 1.00 10.79 ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 164.850 218.435 169.965 1.00 13.70 ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 163.966 219.239 170.274 1.00 18.10 ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 165.833 218.138 167.687 1.00 10.87 ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 166.791 218.605 166.754 1.00 12.63 ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 164.859 217.187 170.419 1.00 13.14 ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 163.747 216.618 171.176 1.00 14.00 ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 163.944 216.962 172.650 1.00 15.63 ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 164.962 216.561 173.233 1.00 15.64 ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 163.654 215.102 170.978 1.00 10.56 ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 163.573 214.765 169.488 1.00 10.44 ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 162.452 214.542 171.719 1.00 12.47 ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 163.558 213.285 169.201 1.00 10.80 ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 163.020 217.689 173.275 1.00 18.85 ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 163.118 217.913 174.721 1.00 19.01 ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 162.913 216.620 175.493 1.00 20.56 ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 162.153 215.738 175.086 1.00 23.22 ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 161.995 218.919 175.008 1.00 19.89 ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 161.568 219.442 173.668 1.00 22.45 ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 161.840 218.345 172.694 1.00 20.28 ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 163.604 216.517 176.629 1.00 19.49 ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 163.512 215.309 177.441 1.00 20.37 ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 162.219 215.252 178.245 1.00 25.82 ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 161.690 214.159 178.474 1.00 24.31 ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 164.717 215.209 178.376 1.00 18.40 ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 166.009 214.708 177.728 1.00 17.84 ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 167.124 214.618 178.752 1.00 20.04 ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 165.783 213.366 177.057 1.00 17.98 ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 161.703 216.401 178.688 1.00 31.38 ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 160.469 216.405 179.467 1.00 30.47 ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 159.283 215.925 178.638 1.00 30.46 ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 158.436 215.176 179.136 1.00 32.36 ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 160.214 217.800 180.040 1.00 31.68 ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 160.071 218.866 178.965 1.00 36.93 ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 160.218 218.546 177.768 1.00 36.89 ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 159.810 220.033 179.325 1.00 38.23 ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 159.208 216.339 177.379 1.00 31.95 ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 158.140 215.904 176.485 1.00 33.49 ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 158.538 216.091 175.025 1.00 30.75 ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 159.194 217.069 174.668 0.00 32.68 ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 156.845 216.663 176.779 1.00 36.25 ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 155.640 216.172 175.987 1.00 37.29 ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 155.108 214.843 176.486 1.00 37.74 ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 155.698 213.797 176.148 1.00 36.25 ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 154.096 214.846 177.219 1.00 36.07 ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 162.167 226.495 176.065 1.00 30.66 ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 162.093 225.433 177.060 1.00 33.05 ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 163.411 225.302 177.815 1.00 31.69 ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 164.459 225.099 177.202 1.00 29.82 ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 161.729 224.103 176.400 1.00 29.41 ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 161.466 223.106 177.371 1.00 28.17 ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 163.360 225.433 179.143 1.00 32.37 ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 164.594 225.282 179.935 1.00 32.18 ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 165.247 223.923 179.767 1.00 33.15 ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 166.482 223.831 179.721 1.00 34.26 ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 164.113 225.515 181.374 1.00 32.55 ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 162.649 225.217 181.342 1.00 30.85 ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 162.177 225.652 179.991 1.00 30.67 ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 164.448 222.858 179.665 1.00 28.90 ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 165.007 221.532 179.435 1.00 25.16 ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 165.701 221.457 178.081 1.00 23.96 ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 166.775 220.858 177.957 1.00 23.81 ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 163.905 220.477 179.543 1.00 24.86 ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 164.375 219.043 179.348 1.00 27.79 ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 165.007 218.263 180.847 1.00 36.35 ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 166.755 218.630 180.716 1.00 23.78 ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 165.100 222.065 177.055 1.00 25.16 ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 165.730 222.081 175.738 1.00 24.86 ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 167.040 222.857 175.761 1.00 22.77 ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 168.023 222.444 175.139 1.00 26.52 ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 164.772 222.671 174.705 1.00 25.86 ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 164.982 222.202 173.264 1.00 23.11 ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 165.163 220.696 173.213 1.00 20.83 ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 163.821 222.635 172.388 1.00 23.67 ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 167.073 223.988 176.471 1.00 21.60 ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 168.310 224.757 176.573 1.00 21.80 ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 169.388 223.968 177.307 1.00 23.42 ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 170.565 224.001 176.922 1.00 23.43 ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 168.045 226.088 177.275 1.00 22.37 ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 169.196 227.074 177.178 1.00 22.80 ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 169.670 227.274 175.753 1.00 26.90 ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 168.891 227.631 174.871 1.00 28.56 ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 170.957 227.041 175.522 1.00 23.99 ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 169.005 223.255 178.368 1.00 22.15 ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 169.960 222.420 179.090 1.00 23.09 ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 170.506 221.329 178.178 1.00 24.16 ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 171.712 221.050 178.168 1.00 23.92 ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 169.302 221.832 180.352 1.00 22.26 ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 169.095 222.926 181.399 1.00 24.28 ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 170.143 220.702 180.918 1.00 21.46 ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 168.193 222.516 182.536 1.00 24.11 ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 169.627 220.700 177.394 1.00 21.97 ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 170.070 219.668 176.462 1.00 14.44 ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 171.020 220.238 175.417 1.00 16.24 ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 172.021 219.603 175.070 1.00 17.26 ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 168.867 219.019 175.782 1.00 11.91 ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 168.064 218.098 176.669 1.00 11.43 ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 166.730 217.740 176.056 1.00 18.86 ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 165.690 217.847 176.699 1.00 25.02 ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 166.753 217.316 174.799 1.00 17.79 ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 170.718 221.428 174.896 1.00 19.63 ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 171.584 222.038 173.893 1.00 17.54 ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 172.955 222.366 174.470 1.00 20.53 ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 173.982 222.127 173.824 1.00 22.93 ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 170.922 223.293 173.324 1.00 15.09 ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 169.647 223.014 172.551 1.00 16.80 ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 169.340 224.113 171.553 1.00 17.97 ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 168.214 223.763 170.698 1.00 22.21 ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 167.051 224.400 170.691 1.00 21.66 ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 166.826 225.435 171.482 1.00 22.48 ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 166.089 223.986 169.871 1.00 19.29 ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 172.993 222.909 175.688 1.00 16.54 ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 174.276 223.207 176.318 1.00 13.91 ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 175.071 221.932 176.581 1.00 20.13 ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 176.288 221.890 176.356 1.00 20.73 ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 174.056 223.986 177.614 1.00 18.97 ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 173.505 225.376 177.368 1.00 27.05 ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 173.092 225.657 176.223 1.00 28.09 ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 173.489 226.190 178.315 1.00 27.67 ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 174.399 220.876 177.045 1.00 19.77 ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 175.087 219.611 177.286 1.00 12.56 ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 175.619 219.014 175.988 1.00 17.18 ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 176.719 218.455 175.960 1.00 18.91 ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 174.150 218.629 177.985 1.00 10.67 ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 174.846 219.117 174.905 1.00 17.99 ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 175.302 218.620 173.612 1.00 13.18 ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 176.502 219.413 173.110 1.00 13.36 ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 177.420 218.845 172.508 1.00 14.41 ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 174.162 218.669 172.597 1.00 11.55 ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 176.503 220.728 173.335 1.00 17.88 ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 177.668 221.534 172.986 1.00 15.58 ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 178.891 221.102 173.784 1.00 14.67 ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 180.004 221.041 173.248 1.00 11.35 ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 177.373 223.016 173.218 1.00 16.13 ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 176.215 223.396 172.468 1.00 19.00 ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 178.552 223.868 172.781 1.00 15.26 ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 178.706 220.800 175.070 1.00 17.08 ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 179.838 220.403 175.903 1.00 17.82 ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 180.366 219.032 175.489 1.00 18.96 ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 181.580 218.802 175.469 1.00 18.54 ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 179.446 220.442 177.392 1.00 14.55 ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 179.099 221.872 177.805 1.00 16.50 ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 180.576 219.917 178.259 1.00 15.16 ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 178.265 221.955 179.055 1.00 18.99 ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 179.471 218.102 175.146 1.00 17.03 ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 179.888 216.753 174.774 1.00 12.82 ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 180.381 216.646 173.339 1.00 14.79 ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 180.840 215.570 172.943 1.00 16.26 ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 178.747 215.754 174.975 1.00 12.63 ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 178.327 215.556 176.417 1.00 15.59 ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 176.814 214.591 176.566 1.00 23.11 ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 175.850 215.283 175.233 1.00 10.64 ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 180.287 217.718 172.554 1.00 15.77 ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 180.684 217.650 171.149 1.00 12.62 ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 182.133 217.218 170.945 1.00 16.78 ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 182.372 216.354 170.087 1.00 17.81 ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 180.405 218.995 170.472 1.00 13.68 ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 180.524 218.959 168.959 1.00 13.33 ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 179.410 218.168 168.302 1.00 14.00 ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 178.235 218.521 168.408 1.00 11.57 ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 179.775 217.093 167.614 1.00 17.84 ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 183.131 217.758 171.659 1.00 13.26 ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 184.516 217.332 171.391 1.00 11.58 ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 184.757 215.846 171.577 1.00 14.54 ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 185.555 215.262 170.831 1.00 15.38 ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 185.334 218.159 172.391 1.00 13.14 ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 184.506 219.351 172.653 1.00 13.67 ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 183.092 218.865 172.631 1.00 13.70 ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 184.098 215.211 172.545 1.00 14.77 ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 184.327 213.795 172.803 1.00 13.82 ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 183.568 212.887 171.847 1.00 14.92 ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 183.983 211.740 171.644 1.00 17.66 ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 183.950 213.464 174.247 1.00 11.67 ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 184.491 214.460 175.248 1.00 10.04 ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 185.823 214.427 175.633 1.00 12.08 ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 183.675 215.437 175.797 1.00 10.90 ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 186.326 215.335 176.541 1.00 13.04 ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 184.168 216.350 176.706 1.00 12.91 ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 185.493 216.293 177.075 1.00 15.04 ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 185.991 217.199 177.981 1.00 19.18 ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 182.476 213.362 171.261 1.00 14.64 ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 181.707 212.579 170.294 1.00 11.68 ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 182.149 212.906 168.870 1.00 16.89 ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 181.376 213.376 168.035 1.00 21.69 ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 180.215 212.826 170.484 1.00 11.50 ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 179.627 212.103 171.657 1.00 9.14  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 179.419 210.737 171.612 1.00 10.77 ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 179.286 212.789 172.809 1.00 9.54  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 178.879 210.069 172.689 1.00 8.76  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 178.746 212.126 173.887 1.00 9.91  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 178.543 210.764 173.828 1.00 10.63 ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 183.428 212.652 168.603 1.00 16.43 ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 184.028 212.890 167.300 1.00 16.93 ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 184.759 211.637 166.844 1.00 19.25 ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 184.894 210.662 167.585 1.00 22.81 ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 185.002 214.077 167.328 1.00 17.44 ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 186.056 213.813 168.263 1.00 13.47 ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 184.285 215.356 167.721 1.00 15.88 ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 185.226 211.670 165.599 1.00 25.42 ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 186.063 210.594 165.088 1.00 24.85 ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 187.381 210.565 165.849 1.00 26.95 ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 188.004 211.609 166.068 1.00 28.69 ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 186.317 210.782 163.593 1.00 25.87 ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 185.102 210.826 162.870 1.00 26.97 ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 187.804 209.366 166.248 1.00 28.86 ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 189.014 209.182 167.049 1.00 29.28 ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 188.942 210.035 168.317 1.00 30.52 ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 189.909 210.683 168.720 1.00 32.40 ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 190.266 209.499 166.222 1.00 30.93 ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 191.560 209.121 166.927 1.00 37.78 ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 191.552 208.635 168.059 1.00 39.30 ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 192.682 209.348 166.256 1.00 33.47 ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 187.761 210.056 168.936 1.00 24.60 ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 187.540 210.793 170.159 1.00 20.32 ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 187.642 209.912 171.390 1.00 19.91 ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 188.034 208.745 171.332 1.00 22.51 ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 187.277 210.496 172.533 1.00 16.95 ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 187.327 209.752 173.789 1.00 13.64 ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 186.377 208.563 173.759 1.00 12.89 ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 186.747 207.447 174.144 1.00 15.82 ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 186.992 210.676 174.959 1.00 11.59 ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 186.749 209.980 176.301 1.00 14.66 ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 188.058 209.498 176.902 1.00 16.27 ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 186.016 210.897 177.268 1.00 11.17 ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 185.147 208.778 173.287 1.00 11.98 ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 184.157 207.706 173.280 1.00 11.97 ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 184.556 206.611 172.298 1.00 15.54 ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 184.422 205.419 172.594 1.00 18.42 ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 182.761 208.269 172.964 1.00 7.66  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 181.713 207.182 173.114 1.00 5.83  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 182.449 209.444 173.871 1.00 8.74  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 185.052 206.991 171.118 1.00 13.56 ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 185.418 205.997 170.114 1.00 13.43 ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 186.596 205.148 170.577 1.00 16.07 ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 186.571 203.917 170.460 1.00 18.16 ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 185.739 206.685 168.788 1.00 15.12 ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 184.628 207.494 168.386 1.00 16.21 ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 186.022 205.653 167.710 1.00 15.74 ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 187.641 205.790 171.106 1.00 13.98 ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 188.790 205.044 171.607 1.00 12.20 ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 188.404 204.175 172.796 1.00 17.12 ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 188.877 203.039 172.925 1.00 18.92 ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 189.919 206.003 171.981 1.00 13.79 ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 190.434 206.836 170.820 1.00 18.95 ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 191.431 207.885 171.282 1.00 17.62 ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 192.593 207.255 172.026 1.00 20.71 ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 193.629 208.262 172.382 1.00 20.93 ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 187.547 204.693 173.678 1.00 18.35 ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 187.093 203.905 174.817 1.00 9.97  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 186.313 202.679 174.366 1.00 11.36 ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 186.492 201.588 174.915 1.00 19.08 ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 186.249 204.772 175.750 1.00 9.33  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 185.440 202.837 173.368 1.00 8.95  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 184.689 201.700 172.846 1.00 10.43 ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 185.612 200.684 172.185 1.00 13.05 ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 185.443 199.470 172.363 1.00 15.18 ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 183.628 202.189 171.860 1.00 9.37  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 182.620 201.169 171.326 1.00 12.94 ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 181.601 200.807 172.389 1.00 12.16 ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 181.928 201.716 170.091 1.00 12.72 ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 186.599 201.162 171.423 1.00 15.08 ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 187.552 200.257 170.792 1.00 15.65 ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 188.331 199.465 171.833 1.00 17.05 ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 188.553 198.260 171.668 1.00 17.76 ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 188.505 201.046 169.892 1.00 15.38 ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 189.137 200.224 168.785 1.00 16.69 ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 189.538 201.067 167.593 1.00 23.62 ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 190.032 202.195 167.800 1.00 20.45 ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 189.361 200.603 166.446 1.00 27.09 ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 188.758 200.126 172.910 1.00 15.53 ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 189.462 199.421 173.976 1.00 16.90 ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 188.546 198.435 174.692 1.00 17.68 ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 188.954 197.309 174.995 1.00 20.28 ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 190.049 200.422 174.969 1.00 14.28 ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 190.811 199.782 176.087 1.00 15.88 ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 192.085 199.280 175.928 1.00 17.08 ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 190.478 199.557 177.378 1.00 17.82 ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 192.504 198.778 177.074 1.00 18.53 ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 191.548 198.932 177.971 1.00 19.65 ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 187.305 198.842 174.974 1.00 13.72 ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 186.378 197.981 175.698 1.00 10.40 ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 186.007 196.744 174.894 1.00 11.32 ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 185.704 195.698 175.475 1.00 17.13 ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 185.122 198.761 176.075 1.00 8.82  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 186.017 196.843 173.562 1.00 13.27 ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 185.753 195.664 172.745 1.00 11.97 ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 186.815 194.587 172.924 1.00 13.60 ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 186.572 193.428 172.569 1.00 13.55 ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 185.647 196.054 171.271 1.00 14.01 ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 184.234 196.231 170.794 1.00 18.90 ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 183.496 197.340 171.164 1.00 16.26 ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 183.643 195.281 169.979 1.00 17.37 ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 182.199 197.502 170.727 1.00 12.22 ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 182.345 195.438 169.540 1.00 14.65 ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 181.622 196.550 169.915 1.00 13.61 ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 187.982 194.939 173.463 1.00 18.73 ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 189.050 193.980 173.701 1.00 17.29 ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 188.988 193.339 175.082 1.00 16.97 ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 189.744 192.398 175.344 1.00 20.11 ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 190.414 194.656 173.522 1.00 16.89 ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 190.512 195.536 172.289 1.00 20.14 ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 191.877 196.175 172.139 1.00 24.62 ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 192.816 195.833 172.858 1.00 25.70 ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 191.994 197.110 171.203 1.00 21.62 ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 188.117 193.818 175.965 1.00 18.06 ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 187.995 193.254 177.299 1.00 13.30 ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 187.091 192.024 177.271 1.00 15.17 ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 186.634 191.574 176.218 1.00 19.10 ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 187.462 194.301 178.274 1.00 12.59 ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 188.206 195.636 178.335 1.00 17.11 ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 187.511 196.586 179.296 1.00 16.09 ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 189.652 195.425 178.742 1.00 17.14 ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 186.828 191.469 178.451 1.00 10.12 ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 185.959 190.311 178.601 1.00 13.00 ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 184.716 190.712 179.379 1.00 13.84 ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 184.817 191.243 180.491 1.00 12.85 ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 186.685 189.167 179.311 1.00 14.93 ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 185.859 187.896 179.430 1.00 17.55 ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 186.621 186.767 180.091 1.00 22.33 ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 187.789 186.984 180.477 1.00 22.35 ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 186.052 185.665 180.226 1.00 24.71 ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 183.549 190.452 178.799 1.00 13.04 ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 182.274 190.825 179.387 1.00 7.46  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 181.431 189.581 179.627 1.00 7.50  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 181.591 188.556 178.959 1.00 8.94  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 181.519 191.812 178.487 1.00 3.95  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 182.364 192.941 177.988 1.00 6.97  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 182.417 194.166 178.617 1.00 8.30  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 183.194 193.029 176.923 1.00 7.14  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 183.243 194.960 177.960 1.00 8.19  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 183.727 194.294 176.928 1.00 8.84  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 180.522 189.684 180.601 1.00 6.24  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 179.650 188.562 180.924 1.00 3.44  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 178.700 188.244 179.776 1.00 6.46  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 178.177 187.127 179.699 1.00 9.67  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 178.873 188.844 182.224 1.00 2.92  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 178.460 187.531 182.890 1.00 5.74  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 177.664 189.725 181.957 1.00 2.88  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 179.625 186.629 183.222 1.00 9.21  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 178.468 189.199 178.879 1.00 6.53  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 177.663 188.992 177.686 1.00 2.46  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 178.422 189.525 176.482 1.00 5.96  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 179.317 190.364 176.611 1.00 9.63  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 176.298 189.678 177.795 1.00 3.41  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 175.376 189.059 178.823 1.00 7.13  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 173.667 189.042 178.263 1.00 19.12 ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 172.893 188.140 179.595 1.00 7.54  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 178.063 189.018 175.305 1.00 4.75  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 178.702 189.468 174.076 1.00 3.20  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 178.511 190.968 173.904 1.00 4.75  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 177.396 191.483 174.025 1.00 9.74  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 178.126 188.719 172.877 1.00 4.68  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 178.857 187.423 172.595 1.00 11.75 ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 180.105 187.440 172.560 1.00 16.00 ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 178.182 186.389 172.407 1.00 10.30 ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 179.604 191.671 173.620 1.00 3.71  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 179.577 193.123 173.529 1.00 4.77  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 179.229 193.558 172.114 1.00 9.03  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 179.857 193.118 171.146 1.00 11.37 ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 180.918 193.725 173.942 1.00 7.90  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 180.809 195.181 174.398 1.00 7.63  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 180.138 195.255 175.757 1.00 9.13  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 182.165 195.863 174.421 1.00 6.15  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 178.227 194.423 172.002 1.00 6.03  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 177.856 195.046 170.745 1.00 5.98  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 177.957 196.556 170.894 1.00 5.57  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 177.825 197.097 171.995 1.00 7.11  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 176.439 194.650 170.314 1.00 8.57  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 175.548 194.752 171.431 1.00 13.44 ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 176.424 193.223 169.789 1.00 4.64  ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 178.210 197.231 169.772 1.00 3.57  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 178.404 198.676 169.801 1.00 6.32  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 177.148 199.395 170.279 1.00 5.74  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 177.219 200.315 171.103 1.00 6.97  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 178.806 199.168 168.411 1.00 3.96  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 178.823 200.676 168.261 1.00 5.61  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 179.203 201.065 166.845 1.00 10.09 ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 178.294 200.477 165.870 1.00 11.68 ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 178.373 200.662 164.561 1.00 10.36 ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 179.314 201.423 164.026 1.00 7.65  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 177.485 200.070 163.766 1.00 8.35  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 175.983 198.976 169.783 1.00 5.90  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 174.768 199.739 170.036 1.00 4.44  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 174.266 199.547 171.460 1.00 5.56  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 173.625 200.438 172.019 1.00 7.90  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 173.688 199.377 169.021 1.00 4.23  ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 173.794 200.200 167.739 1.00 3.26  ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 172.598 199.956 166.863 1.00 12.97 ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 173.916 201.676 168.068 1.00 2.25  ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 174.555 198.399 172.074 1.00 4.66  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 174.208 198.228 173.481 1.00 2.70  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 174.923 199.261 174.344 1.00 8.49  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 174.300 199.978 175.140 1.00 13.44 ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 174.552 196.811 173.944 1.00 0.00  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 174.265 196.571 175.415 1.00 0.66  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 174.253 195.097 175.767 1.00 1.81  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 175.523 194.445 175.479 1.00 8.12  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 176.288 193.863 176.392 1.00 8.53  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 175.960 193.867 177.672 1.00 10.69 ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 177.412 193.264 176.012 1.00 7.92  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 176.243 199.366 174.166 1.00 4.38  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 177.027 200.343 174.910 1.00 0.00  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 176.597 201.765 174.580 1.00 3.03  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 176.496 202.611 175.475 1.00 8.37  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 178.511 200.155 174.606 1.00 1.44  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 179.141 198.511 174.972 1.00 19.11 ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 176.351 202.049 173.300 1.00 3.19  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 175.978 203.406 172.916 1.00 1.92  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 174.618 203.793 173.483 1.00 2.54  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 174.435 204.924 173.939 1.00 11.98 ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 176.002 203.548 171.395 1.00 5.42  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 177.400 203.510 170.776 1.00 5.38  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 177.383 204.053 169.357 1.00 5.66  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 178.395 204.276 171.636 1.00 0.24  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 173.653 202.871 173.472 1.00 0.00  ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 172.364 203.158 174.079 1.00 0.48  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 172.464 203.359 175.576 1.00 8.80  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 171.806 204.237 176.138 1.00 12.56 ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 173.295 202.551 176.242 1.00 7.38  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 173.533 202.756 177.667 1.00 1.67  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 174.088 204.151 177.928 1.00 3.51  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 173.607 204.876 178.808 1.00 7.98  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 174.505 201.697 178.182 1.00 1.79  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 173.953 200.401 178.074 1.00 1.82  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 175.096 204.546 177.148 1.00 0.83  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 175.723 205.848 177.331 1.00 1.73  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 174.740 206.981 177.060 1.00 5.91  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 174.715 207.977 177.791 1.00 11.43 ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 176.946 205.962 176.420 1.00 2.83  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 177.684 207.295 176.351 1.00 4.75  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 178.411 207.573 177.648 1.00 5.61  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 178.658 207.288 175.191 1.00 6.51  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 173.925 206.848 176.012 1.00 1.71  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 172.967 207.898 175.682 1.00 2.67  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 171.899 208.028 176.757 1.00 8.29  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 171.496 209.144 177.108 1.00 11.99 ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 172.333 207.623 174.318 1.00 0.79  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 173.323 207.560 173.186 1.00 3.34  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 174.563 208.168 173.294 1.00 2.33  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 173.014 206.894 172.015 1.00 5.05  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 175.473 208.109 172.258 1.00 1.77  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 173.919 206.832 170.976 1.00 2.15  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 175.150 207.441 171.098 1.00 2.98  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 171.427 206.901 177.299 1.00 5.69  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 170.469 206.960 178.397 1.00 4.31  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 171.081 207.628 179.621 1.00 6.70  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 170.427 208.437 180.292 1.00 9.46  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 169.977 205.556 178.740 1.00 4.12  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 169.394 204.934 177.609 1.00 7.97  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 172.342 207.313 179.925 1.00 2.88  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 172.985 207.934 181.077 1.00 1.66  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 173.185 209.432 180.865 1.00 5.14  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 173.055 210.219 181.808 1.00 10.26 ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 174.310 207.237 181.376 1.00 4.00  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 174.143 205.776 181.766 1.00 2.98  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 175.676 204.973 182.258 1.00 7.28  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 175.947 205.732 183.854 1.00 5.01  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 173.483 209.853 179.635 1.00 5.12  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 173.632 211.284 179.372 1.00 4.59  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 172.291 212.007 179.444 1.00 7.07  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 172.217 213.154 179.908 1.00 12.07 ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 174.298 211.504 178.016 1.00 1.69  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 175.724 210.962 177.927 1.00 2.97  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 176.203 210.925 176.487 1.00 5.64  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 176.668 211.774 178.797 1.00 4.11  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 171.217 211.354 178.996 1.00 3.98  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 169.884 211.911 179.200 1.00 4.45  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 169.584 212.061 180.686 1.00 8.11  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 168.993 213.061 181.115 1.00 10.88 ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 168.834 211.027 178.530 1.00 4.59  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 168.871 211.070 177.035 1.00 8.05  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 168.186 210.172 176.247 1.00 8.40  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 169.511 211.905 176.184 1.00 9.92  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 168.401 210.450 174.975 1.00 10.52 ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 169.203 211.499 174.908 1.00 13.62 ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 169.987 211.072 181.485 1.00 10.10 ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 169.818 211.178 182.932 1.00 8.11  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 170.632 212.333 183.498 1.00 10.51 ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 170.199 212.998 184.442 1.00 21.01 ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 170.209 209.866 183.607 1.00 5.64  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 169.798 209.788 185.067 1.00 8.44  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 168.335 210.123 185.278 1.00 13.21 ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 167.458 209.577 184.609 1.00 11.77 ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 168.065 211.023 186.214 1.00 11.82 ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 171.825 212.575 182.951 1.00 4.78  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 172.622 213.718 183.391 1.00 4.55  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 171.914 215.035 183.093 1.00 12.33 ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 171.900 215.949 183.929 1.00 18.71 ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 173.994 213.693 182.721 1.00 5.25  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 171.328 215.152 181.901 1.00 15.09 ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 170.572 216.358 181.570 1.00 13.22 ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 169.377 216.528 182.502 1.00 14.07 ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 169.076 217.643 182.951 1.00 18.38 ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 170.119 216.313 180.112 1.00 9.88  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 171.462 216.366 178.910 1.00 19.07 ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 168.684 215.429 182.808 1.00 10.70 ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 167.564 215.497 183.741 1.00 13.34 ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 168.028 215.885 185.139 1.00 15.29 ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 167.321 216.598 185.856 1.00 20.65 ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 166.822 214.161 183.769 1.00 11.01 ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 166.053 213.862 182.497 1.00 14.86 ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 165.373 212.507 182.568 1.00 14.15 ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 164.355 212.352 181.538 1.00 17.66 ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 163.160 212.928 181.569 1.00 21.95 ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 162.790 213.699 182.579 1.00 15.97 ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 162.314 212.720 180.565 1.00 18.73 ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 169.210 215.417 185.547 1.00 10.64 ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 169.768 215.817 186.834 1.00 11.90 ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 170.059 217.309 186.865 1.00 15.92 ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 169.818 217.977 187.877 1.00 18.60 ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 171.042 215.024 187.126 1.00 10.16 ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 170.769 213.563 187.396 1.00 13.86 ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 169.616 213.139 187.471 1.00 17.92 ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 171.830 212.781 187.544 1.00 14.73 ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 170.595 217.848 185.767 1.00 17.90 ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 170.842 219.287 185.695 1.00 20.46 ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 169.529 220.055 185.792 1.00 20.35 ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 169.437 221.077 186.488 1.00 22.28 ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 171.615 219.635 184.410 1.00 20.76 ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 171.707 221.143 184.237 1.00 20.61 ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 173.000 219.014 184.444 1.00 16.64 ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 168.492 219.577 185.102 1.00 19.23 ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 167.185 220.225 185.185 1.00 17.88 ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 166.627 220.172 186.604 1.00 21.35 ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 166.050 221.151 187.091 1.00 24.05 ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 166.212 219.576 184.204 1.00 17.69 ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 166.783 219.033 187.278 1.00 24.34 ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 166.304 218.904 188.651 1.00 24.68 ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 167.057 219.844 189.586 1.00 24.47 ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 166.459 220.451 190.482 1.00 28.49 ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 166.437 217.453 189.113 1.00 23.12 ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 166.660 217.278 190.606 1.00 24.47 ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 166.945 215.838 190.982 1.00 29.82 ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 166.117 214.953 190.768 1.00 29.61 ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 168.125 215.594 191.543 1.00 27.01 ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 168.372 219.972 189.395 1.00 24.78 ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 169.147 220.916 190.192 1.00 24.19 ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 168.685 222.347 189.953 1.00 25.23 ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 168.598 223.144 190.894 1.00 29.67 ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 170.636 220.775 189.877 1.00 26.48 ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 171.515 221.789 190.572 1.00 26.76 ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 172.025 221.544 191.840 1.00 29.01 ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 171.852 222.987 189.953 1.00 29.13 ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 172.831 222.466 192.475 1.00 30.17 ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 172.658 223.913 190.582 1.00 28.82 ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 173.145 223.648 191.841 1.00 28.96 ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 173.949 224.569 192.470 1.00 30.01 ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 168.398 222.695 188.696 1.00 29.09 ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 167.883 224.029 188.403 1.00 29.69 ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 166.538 224.259 189.083 1.00 32.61 ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 166.275 225.349 189.604 1.00 32.05 ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 167.763 224.227 186.893 1.00 28.34 ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 169.029 224.784 186.278 1.00 33.69 ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 170.032 224.978 186.964 1.00 33.47 ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 168.988 225.048 184.979 1.00 34.65 ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 165.672 223.244 189.077 1.00 33.20 ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 164.377 223.369 189.742 1.00 31.46 ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 164.539 223.532 191.248 1.00 33.04 ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 163.803 224.299 191.880 1.00 33.78 ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 163.504 222.156 189.423 1.00 30.06 ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 165.494 222.813 191.843 1.00 33.16 ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 165.710 222.899 193.283 1.00 33.66 ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 166.345 224.219 193.701 1.00 34.38 ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 166.281 224.576 194.881 1.00 35.75 ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 166.581 221.735 193.756 1.00 31.60 ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 165.822 220.425 193.811 1.00 35.75 ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 164.594 220.409 193.915 1.00 34.77 ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 166.548 219.315 193.740 1.00 34.13 ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 166.958 224.944 192.768 1.00 36.71 ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 167.597 226.230 193.046 1.00 36.62 ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 167.072 227.260 192.053 1.00 39.12 ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 167.778 227.655 191.117 1.00 41.61 ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 169.121 226.123 192.962 1.00 36.88 ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 169.718 225.154 193.934 1.00 38.40 ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 169.407 223.811 193.937 1.00 37.19 ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 170.619 225.332 194.929 1.00 39.49 ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 170.085 223.206 194.896 1.00 36.91 ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 170.828 224.107 195.513 1.00 39.15 ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 165.824 227.707 192.222 1.00 42.05 ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 165.262 228.670 191.259 1.00 44.10 ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 166.031 229.978 191.189 1.00 44.88 ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 166.142 230.569 190.106 1.00 43.28 ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 163.828 228.880 191.772 1.00 43.89 ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 163.557 227.717 192.677 1.00 40.65 ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 164.874 227.387 193.298 1.00 40.52 ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 166.567 230.449 192.315 1.00 50.78 ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 167.268 231.730 192.319 1.00 51.86 ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 168.625 231.626 191.634 1.00 51.14 ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 169.012 232.518 190.873 1.00 49.48 ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 167.425 232.236 193.752 1.00 51.29 ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 167.868 233.685 193.811 1.00 54.21 ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 167.131 234.553 193.300 1.00 54.23 ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 168.951 233.956 194.371 1.00 52.65 ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 169.361 230.544 191.891 1.00 52.09 ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 170.712 230.356 191.365 1.00 53.48 ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 170.763 229.062 190.562 1.00 53.56 ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 170.994 227.980 191.124 1.00 52.23 ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 171.740 230.339 192.494 1.00 54.08 ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 171.958 231.679 193.135 1.00 55.41 ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 172.252 232.791 192.363 1.00 53.52 ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 171.868 231.827 194.508 1.00 53.32 ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 172.453 234.025 192.951 1.00 52.61 ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 172.066 233.059 195.101 1.00 53.11 ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 172.360 234.159 194.321 1.00 53.91 ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 170.557 229.123 189.251 1.00 47.31 ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 170.653 227.918 188.425 1.00 43.56 ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 172.103 227.614 188.069 1.00 45.03 ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 173.025 228.367 188.381 1.00 45.37 ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 169.833 228.268 187.177 1.00 41.76 ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 169.660 229.769 187.199 1.00 42.19 ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 170.281 230.324 188.449 1.00 45.17 ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 172.287 226.475 187.406 1.00 40.07 ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 173.620 226.052 187.002 1.00 40.21 ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 174.206 227.020 185.982 1.00 40.60 ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 173.521 227.461 185.054 1.00 39.46 ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 173.574 224.641 186.416 1.00 37.85 ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 174.908 223.917 186.436 1.00 38.79 ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 174.720 222.125 186.390 1.00 47.37 ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 174.708 221.743 188.137 1.00 38.75 ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 175.481 227.350 186.158 1.00 41.93 ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 176.190 228.233 185.247 1.00 42.92 ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 176.953 227.410 184.211 1.00 43.60 ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 176.881 226.180 184.177 1.00 47.23 ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 177.121 229.167 186.021 1.00 44.52 ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 176.391 230.258 186.786 1.00 45.83 ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 175.523 231.115 185.885 1.00 46.52 ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 175.933 231.498 184.789 1.00 46.04 ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 174.313 231.420 186.342 1.00 43.81 ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 177.694 228.109 183.349 1.00 40.71 ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 178.358 227.445 182.230 1.00 41.18 ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 179.488 226.549 182.723 1.00 41.93 ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 179.591 225.385 182.323 1.00 41.65 ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 178.862 228.482 181.213 1.00 43.90 ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 177.678 229.139 180.500 1.00 42.69 ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 179.792 227.832 180.202 1.00 41.00 ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 176.820 228.158 179.732 1.00 40.68 ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 180.353 227.072 183.597 1.00 40.53 ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 181.513 226.296 184.030 1.00 39.86 ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 181.102 225.084 184.860 1.00 41.32 ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 181.666 223.992 184.698 1.00 38.95 ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 182.487 227.191 184.802 1.00 38.65 ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 181.963 227.736 186.121 1.00 40.67 ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 182.947 228.664 186.801 1.00 44.51 ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 184.035 228.901 186.233 1.00 44.81 ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 182.634 229.159 187.903 1.00 43.88 ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 180.118 225.252 185.747 1.00 40.53 ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 179.630 224.124 186.532 1.00 37.71 ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 179.020 223.061 185.632 1.00 36.47 ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 179.252 221.860 185.827 1.00 41.50 ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 178.610 224.607 187.562 1.00 36.25 ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 178.261 223.584 188.626 1.00 36.71 ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 177.539 224.201 189.808 1.00 38.72 ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 176.465 223.748 190.200 1.00 38.96 ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 178.126 225.244 190.381 1.00 37.73 ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 178.240 223.487 184.636 1.00 28.41 ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 177.649 222.539 183.702 1.00 27.12 ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 178.723 221.799 182.915 1.00 28.90 ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 178.623 220.587 182.712 1.00 31.38 ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 176.689 223.261 182.757 1.00 26.57 ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 175.870 222.389 181.806 1.00 25.39 ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 175.231 221.237 182.554 1.00 28.10 ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 174.812 223.218 181.103 1.00 27.00 ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 179.761 222.512 182.472 1.00 26.10 ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 180.843 221.866 181.734 1.00 24.87 ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 181.542 220.820 182.592 1.00 24.90 ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 181.777 219.689 182.147 1.00 24.38 ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 181.847 222.909 181.244 1.00 24.27 ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 181.300 223.872 180.208 1.00 29.22 ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 182.392 224.480 179.352 1.00 33.46 ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 183.544 224.005 179.435 1.00 32.03 ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 182.100 225.436 178.602 1.00 31.48 ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 181.882 221.182 183.832 1.00 26.75 ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 182.561 220.240 184.718 1.00 23.10 ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 181.698 219.010 184.971 1.00 23.32 ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 182.166 217.866 184.850 1.00 24.41 ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 182.913 220.927 186.038 1.00 23.33 ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 184.319 221.495 186.097 1.00 26.13 ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 184.661 221.946 187.506 1.00 26.01 ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 183.501 222.507 188.190 1.00 27.90 ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 183.346 223.793 188.470 1.00 28.61 ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 184.263 224.689 188.139 1.00 28.68 ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 182.243 224.193 189.097 1.00 26.20 ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 180.424 219.230 185.311 1.00 20.11 ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 179.535 218.112 185.598 1.00 15.36 ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 179.358 217.221 184.378 1.00 18.51 ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 179.398 215.993 184.494 1.00 22.09 ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 178.178 218.623 186.080 1.00 13.91 ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 177.188 217.510 186.338 1.00 17.34 ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 177.395 216.596 187.358 1.00 16.46 ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 176.054 217.367 185.550 1.00 18.26 ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 176.501 215.575 187.596 1.00 14.69 ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 175.152 216.347 185.781 1.00 14.51 ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 175.382 215.455 186.805 1.00 15.74 ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 174.487 214.436 187.042 1.00 18.67 ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 179.176 217.817 183.199 1.00 15.64 ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 178.918 217.027 182.002 1.00 13.34 ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 180.152 216.227 181.608 1.00 14.72 ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 180.044 215.060 181.225 1.00 21.34 ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 178.429 217.933 180.859 1.00 16.43 ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 176.999 218.400 181.129 1.00 16.45 ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 178.487 217.200 179.537 1.00 15.53 ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 176.028 217.275 181.403 1.00 13.67 ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 181.343 216.823 181.707 1.00 12.69 ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 182.558 216.087 181.366 1.00 12.76 ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 182.781 214.918 182.320 1.00 17.45 ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 183.034 213.780 181.889 1.00 17.71 ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 183.759 217.033 181.385 1.00 13.46 ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 183.792 218.018 180.232 1.00 15.80 ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 184.739 219.171 180.483 1.00 19.77 ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 185.802 218.997 181.078 1.00 20.34 ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 184.357 220.358 180.030 1.00 20.79 ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 182.692 215.179 183.628 1.00 17.51 ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 182.910 214.110 184.596 1.00 13.97 ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 181.853 213.022 184.461 1.00 10.56 ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 182.167 211.827 184.537 1.00 12.32 ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 182.928 214.684 186.010 1.00 15.24 ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 184.207 215.420 186.355 1.00 14.97 ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 183.965 216.463 187.429 1.00 17.80 ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 185.211 217.009 187.956 1.00 18.38 ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 185.967 217.897 187.327 1.00 20.29 ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 185.636 218.370 186.137 1.00 20.88 ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 187.085 218.324 187.908 1.00 21.01 ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 180.594 213.411 184.242 1.00 6.17  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 179.541 212.422 184.066 1.00 6.53  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 179.701 211.656 182.764 1.00 8.41  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 179.306 210.493 182.690 1.00 14.34 ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 178.169 213.089 184.117 1.00 4.07  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 177.053 212.124 184.437 1.00 4.82  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 176.445 211.381 183.436 1.00 2.24  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 176.613 211.948 185.740 1.00 8.89  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 175.430 210.496 183.723 1.00 2.94  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 175.597 211.065 186.036 1.00 12.39 ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 175.008 210.341 185.024 1.00 10.75 ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 173.996 209.459 185.313 1.00 12.04 ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 180.262 212.278 181.729 1.00 9.44  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 180.539 211.542 180.503 1.00 7.30  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 181.586 210.466 180.741 1.00 8.24  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 181.436 209.333 180.268 1.00 9.26  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 180.993 212.497 179.402 1.00 7.49  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 181.269 211.821 178.058 1.00 8.59  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 180.017 211.796 177.205 1.00 9.35  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 182.402 212.518 177.336 1.00 14.06 ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 182.645 210.795 181.481 1.00 11.63 ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 183.638 209.776 181.823 1.00 8.00  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 182.998 208.663 182.649 1.00 6.06  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 183.219 207.467 182.400 1.00 6.20  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 184.832 210.412 182.560 1.00 7.60  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 185.814 209.341 183.000 1.00 4.43  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 185.517 211.436 181.672 1.00 10.83 ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 182.182 209.044 183.636 1.00 8.18  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 181.517 208.071 184.500 1.00 6.20  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 180.581 207.164 183.704 1.00 5.09  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 180.554 205.942 183.915 1.00 8.90  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 180.774 208.833 185.600 1.00 4.71  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 179.654 208.111 186.311 1.00 5.48  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 179.897 207.380 187.465 1.00 6.36  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 178.345 208.205 185.860 1.00 8.64  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 178.873 206.737 188.129 1.00 9.05  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 177.317 207.563 186.518 1.00 7.05  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 177.586 206.830 187.650 1.00 8.80  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 176.561 206.189 188.308 1.00 9.40  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 179.824 207.739 182.770 1.00 3.55  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 178.886 206.961 181.969 1.00 3.95  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 179.613 206.061 180.980 1.00 3.95  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 179.160 204.947 180.708 1.00 4.70  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 177.923 207.896 181.239 1.00 4.52  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 180.737 206.522 180.431 1.00 4.24  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 181.546 205.652 179.582 1.00 3.12  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 182.035 204.450 180.379 1.00 7.21  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 181.960 203.305 179.915 1.00 8.62  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 182.715 206.438 178.964 1.00 1.19  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 182.211 207.371 177.866 1.00 6.39  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 183.761 205.494 178.405 1.00 4.47  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 183.282 208.269 177.302 1.00 11.29 ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 182.521 204.691 181.601 1.00 10.72 ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 182.952 203.586 182.455 1.00 5.77  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 181.814 202.609 182.727 1.00 4.71  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 181.994 201.392 182.615 1.00 5.87  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 183.506 204.121 183.773 1.00 2.53  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 184.889 204.760 183.745 1.00 7.38  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 185.188 205.394 185.083 1.00 10.75 ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 185.913 203.694 183.432 1.00 12.40 ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 180.638 203.121 183.084 1.00 5.18  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 179.554 202.240 183.503 1.00 2.01  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 178.770 201.646 182.341 1.00 3.35  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 177.967 200.736 182.563 1.00 7.71  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 178.606 202.986 184.438 1.00 0.61  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 178.993 202.846 185.871 1.00 3.39  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 179.404 203.837 186.707 1.00 3.60  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 179.022 201.638 186.638 1.00 6.44  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 179.681 203.326 187.949 1.00 7.96  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 179.454 201.976 187.933 1.00 7.65  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 178.720 200.302 186.355 1.00 3.68  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 179.593 201.030 188.943 1.00 8.18  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 178.857 199.365 187.358 1.00 3.79  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 179.290 199.733 188.637 1.00 8.09  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 178.981 202.126 181.117 1.00 4.35  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 178.316 201.574 179.947 1.00 0.13  ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 179.199 200.634 179.148 1.00 3.82  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 178.695 199.656 178.589 1.00 5.80  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 177.839 202.704 179.031 1.00 0.08  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 177.008 203.609 179.733 1.00 5.81  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 180.499 200.904 179.079 1.00 5.90  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 181.413 200.060 178.327 1.00 3.38  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 182.017 198.944 179.167 1.00 7.91  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 182.660 198.049 178.609 1.00 17.80 ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 182.535 200.914 177.722 1.00 5.40  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 182.312 201.570 176.357 1.00 3.54  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 180.949 202.229 176.241 1.00 1.65  ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 183.395 202.592 176.117 1.00 6.84  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 181.825 198.974 180.489 1.00 6.97  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 182.358 197.932 181.358 1.00 1.97  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 181.369 197.530 182.448 1.00 4.25  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 181.766 196.886 183.424 1.00 12.30 ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 183.670 198.378 182.003 1.00 5.38  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 183.476 199.534 182.799 1.00 10.68 ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 180.094 197.901 182.312 1.00 4.65  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 179.113 197.534 183.318 1.00 2.58  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 178.885 196.041 183.417 1.00 5.64  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 178.615 195.523 184.503 1.00 9.62  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 178.989 195.329 182.295 1.00 3.01  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 178.763 193.890 182.243 1.00 0.75  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 180.063 193.095 182.305 1.00 4.97  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 180.162 192.020 181.707 1.00 11.33 ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 177.978 193.526 180.984 1.00 2.70  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 178.709 193.905 179.714 1.00 9.59  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 179.513 194.857 179.751 1.00 8.68  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 178.473 193.256 178.675 1.00 13.41 ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 181.064 193.604 183.019 1.00 4.10  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 182.351 192.943 183.152 1.00 4.42  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 182.766 192.933 184.617 1.00 9.77  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 182.201 193.645 185.452 1.00 9.59  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 183.421 193.628 182.291 1.00 4.40  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 183.494 195.013 182.575 1.00 7.32  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 183.767 192.112 184.924 1.00 11.98 ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 184.237 191.964 186.292 1.00 8.85  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 184.929 193.242 186.763 1.00 14.83 ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 185.091 194.212 186.020 1.00 18.11 ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 185.186 190.774 186.401 1.00 8.85  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 184.561 189.440 186.051 1.00 13.09 ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 185.559 188.316 186.247 1.00 16.71 ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 186.849 188.627 185.644 1.00 20.07 ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 187.141 188.443 184.364 1.00 22.43 ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 186.257 187.942 183.516 1.00 20.46 ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 188.354 188.764 183.923 1.00 17.09 ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 185.347 193.232 188.032 1.00 15.46 ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 186.027 194.393 188.598 1.00 14.06 ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 187.371 194.628 187.921 1.00 15.80 ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 187.790 195.779 187.741 1.00 19.87 ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 186.204 194.205 190.105 1.00 17.85 ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 187.067 195.209 190.872 1.00 22.59 ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 186.606 196.636 190.610 1.00 20.60 ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 187.052 194.899 192.359 1.00 17.36 ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 188.064 193.552 187.538 1.00 14.37 ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 189.358 193.703 186.880 1.00 15.62 ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 189.223 194.441 185.554 1.00 20.89 ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 190.023 195.331 185.245 1.00 23.58 ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 190.002 192.335 186.666 1.00 18.74 ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 191.382 192.398 186.034 1.00 21.29 ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 192.019 191.021 185.945 1.00 21.99 ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 191.398 190.201 184.828 1.00 20.65 ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 192.106 188.907 184.633 1.00 18.79 ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 188.208 194.095 184.760 1.00 16.46 ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 188.026 194.758 183.475 1.00 11.71 ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 187.555 196.198 183.644 1.00 13.05 ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 187.925 197.067 182.847 1.00 21.13 ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 187.050 193.966 182.611 1.00 8.64  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 187.544 192.573 182.271 1.00 14.30 ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 189.132 192.602 181.420 1.00 33.97 ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 189.510 190.854 181.344 1.00 18.65 ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 186.744 196.468 184.669 1.00 6.32  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 186.378 197.850 184.968 1.00 9.09  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 187.609 198.672 185.327 1.00 16.87 ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 187.756 199.815 184.876 1.00 20.72 ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 185.356 197.887 186.102 1.00 10.46 ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 184.043 197.207 185.766 1.00 10.88 ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 183.124 197.149 186.970 1.00 9.98  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 181.852 196.516 186.648 1.00 6.77  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 180.928 196.196 187.544 1.00 12.57 ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 181.102 196.437 188.831 1.00 15.24 ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 179.800 195.623 187.136 1.00 9.50  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 188.508 198.102 186.132 1.00 17.29 ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 189.753 198.790 186.457 1.00 15.95 ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 190.610 198.997 185.214 1.00 16.09 ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 191.246 200.045 185.058 1.00 16.67 ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 190.524 198.007 187.519 1.00 13.14 ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 190.648 198.002 184.325 1.00 15.75 ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 191.409 198.137 183.084 1.00 16.51 ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 190.878 199.287 182.237 1.00 17.50 ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 191.649 200.104 181.716 1.00 19.52 ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 191.357 196.829 182.295 1.00 12.96 ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 192.193 195.706 182.876 1.00 18.76 ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 192.306 194.525 181.934 1.00 24.36 ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 192.295 194.743 180.705 1.00 21.85 ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 192.401 193.379 182.420 1.00 21.21 ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 189.553 199.361 182.082 1.00 15.10 ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 188.966 200.443 181.299 1.00 15.79 ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 189.209 201.793 181.958 1.00 14.59 ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 189.471 202.789 181.273 1.00 18.85 ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 187.470 200.207 181.099 1.00 14.99 ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 186.803 201.190 180.136 1.00 14.39 ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 187.419 201.092 178.750 1.00 13.23 ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 185.308 200.959 180.072 1.00 10.83 ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 189.121 201.851 183.290 1.00 12.24 ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 189.421 203.094 183.981 1.00 15.40 ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 190.852 203.546 183.769 1.00 19.12 ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 191.112 204.730 183.540 1.00 20.20 ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 191.800 202.609 183.836 1.00 18.89 ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 193.198 202.946 183.590 1.00 16.23 ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 193.405 203.432 182.160 1.00 20.36 ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 194.125 204.412 181.927 1.00 21.21 ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 194.088 201.737 183.878 1.00 16.26 ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 194.186 201.377 185.350 1.00 20.04 ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 194.416 199.894 185.573 1.00 22.46 ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 194.682 199.178 184.584 1.00 23.26 ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 194.327 199.444 186.735 1.00 18.81 ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 192.777 202.765 181.188 1.00 19.73 ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 192.917 203.200 179.801 1.00 16.57 ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 192.348 204.598 179.599 1.00 18.62 ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 192.963 205.435 178.925 1.00 25.75 ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 192.240 202.208 178.858 1.00 15.19 ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 192.385 202.587 177.402 1.00 20.45 ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 193.542 202.284 176.699 1.00 20.02 ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 191.372 203.262 176.733 1.00 21.85 ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 193.684 202.632 175.371 1.00 21.52 ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 191.506 203.615 175.405 1.00 19.29 ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 192.662 203.297 174.729 1.00 21.31 ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 192.799 203.647 173.407 1.00 21.22 ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 191.175 204.873 180.173 1.00 15.50 ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 190.586 206.203 180.041 1.00 13.95 ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 191.483 207.245 180.694 1.00 18.74 ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 191.725 208.317 180.130 1.00 26.53 ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 189.161 206.228 180.620 1.00 15.64 ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 188.233 205.370 179.763 1.00 19.88 ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 188.641 207.652 180.710 1.00 15.17 ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 186.864 205.182 180.350 1.00 15.07 ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 192.009 206.938 181.883 1.00 19.15 ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 192.954 207.844 182.527 1.00 22.73 ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 194.152 208.117 181.628 1.00 23.28 ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 194.675 209.237 181.595 1.00 23.21 ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 193.412 207.262 183.863 1.00 21.41 ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 194.019 208.283 184.808 1.00 19.82 ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 194.559 207.614 186.058 1.00 23.21 ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 193.565 207.564 187.122 1.00 22.92 ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 193.240 208.591 187.892 1.00 25.72 ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 193.816 209.773 187.748 1.00 26.51 ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 192.314 208.429 188.833 1.00 24.64 ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 194.603 207.099 180.894 1.00 20.79 ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 195.694 207.298 179.946 1.00 21.73 ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 195.286 208.227 178.808 1.00 25.75 ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 196.078 209.076 178.382 1.00 26.90 ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 196.158 205.954 179.388 1.00 18.64 ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 196.940 205.102 180.366 1.00 21.08 ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 196.994 203.659 179.897 1.00 24.59 ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 196.988 203.564 178.443 1.00 27.42 ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 196.993 202.425 177.765 1.00 28.60 ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 197.000 201.254 178.383 1.00 26.79 ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 196.989 202.458 176.436 1.00 23.72 ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 194.058 208.086 178.302 1.00 23.90 ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 193.692 208.710 177.029 1.00 18.63 ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 192.811 209.947 177.165 1.00 20.07 ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 192.517 210.589 176.143 1.00 23.11 ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 192.990 207.700 176.097 1.00 19.79 ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 191.587 207.386 176.617 1.00 19.70 ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 193.820 206.436 175.960 1.00 20.26 ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 190.597 207.034 175.532 1.00 21.94 ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 192.375 210.307 178.368 1.00 22.19 ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 191.451 211.424 178.510 1.00 22.57 ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 192.168 212.673 179.008 1.00 24.03 ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 193.253 212.614 179.590 1.00 26.23 ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 190.300 211.082 179.461 1.00 22.20 ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 189.250 212.041 179.294 1.00 23.47 ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 190.767 211.137 180.906 1.00 23.00 ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 191.538 213.820 178.755 1.00 25.19 ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 191.978 215.100 179.285 1.00 27.04 ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 191.046 215.633 180.363 1.00 25.54 ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 191.339 216.674 180.962 1.00 26.13 ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 192.103 216.134 178.159 1.00 27.59 ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 190.812 216.677 177.860 1.00 27.22 ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 192.681 215.491 176.908 1.00 24.27 ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 189.934 214.956 180.618 1.00 22.13 ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 189.006 215.369 181.676 1.00 24.70 ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 189.685 215.202 183.028 1.00 25.02 ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 190.426 214.222 183.224 1.00 24.27 ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 187.717 214.545 181.598 1.00 22.55 ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 186.657 215.105 182.530 1.00 21.72 ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 187.204 214.501 180.167 1.00 20.48 ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 189.495 216.123 183.974 1.00 24.76 ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 190.038 215.910 185.320 1.00 23.62 ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 189.480 214.639 185.942 1.00 23.06 ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 188.300 214.316 185.792 1.00 24.34 ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 189.592 217.159 186.084 1.00 25.37 ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 189.411 218.197 185.033 1.00 22.39 ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 188.924 217.470 183.814 1.00 22.47 ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 190.339 213.924 186.651 1.00 24.78 ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 190.035 212.617 187.208 1.00 24.39 ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 190.474 212.567 188.661 1.00 26.44 ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 191.329 213.351 189.086 1.00 26.69 ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 190.732 211.506 186.407 1.00 21.04 ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 190.111 211.190 185.045 1.00 21.80 ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 190.697 209.919 184.474 1.00 23.74 ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 188.602 211.080 185.157 1.00 22.25 ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 189.894 211.667 189.458 1.00 27.24 ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 190.313 211.550 190.859 1.00 26.66 ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 191.795 211.221 190.972 1.00 30.05 ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 192.339 210.437 190.191 1.00 29.55 ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 189.440 210.411 191.396 1.00 24.63 ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 188.247 210.405 190.509 1.00 23.54 ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 188.746 210.795 189.152 1.00 23.80 ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 192.442 211.829 191.961 1.00 35.42 ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 193.882 211.717 192.148 1.00 33.34 ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 194.270 210.632 193.145 1.00 34.37 ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 195.409 210.628 193.621 1.00 34.27 ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 194.459 213.062 192.596 1.00 35.14 ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 193.811 213.482 193.802 1.00 36.35 ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 194.246 214.115 191.520 1.00 31.98 ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 193.354 209.729 193.474 1.00 39.02 ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 193.674 208.652 194.399 1.00 38.87 ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 194.736 207.742 193.788 1.00 40.88 ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 194.604 207.339 192.624 1.00 40.11 ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 192.420 207.848 194.738 1.00 38.52 ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 195.798 207.409 194.525 1.00 45.41 ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 196.881 206.607 193.931 1.00 44.95 ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 196.445 205.232 193.450 1.00 43.72 ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 196.968 204.751 192.436 1.00 44.60 ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 197.904 206.502 195.072 1.00 44.36 ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 197.116 206.744 196.318 1.00 44.63 ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 196.053 207.728 195.939 1.00 43.71 ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 195.504 204.585 194.136 1.00 39.65 ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 195.119 203.219 193.799 1.00 40.45 ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 193.621 202.999 193.651 1.00 42.25 ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 193.230 201.996 193.042 1.00 40.45 ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 195.654 202.237 194.854 1.00 39.33 ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 197.053 201.750 194.538 1.00 42.76 ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 197.650 202.144 193.537 1.00 42.68 ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 197.585 200.885 195.394 1.00 42.00 ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 192.779 203.878 194.177 1.00 38.98 ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 191.329 203.676 194.071 1.00 34.16 ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 190.896 203.905 192.627 1.00 32.52 ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 191.179 204.974 192.061 1.00 33.58 ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 190.588 204.615 195.028 1.00 32.66 ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 190.902 204.270 196.488 1.00 33.94 ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 189.091 204.541 194.786 1.00 31.44 ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 192.084 205.018 197.072 1.00 34.53 ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 190.219 202.949 191.996 1.00 25.93 ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 189.816 203.126 190.597 1.00 25.24 ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 188.731 204.183 190.452 1.00 24.61 ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 188.033 204.542 191.401 1.00 24.12 ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 189.298 201.742 190.197 1.00 24.29 ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 188.879 201.115 191.478 1.00 24.41 ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 189.819 201.636 192.528 1.00 25.09 ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 188.605 204.689 189.221 1.00 18.94 ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 187.604 205.711 188.934 1.00 15.53 ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 186.196 205.152 189.089 1.00 15.95 ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 185.248 205.903 189.348 1.00 20.39 ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 187.826 206.292 187.525 1.00 17.35 ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 189.311 206.571 187.291 1.00 19.82 ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 187.034 207.575 187.344 1.00 17.86 ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 189.698 206.582 185.833 1.00 17.94 ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 186.028 203.835 188.941 1.00 13.58 ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 184.712 203.221 189.076 1.00 12.64 ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 184.176 203.345 190.496 1.00 15.42 ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 182.979 203.144 190.724 1.00 18.48 ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 184.766 201.744 188.631 1.00 13.94 ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 183.391 201.276 188.150 1.00 12.49 ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 185.267 200.858 189.758 1.00 14.12 ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 182.982 201.855 186.818 1.00 12.50 ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 185.032 203.682 191.458 1.00 13.61 ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 184.628 203.874 192.843 1.00 12.52 ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 184.206 205.308 193.137 1.00 15.82 ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 183.956 205.640 194.299 1.00 18.02 ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 185.763 203.469 193.785 1.00 13.77 ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 186.011 201.975 193.793 1.00 23.83 ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 185.316 201.252 193.050 1.00 22.19 ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 186.903 201.524 194.540 1.00 24.78 ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 184.129 206.160 192.119 1.00 12.98 ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 183.773 207.560 192.280 1.00 9.54  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 182.502 207.865 191.501 1.00 12.79 ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 182.277 207.310 190.422 1.00 18.19 ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 184.896 208.480 191.794 1.00 12.48 ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 186.076 208.574 192.726 1.00 12.48 ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 187.077 207.615 192.710 1.00 14.57 ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 186.197 209.630 193.616 1.00 16.64 ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 188.159 207.700 193.557 1.00 16.90 ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 187.276 209.724 194.468 1.00 20.46 ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 188.254 208.755 194.434 1.00 20.74 ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 189.332 208.844 195.282 1.00 23.52 ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 181.676 208.747 192.054 1.00 13.50 ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 180.525 209.299 191.360 1.00 10.39 ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 180.783 210.763 191.038 1.00 13.72 ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 181.756 211.368 191.496 1.00 18.35 ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 179.252 209.176 192.202 1.00 12.22 ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 179.291 210.010 193.467 1.00 14.38 ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 177.961 210.055 194.184 1.00 20.17 ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 176.979 209.498 193.655 1.00 22.78 ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 177.897 210.649 195.280 1.00 19.55 ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 179.879 211.335 190.251 1.00 11.71 ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 179.929 212.743 189.888 1.00 11.02 ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 178.809 213.448 190.636 1.00 15.32 ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 177.625 213.207 190.374 1.00 20.20 ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 179.798 212.949 188.375 1.00 10.24 ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 180.061 214.397 188.025 1.00 11.70 ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 180.756 212.035 187.637 1.00 13.31 ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 179.179 214.317 191.568 1.00 14.53 ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 178.200 215.116 192.279 1.00 14.32 ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 177.683 216.237 191.382 1.00 19.01 ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 178.325 216.635 190.407 1.00 18.28 ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 178.803 215.694 193.558 1.00 15.09 ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 179.923 216.510 193.269 1.00 19.03 ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 176.499 216.748 191.727 1.00 23.47 ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 175.896 217.832 190.960 1.00 20.48 ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 176.698 219.121 191.042 1.00 22.73 ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 176.441 220.052 190.271 1.00 26.09 ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 174.447 218.075 191.430 1.00 20.74 ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 173.616 218.702 190.309 1.00 20.98 ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 174.426 218.950 192.673 1.00 20.94 ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 173.563 217.871 189.048 1.00 18.37 ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 177.673 219.198 191.946 1.00 23.53 ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 178.540 220.362 192.049 1.00 22.79 ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 179.676 220.345 191.036 1.00 24.12 ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 180.489 221.274 191.027 1.00 27.60 ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 179.114 220.467 193.465 1.00 23.44 ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 180.010 219.403 193.730 1.00 26.25 ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 179.754 219.319 190.192 1.00 17.78 ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 180.800 219.253 189.192 1.00 21.89 ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 182.132 218.749 189.693 1.00 23.89 ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 183.170 219.103 189.130 1.00 27.25 ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 182.135 217.933 190.744 1.00 20.20 ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 183.361 217.379 191.298 1.00 19.80 ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 183.188 215.887 191.545 1.00 17.30 ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 182.089 215.414 191.846 1.00 21.65 ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 183.753 218.079 192.606 1.00 21.40 ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 184.763 219.203 192.435 1.00 22.97 ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 186.179 218.696 192.235 1.00 26.42 ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 186.402 217.473 192.361 1.00 26.18 ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 187.070 219.524 191.954 1.00 24.97 ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 184.287 215.151 191.409 1.00 14.34 ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 184.282 213.734 191.745 1.00 15.82 ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 184.139 213.553 193.249 1.00 19.49 ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 184.782 214.250 194.038 1.00 24.00 ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 185.572 213.065 191.269 1.00 17.91 ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 185.707 212.944 189.785 1.00 18.06 ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 186.442 213.746 188.965 1.00 19.40 ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 185.108 211.952 188.946 1.00 16.30 ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 186.333 213.318 187.664 1.00 17.79 ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 185.519 212.218 187.626 1.00 16.85 ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 184.260 210.866 189.182 1.00 15.68 ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 185.111 211.440 186.547 1.00 16.23 ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 183.858 210.095 188.109 1.00 12.63 ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 184.283 210.385 186.809 1.00 15.20 ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 183.288 212.612 193.650 1.00 15.25 ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 183.156 212.290 195.060 1.00 15.60 ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 183.167 210.779 195.245 1.00 16.55 ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 182.520 210.055 194.481 1.00 16.64 ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 181.870 212.884 195.650 1.00 14.58 ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 180.738 212.120 195.286 1.00 17.81 ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 183.893 210.275 196.242 1.00 19.20 ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 183.972 208.823 196.428 1.00 13.93 ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 182.611 208.224 196.746 1.00 14.68 ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 181.790 208.828 197.437 1.00 14.96 ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 184.945 208.667 197.600 1.00 13.33 ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 184.874 209.964 198.325 1.00 17.06 ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 184.642 211.008 197.275 1.00 17.48 ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 182.377 207.019 196.223 1.00 14.67 ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 181.146 206.304 196.535 1.00 12.64 ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 181.098 205.885 197.997 1.00 15.05 ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 180.008 205.741 198.566 1.00 17.19 ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 181.006 205.081 195.631 1.00 8.12  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 180.209 205.318 194.387 1.00 10.62 ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 180.630 205.151 193.102 1.00 12.12 ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 178.846 205.746 194.308 1.00 12.03 ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 179.618 205.453 192.227 1.00 11.86 ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 178.510 205.821 192.943 1.00 10.61 ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 177.875 206.074 195.259 1.00 13.05 ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 177.250 206.214 192.506 1.00 8.51  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 176.626 206.462 194.823 1.00 10.40 ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 176.323 206.528 193.460 1.00 10.73 ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 182.262 205.692 198.622 1.00 15.25 ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 182.312 205.282 200.021 1.00 10.61 ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 181.672 206.306 200.947 1.00 13.05 ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 181.251 205.948 202.051 1.00 17.64 ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 183.760 205.036 200.442 1.00 13.40 ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 183.917 204.050 201.586 1.00 16.55 ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 183.652 202.620 201.163 1.00 20.43 ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 182.829 201.927 201.758 1.00 19.52 ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 184.354 202.169 200.129 1.00 17.68 ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 181.592 207.569 200.525 1.00 12.10 ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 180.916 208.580 201.328 1.00 10.85 ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 179.425 208.302 201.469 1.00 13.26 ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 178.798 208.815 202.402 1.00 17.44 ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 181.131 209.966 200.722 1.00 14.52 ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 178.850 207.505 200.571 1.00 13.77 ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 177.443 207.141 200.634 1.00 12.19 ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 177.226 205.756 201.230 1.00 15.25 ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 176.122 205.213 201.126 1.00 18.41 ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 176.817 207.215 199.241 1.00 11.39 ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 176.503 208.631 198.787 1.00 16.47 ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 175.623 208.637 197.551 1.00 15.29 ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 175.245 210.053 197.156 1.00 15.06 ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 174.344 210.076 195.972 1.00 18.40 ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 178.250 205.179 201.848 1.00 17.73 ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 178.148 203.862 202.470 1.00 16.88 ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 178.440 204.004 203.958 1.00 18.49 ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 179.602 203.895 204.376 1.00 19.45 ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 179.107 202.858 201.810 1.00 13.40 ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 178.934 201.481 202.422 1.00 13.81 ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 178.873 202.809 200.312 1.00 13.36 ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 177.434 204.260 204.788 1.00 23.88 ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 177.661 204.365 206.229 1.00 26.80 ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 177.621 203.006 206.915 1.00 31.14 ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 177.087 202.024 206.393 1.00 32.30 ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 176.491 205.242 206.695 1.00 27.13 ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 175.391 204.903 205.745 1.00 24.93 ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 176.037 204.553 204.423 1.00 24.56 ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 178.203 202.969 208.109 1.00 35.14 ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 178.163 201.781 208.959 1.00 37.02 ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 176.841 201.805 209.714 1.00 36.68 ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 176.733 202.347 210.815 1.00 38.30 ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 179.358 201.747 209.902 1.00 39.39 ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 179.370 200.566 210.861 1.00 39.85 ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 180.287 199.449 210.403 1.00 41.51 ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 180.590 199.326 209.217 1.00 43.33 ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 180.736 198.629 211.346 1.00 37.64 ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 175.813 201.218 209.104 1.00 33.61 ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 174.476 201.268 209.678 1.00 33.46 ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 174.351 200.249 210.807 1.00 39.35 ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 175.166 199.336 210.957 1.00 40.87 ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 173.402 201.037 208.599 1.00 33.00 ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 173.399 199.576 208.155 1.00 33.11 ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 173.637 201.954 207.413 1.00 36.24 ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 172.090 199.131 207.541 1.00 33.77 ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 173.308 200.419 211.613 1.00 36.00 ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 172.987 199.511 212.710 1.00 34.76 ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 171.567 199.005 212.484 1.00 37.09 ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 170.595 199.722 212.742 1.00 37.81 ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 173.127 200.206 214.062 1.00 34.31 ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 174.541 200.655 214.384 1.00 35.90 ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 175.484 199.492 214.613 1.00 39.23 ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 175.025 198.440 215.100 1.00 39.14 ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 176.688 199.633 214.308 1.00 39.88 ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 171.450 197.770 211.998 1.00 28.96 ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 170.143 197.195 211.718 1.00 25.79 ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 169.400 196.941 213.024 1.00 30.18 ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 169.998 196.615 214.057 1.00 32.32 ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 170.294 195.899 210.899 1.00 25.43 ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 168.939 195.387 210.441 1.00 26.20 ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 171.206 196.134 209.707 1.00 28.36 ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 168.082 197.115 212.984 1.00 30.98 ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 167.254 196.795 214.135 1.00 27.56 ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 167.263 195.293 214.393 1.00 29.04 ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 167.415 194.483 213.476 1.00 32.25 ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 165.822 197.281 213.915 1.00 27.82 ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 165.725 198.711 213.418 1.00 33.10 ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 165.782 199.723 214.544 1.00 35.29 ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 165.003 199.582 215.509 1.00 33.06 ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 166.608 200.656 214.465 1.00 34.20 ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 167.108 194.927 215.667 1.00 27.01 ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 167.152 193.516 216.040 1.00 27.07 ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 166.016 192.734 215.390 1.00 29.68 ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 166.219 191.611 214.913 1.00 30.33 ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 167.102 193.375 217.562 1.00 27.78 ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 168.226 194.048 218.139 1.00 28.30 ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 167.147 191.912 217.959 1.00 28.72 ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 164.814 193.309 215.352 1.00 28.22 ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 163.685 192.622 214.738 1.00 28.50 ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 163.767 192.590 213.216 1.00 30.87 ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 162.962 191.895 212.587 1.00 33.81 ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 162.370 193.270 215.173 1.00 30.90 ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 162.110 194.602 214.542 1.00 34.76 ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 162.913 195.700 214.762 1.00 36.27 ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 161.133 195.013 213.700 1.00 32.25 ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 162.442 196.730 214.081 1.00 32.77 ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 161.363 196.339 213.429 1.00 32.09 ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 164.707 193.318 212.615 1.00 27.42 ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 164.884 193.347 211.167 1.00 26.86 ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 166.173 192.655 210.738 1.00 26.55 ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 166.760 193.005 209.712 1.00 30.51 ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 164.863 194.786 210.654 1.00 27.91 ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 163.532 195.495 210.828 1.00 30.74 ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 162.741 195.505 209.531 1.00 30.73 ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 161.413 196.225 209.700 1.00 32.13 ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 160.482 195.477 210.588 1.00 30.42 ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 166.624 191.670 211.510 1.00 23.77 ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 167.882 190.989 211.222 1.00 22.38 ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 167.679 190.047 210.042 1.00 23.55 ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 166.838 189.145 210.094 1.00 24.70 ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 168.394 190.230 212.453 1.00 18.16 ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 169.415 189.190 212.047 1.00 17.18 ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 169.004 191.198 213.447 1.00 21.50 ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 168.451 190.266 208.975 1.00 22.33 ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 168.427 189.430 207.774 1.00 19.50 ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 167.024 189.313 207.184 1.00 25.14 ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 166.648 188.266 206.654 1.00 24.40 ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 169.012 188.043 208.051 1.00 13.54 ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 166.243 190.386 207.271 1.00 28.98 ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 164.925 190.396 206.664 1.00 29.85 ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 165.051 190.451 205.141 1.00 33.37 ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 166.065 190.914 204.613 1.00 31.48 ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 164.112 191.584 207.170 1.00 28.11 ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 164.041 189.964 204.413 1.00 37.59 ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 164.139 189.966 202.943 1.00 36.26 ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 164.302 191.349 202.337 1.00 36.81 ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 164.945 191.480 201.287 1.00 37.37 ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 162.820 189.311 202.502 1.00 35.10 ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 161.926 189.356 203.700 1.00 36.33 ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 162.824 189.284 204.885 1.00 36.07 ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 163.744 192.385 202.957 1.00 32.54 ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 163.787 193.735 202.411 1.00 29.99 ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 164.872 194.599 203.043 1.00 27.80 ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 164.918 195.804 202.778 1.00 28.36 ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 162.425 194.412 202.576 1.00 31.64 ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 161.922 194.372 204.006 1.00 38.77 ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 161.354 193.334 204.409 1.00 37.56 ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 162.096 195.376 204.727 1.00 38.34 ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 165.741 194.020 203.866 1.00 23.75 ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 166.798 194.765 204.541 1.00 23.60 ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 168.084 194.605 203.746 1.00 20.64 ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 168.526 193.481 203.478 1.00 21.76 ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 166.979 194.292 205.992 1.00 23.61 ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 168.279 194.831 206.564 1.00 19.67 ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 165.807 194.745 206.839 1.00 26.46 ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 168.683 195.731 203.367 1.00 13.46 ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 169.911 195.757 202.583 1.00 11.51 ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 170.955 196.532 203.374 1.00 11.63 ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 170.725 197.687 203.748 1.00 14.35 ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 169.695 196.396 201.203 1.00 10.43 ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 170.986 196.384 200.403 1.00 6.91  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 168.586 195.681 200.456 1.00 12.36 ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 172.094 195.898 203.630 1.00 7.87  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 173.223 196.583 204.251 1.00 4.68  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 173.988 197.295 203.142 1.00 9.85  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 174.504 196.636 202.228 1.00 9.71  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 174.125 195.608 205.021 1.00 4.95  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 175.373 196.321 205.510 1.00 6.92  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 173.367 194.997 206.185 1.00 9.56  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 174.078 198.622 203.172 1.00 10.05 ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 174.720 199.342 202.067 1.00 6.66  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 176.203 199.012 201.967 1.00 9.69  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 176.923 198.992 202.965 1.00 11.81 ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 174.492 200.814 202.425 1.00 6.34  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 174.283 200.814 203.902 1.00 8.87  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 173.552 199.542 204.193 1.00 10.46 ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 176.647 198.744 200.742 1.00 4.79  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 178.051 198.539 200.427 1.00 4.88  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 178.401 199.389 199.213 1.00 6.96  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 177.561 200.112 198.672 1.00 11.58 ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 178.370 197.062 200.154 1.00 6.83  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 177.579 196.592 199.058 1.00 13.68 ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 178.083 196.216 201.383 1.00 6.29  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 179.663 199.303 198.788 1.00 5.96  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 180.090 200.026 197.595 1.00 3.53  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 179.350 199.520 196.362 1.00 5.21  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 178.749 200.302 195.613 1.00 12.96 ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 181.601 199.880 197.416 1.00 4.76  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 182.291 200.801 196.413 1.00 7.44  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 182.527 202.162 197.030 1.00 13.51 ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 183.599 200.192 195.945 1.00 8.96  ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 179.366 198.202 196.150 1.00 1.37  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 178.674 197.624 195.004 1.00 2.09  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 177.180 197.900 195.068 1.00 1.84  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 176.555 198.193 194.044 1.00 9.08  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 178.938 196.121 194.935 1.00 6.50  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 180.334 195.797 194.449 1.00 15.97 ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 180.678 196.196 193.319 1.00 15.88 ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 181.088 195.139 195.197 1.00 17.15 ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 176.596 197.819 196.264 1.00 2.20  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 175.163 198.048 196.405 1.00 3.02  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 174.777 199.452 195.960 1.00 5.06  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 173.856 199.619 195.154 1.00 9.50  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 174.736 197.806 197.853 1.00 3.94  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 174.685 196.397 198.107 1.00 7.05  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 173.369 198.408 198.120 1.00 3.94  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 175.486 200.473 196.445 1.00 3.90  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 175.116 201.843 196.106 1.00 3.39  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 175.417 202.139 194.639 1.00 3.40  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 174.629 202.809 193.958 1.00 8.59  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 175.800 202.850 197.053 1.00 5.50  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 175.367 202.601 198.488 1.00 5.65  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 177.313 202.790 196.933 1.00 5.37  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 176.544 201.638 194.123 1.00 2.70  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 176.862 201.864 192.715 1.00 1.53  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 175.803 201.250 191.807 1.00 4.61  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 175.313 201.902 190.873 1.00 13.74 ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 178.242 201.293 192.388 1.00 0.97  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 179.387 202.006 193.072 1.00 4.39  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 180.724 201.512 192.558 1.00 5.88  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 180.753 200.061 192.436 1.00 6.29  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 181.859 199.328 192.468 1.00 10.64 ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 183.049 199.882 192.628 1.00 8.31  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 181.767 198.009 192.338 1.00 10.96 ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 175.424 200.000 192.077 1.00 1.71  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 174.435 199.332 191.243 1.00 0.00  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 173.058 199.959 191.409 1.00 1.72  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 172.296 200.041 190.443 1.00 4.52  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 174.400 197.842 191.571 1.00 0.00  ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 175.663 197.120 191.224 1.00 1.81  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 175.963 195.868 191.713 1.00 8.41  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 176.704 197.475 190.435 1.00 5.66  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 177.135 195.483 191.241 1.00 7.65  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 177.606 196.440 190.462 1.00 4.91  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 172.719 200.413 192.617 1.00 3.71  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 171.444 201.096 192.808 1.00 0.79  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 171.384 202.382 191.999 1.00 4.76  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 170.364 202.675 191.364 1.00 10.42 ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 171.219 201.392 194.290 1.00 0.94  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 170.603 200.251 195.071 1.00 6.28  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 170.657 200.486 196.566 1.00 12.81 ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 170.891 201.640 196.980 1.00 15.36 ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 170.470 199.517 197.329 1.00 12.26 ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 172.468 203.163 192.005 1.00 6.14  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 172.492 204.390 191.215 1.00 2.09  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 172.386 204.091 189.727 1.00 3.66  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 171.640 204.763 189.001 1.00 6.12  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 173.764 205.180 191.514 1.00 2.44  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 173.117 203.080 189.253 1.00 3.25  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 173.053 202.728 187.837 1.00 1.81  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 171.656 202.259 187.441 1.00 7.08  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 171.133 202.649 186.387 1.00 11.85 ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 174.094 201.654 187.528 1.00 1.12  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 174.351 201.323 186.061 1.00 2.93  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 175.054 202.476 185.377 1.00 6.31  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 175.176 200.055 185.960 1.00 6.02  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 171.033 201.427 188.278 1.00 4.27  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 169.695 200.934 187.974 1.00 0.87  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 168.667 202.054 188.018 1.00 1.59  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 167.725 202.058 187.226 1.00 4.56  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 169.307 199.816 188.939 1.00 2.09  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 170.083 198.510 188.805 1.00 0.75  ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 169.585 197.505 189.822 1.00 7.34  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 169.968 197.961 187.401 1.00 1.86  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 168.813 203.002 188.946 1.00 0.86  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 167.922 204.155 188.951 1.00 0.97  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 168.088 204.972 187.678 1.00 4.63  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 167.101 205.430 187.091 1.00 5.73  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 168.179 205.020 190.186 1.00 2.75  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 167.250 206.209 190.314 1.00 5.84  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 167.516 207.403 189.655 1.00 7.39  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 166.106 206.136 191.094 1.00 5.83  ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 166.669 208.487 189.768 1.00 7.24  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 165.254 207.215 191.214 1.00 9.90  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 165.540 208.387 190.549 1.00 10.90 ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 164.693 209.464 190.667 1.00 11.49 ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 169.334 205.155 187.234 1.00 6.36  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 169.580 205.878 185.991 1.00 4.06  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 168.894 205.196 184.814 1.00 3.46  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 168.276 205.860 183.975 1.00 6.08  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 171.083 205.990 185.741 1.00 3.36  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 171.664 206.889 186.693 1.00 8.01  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 171.363 206.492 184.337 1.00 3.47  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 168.986 203.869 184.741 1.00 4.89  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 168.399 203.160 183.607 1.00 2.16  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 166.881 203.035 183.706 1.00 3.40  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 166.200 203.043 182.676 1.00 8.64  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 169.040 201.780 183.466 1.00 0.00  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 170.411 201.841 182.872 1.00 2.20  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 170.928 202.853 182.119 1.00 4.08  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 171.440 200.853 182.979 1.00 1.96  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 172.216 202.557 181.751 1.00 6.11  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 172.554 201.335 182.266 1.00 4.35  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 171.527 199.609 183.608 1.00 3.53  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 173.742 200.616 182.165 1.00 6.34  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 172.705 198.897 183.505 1.00 8.41  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 173.796 199.402 182.789 1.00 9.16  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 166.334 202.912 184.917 1.00 4.28  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 164.894 202.758 185.092 1.00 0.91  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 164.156 204.079 184.926 1.00 7.90  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 163.037 204.104 184.402 1.00 14.17 ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 164.590 202.161 186.465 1.00 1.31  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 164.811 200.661 186.666 1.00 3.06  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 165.123 200.358 188.119 1.00 1.78  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 163.591 199.884 186.215 1.00 5.37  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 164.756 205.186 185.376 1.00 8.19  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 164.094 206.482 185.261 1.00 3.51  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 163.854 206.861 183.808 1.00 5.71  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 162.940 207.638 183.511 1.00 8.49  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 164.920 207.557 185.963 1.00 6.73  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 164.658 206.327 182.893 1.00 0.88  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 164.462 206.523 181.466 1.00 0.54  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 163.488 205.518 180.868 1.00 6.47  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 163.245 205.560 179.658 1.00 9.70  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 165.804 206.435 180.734 1.00 3.19  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 166.828 207.461 181.187 1.00 10.11 ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 166.480 208.868 180.745 1.00 17.12 ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 165.889 209.024 179.655 1.00 16.25 ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 166.797 209.819 181.488 1.00 14.73 ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 162.937 204.617 181.687 1.00 6.86  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 162.041 203.554 181.233 1.00 2.77  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 162.715 202.656 180.203 1.00 4.32  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 162.058 202.073 179.339 1.00 8.64  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 160.729 204.123 180.686 1.00 2.98  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 160.081 205.116 181.597 1.00 6.76  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 159.792 204.835 182.915 1.00 10.45 ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 159.672 206.387 181.386 1.00 5.33  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 159.231 205.890 183.474 1.00 9.39  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 159.145 206.847 182.567 1.00 7.62  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 164.027 202.544 180.296 1.00 3.53  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 164.855 201.706 179.439 1.00 5.90  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 164.857 200.277 179.965 1.00 8.57  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 165.144 200.061 181.148 1.00 9.45  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 166.281 202.241 179.388 1.00 4.46  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 167.234 201.427 178.534 1.00 7.75  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 167.227 201.900 177.091 1.00 9.12  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 168.413 201.341 176.324 1.00 9.68  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 168.297 201.597 174.862 1.00 13.14 ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 164.526 199.286 179.137 1.00 6.24  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 164.636 197.894 179.584 1.00 7.93  ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 166.079 197.564 179.929 1.00 8.19  ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 167.009 198.025 179.268 1.00 13.33 ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 164.146 197.095 178.375 1.00 3.14  ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 164.415 197.988 177.217 1.00 2.42  ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 164.167 199.379 177.714 1.00 2.56  ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 166.265 196.763 180.974 1.00 5.30  ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 167.613 196.477 181.449 1.00 3.05  ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 167.713 195.017 181.863 1.00 5.49  ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 166.706 194.329 182.022 1.00 8.32  ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 168.012 197.405 182.606 1.00 4.77  ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 167.204 197.371 183.903 1.00 3.21  ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 167.838 196.434 184.912 1.00 6.24  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 167.082 198.765 184.479 1.00 3.53  ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 168.949 194.547 182.018 1.00 8.50  ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 169.234 193.168 182.390 1.00 5.58  ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 170.304 193.163 183.472 1.00 8.35  ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 171.307 193.878 183.366 1.00 14.88 ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 169.688 192.334 181.175 1.00 6.50  ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 170.251 190.999 181.621 1.00 7.36  ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 168.534 192.128 180.211 1.00 13.57 ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 170.078 192.375 184.521 1.00 7.80  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 171.071 192.123 185.561 1.00 0.00  ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 171.568 190.693 185.381 1.00 0.00  ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 170.809 189.735 185.540 1.00 8.16  ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 170.484 192.329 186.953 1.00 0.67  ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 169.828 193.668 187.281 1.00 2.05  ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 168.320 193.557 187.171 1.00 3.77  ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 170.232 194.119 188.668 1.00 0.46  ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 172.847 190.552 185.054 1.00 0.50  ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 173.466 189.249 184.868 1.00 0.00  ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 174.447 189.012 186.008 1.00 2.70  ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 175.177 189.926 186.403 1.00 11.13 ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 174.173 189.163 183.516 1.00 1.15  ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 174.811 187.525 183.118 1.00 9.18  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 174.449 187.798 186.544 1.00 0.00  ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 175.349 187.449 187.612 1.00 0.00  ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 175.062 186.068 188.158 1.00 4.56  ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 174.069 185.429 187.798 1.00 6.46  ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 175.928 185.581 189.038 1.00 7.64  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 175.717 184.264 189.639 1.00 3.01  ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 174.466 184.260 190.500 1.00 3.63  ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 174.072 185.306 191.035 1.00 5.64  ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 176.979 184.056 190.486 1.00 1.40  ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 177.979 185.020 189.937 1.00 2.99  ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 177.181 186.198 189.496 1.00 3.76  ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 173.804 183.115 190.638 1.00 1.88  ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 172.593 183.059 191.468 1.00 3.01  ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 172.895 183.422 192.914 1.00 1.40  ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 173.902 182.995 193.481 1.00 5.54  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 172.134 181.604 191.330 1.00 4.17  ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 173.347 180.857 190.892 1.00 3.52  ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 174.126 181.807 190.042 1.00 3.52  ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 172.006 184.212 193.510 1.00 0.21  ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 172.171 184.659 194.874 1.00 0.00  ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 173.103 185.836 195.059 1.00 2.53  ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 173.389 186.201 196.204 1.00 6.76  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 173.587 186.440 193.971 1.00 3.37  ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 174.541 187.538 194.097 1.00 1.80  ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 173.873 188.801 194.626 1.00 6.08  ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 174.508 189.601 195.323 1.00 8.64  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 175.210 187.807 192.751 1.00 0.60  ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 174.270 188.265 191.798 1.00 2.05  ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 172.598 189.003 194.307 1.00 2.17  ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 171.897 190.182 194.775 1.00 0.91  ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 171.221 190.982 193.682 1.00 3.53  ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 170.948 192.172 193.861 1.00 4.12  ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 170.954 190.345 192.541 1.00 2.92  ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 170.312 191.037 191.429 1.00 0.00  ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 168.906 191.499 191.801 1.00 0.54  ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 168.557 192.672 191.637 1.00 8.35  ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 170.273 190.124 190.202 1.00 0.00  ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 171.636 189.645 189.745 1.00 0.33  ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 171.519 188.724 188.546 1.00 2.02  ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 170.891 187.396 188.922 1.00 0.50  ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 171.733 186.635 189.882 1.00 0.00  ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 168.084 190.575 192.308 1.00 0.27  ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 166.724 190.929 192.704 1.00 1.18  ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 166.729 191.913 193.866 1.00 2.07  ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 165.930 192.858 193.894 1.00 6.54  ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 165.942 189.669 193.075 1.00 2.30  ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 166.012 188.729 191.997 1.00 8.29  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 164.491 190.005 193.349 1.00 4.25  ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 167.620 191.703 194.835 1.00 2.78  ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 167.717 192.611 195.973 1.00 0.48  ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 168.079 194.020 195.525 1.00 1.54  ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 167.451 194.996 195.953 1.00 5.36  ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 168.747 192.079 196.967 1.00 2.77  ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 168.923 192.935 198.200 1.00 4.64  ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 170.554 192.748 198.936 1.00 8.64  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 171.585 193.485 197.672 1.00 1.09  ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 169.085 194.146 194.656 1.00 3.35  ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 169.479 195.459 194.158 1.00 3.91  ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 168.374 196.100 193.331 1.00 2.04  ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 168.139 197.309 193.446 1.00 6.04  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 170.758 195.353 193.328 1.00 5.04  ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 171.758 194.652 194.075 1.00 10.35 ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 171.276 196.734 192.985 1.00 2.76  ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 167.689 195.318 192.495 1.00 0.45  ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 166.604 195.882 191.699 1.00 0.84  ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 165.478 196.401 192.582 1.00 2.60  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 164.944 197.487 192.335 1.00 8.00  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 166.068 194.846 190.715 1.00 2.34  ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 164.825 195.348 189.980 1.00 4.34  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 165.215 196.306 188.867 1.00 2.74  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 164.003 194.197 189.447 1.00 6.19  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 165.096 195.642 193.611 1.00 2.65  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 164.033 196.101 194.498 1.00 0.00  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 164.469 197.321 195.299 1.00 2.14  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 163.672 198.242 195.521 1.00 5.13  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 163.591 194.971 195.425 1.00 2.41  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 162.744 193.933 194.748 1.00 3.72  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 162.131 194.205 193.539 1.00 3.96  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 162.549 192.692 195.327 1.00 7.05  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 161.348 193.257 192.914 1.00 5.31  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 161.765 191.741 194.706 1.00 8.96  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 161.166 192.024 193.497 1.00 5.82  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 165.731 197.354 195.732 1.00 3.34  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 166.225 198.520 196.456 1.00 1.98  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 166.240 199.757 195.568 1.00 4.49  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 165.983 200.871 196.038 1.00 8.06  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 167.619 198.235 197.010 1.00 2.54  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 168.076 199.310 197.809 1.00 7.01  ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 166.546 199.584 194.280 1.00 4.92  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 166.515 200.713 193.356 1.00 3.29  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 165.085 201.150 193.061 1.00 1.81  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 164.805 202.348 192.959 1.00 8.29  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 167.243 200.355 192.061 1.00 1.55  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 164.170 200.189 192.916 1.00 2.88  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 162.771 200.510 192.660 1.00 1.58  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 162.102 201.165 193.856 1.00 4.50  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 161.110 201.880 193.681 1.00 7.67  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 162.004 199.246 192.269 1.00 1.28  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 162.091 198.806 190.806 1.00 0.08  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 161.645 197.363 190.659 1.00 0.00  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 161.257 199.716 189.924 1.00 5.39  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 162.611 200.929 195.068 1.00 9.71  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 162.079 201.615 196.240 1.00 8.50  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 162.247 203.125 196.146 1.00 8.62  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 161.496 203.863 196.795 1.00 12.84 ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 162.753 201.092 197.508 1.00 6.75  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 161.953 200.025 198.234 1.00 9.13  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 162.491 199.777 199.633 1.00 9.57  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 163.712 198.980 199.622 1.00 11.34 ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 163.738 197.655 199.605 1.00 13.13 ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 162.625 196.941 199.584 1.00 10.88 ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 164.912 197.029 199.610 1.00 10.84 ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 163.206 203.602 195.355 1.00 5.73  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 163.389 205.029 195.131 1.00 8.74  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 162.500 205.572 194.020 1.00 14.30 ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 162.558 206.772 193.732 1.00 18.06 ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 164.855 205.327 194.808 1.00 7.82  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 161.688 204.721 193.390 1.00 14.38 ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 160.779 205.112 192.314 1.00 13.59 ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 159.363 204.752 192.743 1.00 15.98 ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 158.883 203.640 192.467 1.00 14.16 ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 161.157 204.424 191.005 1.00 10.22 ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 162.467 204.878 190.362 1.00 5.88  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 163.075 203.760 189.536 1.00 7.50  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 162.242 206.112 189.508 1.00 12.97 ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 158.657 205.658 193.426 1.00 18.80 ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 157.336 205.305 193.968 1.00 21.48 ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 156.267 205.085 192.913 1.00 19.80 ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 155.271 204.412 193.201 1.00 18.61 ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 156.994 206.503 194.862 1.00 20.22 ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 157.755 207.637 194.272 1.00 20.45 ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 159.022 207.057 193.707 1.00 16.64 ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 156.434 205.624 191.705 1.00 17.30 ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 155.440 205.494 190.649 1.00 16.08 ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 155.662 204.263 189.783 1.00 15.94 ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 155.234 204.249 188.622 1.00 21.43 ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 155.430 206.751 189.776 1.00 18.56 ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 154.895 207.964 190.506 1.00 26.26 ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 154.054 207.791 191.414 1.00 26.02 ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 155.312 209.093 190.172 1.00 26.95 ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 156.317 203.233 190.312 1.00 15.96 ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 156.654 202.042 189.544 1.00 9.12  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 156.241 200.812 190.339 1.00 8.97  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 156.760 200.578 191.435 1.00 14.67 ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 158.151 202.005 189.228 1.00 6.07  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 158.494 202.499 187.835 1.00 8.08  ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 160.269 202.576 187.541 1.00 22.21 ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 160.377 204.072 186.562 1.00 8.44  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 155.318 200.033 189.785 1.00 3.42  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 154.861 198.792 190.395 1.00 5.84  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 155.497 197.620 189.664 1.00 6.48  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 155.368 197.505 188.443 1.00 7.63  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 153.335 198.682 190.351 1.00 7.87  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 152.813 197.259 190.490 1.00 10.95 ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 151.352 197.130 190.101 1.00 17.11 ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 150.586 196.505 190.864 1.00 15.52 ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 150.970 197.652 189.033 1.00 15.72 ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 156.177 196.754 190.409 1.00 6.12  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 156.937 195.650 189.835 1.00 1.79  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 156.109 194.373 189.922 1.00 4.30  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 155.474 194.098 190.948 1.00 11.53 ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 158.302 195.489 190.529 1.00 0.75  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 158.140 195.096 191.989 1.00 4.72  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 159.156 194.470 189.793 1.00 5.49  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 156.081 193.621 188.826 1.00 1.34  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 155.407 192.331 188.752 1.00 2.06  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 156.450 191.295 188.362 1.00 4.20  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 157.117 191.439 187.329 1.00 9.65  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 154.244 192.349 187.749 1.00 4.23  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 153.899 190.938 187.307 1.00 5.03  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 153.034 193.032 188.359 1.00 8.02  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 156.590 190.257 189.179 1.00 4.65  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 157.621 189.262 188.958 1.00 1.76  ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 157.178 188.066 188.143 1.00 3.82  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 156.203 187.392 188.488 1.00 9.40  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 157.891 187.797 187.054 1.00 2.71  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 157.687 186.616 186.229 1.00 2.78  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 158.914 185.723 186.338 1.00 1.81  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 160.047 186.211 186.369 1.00 8.51  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 157.454 186.995 184.764 1.00 2.13  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 156.191 187.782 184.423 1.00 6.19  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 156.486 189.267 184.348 1.00 5.48  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 155.618 187.285 183.112 1.00 7.90  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 158.687 184.417 186.400 1.00 2.96  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 159.760 183.443 186.573 1.00 3.88  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 159.833 182.582 185.320 1.00 4.36  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 159.040 181.651 185.146 1.00 6.41  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 159.530 182.605 187.822 1.00 6.07  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 159.135 183.448 189.012 1.00 10.00 ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 157.954 183.579 189.327 1.00 14.00 ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 160.124 184.029 189.679 1.00 7.53  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 160.785 182.899 184.449 1.00 3.42  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 160.954 182.153 183.214 1.00 0.00  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 161.512 180.763 183.496 1.00 3.22  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 162.281 180.554 184.437 1.00 11.33 ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 161.889 182.898 182.260 1.00 0.00  ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 161.242 184.048 181.540 1.00 0.00  ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 160.058 184.600 181.994 1.00 2.43  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 161.826 184.576 180.403 1.00 0.08  ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 159.472 185.654 181.329 1.00 1.57  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 161.242 185.630 179.734 1.00 2.37  ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 160.064 186.169 180.197 1.00 0.68  ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 161.107 179.807 182.669 1.00 0.94  ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 161.641 178.458 182.695 1.00 1.66  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 161.957 178.043 181.265 1.00 2.02  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 161.832 178.834 180.328 1.00 8.64  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 160.663 177.479 183.357 1.00 6.20  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 159.436 177.427 182.653 1.00 12.58 ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 162.375 176.788 181.094 1.00 0.95  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 162.689 176.303 179.757 1.00 0.63  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 161.455 176.267 178.866 1.00 7.24  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 161.570 176.417 177.645 1.00 12.59 ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 163.327 174.918 179.834 1.00 5.56  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 162.351 173.921 180.072 1.00 11.75 ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 160.274 176.084 179.451 1.00 7.67  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 159.031 175.984 178.700 1.00 5.53  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 158.292 177.313 178.603 1.00 5.12  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 157.119 177.329 178.223 1.00 5.51  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 158.121 174.929 179.328 1.00 7.52  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 158.947 178.419 178.941 1.00 7.79  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 158.286 179.715 178.918 1.00 2.73  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 158.052 180.174 177.484 1.00 6.27  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 158.953 180.116 176.643 1.00 11.87 ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 159.120 180.748 179.674 1.00 0.13  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 159.191 180.382 181.057 1.00 5.98  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 158.497 182.128 179.561 1.00 1.86  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 156.837 180.622 177.211 1.00 4.17  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 156.420 181.175 175.932 1.00 1.63  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 155.842 182.555 176.179 1.00 1.87  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 155.610 182.943 177.328 1.00 6.71  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 155.382 180.261 175.256 1.00 5.83  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 154.252 180.096 176.121 1.00 10.73 ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 155.985 178.902 174.946 1.00 5.85  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 155.607 183.346 175.114 1.00 1.87  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 154.973 184.659 175.303 1.00 3.14  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 153.616 184.593 175.989 1.00 6.96  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 153.068 185.624 176.390 1.00 8.97  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 154.839 185.188 173.871 1.00 0.38  ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 155.950 184.553 173.143 1.00 0.01  ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 156.131 183.191 173.744 1.00 3.72  ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 153.067 183.385 176.128 1.00 6.55  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 151.769 183.224 176.768 1.00 3.43  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 151.813 183.631 178.238 1.00 3.29  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 150.822 184.140 178.768 1.00 7.67  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 151.295 181.778 176.619 1.00 3.41  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 150.089 181.391 177.467 1.00 8.66  ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 148.793 182.047 177.008 1.00 17.12 ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 147.737 181.744 177.602 1.00 15.95 ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 148.816 182.850 176.052 1.00 13.15 ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 152.949 183.423 178.908 1.00 1.29  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 153.096 183.886 180.286 1.00 3.09  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 152.994 185.405 180.367 1.00 7.29  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 152.302 185.954 181.235 1.00 11.83 ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 154.432 183.403 180.851 1.00 4.87  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 154.635 183.407 182.367 1.00 6.35  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 154.040 182.159 182.993 1.00 10.87 ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 156.111 183.524 182.706 1.00 0.00  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 153.674 186.103 179.454 1.00 4.04  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 153.576 187.556 179.407 1.00 4.03  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 152.159 188.000 179.077 1.00 4.85  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 151.675 189.004 179.609 1.00 7.95  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 154.566 188.117 178.386 1.00 6.69  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 156.052 187.979 178.717 1.00 5.33  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 156.897 188.275 177.493 1.00 8.12  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 156.435 188.897 179.858 1.00 3.79  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 151.478 187.268 178.195 1.00 4.05  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 150.101 187.615 177.854 1.00 5.02  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 149.168 187.435 179.047 1.00 6.54  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 148.257 188.242 179.253 1.00 12.65 ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 149.631 186.783 176.663 1.00 7.56  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 150.363 187.063 175.349 1.00 3.79  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 149.797 186.219 174.224 1.00 2.15  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 150.292 188.539 175.005 1.00 5.49  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 149.374 186.379 179.839 1.00 4.30  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 148.594 186.203 181.062 1.00 1.28  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 148.855 187.332 182.051 1.00 7.41  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 147.921 187.851 182.679 1.00 14.44 ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 148.915 184.853 181.704 1.00 6.05  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 148.481 183.648 180.895 1.00 8.83  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 146.976 183.462 180.956 1.00 15.92 ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 146.573 182.069 180.509 1.00 14.72 ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 147.328 181.015 181.243 1.00 15.14 ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 150.121 187.722 182.209 1.00 7.27  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 150.437 188.840 183.094 1.00 6.59  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 149.775 190.126 182.608 1.00 5.80  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 149.271 190.918 183.412 1.00 7.42  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 151.952 189.012 183.199 1.00 6.60  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 152.508 187.891 183.892 1.00 8.87  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 152.298 190.285 183.956 1.00 7.21  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 149.767 190.347 181.292 1.00 4.87  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 149.102 191.519 180.732 1.00 6.47  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 147.601 191.474 180.983 1.00 7.65  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 146.991 192.488 181.343 1.00 12.71 ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 149.387 191.615 179.235 1.00 9.25  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 150.795 192.017 178.908 1.00 6.89  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 151.584 192.653 179.848 1.00 5.54  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 151.331 191.751 177.661 1.00 5.67  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 152.877 193.022 179.547 1.00 10.27 ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 152.623 192.117 177.354 1.00 4.43  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 153.399 192.753 178.300 1.00 8.37  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 146.985 190.309 180.788 1.00 5.28  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 145.559 190.147 181.041 1.00 6.81  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 145.199 190.363 182.502 1.00 9.99  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 144.082 190.810 182.785 1.00 13.71 ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 145.099 188.755 180.604 1.00 8.32  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 144.712 188.703 179.141 1.00 17.18 ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 143.766 189.419 178.750 1.00 16.81 ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 145.353 187.947 178.381 1.00 17.06 ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 146.103 190.058 183.427 1.00 9.19  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 145.834 190.281 184.841 1.00 7.15  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 146.079 191.717 185.283 1.00 7.06  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 145.212 192.315 185.927 1.00 8.40  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 146.680 189.336 185.700 1.00 8.15  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 146.349 189.385 187.159 1.00 14.30 ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 146.643 190.470 187.955 1.00 11.99 ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 145.736 188.485 187.963 1.00 17.51 ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 146.233 190.235 189.188 1.00 12.41 ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 145.677 189.036 189.219 1.00 16.86 ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 147.235 192.293 184.955 1.00 7.98  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 147.635 193.587 185.490 1.00 5.59  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 147.348 194.758 184.559 1.00 10.20 ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 147.447 195.909 184.996 1.00 12.00 ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 149.132 193.578 185.828 1.00 3.31  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 149.489 192.684 186.990 1.00 5.16  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 149.276 193.096 188.298 1.00 6.16  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 150.028 191.424 186.780 1.00 9.07  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 149.598 192.281 189.362 1.00 8.15  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 150.351 190.602 187.839 1.00 9.71  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 150.134 191.034 189.128 1.00 10.09 ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 150.456 190.216 190.186 1.00 13.63 ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 146.999 194.505 183.301 1.00 11.68 ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 146.799 195.566 182.327 1.00 7.39  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 145.453 195.387 181.640 1.00 13.26 ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 144.746 194.398 181.846 1.00 16.20 ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 147.924 195.589 181.284 1.00 7.40  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 149.590 195.581 181.971 1.00 22.39 ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 145.105 196.370 180.813 1.00 11.43 ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 143.860 196.358 180.064 1.00 7.96  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 144.103 196.908 178.667 1.00 11.38 ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 144.966 197.768 178.457 1.00 12.97 ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 142.770 197.176 180.769 1.00 9.58  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 143.148 198.626 181.013 1.00 16.41 ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 142.099 199.376 181.808 1.00 21.06 ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 141.085 198.754 182.189 1.00 20.20 ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 142.287 200.586 182.049 1.00 21.39 ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 143.325 196.397 177.716 1.00 10.18 ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 143.336 196.858 176.335 1.00 7.61  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 142.205 197.857 176.140 1.00 11.74 ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 141.065 197.592 176.535 1.00 16.36 ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 143.163 195.695 175.355 1.00 9.35  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 144.165 194.572 175.495 1.00 10.25 ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 144.019 193.603 176.477 1.00 12.63 ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 145.245 194.468 174.630 1.00 10.96 ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 144.928 192.572 176.603 1.00 13.18 ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 146.157 193.439 174.747 1.00 11.74 ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 145.994 192.494 175.735 1.00 12.95 ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 146.899 191.467 175.858 1.00 15.35 ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 142.517 198.998 175.534 1.00 10.44 ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 141.512 200.009 175.247 1.00 11.63 ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 141.630 200.458 173.798 1.00 13.94 ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 142.721 200.490 173.224 1.00 19.03 ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 141.634 201.216 176.191 1.00 14.21 ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 142.828 202.114 175.926 1.00 16.87 ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 142.752 203.380 176.763 1.00 16.51 ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 143.790 204.336 176.401 1.00 15.82 ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 144.997 204.375 176.950 1.00 16.83 ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 145.354 203.522 177.896 1.00 13.12 ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 145.867 205.294 176.540 1.00 16.17 ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 140.486 200.797 173.211 1.00 21.03 ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 140.425 201.269 171.836 1.00 22.09 ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 140.531 202.788 171.810 1.00 25.70 ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 139.801 203.481 172.526 1.00 29.88 ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 139.128 200.817 171.166 1.00 22.59 ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 139.190 199.430 170.545 1.00 25.47 ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 139.428 199.506 169.043 1.00 26.50 ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 139.479 198.186 168.429 1.00 27.00 ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 140.334 197.831 167.481 1.00 27.66 ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 141.227 198.682 167.002 1.00 24.72 ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 140.295 196.591 167.001 1.00 25.59 ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 141.436 203.295 170.989 1.00 23.99 ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 141.700 204.709 170.794 1.00 24.94 ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 141.710 204.973 169.298 1.00 27.20 ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 141.824 204.035 168.501 1.00 28.52 ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 143.047 205.117 171.413 1.00 24.04 ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 144.118 204.569 170.634 1.00 22.52 ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 143.161 204.615 172.843 1.00 22.38 ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 141.581 206.238 168.878 1.00 28.91 ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 141.607 206.536 167.439 1.00 27.46 ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 142.855 206.019 166.737 1.00 27.61 ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 142.823 205.747 165.533 1.00 29.19 ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 141.540 208.067 167.404 1.00 28.29 ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 140.795 208.426 168.633 1.00 28.54 ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 141.197 207.420 169.675 1.00 28.12 ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 143.956 205.877 167.474 1.00 29.01 ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 145.205 205.393 166.901 1.00 29.16 ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 145.362 203.878 166.965 1.00 27.91 ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 146.321 203.351 166.391 1.00 30.19 ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 146.393 206.057 167.599 1.00 28.89 ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 146.213 207.553 167.751 1.00 31.04 ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 145.364 208.012 168.514 1.00 31.10 ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 147.011 208.323 167.022 1.00 30.60 ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 144.465 203.164 167.635 1.00 22.18 ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 144.519 201.719 167.659 1.00 21.29 ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 144.256 201.188 169.051 1.00 22.55 ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 143.669 201.863 169.891 1.00 27.60 ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 144.688 199.957 169.291 1.00 14.77 ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 144.522 199.318 170.591 1.00 9.12  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 145.756 199.595 171.433 1.00 10.25 ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 146.888 199.393 170.979 1.00 18.26 ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 144.285 197.808 170.437 1.00 10.37 ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 144.220 197.143 171.801 1.00 11.37 ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 143.007 197.556 169.666 1.00 17.17 ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 145.542 200.063 172.659 1.00 10.56 ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 146.622 200.388 173.582 1.00 9.12  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 146.463 199.529 174.825 1.00 9.76  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 145.380 199.478 175.418 1.00 15.64 ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 146.627 201.884 173.945 1.00 8.85  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 147.647 202.161 175.032 1.00 8.40  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 146.918 202.724 172.714 1.00 11.73 ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 147.538 198.847 175.209 1.00 4.31  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 147.574 198.042 176.423 1.00 5.19  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 148.295 198.832 177.505 1.00 8.98  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 149.485 199.135 177.370 1.00 12.51 ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 148.274 196.708 176.176 1.00 4.44  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 148.444 195.796 177.389 1.00 4.48  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 147.119 195.168 177.769 1.00 7.81  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 149.479 194.729 177.104 1.00 5.69  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 147.577 199.155 178.576 1.00 10.48 ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 148.117 199.992 179.637 1.00 6.33  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 147.741 199.408 180.988 1.00 13.54 ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 146.719 198.724 181.105 1.00 17.77 ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 147.599 201.435 179.532 1.00 6.62  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 148.542 199.661 182.024 1.00 13.36 ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 148.206 199.140 183.353 1.00 12.59 ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 146.873 199.682 183.849 1.00 16.29 ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 146.471 200.801 183.523 1.00 14.40 ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 149.365 199.628 184.229 1.00 9.21  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 150.489 199.828 183.281 1.00 9.55  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 149.864 200.305 182.007 1.00 12.11 ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 146.182 198.859 184.639 1.00 18.99 ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 144.904 199.274 185.210 1.00 17.04 ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 145.098 200.467 186.136 1.00 19.76 ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 144.294 201.405 186.141 1.00 21.15 ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 144.232 198.095 185.936 1.00 16.63 ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 142.807 198.454 186.317 1.00 19.74 ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 144.255 196.854 185.062 1.00 16.35 ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 146.160 200.444 186.939 1.00 18.59 ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 146.480 201.581 187.790 1.00 21.08 ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 146.877 202.778 186.935 1.00 20.20 ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 147.669 202.649 185.997 1.00 21.89 ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 147.606 201.220 188.755 1.00 18.93 ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 147.132 200.635 190.071 1.00 20.80 ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 148.198 200.684 191.148 1.00 25.88 ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 148.968 199.738 191.318 1.00 23.65 ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 148.249 201.790 191.880 1.00 25.13 ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 146.326 203.943 187.258 1.00 20.01 ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 146.589 205.157 186.500 1.00 21.19 ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 147.809 205.875 187.059 1.00 23.42 ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 147.969 206.000 188.277 1.00 21.95 ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 145.377 206.089 186.528 1.00 24.91 ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 144.337 205.934 185.414 1.00 26.97 ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 144.968 206.199 184.053 1.00 23.97 ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 143.681 204.563 185.449 1.00 24.11 ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 148.667 206.346 186.160 1.00 22.19 ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 149.859 207.063 186.559 1.00 19.23 ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 150.989 206.199 187.064 1.00 19.21 ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 152.004 206.739 187.519 1.00 20.79 ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 150.852 204.879 186.999 1.00 18.71 ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 151.869 203.953 187.472 1.00 13.24 ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 152.487 203.219 186.293 1.00 12.10 ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 151.796 202.879 185.328 1.00 16.05 ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 151.275 202.943 188.457 1.00 10.97 ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 150.872 203.538 189.795 1.00 16.41 ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 151.958 203.340 190.838 1.00 18.96 ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 151.598 204.026 192.144 1.00 21.01 ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 151.440 205.496 191.974 1.00 20.54 ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 153.792 202.980 186.374 1.00 7.79  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 154.521 202.234 185.361 1.00 4.37  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 154.706 200.799 185.829 1.00 5.20  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 155.205 200.562 186.934 1.00 13.65 ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 155.880 202.876 185.077 1.00 5.98  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 155.829 203.950 184.042 1.00 6.20  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 155.352 205.217 184.200 1.00 7.73  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 156.270 203.855 182.684 1.00 5.32  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 155.468 205.917 183.024 1.00 7.53  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 156.029 205.101 182.076 1.00 8.10  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 156.845 202.833 181.922 1.00 4.20  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 156.342 205.356 180.745 1.00 9.62  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 157.155 203.089 180.600 1.00 4.48  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 156.904 204.338 180.026 1.00 6.36  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 154.303 199.848 184.993 1.00 3.55  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 154.443 198.435 185.312 1.00 0.95  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 155.822 197.951 184.886 1.00 2.67  ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 156.217 198.120 183.729 1.00 9.04  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 153.354 197.612 184.628 1.00 3.08  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 153.171 196.191 185.161 1.00 2.91  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 152.552 196.218 186.544 1.00 6.76  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 152.323 195.368 184.216 1.00 4.30  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 156.548 197.355 185.823 1.00 2.34  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 157.893 196.849 185.594 1.00 0.94  ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 157.799 195.329 185.606 1.00 1.84  ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 157.648 194.716 186.666 1.00 9.10  ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 158.883 197.355 186.646 1.00 0.00  ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 160.296 196.941 186.286 1.00 0.00  ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 158.778 198.859 186.797 1.00 1.46  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 157.886 194.713 184.432 1.00 0.00  ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 157.842 193.257 184.331 1.00 0.00  ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 159.241 192.720 184.594 1.00 1.58  ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 160.113 192.780 183.726 1.00 12.58 ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 157.328 192.826 182.962 1.00 3.43  ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 155.812 192.835 182.776 1.00 5.70  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 155.319 194.226 182.428 1.00 6.46  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 155.399 191.837 181.713 1.00 7.57  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 159.460 192.197 185.796 1.00 0.00  ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 160.766 191.681 186.191 1.00 1.71  ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 160.821 190.190 185.888 1.00 3.86  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 160.241 189.382 186.618 1.00 8.16  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 161.026 191.951 187.671 1.00 0.00  ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 162.260 191.282 188.197 1.00 3.77  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 163.469 191.413 187.537 1.00 4.60  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 162.212 190.522 189.351 1.00 4.25  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 164.606 190.803 188.020 1.00 2.82  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 163.346 189.907 189.837 1.00 6.32  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 164.544 190.049 189.170 1.00 4.44  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 161.520 189.825 184.817 1.00 1.03  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 161.686 188.435 184.417 1.00 0.00  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 162.996 187.918 184.999 1.00 1.59  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 164.050 188.530 184.800 1.00 10.30 ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 161.675 188.307 182.896 1.00 3.13  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 160.239 189.068 182.101 1.00 12.75 ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 162.931 186.794 185.710 1.00 0.81  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 164.051 186.360 186.535 1.00 3.19  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 164.992 185.381 185.845 1.00 7.41  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 166.114 185.189 186.324 1.00 11.92 ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 163.531 185.726 187.828 1.00 2.20  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 164.547 185.772 188.951 1.00 11.10 ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 165.600 186.422 188.781 1.00 9.46  ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 164.294 185.156 190.008 1.00 13.88 ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 164.570 184.741 184.759 1.00 0.03  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 165.388 183.729 184.089 1.00 0.22  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 165.330 183.908 182.573 1.00 5.43  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 165.052 182.970 181.829 1.00 9.34  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 164.952 182.323 184.488 1.00 2.85  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 164.995 182.045 185.984 1.00 6.59  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 166.393 181.742 186.487 1.00 12.93 ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 167.324 181.665 185.659 1.00 15.44 ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 166.561 181.577 187.712 1.00 14.20 ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 165.597 185.131 182.104 1.00 3.22  ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 165.329 185.492 180.711 1.00 0.38  ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 166.036 184.571 179.722 1.00 3.25  ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 165.541 184.357 178.609 1.00 9.42  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 165.714 186.962 180.456 1.00 0.00  ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 167.073 187.274 181.080 1.00 4.05  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 164.646 187.897 180.982 1.00 1.66  ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 167.664 188.576 180.611 1.00 8.29  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 167.189 184.014 180.090 1.00 1.93  ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 167.963 183.197 179.164 1.00 0.00  ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 167.721 181.701 179.335 1.00 2.33  ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 168.400 180.899 178.687 1.00 9.44  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 169.455 183.508 179.295 1.00 0.00  ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 169.949 183.422 180.720 1.00 4.31  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 169.197 183.092 181.634 1.00 12.28 ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 171.229 183.717 180.917 1.00 4.90  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 166.779 181.307 180.185 1.00 0.66  ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 166.399 179.903 180.330 1.00 0.83  ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 165.493 179.382 179.214 1.00 5.20  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 165.681 178.237 178.785 1.00 9.43  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 165.722 179.656 181.680 1.00 1.10  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 166.637 179.212 182.818 1.00 1.18  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 165.829 178.927 184.067 1.00 7.89  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 167.419 177.982 182.405 1.00 4.03  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 164.475 180.161 178.735 1.00 0.00  ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 163.552 179.631 177.717 1.00 0.00  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 164.206 178.844 176.591 1.00 3.27  ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 165.298 179.183 176.128 1.00 8.88  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 162.882 180.898 177.184 1.00 0.24  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 162.802 181.765 178.367 1.00 0.00  ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 164.015 181.481 179.210 1.00 0.71  ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 163.527 177.784 176.158 1.00 4.26  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 164.110 176.840 175.215 1.00 1.58  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 164.460 177.516 173.897 1.00 3.23  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 163.669 178.284 173.344 1.00 10.29 ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 163.143 175.683 174.963 1.00 4.80  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 163.424 174.487 175.847 1.00 11.60 ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 164.606 174.252 176.171 1.00 11.46 ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 162.463 173.780 176.217 1.00 9.78  ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 165.658 177.225 173.404 1.00 3.12  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 166.092 177.650 172.083 1.00 0.59  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 165.832 176.508 171.109 1.00 2.99  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 166.281 175.382 171.341 1.00 12.94 ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 167.573 178.022 172.105 1.00 0.30  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 168.000 178.992 171.030 1.00 3.86  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 169.587 179.762 171.398 1.00 15.25 ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 169.072 181.420 171.825 1.00 5.38  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 165.107 176.790 170.029 1.00 2.19  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 164.764 175.732 169.090 1.00 4.78  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 166.005 175.323 168.300 1.00 7.80  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 167.116 175.813 168.527 1.00 8.35  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 163.642 176.179 168.156 1.00 4.24  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 163.964 177.463 167.425 1.00 7.77  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 164.687 178.303 167.987 1.00 12.88 ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 163.476 177.641 166.290 1.00 9.53  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 165.814 174.409 167.349 1.00 4.72  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 166.928 173.946 166.535 1.00 7.19  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 167.481 175.032 165.624 1.00 8.86  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 168.547 174.835 165.031 1.00 13.91 ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 166.503 172.733 165.706 1.00 4.94  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 165.184 172.913 164.984 1.00 10.22 ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 164.967 171.829 163.943 1.00 8.95  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 164.642 170.496 164.590 1.00 9.65  ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 164.333 169.452 163.574 1.00 12.87 ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 166.789 176.165 165.498 1.00 6.58  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 167.229 177.273 164.661 1.00 7.38  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 167.683 178.479 165.480 1.00 6.11  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 167.722 179.596 164.957 1.00 10.81 ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 166.115 177.666 163.695 1.00 5.71  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 165.571 176.498 162.907 1.00 4.90  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 166.304 175.930 161.876 1.00 5.94  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 164.326 175.960 163.197 1.00 4.19  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 165.812 174.861 161.154 1.00 7.31  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 163.824 174.896 162.479 1.00 6.67  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 164.572 174.349 161.460 1.00 9.72  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 164.077 173.286 160.745 1.00 12.16 ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 168.024 178.272 166.749 1.00 4.89  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 168.618 179.314 167.564 1.00 5.38  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 167.746 180.520 167.851 1.00 3.30  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 168.203 181.659 167.717 1.00 8.57  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 166.494 180.296 168.248 1.00 1.08  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 165.582 181.390 168.554 1.00 2.05  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 164.784 181.068 169.810 1.00 4.24  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 164.253 179.963 169.946 1.00 7.86  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 164.629 181.656 167.383 1.00 5.18  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 165.382 182.094 166.245 1.00 9.06  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 163.610 182.722 167.744 1.00 3.08  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 164.703 182.028 170.722 1.00 8.04  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 163.820 181.934 171.877 1.00 3.32  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 162.584 182.777 171.594 1.00 5.17  ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 162.688 183.994 171.410 1.00 7.79  ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 164.528 182.401 173.147 1.00 0.00  ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 165.662 181.493 173.586 1.00 2.07  ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 166.655 182.189 174.490 1.00 4.22  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 167.287 183.169 174.099 1.00 9.73  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 166.801 181.685 175.708 1.00 1.40  ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 161.418 182.127 171.553 1.00 2.45  ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 160.203 182.809 171.118 1.00 1.19  ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 159.834 183.951 172.053 1.00 3.28  ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 159.433 185.029 171.599 1.00 8.57  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 159.050 181.814 171.008 1.00 3.62  ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 157.737 182.444 170.580 1.00 2.46  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 156.615 181.424 170.536 1.00 2.85  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 156.860 180.385 169.546 1.00 7.19  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 156.081 179.329 169.363 1.00 9.93  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 154.993 179.138 170.092 1.00 7.43  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 156.402 178.442 168.427 1.00 8.38  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 159.956 183.740 173.365 1.00 5.46  ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 159.634 184.808 174.305 1.00 2.11  ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 160.652 185.939 174.205 1.00 1.98  ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 160.304 187.112 174.382 1.00 7.52  ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 159.520 184.254 175.737 1.00 0.65  ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 160.870 183.817 176.257 1.00 2.93  ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 158.899 185.289 176.658 1.00 0.00  ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 161.915 185.620 173.913 1.00 2.60  ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 162.912 186.669 173.727 1.00 3.19  ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 162.600 187.482 172.479 1.00 3.69  ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 162.742 188.708 172.473 1.00 4.86  ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 164.325 186.061 173.681 1.00 4.20  ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 164.679 185.448 175.037 1.00 3.37  ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 165.352 187.115 173.298 1.00 2.83  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 164.492 186.394 176.198 1.00 2.72  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 162.158 186.819 171.408 1.00 3.29  ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 161.721 187.541 170.216 1.00 1.13  ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 160.508 188.411 170.516 1.00 5.14  ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 160.401 189.535 170.014 1.00 8.24  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 161.408 186.557 169.091 1.00 1.65  ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 162.573 185.868 168.676 1.00 6.71  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 159.584 187.905 171.333 1.00 4.66  ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 158.408 188.681 171.719 1.00 0.00  ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 158.803 189.936 172.489 1.00 1.25  ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 158.298 191.032 172.217 1.00 7.98  ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 157.476 187.800 172.552 1.00 1.37  ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 156.131 188.408 172.820 1.00 6.20  ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 155.235 188.621 171.790 1.00 6.74  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 155.756 188.743 174.109 1.00 2.71  ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 153.996 189.169 172.039 1.00 3.77  ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 154.517 189.292 174.362 1.00 0.00  ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 153.638 189.506 173.327 1.00 2.31  ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 159.719 189.795 173.449 1.00 1.01  ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 160.156 190.944 174.241 1.00 1.58  ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 160.936 191.922 173.370 1.00 5.29  ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 160.824 193.144 173.523 1.00 11.19 ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 160.983 190.481 175.453 1.00 0.73  ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 160.147 189.574 176.355 1.00 0.83  ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 161.485 191.673 176.245 1.00 0.77  ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 160.931 188.951 177.482 1.00 2.71  ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 161.738 191.400 172.441 1.00 2.84  ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 162.480 192.264 171.531 1.00 0.12  ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 161.538 193.049 170.629 1.00 3.09  ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 161.785 194.221 170.334 1.00 4.98  ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 163.463 191.430 170.709 1.00 0.72  ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 164.386 192.235 169.814 1.00 2.12  ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 163.894 192.256 168.381 1.00 6.90  ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 164.811 192.968 167.502 1.00 11.03 ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 164.558 193.257 166.234 1.00 10.48 ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 163.432 192.883 165.651 1.00 8.62  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 165.460 193.935 165.532 1.00 13.52 ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 160.460 192.414 170.169 1.00 5.55  ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 159.461 193.128 169.383 1.00 1.67  ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 158.748 194.181 170.221 1.00 1.97  ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 158.491 195.294 169.749 1.00 5.70  ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 158.457 192.140 168.792 1.00 0.00  ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 157.240 192.791 168.167 1.00 2.94  ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 156.192 191.782 167.758 1.00 6.79  ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 155.708 191.007 168.582 1.00 6.54  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 155.833 191.787 166.482 1.00 10.76 ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 158.422 193.848 171.469 1.00 4.76  ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 157.729 194.784 172.346 1.00 0.00  ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 158.600 195.956 172.774 1.00 2.27  ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 158.064 197.016 173.115 1.00 4.87  ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 157.204 194.045 173.577 1.00 0.19  ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 155.929 193.266 173.311 1.00 6.12  ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 155.080 192.760 174.813 1.00 19.82 ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 156.415 191.946 175.681 1.00 6.60  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 159.917 195.793 172.774 1.00 6.83  ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 160.822 196.889 173.113 1.00 5.68  ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 161.190 197.709 171.884 1.00 5.22  ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 161.077 198.937 171.885 1.00 9.08  ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 162.081 196.335 173.813 1.00 1.78  ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 163.139 197.413 173.909 1.00 7.56  ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 161.730 195.806 175.192 1.00 0.82  ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 161.641 197.041 170.820 1.00 2.95  ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 162.051 197.735 169.604 1.00 0.35  ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 160.879 198.415 168.910 1.00 7.73  ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 161.004 199.564 168.471 1.00 13.79 ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 162.735 196.748 168.658 1.00 2.47  ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 162.701 197.140 167.191 1.00 10.73 ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 163.843 198.054 166.801 1.00 16.71 ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 164.649 198.417 167.681 1.00 21.30 ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 163.936 198.413 165.608 1.00 13.99 ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 159.739 197.735 168.802 1.00 5.10  ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 158.586 198.257 168.083 1.00 0.97  ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 157.526 198.853 168.998 1.00 5.68  ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 156.568 199.453 168.503 1.00 11.44 ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 157.964 197.157 167.218 1.00 1.85  ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 158.877 196.642 166.150 1.00 6.65  ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 159.715 197.462 165.429 1.00 8.56  ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 159.092 195.387 165.690 1.00 7.58  ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 160.403 196.738 164.566 1.00 8.99  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 160.045 195.475 164.705 1.00 7.59  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 157.667 198.705 170.312 1.00 5.78  ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 156.729 199.317 171.235 1.00 1.75  ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 155.367 198.661 171.280 1.00 1.83  ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 154.386 199.316 171.644 1.00 10.55 ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 155.277 197.388 170.921 1.00 1.96  ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 153.998 196.709 170.958 1.00 1.03  ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 154.111 195.304 170.410 1.00 4.31  ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 155.206 194.811 170.134 1.00 12.74 ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 152.956 194.666 170.254 1.00 9.40  ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 152.895 193.300 169.747 1.00 4.91  ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 151.615 193.138 168.934 1.00 6.62  ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 150.943 194.115 168.598 1.00 10.88 ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 152.992 192.288 170.895 1.00 4.63  ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 151.872 192.384 171.894 1.00 5.01  ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 151.946 193.268 172.954 1.00 7.08  ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 150.755 191.577 171.780 1.00 3.23  ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 150.922 193.353 173.872 1.00 7.07  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 149.730 191.660 172.696 1.00 1.73  ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 149.813 192.548 173.743 1.00 3.66  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 151.283 191.892 168.605 1.00 7.40  ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 150.104 191.567 167.814 1.00 6.10  ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 149.176 190.673 168.622 1.00 12.56 ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 149.602 189.632 169.131 1.00 15.57 ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 150.489 190.865 166.510 1.00 6.70  ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 150.712 191.789 165.335 1.00 8.83  ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 149.647 192.419 164.710 1.00 7.30  ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 151.989 192.020 164.842 1.00 9.48  ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 149.846 193.257 163.634 1.00 9.49  ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 152.197 192.857 163.766 1.00 7.27  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 151.123 193.473 163.165 1.00 10.99 ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 151.325 194.310 162.094 1.00 14.66 ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 147.913 191.076 168.736 1.00 8.84  ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 146.874 190.204 169.263 1.00 4.77  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 146.464 189.224 168.174 1.00 10.03 ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 145.963 189.632 167.118 1.00 16.87 ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 145.667 191.012 169.734 1.00 3.10  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 145.694 191.373 171.203 1.00 12.76 ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 144.317 191.781 171.689 1.00 15.22 ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 143.705 192.779 170.819 1.00 14.74 ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 142.591 193.438 171.105 1.00 11.90 ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 141.950 193.250 172.246 1.00 10.18 ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 142.110 194.313 170.226 1.00 12.17 ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 146.686 187.936 168.434 1.00 8.34  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 146.371 186.880 167.485 1.00 8.92  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 144.909 186.464 167.526 1.00 9.08  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 144.492 185.647 166.699 1.00 14.66 ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 147.260 185.662 167.746 1.00 8.07  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 147.120 185.253 169.112 1.00 11.14 ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 148.716 186.002 167.473 1.00 6.84  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 144.129 186.986 168.474 1.00 4.92  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 142.690 186.764 168.438 1.00 8.83  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 142.063 187.454 167.234 1.00 9.10  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 141.180 186.893 166.578 1.00 13.06 ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 142.050 187.252 169.735 1.00 9.20  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 141.846 188.654 169.706 1.00 10.58 ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 142.512 188.674 166.928 1.00 4.06  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 142.018 189.418 165.777 1.00 3.68  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 143.143 190.014 164.935 1.00 9.57  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 142.869 190.852 164.071 1.00 11.95 ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 141.060 190.527 166.228 1.00 6.49  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 141.625 191.358 167.360 1.00 13.61 ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 142.711 191.010 167.867 1.00 14.88 ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 140.983 192.357 167.745 1.00 16.63 ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 144.391 189.597 165.163 1.00 10.83 ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 145.548 190.076 164.402 1.00 5.77  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 145.648 191.599 164.443 1.00 5.64  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 145.854 192.258 163.422 1.00 11.19 ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 145.505 189.576 162.956 1.00 7.20  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 145.886 188.120 162.768 1.00 9.89  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 144.806 187.166 163.215 1.00 9.38  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 145.025 186.334 164.094 1.00 11.11 ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 143.632 187.273 162.608 1.00 8.90  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 145.503 192.162 165.637 1.00 5.06  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 145.457 193.609 165.812 1.00 8.96  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 146.726 194.093 166.499 1.00 11.97 ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 147.137 193.529 167.514 1.00 17.24 ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 144.230 194.024 166.627 1.00 13.52 ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 143.040 193.662 165.915 1.00 17.34 ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 144.228 195.523 166.867 1.00 11.78 ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 147.347 195.131 165.944 1.00 8.10  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 148.531 195.696 166.574 1.00 7.27  ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 148.150 196.390 167.876 1.00 10.57 ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 147.307 197.292 167.891 1.00 11.34 ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 149.223 196.683 165.637 1.00 7.67  ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 150.441 197.308 166.241 1.00 9.08  ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 150.547 198.568 166.751 1.00 10.21 ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 151.726 196.699 166.407 1.00 5.63  ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 151.819 198.783 167.222 1.00 6.21  ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 152.562 197.650 167.023 1.00 7.68  ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 152.251 195.443 166.093 1.00 4.63  ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 153.893 197.384 167.330 1.00 8.37  ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 153.571 195.181 166.400 1.00 3.71  ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 154.377 196.146 167.011 1.00 7.12  ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 148.775 195.964 168.970 1.00 11.34 ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 148.534 196.512 170.298 1.00 9.15  ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 149.795 197.236 170.741 1.00 9.37  ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 150.886 196.655 170.731 1.00 13.51 ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 148.152 195.411 171.304 1.00 8.34  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 148.055 195.984 172.698 1.00 11.45 ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 146.848 194.760 170.898 1.00 14.25 ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 149.643 198.498 171.129 1.00 7.45  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 150.762 199.341 171.524 1.00 3.92  ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 150.869 199.378 173.041 1.00 7.08  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 149.884 199.663 173.729 1.00 16.45 ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 150.590 200.756 170.970 1.00 5.64  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 151.416 201.807 171.686 1.00 9.74  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 151.462 203.101 170.896 1.00 11.89 ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 151.750 204.286 171.802 1.00 12.52 ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 150.653 204.512 172.781 1.00 17.59 ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 152.056 199.077 173.556 1.00 6.11  ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 152.277 199.117 174.995 1.00 4.02  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 152.321 200.556 175.487 1.00 6.05  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 152.817 201.451 174.798 1.00 8.72  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 153.580 198.407 175.355 1.00 4.96  ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 153.687 196.924 175.010 1.00 2.61  ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 154.938 196.335 175.631 1.00 4.06  ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 152.455 196.181 175.479 1.00 5.24  ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 151.803 200.777 176.693 1.00 4.65  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 151.867 202.088 177.324 1.00 6.43  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 152.154 201.904 178.804 1.00 7.09  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 151.542 201.052 179.452 1.00 14.08 ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 150.560 202.862 177.123 1.00 9.20  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 150.656 204.342 177.444 1.00 12.05 ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 149.317 204.944 177.808 1.00 17.18 ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 148.354 204.760 177.036 1.00 15.10 ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 149.224 205.602 178.866 1.00 16.09 ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 153.085 202.703 179.328 1.00 4.25  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 153.450 202.672 180.747 1.00 5.22  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 153.901 201.280 181.186 1.00 5.64  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 153.560 200.814 182.275 1.00 6.47  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 152.299 203.171 181.621 1.00 5.81  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 152.140 204.680 181.635 1.00 5.47  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 151.067 205.115 182.616 1.00 8.26  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 149.728 204.784 182.144 1.00 10.00 ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 148.901 203.951 182.760 1.00 13.56 ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 149.245 203.334 183.876 1.00 10.50 ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 147.697 203.731 182.240 1.00 15.59 ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 154.674 200.611 180.335 1.00 5.55  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 155.201 199.280 180.616 1.00 2.57  ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 156.675 199.253 180.237 1.00 5.32  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 157.044 199.678 179.138 1.00 9.47  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 154.425 198.188 179.854 1.00 2.96  ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 153.027 198.010 180.446 1.00 3.16  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 155.182 196.872 179.881 1.00 3.17  ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 152.109 197.172 179.593 1.00 2.25  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 157.514 198.754 181.145 1.00 2.76  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 158.941 198.603 180.903 1.00 4.20  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 159.384 197.213 181.337 1.00 3.37  ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 158.641 196.477 181.990 1.00 2.90  ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 159.755 199.678 181.630 1.00 4.03  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 159.395 199.848 183.086 1.00 2.65  ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 160.373 200.737 183.814 1.00 3.81  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 161.512 200.909 183.383 1.00 8.75  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 159.932 201.317 184.919 1.00 3.47  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 160.615 196.855 180.973 1.00 5.12  ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 161.104 195.494 181.145 1.00 0.00  ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 162.437 195.477 181.876 1.00 3.01  ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 163.396 196.146 181.466 1.00 9.07  ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 161.239 194.790 179.794 1.00 3.44  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 159.946 194.673 179.047 1.00 8.15  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 159.127 193.573 179.226 1.00 4.35  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 159.543 195.669 178.176 1.00 8.04  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 157.935 193.465 178.544 1.00 3.97  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 158.352 195.567 177.492 1.00 6.72  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 157.546 194.467 177.678 1.00 5.65  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 162.490 194.693 182.948 1.00 1.48  ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 163.722 194.364 183.652 1.00 1.14  ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 163.864 192.850 183.647 1.00 2.16  ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 162.905 192.132 183.947 1.00 4.95  ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 163.723 194.909 185.089 1.00 0.00  ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 164.935 194.399 185.839 1.00 2.69  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 163.704 196.423 185.078 1.00 4.00  ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 165.045 192.369 183.285 1.00 2.57  ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 165.331 190.951 183.281 1.00 0.61  ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 166.493 190.639 184.202 1.00 3.09  ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 167.341 191.489 184.466 1.00 12.11 ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 166.514 189.412 184.704 1.00 0.11  ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 167.627 188.911 185.493 1.00 0.00  ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 168.042 187.560 184.940 1.00 1.73  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 167.216 186.808 184.417 1.00 7.97  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 167.269 188.788 186.977 1.00 0.00  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 169.335 187.265 185.033 1.00 0.00  ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 169.822 186.005 184.494 1.00 1.48  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 171.173 185.670 185.100 1.00 4.94  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 171.861 186.528 185.656 1.00 6.98  ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 169.926 186.055 182.967 1.00 2.38  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 170.797 187.498 182.337 1.00 12.28 ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 171.527 184.403 184.994 1.00 4.59  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 172.856 183.890 185.266 1.00 0.93  ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 173.712 184.002 184.012 1.00 4.66  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 173.184 184.164 182.908 1.00 9.82  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 172.768 182.438 185.730 1.00 0.77  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 171.999 182.291 187.025 1.00 3.32  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 171.836 183.251 187.774 1.00 4.11  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 171.523 181.084 187.296 1.00 5.67  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 175.036 183.942 184.144 1.00 4.37  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 175.902 184.052 182.966 1.00 3.82  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 175.561 182.994 181.933 1.00 5.21  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 175.213 181.859 182.287 1.00 5.29  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 177.306 183.837 183.544 1.00 4.69  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 177.198 184.319 184.939 1.00 3.70  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 175.814 183.958 185.395 1.00 3.85  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 175.637 183.335 180.645 1.00 6.99  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 175.235 182.373 179.605 1.00 3.97  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 176.073 181.111 179.581 1.00 6.78  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 175.642 180.110 178.997 1.00 11.07 ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 175.390 183.173 178.304 1.00 5.85  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 176.335 184.278 178.644 1.00 4.62  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 176.070 184.621 180.074 1.00 4.94  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 177.258 181.126 180.191 1.00 7.04  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 178.090 179.935 180.272 1.00 6.60  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 177.595 178.935 181.307 1.00 10.23 ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 178.100 177.808 181.346 1.00 15.88 ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 179.534 180.328 180.589 1.00 10.68 ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 179.572 181.060 181.819 1.00 9.56  ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 180.100 181.193 179.478 1.00 6.77  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 176.631 179.313 182.142 1.00 6.80  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 176.071 178.385 183.106 1.00 6.25  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 175.248 177.312 182.392 1.00 8.87  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 174.697 177.557 181.317 1.00 8.01  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 175.198 179.124 184.117 1.00 6.73  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 176.010 179.800 185.202 1.00 11.12 ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 177.248 179.880 185.057 1.00 10.03 ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 175.411 180.248 186.202 1.00 12.28 ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 175.164 176.110 182.961 1.00 6.82  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 174.384 175.048 182.316 1.00 7.15  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 172.909 175.411 182.230 1.00 6.89  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 172.311 175.904 183.188 1.00 5.50  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 174.615 173.834 183.225 1.00 7.81  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 175.046 174.406 184.528 1.00 11.30 ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 175.814 175.644 184.198 1.00 8.49  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 172.323 175.155 181.062 1.00 6.72  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 170.932 175.457 180.815 1.00 5.18  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 170.647 176.874 180.368 1.00 6.25  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 169.495 177.177 180.034 1.00 9.71  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 171.649 177.745 180.341 1.00 4.32  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 171.472 179.133 179.943 1.00 2.49  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 171.960 179.331 178.515 1.00 6.62  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 173.004 178.799 178.125 1.00 10.05 ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 172.221 180.076 180.886 1.00 1.19  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 172.038 179.752 182.357 1.00 2.70  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 170.585 179.874 182.764 1.00 4.30  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 170.405 179.761 184.206 1.00 7.98  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 170.363 178.614 184.869 1.00 7.45  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 170.500 177.453 184.252 1.00 7.03  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 170.176 178.632 186.185 1.00 5.71  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 171.202 180.100 177.742 1.00 3.73  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 171.530 180.363 176.354 1.00 3.44  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 171.935 181.821 176.167 1.00 3.60  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 171.454 182.703 176.885 1.00 4.68  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 170.340 180.054 175.437 1.00 5.59  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 170.313 178.634 174.907 1.00 5.06  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 169.779 177.668 175.948 1.00 5.79  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 168.346 177.994 176.317 1.00 2.30  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 167.802 177.031 177.313 1.00 1.01  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 172.823 182.111 175.217 1.00 4.36  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 173.185 183.509 174.953 1.00 2.40  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 172.029 184.251 174.299 1.00 5.73  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 171.428 183.769 173.336 1.00 10.97 ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 174.391 183.395 174.015 1.00 3.02  ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 174.229 182.070 173.360 1.00 3.22  ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 173.588 181.174 174.377 1.00 4.63  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 171.718 185.430 174.832 1.00 5.01  ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 170.628 186.227 174.294 1.00 3.52  ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 170.987 186.762 172.913 1.00 6.95  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 172.160 186.957 172.582 1.00 10.96 ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 170.295 187.383 175.236 1.00 2.41  ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 169.683 186.991 176.582 1.00 4.61  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 169.729 188.157 177.553 1.00 3.53  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 168.260 186.497 176.402 1.00 1.87  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 169.960 186.993 172.101 1.00 5.42  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 170.171 187.482 170.746 1.00 5.54  ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 170.801 188.866 170.767 1.00 7.11  ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 170.521 189.681 171.651 1.00 12.90 ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 168.845 187.518 169.986 1.00 7.05  ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 169.026 188.001 168.668 1.00 10.99 ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 171.670 189.127 169.788 1.00 5.62  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 172.301 190.440 169.691 1.00 4.59  ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 171.274 191.522 169.392 1.00 5.49  ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 171.411 192.662 169.851 1.00 8.78  ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 173.389 190.421 168.620 1.00 8.94  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 174.665 189.783 169.070 1.00 10.73 ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 175.754 189.631 168.240 1.00 12.53 ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 175.028 189.260 170.265 1.00 11.47 ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 176.732 189.042 168.902 1.00 12.27 ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 176.316 188.806 170.134 1.00 11.86 ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 170.238 191.185 168.624 1.00 6.44  ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 169.171 192.144 168.359 1.00 6.21  ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 168.431 192.506 169.639 1.00 9.81  ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 168.043 193.664 169.834 1.00 13.09 ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 168.208 191.578 167.316 1.00 4.15  ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 168.883 191.198 166.012 1.00 5.72  ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 167.872 190.758 164.974 1.00 9.08  ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 167.582 191.817 164.015 1.00 5.70  ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 166.692 191.717 163.039 1.00 4.55  ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 165.987 190.614 162.856 1.00 9.04  ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 166.503 192.751 162.226 1.00 3.00  ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 168.215 191.528 170.518 1.00 7.52  ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 167.618 191.818 171.817 1.00 1.01  ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 168.591 192.577 172.712 1.00 4.82  ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 168.212 193.549 173.374 1.00 16.34 ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 167.170 190.524 172.493 1.00 4.15  ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 166.637 190.721 173.883 1.00 6.83  ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 165.484 191.456 174.098 1.00 8.39  ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 167.294 190.182 174.973 1.00 8.66  ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 164.995 191.642 175.375 1.00 4.91  ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 166.809 190.366 176.250 1.00 8.07  ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 165.658 191.096 176.451 1.00 6.58  ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 169.855 192.145 172.742 1.00 8.07  ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 170.838 192.780 173.614 1.00 5.09  ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 171.115 194.220 173.207 1.00 7.98  ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 171.601 195.008 174.023 1.00 20.14 ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 172.137 191.975 173.617 1.00 9.93  ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 172.140 190.696 174.452 1.00 8.54  ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 173.535 190.102 174.508 1.00 9.66  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 171.619 190.975 175.849 1.00 11.88 ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 170.821 194.578 171.956 1.00 7.82  ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 171.029 195.951 171.510 1.00 8.03  ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 170.187 196.941 172.308 1.00 9.10  ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 170.624 198.071 172.553 1.00 11.98 ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 170.717 196.053 170.016 1.00 9.54  ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 170.496 197.460 169.503 1.00 12.51 ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 170.078 197.449 168.046 1.00 11.94 ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 169.667 198.773 167.592 1.00 9.15  ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 168.500 199.040 167.027 1.00 13.32 ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 167.609 198.090 166.796 1.00 18.04 ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 168.220 200.292 166.679 1.00 17.68 ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 168.996 196.536 172.738 1.00 9.55  ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 168.070 197.423 173.427 1.00 8.67  ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 168.164 197.349 174.945 1.00 10.07 ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 167.524 198.154 175.626 1.00 10.20 ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 166.634 197.117 172.998 1.00 8.63  ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 166.433 197.119 171.516 1.00 7.69  ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 166.266 195.963 170.786 1.00 11.10 ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 166.355 198.139 170.629 1.00 7.38  ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 166.108 196.268 169.511 1.00 12.27 ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 166.156 197.583 169.389 1.00 13.37 ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 168.935 196.415 175.496 1.00 14.48 ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 168.969 196.237 176.947 1.00 12.30 ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 170.391 196.391 177.481 1.00 8.09  ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 171.268 195.570 177.175 1.00 12.73 ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 168.356 194.884 177.352 1.00 8.98  ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 166.860 194.896 177.106 1.00 12.18 ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 168.983 193.740 176.579 1.00 12.23 ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 170.673 197.440 178.249 1.00 2.23  ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 171.939 197.490 178.988 1.00 5.78  ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 172.015 196.369 180.012 1.00 9.33  ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 171.028 196.037 180.670 1.00 16.45 ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 171.902 198.864 179.664 1.00 4.49  ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 170.471 199.280 179.635 1.00 4.46  ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 169.905 198.686 178.391 1.00 6.07  ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 173.211 195.809 180.167 1.00 7.50  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 173.453 194.685 181.062 1.00 5.47  ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 174.413 195.136 182.153 1.00 7.82  ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 175.459 195.725 181.863 1.00 14.16 ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 174.020 193.469 180.306 1.00 2.89  ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 174.400 192.368 181.278 1.00 2.54  ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 173.013 192.966 179.285 1.00 7.23  ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 174.049 194.865 183.404 1.00 4.42  ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 174.895 195.152 184.556 1.00 1.86  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 175.265 193.831 185.218 1.00 3.22  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 174.400 192.976 185.439 1.00 5.28  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 174.211 196.114 185.548 1.00 0.00  ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 172.896 195.544 186.056 1.00 6.91  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 175.140 196.423 186.710 1.00 1.02  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 176.553 193.654 185.502 1.00 1.84  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 177.060 192.413 186.074 1.00 0.00  ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 177.122 192.556 187.590 1.00 4.57  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 177.963 193.291 188.119 1.00 6.08  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 178.430 192.070 185.497 1.00 3.22  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 178.990 190.760 186.001 1.00 7.33  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 178.281 189.578 185.848 1.00 4.42  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 180.228 190.706 186.625 1.00 7.94  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 178.787 188.380 186.306 1.00 1.64  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 180.742 189.511 187.085 1.00 4.65  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 180.017 188.352 186.922 1.00 4.92  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 180.523 187.157 187.379 1.00 11.79 ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 176.236 191.853 188.286 1.00 4.67  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 176.198 191.840 189.742 1.00 1.18  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 176.862 190.543 190.188 1.00 4.25  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 176.260 189.469 190.128 1.00 7.62  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 174.769 191.962 190.276 1.00 0.00  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 174.767 191.932 191.793 1.00 2.58  ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 174.118 193.234 189.763 1.00 1.14  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 178.110 190.639 190.630 1.00 2.63  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 178.869 189.481 191.069 1.00 0.85  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 178.673 189.254 192.567 1.00 4.02  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 178.068 190.065 193.271 1.00 8.75  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 180.351 189.663 190.736 1.00 4.64  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 181.111 188.353 190.701 1.00 11.48 ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 180.487 187.294 190.918 1.00 9.08  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 182.335 188.383 190.457 1.00 8.88  ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 179.188 188.128 193.049 1.00 5.87  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 179.091 187.817 194.466 1.00 3.11  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 179.825 188.875 195.284 1.00 7.23  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 180.888 189.354 194.869 1.00 7.87  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 179.685 186.440 194.765 1.00 2.25  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 178.804 185.273 194.390 1.00 3.18  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 177.458 185.261 194.721 1.00 3.63  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 179.325 184.173 193.728 1.00 3.57  ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 176.653 184.193 194.389 1.00 1.62  ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 178.527 183.101 193.393 1.00 4.59  ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 177.193 183.115 193.726 1.00 3.64  ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 176.395 182.049 193.391 1.00 6.07  ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 179.288 189.272 196.436 1.00 7.19  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 180.039 190.169 197.320 1.00 4.49  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 181.352 189.530 197.746 1.00 7.60  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 181.427 188.327 197.999 1.00 10.66 ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 179.094 190.366 198.512 1.00 2.39  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 177.739 190.068 197.975 1.00 4.06  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 177.931 189.006 196.936 1.00 3.85  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 182.394 190.351 197.823 1.00 10.10 ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 183.702 189.875 198.199 1.00 11.54 ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 183.760 189.500 199.664 1.00 13.23 ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 182.833 189.772 200.434 1.00 13.54 ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 184.850 188.845 200.075 1.00 14.01 ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 184.993 188.493 201.497 1.00 9.79  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 184.910 189.694 202.425 1.00 11.76 ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 184.340 189.585 203.515 1.00 13.40 ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 186.375 187.829 201.547 1.00 10.34 ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 186.568 187.276 200.180 1.00 12.47 ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 185.910 188.251 199.245 1.00 14.22 ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 185.457 190.841 202.019 1.00 14.17 ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 185.303 192.052 202.817 1.00 12.60 ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 183.854 192.522 202.831 1.00 11.27 ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 183.337 192.932 203.877 1.00 12.86 ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 186.220 193.153 202.284 1.00 11.98 ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 183.180 192.473 201.680 1.00 7.35  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 181.777 192.869 201.624 1.00 6.11  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 180.907 191.920 202.439 1.00 10.87 ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 180.005 192.355 203.165 1.00 19.73 ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 181.305 192.921 200.171 1.00 11.36 ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 182.131 193.772 199.397 1.00 16.30 ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 181.162 190.614 202.323 1.00 10.20 ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 180.431 189.647 203.135 1.00 9.47  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 180.670 189.895 204.615 1.00 9.56  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 179.731 189.853 205.421 1.00 12.65 ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 180.852 188.225 202.767 1.00 5.31  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 180.402 187.657 201.424 1.00 7.42  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 180.916 186.242 201.275 1.00 7.65  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 178.892 187.694 201.303 1.00 10.04 ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 181.923 190.159 204.988 1.00 10.81 ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 182.242 190.442 206.380 1.00 8.11  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 181.479 191.662 206.870 1.00 9.19  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 180.881 191.634 207.943 1.00 15.86 ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 183.748 190.646 206.546 1.00 9.46  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 184.450 189.559 205.931 1.00 13.40 ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 184.115 190.702 208.019 1.00 6.88  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 181.449 192.728 206.069 1.00 7.95  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 180.728 193.934 206.470 1.00 9.70  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 179.242 193.654 206.659 1.00 11.36 ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 178.673 193.938 207.723 1.00 17.54 ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 180.943 195.034 205.431 1.00 8.75  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 179.974 196.195 205.548 1.00 13.89 ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 180.256 197.294 204.543 1.00 18.99 ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 181.218 197.219 203.778 1.00 15.01 ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 179.415 198.321 204.537 1.00 13.99 ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 178.602 193.062 205.645 1.00 6.84  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 177.155 192.859 205.688 1.00 5.78  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 176.770 191.962 206.856 1.00 11.66 ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 175.905 192.302 207.676 1.00 14.30 ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 176.656 192.275 204.355 1.00 1.80  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 177.017 193.190 203.188 1.00 9.92  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 175.160 192.029 204.411 1.00 2.06  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 176.999 192.493 201.848 1.00 7.48  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 177.417 190.804 206.963 1.00 11.19 ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 176.979 189.848 207.963 1.00 6.30  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 177.556 190.130 209.339 1.00 4.74  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 176.989 189.665 210.327 1.00 13.39 ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 177.294 188.434 207.483 1.00 6.76  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 176.521 188.124 206.224 1.00 4.82  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 175.138 188.012 206.252 1.00 6.17  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 177.160 188.000 205.001 1.00 8.45  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 174.418 187.751 205.107 1.00 6.34  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 176.446 187.739 203.848 1.00 6.93  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 175.077 187.616 203.908 1.00 4.56  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 174.361 187.355 202.763 1.00 2.72  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 178.611 190.939 209.445 1.00 1.06  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 178.982 191.475 210.738 1.00 8.40  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 177.966 192.473 211.245 1.00 13.63 ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 177.652 192.498 212.435 1.00 18.46 ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 177.429 193.306 210.349 1.00 10.53 ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 176.328 194.179 210.742 1.00 10.80 ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 175.124 193.365 211.201 1.00 12.55 ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 174.529 193.654 212.249 1.00 15.23 ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 175.943 195.093 209.579 1.00 11.11 ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 177.092 195.837 209.155 1.00 14.14 ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 174.851 196.056 209.998 1.00 17.06 ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 174.770 192.327 210.438 1.00 13.70 ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 173.637 191.486 210.823 1.00 10.03 ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 173.884 190.774 212.150 1.00 11.93 ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 172.984 190.697 212.992 1.00 15.65 ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 173.325 190.475 209.722 1.00 9.01  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 172.498 191.035 208.603 1.00 11.87 ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 171.446 191.894 208.868 1.00 13.70 ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 172.759 190.691 207.290 1.00 10.33 ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 170.681 192.410 207.843 1.00 11.97 ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 171.994 191.202 206.261 1.00 10.58 ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 170.955 192.062 206.538 1.00 12.26 ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 175.096 190.256 212.361 1.00 11.78 ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 175.396 189.546 213.599 1.00 10.94 ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 175.447 190.493 214.790 1.00 12.44 ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 175.042 190.124 215.895 1.00 16.22 ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 176.713 188.785 213.462 1.00 8.62  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 176.587 187.555 212.590 1.00 9.77  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 177.579 186.906 212.266 1.00 8.30  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 175.361 187.225 212.206 1.00 11.38 ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 175.957 191.711 214.595 1.00 12.58 ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 175.938 192.698 215.667 1.00 12.31 ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 174.511 193.061 216.044 1.00 14.42 ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 174.196 193.221 217.229 1.00 20.03 ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 176.717 193.942 215.249 1.00 14.19 ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 178.153 193.969 215.730 1.00 17.58 ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 178.823 195.284 215.372 1.00 17.05 ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 179.454 195.227 214.061 1.00 17.29 ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 179.030 195.893 212.996 1.00 19.89 ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 177.972 196.684 213.053 1.00 18.28 ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 179.684 195.763 211.845 1.00 17.86 ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 173.634 193.206 215.048 1.00 17.07 ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 172.228 193.461 215.344 1.00 17.88 ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 171.588 192.279 216.062 1.00 20.29 ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 170.782 192.461 216.981 1.00 23.25 ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 171.473 193.780 214.055 1.00 18.85 ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 171.939 191.057 215.655 1.00 18.62 ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 171.299 189.865 216.205 1.00 17.14 ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 171.751 189.593 217.636 1.00 21.12 ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 170.930 189.288 218.510 1.00 26.35 ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 171.595 188.667 215.305 1.00 13.00 ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 171.585 187.325 216.006 1.00 14.40 ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 172.143 186.008 214.913 1.00 24.75 ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 173.875 185.921 215.357 1.00 18.78 ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 173.052 189.702 217.899 1.00 19.10 ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 173.619 189.344 219.193 1.00 17.62 ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 173.334 190.373 220.275 1.00 18.34 ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 173.723 190.155 221.428 1.00 24.06 ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 175.130 189.132 219.063 1.00 18.12 ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 175.554 187.796 218.446 1.00 20.84 ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 177.030 187.541 218.670 1.00 21.16 ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 174.728 186.656 219.013 1.00 20.18 ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 172.680 191.485 219.940 1.00 21.21 ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 172.236 192.425 220.959 1.00 25.01 ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 171.165 191.835 221.865 1.00 26.03 ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 170.891 192.408 222.925 1.00 27.17 ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 171.713 193.704 220.304 1.00 24.21 ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 172.805 194.661 219.854 1.00 23.21 ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 172.260 196.066 219.659 1.00 23.53 ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 171.387 196.157 218.497 1.00 26.78 ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 171.774 196.579 217.301 1.00 28.99 ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 173.020 196.961 217.073 1.00 26.12 ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 170.889 196.619 216.309 1.00 27.19 ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 170.552 190.717 221.470 1.00 26.22 ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 169.587 190.048 222.337 1.00 28.98 ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 170.250 189.555 223.617 1.00 30.63 ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 169.692 189.699 224.711 1.00 31.77 ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 168.939 188.884 221.592 1.00 25.80 ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 168.033 189.244 220.414 1.00 26.61 ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 167.865 188.053 219.488 1.00 25.03 ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 166.683 189.735 220.911 1.00 27.90 ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 171.438 188.973 223.501 1.00 29.45 ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 172.179 188.462 224.650 1.00 31.00 ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 173.449 189.289 224.813 1.00 32.72 ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 174.405 189.108 224.046 1.00 31.63 ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 172.501 186.969 224.487 1.00 30.08 ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 171.262 186.209 224.007 1.00 30.51 ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 173.010 186.390 225.796 1.00 32.83 ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 171.416 184.707 224.028 1.00 33.39 ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 173.498 190.209 225.782 1.00 38.56 ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 174.686 191.073 225.909 1.00 37.70 ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 175.981 190.308 226.119 1.00 34.55 ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 177.022 190.703 225.576 1.00 37.45 ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 174.342 191.954 227.119 1.00 36.51 ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 172.849 191.942 227.184 1.00 35.97 ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 172.441 190.571 226.741 1.00 34.87 ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 175.946 189.209 226.875 1.00 30.28 ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 177.168 188.464 227.162 1.00 33.44 ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 177.811 187.897 225.905 1.00 35.46 ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 179.008 187.594 225.917 1.00 33.97 ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 176.871 187.335 228.151 1.00 36.21 ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 176.030 186.354 227.569 1.00 37.65 ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 177.047 187.747 224.827 1.00 34.42 ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 177.563 187.240 223.563 1.00 29.61 ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 177.985 188.342 222.602 1.00 33.50 ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 178.484 188.032 221.516 1.00 34.19 ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 176.514 186.353 222.885 1.00 30.30 ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 176.192 185.018 223.556 1.00 31.89 ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 175.162 184.253 222.743 1.00 29.17 ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 177.455 184.196 223.734 1.00 32.56 ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 177.811 189.614 222.974 1.00 34.38 ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 178.079 190.698 222.031 1.00 32.08 ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 179.539 190.711 221.592 1.00 31.82 ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 179.834 190.911 220.407 1.00 33.38 ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 177.673 192.036 222.649 1.00 30.98 ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 176.174 192.152 222.872 1.00 33.36 ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 175.679 193.583 222.754 1.00 35.37 ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 176.478 194.507 223.551 1.00 38.73 ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 176.375 195.828 223.492 1.00 37.92 ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 175.522 196.420 222.673 1.00 34.29 ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 177.147 196.573 224.279 1.00 36.81 ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 180.462 190.460 222.522 1.00 26.60 ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 181.878 190.428 222.176 1.00 28.80 ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 182.219 189.316 221.194 1.00 28.84 ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 183.301 189.351 220.599 1.00 28.88 ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 182.728 190.274 223.440 1.00 30.13 ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 184.117 190.339 223.094 1.00 29.67 ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 182.441 188.948 224.121 1.00 27.57 ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 181.334 188.340 221.010 1.00 25.01 ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 181.541 187.270 220.046 1.00 22.85 ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 180.920 187.574 218.688 1.00 25.81 ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 180.832 186.674 217.847 1.00 26.20 ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 180.983 185.954 220.591 1.00 26.37 ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 181.652 185.494 221.865 1.00 28.34 ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 182.867 184.823 221.827 1.00 24.17 ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 181.072 185.728 223.103 1.00 26.29 ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 183.484 184.400 222.985 1.00 23.40 ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 181.682 185.309 224.267 1.00 25.07 ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 182.889 184.645 224.202 1.00 26.80 ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 183.504 184.223 225.359 1.00 26.30 ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 180.479 188.814 218.460 1.00 25.38 ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 179.924 189.164 217.157 1.00 20.14 ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 180.994 189.151 216.073 1.00 18.92 ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 180.763 188.635 214.973 1.00 18.21 ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 179.247 190.532 217.227 1.00 18.48 ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 182.166 189.717 216.358 1.00 18.54 ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 183.228 189.776 215.354 1.00 18.69 ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 183.757 188.406 214.949 1.00 18.27 ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 183.854 188.145 213.737 1.00 15.06 ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 184.356 190.685 215.851 1.00 19.27 ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 183.930 192.121 216.102 1.00 23.20 ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 183.549 192.847 214.826 1.00 25.46 ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 184.446 193.426 214.180 1.00 24.04 ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 182.351 192.837 214.469 1.00 23.11 ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 184.125 187.490 215.873 1.00 21.48 ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 184.663 186.197 215.426 1.00 15.57 ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 183.631 185.345 214.707 1.00 16.37 ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 183.917 184.781 213.645 1.00 19.10 ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 185.124 185.535 216.733 1.00 14.75 ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 184.323 186.188 217.791 1.00 16.43 ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 184.154 187.604 217.343 1.00 19.36 ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 182.419 185.279 215.268 1.00 16.68 ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 181.380 184.401 214.739 1.00 13.42 ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 181.165 184.640 213.251 1.00 14.21 ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 181.274 183.715 212.436 1.00 13.73 ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 180.080 184.625 215.514 1.00 12.63 ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 178.770 184.154 214.881 1.00 12.35 ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 178.672 182.647 214.932 1.00 13.31 ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 177.575 184.791 215.572 1.00 16.50 ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 180.926 185.901 212.879 1.00 14.57 ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 180.751 186.250 211.474 1.00 12.16 ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 181.899 185.713 210.638 1.00 8.92  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 181.684 185.011 209.643 1.00 10.58 ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 180.646 187.765 211.316 1.00 9.86  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 179.520 188.250 212.056 1.00 10.97 ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 180.489 188.137 209.851 1.00 9.63  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 183.134 185.989 211.069 1.00 7.21  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 184.298 185.504 210.339 1.00 8.79  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 184.193 184.006 210.115 1.00 8.93  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 184.257 183.531 208.973 1.00 11.24 ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 185.578 185.855 211.095 1.00 8.02  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 183.940 183.256 211.193 1.00 10.74 ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 183.791 181.812 211.063 1.00 11.04 ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 182.750 181.489 210.008 1.00 9.26  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 183.037 180.780 209.034 1.00 11.12 ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 183.410 181.199 212.410 1.00 12.24 ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 181.561 182.084 210.145 1.00 8.80  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 180.516 181.921 209.143 1.00 4.82  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 181.094 182.122 207.753 1.00 7.20  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 181.153 181.183 206.947 1.00 12.89 ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 179.377 182.910 209.413 1.00 1.03  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 178.623 182.641 210.704 1.00 9.76  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 176.929 183.256 210.735 1.00 12.75 ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 177.087 184.754 209.773 1.00 6.57  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 181.642 183.316 207.511 1.00 8.72  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 182.147 183.637 206.184 1.00 8.35  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 183.145 182.581 205.746 1.00 11.11 ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 183.009 181.983 204.669 1.00 11.42 ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 182.770 185.044 206.168 1.00 5.75  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 183.515 185.279 204.866 1.00 5.66  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 181.698 186.101 206.372 1.00 8.04  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 184.096 182.257 206.628 1.00 13.34 ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 185.131 181.301 206.261 1.00 8.76  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 184.501 180.006 205.784 1.00 7.11  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 184.732 179.570 204.648 1.00 11.25 ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 186.066 181.047 207.440 1.00 7.70  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 187.039 179.905 207.203 1.00 8.61  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 188.321 180.058 207.988 1.00 16.45 ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 188.258 180.486 209.158 1.00 17.53 ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 189.397 179.751 207.433 1.00 17.24 ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 183.608 179.437 206.599 1.00 5.77  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 183.023 178.159 206.219 1.00 6.25  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 182.297 178.290 204.895 1.00 8.89  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 182.492 177.470 203.988 1.00 10.89 ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 182.079 177.644 207.302 1.00 5.78  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 181.496 176.300 206.988 1.00 9.63  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 182.319 175.207 206.786 1.00 10.37 ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 180.128 176.131 206.871 1.00 11.72 ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 181.790 173.970 206.485 1.00 11.61 ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 179.595 174.894 206.572 1.00 9.42  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 180.426 173.815 206.376 1.00 9.80  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 181.521 179.366 204.737 1.00 9.89  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 180.809 179.574 203.486 1.00 6.60  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 181.783 179.524 202.323 1.00 9.37  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 181.629 178.707 201.405 1.00 12.73 ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 180.063 180.909 203.528 1.00 7.28  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 179.660 181.436 202.172 1.00 10.62 ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 178.594 180.879 201.479 1.00 9.82  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 180.340 182.495 201.589 1.00 8.62  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 178.223 181.359 200.241 1.00 6.86  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 179.976 182.979 200.353 1.00 8.72  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 178.916 182.410 199.684 1.00 6.91  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 178.556 182.896 198.450 1.00 6.94  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 182.856 180.315 202.410 1.00 8.95  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 183.835 180.339 201.332 1.00 6.23  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 184.347 178.936 201.054 1.00 9.61  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 184.345 178.476 199.906 1.00 13.06 ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 184.988 181.277 201.685 1.00 7.07  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 184.466 182.541 202.109 1.00 9.33  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 185.889 181.485 200.482 1.00 8.42  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 184.710 178.212 202.115 1.00 10.81 ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 185.251 176.872 201.937 1.00 9.08  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 184.258 175.999 201.189 1.00 11.54 ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 184.610 175.353 200.193 1.00 15.87 ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 185.601 176.271 203.298 1.00 6.75  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 186.744 176.988 203.996 1.00 9.91  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 187.105 176.334 205.631 1.00 27.99 ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 187.820 174.755 205.197 1.00 14.16 ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 182.991 176.029 201.607 1.00 8.48  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 181.988 175.232 200.915 1.00 6.18  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 181.870 175.670 199.466 1.00 8.47  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 181.857 174.833 198.554 1.00 11.84 ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 180.643 175.342 201.629 1.00 12.77 ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 180.786 175.084 203.014 1.00 17.67 ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 181.851 176.984 199.229 1.00 10.58 ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 181.723 177.479 197.868 1.00 6.43  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 182.929 177.107 197.021 1.00 12.89 ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 182.827 177.086 195.790 1.00 18.03 ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 181.517 178.992 197.880 1.00 4.36  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 181.010 179.559 196.571 1.00 9.12  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 180.768 181.049 196.646 1.00 12.12 ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 181.061 181.689 197.653 1.00 14.99 ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 180.224 181.612 195.577 1.00 9.00  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 184.062 176.799 197.653 1.00 15.68 ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 185.225 176.333 196.914 1.00 14.43 ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 185.266 174.820 196.781 1.00 17.57 ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 185.919 174.309 195.864 1.00 19.90 ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 186.511 176.821 197.588 1.00 14.63 ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 187.741 176.762 196.697 1.00 20.33 ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 189.013 177.129 197.431 1.00 24.36 ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 188.973 177.239 198.674 1.00 21.99 ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 190.055 177.305 196.765 1.00 22.53 ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 184.574 174.093 197.658 1.00 19.38 ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 184.682 172.641 197.667 1.00 12.43 ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 183.601 171.975 196.828 1.00 18.43 ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 183.889 171.029 196.086 1.00 23.03 ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 184.629 172.122 199.106 1.00 10.28 ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 184.463 170.620 199.224 1.00 16.35 ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 185.737 169.889 198.833 1.00 19.10 ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 185.778 168.534 199.368 1.00 23.89 ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 185.070 167.517 198.896 1.00 27.09 ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 184.260 167.659 197.859 1.00 23.27 ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 185.176 166.325 199.477 1.00 22.12 ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 182.365 172.453 196.922 1.00 18.68 ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 181.237 171.875 196.203 1.00 12.50 ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 180.811 172.836 195.102 1.00 20.25 ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 180.354 173.948 195.385 1.00 21.11 ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 180.078 171.591 197.155 1.00 8.49  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 180.494 170.899 198.420 1.00 13.14 ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 180.913 169.582 198.399 1.00 13.10 ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 180.476 171.571 199.630 1.00 14.59 ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 181.302 168.947 199.559 1.00 13.75 ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 180.862 170.939 200.793 1.00 13.04 ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 181.276 169.626 200.758 1.00 13.85 ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 180.959 172.404 193.852 1.00 19.99 ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 180.627 173.215 192.691 1.00 16.47 ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 179.639 172.461 191.814 1.00 15.74 ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 179.309 171.299 192.063 1.00 17.02 ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 181.880 173.585 191.885 1.00 21.47 ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 182.552 172.389 191.473 1.00 25.83 ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 182.825 174.425 192.725 1.00 19.85 ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 179.165 173.141 190.767 1.00 19.85 ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 178.187 172.549 189.862 1.00 18.94 ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 178.766 171.424 189.015 1.00 21.71 ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 177.995 170.684 188.396 1.00 23.53 ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 177.594 173.625 188.955 1.00 16.10 ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 176.540 174.485 189.627 1.00 15.23 ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 175.653 175.200 188.631 1.00 21.32 ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 175.691 176.425 188.514 1.00 24.87 ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 174.843 174.438 187.908 1.00 21.25 ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 180.092 171.283 188.962 1.00 23.05 ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 180.683 170.151 188.255 1.00 22.81 ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 180.298 168.836 188.918 1.00 25.92 ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 179.997 167.850 188.234 1.00 27.34 ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 182.203 170.295 188.203 1.00 25.53 ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 182.641 171.673 187.759 1.00 32.64 ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 182.437 172.013 186.574 1.00 33.85 ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 183.189 172.417 188.598 1.00 31.37 ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 180.303 168.800 190.252 1.00 21.65 ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 179.947 167.582 190.969 1.00 18.83 ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 178.457 167.290 190.835 1.00 20.98 ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 178.059 166.253 190.293 1.00 21.72 ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 180.343 167.707 192.440 1.00 19.81 ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 181.758 167.914 192.540 1.00 20.18 ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 179.968 166.447 193.199 1.00 20.52 ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 177.618 168.197 191.325 1.00 18.60 ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 176.174 168.060 191.247 1.00 12.70 ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 175.555 169.369 190.789 1.00 12.77 ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 176.065 170.448 191.108 1.00 13.41 ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 175.578 167.657 192.603 1.00 11.89 ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 176.172 166.392 193.196 1.00 13.85 ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 175.611 165.137 192.568 1.00 14.10 ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 174.570 165.168 191.913 1.00 15.70 ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 176.300 164.020 192.761 1.00 16.11 ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 174.454 169.308 190.034 1.00 15.14 ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 173.831 170.548 189.547 1.00 13.37 ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 173.343 171.469 190.650 1.00 14.44 ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 173.336 172.692 190.463 1.00 14.65 ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 172.668 170.038 188.684 1.00 15.70 ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 172.405 168.654 189.174 1.00 16.64 ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 173.741 168.109 189.564 1.00 17.01 ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 172.934 170.928 191.793 1.00 13.25 ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 172.353 171.729 192.862 1.00 10.57 ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 173.384 172.242 193.857 1.00 10.78 ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 173.001 172.857 194.856 1.00 13.52 ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 171.280 170.924 193.604 1.00 7.71  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 171.796 169.678 194.250 1.00 8.96  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 172.170 168.564 193.530 1.00 12.20 ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 171.995 169.367 195.553 1.00 7.48  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 172.580 167.622 194.359 1.00 7.98  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 172.483 168.083 195.593 1.00 6.89  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 174.673 172.009 193.614 1.00 7.85  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 175.728 172.490 194.507 1.00 6.59  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 176.009 173.963 194.208 1.00 11.47 ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 177.057 174.347 193.686 1.00 16.87 ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 176.985 171.644 194.361 1.00 9.84  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 176.921 170.307 195.062 1.00 12.23 ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 175.789 169.916 195.762 1.00 9.62  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 178.000 169.435 195.025 1.00 14.54 ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 175.733 168.695 196.401 1.00 10.49 ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 177.953 168.214 195.659 1.00 12.13 ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 176.818 167.849 196.346 1.00 12.47 ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 176.772 166.630 196.980 1.00 15.37 ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 175.034 174.799 194.551 1.00 11.24 ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 175.120 176.241 194.359 1.00 6.18  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 175.074 176.898 195.728 1.00 7.21  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 174.071 176.787 196.443 1.00 9.27  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 173.990 176.768 193.462 1.00 8.82  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 174.126 176.210 192.045 1.00 11.68 ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 173.991 178.285 193.442 1.00 9.25  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 172.803 175.896 191.388 1.00 10.05 ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 176.154 177.585 196.090 1.00 5.80  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 176.256 178.285 197.363 1.00 4.90  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 176.373 179.776 197.094 1.00 9.93  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 177.154 180.197 196.233 1.00 15.71 ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 177.449 177.777 198.174 1.00 5.64  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 177.290 176.343 198.620 1.00 6.80  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 176.495 176.021 199.708 1.00 7.43  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 177.924 175.312 197.945 1.00 8.68  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 176.341 174.711 200.117 1.00 7.65  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 177.776 174.000 198.345 1.00 8.54  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 176.985 173.705 199.431 1.00 9.52  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 176.835 172.400 199.836 1.00 12.97 ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 175.601 180.567 197.826 1.00 3.08  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 175.463 181.987 197.553 1.00 2.02  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 175.284 182.709 198.876 1.00 5.44  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 175.112 182.072 199.923 1.00 9.90  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 174.277 182.254 196.619 1.00 3.57  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 173.119 181.569 197.063 1.00 8.13  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 175.332 184.053 198.872 1.00 3.85  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 175.017 184.803 200.096 1.00 2.59  ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 173.627 184.514 200.642 1.00 2.55  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 173.305 184.903 201.768 1.00 11.02 ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 175.149 186.263 199.649 1.00 4.08  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 176.171 186.216 198.583 1.00 4.81  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 175.945 184.922 197.851 1.00 3.11  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 172.793 183.841 199.848 1.00 0.90  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 171.507 183.372 200.353 1.00 2.70  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 171.701 182.406 201.515 1.00 4.89  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 170.950 182.441 202.495 1.00 10.02 ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 170.717 182.704 199.230 1.00 5.17  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 170.082 183.673 198.254 1.00 7.09  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 168.851 183.066 197.611 1.00 5.92  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 169.198 182.214 196.482 1.00 5.28  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 168.918 182.497 195.218 1.00 8.21  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 168.277 183.603 194.883 1.00 4.89  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 169.288 181.647 194.266 1.00 8.88  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 172.709 181.536 201.420 1.00 5.49  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 173.001 180.615 202.514 1.00 3.83  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 173.441 181.371 203.761 1.00 5.02  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 173.073 181.006 204.881 1.00 10.95 ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 174.068 179.611 202.082 1.00 4.91  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 173.939 179.156 200.639 1.00 10.30 ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 172.784 178.203 200.422 1.00 12.39 ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 172.187 177.746 201.419 1.00 14.25 ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 172.465 177.916 199.250 1.00 11.92 ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 174.231 182.430 203.588 1.00 3.42  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 174.657 183.227 204.734 1.00 3.71  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 173.479 183.959 205.369 1.00 4.98  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 173.389 184.061 206.601 1.00 12.93 ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 175.742 184.210 204.301 1.00 0.83  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 177.114 183.576 204.147 1.00 3.76  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 178.465 184.665 204.617 1.00 23.87 ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 178.187 184.793 206.376 1.00 8.23  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 172.568 184.478 204.544 1.00 1.48  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 171.365 185.113 205.074 1.00 1.34  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 170.507 184.113 205.838 1.00 6.23  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 169.979 184.426 206.911 1.00 10.18 ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 170.564 185.753 203.939 1.00 1.86  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 171.355 186.766 203.308 1.00 6.35  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 169.288 186.378 204.471 1.00 6.34  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 170.361 182.899 205.302 1.00 4.59  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 169.616 181.861 206.008 1.00 0.73  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 170.313 181.474 207.305 1.00 6.38  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 169.655 181.168 208.304 1.00 9.72  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 169.441 180.640 205.109 1.00 0.87  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 168.175 180.659 204.274 1.00 5.11  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 168.252 179.647 203.146 1.00 10.78 ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 167.585 180.118 201.939 1.00 15.03 ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 168.026 179.901 200.706 1.00 14.66 ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 169.135 179.214 200.481 1.00 8.50  ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 167.338 180.383 199.677 1.00 12.02 ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 171.646 181.477 207.304 1.00 3.47  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 172.413 181.211 208.516 1.00 2.74  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 172.098 182.235 209.595 1.00 5.60  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 171.803 181.883 210.746 1.00 12.00 ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 173.903 181.232 208.172 1.00 1.58  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 174.769 180.355 209.003 1.00 5.10  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 174.473 179.815 210.215 1.00 4.84  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 176.087 179.909 208.673 1.00 7.09  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 175.527 179.058 210.665 1.00 2.99  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 176.532 179.102 209.735 1.00 6.20  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 176.935 180.114 207.581 1.00 8.18  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 177.785 178.499 209.737 1.00 7.41  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 178.179 179.517 207.586 1.00 6.26  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 178.593 178.719 208.656 1.00 5.90  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 172.155 183.516 209.232 1.00 6.43  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 171.870 184.579 210.192 1.00 6.24  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 170.429 184.476 210.679 1.00 5.72  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 170.147 184.633 211.872 1.00 8.34  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 172.168 185.957 209.575 1.00 7.59  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 171.866 187.056 210.570 1.00 6.64  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 173.616 186.034 209.130 1.00 7.52  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 169.497 184.199 209.762 1.00 8.28  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 168.093 184.062 210.136 1.00 8.37  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 167.888 182.913 211.116 1.00 13.59 ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 167.155 183.048 212.101 1.00 18.68 ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 167.234 183.855 208.889 1.00 9.70  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 166.825 185.132 208.180 1.00 13.64 ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 166.177 186.126 209.130 1.00 17.69 ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 165.133 185.522 209.948 1.00 17.99 ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 164.425 186.176 210.857 1.00 19.73 ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 164.620 187.463 211.090 1.00 17.45 ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 163.497 185.523 211.550 1.00 16.09 ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 168.520 181.769 210.854 1.00 8.63  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 168.352 180.625 211.733 1.00 5.48  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 168.935 180.859 213.112 1.00 7.00  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 168.309 180.529 214.125 1.00 13.19 ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 170.136 181.436 213.174 1.00 11.57 ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 170.737 181.731 214.472 1.00 9.09  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 169.889 182.745 215.231 1.00 11.69 ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 169.680 182.619 216.444 1.00 16.94 ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 172.189 182.212 214.305 1.00 5.96  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 173.012 181.168 213.553 1.00 6.80  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 172.815 182.472 215.661 1.00 9.37  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 174.462 181.550 213.379 1.00 10.90 ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 169.380 183.762 214.529 1.00 10.86 ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 168.530 184.755 215.176 1.00 8.89  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 167.243 184.134 215.702 1.00 15.96 ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 166.798 184.455 216.809 1.00 23.58 ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 168.218 185.888 214.199 1.00 13.78 ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 167.214 186.874 214.717 1.00 17.24 ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 167.575 187.822 215.657 1.00 19.90 ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 165.908 186.855 214.261 1.00 16.00 ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 166.654 188.729 216.134 1.00 19.86 ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 164.983 187.759 214.733 1.00 17.63 ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 165.355 188.696 215.672 1.00 20.40 ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 166.620 183.253 214.916 1.00 14.91 ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 165.387 182.610 215.357 1.00 15.07 ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 165.633 181.720 216.566 1.00 16.99 ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 164.803 181.659 217.481 1.00 20.10 ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 164.772 181.806 214.213 1.00 12.56 ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 163.882 182.621 213.294 1.00 16.78 ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 163.870 182.093 211.874 1.00 22.47 ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 163.009 182.532 211.083 1.00 23.02 ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 164.722 181.241 211.548 1.00 21.10 ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 166.763 181.011 216.585 1.00 17.46 ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 167.099 180.201 217.750 1.00 14.84 ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 167.351 181.069 218.978 1.00 18.03 ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 166.932 180.719 220.087 1.00 22.80 ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 168.314 179.327 217.449 1.00 12.80 ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 168.033 182.204 218.803 1.00 16.62 ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 168.431 183.034 219.933 1.00 17.43 ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 167.329 183.962 220.426 1.00 22.00 ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 167.446 184.497 221.534 1.00 25.50 ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 169.653 183.873 219.556 1.00 18.43 ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 170.983 183.135 219.439 1.00 18.53 ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 172.092 184.106 219.082 1.00 20.37 ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 171.292 182.425 220.737 1.00 21.62 ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 166.279 184.177 219.635 1.00 20.21 ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 165.275 185.176 219.997 1.00 21.99 ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 164.545 184.864 221.300 1.00 24.68 ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 164.469 185.756 222.161 1.00 23.07 ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 164.291 185.359 218.836 1.00 23.41 ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 163.403 186.582 218.967 1.00 23.52 ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 162.046 186.344 218.332 1.00 23.96 ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 162.153 185.623 217.070 1.00 24.51 ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 162.081 186.193 215.875 1.00 26.13 ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 161.894 187.496 215.741 1.00 26.29 ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 162.198 185.437 214.787 1.00 25.46 ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 163.994 183.663 221.521 1.00 27.22 ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 163.273 183.428 222.782 1.00 25.92 ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 164.180 183.302 223.991 1.00 27.49 ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 163.723 183.553 225.113 1.00 27.76 ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 162.516 182.122 222.515 1.00 26.82 ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 163.368 181.409 221.539 1.00 25.74 ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 163.944 182.474 220.648 1.00 26.73 ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 165.440 182.920 223.806 1.00 29.38 ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 166.339 182.725 224.934 1.00 30.16 ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 166.666 184.054 225.602 1.00 34.68 ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 166.864 185.074 224.935 1.00 35.52 ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 167.627 182.042 224.473 1.00 26.85 ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 167.469 180.800 223.595 1.00 29.60 ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 168.823 180.161 223.334 1.00 30.39 ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 166.520 179.800 224.234 1.00 31.12 ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 166.723 184.038 226.934 1.00 41.27 ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 167.098 185.225 227.693 1.00 42.55 ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 168.589 185.281 227.985 1.00 42.09 ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 169.144 186.377 228.135 1.00 42.21 ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 166.310 185.284 229.006 1.00 39.75 ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 166.636 184.164 229.981 1.00 40.44 ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 166.365 184.549 231.421 1.00 43.37 ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 165.583 185.496 231.648 1.00 43.59 ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 166.937 183.907 232.328 1.00 43.47 ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 169.251 184.130 228.068 1.00 37.40 ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 170.689 184.073 228.273 1.00 37.46 ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 171.212 182.772 227.685 1.00 37.76 ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 170.474 181.790 227.564 1.00 38.45 ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 171.062 184.176 229.757 1.00 37.29 ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 172.488 184.176 229.894 1.00 37.73 ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 170.481 183.008 230.539 1.00 35.46 ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 172.492 182.776 227.319 1.00 31.08 ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 173.110 181.603 226.717 1.00 26.50 ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 174.627 181.742 226.730 1.00 28.77 ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 175.158 182.803 226.375 1.00 30.17 ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 172.609 181.406 225.287 1.00 27.13 ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 173.133 180.178 224.542 1.00 30.44 ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 172.289 178.957 224.869 1.00 32.15 ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 173.154 180.430 223.048 1.00 27.37 ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 175.357 180.704 227.129 1.00 30.07 ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 176.821 180.759 227.063 1.00 30.82 ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 177.304 180.693 225.623 1.00 29.39 ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 176.539 180.464 224.684 1.00 29.49 ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 177.261 179.531 227.862 1.00 26.46 ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 176.113 178.587 227.754 1.00 27.74 ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 174.874 179.440 227.709 1.00 27.66 ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 178.612 180.904 225.458 1.00 23.70 ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 179.202 180.880 224.123 1.00 22.81 ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 179.075 179.497 223.498 1.00 25.12 ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 178.909 179.373 222.278 1.00 24.18 ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 180.669 181.358 224.176 1.00 22.60 ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 181.531 180.397 224.983 1.00 25.38 ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 181.225 181.529 222.771 1.00 23.73 ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 179.129 178.441 224.314 1.00 24.75 ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 179.031 177.084 223.782 1.00 25.09 ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 177.686 176.852 223.105 1.00 25.52 ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 177.613 176.186 222.067 1.00 25.80 ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 179.257 176.064 224.897 1.00 27.95 ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 180.719 175.790 225.199 1.00 28.21 ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 181.281 176.720 226.253 1.00 28.05 ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 180.516 177.550 226.785 1.00 26.07 ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 182.489 176.620 226.552 1.00 29.95 ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 176.609 177.391 223.679 1.00 21.74 ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 175.316 177.299 223.021 1.00 19.48 ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 175.292 178.019 221.686 1.00 21.33 ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 174.696 177.538 220.720 1.00 24.91 ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 175.942 179.184 221.616 1.00 17.04 ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 176.020 179.911 220.354 1.00 15.79 ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 176.771 179.107 219.302 1.00 17.39 ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 176.350 179.044 218.140 1.00 19.06 ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 176.691 181.268 220.574 1.00 19.30 ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 176.938 182.127 219.333 1.00 18.43 ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 175.644 182.765 218.858 1.00 17.35 ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 177.989 183.187 219.613 1.00 17.47 ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 177.884 178.477 219.689 1.00 16.29 ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 178.627 177.660 218.735 1.00 12.96 ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 177.821 176.436 218.327 1.00 14.59 ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 177.898 175.992 217.176 1.00 17.45 ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 180.004 177.259 219.295 1.00 14.08 ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 180.663 178.440 220.000 1.00 16.00 ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 180.904 176.757 218.181 1.00 14.71 ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 180.795 179.662 219.132 1.00 19.57 ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 177.045 175.862 219.248 1.00 14.31 ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 176.201 174.727 218.888 1.00 11.60 ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 175.131 175.131 217.880 1.00 12.58 ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 174.873 174.397 216.918 1.00 16.43 ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 175.568 174.123 220.139 1.00 15.67 ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 174.996 172.734 219.920 1.00 17.52 ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 174.881 171.962 221.221 1.00 17.50 ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 174.339 170.625 221.012 1.00 19.10 ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 175.038 169.597 220.552 1.00 21.62 ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 176.318 169.712 220.245 1.00 22.54 ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 174.435 168.421 220.396 1.00 20.49 ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 174.501 176.291 218.078 1.00 11.95 ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 173.517 176.777 217.112 1.00 8.56  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 174.177 177.044 215.765 1.00 11.35 ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 173.622 176.721 214.706 1.00 12.65 ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 172.805 178.032 217.647 1.00 5.12  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 172.094 177.731 218.963 1.00 14.84 ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 171.812 178.554 216.627 1.00 5.84  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 171.427 178.934 219.582 1.00 18.12 ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 175.363 177.654 215.784 1.00 11.54 ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 176.096 177.925 214.552 1.00 4.98  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 176.404 176.635 213.799 1.00 7.50  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 176.194 176.546 212.582 1.00 12.02 ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 177.376 178.692 214.894 1.00 6.90  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 178.324 178.903 213.760 1.00 8.51  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 178.369 179.972 212.920 1.00 5.62  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 179.399 178.042 213.372 1.00 9.09  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 179.392 179.822 212.018 1.00 6.24  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 180.040 178.642 212.274 1.00 7.84  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 179.874 176.814 213.839 1.00 9.27  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 181.128 178.060 211.637 1.00 10.34 ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 180.954 176.239 213.206 1.00 9.61  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 181.570 176.860 212.116 1.00 11.68 ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 176.883 175.616 214.514 1.00 8.48  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 177.183 174.334 213.884 1.00 6.98  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 175.921 173.666 213.353 1.00 9.70  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 175.937 173.080 212.265 1.00 14.80 ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 177.896 173.418 214.876 1.00 9.07  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 174.821 173.735 214.106 1.00 6.88  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 173.574 173.132 213.649 1.00 5.72  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 173.084 173.792 212.367 1.00 8.58  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 172.658 173.107 211.430 1.00 13.19 ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 172.509 173.237 214.738 1.00 6.62  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 171.170 172.710 214.325 1.00 6.10  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 170.110 173.532 214.017 1.00 8.73  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 170.724 171.442 214.166 1.00 8.86  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 169.065 172.793 213.688 1.00 8.69  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 169.411 171.521 213.769 1.00 4.59  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 173.142 175.121 212.306 1.00 9.15  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 172.693 175.816 211.105 1.00 3.34  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 173.623 175.543 209.930 1.00 3.50  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 173.166 175.419 208.787 1.00 11.17 ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 172.578 177.313 211.378 1.00 6.51  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 171.463 177.670 212.341 1.00 5.49  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 170.092 177.307 211.804 1.00 12.34 ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 169.904 177.350 210.571 1.00 14.44 ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 169.205 176.976 212.616 1.00 12.93 ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 174.929 175.437 210.189 1.00 2.43  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 175.858 175.052 209.131 1.00 1.15  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 175.526 173.669 208.589 1.00 7.40  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 175.553 173.445 207.374 1.00 9.65  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 177.294 175.092 209.651 1.00 2.78  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 175.211 172.728 209.480 1.00 9.99  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 174.819 171.390 209.047 1.00 4.34  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 173.541 171.430 208.222 1.00 4.79  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 173.430 170.745 207.200 1.00 8.77  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 174.636 170.480 210.261 1.00 6.22  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 175.889 170.124 211.055 1.00 5.97  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 175.517 169.433 212.353 1.00 7.99  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 176.787 169.240 210.222 1.00 5.71  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 172.560 172.225 208.654 1.00 4.35  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 171.283 172.262 207.950 1.00 3.94  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 171.401 172.940 206.591 1.00 4.02  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 170.658 172.596 205.664 1.00 5.23  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 170.227 172.965 208.801 1.00 4.37  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 169.903 172.260 210.111 1.00 5.90  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 169.057 171.011 209.905 1.00 3.70  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 169.851 169.855 209.504 1.00 7.26  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 170.684 169.198 210.300 1.00 10.44 ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 170.851 169.546 211.566 1.00 7.44  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 171.368 168.167 209.815 1.00 8.69  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 172.316 173.895 206.446 1.00 4.12  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 172.411 174.641 205.198 1.00 2.55  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 173.377 174.018 204.199 1.00 5.74  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 173.078 173.975 203.002 1.00 14.56 ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 172.834 176.082 205.479 1.00 1.90  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 171.794 176.945 206.183 1.00 1.27  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 172.419 178.258 206.574 1.00 3.66  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 170.591 177.166 205.286 1.00 8.62  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 174.530 173.534 204.656 1.00 2.21  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 175.588 173.107 203.756 1.00 4.12  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 175.709 171.597 203.615 1.00 9.31  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 176.421 171.135 202.717 1.00 14.02 ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 176.935 173.680 204.222 1.00 4.89  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 176.980 175.182 204.235 1.00 4.70  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 176.563 175.891 205.347 1.00 7.40  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 177.438 175.884 203.135 1.00 2.79  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 176.600 177.269 205.362 1.00 3.79  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 177.478 177.262 203.145 1.00 5.20  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 177.059 177.956 204.260 1.00 5.45  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 175.038 170.817 204.461 1.00 9.13  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 175.176 169.366 204.441 1.00 5.69  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 173.913 168.629 204.022 1.00 9.02  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 174.013 167.490 203.559 1.00 15.64 ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 175.613 168.856 205.821 1.00 3.12  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 176.199 167.459 205.809 1.00 7.16  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 176.457 166.927 207.200 1.00 12.88 ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 175.568 166.923 208.051 1.00 13.21 ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 177.678 166.466 207.438 1.00 16.68 ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 172.737 169.244 204.166 1.00 6.19  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 171.496 168.551 203.837 1.00 4.29  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 171.400 168.224 202.354 1.00 4.18  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 170.753 167.240 201.980 1.00 12.10 ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 170.296 169.393 204.270 1.00 10.55 ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 170.024 169.298 205.755 1.00 13.39 ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 170.843 168.690 206.475 1.00 10.58 ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 168.987 169.831 206.203 1.00 10.26 ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 172.024 169.030 201.498 1.00 6.30  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 171.950 168.837 200.058 1.00 4.28  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 173.028 167.910 199.514 1.00 7.92  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 172.974 167.552 198.332 1.00 12.29 ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 172.049 170.187 199.344 1.00 5.15  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 173.463 170.733 199.266 1.00 6.27  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 173.505 172.052 198.521 1.00 7.13  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 172.919 173.133 199.303 1.00 10.61 ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 172.578 174.314 198.807 1.00 10.52 ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 172.751 174.602 197.528 1.00 7.92  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 172.050 175.228 199.615 1.00 9.61  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 173.996 167.514 200.334 1.00 10.78 ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 175.122 166.732 199.841 1.00 9.45  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 174.689 165.317 199.484 1.00 10.20 ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 173.850 164.714 200.157 1.00 14.68 ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 176.236 166.697 200.883 1.00 8.86  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 176.890 168.054 201.138 1.00 4.19  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 178.005 167.917 202.148 1.00 11.70 ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 177.405 168.648 199.841 1.00 5.15  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 175.280 164.787 198.416 1.00 8.85  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 174.907 163.474 197.899 1.00 11.97 ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 175.770 162.370 198.498 1.00 18.16 ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 175.253 161.374 199.011 1.00 21.23 ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 174.990 163.475 196.358 1.00 7.63  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 174.702 162.091 195.811 1.00 9.28  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 174.031 164.495 195.778 1.00 10.16 ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 177.087 162.525 198.442 1.00 20.87 ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 178.005 161.483 198.876 1.00 20.84 ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 178.306 161.606 200.366 1.00 22.26 ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 178.141 162.663 200.978 1.00 21.57 ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 179.306 161.541 198.072 1.00 23.52 ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 179.147 161.863 196.581 1.00 23.10 ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 178.393 160.806 195.779 1.00 27.62 ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 177.808 159.872 196.368 1.00 26.65 ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 178.385 160.915 194.536 1.00 26.78 ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 178.756 160.491 200.949 1.00 28.38 ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 179.085 160.464 202.369 1.00 30.44 ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 180.396 161.176 202.672 1.00 30.24 ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 180.534 161.777 203.744 1.00 27.14 ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 179.149 159.020 202.867 1.00 29.58 ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 177.778 158.403 203.043 1.00 32.86 ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 176.865 158.747 202.264 1.00 29.04 ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 177.613 157.571 203.960 1.00 33.59 ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 181.366 161.115 201.757 1.00 27.89 ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 182.629 161.803 201.985 1.00 27.37 ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 182.443 163.315 202.018 1.00 28.79 ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 183.134 164.004 202.773 1.00 31.05 ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 183.652 161.401 200.919 1.00 28.10 ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 183.259 161.728 199.488 1.00 31.71 ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 183.830 163.051 199.014 1.00 36.89 ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 184.769 163.561 199.661 1.00 34.56 ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 183.346 163.577 197.990 1.00 36.03 ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 181.507 163.842 201.226 1.00 21.66 ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 181.210 165.269 201.276 1.00 17.29 ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 180.653 165.670 202.637 1.00 18.52 ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 181.039 166.704 203.198 1.00 22.52 ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 180.230 165.634 200.162 1.00 17.02 ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 180.800 165.462 198.764 1.00 20.41 ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 179.727 165.424 197.694 1.00 22.93 ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 178.531 165.441 198.046 1.00 25.27 ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 180.081 165.377 196.497 1.00 23.56 ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 179.744 164.862 203.189 1.00 15.28 ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 179.185 165.168 204.503 1.00 14.58 ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 180.235 165.035 205.599 1.00 21.94 ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 180.246 165.821 206.555 1.00 24.57 ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 177.988 164.260 204.779 1.00 16.26 ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 176.903 164.355 203.722 1.00 15.15 ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 175.636 163.644 204.152 1.00 17.36 ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 175.569 162.292 203.615 1.00 23.49 ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 174.740 161.907 202.656 1.00 25.03 ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 173.884 162.751 202.103 1.00 21.22 ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 174.770 160.644 202.238 1.00 22.64 ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 181.123 164.045 205.483 1.00 22.95 ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 182.223 163.924 206.436 1.00 21.98 ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 183.141 165.139 206.368 1.00 21.28 ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 183.582 165.656 207.404 1.00 24.58 ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 183.006 162.640 206.169 1.00 22.17 ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 183.973 162.254 207.273 1.00 23.22 ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 185.212 161.585 206.701 1.00 24.46 ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 186.231 162.561 206.331 1.00 27.06 ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 186.572 162.852 205.083 1.00 29.48 ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 186.002 162.250 204.053 1.00 27.94 ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 187.507 163.771 204.864 1.00 26.09 ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 183.439 165.606 205.153 1.00 14.82 ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 184.233 166.818 204.991 1.00 14.40 ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 183.543 168.010 205.634 1.00 17.96 ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 184.188 168.822 206.306 1.00 25.05 ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 184.485 167.081 203.505 1.00 19.03 ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 185.328 168.291 203.226 1.00 22.71 ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 186.670 168.315 202.990 1.00 23.58 ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 184.880 169.651 203.135 1.00 19.06 ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 187.089 169.604 202.769 1.00 19.48 ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 186.010 170.443 202.852 1.00 16.89 ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 183.639 170.276 203.272 1.00 17.19 ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 185.933 171.824 202.703 1.00 16.59 ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 183.566 171.647 203.126 1.00 17.01 ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 184.704 172.406 202.844 1.00 17.36 ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 182.229 168.130 205.438 1.00 17.29 ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 181.493 169.237 206.040 1.00 15.07 ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 181.558 169.185 207.560 1.00 17.23 ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 181.792 170.207 208.210 1.00 23.38 ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 180.040 169.225 205.560 1.00 16.54 ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 180.012 169.325 204.133 1.00 17.94 ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 179.272 170.392 206.156 1.00 14.60 ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 181.371 167.998 208.145 1.00 15.48 ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 181.458 167.865 209.599 1.00 19.03 ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 182.836 168.271 210.106 1.00 22.48 ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 182.967 169.097 211.025 1.00 23.78 ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 181.148 166.426 210.013 1.00 19.58 ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 179.707 166.044 209.771 1.00 22.24 ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 178.848 166.946 209.765 1.00 23.22 ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 179.431 164.841 209.590 1.00 22.43 ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 183.884 167.699 209.506 1.00 19.55 ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 185.241 167.977 209.958 1.00 19.77 ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 185.573 169.454 209.823 1.00 24.05 ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 186.199 170.040 210.711 1.00 29.34 ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 186.243 167.133 209.170 1.00 24.09 ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 186.180 165.648 209.474 1.00 25.36 ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 186.842 164.807 208.403 1.00 26.53 ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 187.257 165.376 207.372 1.00 25.01 ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 186.949 163.578 208.591 1.00 26.82 ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 185.147 170.081 208.726 1.00 18.47 ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 185.501 171.472 208.495 1.00 14.40 ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 184.688 172.427 209.356 1.00 16.29 ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 185.210 173.469 209.760 1.00 23.18 ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 185.355 171.796 207.012 1.00 15.91 ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 186.419 171.117 206.175 1.00 25.26 ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 187.426 171.722 205.819 1.00 28.73 ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 186.215 169.838 205.890 1.00 24.37 ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 183.434 172.095 209.674 1.00 14.42 ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 182.709 172.867 210.681 1.00 15.48 ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 183.453 172.821 212.007 1.00 17.21 ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 183.652 173.851 212.666 1.00 20.14 ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 181.265 172.355 210.830 1.00 15.77 ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 180.472 172.583 209.547 1.00 17.38 ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 180.575 173.018 212.006 1.00 15.94 ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 179.140 171.884 209.527 1.00 14.39 ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 183.890 171.625 212.410 1.00 24.06 ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 184.636 171.507 213.659 1.00 24.09 ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 185.909 172.348 213.625 1.00 24.74 ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 186.193 173.108 214.560 1.00 25.75 ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 184.963 170.038 213.933 1.00 24.75 ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 183.845 169.319 214.661 1.00 28.05 ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 182.673 169.708 214.483 1.00 27.04 ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 184.139 168.364 215.409 1.00 30.63 ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 186.682 172.235 212.541 1.00 19.10 ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 187.952 172.951 212.460 1.00 16.56 ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 187.745 174.459 212.439 1.00 21.21 ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 188.487 175.197 213.095 1.00 26.12 ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 188.745 172.507 211.230 1.00 17.55 ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 187.977 172.748 210.047 1.00 18.70 ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 189.099 171.032 211.322 1.00 18.27 ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 186.743 174.942 211.698 1.00 18.98 ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 186.486 176.380 211.643 1.00 18.34 ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 186.058 176.898 213.010 1.00 18.46 ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 186.521 177.957 213.460 1.00 21.52 ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 185.435 176.693 210.561 1.00 12.96 ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 184.898 178.102 210.734 1.00 13.18 ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 186.032 176.520 209.177 1.00 11.40 ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 185.175 176.165 213.695 1.00 16.46 ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 184.722 176.608 215.007 1.00 15.99 ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 185.871 176.657 216.006 1.00 21.95 ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 185.971 177.599 216.799 1.00 21.29 ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 183.610 175.696 215.515 1.00 18.57 ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 186.746 175.647 215.990 1.00 23.33 ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 187.906 175.694 216.877 1.00 22.72 ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 188.883 176.793 216.478 1.00 22.51 ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 189.539 177.379 217.348 1.00 25.32 ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 188.612 174.336 216.917 1.00 21.88 ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 188.066 173.265 217.870 1.00 24.29 ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 188.214 173.739 219.307 1.00 25.50 ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 186.621 172.886 217.591 1.00 25.21 ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 189.002 177.084 215.181 1.00 18.72 ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 189.921 178.123 214.733 1.00 18.45 ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 189.461 179.506 215.174 1.00 18.17 ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 190.280 180.333 215.593 1.00 20.87 ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 190.073 178.062 213.215 1.00 17.88 ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 190.940 179.157 212.626 1.00 19.37 ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 190.884 179.142 211.108 1.00 20.75 ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 191.762 180.228 210.512 1.00 22.75 ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 191.901 180.082 209.037 1.00 20.15 ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 188.160 179.779 215.090 1.00 18.50 ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 187.652 181.106 215.415 1.00 18.96 ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 187.121 181.228 216.837 1.00 22.53 ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 186.905 182.351 217.300 1.00 20.22 ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 186.555 181.509 214.423 1.00 14.29 ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 187.070 181.797 213.049 1.00 14.63 ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 187.622 183.011 212.704 1.00 15.98 ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 187.136 181.024 211.941 1.00 17.22 ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 187.997 182.976 211.438 1.00 18.69 ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 187.712 181.782 210.952 1.00 18.11 ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 186.910 180.117 217.538 1.00 26.02 ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 186.442 180.133 218.924 1.00 23.97 ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 187.319 179.219 219.767 1.00 28.39 ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 186.894 178.124 220.163 1.00 34.12 ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 184.976 179.715 219.018 1.00 20.79 ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 184.015 180.766 218.556 1.00 18.31 ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 183.577 181.751 219.424 1.00 22.60 ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 183.543 180.768 217.256 1.00 19.13 ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 182.689 182.716 219.006 1.00 22.08 ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 182.653 181.733 216.832 1.00 20.84 ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 182.227 182.708 217.708 1.00 22.02 ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 188.549 179.631 220.063 1.00 30.77 ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 189.388 178.844 220.970 1.00 32.04 ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 188.905 178.984 222.405 1.00 35.00 ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 188.111 179.865 222.747 1.00 37.20 ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 190.788 179.443 220.788 1.00 32.09 ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 190.681 180.393 219.623 1.00 29.62 ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 189.255 180.822 219.572 1.00 29.87 ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 189.397 178.080 223.252 1.00 38.86 ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 189.111 178.096 224.686 1.00 40.62 ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 187.612 177.960 224.957 1.00 41.31 ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 187.021 178.722 225.724 1.00 43.04 ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 189.674 179.360 225.343 1.00 39.44 ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 191.188 179.361 225.396 1.00 43.28 ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 191.812 178.340 225.691 1.00 46.38 ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 191.789 180.508 225.105 1.00 43.06 ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 186.995 176.972 224.311 1.00 38.20 ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 185.600 176.632 224.547 1.00 39.41 ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 185.506 175.134 224.795 1.00 40.12 ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 186.404 174.363 224.448 1.00 42.09 ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 184.676 177.035 223.375 1.00 40.52 ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 185.068 176.285 222.102 1.00 39.31 ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 184.712 178.539 223.153 1.00 39.94 ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 184.075 176.443 220.972 1.00 35.91 ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 184.400 174.728 225.408 1.00 39.22 ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 184.142 173.314 225.665 1.00 40.38 ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 183.821 172.636 224.339 1.00 40.62 ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 182.714 172.764 223.813 1.00 42.03 ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 183.001 173.153 226.663 1.00 41.79 ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 183.128 171.896 227.497 1.00 44.21 ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 183.979 171.046 227.166 1.00 43.43 ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 182.375 171.759 228.483 1.00 45.36 ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 184.801 171.915 223.788 1.00 39.45 ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 184.619 171.294 222.482 1.00 40.09 ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 183.513 170.246 222.510 1.00 41.62 ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 182.658 170.211 221.618 1.00 41.22 ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 185.932 170.668 222.014 1.00 38.42 ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 186.045 170.510 220.510 1.00 37.88 ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 187.456 170.088 220.108 1.00 39.29 ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 187.656 169.925 218.669 1.00 42.11 ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 186.884 169.225 217.845 1.00 42.42 ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 185.858 168.511 218.285 1.00 40.51 ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 187.163 169.219 216.545 1.00 39.24 ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 183.510 169.384 223.530 1.00 44.46 ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 182.511 168.322 223.594 1.00 43.87 ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 181.117 168.878 223.849 1.00 43.31 ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 180.134 168.383 223.286 1.00 46.44 ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 182.889 167.309 224.672 1.00 44.75 ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 182.435 165.892 224.367 1.00 44.50 ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 183.121 165.310 223.145 1.00 45.75 ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 184.332 165.019 223.226 1.00 45.81 ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 182.447 165.147 222.106 1.00 45.12 ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 181.010 169.902 224.700 1.00 36.95 ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 179.700 170.452 225.032 1.00 39.04 ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 179.027 171.072 223.813 1.00 38.77 ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 177.819 170.903 223.612 1.00 35.56 ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 179.832 171.482 226.152 1.00 38.11 ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 178.506 171.981 226.696 1.00 37.98 ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 178.711 172.940 227.856 1.00 39.11 ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 179.136 172.199 229.113 1.00 38.16 ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 179.178 173.097 230.302 1.00 37.20 ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 179.789 171.788 222.990 1.00 36.67 ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 179.242 172.494 221.841 1.00 33.46 ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 179.336 171.705 220.544 1.00 35.19 ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 178.806 172.158 219.524 1.00 36.54 ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 179.945 173.844 221.671 1.00 30.56 ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 179.992 170.541 220.545 1.00 39.26 ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 180.147 169.772 219.315 1.00 36.50 ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 179.912 168.283 219.526 1.00 40.58 ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 180.588 167.454 218.906 1.00 40.94 ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 181.529 169.991 218.695 1.00 38.66 ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 181.780 171.419 218.267 1.00 38.83 ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 181.106 171.699 216.622 1.00 55.54 ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 181.114 173.482 216.562 1.00 37.06 ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 178.969 167.918 220.391 1.00 38.21 ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 178.510 166.536 220.421 1.00 38.17 ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 177.837 166.213 219.095 1.00 37.88 ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 176.911 166.911 218.676 1.00 40.72 ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 177.543 166.319 221.584 1.00 38.37 ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 178.150 166.649 222.820 1.00 39.95 ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 178.303 165.153 218.440 1.00 38.38 ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 177.939 164.912 217.044 1.00 40.54 ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 176.439 164.871 216.774 1.00 44.80 ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 176.015 165.450 215.759 1.00 46.46 ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 178.621 163.630 216.547 1.00 43.71 ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 180.130 163.768 216.380 1.00 45.56 ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 180.472 164.803 215.307 1.00 45.83 ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 180.582 166.154 215.851 1.00 48.57 ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 180.524 167.265 215.128 1.00 46.16 ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 180.339 167.229 213.819 1.00 42.62 ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 180.647 168.441 215.735 1.00 41.88 ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 175.589 164.234 217.592 1.00 36.47 ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 174.146 164.358 217.346 1.00 30.93 ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 173.643 165.756 217.668 1.00 30.15 ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 172.988 165.964 218.693 1.00 32.22 ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 173.528 163.305 218.275 1.00 30.64 ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 174.659 162.438 218.712 1.00 33.35 ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 175.871 163.300 218.694 1.00 32.10 ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 173.948 166.723 216.801 1.00 21.48 ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 173.507 168.098 217.005 1.00 20.02 ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 172.052 168.202 216.574 1.00 18.28 ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 171.752 168.383 215.388 1.00 16.36 ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 174.384 169.102 216.235 1.00 19.22 ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 175.823 169.063 216.740 1.00 20.02 ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 173.856 170.502 216.420 1.00 17.63 ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 176.795 169.826 215.872 1.00 18.53 ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 171.138 168.082 217.531 1.00 16.03 ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 169.708 168.086 217.262 1.00 14.39 ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 169.062 169.260 217.979 1.00 15.30 ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 169.329 169.491 219.163 1.00 19.02 ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 169.061 166.773 217.707 1.00 17.54 ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 169.547 165.518 216.990 1.00 17.08 ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 168.906 164.280 217.585 1.00 20.02 ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 169.253 165.620 215.509 1.00 12.76 ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 168.221 169.995 217.262 1.00 10.77 ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 167.451 171.095 217.818 1.00 8.10  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 165.984 170.879 217.489 1.00 10.58 ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 165.644 170.509 216.361 1.00 17.56 ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 167.920 172.444 217.261 1.00 13.12 ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 169.090 173.048 218.000 1.00 10.99 ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 170.349 172.473 217.935 1.00 11.34 ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 168.935 174.201 218.755 1.00 9.18  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 171.419 173.023 218.606 1.00 11.38 ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 169.999 174.759 219.428 1.00 10.89 ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 171.238 174.166 219.352 1.00 13.27 ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 172.303 174.720 220.023 1.00 15.66 ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 165.115 171.107 218.471 1.00 10.73 ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 163.691 170.903 218.256 1.00 14.10 ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 162.903 171.703 219.280 1.00 15.91 ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 163.365 171.931 220.400 1.00 19.83 ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 163.319 169.420 218.342 1.00 13.21 ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 161.952 169.221 218.028 1.00 13.55 ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 161.703 172.122 218.877 1.00 15.75 ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 160.760 172.792 219.763 1.00 14.77 ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 159.574 171.899 220.110 1.00 17.89 ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 158.495 172.403 220.437 1.00 17.83 ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 160.277 174.103 219.142 1.00 15.51 ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 159.570 173.898 217.817 1.00 17.01 ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 159.519 172.788 217.289 1.00 18.52 ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 159.017 174.975 217.274 1.00 14.54 ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 159.749 170.583 220.023 1.00 19.25 ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 158.682 169.642 220.332 1.00 17.02 ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 158.598 169.311 221.814 1.00 19.28 ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 157.498 169.087 222.329 1.00 22.91 ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 158.875 168.352 219.532 1.00 14.28 ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 158.416 168.454 218.112 1.00 15.12 ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 157.546 169.367 217.597 1.00 16.84 ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 158.806 167.611 217.022 1.00 15.33 ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 157.368 169.145 216.254 1.00 15.53 ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 158.130 168.071 215.876 1.00 14.44 ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 159.659 166.510 216.905 1.00 17.26 ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 158.282 167.470 214.630 1.00 11.25 ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 159.808 165.916 215.667 1.00 16.29 ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 159.124 166.398 214.546 1.00 12.76 ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 159.732 169.281 222.511 1.00 18.66 ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 159.768 168.968 223.933 1.00 21.00 ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 159.734 170.205 224.817 1.00 23.30 ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 159.800 170.074 226.044 1.00 25.90 ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 161.015 168.142 224.258 1.00 22.21 ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 161.081 166.749 223.629 1.00 19.37 ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 162.152 165.915 224.304 1.00 20.87 ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 159.732 166.064 223.724 1.00 20.74 ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 159.633 171.395 224.233 1.00 26.37 ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 159.586 172.636 224.994 1.00 28.31 ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 158.917 173.696 224.129 1.00 28.88 ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 158.584 173.455 222.966 1.00 30.83 ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 160.986 173.071 225.432 1.00 29.02 ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 161.818 173.294 224.308 1.00 26.41 ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 158.714 174.878 224.710 1.00 31.21 ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 158.128 175.975 223.950 1.00 33.56 ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 159.135 176.622 223.009 1.00 32.89 ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 158.751 177.117 221.944 1.00 33.05 ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 157.542 177.022 224.898 1.00 34.11 ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 158.478 177.458 226.012 1.00 35.12 ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 158.003 178.757 226.646 1.00 34.94 ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 159.108 179.421 227.450 1.00 34.55 ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 159.451 178.641 228.671 1.00 36.44 ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 160.413 176.622 223.373 1.00 28.26 ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 161.456 177.279 222.602 1.00 27.56 ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 162.236 176.266 221.776 1.00 27.10 ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 162.182 175.056 222.013 1.00 28.59 ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 162.415 178.043 223.521 1.00 27.54 ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 161.720 179.130 224.313 1.00 32.44 ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 160.730 179.696 223.803 1.00 31.56 ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 162.163 179.420 225.443 1.00 33.44 ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 162.968 176.783 220.793 1.00 21.47 ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 163.820 175.973 219.924 1.00 15.42 ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 165.150 175.753 220.633 1.00 14.99 ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 166.078 176.558 220.531 1.00 21.36 ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 164.004 176.651 218.573 1.00 16.12 ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 164.482 175.732 217.477 1.00 16.10 ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 163.694 174.681 217.033 1.00 14.29 ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 165.718 175.922 216.877 1.00 17.38 ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 164.126 173.841 216.030 1.00 12.94 ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 166.157 175.089 215.872 1.00 14.98 ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 165.359 174.049 215.452 1.00 14.88 ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 165.794 173.215 214.452 1.00 14.03 ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 165.243 174.644 221.357 1.00 13.74 ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 166.421 174.336 222.166 1.00 16.34 ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 166.933 172.960 221.761 1.00 15.96 ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 166.192 172.159 221.170 1.00 17.77 ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 166.103 174.392 223.680 1.00 17.44 ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 165.051 173.345 224.045 1.00 17.37 ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 165.643 175.783 224.079 1.00 18.71 ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 164.855 173.176 225.533 1.00 18.27 ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 168.204 172.662 222.042 1.00 14.79 ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 168.735 171.339 221.697 1.00 15.32 ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 167.968 170.231 222.405 1.00 18.03 ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 167.547 170.373 223.553 1.00 20.08 ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 170.195 171.406 222.164 1.00 10.97 ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 170.252 172.548 223.116 1.00 11.20 ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 169.242 173.530 222.624 1.00 14.70 ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 167.791 169.117 221.700 1.00 17.78 ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 166.983 168.000 222.170 1.00 18.03 ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 167.842 166.744 222.195 1.00 21.80 ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 168.693 166.542 221.321 1.00 19.29 ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 165.727 167.802 221.290 1.00 15.89 ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 166.108 167.399 219.873 1.00 16.22 ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 164.793 166.777 221.909 1.00 20.98 ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 167.643 165.921 223.219 1.00 26.20 ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 168.340 164.648 223.304 1.00 26.84 ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 167.750 163.651 222.313 1.00 26.34 ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 166.550 163.660 222.029 1.00 26.76 ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 168.260 164.087 224.724 1.00 28.59 ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 169.383 163.120 225.030 1.00 31.37 ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 170.297 162.984 224.190 1.00 28.76 ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 169.352 162.497 226.111 1.00 31.57 ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 168.615 162.783 221.783 1.00 22.86 ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 168.179 161.837 220.762 1.00 23.90 ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 167.172 160.835 221.315 1.00 28.47 ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 166.188 160.504 220.644 1.00 27.62 ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 169.386 161.113 220.169 1.00 25.16 ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 169.107 160.440 218.835 1.00 25.32 ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 170.374 160.124 218.066 1.00 26.02 ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 171.206 159.337 218.515 1.00 26.12 ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 170.526 160.741 216.900 1.00 23.44 ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 167.395 160.338 222.534 1.00 29.49 ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 166.499 159.329 223.093 1.00 25.25 ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 165.156 159.929 223.493 1.00 25.40 ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 164.104 159.318 223.266 1.00 27.14 ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 167.161 158.645 224.287 1.00 28.01 ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 168.336 157.757 223.910 1.00 32.04 ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 168.053 156.910 222.684 1.00 32.20 ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 167.165 156.035 222.756 1.00 31.64 ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 168.720 157.120 221.648 1.00 27.41 ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 165.168 161.118 224.097 1.00 29.49 ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 163.915 161.786 224.433 1.00 30.01 ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 163.123 162.117 223.175 1.00 29.45 ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 161.898 161.940 223.134 1.00 29.99 ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 164.198 163.052 225.241 1.00 26.60 ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 164.545 162.793 226.694 1.00 28.92 ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 164.899 164.062 227.442 1.00 33.08 ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 164.015 164.932 227.592 1.00 35.06 ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 166.063 164.190 227.878 1.00 31.95 ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 163.812 162.590 222.135 1.00 23.79 ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 163.153 162.842 220.861 1.00 22.02 ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 162.579 161.560 220.279 1.00 24.73 ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 161.472 161.560 219.733 1.00 27.43 ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 164.132 163.485 219.880 1.00 18.71 ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 163.652 163.636 218.437 1.00 17.10 ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 162.663 164.781 218.318 1.00 19.35 ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 164.832 163.840 217.505 1.00 22.74 ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 163.318 160.453 220.384 1.00 21.77 ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 162.824 159.182 219.870 1.00 19.37 ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 161.562 158.742 220.600 1.00 20.88 ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 160.603 158.285 219.972 1.00 20.13 ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 163.908 158.111 219.987 1.00 22.41 ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 163.610 156.843 219.209 1.00 22.27 ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 164.518 155.708 219.646 1.00 20.62 ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 165.926 156.073 219.552 1.00 21.71 ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 166.638 156.023 218.434 1.00 24.76 ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 166.104 155.622 217.292 1.00 20.55 ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 167.917 156.383 218.465 1.00 24.68 ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 161.541 158.878 221.927 1.00 20.97 ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 160.352 158.502 222.689 1.00 19.68 ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 159.161 159.387 222.331 1.00 23.83 ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 158.034 158.896 222.164 1.00 27.51 ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 160.644 158.579 224.187 1.00 20.37 ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 161.819 157.715 224.595 1.00 27.33 ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 162.292 156.918 223.759 1.00 25.45 ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 162.272 157.835 225.753 1.00 28.86 ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 159.392 160.697 222.210 1.00 20.48 ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 158.309 161.605 221.847 1.00 16.97 ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 157.769 161.289 220.459 1.00 16.72 ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 156.551 161.292 220.241 1.00 20.39 ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 158.794 163.051 221.924 1.00 16.69 ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 157.750 164.070 221.532 1.00 17.37 ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 156.761 164.458 222.425 1.00 16.13 ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 157.757 164.649 220.272 1.00 18.36 ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 155.806 165.389 222.072 1.00 16.46 ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 156.808 165.579 219.911 1.00 17.77 ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 155.836 165.947 220.813 1.00 19.52 ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 154.888 166.876 220.451 1.00 20.43 ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 158.662 161.007 219.507 1.00 11.94 ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 158.230 160.661 218.158 1.00 17.41 ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 157.492 159.329 218.158 1.00 19.50 ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 156.546 159.137 217.395 1.00 20.38 ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 159.431 160.658 217.194 1.00 17.62 ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 159.032 160.113 215.836 1.00 14.77 ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 159.979 162.065 217.037 1.00 17.97 ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 157.899 158.391 219.017 1.00 18.69 ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 157.169 157.131 219.137 1.00 15.76 ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 155.738 157.365 219.601 1.00 17.28 ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 154.788 156.806 219.038 1.00 20.93 ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 157.894 156.192 220.104 1.00 15.72 ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 159.096 155.483 219.514 1.00 19.10 ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 159.827 154.669 220.567 1.00 20.35 ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 161.106 154.068 220.010 1.00 20.03 ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 161.876 153.343 221.056 1.00 19.38 ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 155.563 158.188 220.636 1.00 15.84 ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 154.215 158.469 221.129 1.00 16.08 ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 153.380 159.180 220.068 1.00 18.68 ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 152.212 158.829 219.827 1.00 20.34 ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 154.291 159.303 222.408 1.00 13.54 ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 153.969 160.184 219.414 1.00 16.55 ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 153.255 160.893 218.359 1.00 18.79 ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 152.933 159.971 217.193 1.00 16.10 ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 151.902 160.140 216.541 1.00 16.07 ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 154.074 162.093 217.884 1.00 19.51 ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 154.311 163.144 218.954 1.00 17.17 ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 153.059 163.403 219.772 1.00 14.92 ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 152.047 164.121 219.007 1.00 17.60 ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 150.757 164.151 219.316 1.00 19.70 ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 150.284 163.510 220.373 1.00 19.60 ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 149.921 164.841 218.546 1.00 19.32 ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 153.786 158.981 216.932 1.00 13.60 ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 153.522 158.029 215.862 1.00 15.77 ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 152.381 157.096 216.227 1.00 19.29 ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 151.586 156.718 215.364 1.00 23.44 ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 154.788 157.232 215.546 1.00 15.92 ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 155.650 157.750 214.397 1.00 18.23 ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 156.842 156.838 214.178 1.00 16.39 ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 154.830 157.876 213.125 1.00 17.40 ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 152.289 156.699 217.498 1.00 20.10 ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 151.131 155.920 217.935 1.00 18.55 ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 149.844 156.706 217.725 1.00 20.52 ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 148.856 156.185 217.183 1.00 21.84 ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 151.282 155.518 219.402 1.00 19.23 ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 152.554 154.756 219.723 1.00 22.19 ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 152.488 154.137 221.110 1.00 24.54 ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 153.848 153.609 221.544 1.00 24.25 ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 154.192 154.033 222.928 1.00 17.32 ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 149.846 157.981 218.129 1.00 21.72 ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 148.665 158.818 217.915 1.00 19.90 ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 148.383 158.979 216.424 1.00 23.37 ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 147.224 159.008 215.994 1.00 23.92 ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 148.840 160.180 218.612 1.00 20.65 ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 147.571 161.004 218.484 1.00 19.56 ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 149.197 159.982 220.074 1.00 23.17 ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 149.441 159.084 215.615 1.00 23.13 ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 149.289 159.211 214.168 1.00 19.38 ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 148.654 157.965 213.567 1.00 18.51 ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 147.784 158.061 212.693 1.00 19.26 ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 150.660 159.479 213.544 1.00 15.99 ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 150.628 159.721 212.065 1.00 14.47 ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 149.985 160.828 211.541 1.00 17.23 ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 151.262 158.851 211.196 1.00 15.88 ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 149.967 161.055 210.180 1.00 17.38 ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 151.243 159.070 209.836 1.00 15.85 ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 150.594 160.174 209.327 1.00 17.00 ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 149.084 156.783 214.016 1.00 17.66 ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 148.491 155.543 213.529 1.00 21.41 ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 147.023 155.458 213.909 1.00 27.59 ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 146.181 155.069 213.090 1.00 27.53 ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 149.233 154.326 214.083 1.00 23.15 ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 150.715 154.286 213.803 1.00 22.03 ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 151.225 154.690 212.579 1.00 22.61 ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 151.602 153.798 214.753 1.00 22.33 ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 152.580 154.646 212.324 1.00 20.82 ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 152.957 153.746 214.506 1.00 23.00 ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 153.440 154.170 213.289 1.00 25.09 ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 154.790 154.117 213.040 1.00 27.78 ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 146.691 155.818 215.151 1.00 34.25 ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 145.310 155.674 215.591 1.00 32.90 ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 144.374 156.712 214.983 1.00 33.37 ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 143.156 156.579 215.135 1.00 36.12 ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 145.232 155.736 217.118 1.00 30.34 ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 145.078 157.135 217.684 1.00 34.80 ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 145.092 157.151 219.199 1.00 39.04 ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 145.940 156.456 219.796 1.00 37.59 ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 144.252 157.859 219.794 1.00 37.51 ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 144.896 157.728 214.298 1.00 32.71 ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 144.053 158.799 213.778 1.00 33.90 ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 144.125 158.979 212.271 1.00 35.46 ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 143.084 159.153 211.631 1.00 36.83 ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 144.413 160.128 214.456 1.00 34.23 ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 144.083 160.177 215.936 1.00 36.64 ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 144.435 161.508 216.564 1.00 38.86 ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 144.948 162.390 215.843 1.00 37.33 ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 144.198 161.675 217.778 1.00 39.65 ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 145.318 158.947 211.675 1.00 33.65 ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 145.489 159.344 210.282 1.00 29.15 ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 145.903 158.192 209.375 1.00 27.99 ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 145.197 157.884 208.411 1.00 32.43 ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 146.517 160.480 210.191 1.00 26.55 ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 145.979 161.841 210.586 1.00 28.46 ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 145.175 162.490 209.481 1.00 33.54 ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 145.354 162.101 208.308 1.00 33.94 ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 144.364 163.391 209.782 1.00 34.88 ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 147.031 157.544 209.656 1.00 24.02 ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 147.594 156.546 208.748 1.00 23.82 ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 148.173 155.414 209.581 1.00 23.68 ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 149.121 155.626 210.343 1.00 29.04 ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 148.664 157.166 207.850 1.00 24.88 ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 149.148 156.319 206.678 1.00 25.52 ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 148.010 156.113 205.702 1.00 26.88 ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 150.332 156.975 205.990 1.00 23.45 ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 147.613 154.215 209.431 1.00 22.87 ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 148.032 153.063 210.230 1.00 25.55 ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 149.081 152.236 209.483 1.00 28.87 ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 148.894 151.060 209.174 1.00 31.02 ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 146.824 152.217 210.606 1.00 27.93 ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 147.046 151.418 211.875 1.00 33.37 ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 148.000 150.612 211.911 1.00 33.37 ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 146.269 151.595 212.835 1.00 32.90 ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 150.204 152.880 209.197 1.00 25.37 ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 151.352 152.243 208.571 1.00 24.68 ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 152.528 152.338 209.534 1.00 23.84 ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 153.180 153.379 209.632 1.00 26.86 ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 151.690 152.892 207.217 1.00 24.81 ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 152.949 152.277 206.634 1.00 22.47 ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 150.526 152.745 206.251 1.00 23.98 ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 152.819 151.271 210.278 1.00 21.69 ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 153.892 151.339 211.278 1.00 19.73 ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 155.236 151.672 210.646 1.00 21.05 ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 155.576 151.183 209.567 1.00 26.07 ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 153.894 149.934 211.890 1.00 18.84 ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 152.521 149.414 211.640 1.00 20.29 ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 152.116 149.979 210.312 1.00 20.34 ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 156.005 152.506 211.342 1.00 15.53 ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 157.293 152.984 210.860 1.00 14.73 ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 158.378 152.627 211.865 1.00 17.75 ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 158.206 152.834 213.071 1.00 20.46 ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 157.272 154.497 210.629 1.00 11.83 ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 156.132 155.062 209.784 1.00 13.79 ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 156.315 156.557 209.587 1.00 16.27 ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 156.053 154.351 208.445 1.00 12.87 ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 159.493 152.093 211.364 1.00 14.38 ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 160.637 151.823 212.223 1.00 12.29 ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 161.456 153.095 212.379 1.00 11.71 ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 161.827 153.745 211.392 1.00 15.68 ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 161.485 150.677 211.647 1.00 15.88 ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 162.792 150.544 212.411 1.00 16.97 ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 160.705 149.372 211.679 1.00 14.24 ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 161.739 153.462 213.625 1.00 10.81 ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 162.431 154.705 213.945 1.00 16.09 ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 163.923 154.434 214.076 1.00 17.03 ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 164.344 153.626 214.909 1.00 24.90 ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 161.882 155.322 215.230 1.00 13.89 ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 160.532 156.028 215.143 1.00 13.54 ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 160.256 156.765 216.433 1.00 13.69 ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 160.508 156.983 213.971 1.00 16.24 ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 164.714 155.111 213.251 1.00 10.13 ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 166.159 155.151 213.392 1.00 11.74 ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 166.621 156.601 213.294 1.00 14.72 ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 165.828 157.509 213.034 1.00 19.56 ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 166.856 154.247 212.361 1.00 12.60 ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 166.476 154.527 210.934 1.00 16.02 ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 165.414 153.860 210.350 1.00 10.48 ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 167.200 155.422 210.169 1.00 17.43 ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 165.066 154.097 209.037 1.00 7.72  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 166.853 155.664 208.853 1.00 13.08 ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 165.787 154.999 208.287 1.00 9.54  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 167.919 156.811 213.524 1.00 11.45 ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 168.431 158.162 213.748 1.00 15.12 ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 168.200 159.071 212.547 1.00 16.20 ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 167.849 160.248 212.706 1.00 18.75 ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 169.919 158.094 214.094 1.00 17.23 ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 170.205 157.151 215.244 1.00 18.66 ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 169.286 156.613 215.861 1.00 16.86 ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 171.482 156.943 215.538 1.00 15.44 ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 168.395 158.547 211.335 1.00 11.77 ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 168.182 159.364 210.146 1.00 10.59 ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 166.720 159.774 210.011 1.00 12.05 ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 166.421 160.854 209.490 1.00 14.47 ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 168.660 158.623 208.898 1.00 9.06  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 170.164 158.388 208.853 1.00 14.28 ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 170.584 157.092 209.519 1.00 23.44 ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 170.206 156.867 210.689 1.00 24.17 ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 171.298 156.298 208.871 1.00 20.48 ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 165.795 158.938 210.485 1.00 8.13  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 164.383 159.318 210.475 1.00 9.07  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 164.151 160.514 211.392 1.00 13.10 ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 163.405 161.441 211.057 1.00 19.94 ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 163.495 158.124 210.868 1.00 7.41  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 162.089 158.592 211.176 1.00 6.35  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 163.462 157.113 209.748 1.00 11.10 ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 164.780 160.503 212.570 1.00 6.01  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 164.665 161.640 213.479 1.00 7.44  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 165.242 162.902 212.850 1.00 13.97 ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 164.631 163.978 212.918 1.00 19.47 ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 165.371 161.323 214.799 1.00 11.52 ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 164.946 160.036 215.507 1.00 11.43 ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 165.582 159.944 216.881 1.00 14.88 ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 163.433 159.955 215.612 1.00 13.57 ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 166.408 162.783 212.211 1.00 9.91  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 166.996 163.931 211.529 1.00 7.44  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 166.053 164.467 210.458 1.00 6.19  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 165.834 165.681 210.353 1.00 12.45 ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 168.336 163.541 210.906 1.00 9.42  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 169.367 163.144 211.939 1.00 17.55 ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 169.253 163.593 213.097 1.00 19.92 ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 170.297 162.387 211.592 1.00 19.30 ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 165.477 163.568 209.661 1.00 3.19  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 164.623 163.982 208.555 1.00 5.22  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 163.347 164.646 209.049 1.00 6.87  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 162.916 165.658 208.486 1.00 15.99 ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 164.303 162.780 207.671 1.00 8.03  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 165.495 162.228 206.953 1.00 9.23  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 165.552 160.933 206.490 1.00 10.46 ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 166.677 162.799 206.622 1.00 7.18  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 166.717 160.728 205.904 1.00 10.25 ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 167.419 161.845 205.970 1.00 8.71  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 162.720 164.095 210.090 1.00 4.45  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 161.497 164.711 210.595 1.00 7.33  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 161.804 166.069 211.214 1.00 4.89  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 161.010 167.007 211.097 1.00 7.08  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 160.758 163.779 211.577 1.00 7.87  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 160.355 162.487 210.883 1.00 4.80  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 161.587 163.494 212.813 1.00 7.76  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 162.968 166.209 211.858 1.00 4.19  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 163.349 167.520 212.380 1.00 6.68  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 163.540 168.532 211.255 1.00 6.27  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 163.090 169.679 211.360 1.00 10.35 ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 164.617 167.397 213.224 1.00 6.99  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 164.432 166.744 214.596 1.00 7.16  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 165.671 166.934 215.453 1.00 9.90  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 163.207 167.303 215.295 1.00 5.81  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 164.195 168.124 210.164 1.00 6.78  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 164.376 169.027 209.028 1.00 2.94  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 163.039 169.418 208.407 1.00 3.59  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 162.815 170.588 208.062 1.00 9.86  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 165.271 168.380 207.975 1.00 5.67  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 166.655 168.004 208.458 1.00 6.06  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 167.375 167.181 207.407 1.00 6.44  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 168.451 166.381 207.976 1.00 9.63  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 169.259 165.606 207.267 1.00 14.93 ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 169.142 165.502 205.953 1.00 9.72  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 170.209 164.916 207.893 1.00 14.37 ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 162.141 168.444 208.244 1.00 4.34  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 160.843 168.727 207.640 1.00 6.77  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 160.032 169.660 208.529 1.00 3.80  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 159.341 170.556 208.037 1.00 3.61  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 160.092 167.415 207.344 1.00 5.17  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 160.863 166.582 206.321 1.00 2.63  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 158.703 167.701 206.812 1.00 2.06  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 160.294 165.201 206.113 1.00 3.54  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 160.105 169.471 209.849 1.00 3.83  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 159.440 170.393 210.766 1.00 3.59  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 160.023 171.796 210.650 1.00 7.85  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 159.280 172.788 210.631 1.00 10.31 ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 159.559 169.875 212.197 1.00 3.58  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 158.808 170.733 213.192 1.00 15.26 ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 157.563 170.795 213.104 1.00 17.31 ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 159.460 171.345 214.064 1.00 19.17 ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 161.353 171.896 210.566 1.00 11.07 ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 161.999 173.191 210.386 1.00 5.00  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 161.457 173.905 209.157 1.00 5.76  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 161.129 175.096 209.208 1.00 4.26  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 163.511 173.011 210.259 1.00 3.62  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 164.266 172.992 211.566 1.00 7.64  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 165.750 172.821 211.308 1.00 8.83  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 166.155 173.449 210.056 1.00 11.15 ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 166.919 174.528 209.971 1.00 12.35 ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 167.385 175.132 211.053 1.00 6.27  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 167.227 175.013 208.772 1.00 11.82 ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 161.360 173.189 208.038 1.00 9.35  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 160.894 173.823 206.807 1.00 7.28  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 159.409 174.160 206.901 1.00 7.42  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 158.969 175.214 206.427 1.00 10.25 ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 161.203 172.936 205.590 1.00 8.00  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 162.701 172.645 205.518 1.00 7.85  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 160.751 173.621 204.318 1.00 6.39  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 163.566 173.877 205.653 1.00 7.31  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 158.614 173.278 207.511 1.00 8.06  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 157.183 173.525 207.647 1.00 6.38  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 156.875 174.690 208.575 1.00 7.44  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 155.773 175.243 208.505 1.00 7.76  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 156.476 172.270 208.157 1.00 4.22  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 156.143 171.281 207.081 1.00 5.37  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 156.249 171.628 205.747 1.00 8.19  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 155.721 170.006 207.404 1.00 4.80  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 155.941 170.720 204.759 1.00 8.57  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 155.413 169.092 206.419 1.00 5.08  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 155.524 169.450 205.096 1.00 6.80  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 157.809 175.069 209.442 1.00 9.87  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 157.595 176.203 210.330 1.00 8.30  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 158.020 177.533 209.718 1.00 8.15  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 157.956 178.559 210.402 1.00 11.33 ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 158.339 175.988 211.652 1.00 8.28  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 157.697 174.955 212.560 1.00 7.69  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 158.418 174.882 213.892 1.00 8.55  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 159.799 174.442 213.736 1.00 12.87 ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 160.856 175.223 213.907 1.00 14.76 ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 160.727 176.494 214.248 1.00 10.48 ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 162.072 174.717 213.727 1.00 16.26 ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 158.450 177.546 208.441 1.00 8.36  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 158.892 178.769 207.790 1.00 8.13  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 157.824 179.297 206.841 1.00 8.65  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 157.043 178.523 206.280 1.00 11.79 ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 160.183 178.534 207.004 1.00 5.87  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 161.373 178.117 207.847 1.00 6.79  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 162.557 177.699 206.999 1.00 15.25 ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 162.506 177.757 205.771 1.00 15.16 ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 163.632 177.270 207.651 1.00 15.71 ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 157.764 180.613 206.638 1.00 12.78 ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 156.845 181.155 205.630 1.00 9.87  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 157.349 180.861 204.226 1.00 8.16  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 158.539 181.000 203.934 1.00 12.06 ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 156.844 182.658 205.924 1.00 10.60 ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 158.173 182.909 206.547 1.00 10.82 ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 158.498 181.675 207.345 1.00 12.14 ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 156.422 180.457 203.355 1.00 9.15  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 156.752 180.046 201.990 1.00 8.78  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 157.814 178.952 201.998 1.00 9.31  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 158.742 178.945 201.187 1.00 7.77  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 157.200 181.239 201.145 1.00 6.66  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 156.866 181.115 199.669 1.00 8.43  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 157.212 182.366 198.887 1.00 11.13 ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 157.767 183.318 199.433 1.00 11.59 ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 156.887 182.370 197.602 1.00 10.29 ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 157.677 178.017 202.935 1.00 9.97  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 158.642 176.949 203.093 1.00 5.83  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 158.306 175.720 202.276 1.00 6.48  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 157.421 174.943 202.643 1.00 10.39 ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 159.011 175.536 201.166 1.00 7.50  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 158.799 174.408 200.275 1.00 4.39  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 159.966 173.437 200.380 1.00 4.12  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 161.104 173.835 200.633 1.00 11.54 ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 158.636 174.879 198.828 1.00 6.55  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 157.657 175.998 198.663 1.00 4.40  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 156.320 175.868 198.969 1.00 3.70  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 157.821 177.270 198.225 1.00 8.44  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 155.701 177.010 198.725 1.00 6.58  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 156.590 177.876 198.274 1.00 12.52 ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 159.673 172.157 200.174 1.00 2.82  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 160.653 171.096 200.331 1.00 1.85  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 160.880 170.381 199.008 1.00 2.53  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 159.969 170.253 198.185 1.00 11.31 ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 160.205 170.079 201.384 1.00 3.50  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 160.643 170.343 202.822 1.00 4.63  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 159.842 169.492 203.786 1.00 4.47  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 162.125 170.081 202.974 1.00 2.78  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 162.113 169.916 198.810 1.00 2.51  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 162.480 169.067 197.678 1.00 2.67  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 163.221 167.871 198.267 1.00 4.22  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 164.428 167.935 198.514 1.00 7.63  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 163.325 169.821 196.658 1.00 6.35  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 163.796 169.013 195.448 1.00 3.70  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 162.614 168.422 194.703 1.00 4.15  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 164.633 169.874 194.522 1.00 6.87  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 162.490 166.788 198.515 1.00 4.05  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 163.056 165.580 199.101 1.00 3.41  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 163.477 164.650 197.972 1.00 3.84  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 162.634 164.160 197.214 1.00 6.84  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 162.046 164.903 200.024 1.00 3.65  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 161.399 165.781 201.094 1.00 4.39  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 160.526 164.946 202.007 1.00 1.59  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 162.456 166.517 201.892 1.00 9.35  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 164.778 164.403 197.857 1.00 3.51  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 165.330 163.576 196.793 1.00 4.62  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 165.843 162.288 197.416 1.00 5.52  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 166.710 162.322 198.295 1.00 8.97  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 166.447 164.302 196.030 1.00 5.86  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 165.969 165.683 195.585 1.00 4.74  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 166.886 163.486 194.833 1.00 6.80  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 166.990 166.446 194.787 1.00 8.94  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 165.313 161.158 196.967 1.00 3.95  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 165.734 159.882 197.512 1.00 4.02  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 165.058 158.736 196.796 1.00 6.69  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 164.164 158.927 195.969 1.00 9.85  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 165.510 157.528 197.135 1.00 4.96  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 164.975 156.321 196.522 1.00 5.30  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 163.524 156.126 196.949 1.00 8.78  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 163.140 156.422 198.089 1.00 15.33 ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 165.845 155.109 196.903 1.00 3.16  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 165.227 153.812 196.414 1.00 8.04  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 167.246 155.274 196.343 1.00 9.37  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 162.703 155.641 196.019 1.00 3.64  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 161.301 155.387 196.320 1.00 4.85  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 161.175 154.364 197.440 1.00 5.82  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 161.971 153.430 197.541 1.00 11.98 ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 160.573 154.897 195.070 1.00 7.03  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 160.653 155.852 194.029 1.00 12.80 ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 160.177 154.554 198.298 1.00 2.78  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 160.001 153.683 199.438 1.00 0.65  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 160.863 154.012 200.635 1.00 6.78  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 160.859 153.249 201.607 1.00 10.80 ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 161.604 155.121 200.597 1.00 7.18  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 162.442 155.497 201.727 1.00 6.28  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 161.648 156.149 202.848 1.00 7.96  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 162.177 156.311 203.953 1.00 12.53 ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 163.557 156.437 201.270 1.00 4.05  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 160.400 156.527 202.595 1.00 4.65  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 159.573 157.159 203.599 1.00 3.76  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 159.408 158.654 203.469 1.00 2.89  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 158.936 159.286 204.418 1.00 7.69  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 159.782 159.243 202.332 1.00 2.37  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 159.687 160.691 202.171 1.00 1.83  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 158.245 161.170 202.300 1.00 4.76  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 157.949 162.093 203.068 1.00 6.50  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 160.273 161.102 200.821 1.00 2.81  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 161.585 160.418 200.484 1.00 2.50  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 162.233 161.035 199.260 1.00 3.53  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 161.415 160.777 198.010 1.00 7.95  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 161.363 159.332 197.666 1.00 4.61  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 157.330 160.544 201.556 1.00 8.04  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 155.927 160.945 201.618 1.00 2.40  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 155.332 160.676 202.995 1.00 6.26  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 154.598 161.510 203.535 1.00 13.26 ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 155.122 160.219 200.542 1.00 3.83  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 155.733 160.429 199.263 1.00 6.68  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 153.695 160.734 200.503 1.00 7.38  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 155.637 159.514 203.577 1.00 6.26  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 155.084 159.173 204.885 1.00 3.00  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 155.597 160.118 205.964 1.00 4.81  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 154.828 160.580 206.815 1.00 10.21 ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 155.423 157.724 205.235 1.00 4.71  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 155.223 156.896 204.083 1.00 14.19 ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 154.536 157.232 206.364 1.00 4.89  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 156.898 160.417 205.946 1.00 4.03  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 157.451 161.343 206.928 1.00 2.07  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 156.892 162.746 206.736 1.00 4.47  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 156.615 163.450 207.714 1.00 9.26  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 158.977 161.353 206.846 1.00 0.91  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 159.700 160.126 207.405 1.00 2.52  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 161.171 160.429 207.629 1.00 7.52  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 159.047 159.642 208.689 1.00 2.53  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 156.721 163.170 205.481 1.00 4.26  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 156.128 164.478 205.225 1.00 2.24  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 154.704 164.549 205.759 1.00 5.03  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 154.317 165.545 206.381 1.00 11.36 ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 156.154 164.779 203.727 1.00 2.35  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 157.469 164.674 203.213 1.00 8.76  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 153.911 163.498 205.534 1.00 5.84  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 152.549 163.469 206.055 1.00 3.78  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 152.538 163.485 207.577 1.00 7.61  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 151.724 164.185 208.192 1.00 11.01 ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 151.811 162.240 205.530 1.00 3.30  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 151.533 162.273 204.040 1.00 6.47  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 150.843 161.004 203.581 1.00 5.24  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 149.456 160.953 204.022 1.00 12.81 ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 148.529 160.169 203.488 1.00 17.28 ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 148.810 159.354 202.484 1.00 15.93 ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 147.293 160.203 203.973 1.00 13.07 ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 153.436 162.722 208.203 1.00 6.08  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 153.495 162.688 209.661 1.00 4.74  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 153.849 164.055 210.232 1.00 8.25  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 153.231 164.510 211.202 1.00 10.68 ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 154.508 161.639 210.117 1.00 5.57  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 154.850 161.720 211.576 1.00 9.35  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 153.865 161.604 212.541 1.00 13.43 ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 156.159 161.913 211.985 1.00 9.21  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 154.177 161.679 213.883 1.00 12.74 ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 156.475 161.988 213.324 1.00 8.65  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 155.484 161.871 214.275 1.00 11.24 ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 154.835 164.731 209.640 1.00 7.74  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 155.241 166.035 210.152 1.00 4.79  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 154.156 167.075 209.898 1.00 8.65  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 153.900 167.940 210.744 1.00 14.51 ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 156.591 166.454 209.545 1.00 1.95  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 156.953 167.855 209.991 1.00 8.31  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 157.675 165.477 209.953 1.00 2.62  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 153.497 167.010 208.738 1.00 5.31  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 152.404 167.935 208.461 1.00 1.75  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 151.260 167.742 209.445 1.00 6.68  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 150.645 168.716 209.893 1.00 13.08 ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 151.916 167.756 207.025 1.00 0.00  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 150.955 166.489 209.790 1.00 6.38  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 149.959 166.231 210.824 1.00 7.95  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 150.415 166.775 212.169 1.00 8.94  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 149.606 167.306 212.940 1.00 13.41 ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 149.677 164.733 210.916 1.00 12.56 ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 148.897 164.343 212.132 1.00 14.75 ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 147.543 164.385 212.283 1.00 13.64 ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 149.424 163.848 213.368 1.00 10.05 ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 147.194 163.948 213.538 1.00 16.07 ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 148.332 163.614 214.223 1.00 11.72 ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 150.714 163.585 213.834 1.00 9.60  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 148.490 163.126 215.516 1.00 12.79 ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 150.868 163.101 215.117 1.00 11.77 ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 149.764 162.876 215.943 1.00 14.39 ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 151.708 166.645 212.475 1.00 5.85  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 152.231 167.180 213.728 1.00 6.58  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 152.096 168.696 213.787 1.00 10.84 ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 151.743 169.254 214.830 1.00 13.51 ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 153.692 166.770 213.903 1.00 6.14  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 153.878 165.456 214.627 1.00 10.91 ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 155.465 165.393 215.469 1.00 29.69 ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 155.024 166.167 217.019 1.00 13.01 ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 152.375 169.377 212.680 1.00 12.64 ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 152.310 170.830 212.623 1.00 7.93  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 150.911 171.353 212.328 1.00 13.22 ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 150.719 172.571 212.278 1.00 17.89 ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 153.288 171.359 211.570 1.00 4.22  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 154.707 171.440 212.087 1.00 10.23 ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 155.082 172.405 212.752 1.00 13.37 ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 155.506 170.425 211.787 1.00 10.29 ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 149.934 170.472 212.133 1.00 9.23  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 148.580 170.886 211.845 1.00 3.95  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 148.289 171.185 210.391 1.00 6.86  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 147.179 171.634 210.083 1.00 12.20 ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 149.242 170.963 209.492 1.00 4.45  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 148.998 171.199 208.077 1.00 4.06  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 148.128 170.093 207.498 1.00 3.99  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 148.267 168.920 207.853 1.00 6.80  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 150.318 171.280 207.308 1.00 7.61  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 151.520 171.989 207.937 1.00 6.90  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 152.656 172.068 206.935 1.00 5.92  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 151.159 173.372 208.434 1.00 9.59  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 147.224 170.472 206.599 1.00 5.54  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 146.377 169.515 205.901 1.00 4.93  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 147.102 169.019 204.658 1.00 8.23  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 147.561 169.819 203.843 1.00 11.73 ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 145.042 170.151 205.519 1.00 5.85  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 144.416 170.734 206.647 1.00 12.84 ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 147.213 167.703 204.525 1.00 9.01  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 147.963 167.113 203.421 1.00 5.89  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 147.073 167.051 202.188 1.00 4.69  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 145.951 166.532 202.241 1.00 11.38 ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 148.485 165.719 203.803 1.00 6.59  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 148.934 164.962 202.566 1.00 8.24  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 149.622 165.839 204.801 1.00 5.43  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 147.568 167.584 201.075 1.00 1.58  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 146.867 167.532 199.799 1.00 7.15  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 147.747 166.846 198.767 1.00 10.50 ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 148.884 167.266 198.535 1.00 12.20 ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 146.482 168.932 199.311 1.00 4.66  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 145.567 168.921 198.105 1.00 8.41  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 146.079 168.816 196.818 1.00 8.10  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 144.192 169.009 198.253 1.00 14.09 ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 145.249 168.800 195.717 1.00 11.44 ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 143.352 168.996 197.157 1.00 13.80 ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 143.887 168.892 195.893 1.00 15.11 ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 143.054 168.878 194.797 1.00 16.78 ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 147.211 165.802 198.140 1.00 10.03 ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 147.887 165.094 197.064 1.00 8.36  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 146.946 164.986 195.875 1.00 15.61 ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 145.755 164.709 196.041 1.00 17.83 ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 148.336 163.699 197.508 1.00 9.61  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 149.072 163.677 198.836 1.00 12.23 ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 149.535 162.290 199.223 1.00 14.01 ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 149.015 161.689 200.162 1.00 14.07 ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 150.520 161.772 198.498 1.00 8.96  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 147.480 165.208 194.680 1.00 18.66 ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 146.678 165.122 193.466 1.00 21.93 ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 146.500 163.658 193.087 1.00 24.14 ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 147.469 162.892 193.034 1.00 23.49 ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 147.320 165.927 192.323 1.00 21.50 ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 148.799 165.576 192.171 1.00 23.84 ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 147.150 167.419 192.563 1.00 22.36 ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 149.474 166.292 191.024 1.00 24.41 ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 145.253 163.261 192.839 1.00 30.90 ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 144.925 161.880 192.486 1.00 30.09 ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 145.035 161.743 190.973 1.00 32.24 ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 144.066 161.922 190.236 1.00 33.94 ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 143.536 161.513 192.992 1.00 29.65 ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 143.348 161.750 194.479 1.00 29.73 ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 144.370 160.973 195.293 1.00 28.21 ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 144.395 161.438 196.739 1.00 30.20 ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 143.039 161.425 197.351 1.00 33.26 ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 146.236 161.420 190.508 1.00 29.25 ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 146.513 161.336 189.080 1.00 30.76 ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 146.046 159.991 188.545 1.00 31.01 ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 146.326 158.938 189.131 1.00 32.92 ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 148.012 161.555 188.812 1.00 30.93 ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 148.315 161.416 187.330 1.00 29.29 ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 148.446 162.918 189.320 1.00 30.73 ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 145.321 160.023 187.428 1.00 36.94 ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 144.922 158.806 186.735 1.00 37.67 ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 145.313 158.893 185.264 1.00 40.06 ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 146.013 159.827 184.861 1.00 41.35 ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 143.421 158.557 186.891 1.00 37.81 ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 142.578 159.780 186.696 1.00 38.24 ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 142.297 160.301 185.453 1.00 38.50 ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 141.952 160.581 187.590 1.00 37.31 ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 141.536 161.372 185.589 1.00 38.62 ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 141.312 161.563 186.876 1.00 39.84 ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 144.873 157.924 184.456 1.00 45.00 ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 145.291 157.887 183.057 1.00 46.81 ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 144.697 159.038 182.254 1.00 47.88 ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 145.299 159.478 181.268 1.00 45.93 ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 144.910 156.550 182.425 1.00 46.42 ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 143.438 156.194 182.543 1.00 48.74 ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 143.176 154.778 182.057 1.00 48.82 ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 143.477 154.624 180.639 1.00 48.84 ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 144.463 153.877 180.160 1.00 48.46 ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 145.269 153.199 180.960 1.00 46.68 ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 144.646 153.812 178.844 1.00 47.35 ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 143.530 159.538 182.653 1.00 45.95 ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 142.869 160.633 181.958 1.00 46.00 ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 143.145 161.985 182.601 1.00 44.46 ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 142.477 162.969 182.266 1.00 45.58 ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 141.362 160.382 181.893 1.00 47.60 ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 140.970 159.198 181.022 1.00 47.19 ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 141.680 159.245 179.677 1.00 46.01 ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 141.408 157.992 178.865 1.00 45.61 ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 141.536 156.759 179.689 1.00 46.40 ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 144.113 162.057 183.512 1.00 34.91 ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 144.446 163.310 184.177 1.00 32.93 ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 145.171 164.234 183.204 1.00 35.54 ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 146.231 163.881 182.677 1.00 36.41 ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 145.309 163.031 185.402 1.00 32.90 ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 145.279 164.115 186.451 1.00 33.01 ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 144.303 164.127 187.437 1.00 33.42 ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 146.235 165.121 186.465 1.00 32.13 ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 144.275 165.111 188.401 1.00 31.76 ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 146.214 166.110 187.425 1.00 31.86 ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 145.232 166.101 188.389 1.00 30.32 ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 145.207 167.084 189.347 1.00 30.85 ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 144.607 165.412 182.970 1.00 35.54 ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 145.141 166.377 182.019 1.00 33.87 ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 145.521 167.667 182.740 1.00 32.42 ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 145.430 167.776 183.964 1.00 33.72 ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 144.134 166.660 180.900 1.00 34.21 ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 142.939 167.222 181.458 1.00 31.71 ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 143.790 165.385 180.150 1.00 33.77 ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 145.959 168.654 181.952 1.00 33.09 ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 146.346 169.933 182.521 1.00 33.14 ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 145.193 170.683 183.158 1.00 34.03 ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 145.388 171.415 184.130 1.00 33.19 ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 143.983 170.530 182.610 1.00 36.35 ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 142.817 171.187 183.190 1.00 32.14 ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 142.516 170.649 184.582 1.00 34.63 ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 142.147 171.408 185.486 1.00 36.95 ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 141.602 171.017 182.272 1.00 33.43 ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 141.653 171.767 180.935 1.00 35.46 ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 142.731 171.280 179.971 1.00 38.56 ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 142.703 171.710 178.799 1.00 38.13 ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 143.590 170.460 180.358 1.00 36.63 ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 142.665 169.335 184.771 1.00 31.17 ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 142.469 168.753 186.096 1.00 30.67 ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 143.482 169.300 187.091 1.00 29.48 ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 143.139 169.590 188.245 1.00 31.28 ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 142.560 167.231 186.018 1.00 32.53 ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 141.589 166.642 185.022 1.00 34.68 ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 140.370 166.678 185.286 1.00 34.71 ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 142.045 166.148 183.970 1.00 33.52 ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 144.740 169.445 186.669 1.00 24.03 ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 145.745 170.017 187.554 1.00 25.25 ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 145.447 171.474 187.863 1.00 27.88 ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 145.692 171.939 188.980 1.00 31.36 ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 147.130 169.897 186.938 1.00 23.41 ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 148.235 170.313 187.860 1.00 24.24 ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 148.425 169.672 189.070 1.00 24.20 ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 149.091 171.342 187.508 1.00 26.92 ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 149.446 170.051 189.914 1.00 22.68 ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 150.113 171.722 188.347 1.00 26.80 ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 150.290 171.078 189.551 1.00 23.73 ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 144.959 172.224 186.875 1.00 23.83 ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 144.574 173.605 187.139 1.00 17.61 ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 143.444 173.670 188.155 1.00 17.22 ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 143.449 174.524 189.045 1.00 22.69 ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 144.177 174.304 185.840 1.00 24.72 ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 145.357 174.518 184.915 1.00 30.67 ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 146.419 173.907 185.151 1.00 30.44 ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 145.224 175.307 183.955 1.00 29.71 ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 142.470 172.767 188.043 1.00 21.90 ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 141.384 172.726 189.019 1.00 22.67 ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 141.901 172.376 190.411 1.00 23.77 ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 141.472 172.967 191.409 1.00 24.60 ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 140.317 171.727 188.577 1.00 20.44 ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 138.952 171.977 189.190 1.00 24.54 ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 138.575 173.447 189.196 1.00 29.88 ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 138.464 174.038 188.101 1.00 30.71 ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 138.396 174.013 190.294 1.00 27.93 ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 142.821 171.411 190.497 1.00 22.46 ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 143.396 171.055 191.791 1.00 18.90 ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 144.193 172.212 192.384 1.00 20.66 ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 144.120 172.472 193.591 1.00 23.04 ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 144.275 169.810 191.652 1.00 18.44 ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 143.465 168.531 191.594 1.00 25.48 ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 142.267 168.570 191.941 1.00 25.19 ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 144.026 167.485 191.208 1.00 28.41 ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 144.958 172.917 191.549 1.00 17.87 ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 145.693 174.088 192.015 1.00 14.20 ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 144.741 175.169 192.501 1.00 18.67 ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 145.004 175.825 193.515 1.00 21.15 ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 146.583 174.631 190.898 1.00 15.45 ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 147.972 174.016 190.731 1.00 17.17 ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 148.746 174.752 189.650 1.00 16.34 ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 148.729 174.034 192.045 1.00 20.43 ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 143.635 175.376 191.785 1.00 16.99 ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 142.634 176.340 192.225 1.00 13.33 ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 142.058 175.945 193.576 1.00 17.37 ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 141.863 176.799 194.446 1.00 22.41 ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 141.521 176.454 191.186 1.00 15.61 ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 141.870 177.302 189.983 1.00 17.03 ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 140.732 177.318 188.982 1.00 20.18 ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 141.218 177.330 187.608 1.00 22.61 ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 140.946 176.393 186.709 1.00 23.66 ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 140.180 175.356 187.004 1.00 22.06 ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 141.455 176.500 185.486 1.00 24.61 ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 141.778 174.655 193.767 1.00 14.76 ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 141.264 174.188 195.051 1.00 14.76 ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 142.263 174.451 196.172 1.00 19.29 ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 141.899 174.959 197.242 1.00 22.63 ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 140.932 172.698 194.969 1.00 14.56 ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 139.969 172.478 193.932 1.00 19.16 ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 140.371 172.203 196.289 1.00 17.31 ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 143.535 174.119 195.939 1.00 18.43 ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 144.557 174.313 196.965 1.00 12.59 ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 144.714 175.791 197.294 1.00 13.48 ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 144.802 176.175 198.467 1.00 16.67 ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 145.893 173.693 196.520 1.00 13.97 ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 146.953 173.910 197.580 1.00 14.01 ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 145.724 172.219 196.255 1.00 15.40 ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 144.761 176.643 196.267 1.00 13.26 ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 144.931 178.072 196.494 1.00 13.25 ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 143.718 178.669 197.194 1.00 17.45 ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 143.862 179.543 198.054 1.00 20.62 ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 145.200 178.788 195.173 1.00 17.35 ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 146.514 178.432 194.477 1.00 16.03 ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 146.814 179.405 193.350 1.00 17.85 ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 147.658 178.388 195.473 1.00 17.06 ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 142.514 178.218 196.839 1.00 16.74 ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 141.315 178.690 197.518 1.00 16.53 ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 141.331 178.304 198.989 1.00 18.75 ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 140.976 179.109 199.856 1.00 19.21 ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 140.070 178.123 196.835 1.00 16.96 ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 139.399 179.068 195.862 1.00 21.50 ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 138.609 178.295 194.823 1.00 19.38 ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 137.943 179.175 193.873 1.00 23.60 ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 137.697 178.858 192.610 1.00 27.69 ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 138.049 177.685 192.110 1.00 22.08 ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 137.083 179.741 191.827 1.00 28.92 ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 141.738 177.069 199.290 1.00 18.43 ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 141.747 176.624 200.679 1.00 15.20 ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 142.826 177.333 201.489 1.00 16.51 ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 142.600 177.691 202.650 1.00 21.33 ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 141.930 175.110 200.742 1.00 13.41 ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 140.728 174.315 200.276 1.00 14.45 ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 141.059 172.837 200.170 1.00 18.71 ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 141.595 172.310 201.417 1.00 16.76 ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 142.167 171.121 201.543 1.00 15.96 ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 142.295 170.303 200.512 1.00 15.29 ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 142.624 170.743 202.734 1.00 14.77 ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 144.002 177.548 200.901 1.00 13.33 ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 145.132 178.096 201.640 1.00 10.13 ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 145.198 179.618 201.626 1.00 13.59 ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 145.949 180.193 202.420 1.00 20.04 ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 146.444 177.532 201.087 1.00 11.56 ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 146.717 178.050 199.798 1.00 14.58 ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 144.440 180.285 200.760 1.00 16.73 ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 144.509 181.727 200.666 1.00 15.83 ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 143.242 182.425 201.108 1.00 21.17 ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 143.293 183.533 201.652 1.00 26.75 ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 142.096 181.789 200.882 1.00 21.08 ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 140.809 182.350 201.270 1.00 21.11 ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 140.315 181.827 202.611 1.00 25.33 ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 139.706 182.579 203.376 1.00 27.91 ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 139.759 182.059 200.193 1.00 22.80 ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 140.211 182.621 198.539 1.00 32.14 ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 140.564 180.556 202.914 1.00 23.04 ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 140.100 179.944 204.151 1.00 22.12 ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 141.140 179.974 205.262 1.00 23.60 ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 140.864 179.472 206.356 1.00 25.23 ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 139.667 178.499 203.890 1.00 21.37 ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 138.839 178.321 202.630 1.00 21.77 ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 137.461 178.940 202.783 1.00 25.08 ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 136.601 178.683 201.557 1.00 25.19 ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 135.554 179.726 201.386 1.00 24.96 ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 142.318 180.550 205.011 1.00 21.61 ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 143.393 180.624 206.002 1.00 23.36 ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 143.745 179.240 206.541 1.00 23.06 ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 143.943 179.046 207.741 1.00 23.05 ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 143.027 181.578 207.141 1.00 20.84 ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 144.240 182.055 207.914 1.00 21.70 ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 145.248 182.447 207.330 1.00 21.26 ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 144.146 182.020 209.238 1.00 23.36 ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 143.821 178.267 205.640 1.00 16.51 ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 144.107 176.884 205.997 1.00 11.26 ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 145.538 176.540 205.607 1.00 15.89 ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 145.931 176.715 204.450 1.00 22.55 ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 143.127 175.936 205.308 1.00 11.44 ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 143.536 174.478 205.342 1.00 15.28 ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 142.532 173.579 204.648 1.00 22.31 ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 141.445 174.073 204.279 1.00 20.53 ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 142.829 172.379 204.470 1.00 20.31 ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 146.312 176.053 206.574 1.00 13.24 ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 147.685 175.639 206.318 1.00 8.76  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 147.677 174.289 205.613 1.00 9.42  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 147.174 173.303 206.159 1.00 12.16 ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 148.467 175.564 207.625 1.00 7.53  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 148.808 176.914 208.226 1.00 8.87  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 149.803 176.770 209.363 1.00 11.18 ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 149.163 176.100 210.568 1.00 12.26 ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 150.082 176.065 211.738 1.00 14.05 ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 148.235 174.242 204.406 1.00 7.07  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 148.172 173.057 203.558 1.00 7.20  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 149.579 172.664 203.139 1.00 8.72  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 150.345 173.503 202.652 1.00 13.76 ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 147.291 173.289 202.317 1.00 5.92  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 145.825 173.411 202.720 1.00 7.16  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 147.473 172.166 201.309 1.00 7.74  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 144.890 173.414 201.548 1.00 11.53 ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 149.907 171.387 203.320 1.00 4.91  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 151.110 170.783 202.766 1.00 4.13  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 150.716 170.061 201.483 1.00 3.25  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 150.061 169.014 201.525 1.00 13.05 ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 151.755 169.826 203.765 1.00 4.98  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 151.099 170.634 200.348 1.00 1.79  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 150.803 170.074 199.032 1.00 2.70  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 151.947 169.142 198.658 1.00 7.06  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 153.030 169.591 198.280 1.00 15.58 ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 150.624 171.194 198.014 1.00 3.41  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 150.279 170.717 196.634 1.00 7.64  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 149.518 169.578 196.447 1.00 12.08 ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 150.715 171.416 195.523 1.00 9.47  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 149.200 169.143 195.176 1.00 14.83 ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 150.400 170.985 194.252 1.00 12.25 ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 149.642 169.848 194.078 1.00 14.40 ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 151.716 167.839 198.770 1.00 5.05  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 152.745 166.845 198.491 1.00 5.49  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 152.620 166.412 197.038 1.00 8.57  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 151.565 165.930 196.611 1.00 16.39 ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 152.633 165.642 199.439 1.00 5.55  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 152.615 166.114 200.892 1.00 5.31  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 153.784 164.680 199.212 1.00 7.58  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 152.610 164.993 201.894 1.00 3.68  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 153.698 166.579 196.277 1.00 6.42  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 153.714 166.282 194.855 1.00 13.38 ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 154.942 165.449 194.524 1.00 12.56 ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 156.046 165.744 194.992 1.00 16.45 ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 153.705 167.572 194.029 1.00 13.10 ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 153.264 167.401 192.590 1.00 17.95 ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 153.235 168.971 191.710 1.00 36.43 ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 153.238 168.412 190.011 1.00 21.44 ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 154.747 164.408 193.723 1.00 16.68 ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 155.818 163.521 193.301 1.00 14.81 ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 156.152 163.769 191.837 1.00 18.83 ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 155.340 164.297 191.072 1.00 23.62 ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 155.430 162.055 193.516 1.00 15.43 ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 156.611 161.111 193.386 1.00 22.28 ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 157.537 161.196 194.219 1.00 21.99 ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 156.613 160.285 192.449 1.00 28.62 ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 157.373 163.386 191.454 1.00 20.71 ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 157.790 163.535 190.063 1.00 23.40 ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 156.942 162.684 189.130 1.00 26.28 ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 156.781 163.026 187.952 1.00 26.10 ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 159.269 163.173 189.916 1.00 22.15 ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 159.604 161.756 190.346 1.00 25.19 ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 160.850 161.222 189.673 1.00 28.68 ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 161.551 162.011 189.007 1.00 28.34 ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 161.129 160.013 189.809 1.00 23.84 ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 156.395 161.574 189.629 1.00 27.06 ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 155.515 160.749 188.809 1.00 28.25 ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 154.196 161.451 188.523 1.00 29.15 ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 153.554 161.172 187.503 1.00 29.95 ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 155.268 159.405 189.492 1.00 28.67 ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 154.707 159.583 190.779 1.00 27.95 ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 153.774 162.359 189.407 1.00 28.94 ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 152.547 163.112 189.184 1.00 27.62 ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 152.667 164.088 188.021 1.00 31.08 ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 151.642 164.556 187.515 1.00 37.44 ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 152.160 163.867 190.456 1.00 26.63 ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 151.700 162.943 191.565 1.00 28.99 ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 151.526 161.743 191.355 1.00 29.08 ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 151.508 163.498 192.755 1.00 27.26 ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 153.885 164.405 187.591 1.00 31.00 ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 154.104 165.342 186.494 1.00 31.30 ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 153.944 164.589 185.177 1.00 35.78 ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 154.778 163.754 184.822 1.00 40.07 ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 155.483 166.002 186.588 1.00 30.91 ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 155.681 166.977 185.440 1.00 30.70 ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 155.645 166.703 187.925 1.00 29.91 ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 152.867 164.884 184.449 1.00 35.66 ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 152.602 164.251 183.165 1.00 36.69 ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 152.961 165.129 181.972 1.00 36.11 ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 153.080 164.612 180.855 1.00 38.04 ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 151.124 163.855 183.068 1.00 36.44 ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 150.645 162.773 184.038 1.00 37.28 ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 149.142 162.587 183.925 1.00 37.40 ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 151.373 161.461 183.791 1.00 37.04 ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 153.129 166.431 182.184 1.00 35.46 ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 153.395 167.388 181.120 1.00 39.18 ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 154.265 168.502 181.684 1.00 39.89 ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 154.415 168.641 182.900 1.00 39.24 ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 152.100 167.971 180.537 1.00 38.12 ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 151.310 166.956 179.734 1.00 40.89 ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 151.753 166.600 178.622 1.00 40.87 ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 150.243 166.518 180.214 1.00 40.57 ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 154.846 169.297 180.782 1.00 37.47 ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 155.657 170.428 181.218 1.00 36.78 ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 154.816 171.576 181.761 1.00 34.66 ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 155.343 172.421 182.494 1.00 36.65 ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 156.533 170.926 180.069 1.00 34.05 ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 157.358 171.996 180.490 1.00 32.49 ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 153.527 171.637 181.413 1.00 28.81 ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 152.667 172.663 181.981 1.00 27.87 ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 152.510 172.516 183.481 1.00 32.03 ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 152.423 173.512 184.209 1.00 34.57 ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 152.466 171.272 183.962 1.00 29.28 ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 152.484 171.008 185.396 1.00 26.49 ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 153.656 171.727 186.048 1.00 26.36 ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 153.491 172.468 187.026 1.00 28.82 ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 152.605 169.501 185.638 1.00 28.69 ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 151.410 168.702 185.199 1.00 29.04 ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 150.283 168.601 185.985 1.00 28.43 ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 151.413 168.070 183.976 1.00 32.82 ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 149.199 167.851 185.566 1.00 28.90 ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 150.330 167.333 183.551 1.00 33.01 ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 149.221 167.228 184.345 1.00 30.24 ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 154.852 171.539 185.485 1.00 24.24 ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 156.053 172.131 186.052 1.00 25.81 ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 156.062 173.644 185.904 1.00 22.21 ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 156.576 174.338 186.781 1.00 23.40 ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 157.293 171.522 185.399 1.00 27.20 ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 157.681 170.139 185.922 1.00 27.49 ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 159.077 169.762 185.460 1.00 25.73 ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 157.576 170.084 187.441 1.00 24.69 ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 155.505 174.175 184.816 1.00 19.64 ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 155.459 175.626 184.648 1.00 17.37 ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 154.578 176.277 185.711 1.00 20.36 ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 154.980 177.256 186.360 1.00 24.54 ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 154.964 175.975 183.245 1.00 17.23 ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 154.824 177.462 182.982 1.00 20.60 ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 156.072 178.066 182.372 1.00 22.34 ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 157.160 177.481 182.545 1.00 22.97 ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 155.964 179.124 181.719 1.00 20.80 ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 153.371 175.740 185.910 1.00 17.76 ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 152.492 176.288 186.938 1.00 15.29 ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 153.086 176.100 188.327 1.00 17.47 ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 152.984 176.992 189.180 1.00 19.91 ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 151.104 175.656 186.851 1.00 20.44 ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 150.537 175.595 185.444 1.00 23.37 ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 149.025 175.734 185.439 1.00 23.10 ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 148.600 177.127 185.368 1.00 24.39 ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 148.584 177.847 184.256 1.00 24.04 ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 148.967 177.340 183.096 1.00 23.41 ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 148.170 179.111 184.306 1.00 23.62 ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 153.723 174.950 188.575 1.00 20.78 ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 154.363 174.733 189.867 1.00 16.19 ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 155.510 175.712 190.090 1.00 13.85 ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 155.694 176.213 191.201 1.00 16.03 ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 154.855 173.291 189.971 1.00 15.84 ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 153.768 172.303 190.345 1.00 17.42 ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 152.491 173.056 191.371 1.00 30.65 ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 153.291 173.043 192.972 1.00 16.58 ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 156.292 175.989 189.046 1.00 14.37 ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 157.372 176.966 189.143 1.00 13.43 ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 156.828 178.335 189.520 1.00 13.29 ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 157.335 178.988 190.444 1.00 15.98 ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 158.117 177.017 187.803 1.00 12.82 ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 159.236 178.048 187.774 1.00 16.83 ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 159.543 178.693 188.771 1.00 20.60 ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 159.847 178.206 186.608 1.00 15.55 ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 155.783 178.781 188.822 1.00 13.43 ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 155.217 180.092 189.124 1.00 14.05 ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 154.670 180.142 190.547 1.00 14.47 ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 154.889 181.122 191.270 1.00 11.67 ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 154.125 180.442 188.117 1.00 15.38 ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 154.657 180.361 186.790 1.00 13.54 ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 153.622 181.850 188.364 1.00 16.92 ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 153.967 179.089 190.970 1.00 16.80 ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 153.390 179.067 192.311 1.00 12.53 ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 154.475 179.053 193.383 1.00 12.69 ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 154.365 179.742 194.403 1.00 13.71 ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 152.467 177.857 192.458 1.00 12.63 ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 151.951 177.545 193.861 1.00 11.19 ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 151.169 178.720 194.417 1.00 16.23 ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 151.095 176.293 193.837 1.00 11.82 ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 155.531 178.262 193.176 1.00 15.76 ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 156.611 178.189 194.152 1.00 8.83  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 157.338 179.518 194.270 1.00 11.87 ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 157.686 179.947 195.377 1.00 11.36 ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 157.596 177.084 193.768 1.00 6.80  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 157.149 175.631 193.925 1.00 8.19  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 158.113 174.702 193.209 1.00 9.61  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 157.041 175.265 195.385 1.00 9.32  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 157.581 180.187 193.143 1.00 14.25 ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 158.378 181.405 193.185 1.00 8.46  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 157.571 182.597 193.687 1.00 11.21 ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 158.023 183.327 194.575 1.00 13.52 ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 158.961 181.692 191.805 1.00 6.75  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 156.375 182.813 193.138 1.00 13.00 ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 155.599 184.004 193.466 1.00 14.56 ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 154.518 183.767 194.506 1.00 16.89 ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 154.180 184.691 195.251 1.00 18.55 ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 154.947 184.579 192.204 1.00 11.17 ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 155.961 184.970 191.153 1.00 11.30 ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 156.841 185.793 191.398 1.00 7.68  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 155.840 184.382 189.968 1.00 13.57 ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 153.966 182.561 194.581 1.00 15.22 ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 152.822 182.302 195.422 1.00 9.67  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 151.484 182.509 194.753 1.00 15.48 ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 150.457 182.468 195.438 1.00 19.03 ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 151.462 182.732 193.440 1.00 22.63 ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 150.216 182.930 192.714 1.00 21.41 ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 150.461 182.685 191.233 1.00 23.51 ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 151.456 183.158 190.678 1.00 23.75 ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 149.655 184.340 192.959 1.00 19.63 ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 150.576 185.489 192.561 1.00 22.87 ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 150.399 185.920 191.119 1.00 29.61 ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 149.341 185.616 190.532 1.00 31.84 ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 151.322 186.562 190.573 1.00 31.00 ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 149.570 181.920 190.610 1.00 23.59 ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 149.623 181.653 189.174 1.00 24.27 ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 148.832 182.748 188.467 1.00 26.98 ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 147.669 182.992 188.822 1.00 25.16 ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 149.084 180.252 188.849 1.00 26.83 ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 149.253 179.938 187.374 1.00 23.02 ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 149.786 179.208 189.702 1.00 21.43 ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 149.412 183.437 187.477 1.00 32.51 ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 148.742 184.613 186.903 1.00 30.85 ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 147.461 184.291 186.148 1.00 30.27 ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 146.467 185.012 186.275 1.00 33.02 ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 149.808 185.192 185.965 1.00 29.29 ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 150.647 184.019 185.588 1.00 29.76 ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 150.695 183.154 186.813 1.00 30.61 ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 147.467 183.220 185.361 1.00 21.21 ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 146.316 182.896 184.542 1.00 21.34 ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 145.472 181.755 185.069 1.00 25.24 ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 144.667 181.182 184.330 1.00 29.40 ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 145.644 181.410 186.347 1.00 23.64 ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 144.904 180.281 186.902 1.00 26.09 ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 143.433 180.623 187.101 1.00 26.50 ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 142.553 179.822 186.764 1.00 27.24 ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 145.537 179.834 188.216 1.00 25.30 ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 145.151 178.432 188.687 1.00 19.61 ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 145.744 177.382 187.766 1.00 20.71 ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 145.607 178.208 190.115 1.00 18.64 ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 143.144 181.803 187.643 1.00 24.47 ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 141.773 182.246 187.882 1.00 24.87 ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 141.401 183.246 186.792 1.00 29.25 ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 141.911 184.369 186.765 1.00 31.83 ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 141.625 182.862 189.270 1.00 27.65 ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 141.917 181.911 190.398 1.00 26.99 ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 143.220 181.652 190.789 1.00 27.91 ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 140.884 181.281 191.069 1.00 26.23 ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 143.484 180.783 191.828 1.00 24.98 ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 141.145 180.409 192.108 1.00 23.91 ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 142.447 180.160 192.487 1.00 24.73 ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 140.512 182.834 185.894 1.00 32.00 ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 140.027 183.690 184.825 1.00 34.11 ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 138.534 183.467 184.629 1.00 37.85 ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 137.997 182.402 184.943 1.00 35.71 ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 140.779 183.435 183.510 1.00 32.46 ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 140.860 181.971 183.113 1.00 34.45 ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 141.805 181.737 181.949 1.00 36.07 ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 141.325 181.362 180.859 1.00 34.80 ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 143.025 181.932 182.123 1.00 31.41 ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 137.867 184.491 184.098 1.00 36.88 ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 136.434 184.391 183.876 1.00 35.70 ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 135.667 184.424 185.185 1.00 38.32 ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 135.999 185.170 186.112 1.00 37.49 ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 134.614 183.606 185.259 1.00 39.94 ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 133.819 183.522 186.479 1.00 38.42 ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 134.613 182.950 187.645 1.00 37.54 ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 134.265 183.204 188.805 1.00 36.35 ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 132.566 182.680 186.234 1.00 38.50 ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 132.872 181.375 185.526 1.00 39.14 ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 134.039 181.169 185.131 1.00 42.67 ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 131.943 180.556 185.362 1.00 36.32 ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 135.670 182.183 187.363 1.00 34.34 ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 136.526 181.686 188.434 1.00 33.26 ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 137.183 182.836 189.182 1.00 34.55 ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 137.287 182.807 190.414 1.00 33.21 ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 137.586 180.741 187.866 1.00 31.71 ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 137.037 179.425 187.342 1.00 35.34 ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 136.616 178.481 188.452 1.00 39.97 ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 136.980 178.731 189.619 1.00 37.66 ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 135.919 177.487 188.157 1.00 38.73 ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 137.627 183.862 188.454 1.00 33.95 ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 138.219 185.026 189.103 1.00 33.45 ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 137.200 185.755 189.968 1.00 37.10 ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 137.528 186.216 191.066 1.00 36.33 ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 138.811 185.971 188.058 1.00 31.92 ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 139.603 187.112 188.655 1.00 32.64 ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 140.834 186.889 189.252 1.00 34.69 ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 139.116 188.411 188.625 1.00 32.46 ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 141.561 187.926 189.801 1.00 35.12 ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 139.835 189.454 189.170 1.00 34.66 ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 141.056 189.206 189.758 1.00 35.49 ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 141.777 190.243 190.304 1.00 35.41 ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 135.960 185.879 189.490 1.00 35.67 ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 134.926 186.538 190.284 1.00 33.58 ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 134.622 185.756 191.556 1.00 36.18 ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 134.474 186.343 192.638 1.00 37.52 ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 133.659 186.720 189.449 1.00 34.27 ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 134.522 184.429 191.448 1.00 35.87 ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 134.302 183.608 192.633 1.00 36.56 ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 135.467 183.735 193.608 1.00 35.25 ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 135.261 183.844 194.825 1.00 35.37 ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 134.094 182.148 192.232 1.00 38.43 ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 133.017 182.059 191.292 1.00 35.90 ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 133.766 181.302 193.451 1.00 35.55 ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 136.697 183.727 193.091 1.00 31.79 ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 137.864 183.891 193.948 1.00 34.15 ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 137.847 185.241 194.647 1.00 34.35 ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 138.194 185.340 195.827 1.00 32.80 ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 139.146 183.733 193.130 1.00 33.42 ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 140.425 184.213 193.817 1.00 31.83 ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 140.850 183.232 194.896 1.00 31.37 ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 141.541 184.429 192.808 1.00 30.96 ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 137.454 186.297 193.933 1.00 36.62 ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 137.396 187.623 194.540 1.00 35.08 ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 136.338 187.684 195.633 1.00 36.21 ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 136.562 188.295 196.684 1.00 35.91 ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 137.132 188.676 193.467 1.00 33.96 ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 138.325 188.937 192.564 1.00 35.95 ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 139.740 189.610 193.456 1.00 44.64 ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 140.858 188.212 193.425 1.00 36.20 ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 135.180 187.060 195.405 1.00 39.11 ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 134.157 187.014 196.448 1.00 40.63 ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 134.656 186.264 197.680 1.00 39.61 ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 134.466 186.719 198.819 1.00 39.73 ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 132.884 186.364 195.908 1.00 39.56 ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 132.447 187.065 194.737 1.00 40.67 ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 131.782 186.404 196.954 1.00 38.57 ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 135.307 185.118 197.472 1.00 35.05 ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 135.832 184.352 198.599 1.00 34.80 ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 136.930 185.121 199.327 1.00 37.45 ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 137.027 185.057 200.557 1.00 37.62 ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 136.346 182.994 198.120 1.00 34.76 ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 135.292 182.151 197.424 1.00 36.80 ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 135.538 180.664 197.571 1.00 38.63 ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 135.732 180.161 198.677 1.00 38.70 ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 135.532 179.952 196.451 1.00 37.58 ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 137.765 185.850 198.586 1.00 37.42 ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 138.805 186.660 199.207 1.00 35.04 ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 138.208 187.798 200.021 1.00 36.42 ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 138.718 188.136 201.093 1.00 37.81 ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 139.755 187.205 198.142 1.00 33.42 ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 140.837 185.966 197.408 1.00 43.84 ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 137.134 188.413 199.521 1.00 38.97 ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 136.451 189.444 200.293 1.00 38.69 ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 135.880 188.868 201.582 1.00 40.02 ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 135.998 189.481 202.652 1.00 38.21 ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 135.344 190.082 199.453 1.00 37.82 ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 134.880 191.437 199.957 1.00 38.54 ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 133.713 191.954 199.131 1.00 40.34 ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 133.296 193.346 199.570 1.00 39.38 ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 134.426 194.311 199.502 1.00 39.30 ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 135.271 187.681 201.503 1.00 41.77 ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 134.763 187.032 202.710 1.00 42.10 ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 135.887 186.729 203.694 1.00 44.18 ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 135.746 186.952 204.902 1.00 43.36 ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 134.016 185.751 202.342 1.00 39.88 ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 132.767 185.974 201.509 1.00 43.17 ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 132.129 184.674 201.061 1.00 46.70 ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 132.721 183.603 201.311 1.00 44.35 ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 131.035 184.720 200.459 1.00 45.97 ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 137.018 186.226 203.192 1.00 38.37 ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 138.134 185.914 204.070 1.00 34.73 ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 138.744 187.147 204.710 1.00 36.11 ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 139.136 187.120 205.879 1.00 37.92 ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 138.845 188.240 203.952 1.00 36.95 ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 139.357 189.485 204.510 1.00 38.84 ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 138.406 190.053 205.553 1.00 42.51 ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 138.846 190.611 206.565 1.00 40.08 ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 139.603 190.500 203.393 1.00 38.77 ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 137.096 189.931 205.322 1.00 45.50 ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 136.132 190.340 206.337 1.00 45.60 ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 136.270 189.491 207.595 1.00 44.47 ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 136.155 190.002 208.715 1.00 44.02 ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 134.710 190.253 205.782 1.00 44.65 ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 133.728 191.196 206.455 1.00 45.36 ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 134.329 192.562 206.735 1.00 48.83 ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 134.607 193.333 205.817 1.00 48.01 ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 134.534 192.865 208.012 1.00 45.98 ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 136.511 188.190 207.425 1.00 42.81 ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 136.756 187.327 208.578 1.00 41.37 ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 138.012 187.753 209.328 1.00 42.66 ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 138.033 187.764 210.564 1.00 44.68 ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 136.872 185.870 208.126 1.00 40.43 ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 135.545 185.222 207.769 1.00 42.80 ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 135.728 183.768 207.354 1.00 43.22 ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 136.720 183.051 208.255 1.00 44.45 ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 136.078 182.548 209.500 1.00 44.49 ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 139.070 188.107 208.596 1.00 41.52 ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 140.303 188.561 209.229 1.00 41.53 ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 140.189 189.979 209.769 1.00 42.83 ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 141.023 190.388 210.583 1.00 42.36 ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 141.464 188.472 208.235 1.00 41.18 ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 142.839 188.416 208.882 1.00 40.60 ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 143.848 187.666 208.037 1.00 43.97 ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 143.779 186.420 207.993 1.00 43.82 ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 144.711 188.323 207.417 1.00 42.12 ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 139.181 190.734 209.342 1.00 44.42 ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 139.001 192.093 209.805 1.00 45.34 ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 139.620 193.165 208.939 1.00 44.49 ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 139.761 194.304 209.403 1.00 44.33 ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 140.000 192.846 207.707 1.00 47.80 ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 140.601 193.822 206.811 1.00 49.42 ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 139.542 194.455 205.916 1.00 50.22 ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 138.564 193.812 205.523 1.00 47.58 ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 141.689 193.174 205.954 1.00 46.27 ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 142.923 192.673 206.704 1.00 46.24 ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 143.853 191.931 205.764 1.00 46.93 ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 143.645 193.826 207.379 1.00 47.15 ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 139.751 195.729 205.595 1.00 58.16 ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 138.834 196.499 204.754 1.00 57.88 ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 139.411 196.574 203.340 1.00 58.89 ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 140.095 197.526 202.962 1.00 59.73 ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 138.559 197.867 205.383 1.00 58.90 ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 139.753 198.814 205.510 1.00 61.78 ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 139.344 200.352 206.354 1.00 68.18 ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 139.187 199.778 208.043 1.00 60.82 ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 139.132 195.543 202.547 1.00 47.81 ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 139.585 195.463 201.166 1.00 45.59 ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 138.377 195.339 200.251 1.00 46.35 ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 137.516 194.480 200.466 1.00 45.50 ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 140.532 194.278 200.965 1.00 45.73 ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 141.593 194.069 202.044 1.00 46.24 ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 142.251 192.710 201.885 1.00 46.61 ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 142.633 195.177 201.997 1.00 46.15 ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 138.316 196.198 199.234 1.00 46.96 ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 137.200 196.189 198.299 1.00 46.63 ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 137.695 196.074 196.863 1.00 47.31 ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 137.052 195.431 196.027 1.00 46.76 ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 136.348 197.449 198.470 1.00 48.71 ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 135.060 197.397 197.674 1.00 50.98 ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 134.242 196.486 197.924 1.00 50.89 ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 134.865 198.265 196.798 1.00 50.30 ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 138.833 196.695 196.569 1.00 44.98 ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 139.389 196.645 195.225 1.00 45.20 ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 139.913 195.249 194.911 1.00 44.40 ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 140.360 194.513 195.795 1.00 45.65 ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 140.511 197.671 195.071 1.00 43.97 ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 141.206 197.485 193.850 1.00 44.90 ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 139.850 194.887 193.628 1.00 39.46 ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 140.302 193.563 193.212 1.00 40.64 ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 141.805 193.403 193.396 1.00 40.11 ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 142.281 192.312 193.732 1.00 40.76 ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 139.910 193.306 191.758 1.00 41.62 ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 138.440 193.123 191.552 1.00 42.76 ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 137.734 192.082 192.116 1.00 41.53 ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 137.542 193.841 190.836 1.00 44.84 ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 136.464 192.171 191.762 1.00 40.95 ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 136.321 193.229 190.985 1.00 45.10 ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 142.572 194.474 193.174 1.00 36.57 ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 144.021 194.389 193.324 1.00 35.35 ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 144.418 194.117 194.770 1.00 36.07 ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 145.280 193.268 195.032 1.00 37.25 ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 144.675 195.675 192.820 1.00 37.49 ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 144.500 195.913 191.329 1.00 40.08 ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 145.206 197.165 190.852 1.00 42.04 ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 145.737 197.910 191.701 1.00 42.16 ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 145.233 197.403 189.625 1.00 40.05 ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 143.803 194.824 195.720 1.00 37.88 ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 144.105 194.584 197.129 1.00 34.69 ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 143.674 193.188 197.555 1.00 35.08 ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 144.375 192.522 198.327 1.00 35.81 ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 143.430 195.645 197.998 1.00 35.54 ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 143.720 197.073 197.571 1.00 38.27 ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 142.598 198.028 197.935 1.00 41.81 ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 141.870 197.747 198.910 1.00 41.20 ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 142.446 199.059 197.246 1.00 39.73 ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 142.522 192.729 197.060 1.00 32.12 ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 142.076 191.373 197.359 1.00 32.58 ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 143.067 190.341 196.839 1.00 32.58 ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 143.384 189.371 197.534 1.00 30.67 ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 140.690 191.134 196.762 1.00 29.95 ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 139.502 191.706 197.533 1.00 30.45 ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 138.195 191.217 196.936 1.00 33.27 ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 139.593 191.331 199.002 1.00 32.04 ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 143.575 190.538 195.620 1.00 28.27 ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 144.531 189.585 195.066 1.00 21.54 ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 145.858 189.628 195.811 1.00 23.64 ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 146.502 188.590 195.996 1.00 26.77 ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 144.747 189.844 193.577 1.00 20.65 ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 145.239 188.621 192.838 1.00 25.07 ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 144.409 187.528 192.641 1.00 25.09 ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 146.539 188.550 192.357 1.00 25.25 ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 144.851 186.405 191.974 1.00 23.34 ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 146.992 187.429 191.689 1.00 21.42 ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 146.144 186.360 191.500 1.00 24.15 ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 146.587 185.241 190.834 1.00 27.70 ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 146.295 190.815 196.236 1.00 21.44 ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 147.526 190.899 197.018 1.00 18.99 ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 147.378 190.194 198.359 1.00 23.13 ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 148.288 189.475 198.797 1.00 28.25 ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 147.929 192.360 197.217 1.00 21.84 ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 148.326 193.070 195.934 1.00 22.41 ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 148.584 194.547 196.176 1.00 22.64 ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 148.888 195.270 194.875 1.00 24.63 ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 149.106 196.727 195.085 1.00 24.31 ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 146.236 190.378 199.027 1.00 18.91 ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 145.987 189.663 200.276 1.00 17.82 ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 145.930 188.159 200.045 1.00 21.60 ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 146.450 187.379 200.851 1.00 25.42 ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 144.691 190.160 200.916 1.00 19.86 ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 144.246 189.342 202.089 1.00 21.03 ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 144.631 189.494 203.387 1.00 20.89 ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 143.324 188.247 202.069 1.00 23.62 ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 144.009 188.559 204.179 1.00 20.55 ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 143.201 187.781 203.392 1.00 23.42 ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 142.592 187.612 201.061 1.00 24.55 ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 142.377 186.712 203.733 1.00 23.01 ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 141.775 186.553 201.401 1.00 22.14 ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 141.675 186.113 202.725 1.00 22.66 ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 145.299 187.736 198.948 1.00 18.26 ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 145.241 186.318 198.614 1.00 14.06 ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 146.634 185.745 198.391 1.00 17.38 ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 146.948 184.649 198.867 1.00 26.09 ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 144.371 186.128 197.372 1.00 16.60 ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 144.379 184.734 196.824 1.00 14.37 ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 143.703 183.718 197.472 1.00 15.92 ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 145.046 184.445 195.647 1.00 15.80 ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 143.701 182.440 196.962 1.00 17.72 ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 145.049 183.167 195.135 1.00 16.95 ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 144.374 182.164 195.793 1.00 19.30 ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 147.486 186.476 197.670 1.00 16.20 ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 148.847 186.015 197.426 1.00 13.92 ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 149.640 185.933 198.723 1.00 12.55 ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 150.395 184.977 198.938 1.00 20.30 ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 149.542 186.940 196.426 1.00 14.35 ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 148.876 186.858 195.160 1.00 19.24 ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 150.996 186.545 196.248 1.00 14.57 ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 149.480 186.923 199.604 1.00 11.51 ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 150.166 186.874 200.892 1.00 15.03 ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 149.706 185.675 201.713 1.00 17.63 ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 150.524 184.994 202.347 1.00 20.14 ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 149.934 188.174 201.661 1.00 14.69 ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 148.579 188.301 202.056 1.00 21.01 ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 148.400 185.398 201.713 1.00 13.85 ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 147.886 184.249 202.453 1.00 12.29 ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 148.410 182.937 201.880 1.00 11.26 ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 148.776 182.025 202.632 1.00 11.84 ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 146.360 184.264 202.446 1.00 11.31 ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 145.754 185.360 203.296 1.00 15.22 ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 146.023 185.165 204.770 1.00 21.28 ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 146.796 185.905 205.375 1.00 19.58 ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 145.385 184.160 205.360 1.00 20.36 ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 148.452 182.822 200.552 1.00 11.14 ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 148.980 181.612 199.927 1.00 7.92  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 150.452 181.437 200.270 1.00 8.96  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 150.914 180.322 200.546 1.00 14.75 ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 148.755 181.650 198.405 1.00 7.03  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 149.489 180.502 197.741 1.00 9.66  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 147.274 181.583 198.089 1.00 13.33 ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 151.213 182.533 200.259 1.00 10.06 ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 152.623 182.472 200.625 1.00 8.82  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 152.780 181.997 202.063 1.00 13.56 ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 153.634 181.157 202.368 1.00 19.08 ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 153.284 183.846 200.407 1.00 6.13  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 153.561 184.075 198.920 1.00 9.47  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 154.563 183.966 201.218 1.00 7.91  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 154.051 185.465 198.601 1.00 10.71 ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 151.951 182.517 202.966 1.00 11.58 ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 152.080 182.191 204.381 1.00 8.49  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 151.543 180.808 204.738 1.00 10.61 ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 151.934 180.263 205.775 1.00 12.89 ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 151.364 183.245 205.225 1.00 8.89  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 152.059 183.573 206.535 1.00 13.00 ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 151.313 184.657 207.292 1.00 14.28 ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 149.868 184.509 207.170 1.00 17.74 ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 149.134 183.686 207.906 1.00 15.38 ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 149.678 182.921 208.838 1.00 12.17 ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 147.821 183.630 207.703 1.00 13.97 ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 150.667 180.226 203.917 1.00 10.61 ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 149.954 179.016 204.311 1.00 10.50 ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 150.336 177.765 203.534 1.00 11.06 ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 150.244 176.669 204.087 1.00 15.81 ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 148.442 179.224 204.175 1.00 8.52  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 147.890 180.176 205.214 1.00 12.50 ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 148.280 180.136 206.380 1.00 13.53 ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 146.972 181.038 204.797 1.00 15.04 ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 150.754 177.887 202.279 1.00 5.76  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 150.985 176.730 201.424 1.00 3.78  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 152.447 176.307 201.480 1.00 12.52 ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 153.344 177.120 201.231 1.00 14.90 ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 150.580 177.032 199.981 1.00 7.76  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 150.696 175.872 198.994 1.00 7.91  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 149.925 174.668 199.501 1.00 10.17 ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 150.199 176.285 197.620 1.00 5.86  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 152.681 175.035 201.806 1.00 8.47  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 154.015 174.440 201.805 1.00 5.09  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 154.012 173.290 200.809 1.00 4.00  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 153.331 172.285 201.025 1.00 11.24 ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 154.403 173.948 203.198 1.00 0.72  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 154.345 175.004 204.256 1.00 2.22  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 153.260 175.163 205.090 1.00 8.56  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 155.239 175.955 204.618 1.00 2.59  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 153.487 176.165 205.920 1.00 6.45  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 154.681 176.663 205.654 1.00 6.15  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 154.766 173.427 199.725 1.00 5.80  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 154.813 172.419 198.673 1.00 1.87  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 156.006 171.507 198.914 1.00 6.70  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 157.149 171.974 199.003 1.00 13.51 ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 154.888 173.066 197.280 1.00 3.88  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 155.133 172.010 196.220 1.00 5.29  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 153.612 173.835 196.985 1.00 7.38  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 155.745 170.208 199.015 1.00 7.27  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 156.772 169.199 199.246 1.00 4.43  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 156.908 168.381 197.971 1.00 4.25  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 156.039 167.559 197.657 1.00 10.45 ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 156.431 168.303 200.443 1.00 2.92  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 157.629 167.457 200.830 1.00 7.91  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 155.964 169.146 201.612 1.00 2.06  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 157.997 168.592 197.243 1.00 3.02  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 158.256 167.888 195.996 1.00 0.78  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 159.213 166.733 196.256 1.00 7.26  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 160.289 166.930 196.829 1.00 14.71 ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 158.839 168.836 194.947 1.00 4.06  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 158.632 168.380 193.534 1.00 12.04 ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 157.482 168.720 192.844 1.00 11.21 ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 159.588 167.609 192.893 1.00 14.70 ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 157.289 168.301 191.543 1.00 14.05 ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 159.400 167.187 191.592 1.00 14.70 ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 158.249 167.534 190.916 1.00 17.15 ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 158.817 165.534 195.841 1.00 6.53  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 159.613 164.331 196.036 1.00 5.91  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 159.978 163.734 194.686 1.00 11.07 ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 159.132 163.634 193.793 1.00 19.85 ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 158.864 163.293 196.881 1.00 7.19  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 157.790 162.735 196.115 1.00 17.88 ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 158.304 163.929 198.142 1.00 5.13  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 161.240 163.336 194.541 1.00 7.72  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 161.713 162.768 193.289 1.00 10.89 ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 162.867 161.816 193.564 1.00 9.90  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 163.498 161.861 194.623 1.00 13.18 ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 162.140 163.859 192.301 1.00 12.07 ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 163.220 164.786 192.825 1.00 10.47 ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 163.713 166.015 191.604 1.00 29.93 ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 164.577 164.987 190.423 1.00 16.34 ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 163.129 160.943 192.593 1.00 9.97  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 164.208 159.976 192.674 1.00 10.25 ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 165.552 160.640 192.374 1.00 16.25 ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 165.613 161.634 191.644 1.00 16.74 ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 163.968 158.832 191.696 1.00 12.35 ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 163.097 157.740 192.280 1.00 12.05 ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 163.383 157.212 193.354 1.00 13.29 ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 162.023 157.401 191.580 1.00 11.64 ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 166.649 160.106 192.922 1.00 16.93 ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 167.974 160.725 192.707 1.00 17.15 ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 168.568 160.389 191.344 1.00 19.39 ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 169.615 159.746 191.213 1.00 23.77 ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 168.792 160.153 193.867 1.00 12.49 ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 168.198 158.820 194.110 1.00 11.01 ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 166.726 158.951 193.833 1.00 14.78 ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 167.889 160.830 190.290 1.00 22.95 ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 168.389 160.639 188.939 1.00 27.74 ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 169.512 161.626 188.644 1.00 30.66 ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 169.559 162.733 189.188 1.00 26.69 ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 167.263 160.808 187.919 1.00 28.62 ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 167.754 160.692 186.595 1.00 29.77 ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 170.428 161.212 187.767 1.00 37.62 ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 171.568 162.055 187.422 1.00 35.96 ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 171.185 163.108 186.388 1.00 34.78 ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 171.294 164.313 186.641 1.00 34.05 ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 172.724 161.190 186.911 1.00 36.47 ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 173.064 160.186 187.852 1.00 34.81 ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 170.735 162.668 185.211 1.00 37.28 ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 170.346 163.611 184.169 1.00 38.19 ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 169.005 164.268 184.472 1.00 36.94 ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 168.756 165.397 184.033 1.00 36.31 ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 170.299 162.906 182.814 1.00 36.56 ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 169.543 161.588 182.828 1.00 39.64 ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 169.356 161.010 181.439 1.00 41.38 ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 169.832 161.630 180.465 1.00 41.26 ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 168.733 159.934 181.322 1.00 37.37 ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 168.133 163.578 185.210 1.00 31.45 ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 166.848 164.162 185.557 1.00 30.73 ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 166.984 165.398 186.425 1.00 29.49 ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 166.247 166.371 186.253 1.00 28.84 ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 167.926 165.376 187.370 1.00 25.99 ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 168.158 166.543 188.213 1.00 24.23 ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 168.642 167.733 187.392 1.00 22.38 ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 168.186 168.866 187.594 1.00 23.80 ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 169.163 166.201 189.311 1.00 26.63 ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 169.061 166.999 190.611 1.00 25.62 ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 167.688 166.823 191.231 1.00 19.57 ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 170.147 166.572 191.580 1.00 23.12 ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 169.567 167.495 186.459 1.00 23.97 ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 170.052 168.576 185.607 1.00 25.51 ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 168.942 169.118 184.716 1.00 25.20 ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 168.854 170.330 184.490 1.00 25.25 ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 171.232 168.091 184.764 1.00 26.04 ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 172.387 167.534 185.580 1.00 26.56 ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 173.684 167.552 184.789 1.00 26.71 ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 173.706 166.455 183.740 1.00 28.38 ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 174.968 165.667 183.788 1.00 27.53 ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 168.091 168.234 184.190 1.00 23.14 ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 166.961 168.688 183.387 1.00 23.03 ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 165.995 169.526 184.216 1.00 23.48 ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 165.499 170.560 183.752 1.00 29.09 ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 166.239 167.490 182.772 1.00 25.52 ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 164.925 167.871 182.123 1.00 27.58 ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 164.951 168.567 181.086 1.00 28.95 ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 163.863 167.476 182.649 1.00 28.57 ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 165.715 169.095 185.448 1.00 22.67 ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 164.790 169.828 186.304 1.00 22.71 ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 165.374 171.159 186.756 1.00 18.79 ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 164.623 172.099 187.037 1.00 18.84 ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 164.412 168.977 187.514 1.00 22.60 ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 163.115 169.391 188.181 1.00 22.99 ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 161.923 168.703 187.541 1.00 23.74 ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 161.874 167.283 187.872 1.00 23.47 ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 161.148 166.386 187.218 1.00 24.97 ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 160.394 166.728 186.186 1.00 25.74 ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 161.182 165.115 187.608 1.00 25.13 ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 166.704 171.259 186.838 1.00 18.41 ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 167.329 172.520 187.214 1.00 17.90 ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 167.024 173.636 186.224 1.00 21.74 ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 167.129 174.815 186.582 1.00 22.21 ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 168.842 172.340 187.347 1.00 17.10 ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 166.651 173.294 184.993 1.00 21.42 ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 166.266 174.273 183.984 1.00 21.51 ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 164.769 174.289 183.717 1.00 15.68 ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 164.200 175.358 183.475 1.00 18.35 ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 167.013 174.008 182.674 1.00 18.56 ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 164.114 173.126 183.753 1.00 13.71 ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 162.674 173.084 183.517 1.00 16.65 ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 161.908 173.781 184.635 1.00 18.19 ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 160.914 174.471 184.376 1.00 19.25 ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 162.206 171.637 183.371 1.00 21.93 ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 163.096 170.935 182.495 1.00 21.13 ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 160.804 171.592 182.790 1.00 20.54 ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 162.339 173.604 185.881 1.00 15.85 ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 161.728 174.255 187.040 1.00 13.28 ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 162.832 174.853 187.901 1.00 15.06 ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 163.276 174.236 188.880 1.00 17.33 ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 160.871 173.274 187.840 1.00 20.11 ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 160.062 173.958 188.781 1.00 22.43 ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 163.313 176.050 187.556 1.00 17.58 ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 164.381 176.668 188.360 1.00 16.91 ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 163.994 176.922 189.808 1.00 16.93 ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 164.851 176.807 190.694 1.00 19.95 ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 164.666 177.979 187.612 1.00 12.05 ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 163.441 178.237 186.799 1.00 9.99  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 162.925 176.889 186.412 1.00 14.71 ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 162.729 177.256 190.083 1.00 11.93 ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 162.313 177.536 191.453 1.00 9.57  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 162.411 176.314 192.354 1.00 12.71 ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 162.430 176.466 193.579 1.00 14.25 ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 160.888 178.079 191.480 1.00 8.66  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 162.466 175.111 191.780 1.00 12.53 ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 162.689 173.916 192.583 1.00 12.95 ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 164.063 173.914 193.234 1.00 12.72 ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 164.284 173.155 194.182 1.00 17.37 ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 162.520 172.663 191.724 1.00 9.87  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 161.163 171.963 191.781 1.00 8.82  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 161.224 170.635 191.051 1.00 13.73 ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 160.722 171.764 193.217 1.00 9.74  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 164.987 174.742 192.749 1.00 9.15  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 166.331 174.808 193.298 1.00 10.70 ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 166.662 176.164 193.903 1.00 9.63  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 167.772 176.344 194.414 1.00 11.80 ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 167.359 174.453 192.216 1.00 9.90  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 167.298 173.018 191.776 1.00 12.27 ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 166.323 172.591 190.889 1.00 11.56 ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 168.204 172.091 192.260 1.00 17.17 ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 166.259 171.271 190.489 1.00 14.79 ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 168.146 170.770 191.863 1.00 15.74 ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 167.172 170.361 190.977 1.00 14.81 ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 165.737 177.119 193.861 1.00 7.52  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 165.919 178.421 194.484 1.00 9.68  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 164.935 178.700 195.607 1.00 14.94 ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 165.296 179.383 196.567 1.00 13.72 ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 165.791 179.542 193.440 1.00 9.97  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 166.734 179.362 192.272 1.00 17.15 ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 167.676 178.573 192.335 1.00 21.15 ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 166.484 180.093 191.195 1.00 15.84 ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 163.705 178.196 195.511 1.00 11.96 ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 162.684 178.433 196.518 1.00 9.52  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 162.389 177.215 197.378 1.00 15.88 ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 161.690 177.348 198.390 1.00 17.17 ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 161.384 178.906 195.851 1.00 9.10  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 161.531 180.181 195.042 1.00 10.23 ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 162.249 181.260 195.836 1.00 12.69 ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 161.726 182.591 195.557 1.00 15.72 ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 161.951 183.269 194.439 1.00 14.02 ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 162.705 182.775 193.471 1.00 11.27 ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 161.407 184.474 194.291 1.00 12.22 ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 162.892 176.041 197.011 1.00 11.30 ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 162.657 174.810 197.752 1.00 6.10  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 163.939 174.385 198.451 1.00 5.69  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 164.998 174.304 197.821 1.00 7.42  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 162.172 173.697 196.822 1.00 5.37  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 160.610 174.043 195.991 1.00 23.60 ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 163.840 174.117 199.751 1.00 7.17  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 164.973 173.580 200.494 1.00 5.05  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 165.170 172.129 200.081 1.00 4.86  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 164.249 171.311 200.176 1.00 9.69  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 164.750 173.706 202.005 1.00 0.57  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 165.803 172.917 202.762 1.00 4.57  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 164.775 175.165 202.421 1.00 7.46  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 166.370 171.807 199.607 1.00 4.57  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 166.665 170.480 199.089 1.00 5.65  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 167.206 169.598 200.205 1.00 8.21  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 168.166 169.969 200.888 1.00 8.98  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 167.672 170.565 197.941 1.00 3.37  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 167.779 169.375 196.985 1.00 5.96  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 168.191 169.854 195.605 1.00 11.32 ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 168.759 168.335 197.497 1.00 6.96  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 166.588 168.434 200.388 1.00 7.56  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 167.045 167.441 201.349 1.00 4.79  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 167.297 166.135 200.611 1.00 3.99  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 166.371 165.555 200.032 1.00 10.58 ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 166.026 167.241 202.471 1.00 3.71  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 166.059 168.359 203.490 1.00 9.42  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 167.122 168.878 203.822 1.00 9.91  ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 164.894 168.727 204.000 1.00 13.74 ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 168.545 165.678 200.635 1.00 2.25  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 168.930 164.431 199.979 1.00 3.85  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 168.777 163.299 200.983 1.00 8.88  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 169.700 162.965 201.725 1.00 9.41  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 170.351 164.517 199.440 1.00 4.49  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 170.597 163.599 198.292 1.00 5.38  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 170.865 162.265 198.352 1.00 4.79  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 170.585 163.943 196.903 1.00 8.41  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 171.026 161.757 197.088 1.00 5.99  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 170.858 162.768 196.180 1.00 6.72  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 170.372 165.132 196.201 1.00 8.83  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 170.926 162.745 194.790 1.00 8.14  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 170.438 165.108 194.821 1.00 10.06 ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 170.714 163.923 194.130 1.00 9.93  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 167.582 162.707 201.010 1.00 6.45  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 167.376 161.519 201.829 1.00 3.44  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 168.183 160.347 201.286 1.00 7.03  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 168.785 159.590 202.056 1.00 8.94  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 165.890 161.163 201.883 1.00 3.85  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 165.061 162.100 202.722 1.00 7.30  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 165.585 163.288 203.202 1.00 11.23 ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 163.748 161.785 203.029 1.00 8.66  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 164.819 164.142 203.970 1.00 11.20 ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 162.977 162.633 203.796 1.00 6.77  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 163.513 163.814 204.266 1.00 12.16 ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 168.212 160.190 199.963 1.00 5.37  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 168.939 159.103 199.345 1.00 2.28  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 168.341 157.754 199.703 1.00 8.03  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 167.160 157.630 200.040 1.00 11.07 ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 169.178 156.727 199.629 1.00 9.84  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 168.810 155.389 200.060 1.00 8.16  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 169.223 155.189 201.512 1.00 5.76  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 170.060 155.918 202.050 1.00 9.57  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 169.467 154.331 199.169 1.00 11.12 ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 168.734 153.005 199.199 1.00 17.62 ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 168.033 152.730 200.193 1.00 16.59 ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 168.859 152.235 198.223 1.00 18.17 ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 168.612 154.194 202.150 1.00 3.93  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 168.959 153.885 203.530 1.00 5.83  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 170.409 153.430 203.612 1.00 9.33  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 170.837 152.538 202.876 1.00 7.89  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 168.033 152.808 204.088 1.00 5.24  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 166.636 153.278 204.333 1.00 8.31  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 166.123 154.506 204.045 1.00 6.55  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 165.572 152.527 204.929 1.00 11.46 ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 164.802 154.566 204.418 1.00 4.36  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 164.441 153.362 204.963 1.00 7.92  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 165.466 151.228 205.431 1.00 7.95  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 163.219 152.943 205.481 1.00 7.91  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 164.253 150.813 205.943 1.00 5.49  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 163.147 151.667 205.965 1.00 8.71  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 171.162 154.049 204.514 1.00 12.19 ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 172.569 153.725 204.671 1.00 9.26  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 172.728 152.370 205.351 1.00 11.44 ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 171.762 151.745 205.797 1.00 14.08 ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 173.280 154.814 205.469 1.00 12.05 ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 172.720 154.943 206.764 1.00 13.70 ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 173.980 151.913 205.422 1.00 13.55 ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 174.273 150.664 206.116 1.00 9.71  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 173.854 150.743 207.578 1.00 11.55 ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 173.321 149.778 208.135 1.00 17.56 ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 175.761 150.340 205.997 1.00 12.25 ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 176.138 150.326 204.615 1.00 14.81 ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 176.063 148.988 206.609 1.00 17.63 ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 174.079 151.896 208.210 1.00 13.70 ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 173.618 152.095 209.578 1.00 13.77 ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 172.098 152.027 209.664 1.00 13.85 ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 171.549 151.435 210.598 1.00 17.33 ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 174.129 153.432 210.111 1.00 15.38 ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 173.370 153.954 211.318 1.00 21.35 ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 173.816 155.342 211.729 1.00 27.69 ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 175.037 155.609 211.695 1.00 27.53 ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 172.948 156.167 212.081 1.00 22.42 ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 171.403 152.630 208.695 1.00 14.16 ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 169.944 152.596 208.700 1.00 12.77 ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 169.419 151.176 208.531 1.00 14.30 ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 168.491 150.762 209.235 1.00 13.12 ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 169.394 153.503 207.603 1.00 10.55 ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 170.002 150.416 207.599 1.00 13.56 ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 169.587 149.029 207.414 1.00 7.64  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 169.859 148.204 208.663 1.00 9.85  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 169.022 147.392 209.074 1.00 13.45 ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 170.302 148.421 206.208 1.00 5.60  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 170.084 149.076 204.848 1.00 6.43  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 170.930 148.387 203.792 1.00 7.28  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 168.616 149.044 204.466 1.00 6.13  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 171.025 148.401 209.281 1.00 10.04 ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 171.352 147.665 210.496 1.00 11.47 ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 170.376 147.992 211.618 1.00 16.06 ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 169.910 147.093 212.326 1.00 20.24 ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 172.784 147.975 210.927 1.00 14.36 ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 173.241 147.184 212.129 1.00 17.87 ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 173.736 145.896 211.986 1.00 16.03 ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 173.177 147.724 213.405 1.00 17.95 ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 174.151 145.168 213.078 1.00 16.45 ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 173.593 147.001 214.505 1.00 16.86 ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 174.080 145.724 214.335 1.00 18.40 ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 174.495 144.999 215.425 1.00 24.59 ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 170.057 149.276 211.798 1.00 16.93 ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 169.130 149.667 212.853 1.00 13.97 ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 167.732 149.121 212.597 1.00 14.54 ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 167.068 148.650 213.526 1.00 17.77 ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 169.096 151.189 212.984 1.00 13.00 ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 170.342 151.782 213.614 1.00 12.80 ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 170.176 153.244 213.957 1.00 17.29 ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 170.925 154.096 213.480 1.00 14.71 ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 169.187 153.547 214.790 1.00 20.33 ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 167.268 149.174 211.346 1.00 11.01 ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 165.946 148.644 211.023 1.00 10.53 ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 165.897 147.144 211.285 1.00 17.89 ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 164.939 146.635 211.882 1.00 21.40 ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 165.576 148.980 209.566 1.00 10.04 ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 164.447 148.085 209.081 1.00 13.02 ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 165.186 150.440 209.445 1.00 14.06 ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 166.931 146.417 210.859 1.00 14.91 ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 166.965 144.986 211.105 1.00 10.14 ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 167.004 144.646 212.581 1.00 14.48 ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 166.283 143.762 213.042 1.00 19.71 ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 167.837 145.354 213.348 1.00 15.11 ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 167.939 145.073 214.777 1.00 17.77 ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 166.640 145.397 215.502 1.00 20.65 ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 166.218 144.648 216.391 1.00 22.38 ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 169.106 145.850 215.384 1.00 19.15 ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 169.256 145.654 216.881 1.00 22.41 ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 170.507 146.328 217.410 1.00 20.14 ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 171.741 145.512 217.078 1.00 20.83 ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 171.747 144.204 217.789 1.00 24.58 ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 165.992 146.508 215.144 1.00 20.89 ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 164.735 146.864 215.795 1.00 23.69 ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 163.629 145.877 215.446 1.00 25.37 ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 162.867 145.459 216.326 1.00 24.80 ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 164.324 148.284 215.413 1.00 20.60 ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 162.967 148.699 215.960 1.00 22.77 ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 162.943 148.764 217.475 1.00 28.29 ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 163.991 149.078 218.076 1.00 28.06 ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 161.875 148.500 218.065 1.00 30.55 ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 163.521 145.490 214.172 1.00 21.59 ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 162.437 144.592 213.790 1.00 22.91 ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 162.671 143.182 214.316 1.00 22.91 ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 161.726 142.516 214.753 1.00 24.69 ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 162.266 144.567 212.276 1.00 19.33 ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 160.955 143.987 211.835 1.00 20.22 ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 159.848 144.801 211.680 1.00 19.97 ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 160.814 142.628 211.623 1.00 22.56 ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 158.638 144.274 211.290 1.00 21.51 ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 159.606 142.098 211.230 1.00 25.80 ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 158.517 142.921 211.070 1.00 25.42 ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 163.916 142.709 214.287 1.00 21.53 ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 164.225 141.349 214.712 1.00 24.85 ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 164.381 141.221 216.223 1.00 26.72 ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 164.760 140.146 216.698 1.00 30.34 ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 165.501 140.845 214.027 1.00 25.04 ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 166.603 141.687 214.381 1.00 27.47 ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 165.339 140.863 212.514 1.00 23.04 ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 164.111 142.282 216.987 1.00 28.78 ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 164.193 142.173 218.441 1.00 29.53 ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 163.159 141.198 218.987 1.00 32.01 ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 163.411 140.534 219.999 1.00 29.82 ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 164.020 143.547 219.084 1.00 27.89 ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 162.819 144.159 218.651 1.00 27.45 ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 161.995 141.100 218.339 1.00 32.57 ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 160.987 140.134 218.765 1.00 32.66 ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 161.459 138.700 218.561 1.00 35.16 ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 161.110 137.814 219.350 1.00 34.19 ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 159.679 140.380 218.012 1.00 35.51 ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 159.832 140.449 216.498 1.00 35.36 ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 158.480 140.566 215.813 1.00 36.24 ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 158.629 140.715 214.308 1.00 33.75 ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 157.312 140.854 213.624 1.00 32.21 ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 162.245 138.452 217.517 1.00 36.69 ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 162.797 137.126 217.282 1.00 34.69 ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 163.790 136.758 218.374 1.00 33.79 ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 164.451 137.621 218.959 1.00 32.30 ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 163.484 137.068 215.920 1.00 33.05 ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 162.540 136.919 214.750 1.00 34.29 ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 163.368 136.146 213.355 1.00 39.62 ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 164.196 137.549 212.638 1.00 29.15 ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 163.893 135.456 218.647 1.00 42.09 ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 164.830 134.976 219.655 1.00 43.51 ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 166.258 135.324 219.261 1.00 44.68 ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 166.900 136.149 219.918 1.00 47.32 ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 164.682 133.465 219.846 1.00 41.81 ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 165.392 132.962 221.089 1.00 44.57 ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 165.884 133.795 221.877 1.00 45.32 ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 165.446 131.729 221.284 1.00 45.09 ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 166.750 134.721 218.176 1.00 37.24 ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 168.069 135.035 217.615 1.00 36.51 ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 169.174 134.979 218.668 1.00 38.12 ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 170.178 135.691 218.574 1.00 39.89 ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 168.060 136.402 216.926 1.00 35.74 ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 167.543 136.440 215.487 1.00 37.21 ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 167.799 137.801 214.866 1.00 38.35 ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 168.181 135.340 214.657 1.00 36.81 ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 169.003 134.135 219.681 1.00 42.88 ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 169.949 134.023 220.780 1.00 44.16 ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 170.638 132.667 220.723 1.00 45.51 ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 169.971 131.627 220.694 1.00 45.27 ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 169.253 134.203 222.131 1.00 45.80 ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 168.760 135.618 222.402 1.00 44.77 ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 169.886 136.605 222.634 1.00 44.56 ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 171.032 136.166 222.868 1.00 42.55 ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 169.626 137.825 222.581 1.00 44.69 ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 171.969 132.683 220.708 1.00 45.08 ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 172.769 131.462 220.683 1.00 46.17 ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 174.008 131.690 221.537 1.00 46.74 ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 175.025 132.210 221.059 1.00 44.37 ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 173.144 131.070 219.254 1.00 44.33 ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 173.335 129.578 219.047 1.00 45.08 ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 173.695 129.264 217.605 1.00 44.84 ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 175.105 129.721 217.278 1.00 44.08 ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 175.704 128.925 216.173 1.00 43.81 ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 173.954 131.322 222.819 1.00 50.24 ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 175.114 131.551 223.696 1.00 49.52 ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 176.365 130.813 223.258 1.00 48.96 ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 177.477 131.261 223.567 1.00 47.02 ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 174.617 131.064 225.065 1.00 48.98 ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 173.524 130.098 224.749 1.00 48.78 ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 172.858 130.626 223.514 1.00 47.15 ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 176.222 129.695 222.546 1.00 47.66 ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 177.356 128.917 222.074 1.00 46.77 ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 177.846 129.366 220.701 1.00 47.30 ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 178.442 128.565 219.973 1.00 46.95 ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 176.999 127.428 222.043 1.00 46.04 ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 175.884 127.118 221.065 1.00 48.65 ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 174.754 127.579 221.228 1.00 47.79 ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 176.195 126.330 220.043 1.00 47.34 ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 177.602 130.621 220.332 1.00 43.16 ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 178.056 131.133 219.046 1.00 43.21 ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 179.557 131.398 219.084 1.00 41.46 ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 180.057 132.074 219.987 1.00 41.55 ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 177.295 132.412 218.698 1.00 41.80 ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 177.814 133.147 217.482 1.00 38.90 ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 177.699 132.601 216.213 1.00 38.43 ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 178.410 134.394 217.607 1.00 39.11 ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 178.168 133.272 215.101 1.00 39.21 ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 178.882 135.073 216.501 1.00 39.40 ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 178.759 134.508 215.251 1.00 39.54 ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 179.227 135.181 214.148 1.00 39.29 ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 180.275 130.865 218.099 1.00 40.21 ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 181.713 131.067 217.974 1.00 39.90 ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 181.951 132.164 216.946 1.00 39.52 ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 181.592 132.014 215.772 1.00 39.39 ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 182.443 129.774 217.570 1.00 42.03 ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 182.302 128.692 218.646 1.00 42.30 ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 183.912 130.058 217.286 1.00 37.86 ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 181.095 127.794 218.474 1.00 39.80 ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 182.551 133.261 217.384 1.00 39.58 ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 182.849 134.371 216.472 1.00 41.72 ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 183.944 133.940 215.501 1.00 42.42 ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 184.999 133.449 215.942 1.00 41.71 ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 183.270 135.610 217.260 1.00 41.64 ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 183.619 136.748 216.315 1.00 40.39 ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 182.165 136.026 218.218 1.00 40.00 ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 183.750 134.092 214.194 1.00 43.11 ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 184.806 133.727 213.248 1.00 43.20 ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 185.999 134.663 213.358 1.00 45.12 ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 185.878 135.818 213.771 1.00 45.25 ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 184.121 133.858 211.884 1.00 42.14 ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 183.055 134.870 212.108 1.00 42.78 ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 182.569 134.652 213.515 1.00 42.12 ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 187.169 134.138 212.989 1.00 54.71 ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 188.382 134.948 213.024 1.00 57.22 ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 188.286 136.124 212.059 1.00 58.43 ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 188.691 137.243 212.393 1.00 58.27 ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 189.601 134.084 212.700 1.00 57.42 ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 189.927 133.100 213.807 1.00 59.49 ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 189.633 133.406 214.982 1.00 58.53 ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 190.476 132.020 213.500 1.00 58.29 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 187.752 135.890 210.865 1.00 58.76 ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 187.574 136.930 209.853 1.00 59.85 ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 186.078 137.210 209.737 1.00 60.70 ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 185.376 136.603 208.926 1.00 58.34 ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 188.177 136.504 208.518 1.00 57.80 ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 188.068 137.556 207.440 1.00 59.71 ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 188.736 138.767 207.555 1.00 59.34 ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 187.297 137.338 206.306 1.00 60.05 ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 188.641 139.732 206.571 1.00 59.17 ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 187.195 138.298 205.317 1.00 60.31 ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 187.869 139.493 205.455 1.00 60.13 ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 187.770 140.451 204.473 1.00 61.09 ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 185.596 138.136 210.556 1.00 53.32 ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 184.176 138.463 210.566 1.00 51.13 ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 183.801 139.213 209.291 1.00 48.21 ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 184.466 140.194 208.937 1.00 48.42 ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 183.834 139.305 211.793 1.00 49.06 ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 182.348 139.567 211.977 1.00 48.93 ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 181.406 138.072 212.332 1.00 54.74 ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 179.774 138.566 211.784 1.00 48.23 ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 182.753 138.793 208.579 1.00 40.19 ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 182.318 139.543 207.395 1.00 38.21 ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 181.648 140.850 207.782 1.00 39.75 ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 180.422 140.978 207.697 1.00 36.59 ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 181.331 138.591 206.706 1.00 37.32 ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 181.402 137.295 207.468 1.00 37.54 ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 181.898 137.624 208.830 1.00 38.31 ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 182.444 141.824 208.214 1.00 41.08 ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 181.905 143.076 208.738 1.00 38.63 ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 181.362 143.896 207.571 1.00 39.16 ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 182.117 144.331 206.697 1.00 39.53 ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 182.966 143.858 209.522 1.00 38.40 ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 182.484 145.269 209.803 1.00 38.72 ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 183.299 143.135 210.819 1.00 36.40 ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 180.050 144.100 207.555 1.00 30.55 ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 179.395 144.966 206.580 1.00 28.36 ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 179.054 146.317 207.190 1.00 26.23 ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 179.299 147.361 206.585 1.00 27.04 ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 178.137 144.271 206.010 1.00 25.75 ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 177.431 145.181 205.020 1.00 23.28 ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 178.513 142.953 205.359 1.00 25.20 ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 178.486 146.313 208.392 1.00 27.21 ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 178.247 147.543 209.134 1.00 27.72 ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 179.529 147.936 209.855 1.00 33.63 ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 180.049 147.168 210.670 1.00 36.44 ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 177.095 147.354 210.119 1.00 25.72 ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 176.786 148.571 210.960 1.00 26.06 ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 176.870 149.850 210.424 1.00 26.94 ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 176.404 148.443 212.287 1.00 28.99 ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 176.588 150.963 211.189 1.00 29.02 ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 176.118 149.549 213.059 1.00 27.65 ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 176.209 150.806 212.504 1.00 29.19 ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 175.925 151.911 213.272 1.00 29.36 ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 180.041 149.131 209.550 1.00 35.74 ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 181.346 149.534 210.063 1.00 36.43 ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 181.347 149.633 211.583 1.00 37.94 ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 182.313 149.226 212.238 1.00 39.18 ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 181.765 150.862 209.434 1.00 37.50 ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 181.752 150.815 207.920 1.00 41.90 ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 182.574 150.075 207.339 1.00 42.13 ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 180.918 151.515 207.308 1.00 40.67 ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 180.274 150.169 212.165 1.00 35.43 ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 180.179 150.344 213.605 1.00 34.95 ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 179.662 149.100 214.319 1.00 34.85 ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 179.181 149.204 215.455 1.00 35.18 ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 179.290 151.548 213.931 1.00 33.89 ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 180.027 152.878 213.914 1.00 34.56 ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 179.068 154.045 214.071 1.00 34.79 ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 178.368 154.361 212.762 1.00 34.19 ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 177.023 154.959 212.978 1.00 32.30 ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 179.745 147.937 213.684 1.00 32.76 ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 179.365 146.702 214.351 1.00 34.31 ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 180.316 146.436 215.515 1.00 37.55 ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 181.528 146.646 215.386 1.00 37.77 ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 179.395 145.532 213.365 1.00 31.85 ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 178.904 144.171 213.864 1.00 33.18 ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 177.393 144.157 213.981 1.00 31.30 ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 179.377 143.061 212.940 1.00 34.04 ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 179.805 145.994 216.666 1.00 36.78 ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 180.690 145.725 217.807 1.00 36.83 ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 181.747 144.686 217.463 1.00 39.04 ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 181.484 143.715 216.750 1.00 37.43 ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 179.727 145.217 218.885 1.00 35.03 ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 178.423 145.849 218.537 1.00 35.00 ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 178.384 145.902 217.035 1.00 35.47 ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 182.957 144.910 217.978 1.00 47.00 ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 184.075 144.028 217.657 1.00 47.34 ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 183.849 142.574 218.060 1.00 49.25 ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 184.241 141.688 217.281 1.00 47.30 ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 185.364 144.577 218.285 1.00 48.74 ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 185.572 146.072 218.080 1.00 51.63 ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 185.374 146.499 216.637 1.00 51.56 ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 185.964 145.925 215.721 1.00 49.25 ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 184.544 147.515 216.430 1.00 48.28 ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 183.321 142.251 219.242 1.00 49.89 ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 182.878 140.876 219.506 1.00 47.60 ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 181.407 140.699 219.170 1.00 47.21 ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 180.553 140.751 220.069 1.00 47.26 ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 183.133 140.708 221.009 1.00 46.17 ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 183.069 142.100 221.573 1.00 45.11 ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 183.165 143.097 220.440 1.00 45.67 ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 181.059 140.494 217.899 1.00 40.87 ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 179.641 140.479 217.530 1.00 38.55 ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 178.923 139.265 218.095 1.00 36.96 ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 179.464 138.158 218.148 1.00 39.84 ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 179.681 140.437 216.000 1.00 35.92 ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 180.923 139.685 215.697 1.00 37.49 ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 181.903 139.956 216.818 1.00 38.66 ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 177.684 139.489 218.522 1.00 26.93 ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 176.843 138.415 219.020 1.00 28.75 ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 176.123 137.744 217.853 1.00 35.17 ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 176.285 138.117 216.690 1.00 36.21 ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 175.854 138.951 220.055 1.00 29.80 ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 174.955 139.875 219.474 1.00 32.25 ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 175.321 136.723 218.168 1.00 32.26 ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 174.572 136.028 217.126 1.00 30.45 ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 173.567 136.956 216.455 1.00 31.61 ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 173.442 136.966 215.225 1.00 32.66 ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 173.871 134.805 217.716 1.00 31.59 ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 173.252 133.909 216.690 1.00 33.92 ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 173.972 133.360 215.650 1.00 32.52 ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 171.981 133.464 216.544 1.00 32.26 ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 173.170 132.616 214.908 1.00 30.85 ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 171.958 132.663 215.429 1.00 32.84 ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 172.848 137.752 217.251 1.00 27.72 ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 171.869 138.680 216.691 1.00 25.17 ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 172.541 139.727 215.813 1.00 27.84 ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 172.044 140.053 214.726 1.00 32.19 ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 171.090 139.350 217.820 1.00 25.53 ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 169.837 140.079 217.372 1.00 31.03 ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 169.170 140.776 218.543 1.00 28.71 ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 168.655 139.828 219.522 1.00 29.65 ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 167.482 139.216 219.431 1.00 32.01 ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 166.674 139.422 218.404 1.00 32.68 ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 167.111 138.376 220.392 1.00 31.07 ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 173.671 140.271 216.271 1.00 23.06 ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 174.388 141.265 215.482 1.00 21.78 ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 174.896 140.667 214.176 1.00 24.00 ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 174.832 141.314 213.125 1.00 26.48 ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 175.542 141.845 216.297 1.00 21.62 ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 175.096 142.553 217.562 1.00 24.77 ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 176.261 143.048 218.388 1.00 30.28 ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 177.416 142.826 217.973 1.00 33.01 ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 176.023 143.656 219.452 1.00 31.79 ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 175.405 139.434 214.226 1.00 22.36 ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 175.850 138.769 213.007 1.00 20.53 ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 174.687 138.542 212.047 1.00 21.87 ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 174.841 138.687 210.829 1.00 23.86 ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 176.531 137.445 213.349 1.00 21.47 ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 173.514 138.191 212.578 1.00 20.86 ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 172.345 137.981 211.728 1.00 18.12 ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 171.936 139.281 211.042 1.00 19.08 ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 171.652 139.305 209.835 1.00 23.85 ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 171.189 137.387 212.555 1.00 15.44 ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 171.485 135.929 212.913 1.00 18.30 ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 169.881 137.501 211.804 1.00 16.68 ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 171.370 134.978 211.747 1.00 21.66 ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 171.903 140.382 211.793 1.00 13.26 ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 171.516 141.661 211.199 1.00 12.95 ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 172.559 142.115 210.181 1.00 15.37 ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 172.222 142.691 209.137 1.00 21.30 ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 171.284 142.716 212.295 1.00 13.77 ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 170.811 144.016 211.677 1.00 15.73 ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 170.261 142.217 213.297 1.00 12.38 ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 173.838 141.858 210.464 1.00 11.39 ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 174.887 142.166 209.498 1.00 12.23 ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 174.704 141.356 208.220 1.00 16.06 ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 174.914 141.869 207.115 1.00 18.16 ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 176.257 141.899 210.119 1.00 12.55 ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 177.388 142.496 209.314 1.00 20.66 ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 177.479 143.713 209.159 1.00 24.55 ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 178.264 141.643 208.798 1.00 22.04 ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 174.313 140.089 208.355 1.00 13.46 ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 174.035 139.268 207.181 1.00 12.27 ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 172.864 139.824 206.383 1.00 12.99 ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 172.877 139.800 205.149 1.00 16.01 ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 173.763 137.824 207.602 1.00 12.99 ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 174.860 137.291 208.322 1.00 18.88 ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 171.831 140.319 207.070 1.00 8.65  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 170.701 140.930 206.370 1.00 5.90  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 171.139 142.162 205.581 1.00 10.81 ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 170.749 142.349 204.414 1.00 18.88 ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 169.606 141.299 207.369 1.00 2.81  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 168.930 139.908 208.298 1.00 4.27  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 171.954 143.016 206.204 1.00 8.59  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 172.472 144.189 205.503 1.00 7.06  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 173.302 143.762 204.301 1.00 9.54  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 173.218 144.363 203.220 1.00 12.10 ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 173.281 145.076 206.468 1.00 9.08  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 173.800 146.301 205.744 1.00 13.20 ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 172.427 145.484 207.651 1.00 7.40  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 174.110 142.710 204.464 1.00 9.62  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 174.890 142.202 203.343 1.00 12.42 ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 173.987 141.705 202.225 1.00 10.03 ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 174.320 141.846 201.047 1.00 13.62 ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 175.821 141.075 203.790 1.00 11.79 ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 176.522 140.395 202.646 1.00 13.49 ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 177.638 140.970 202.065 1.00 14.42 ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 176.050 139.197 202.134 1.00 11.55 ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 178.278 140.357 201.008 1.00 11.94 ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 176.686 138.583 201.074 1.00 10.19 ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 177.804 139.162 200.513 1.00 11.68 ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 172.857 141.090 202.575 1.00 4.53  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 171.920 140.621 201.555 1.00 7.05  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 171.399 141.797 200.739 1.00 8.93  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 171.353 141.754 199.501 1.00 12.52 ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 170.769 139.830 202.203 1.00 4.66  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 169.660 139.594 201.200 1.00 4.40  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 171.278 138.508 202.746 1.00 6.26  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 171.014 142.877 201.419 1.00 6.45  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 170.545 144.055 200.691 1.00 5.04  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 171.638 144.602 199.771 1.00 8.17  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 171.402 144.883 198.583 1.00 10.73 ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 170.075 145.125 201.678 1.00 5.29  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 169.178 146.157 201.070 1.00 6.58  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 167.871 145.890 200.717 1.00 6.15  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 169.394 147.454 200.754 1.00 8.34  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 167.325 146.980 200.209 1.00 5.36  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 168.227 147.943 200.219 1.00 8.40  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 172.860 144.721 200.297 1.00 7.59  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 173.948 145.278 199.501 1.00 8.40  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 174.321 144.374 198.329 1.00 11.36 ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 174.693 144.869 197.258 1.00 14.66 ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 175.161 145.547 200.390 1.00 8.50  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 174.847 146.419 201.596 1.00 11.34 ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 176.025 147.257 202.041 1.00 16.40 ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 177.149 146.767 202.139 1.00 17.72 ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 175.771 148.530 202.323 1.00 13.51 ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 174.222 143.054 198.495 1.00 9.90  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 174.565 142.163 197.394 1.00 9.12  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 173.469 142.124 196.339 1.00 9.17  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 173.764 141.871 195.170 1.00 9.15  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 174.877 140.751 197.900 1.00 12.90 ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 175.355 139.954 196.811 1.00 19.98 ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 173.651 140.088 198.456 1.00 3.86  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 172.210 142.389 196.703 1.00 13.38 ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 171.217 142.660 195.659 1.00 12.11 ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 171.553 143.929 194.885 1.00 8.94  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 171.393 143.976 193.657 1.00 14.30 ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 169.804 142.736 196.237 1.00 5.34  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 169.041 141.426 196.442 1.00 6.46  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 168.813 140.798 195.079 1.00 4.40  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 169.731 140.443 197.357 1.00 13.21 ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 172.020 144.969 195.579 1.00 8.88  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 172.478 146.161 194.860 1.00 11.59 ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 173.603 145.813 193.886 1.00 14.91 ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 173.604 146.244 192.724 1.00 12.28 ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 172.934 147.232 195.850 1.00 10.46 ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 171.808 147.993 196.476 1.00 10.98 ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 171.012 148.863 195.763 1.00 13.32 ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 171.349 148.018 197.748 1.00 10.53 ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 170.108 149.389 196.570 1.00 15.44 ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 170.290 148.892 197.780 1.00 14.91 ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 174.566 145.014 194.349 1.00 20.40 ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 175.692 144.623 193.502 1.00 16.09 ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 175.237 143.761 192.329 1.00 16.83 ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 175.777 143.870 191.224 1.00 18.30 ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 176.738 143.883 194.334 1.00 13.71 ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 177.532 144.783 195.262 1.00 16.11 ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 177.964 144.073 196.527 1.00 20.51 ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 178.067 142.847 196.561 1.00 20.67 ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 178.216 144.841 197.581 1.00 17.57 ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 174.258 142.881 192.556 1.00 20.89 ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 173.741 142.049 191.475 1.00 21.14 ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 173.053 142.893 190.412 1.00 18.78 ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 173.201 142.630 189.214 1.00 24.22 ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 172.782 140.997 192.031 1.00 20.24 ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 172.289 143.906 190.829 1.00 19.04 ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 171.707 144.815 189.846 1.00 19.30 ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 172.787 145.555 189.074 1.00 23.72 ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 172.657 145.766 187.864 1.00 20.93 ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 170.771 145.815 190.514 1.00 18.69 ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 169.512 145.179 191.023 1.00 20.58 ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 169.035 145.484 192.116 1.00 24.27 ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 168.966 144.270 190.238 1.00 21.12 ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 173.849 145.980 189.761 1.00 27.88 ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 174.940 146.652 189.059 1.00 27.88 ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 175.578 145.730 188.026 1.00 27.32 ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 175.846 146.144 186.892 1.00 28.96 ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 175.985 147.143 190.060 1.00 27.08 ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 175.810 144.470 188.401 1.00 29.69 ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 176.398 143.503 187.479 1.00 32.31 ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 175.487 143.249 186.283 1.00 31.45 ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 175.957 143.166 185.143 1.00 32.74 ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 176.689 142.197 188.221 1.00 31.81 ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 176.467 140.937 187.401 1.00 30.54 ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 176.983 139.709 188.136 1.00 32.21 ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 177.014 138.523 187.288 1.00 35.69 ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 177.410 137.325 187.694 1.00 33.59 ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 177.824 137.117 188.932 1.00 31.82 ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 177.387 136.309 186.835 1.00 33.84 ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 174.181 143.123 186.527 1.00 34.67 ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 173.241 142.893 185.434 1.00 33.42 ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 173.141 144.101 184.511 1.00 33.67 ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 173.023 143.936 183.291 1.00 31.52 ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 171.865 142.535 185.994 1.00 30.85 ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 170.933 141.745 185.075 1.00 29.57 ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 171.438 140.330 184.868 1.00 32.08 ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 169.523 141.732 185.646 1.00 32.56 ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 173.179 145.314 185.067 1.00 34.81 ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 173.082 146.513 184.240 1.00 35.04 ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 174.354 146.735 183.434 1.00 37.74 ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 174.296 147.237 182.305 1.00 35.55 ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 172.780 147.728 185.114 1.00 34.86 ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 175.513 146.381 183.997 1.00 44.33 ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 176.764 146.532 183.260 1.00 44.66 ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 176.783 145.668 182.006 1.00 44.44 ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 177.368 146.058 180.988 1.00 44.36 ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 177.949 146.196 184.171 1.00 43.31 ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 179.213 145.757 183.447 1.00 44.90 ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 180.234 145.188 184.420 1.00 44.53 ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 181.532 144.820 183.717 1.00 44.58 ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 181.602 143.364 183.411 1.00 44.13 ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 176.126 144.512 182.045 1.00 41.93 ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 176.055 143.611 180.903 1.00 42.20 ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 174.929 143.963 179.942 1.00 44.52 ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 174.681 143.212 178.993 1.00 42.46 ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 175.894 142.166 181.382 1.00 43.46 ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 177.170 141.546 181.924 1.00 44.36 ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 177.175 140.008 181.928 1.00 44.99 ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 176.265 139.396 182.894 1.00 45.55 ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 174.960 139.220 182.723 1.00 45.54 ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 174.363 139.515 181.579 1.00 44.55 ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 174.241 138.704 183.715 1.00 43.32 ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 174.239 145.080 180.164 1.00 40.65 ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 173.179 145.517 179.284 1.00 36.23 ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 171.818 144.908 179.549 1.00 37.02 ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 170.896 145.134 178.757 1.00 34.60 ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 171.662 144.148 180.632 1.00 39.85 ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 170.385 143.542 180.939 1.00 34.72 ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 169.407 144.515 181.567 1.00 34.48 ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 169.715 145.677 181.835 1.00 34.35 ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 168.199 144.018 181.805 1.00 34.33 ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 167.125 144.806 182.394 1.00 31.14 ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 167.069 144.546 183.893 1.00 28.60 ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 167.002 143.391 184.326 1.00 28.18 ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 165.785 144.466 181.743 1.00 27.34 ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 164.655 145.406 182.117 1.00 27.57 ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 163.520 145.318 181.111 1.00 31.26 ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 163.878 145.917 179.831 1.00 32.36 ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 164.233 145.231 178.754 1.00 33.83 ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 164.298 143.909 178.766 1.00 30.53 ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 164.533 145.886 177.636 1.00 32.71 ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 167.098 145.620 184.680 1.00 25.78 ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 167.149 145.526 186.130 1.00 24.27 ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 166.015 146.330 186.745 1.00 24.50 ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 165.561 147.328 186.181 1.00 27.83 ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 168.487 146.039 186.686 1.00 29.28 ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 168.509 147.470 186.639 1.00 30.06 ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 169.651 145.495 185.878 1.00 29.98 ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 165.566 145.885 187.915 1.00 19.57 ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 164.554 146.582 188.692 1.00 17.35 ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 165.191 147.145 189.956 1.00 19.52 ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 166.043 146.499 190.572 1.00 23.36 ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 163.395 145.651 189.057 1.00 12.16 ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 162.690 145.050 187.855 1.00 15.00 ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 161.931 146.294 186.798 1.00 24.23 ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 161.118 145.252 185.593 1.00 16.21 ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 164.778 148.353 190.329 1.00 15.67 ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 165.382 149.031 191.464 1.00 13.23 ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 165.070 148.306 192.768 1.00 11.45 ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 163.939 147.872 193.001 1.00 12.18 ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 164.890 150.475 191.540 1.00 11.60 ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 166.084 148.176 193.619 1.00 7.57  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 165.902 147.673 194.975 1.00 6.82  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 165.782 148.857 195.920 1.00 10.96 ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 166.658 149.727 195.964 1.00 12.17 ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 167.051 146.742 195.394 1.00 6.19  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 167.108 145.525 194.480 1.00 9.34  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 166.888 146.315 196.839 1.00 7.73  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 165.899 144.625 194.571 1.00 12.85 ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 164.691 148.889 196.669 1.00 9.08  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 164.324 149.975 197.555 1.00 5.96  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 164.314 149.479 198.994 1.00 8.46  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 164.383 148.269 199.238 1.00 10.03 ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 162.942 150.516 197.167 1.00 5.25  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 161.963 149.482 197.313 1.00 8.02  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 162.952 150.989 195.722 1.00 6.21  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 164.251 150.383 199.974 1.00 8.26  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 164.129 149.927 201.367 1.00 1.96  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 162.906 149.064 201.620 1.00 4.28  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 162.881 148.313 202.604 1.00 10.73 ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 164.065 151.243 202.150 1.00 4.05  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 164.828 152.198 201.319 1.00 7.23  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 164.532 151.828 199.896 1.00 8.69  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 161.883 149.150 200.765 1.00 6.92  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 160.718 148.285 200.918 1.00 4.59  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 161.088 146.823 200.705 1.00 7.37  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 160.509 145.931 201.339 1.00 8.38  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 159.619 148.714 199.948 1.00 3.42  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 159.212 150.168 200.103 1.00 9.74  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 157.757 150.401 199.737 1.00 11.43 ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 156.854 149.483 200.418 1.00 9.33  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 155.589 149.288 200.076 1.00 6.39  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 155.039 149.942 199.066 1.00 3.86  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 154.855 148.422 200.768 1.00 4.88  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 162.049 146.553 199.819 1.00 7.91  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 162.545 145.188 199.662 1.00 3.15  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 163.178 144.691 200.954 1.00 5.15  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 162.955 143.549 201.371 1.00 7.75  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 163.553 145.117 198.515 1.00 4.97  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 162.979 145.457 197.176 1.00 6.49  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 162.516 146.716 196.861 1.00 9.66  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 162.794 144.701 196.068 1.00 6.71  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 162.072 146.722 195.617 1.00 8.73  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 162.229 145.512 195.114 1.00 10.12 ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 163.972 145.545 201.607 1.00 4.94  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 164.562 145.182 202.892 1.00 1.25  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 163.488 144.933 203.939 1.00 3.12  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 163.583 143.982 204.726 1.00 11.46 ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 165.510 146.284 203.357 1.00 4.29  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 166.330 145.917 204.569 1.00 4.24  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 167.259 144.889 204.519 1.00 5.25  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 166.168 146.594 205.769 1.00 4.19  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 168.007 144.550 205.626 1.00 6.05  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 166.911 146.263 206.881 1.00 5.42  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 167.829 145.239 206.804 1.00 5.70  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 168.573 144.905 207.911 1.00 8.81  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 162.461 145.781 203.969 1.00 5.31  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 161.377 145.594 204.927 1.00 4.63  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 160.679 144.260 204.702 1.00 4.76  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 160.427 143.513 205.653 1.00 10.45 ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 160.386 146.750 204.827 1.00 6.47  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 160.936 148.127 205.199 1.00 3.44  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 159.868 149.185 205.023 1.00 7.89  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 161.456 148.123 206.625 1.00 0.58  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 160.375 143.935 203.443 1.00 6.01  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 159.750 142.649 203.148 1.00 4.76  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 160.657 141.496 203.542 1.00 9.63  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 160.184 140.470 204.035 1.00 11.79 ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 159.393 142.551 201.669 1.00 2.22  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 158.265 143.468 201.285 1.00 13.90 ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 157.409 143.760 202.146 1.00 18.28 ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 158.230 143.889 200.117 1.00 14.13 ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 161.964 141.646 203.327 1.00 6.99  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 162.902 140.608 203.732 1.00 0.25  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 162.842 140.382 205.237 1.00 1.90  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 162.807 139.237 205.697 1.00 10.85 ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 164.312 140.993 203.271 1.00 1.67  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 165.419 140.180 203.886 1.00 4.04  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 165.298 138.811 204.057 1.00 10.43 ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 166.599 140.790 204.268 1.00 2.58  ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 166.323 138.077 204.619 1.00 7.36  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 167.623 140.060 204.823 1.00 5.03  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 167.485 138.702 205.000 1.00 7.88  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 162.797 141.460 206.019 1.00 3.91  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 162.805 141.304 207.473 1.00 5.55  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 161.474 140.738 207.976 1.00 9.27  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 161.451 139.889 208.877 1.00 14.52 ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 163.167 142.635 208.154 1.00 5.88  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 164.452 143.199 207.559 1.00 4.02  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 163.438 142.408 209.614 1.00 15.09 ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 165.620 142.243 207.630 1.00 6.82  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 160.346 141.188 207.410 1.00 6.82  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 159.060 140.579 207.762 1.00 7.53  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 159.020 139.099 207.401 1.00 12.60 ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 158.521 138.279 208.181 1.00 16.25 ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 157.884 141.304 207.101 1.00 8.07  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 157.730 142.743 207.555 1.00 14.19 ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 156.992 143.051 208.483 1.00 17.87 ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 158.488 143.630 206.925 1.00 14.29 ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 159.522 138.737 206.218 1.00 6.90  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 159.553 137.333 205.831 1.00 6.31  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 160.441 136.531 206.769 1.00 9.10  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 160.112 135.396 207.126 1.00 16.78 ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 160.036 137.198 204.388 1.00 9.30  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 158.973 137.456 203.368 1.00 7.38  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 159.154 138.317 202.308 1.00 5.92  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 157.718 136.965 203.243 1.00 5.92  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 158.056 138.347 201.575 1.00 4.06  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 157.168 137.535 202.121 1.00 8.97  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 161.573 137.106 207.180 1.00 6.68  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 162.457 136.422 208.113 1.00 7.49  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 161.747 136.155 209.431 1.00 12.50 ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 161.781 135.034 209.949 1.00 17.08 ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 163.721 137.256 208.330 1.00 7.15  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 164.833 136.545 209.064 1.00 9.08  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 164.826 135.166 209.219 1.00 15.60 ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 165.899 137.253 209.594 1.00 10.92 ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 165.841 134.516 209.886 1.00 17.58 ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 166.916 136.613 210.263 1.00 14.42 ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 166.885 135.246 210.406 1.00 16.47 ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 167.902 134.601 211.072 1.00 17.73 ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 161.071 137.169 209.972 1.00 14.23 ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 160.347 136.986 211.225 1.00 15.12 ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 159.260 135.925 211.083 1.00 17.45 ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 159.152 135.009 211.911 1.00 20.45 ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 159.750 138.316 211.682 1.00 17.88 ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 158.450 136.027 210.026 1.00 15.51 ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 157.334 135.103 209.847 1.00 11.28 ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 157.826 133.672 209.681 1.00 15.19 ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 157.309 132.748 210.316 1.00 23.67 ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 156.493 135.525 208.643 1.00 11.41 ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 155.858 136.886 208.826 1.00 16.93 ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 155.965 137.495 209.889 1.00 17.93 ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 155.191 137.372 207.786 1.00 15.47 ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 158.835 133.470 208.827 1.00 12.10 ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 159.369 132.131 208.614 1.00 13.91 ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 160.007 131.582 209.879 1.00 19.77 ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 159.862 130.396 210.185 1.00 23.81 ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 160.377 132.145 207.466 1.00 13.29 ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 159.808 132.422 206.075 1.00 16.99 ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 160.924 132.557 205.061 1.00 15.58 ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 158.844 131.322 205.669 1.00 17.75 ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 160.715 132.427 210.631 1.00 22.42 ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 161.318 131.974 211.879 1.00 22.13 ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 160.258 131.467 212.845 1.00 23.62 ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 160.358 130.347 213.360 1.00 27.38 ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 162.117 133.114 212.506 1.00 23.26 ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 163.079 132.672 213.571 1.00 24.27 ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 164.320 132.162 213.234 1.00 26.42 ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 162.745 132.780 214.910 1.00 23.77 ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 165.207 131.762 214.213 1.00 26.94 ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 163.627 132.381 215.892 1.00 25.98 ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 164.860 131.872 215.543 1.00 27.23 ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 159.220 132.274 213.093 1.00 22.16 ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 158.180 131.839 214.021 1.00 24.11 ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 157.458 130.597 213.512 1.00 27.12 ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 157.192 129.668 214.284 1.00 31.63 ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 157.183 132.967 214.296 1.00 25.99 ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 157.808 134.209 214.852 1.00 31.55 ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 157.788 135.414 214.182 1.00 33.77 ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 158.512 134.425 215.989 1.00 29.26 ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 158.424 136.324 214.898 1.00 31.86 ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 158.872 135.751 215.999 1.00 32.23 ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 157.150 130.548 212.213 1.00 26.55 ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 156.414 129.411 211.668 1.00 26.86 ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 157.223 128.123 211.778 1.00 28.76 ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 156.718 127.097 212.250 1.00 34.88 ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 156.034 129.690 210.214 1.00 25.88 ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 155.256 128.574 209.546 1.00 29.66 ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 155.320 128.647 208.035 1.00 32.68 ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 155.111 129.748 207.484 1.00 31.71 ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 155.576 127.605 207.398 1.00 31.10 ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 158.487 128.161 211.349 1.00 25.40 ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 159.331 126.975 211.413 1.00 28.17 ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 159.575 126.547 212.852 1.00 31.74 ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 159.563 125.349 213.155 1.00 35.45 ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 160.659 127.232 210.700 1.00 28.16 ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 160.531 127.453 209.203 1.00 29.49 ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 159.839 126.284 208.526 1.00 31.86 ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 159.632 126.552 207.046 1.00 29.73 ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 158.857 125.464 206.393 1.00 30.91 ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 159.797 127.506 213.754 1.00 34.53 ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 160.022 127.159 215.152 1.00 36.97 ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 158.794 126.488 215.754 1.00 36.85 ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 158.906 125.463 216.434 1.00 39.49 ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 160.401 128.411 215.943 1.00 37.58 ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 161.088 128.135 217.268 1.00 38.86 ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 162.261 129.081 217.477 1.00 38.01 ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 162.852 128.943 218.804 1.00 42.70 ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 164.139 129.126 219.072 1.00 42.60 ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 165.004 129.446 218.125 1.00 39.19 ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 164.565 128.983 220.324 1.00 38.56 ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 157.605 127.044 215.500 1.00 32.54 ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 156.386 126.446 216.033 1.00 35.25 ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 156.161 125.052 215.463 1.00 40.19 ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 155.808 124.119 216.200 1.00 43.48 ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 155.188 127.347 215.736 1.00 34.85 ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 155.434 128.676 216.157 1.00 37.23 ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 156.363 124.888 214.152 1.00 38.53 ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 156.182 123.577 213.540 1.00 35.58 ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 157.153 122.559 214.119 1.00 37.82 ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 156.772 121.419 214.413 1.00 42.20 ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 156.355 123.677 212.024 1.00 34.06 ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 155.211 124.373 211.307 1.00 36.14 ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 155.526 124.652 209.851 1.00 39.58 ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 156.663 124.361 209.423 1.00 37.89 ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 154.641 125.163 209.135 1.00 41.36 ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 158.417 122.952 214.297 1.00 37.66 ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 159.411 122.031 214.834 1.00 39.65 ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 159.097 121.657 216.278 1.00 43.74 ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 159.244 120.494 216.663 1.00 45.70 ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 160.808 122.638 214.719 1.00 39.25 ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 161.963 121.749 215.177 1.00 42.78 ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 162.005 120.476 214.353 1.00 43.26 ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 163.277 122.492 215.058 1.00 41.92 ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 158.663 122.625 217.092 1.00 47.00 ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 158.289 122.312 218.468 1.00 46.22 ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 157.112 121.346 218.513 1.00 44.58 ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 157.110 120.384 219.293 1.00 47.83 ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 157.962 123.591 219.242 1.00 46.57 ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 159.100 124.592 219.338 1.00 46.83 ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 159.876 124.471 220.632 1.00 50.26 ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 159.319 123.941 221.615 1.00 49.48 ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 161.045 124.909 220.668 1.00 51.35 ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 156.094 121.585 217.681 1.00 44.12 ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 154.937 120.697 217.661 1.00 47.19 ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 155.335 119.289 217.235 1.00 47.80 ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 154.917 118.297 217.850 1.00 48.39 ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 153.863 121.259 216.731 1.00 45.73 ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 152.442 121.048 217.224 1.00 46.66 ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 151.406 121.426 216.187 1.00 49.00 ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 151.732 122.223 215.282 1.00 48.58 ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 150.264 120.929 216.275 1.00 50.25 ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 156.156 119.183 216.188 1.00 47.73 ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 156.597 117.875 215.720 1.00 48.12 ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 157.421 117.159 216.781 1.00 49.92 ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 157.252 115.954 217.000 1.00 52.16 ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 157.400 118.025 214.426 1.00 47.82 ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 157.849 116.710 213.817 1.00 50.56 ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 158.538 116.893 212.478 1.00 52.16 ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 158.722 118.016 212.011 1.00 50.02 ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 158.922 115.786 211.855 1.00 49.90 ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 158.317 117.885 217.454 1.00 46.53 ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 159.147 117.270 218.482 1.00 46.86 ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 158.311 116.787 219.658 1.00 47.49 ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 158.568 115.709 220.205 1.00 47.28 ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 160.219 118.253 218.952 1.00 45.92 ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 161.000 117.789 220.172 1.00 46.54 ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 161.877 116.582 219.892 1.00 48.61 ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 162.080 116.197 218.741 1.00 48.99 ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 162.401 115.978 220.952 1.00 47.89 ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 157.305 117.562 220.067 1.00 48.41 ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 156.470 117.125 221.182 1.00 49.08 ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 155.611 115.924 220.795 1.00 51.50 ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 155.433 114.998 221.597 1.00 53.23 ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 155.622 118.293 221.692 1.00 48.60 ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 154.296 117.906 222.317 1.00 50.21 ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 153.112 119.265 222.261 1.00 58.45 ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 152.594 119.201 220.553 1.00 49.28 ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 155.099 115.900 219.558 1.00 48.94 ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 154.389 114.713 219.085 1.00 48.94 ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 155.296 113.486 219.094 1.00 48.70 ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 154.888 112.401 219.534 1.00 49.27 ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 153.836 114.949 217.680 1.00 48.07 ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 152.716 115.938 217.621 1.00 48.69 ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 151.992 116.312 218.733 1.00 48.09 ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 152.190 116.626 216.581 1.00 49.34 ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 151.067 117.186 218.379 1.00 49.64 ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 151.167 117.396 217.080 1.00 49.41 ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 156.531 113.640 218.609 1.00 46.20 ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 157.462 112.519 218.585 1.00 47.99 ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 157.803 112.056 219.995 1.00 49.90 ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 157.941 110.853 220.244 1.00 52.03 ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 158.729 112.906 217.825 1.00 48.19 ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 158.566 113.071 216.315 1.00 50.19 ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 159.915 113.275 215.656 1.00 47.77 ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 157.848 111.872 215.716 1.00 51.86 ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 157.955 112.999 220.927 1.00 47.36 ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 158.231 112.633 222.312 1.00 48.72 ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 157.080 111.841 222.913 1.00 48.96 ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 157.301 110.837 223.604 1.00 48.58 ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 158.513 113.887 223.138 1.00 47.85 ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 159.993 114.183 223.264 1.00 50.14 ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 160.834 113.346 222.934 1.00 51.29 ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 160.320 115.377 223.741 1.00 49.66 ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 155.840 112.270 222.658 1.00 47.30 ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 154.685 111.532 223.169 1.00 48.49 ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 154.649 110.125 222.583 1.00 49.28 ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 154.425 109.140 223.303 1.00 48.58 ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 153.383 112.299 222.879 1.00 48.58 ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 152.180 111.480 223.315 1.00 47.62 ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 153.389 113.641 223.590 1.00 47.49 ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 154.871 110.007 221.272 1.00 48.59 ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 154.857 108.691 220.649 1.00 47.07 ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 155.944 107.777 221.186 1.00 46.73 ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 155.701 106.597 221.455 1.00 47.54 ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 157.155 108.311 221.351 1.00 45.65 ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 158.257 107.515 221.881 1.00 48.03 ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 157.982 107.081 223.314 1.00 50.85 ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 158.280 105.942 223.692 1.00 48.32 ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 159.561 108.310 221.791 1.00 47.10 ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 160.888 107.601 222.072 1.00 49.64 ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 161.988 108.230 221.239 1.00 47.92 ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 161.253 107.657 223.549 1.00 47.67 ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 157.419 107.977 224.131 1.00 53.25 ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 157.080 107.610 225.500 1.00 51.94 ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 156.044 106.498 225.527 1.00 53.50 ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 156.165 105.544 226.307 1.00 54.41 ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 156.569 108.833 226.263 1.00 53.29 ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 155.677 108.492 227.447 1.00 53.79 ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 155.433 109.700 228.337 1.00 54.67 ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 154.569 110.686 227.698 1.00 54.95 ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 154.973 111.877 227.277 1.00 53.11 ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 156.233 112.261 227.398 1.00 52.21 ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 154.092 112.701 226.720 1.00 50.88 ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 155.020 106.597 224.675 1.00 53.15 ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 154.001 105.551 224.627 1.00 53.74 ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 154.598 104.217 224.197 1.00 52.42 ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 154.278 103.171 224.773 1.00 51.28 ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 152.867 105.965 223.689 1.00 50.72 ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 151.955 107.033 224.267 1.00 53.04 ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 151.479 106.649 225.658 1.00 53.65 ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 150.713 107.786 226.314 1.00 54.22 ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 149.536 108.204 225.507 1.00 53.61 ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 155.477 104.235 223.192 1.00 49.46 ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 156.081 102.993 222.719 1.00 50.42 ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 156.969 102.377 223.797 1.00 51.95 ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 156.958 101.158 224.006 1.00 52.56 ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 156.850 103.239 221.408 1.00 51.61 ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 155.867 103.489 220.262 1.00 51.95 ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 157.743 102.056 221.082 1.00 50.23 ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 156.518 103.577 218.900 1.00 50.89 ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 157.751 103.202 224.498 1.00 53.34 ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 158.608 102.680 225.560 1.00 54.18 ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 157.784 102.107 226.709 1.00 55.06 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 158.133 101.062 227.277 1.00 53.12 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 159.543 103.780 226.065 1.00 53.44 ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 160.564 103.306 227.086 1.00 53.84 ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 161.756 102.652 226.410 1.00 53.00 ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 162.982 102.679 227.305 1.00 53.17 ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 162.619 102.599 228.747 1.00 54.02 ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 156.688 102.780 227.070 1.00 58.44 ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 155.810 102.253 228.108 1.00 59.47 ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 155.201 100.924 227.682 1.00 59.00 ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 155.088 99.995  228.492 1.00 59.72 ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 154.716 103.271 228.432 1.00 58.84 ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 154.241 103.238 229.873 1.00 59.42 ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 153.432 104.464 230.244 1.00 60.82 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 153.087 105.248 229.334 1.00 59.41 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 153.142 104.646 231.445 1.00 60.65 ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 154.809 100.814 226.411 1.00 57.43 ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 154.303 99.546  225.896 1.00 59.43 ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 155.366 98.456  225.977 1.00 59.70 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 155.063 97.306  226.311 1.00 59.93 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 153.823 99.723  224.456 1.00 59.79 ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 152.809 100.735 224.413 1.00 60.67 ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 153.255 98.421  223.911 1.00 58.34 ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 156.617 98.800  225.663 1.00 58.47 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 157.703 97.824  225.734 1.00 58.89 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 157.878 97.328  227.165 1.00 59.17 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 158.025 96.126  227.414 1.00 58.75 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 159.004 98.430  225.180 1.00 59.34 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 160.205 97.587  225.588 1.00 57.76 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 158.927 98.558  223.667 1.00 58.55 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 157.860 98.250  228.129 1.00 61.26 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 157.978 97.844  229.530 1.00 62.92 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 156.804 96.966  229.951 1.00 62.53 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 156.980 95.975  230.677 1.00 61.40 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 158.079 99.077  230.427 1.00 62.49 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 159.418 99.777  230.301 1.00 62.93 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 160.410 99.107  229.948 1.00 61.55 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 159.478 100.999 230.556 1.00 62.08 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 155.594 97.315  229.506 1.00 60.41 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 154.417 96.524  229.850 1.00 60.81 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 154.524 95.108  229.296 1.00 60.97 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 154.239 94.133  229.997 1.00 59.46 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 153.156 97.212  229.330 1.00 59.81 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 152.754 98.434  230.126 1.00 60.33 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 152.478 98.113  231.581 1.00 61.18 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 151.689 97.221  231.891 1.00 60.39 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 153.127 98.841  232.482 1.00 62.06 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 154.935 94.974  228.034 1.00 60.30 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 155.037 93.638  227.456 1.00 60.78 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 156.186 92.867  228.092 1.00 60.98 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 156.153 91.632  228.153 1.00 59.39 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 155.178 93.707  225.923 1.00 59.22 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 154.070 94.557  225.334 1.00 58.40 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 156.538 94.229  225.521 1.00 58.27 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 157.217 93.570  228.571 1.00 63.60 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 158.277 92.896  229.313 1.00 64.50 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 157.750 92.317  230.620 1.00 65.02 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 158.091 91.185  230.985 1.00 62.49 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 159.432 93.863  229.577 1.00 63.57 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 160.766 93.179  229.840 1.00 64.06 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 160.959 92.811  231.300 1.00 65.08 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 160.399 93.510  232.170 1.00 64.74 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 161.672 91.823  231.574 1.00 63.92 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 156.919 93.075  231.338 1.00 65.24 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 156.357 92.551  232.583 1.00 66.56 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 155.296 91.482  232.333 1.00 67.04 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 155.075 90.624  233.200 1.00 64.77 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 155.777 93.686  233.432 1.00 66.31 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 154.328 94.035  233.134 1.00 67.19 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 153.806 95.155  234.011 1.00 67.10 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 154.613 95.767  234.741 1.00 66.67 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 152.587 95.424  233.970 1.00 66.62 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 154.640 91.514  231.170 1.00 65.92 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 153.666 90.474  230.849 1.00 66.36 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 154.318 89.105  230.712 1.00 66.91 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 153.672 88.091  230.978 1.00 66.31 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 152.895 90.828  229.576 1.00 65.48 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 151.488 91.404  229.760 1.00 65.41 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 151.496 92.789  230.384 1.00 64.04 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 150.745 91.420  228.429 1.00 64.94 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 155.589 89.047  230.307 1.00 69.63 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 156.274 87.757  230.257 1.00 70.32 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 156.466 87.175  231.654 1.00 70.25 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 156.266 85.971  231.867 1.00 68.55 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 157.617 87.900  229.543 1.00 69.59 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 157.523 87.787  228.031 1.00 68.79 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 158.900 87.715  227.397 1.00 69.47 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 159.717 88.873  227.738 1.00 71.14 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 160.061 89.824  226.881 1.00 70.78 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 159.676 89.787  225.616 1.00 68.21 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 160.811 90.837  227.303 1.00 69.99 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 156.855 88.013  232.619 1.00 69.80 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 156.963 87.551  233.999 1.00 69.68 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 155.604 87.121  234.536 1.00 69.86 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 155.494 86.102  235.230 1.00 68.02 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 157.566 88.651  234.873 1.00 68.66 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 157.293 88.491  236.360 1.00 67.63 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 157.093 89.839  237.030 1.00 68.75 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 156.015 90.602  236.409 1.00 71.08 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 154.725 90.402  236.639 1.00 70.73 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 154.309 89.469  237.480 1.00 68.91 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 153.828 91.157  236.010 1.00 68.73 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 154.556 87.886  234.220 1.00 66.12 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 153.211 87.494  234.633 1.00 66.16 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 152.815 86.156  234.017 1.00 66.17 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 152.189 85.321  234.677 1.00 65.41 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 152.203 88.580  234.254 1.00 66.40 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 150.797 88.260  234.724 1.00 67.38 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 150.083 87.518  234.015 1.00 66.00 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 150.404 88.750  235.804 1.00 66.36 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 153.172 85.940  232.749 1.00 65.79 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 152.877 84.676  232.082 1.00 66.98 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 153.601 83.515  232.752 1.00 66.06 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 153.023 82.439  232.938 1.00 63.55 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 153.265 84.768  230.607 1.00 66.35 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 153.093 83.517  229.744 1.00 65.61 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 151.650 83.371  229.301 1.00 64.33 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 154.025 83.564  228.543 1.00 63.03 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 154.873 83.710  233.109 1.00 68.18 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 155.613 82.647  233.783 1.00 68.33 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 155.012 82.342  235.153 1.00 67.94 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 154.897 81.171  235.544 1.00 66.64 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 157.087 83.027  233.914 1.00 67.35 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 157.946 81.947  234.554 1.00 66.16 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 159.225 82.518  235.145 1.00 67.00 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 159.002 83.790  235.822 1.00 68.21 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 158.503 83.912  237.045 1.00 68.12 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 158.154 82.852  237.756 1.00 66.64 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 158.351 85.126  237.566 1.00 68.06 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 154.618 83.383  235.892 1.00 66.15 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 153.985 83.177  237.192 1.00 67.56 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 152.674 82.416  237.029 1.00 66.87 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 152.367 81.500  237.803 1.00 64.87 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 153.774 84.526  237.904 1.00 66.88 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 155.119 85.133  238.305 1.00 66.02 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 152.879 84.357  239.124 1.00 65.17 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 155.002 86.462  239.019 1.00 64.92 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 151.882 82.785  236.020 1.00 64.59 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 150.619 82.099  235.773 1.00 65.01 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 150.846 80.643  235.384 1.00 65.45 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 150.083 79.760  235.788 1.00 64.31 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 149.835 82.830  234.685 1.00 64.45 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 149.104 84.073  235.171 1.00 63.93 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 147.962 83.719  236.111 1.00 63.31 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 147.018 82.702  235.486 1.00 64.40 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 146.714 83.024  234.064 1.00 62.98 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 151.884 80.375  234.588 1.00 62.83 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 152.201 78.998  234.221 1.00 61.92 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 152.593 78.179  235.444 1.00 61.98 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 152.172 77.024  235.589 1.00 59.20 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 153.319 78.977  233.180 1.00 59.73 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 154.508 79.544  233.701 1.00 59.22 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 153.403 78.759  236.334 1.00 63.14 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 153.764 78.057  237.564 1.00 62.73 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 152.534 77.791  238.425 1.00 62.11 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 152.387 76.704  238.997 1.00 60.77 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 154.803 78.861  238.345 1.00 61.85 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 155.223 78.225  239.665 1.00 62.05 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 154.433 78.749  240.848 1.00 63.94 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 153.617 79.660  240.708 1.00 65.77 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 154.672 78.174  242.021 1.00 61.04 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 151.637 78.777  238.523 1.00 61.13 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 150.406 78.588  239.284 1.00 62.99 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 149.554 77.478  238.685 1.00 63.67 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 148.983 76.659  239.415 1.00 62.02 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 149.619 79.897  239.336 1.00 62.40 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 148.247 79.773  239.980 1.00 63.15 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 147.388 81.004  239.763 1.00 64.63 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 147.837 81.925  239.047 1.00 64.26 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 146.265 81.050  240.306 1.00 63.33 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 149.454 77.437  237.355 1.00 59.93 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 148.691 76.384  236.696 1.00 60.05 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 149.297 75.014  236.965 1.00 61.22 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 148.571 74.047  237.230 1.00 60.24 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 148.624 76.646  235.193 1.00 60.20 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 147.892 75.574  234.387 1.00 60.55 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 146.536 75.286  235.012 1.00 58.80 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 147.747 75.988  232.933 1.00 57.70 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 150.625 74.907  236.885 1.00 60.47 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 151.273 73.633  237.172 1.00 59.36 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 151.000 73.193  238.602 1.00 59.62 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 150.679 72.023  238.849 1.00 58.65 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 152.777 73.729  236.918 1.00 58.23 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 153.151 73.967  235.465 1.00 59.89 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 154.562 74.493  235.308 1.00 60.75 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 155.240 74.693  236.339 1.00 59.94 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 154.995 74.705  234.156 1.00 59.42 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 151.106 74.121  239.556 1.00 60.17 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 150.853 73.781  240.956 1.00 61.47 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 149.415 73.310  241.139 1.00 59.35 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 149.157 72.281  241.774 1.00 56.77 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 151.176 74.980  241.865 1.00 61.03 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 150.641 74.743  243.269 1.00 58.74 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 152.676 75.227  241.900 1.00 57.93 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 148.460 74.051  240.567 1.00 59.19 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 147.051 73.694  240.715 1.00 60.61 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 146.763 72.321  240.124 1.00 61.52 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 146.124 71.478  240.767 1.00 60.04 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 146.167 74.755  240.058 1.00 61.03 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 146.169 76.105  240.754 1.00 62.33 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 145.381 76.058  242.054 1.00 61.31 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 145.163 77.454  242.614 1.00 60.58 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 144.232 77.450  243.776 1.00 59.37 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 147.230 72.072  238.898 1.00 61.35 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 146.945 70.796  238.248 1.00 60.08 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 147.609 69.637  238.980 1.00 60.10 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 146.986 68.586  239.177 1.00 57.65 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 147.392 70.839  236.787 1.00 58.38 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 146.866 69.664  235.983 1.00 61.05 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 147.281 68.522  236.183 1.00 61.34 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 145.943 69.940  235.070 1.00 60.34 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 148.871 69.804  239.391 1.00 56.54 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 149.562 68.731  240.097 1.00 54.54 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 148.882 68.422  241.424 1.00 55.08 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 148.679 67.253  241.773 1.00 53.17 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 151.029 69.105  240.313 1.00 53.36 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 148.515 69.464  242.178 1.00 56.22 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 147.833 69.245  243.450 1.00 55.92 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 146.486 68.569  243.242 1.00 57.09 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 146.130 67.641  243.981 1.00 55.51 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 147.664 70.571  244.189 1.00 53.77 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 145.729 69.006  242.233 1.00 58.25 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 144.422 68.413  241.974 1.00 58.58 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 144.549 66.941  241.607 1.00 59.76 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 143.800 66.099  242.111 1.00 58.64 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 143.706 69.188  240.867 1.00 55.79 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 145.504 66.606  240.736 1.00 59.11 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 145.676 65.211  240.340 1.00 59.03 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 146.152 64.351  241.507 1.00 59.18 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 145.647 63.240  241.712 1.00 58.94 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 146.650 65.114  239.165 1.00 59.17 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 146.190 65.911  237.959 1.00 59.65 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 145.164 66.590  238.005 1.00 57.97 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 146.947 65.827  236.871 1.00 58.03 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 147.117 64.847  242.286 1.00 60.16 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 147.628 64.067  243.408 1.00 60.70 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 146.558 63.861  244.472 1.00 61.05 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 146.507 62.808  245.117 1.00 60.31 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 148.860 64.748  244.004 1.00 60.23 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 150.044 64.737  243.058 1.00 61.95 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 149.923 64.153  241.960 1.00 61.42 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 151.095 65.310  243.409 1.00 61.53 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 145.692 64.858  244.671 1.00 62.21 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 144.600 64.701  245.625 1.00 63.78 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 143.502 63.800  245.074 1.00 63.41 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 142.819 63.117  245.847 1.00 62.83 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 144.043 66.072  246.000 1.00 63.65 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 144.886 66.824  247.018 1.00 63.80 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 144.103 67.959  247.654 1.00 64.34 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 144.953 68.725  248.655 1.00 63.89 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 144.204 69.854  249.273 1.00 61.36 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 143.312 63.787  243.752 1.00 61.42 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 142.410 62.818  243.142 1.00 61.93 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 142.930 61.398  243.308 1.00 60.90 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 142.139 60.453  243.409 1.00 59.86 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 142.212 63.137  241.660 1.00 61.44 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 141.167 64.193  241.296 1.00 62.34 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 141.236 64.517  239.812 1.00 59.30 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 139.776 63.716  241.675 1.00 60.44 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 144.255 61.227  243.333 1.00 60.05 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 144.831 59.904  243.549 1.00 60.99 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 144.494 59.340  244.924 1.00 61.82 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 144.626 58.129  245.131 1.00 60.85 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 146.349 59.952  243.370 1.00 59.46 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 146.802 60.084  241.926 1.00 59.79 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 148.215 60.636  241.844 1.00 60.39 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 148.502 61.219  240.470 1.00 60.02 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 149.815 61.921  240.434 1.00 58.40 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 144.067 60.180  245.861 1.00 61.82 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 143.701 59.724  247.197 1.00 59.63 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 142.462 58.835  247.160 1.00 57.93 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 141.698 58.848  246.193 0.00 58.52 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 143.461 60.916  248.125 1.00 59.74 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 144.728 61.639  248.554 1.00 59.49 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 144.402 62.932  249.282 1.00 60.30 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 145.664 63.691  249.657 1.00 59.76 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 145.366 65.082  250.095 1.00 58.58 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 134.641 65.528  245.062 1.00 65.42 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 133.800 66.712  245.190 1.00 66.76 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 134.649 67.976  245.251 1.00 68.27 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 134.635 68.788  244.325 1.00 66.28 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 132.913 66.605  246.432 1.00 65.09 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 132.142 65.299  246.525 1.00 65.29 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 131.272 65.222  247.762 1.00 66.24 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 131.258 66.198  248.542 1.00 65.94 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 130.603 64.186  247.957 1.00 66.62 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 135.388 68.142  246.352 1.00 70.40 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 136.312 69.265  246.460 1.00 69.82 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 137.436 69.157  245.438 1.00 70.13 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 137.900 70.178  244.912 1.00 69.00 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 136.876 69.339  247.879 1.00 69.98 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 137.874 70.465  248.104 1.00 70.05 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 138.328 70.557  249.548 1.00 69.87 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 138.031 69.625  250.326 1.00 69.26 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 138.979 71.561  249.906 1.00 68.68 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 137.884 67.936  245.143 1.00 66.23 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 138.913 67.754  244.128 1.00 66.59 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 138.391 68.111  242.742 1.00 65.93 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 139.159 68.560  241.883 1.00 63.99 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 139.424 66.314  244.170 1.00 66.53 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 139.710 65.828  245.575 1.00 66.93 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 140.703 66.414  246.344 1.00 67.01 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 138.987 64.780  246.130 1.00 66.27 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 140.968 65.975  247.628 1.00 67.23 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 139.244 64.332  247.412 1.00 66.72 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 140.237 64.933  248.157 1.00 67.89 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 140.498 64.493  249.434 1.00 66.13 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 137.088 67.932  242.512 1.00 60.01 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 136.481 68.439  241.286 1.00 59.70 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 136.563 69.960  241.225 1.00 59.86 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 136.799 70.532  240.156 1.00 56.98 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 135.030 67.971  241.183 1.00 57.65 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 136.372 70.631  242.362 1.00 60.93 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 136.555 72.080  242.404 1.00 60.88 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 138.006 72.437  242.104 1.00 60.40 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 138.290 73.441  241.436 1.00 57.95 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 136.102 72.638  243.767 1.00 59.35 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 136.114 74.159  243.752 1.00 56.96 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 134.719 72.111  244.121 1.00 57.89 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 138.945 71.623  242.591 1.00 61.16 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 140.356 71.862  242.302 1.00 61.16 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 140.645 71.751  240.809 1.00 61.29 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 141.339 72.600  240.236 1.00 59.58 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 141.227 70.883  243.090 1.00 61.20 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 141.847 71.396  244.392 1.00 62.54 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 140.773 71.659  245.435 1.00 60.07 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 142.882 70.414  244.918 1.00 59.93 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 140.115 70.716  240.154 1.00 58.46 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 140.363 70.581  238.719 1.00 59.46 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 139.635 71.676  237.939 1.00 59.07 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 140.126 72.134  236.898 1.00 56.57 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 139.998 69.169  238.217 1.00 58.23 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 138.484 68.966  238.144 1.00 57.47 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 140.645 68.106  239.092 1.00 56.64 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 138.074 67.668  237.483 1.00 56.01 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 138.479 72.133  238.427 1.00 57.39 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 137.779 73.227  237.757 1.00 58.16 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 138.566 74.530  237.843 1.00 58.35 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 138.672 75.266  236.852 1.00 55.95 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 136.383 73.403  238.355 1.00 57.11 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 136.454 73.885  239.684 1.00 58.41 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 139.125 74.837  239.016 1.00 61.10 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 139.947 76.040  239.121 1.00 61.16 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 141.239 75.893  238.328 1.00 63.46 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 141.752 76.884  237.795 1.00 60.77 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 140.230 76.377  240.588 1.00 60.59 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 141.146 75.414  241.319 1.00 61.65 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 141.294 75.747  242.790 1.00 63.93 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 140.654 76.716  243.249 1.00 63.03 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 142.053 75.043  243.488 1.00 61.82 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 141.763 74.669  238.211 1.00 61.90 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 142.895 74.437  237.321 1.00 61.66 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 142.531 74.752  235.873 1.00 59.82 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 143.320 75.362  235.145 1.00 57.09 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 143.383 72.995  237.453 1.00 58.03 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 141.337 74.341  235.440 1.00 58.97 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 140.884 74.663  234.088 1.00 59.76 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 140.719 76.169  233.902 1.00 59.58 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 141.034 76.715  232.834 1.00 57.76 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 139.570 73.938  233.796 1.00 59.08 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 139.142 73.972  232.340 1.00 59.21 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 137.919 73.116  232.076 1.00 60.23 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 137.915 71.918  232.354 1.00 60.35 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 136.872 73.730  231.537 1.00 59.01 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 140.207 76.854  234.926 1.00 57.92 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 140.090 78.309  234.859 1.00 58.66 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 141.458 78.966  234.704 1.00 59.05 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 141.622 79.909  233.917 1.00 55.81 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 139.375 78.839  236.102 1.00 55.26 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 142.455 78.479  235.450 1.00 60.28 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 143.812 78.997  235.299 1.00 61.44 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 144.359 78.676  233.915 1.00 60.55 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 145.110 79.472  233.340 1.00 59.82 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 144.726 78.456  236.416 1.00 60.98 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 144.173 78.832  237.790 1.00 60.18 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 146.131 79.011  236.272 1.00 59.26 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 143.966 80.319  237.979 1.00 58.69 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 144.004 77.515  233.360 1.00 55.87 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 144.382 77.196  231.985 1.00 56.42 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 143.862 78.256  231.022 1.00 55.90 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 144.603 78.762  230.168 1.00 53.19 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 143.836 75.823  231.584 1.00 56.18 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 144.489 74.633  232.254 1.00 56.96 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 143.684 73.365  232.017 1.00 56.07 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 144.299 72.175  232.733 1.00 55.97 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 144.335 72.378  234.207 1.00 54.98 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 142.576 78.593  231.143 1.00 56.10 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 141.983 79.589  230.255 1.00 57.16 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 142.644 80.951  230.429 1.00 56.67 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 142.934 81.646  229.444 1.00 52.92 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 140.478 79.686  230.508 1.00 53.76 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 142.894 81.349  231.681 1.00 59.94 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 143.537 82.636  231.931 1.00 60.79 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 144.944 82.677  231.343 1.00 60.21 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 145.348 83.682  230.744 1.00 58.07 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 143.568 82.920  233.432 1.00 59.25 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 143.846 84.378  233.745 1.00 60.80 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 143.875 85.197  232.802 1.00 60.11 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 144.038 84.706  234.935 1.00 61.00 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 145.703 81.589  231.497 1.00 59.88 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 147.053 81.530  230.945 1.00 61.03 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 147.028 81.589  229.424 1.00 59.43 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 147.878 82.244  228.806 1.00 57.67 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 147.756 80.260  231.425 1.00 60.73 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 149.183 80.018  230.929 1.00 61.45 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 150.140 81.015  231.554 1.00 59.39 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 149.624 78.595  231.226 1.00 59.08 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 146.066 80.903  228.801 1.00 53.58 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 145.946 80.964  227.346 1.00 54.10 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 145.643 82.380  226.875 1.00 54.62 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 146.234 82.862  225.900 1.00 51.87 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 144.868 79.994  226.867 1.00 52.22 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 144.726 83.069  227.564 1.00 53.29 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 144.420 84.449  227.198 1.00 52.81 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 145.641 85.349  227.364 1.00 53.80 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 145.913 86.210  226.514 1.00 50.77 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 143.251 84.967  228.033 1.00 49.03 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 146.392 85.156  228.451 1.00 56.83 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 147.579 85.970  228.693 1.00 56.36 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 148.617 85.743  227.598 1.00 56.23 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 149.229 86.695  227.099 1.00 55.99 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 148.153 85.675  230.092 1.00 56.10 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 149.562 86.230  230.224 1.00 56.33 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 147.249 86.260  231.166 1.00 54.71 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 148.827 84.484  227.205 1.00 55.28 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 149.808 84.200  226.161 1.00 56.45 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 149.362 84.760  224.812 1.00 56.31 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 150.192 85.236  224.026 1.00 53.61 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 150.079 82.694  226.082 1.00 55.80 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 149.181 81.906  225.140 1.00 55.98 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 149.573 80.444  225.048 1.00 57.27 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 150.728 80.161  224.667 1.00 55.93 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 148.727 79.578  225.359 1.00 56.66 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 148.055 84.730  224.530 1.00 53.90 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 147.562 85.337  223.297 1.00 55.19 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 147.812 86.841  223.288 1.00 56.32 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 148.249 87.404  222.276 1.00 52.95 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 146.074 85.037  223.120 1.00 53.11 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 147.547 87.504  224.418 1.00 56.85 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 147.809 88.939  224.507 1.00 54.93 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 149.295 89.236  224.351 1.00 54.57 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 149.678 90.219  223.705 1.00 54.64 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 147.282 89.488  225.832 1.00 53.61 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 147.572 90.964  226.054 1.00 55.23 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 146.913 91.472  227.328 1.00 56.22 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 145.405 91.575  227.162 1.00 55.26 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 144.763 92.255  228.321 1.00 53.35 ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 150.149 88.393  224.936 1.00 51.25 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 151.593 88.582  224.817 1.00 52.03 ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 152.032 88.466  223.363 1.00 51.89 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 152.839 89.268  222.875 1.00 50.39 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 152.338 87.576  225.718 1.00 52.28 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 153.792 87.448  225.292 1.00 50.81 ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 152.242 87.999  227.175 1.00 52.79 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 151.516 87.462  222.649 1.00 53.64 ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 151.868 87.303  221.240 1.00 54.75 ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 151.396 88.494  220.412 1.00 54.47 ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 152.129 88.986  219.542 1.00 51.03 ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 151.282 86.000  220.695 1.00 52.50 ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 151.910 84.773  221.325 1.00 53.66 ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 152.798 84.880  222.170 1.00 53.65 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 151.449 83.597  220.914 1.00 53.24 ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 150.176 88.975  220.670 1.00 55.06 ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 149.680 90.139  219.941 1.00 54.43 ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 150.545 91.367  220.206 1.00 54.48 ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 150.845 92.141  219.288 1.00 53.30 ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 148.225 90.415  220.318 1.00 53.40 ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 147.687 91.736  219.792 1.00 53.01 ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 146.289 92.018  220.317 1.00 55.14 ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 146.197 91.840  221.761 1.00 57.97 ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 145.099 92.050  222.473 1.00 56.73 ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 143.972 92.445  221.906 1.00 54.27 ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 145.133 91.858  223.789 1.00 55.00 ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 150.962 91.555  221.459 1.00 52.59 ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 151.803 92.698  221.797 1.00 51.90 ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 153.181 92.592  221.151 1.00 51.19 ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 153.751 93.602  220.720 1.00 49.13 ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 151.921 92.810  223.314 1.00 51.60 ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 150.640 92.856  223.917 1.00 53.40 ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 153.736 91.381  221.084 1.00 48.72 ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 155.008 91.193  220.392 1.00 49.65 ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 154.872 91.511  218.907 1.00 49.79 ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 155.777 92.102  218.301 1.00 47.24 ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 155.516 89.764  220.591 1.00 49.48 ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 155.387 89.399  221.971 1.00 48.77 ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 156.976 89.655  220.180 1.00 47.65 ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 153.746 91.119  218.303 1.00 51.93 ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 153.483 91.495  216.918 1.00 53.49 ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 153.415 93.010  216.766 1.00 51.80 ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 153.947 93.574  215.802 1.00 49.85 ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 152.191 90.845  216.430 1.00 50.31 ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 152.767 93.686  217.717 1.00 50.33 ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 152.716 95.146  217.686 1.00 49.31 ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 154.114 95.749  217.737 1.00 50.92 ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 154.423 96.688  216.994 1.00 50.04 ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 151.880 95.666  218.853 1.00 48.46 ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 150.360 95.649  218.713 1.00 52.02 ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 149.727 95.846  220.077 1.00 50.04 ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 149.897 96.722  217.743 1.00 50.13 ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 154.970 95.228  218.619 1.00 54.55 ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 156.323 95.761  218.746 1.00 54.89 ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 157.122 95.560  217.465 1.00 53.93 ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 157.808 96.478  216.994 1.00 51.94 ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 157.045 95.110  219.926 1.00 53.57 ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 156.619 95.515  221.333 1.00 54.91 ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 157.692 95.088  222.313 1.00 53.02 ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 156.370 97.011  221.419 1.00 52.82 ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 157.068 94.353  216.897 1.00 53.45 ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 157.812 94.109  215.667 1.00 54.24 ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 157.250 94.903  214.497 1.00 55.35 ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 157.983 95.178  213.540 1.00 54.23 ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 157.845 92.611  215.343 1.00 52.75 ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 156.495 91.964  215.074 1.00 53.95 ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 156.154 91.922  213.590 1.00 53.66 ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 154.839 91.198  213.352 1.00 53.43 ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 154.472 91.173  211.910 1.00 54.85 ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 155.969 95.279  214.548 1.00 52.91 ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 155.411 96.132  213.506 1.00 52.22 ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 155.830 97.589  213.677 1.00 54.03 ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 156.043 98.296  212.686 1.00 53.13 ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 153.888 96.011  213.498 1.00 52.10 ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 153.332 96.635  212.355 1.00 54.11 ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 155.953 98.057  214.920 1.00 55.36 ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 156.244 99.462  215.196 1.00 54.24 ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 157.730 99.752  215.396 1.00 54.73 ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 158.082 100.903 215.682 1.00 53.84 ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 155.466 99.926  216.430 1.00 51.87 ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 153.939 99.898  216.333 1.00 53.88 ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 153.315 100.692 217.469 1.00 52.27 ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 153.475 100.431 214.986 1.00 53.25 ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 158.596 98.741  215.281 1.00 55.12 ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 160.027 98.966  215.478 1.00 55.49 ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 160.590 99.998  214.502 1.00 55.32 ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 161.393 100.855 214.892 1.00 54.77 ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 160.785 97.646  215.345 1.00 54.44 ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 162.172 97.868  215.171 1.00 54.32 ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 160.203 99.920  213.225 1.00 54.55 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 160.737 100.855 212.237 1.00 55.68 ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 160.306 102.287 212.535 1.00 56.83 ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 161.111 103.222 212.431 1.00 54.19 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 160.293 100.443 210.833 1.00 52.71 ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 159.035 102.475 212.901 1.00 59.56 ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 158.565 103.802 213.276 1.00 58.72 ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 159.305 104.313 214.505 1.00 59.88 ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 159.656 105.497 214.578 1.00 61.88 ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 157.057 103.776 213.529 1.00 59.35 ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 156.207 103.864 212.270 1.00 61.29 ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 156.157 102.557 211.498 1.00 62.10 ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 156.614 101.526 212.033 1.00 61.47 ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 155.656 102.563 210.354 1.00 58.97 ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 159.555 103.433 215.477 1.00 59.78 ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 160.315 103.836 216.657 1.00 60.15 ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 161.717 104.296 216.281 1.00 59.95 ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 162.199 105.317 216.786 1.00 60.44 ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 160.378 102.682 217.657 1.00 59.35 ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 161.163 102.997 218.920 1.00 60.19 ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 161.131 101.832 219.900 1.00 60.79 ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 161.397 100.553 219.251 1.00 62.96 ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 162.600 100.127 218.894 1.00 61.02 ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 163.684 100.854 219.110 1.00 60.77 ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 162.720 98.941  218.304 1.00 58.80 ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 162.384 103.559 215.391 1.00 60.87 ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 163.734 103.936 214.977 1.00 61.92 ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 163.736 105.283 214.262 1.00 60.97 ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 164.577 106.152 214.543 1.00 60.86 ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 164.330 102.851 214.080 1.00 61.62 ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 164.565 101.518 214.775 1.00 62.00 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 165.354 101.657 216.060 1.00 62.55 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 166.383 102.365 216.057 1.00 63.08 ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 164.946 101.056 217.075 1.00 61.23 ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 162.799 105.475 213.331 1.00 60.64 ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 162.738 106.737 212.599 1.00 61.21 ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 162.452 107.904 213.537 1.00 60.23 ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 163.060 108.976 213.415 1.00 58.33 ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 161.678 106.659 211.499 1.00 59.58 ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 161.349 108.002 210.866 1.00 58.65 ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 160.055 107.951 210.069 1.00 60.62 ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 160.022 106.823 209.144 1.00 62.18 ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 159.051 105.921 209.096 1.00 60.98 ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 158.007 105.985 209.906 1.00 58.93 ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 159.129 104.933 208.210 1.00 58.92 ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 161.535 107.712 214.485 1.00 56.79 ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 161.205 108.777 215.424 1.00 56.24 ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 162.377 109.086 216.344 1.00 57.66 ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 162.604 110.249 216.692 1.00 58.76 ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 159.963 108.398 216.224 1.00 55.26 ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 158.728 108.363 215.382 1.00 56.03 ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 158.625 108.719 214.069 1.00 56.69 ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 157.423 107.943 215.788 1.00 57.32 ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 157.335 108.551 213.633 1.00 58.26 ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 156.576 108.074 214.670 1.00 58.99 ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 156.885 107.469 216.989 1.00 57.52 ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 155.224 107.751 214.716 1.00 58.82 ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 155.544 107.150 217.032 1.00 57.78 ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 154.729 107.293 215.904 1.00 57.95 ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 163.135 108.062 216.748 1.00 60.04 ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 164.334 108.308 217.541 1.00 60.52 ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 165.348 109.136 216.761 1.00 59.77 ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 165.928 110.091 217.296 1.00 59.67 ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 164.954 106.983 217.984 1.00 60.35 ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 164.300 106.365 219.208 1.00 60.90 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 164.266 104.850 219.150 1.00 63.04 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 164.620 104.286 218.092 1.00 61.21 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 163.885 104.223 220.160 1.00 60.97 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 165.563 108.796 215.486 1.00 54.69 ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 166.503 109.563 214.674 1.00 54.74 ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 166.049 111.010 214.518 1.00 55.56 ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 166.859 111.944 214.624 1.00 53.54 ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 166.675 108.907 213.303 1.00 54.38 ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 167.244 107.499 213.344 1.00 56.34 ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 168.538 107.442 214.135 1.00 55.47 ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 169.055 106.015 214.242 1.00 54.48 ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 168.052 105.107 214.862 1.00 55.01 ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 164.755 111.221 214.265 1.00 54.15 ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 164.250 112.580 214.097 1.00 52.36 ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 164.339 113.372 215.396 1.00 49.34 ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 164.689 114.558 215.384 1.00 49.51 ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 162.814 112.552 213.577 1.00 52.86 ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 162.704 111.586 212.524 1.00 51.21 ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 162.421 113.920 213.039 1.00 49.79 ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 164.022 112.741 216.530 1.00 45.78 ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 164.147 113.423 217.813 1.00 47.66 ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 165.599 113.748 218.135 1.00 49.04 ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 165.872 114.735 218.827 1.00 48.78 ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 163.533 112.570 218.923 1.00 48.52 ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 163.690 113.191 220.187 1.00 48.19 ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 166.540 112.931 217.653 1.00 48.62 ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 167.951 113.259 217.833 1.00 49.38 ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 168.353 114.456 216.978 1.00 50.16 ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 169.063 115.351 217.451 1.00 49.62 ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 168.816 112.043 217.506 1.00 49.41 ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 170.266 112.163 217.956 1.00 48.85 ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 171.177 112.712 216.873 1.00 48.54 ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 170.716 112.855 215.721 1.00 47.61 ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 172.354 112.999 217.174 1.00 47.41 ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 167.914 114.488 215.720 1.00 51.26 ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 168.249 115.593 214.823 1.00 52.67 ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 167.441 116.864 215.099 1.00 52.08 ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 167.709 117.901 214.474 1.00 51.82 ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 168.066 115.150 213.368 1.00 50.60 ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 166.686 114.849 213.123 1.00 50.04 ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 168.911 113.918 213.073 1.00 49.18 ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 166.447 116.784 215.990 1.00 50.84 ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 165.654 117.943 216.395 1.00 49.83 ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 166.525 119.123 216.822 1.00 50.82 ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 166.264 120.277 216.449 1.00 51.16 ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 164.719 117.511 217.529 1.00 48.20 ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 164.307 118.617 218.459 1.00 48.82 ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 163.418 119.592 218.053 1.00 50.10 ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 164.807 118.668 219.750 1.00 48.94 ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 163.032 120.592 218.920 1.00 51.00 ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 164.432 119.674 220.618 1.00 49.23 ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 163.545 120.639 220.202 1.00 50.40 ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 167.563 118.853 217.617 1.00 49.67 ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 168.453 119.925 218.054 1.00 50.81 ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 169.176 120.559 216.872 1.00 51.18 ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 169.377 121.778 216.840 1.00 49.95 ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 169.455 119.397 219.080 1.00 51.97 ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 168.820 118.851 220.347 1.00 53.17 ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 169.867 118.621 221.425 1.00 51.75 ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 170.188 119.911 222.168 1.00 52.82 ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 169.044 120.388 222.992 1.00 51.14 ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 169.574 119.747 215.890 1.00 47.72 ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 170.237 120.291 214.710 1.00 47.15 ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 169.298 121.194 213.918 1.00 44.42 ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 169.704 122.262 213.438 1.00 45.04 ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 170.761 119.154 213.834 1.00 49.74 ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 171.751 119.630 212.791 1.00 49.80 ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 171.406 119.799 211.622 1.00 49.13 ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 172.991 119.851 213.211 1.00 45.30 ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 168.035 120.783 213.767 1.00 42.24 ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 167.080 121.655 213.083 1.00 44.75 ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 166.888 122.970 213.832 1.00 44.18 ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 166.860 124.042 213.214 1.00 42.23 ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 165.731 120.965 212.853 1.00 43.32 ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 165.752 119.812 211.860 1.00 43.67 ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 165.700 118.452 212.500 1.00 46.52 ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 164.856 118.180 213.352 1.00 44.58 ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 166.593 117.573 212.072 1.00 45.39 ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 166.748 122.916 215.162 1.00 43.63 ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 166.636 124.168 215.910 1.00 41.93 ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 167.882 125.031 215.772 1.00 41.39 ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 167.780 126.263 215.748 1.00 42.67 ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 166.329 123.916 217.385 1.00 40.61 ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 165.724 125.152 218.062 1.00 41.83 ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 163.948 125.424 217.942 1.00 49.82 ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 163.312 123.820 218.368 1.00 45.04 ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 169.061 124.416 215.686 1.00 38.65 ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 170.273 125.196 215.464 1.00 39.82 ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 170.261 125.880 214.102 1.00 39.94 ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 170.708 127.025 213.980 1.00 41.73 ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 171.506 124.303 215.597 1.00 41.79 ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 171.597 123.398 214.512 1.00 44.69 ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 169.759 125.199 213.071 1.00 35.86 ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 169.839 125.713 211.707 1.00 34.70 ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 168.649 126.571 211.282 1.00 32.16 ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 168.670 127.103 210.160 1.00 32.42 ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 169.993 124.551 210.715 1.00 35.90 ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 169.043 123.526 211.024 1.00 37.98 ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 171.397 123.974 210.787 1.00 31.29 ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 167.615 126.700 212.124 1.00 29.35 ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 166.449 127.507 211.747 1.00 27.71 ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 166.852 128.924 211.360 1.00 26.35 ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 166.337 129.478 210.385 1.00 27.59 ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 165.386 127.529 212.866 1.00 27.15 ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 164.817 126.140 213.131 1.00 31.11 ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 164.261 128.488 212.521 1.00 24.12 ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 163.971 126.067 214.377 1.00 32.40 ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 167.749 129.547 212.128 1.00 25.22 ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 168.061 130.956 211.891 1.00 20.57 ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 168.615 131.176 210.489 1.00 20.69 ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 168.097 131.998 209.721 1.00 21.55 ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 169.046 131.458 212.947 1.00 20.80 ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 169.653 130.422 210.123 1.00 19.14 ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 170.231 130.566 208.798 1.00 17.98 ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 169.280 130.154 207.691 1.00 19.72 ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 169.202 130.815 206.649 1.00 20.97 ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 168.543 129.055 207.896 1.00 16.03 ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 167.626 128.597 206.859 1.00 15.03 ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 166.539 129.628 206.590 1.00 17.04 ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 166.213 129.915 205.432 1.00 18.91 ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 167.010 127.259 207.262 1.00 22.21 ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 168.024 126.138 207.288 1.00 27.73 ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 169.069 126.267 206.618 1.00 27.81 ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 167.779 125.128 207.980 1.00 22.74 ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 165.976 130.209 207.651 1.00 14.54 ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 164.931 131.210 207.487 1.00 12.20 ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 165.485 132.498 206.899 1.00 10.72 ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 164.799 133.165 206.118 1.00 13.93 ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 164.244 131.475 208.825 1.00 15.94 ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 163.263 130.086 209.431 1.00 30.54 ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 166.719 132.866 207.250 1.00 9.61  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 167.325 134.040 206.629 1.00 8.19  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 167.449 133.846 205.122 1.00 10.81 ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 167.064 134.722 204.335 1.00 14.42 ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 168.691 134.320 207.263 1.00 9.18  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 169.439 135.613 206.916 1.00 8.96  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 170.341 136.002 208.070 1.00 11.76 ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 170.261 135.480 205.645 1.00 13.27 ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 167.961 132.685 204.701 1.00 13.85 ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 168.087 132.409 203.272 1.00 10.06 ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 166.730 132.388 202.581 1.00 10.89 ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 166.568 132.962 201.498 1.00 13.65 ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 168.814 131.087 203.051 1.00 11.03 ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 170.287 131.054 203.441 1.00 9.65  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 170.907 129.726 203.070 1.00 13.83 ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 170.996 132.180 202.725 1.00 8.51  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 165.743 131.728 203.192 1.00 5.20  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 164.429 131.628 202.568 1.00 3.66  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 163.769 132.995 202.440 1.00 7.43  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 163.177 133.310 201.401 1.00 10.40 ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 163.548 130.676 203.371 1.00 11.19 ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 164.206 129.442 203.582 1.00 14.83 ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 163.857 133.819 203.486 1.00 9.62  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 163.280 135.155 203.437 1.00 5.73  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 163.958 136.014 202.385 1.00 5.93  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 163.288 136.746 201.644 1.00 8.46  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 163.386 135.817 204.805 1.00 5.19  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 165.291 135.950 202.306 1.00 3.71  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 165.994 136.708 201.279 1.00 0.79  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 165.562 136.268 199.889 1.00 5.18  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 165.323 137.104 199.010 1.00 13.02 ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 167.503 136.552 201.452 1.00 5.40  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 165.437 134.956 199.677 1.00 5.97  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 165.031 134.456 198.369 1.00 6.05  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 163.623 134.910 198.009 1.00 5.78  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 163.371 135.326 196.872 1.00 9.67  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 165.128 132.933 198.334 1.00 7.48  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 165.038 132.358 196.954 1.00 7.31  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 166.151 132.329 196.133 1.00 9.56  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 163.843 131.859 196.473 1.00 4.07  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 166.072 131.808 194.861 1.00 11.04 ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 163.759 131.335 195.202 1.00 9.55  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 164.876 131.311 194.395 1.00 13.44 ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 162.688 134.836 198.959 1.00 2.98  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 161.316 135.245 198.672 1.00 1.25  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 161.248 136.738 198.380 1.00 7.17  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 160.594 137.167 197.422 1.00 10.96 ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 160.377 134.863 199.828 1.00 1.52  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 160.355 133.352 200.037 1.00 4.94  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 158.972 135.363 199.559 1.00 4.58  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 159.645 132.947 201.301 1.00 7.88  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 161.920 137.554 199.192 1.00 8.97  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 161.772 138.999 199.073 1.00 0.84  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 162.536 139.578 197.891 1.00 4.78  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 162.125 140.608 197.346 1.00 8.63  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 162.227 139.679 200.361 1.00 1.30  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 163.636 138.949 197.479 1.00 3.39  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 164.542 139.556 196.511 1.00 0.49  ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 164.576 138.843 195.167 1.00 4.88  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 164.498 139.495 194.122 1.00 7.54  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 165.956 139.604 197.099 1.00 2.38  ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 166.134 140.616 198.204 1.00 4.21  ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 166.036 141.976 197.950 1.00 3.63  ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 166.408 140.211 199.501 1.00 6.00  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 166.208 142.900 198.954 1.00 0.82  ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 166.577 141.131 200.511 1.00 8.03  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 166.475 142.472 200.233 1.00 6.04  ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 166.646 143.391 201.238 1.00 12.97 ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 164.692 137.518 195.162 1.00 6.04  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 165.008 136.768 193.953 1.00 4.14  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 163.809 136.547 193.038 1.00 3.58  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 163.894 135.706 192.138 1.00 12.91 ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 165.623 135.418 194.324 1.00 6.11  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 162.707 137.266 193.239 1.00 6.44  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 161.527 137.030 192.421 1.00 4.77  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 161.712 137.411 190.964 1.00 1.30  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 161.294 136.677 190.065 1.00 2.28  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 162.332 138.565 190.707 1.00 2.36  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 162.415 139.080 189.345 1.00 2.26  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 163.464 138.363 188.503 1.00 6.45  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 163.326 138.295 187.278 1.00 7.65  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 162.717 140.579 189.370 1.00 3.62  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 162.910 141.179 187.999 1.00 4.74  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 161.854 141.260 187.102 1.00 9.45  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 164.150 141.655 187.596 1.00 6.71  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 162.026 141.802 185.846 1.00 10.24 ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 164.331 142.201 186.341 1.00 10.32 ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 163.265 142.272 185.470 1.00 11.57 ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 163.437 142.813 184.219 1.00 15.67 ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 164.505 137.827 189.128 1.00 8.30  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 165.634 137.297 188.383 1.00 4.30  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 165.324 135.916 187.814 1.00 6.52  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 164.378 135.238 188.224 1.00 9.96  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 166.870 137.237 189.277 1.00 4.92  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 167.216 138.551 189.907 1.00 8.39  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 167.816 139.553 189.165 1.00 7.11  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 166.922 138.795 191.236 1.00 5.97  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 168.130 140.764 189.739 1.00 6.38  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 167.233 140.007 191.815 1.00 7.53  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 167.838 140.992 191.066 1.00 7.92  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 166.137 135.507 186.844 1.00 7.16  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 166.008 134.192 186.238 1.00 5.67  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 166.706 133.147 187.104 1.00 8.67  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 167.196 133.434 188.198 1.00 16.52 ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 166.566 134.200 184.817 1.00 5.96  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 167.928 134.853 184.727 1.00 12.62 ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 168.456 135.277 185.774 1.00 13.76 ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 168.473 134.942 183.607 1.00 12.95 ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 166.757 131.912 186.602 1.00 8.34  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 167.274 130.803 187.396 1.00 8.54  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 168.740 131.011 187.760 1.00 9.42  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 169.142 130.808 188.913 1.00 8.35  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 167.088 129.493 186.630 1.00 6.76  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 167.747 128.290 187.273 1.00 8.95  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 167.463 127.008 186.522 1.00 12.49 ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 167.336 127.008 185.298 1.00 14.07 ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 167.360 125.904 187.252 1.00 14.26 ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 169.556 131.425 186.786 1.00 8.35  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 170.987 131.566 187.030 1.00 9.36  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 171.277 132.663 188.047 1.00 10.53 ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 172.104 132.478 188.947 1.00 13.72 ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 171.716 131.842 185.715 1.00 12.02 ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 173.224 131.673 185.798 1.00 14.53 ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 173.969 132.651 184.912 1.00 18.60 ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 173.996 133.852 185.177 1.00 16.00 ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 174.580 132.138 183.850 1.00 16.98 ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 170.603 133.809 187.929 1.00 9.29  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 170.845 134.894 188.875 1.00 7.74  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 170.293 134.570 190.257 1.00 6.67  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 170.891 134.959 191.266 1.00 11.23 ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 170.252 136.198 188.349 1.00 6.80  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 170.689 137.422 189.131 1.00 11.79 ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 172.482 137.577 189.220 1.00 28.42 ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 172.822 138.491 187.721 1.00 16.56 ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 169.165 133.860 190.326 1.00 8.10  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 168.666 133.397 191.616 1.00 5.12  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 169.677 132.479 192.290 1.00 9.88  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 169.940 132.603 193.492 1.00 15.26 ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 167.332 132.671 191.438 1.00 5.40  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 166.153 133.570 191.133 1.00 4.91  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 164.868 132.766 191.042 1.00 0.76  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 163.827 133.485 190.319 1.00 3.68  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 162.543 133.159 190.333 1.00 3.66  ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 162.100 132.126 191.029 1.00 3.87  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 161.681 133.889 189.633 1.00 3.39  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 170.256 131.551 191.523 1.00 11.32 ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 171.261 130.656 192.085 1.00 8.37  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 172.502 131.422 192.521 1.00 9.52  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 173.090 131.118 193.564 1.00 15.33 ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 171.627 129.570 191.076 1.00 8.40  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 172.445 128.438 191.671 1.00 10.99 ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 171.906 127.979 193.012 1.00 13.83 ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 170.752 127.564 193.122 1.00 13.77 ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 172.742 128.052 194.040 1.00 12.94 ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 172.919 132.417 191.733 1.00 7.24  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 174.072 133.227 192.116 1.00 6.28  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 173.819 133.965 193.424 1.00 9.54  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 174.682 133.992 194.311 1.00 15.78 ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 174.411 134.223 191.006 1.00 7.09  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 174.933 133.548 189.757 1.00 15.82 ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 175.093 132.328 189.718 1.00 19.92 ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 175.204 134.340 188.729 1.00 14.58 ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 172.636 134.566 193.564 1.00 8.05  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 172.301 135.281 194.790 1.00 3.97  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 172.269 134.339 195.987 1.00 5.54  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 172.803 134.660 197.057 1.00 15.59 ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 170.956 135.985 194.630 1.00 8.45  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 170.933 137.238 193.756 1.00 7.93  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 169.502 137.635 193.459 1.00 5.06  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 171.678 138.375 194.432 1.00 9.05  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 171.645 133.169 195.826 1.00 3.58  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 171.576 132.222 196.932 1.00 7.76  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 172.961 131.719 197.316 1.00 12.16 ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 173.261 131.553 198.502 1.00 15.59 ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 170.659 131.054 196.573 1.00 9.43  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 170.037 130.388 197.764 1.00 8.43  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 168.938 130.948 198.392 1.00 12.54 ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 170.555 129.206 198.263 1.00 8.71  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 168.365 130.342 199.489 1.00 11.67 ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 169.986 128.593 199.361 1.00 11.79 ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 168.889 129.163 199.975 1.00 12.00 ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 173.820 131.473 196.324 1.00 10.11 ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 175.181 131.037 196.610 1.00 9.41  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 175.961 132.118 197.345 1.00 13.67 ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 176.720 131.821 198.274 1.00 14.65 ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 175.888 130.647 195.311 1.00 12.49 ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 175.212 129.533 194.717 1.00 13.00 ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 177.334 130.265 195.579 1.00 16.49 ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 175.786 133.381 196.949 1.00 11.14 ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 176.460 134.474 197.645 1.00 7.53  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 176.005 134.566 199.097 1.00 10.58 ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 176.826 134.710 200.013 1.00 20.49 ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 176.207 135.793 196.916 1.00 5.08  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 176.598 135.667 195.544 1.00 10.13 ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 177.000 136.917 197.561 1.00 5.46  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 174.692 134.477 199.328 1.00 8.92  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 174.183 134.534 200.696 1.00 9.78  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 174.690 133.358 201.525 1.00 13.45 ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 175.061 133.523 202.695 1.00 15.93 ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 172.655 134.558 200.698 1.00 10.18 ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 172.039 135.616 199.840 1.00 10.01 ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 172.580 136.819 199.499 1.00 6.84  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 170.753 135.561 199.214 1.00 8.27  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 171.710 137.516 198.696 1.00 3.12  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 170.581 136.764 198.507 1.00 5.19  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 169.731 134.609 199.182 1.00 6.47  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 169.431 137.042 197.777 1.00 5.74  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 168.591 134.887 198.456 1.00 6.33  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 168.449 136.092 197.764 1.00 8.35  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 174.706 132.160 200.936 1.00 14.45 ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 175.189 130.984 201.650 1.00 14.62 ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 176.668 131.109 201.981 1.00 16.70 ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 177.100 130.722 203.073 1.00 19.51 ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 174.926 129.725 200.826 1.00 16.36 ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 173.543 129.566 200.567 1.00 17.20 ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 177.462 131.639 201.049 1.00 11.70 ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 178.878 131.855 201.321 1.00 14.21 ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 179.072 132.849 202.455 1.00 16.66 ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 179.932 132.651 203.322 1.00 22.00 ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 179.589 132.345 200.058 1.00 14.79 ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 179.898 131.256 199.078 1.00 21.79 ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 180.304 131.513 197.786 1.00 20.85 ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 179.860 129.908 199.200 1.00 20.33 ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 180.504 130.371 197.155 1.00 20.61 ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 180.241 129.381 197.990 1.00 20.18 ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 178.281 133.923 202.468 1.00 16.46 ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 178.392 134.890 203.556 1.00 15.46 ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 178.033 134.265 204.897 1.00 18.87 ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 178.718 134.497 205.899 1.00 25.83 ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 177.510 136.104 203.286 1.00 12.83 ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 177.697 137.211 204.277 1.00 16.62 ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 177.009 137.265 205.470 1.00 17.07 ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 178.502 138.300 204.257 1.00 15.78 ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 177.377 138.345 206.139 1.00 15.05 ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 178.281 138.988 205.424 1.00 18.00 ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 176.959 133.472 204.944 1.00 17.76 ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 176.577 132.855 206.212 1.00 18.96 ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 177.606 131.825 206.662 1.00 24.46 ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 177.863 131.685 207.864 1.00 26.91 ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 175.194 132.218 206.115 1.00 18.81 ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 174.005 133.153 205.911 1.00 17.43 ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 172.752 132.336 205.735 1.00 18.77 ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 173.858 134.115 207.070 1.00 21.10 ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 178.190 131.080 205.720 1.00 24.48 ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 179.250 130.143 206.075 1.00 24.71 ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 180.460 130.875 206.637 1.00 25.56 ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 181.054 130.440 207.631 1.00 28.40 ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 179.651 129.313 204.856 1.00 24.29 ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 178.818 128.062 204.647 1.00 26.30 ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 179.148 127.352 203.349 1.00 28.47 ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 180.123 127.687 202.677 1.00 28.01 ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 178.334 126.366 202.991 1.00 27.53 ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 180.838 131.992 206.015 1.00 23.86 ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 181.981 132.760 206.484 1.00 26.66 ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 181.702 133.440 207.822 1.00 28.92 ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 182.645 133.726 208.568 1.00 34.15 ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 182.377 133.780 205.410 1.00 25.59 ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 183.325 134.877 205.855 1.00 31.44 ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 183.710 135.805 204.721 1.00 34.60 ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 182.884 136.564 204.218 1.00 33.15 ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 184.972 135.749 204.313 1.00 34.51 ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 180.433 133.664 208.157 1.00 27.16 ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 180.047 134.328 209.395 1.00 28.44 ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 179.696 133.349 210.510 1.00 27.97 ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 179.158 133.769 211.538 1.00 27.90 ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 178.869 135.271 209.142 1.00 27.01 ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 179.987 132.060 210.326 1.00 28.81 ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 179.731 131.031 211.339 1.00 31.29 ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 178.257 130.982 211.735 1.00 30.89 ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 177.915 130.824 212.909 1.00 31.60 ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 180.616 131.233 212.572 1.00 31.70 ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 182.068 130.883 212.315 1.00 32.79 ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 182.459 130.595 211.184 1.00 32.70 ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 182.877 130.905 213.367 1.00 34.29 ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 177.374 131.111 210.750 1.00 27.26 ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 175.933 131.015 210.958 1.00 27.33 ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 175.466 129.694 210.362 1.00 28.68 ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 175.660 129.438 209.168 1.00 27.29 ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 175.189 132.205 210.336 1.00 23.55 ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 175.614 133.506 211.020 1.00 24.69 ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 173.688 132.011 210.447 1.00 24.30 ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 174.949 134.739 210.464 1.00 22.35 ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 174.852 128.858 211.196 1.00 29.24 ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 174.464 127.516 210.780 1.00 30.53 ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 173.219 127.555 209.905 1.00 30.73 ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 172.216 128.185 210.262 1.00 29.50 ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 174.223 126.633 212.006 1.00 31.79 ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 175.445 126.438 212.886 1.00 29.56 ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 176.673 126.033 212.094 1.00 32.88 ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 177.663 126.764 212.040 1.00 32.35 ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 176.615 124.862 211.474 1.00 32.38 ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 173.287 126.875 208.761 1.00 27.90 ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 172.151 126.719 207.866 1.00 24.72 ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 172.316 125.408 207.115 1.00 29.49 ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 173.439 125.030 206.763 1.00 31.95 ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 172.038 127.892 206.884 1.00 23.50 ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 173.175 127.974 205.901 1.00 25.04 ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 174.343 128.639 206.228 1.00 25.86 ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 173.069 127.396 204.648 1.00 26.68 ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 175.387 128.716 205.329 1.00 24.80 ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 174.110 127.470 203.746 1.00 26.23 ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 175.269 128.131 204.085 1.00 23.66 ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 171.206 124.717 206.873 1.00 31.27 ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 171.280 123.448 206.165 1.00 31.44 ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 171.509 123.665 204.675 1.00 34.15 ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 171.047 124.648 204.090 1.00 36.96 ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 170.008 122.624 206.375 1.00 32.67 ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 169.810 122.157 207.804 1.00 35.20 ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 168.522 121.361 207.953 1.00 35.39 ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 167.322 122.164 207.762 1.00 36.03 ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 166.094 121.666 207.712 1.00 34.89 ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 165.868 120.369 207.850 1.00 32.90 ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 165.068 122.486 207.515 1.00 35.11 ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 172.242 122.735 204.062 1.00 37.93 ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 172.527 122.760 202.633 1.00 39.74 ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 171.837 121.640 201.869 1.00 39.22 ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 171.520 121.814 200.690 1.00 37.13 ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 174.045 122.678 202.402 1.00 38.08 ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 174.682 123.796 203.034 1.00 37.98 ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 174.385 122.702 200.919 1.00 36.03 ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 171.567 120.510 202.528 1.00 41.57 ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 170.977 119.361 201.849 1.00 40.19 ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 169.590 119.676 201.302 1.00 41.68 ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 169.253 119.273 200.183 1.00 43.01 ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 170.914 118.176 202.811 1.00 38.69 ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 170.352 118.558 204.167 1.00 40.34 ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 170.005 119.743 204.351 1.00 40.04 ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 170.262 117.679 205.050 1.00 39.78 ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 168.772 120.391 202.070 1.00 39.75 ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 167.385 120.634 201.687 1.00 39.91 ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 167.323 121.767 200.670 1.00 38.46 ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 167.973 122.806 200.834 1.00 35.06 ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 166.524 120.941 202.924 1.00 39.67 ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 165.078 121.238 202.514 1.00 37.72 ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 167.114 122.091 203.732 1.00 37.55 ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 164.090 121.160 203.656 1.00 37.06 ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 166.554 121.558 199.604 1.00 32.22 ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 166.310 122.602 198.622 1.00 29.97 ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 165.245 123.564 199.132 1.00 26.94 ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 164.391 123.203 199.945 1.00 28.88 ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 165.878 121.997 197.287 1.00 28.61 ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 165.301 124.805 198.638 1.00 18.52 ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 164.417 125.845 199.153 1.00 16.99 ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 162.954 125.573 198.820 1.00 20.60 ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 162.066 125.973 199.583 1.00 26.19 ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 164.845 127.209 198.613 1.00 15.73 ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 165.207 127.219 197.140 1.00 16.13 ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 165.854 128.538 196.752 1.00 13.86 ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 166.263 128.562 195.354 1.00 13.34 ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 167.493 128.310 194.927 1.00 17.55 ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 168.465 128.000 195.768 1.00 17.33 ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 167.751 128.369 193.624 1.00 18.17 ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 162.682 124.905 197.697 1.00 21.09 ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 161.300 124.633 197.318 1.00 19.06 ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 160.606 123.740 198.340 1.00 18.90 ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 159.450 123.984 198.705 1.00 18.16 ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 161.249 124.001 195.926 1.00 19.21 ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 161.957 122.756 195.935 1.00 24.45 ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 161.875 124.930 194.902 1.00 17.99 ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 161.294 122.702 198.815 1.00 20.24 ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 160.716 121.821 199.821 1.00 21.52 ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 160.720 122.442 201.213 1.00 24.55 ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 159.914 122.042 202.058 1.00 27.09 ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 161.463 120.485 199.843 1.00 23.60 ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 160.910 119.440 198.877 1.00 26.92 ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 161.483 119.568 197.473 1.00 30.71 ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 162.695 119.838 197.344 1.00 27.65 ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 160.722 119.394 196.497 1.00 28.14 ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 161.613 123.401 201.472 1.00 21.45 ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 161.604 124.103 202.752 1.00 19.40 ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 160.432 125.071 202.850 1.00 22.03 ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 159.813 125.199 203.912 1.00 24.54 ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 162.917 124.858 202.950 1.00 19.74 ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 163.115 125.371 204.357 1.00 22.48 ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 163.201 124.499 205.431 1.00 23.83 ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 163.198 126.736 204.612 1.00 21.15 ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 163.378 124.969 206.713 1.00 24.92 ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 163.374 127.216 205.893 1.00 22.85 ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 163.467 126.321 206.942 1.00 25.55 ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 163.639 126.776 208.226 1.00 24.96 ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 160.123 125.769 201.759 1.00 19.17 ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 159.133 126.835 201.774 1.00 14.58 ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 157.742 126.369 201.372 1.00 16.57 ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 156.836 127.200 201.265 1.00 18.60 ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 159.585 127.971 200.857 1.00 14.38 ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 160.718 128.827 201.421 1.00 11.10 ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 161.303 129.712 200.339 1.00 12.82 ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 160.208 129.654 202.585 1.00 10.51 ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 157.550 125.074 201.143 1.00 18.22 ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 156.233 124.551 200.813 1.00 20.30 ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 156.162 123.094 201.241 1.00 24.90 ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 157.184 122.421 201.399 1.00 27.84 ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 155.929 124.689 199.318 1.00 19.60 ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 156.812 123.898 198.543 1.00 19.32 ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 154.940 122.614 201.433 1.00 25.16 ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 154.702 121.224 201.786 1.00 24.42 ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 154.193 120.453 200.574 1.00 27.95 ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 153.792 121.032 199.562 1.00 30.03 ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 153.709 121.116 202.947 1.00 24.56 ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 152.454 121.929 202.717 1.00 30.27 ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 151.647 121.613 201.846 1.00 33.15 ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 152.283 122.984 203.503 1.00 31.01 ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 154.223 119.124 200.691 1.00 30.33 ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 153.878 118.272 199.557 1.00 29.13 ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 152.420 118.443 199.148 1.00 31.15 ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 152.099 118.400 197.955 1.00 32.04 ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 154.177 116.812 199.891 1.00 29.26 ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 151.522 118.625 200.119 1.00 28.35 ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 150.111 118.816 199.791 1.00 28.80 ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 149.901 120.085 198.974 1.00 31.74 ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 149.142 120.088 197.997 1.00 33.20 ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 149.278 118.861 201.071 1.00 31.10 ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 148.844 117.485 201.533 1.00 36.65 ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 148.269 116.737 200.714 1.00 36.36 ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 149.073 117.151 202.714 1.00 33.57 ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 150.568 121.176 199.359 1.00 31.50 ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 150.417 122.426 198.624 1.00 28.23 ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 150.997 122.316 197.221 1.00 27.01 ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 150.422 122.845 196.264 1.00 30.69 ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 151.073 123.570 199.394 1.00 25.95 ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 150.462 124.923 199.100 1.00 31.62 ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 150.858 125.977 200.110 1.00 34.12 ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 151.812 125.737 200.882 1.00 29.70 ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 150.202 127.037 200.142 1.00 32.10 ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 152.131 121.628 197.076 1.00 25.62 ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 152.700 121.422 195.748 1.00 25.78 ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 151.776 120.576 194.879 1.00 27.43 ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 151.610 120.851 193.686 1.00 28.14 ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 154.079 120.776 195.862 1.00 24.30 ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 155.146 121.709 196.402 1.00 25.87 ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 156.528 121.094 196.298 1.00 25.34 ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 156.647 119.887 197.106 1.00 30.73 ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 157.166 119.850 198.325 1.00 28.29 ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 157.614 120.944 198.917 1.00 26.19 ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 157.235 118.689 198.968 1.00 27.63 ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 151.168 119.539 195.460 1.00 29.63 ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 150.221 118.723 194.711 1.00 28.81 ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 149.016 119.545 194.267 1.00 27.29 ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 148.553 119.418 193.127 1.00 28.32 ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 149.774 117.528 195.553 1.00 29.11 ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 148.993 116.429 194.832 1.00 30.87 ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 149.621 116.117 193.483 1.00 30.54 ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 148.912 115.178 195.690 1.00 29.76 ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 148.497 120.396 195.155 1.00 24.52 ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 147.387 121.264 194.776 1.00 26.11 ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 147.800 122.236 193.679 1.00 28.47 ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 147.006 122.548 192.784 1.00 27.17 ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 146.865 122.021 195.998 1.00 26.54 ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 145.564 122.766 195.745 1.00 28.78 ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 145.153 123.598 196.948 1.00 29.72 ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 145.925 124.830 197.053 1.00 29.65 ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 146.910 125.022 197.919 1.00 31.88 ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 147.273 124.079 198.773 1.00 29.03 ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 147.548 126.189 197.927 1.00 27.97 ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 149.038 122.731 193.736 1.00 26.21 ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 149.536 123.614 192.685 1.00 21.75 ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 149.593 122.895 191.344 1.00 24.24 ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 149.209 123.460 190.313 1.00 26.78 ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 150.916 124.150 193.062 1.00 22.50 ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 150.893 125.161 194.162 1.00 22.68 ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 149.844 125.951 194.528 1.00 21.27 ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 151.972 125.493 195.041 1.00 23.82 ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 150.203 126.754 195.582 1.00 22.30 ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 151.505 126.493 195.916 1.00 22.35 ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 153.289 125.043 195.174 1.00 21.86 ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 152.306 127.049 196.908 1.00 19.63 ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 154.082 125.596 196.160 1.00 20.02 ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 153.588 126.588 197.014 1.00 20.10 ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 150.071 121.648 191.333 1.00 25.96 ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 150.057 120.870 190.096 1.00 24.99 ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 148.632 120.654 189.603 1.00 26.96 ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 148.372 120.696 188.395 1.00 26.90 ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 150.762 119.525 190.286 1.00 25.65 ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 152.114 119.576 190.983 1.00 30.14 ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 153.118 120.491 190.300 1.00 31.46 ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 152.985 120.819 189.122 1.00 30.35 ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 154.134 120.907 191.047 1.00 29.04 ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 147.695 120.418 190.523 1.00 28.89 ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 146.297 120.278 190.138 1.00 26.88 ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 145.721 121.570 189.573 1.00 26.18 ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 144.715 121.526 188.857 1.00 27.53 ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 145.464 119.815 191.334 1.00 27.73 ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 146.333 122.717 189.876 1.00 25.84 ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 145.894 124.010 189.364 1.00 25.22 ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 146.665 124.428 188.115 1.00 27.19 ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 146.813 125.627 187.852 1.00 28.98 ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 146.014 125.078 190.448 1.00 24.38 ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 145.125 124.819 191.519 1.00 26.72 ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 147.163 123.457 187.348 1.00 25.26 ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 147.855 123.707 186.083 1.00 24.41 ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 149.104 124.565 186.273 1.00 21.85 ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 149.412 125.433 185.454 1.00 23.32 ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 146.915 124.340 185.054 1.00 27.94 ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 146.722 125.717 185.324 1.00 31.12 ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 149.828 124.326 187.362 1.00 20.03 ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 151.137 124.954 187.510 1.00 22.25 ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 152.209 124.037 186.937 1.00 24.01 ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 152.277 122.864 187.323 1.00 25.09 ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 151.446 125.253 188.970 1.00 22.57 ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 152.841 125.817 189.252 1.00 21.52 ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 152.876 127.320 189.018 1.00 17.97 ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 153.288 125.484 190.663 1.00 21.11 ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 153.038 124.518 186.012 1.00 20.42 ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 154.051 123.645 185.408 1.00 19.02 ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 155.019 123.101 186.447 1.00 20.21 ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 155.372 123.779 187.414 1.00 25.73 ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 154.759 124.562 184.404 1.00 20.09 ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 154.420 125.952 184.831 1.00 20.71 ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 153.070 125.881 185.460 1.00 20.93 ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 155.440 121.854 186.242 1.00 20.85 ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 156.340 121.166 187.167 1.00 22.60 ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 157.762 121.646 186.908 1.00 25.23 ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 158.499 121.082 186.099 1.00 26.78 ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 156.222 119.656 187.008 1.00 22.03 ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 158.149 122.710 187.607 1.00 19.43 ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 159.484 123.270 187.476 1.00 13.85 ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 159.890 123.878 188.809 1.00 14.01 ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 159.053 124.402 189.547 1.00 19.50 ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 159.545 124.321 186.360 1.00 12.94 ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 160.925 124.922 186.196 1.00 18.21 ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 161.920 124.191 186.381 1.00 18.17 ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 161.016 126.126 185.874 1.00 18.21 ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 161.186 123.790 189.117 1.00 14.48 ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 161.685 124.351 190.368 1.00 11.90 ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 161.488 125.862 190.411 1.00 12.43 ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 161.086 126.414 191.442 1.00 17.85 ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 163.158 123.994 190.553 1.00 11.78 ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 163.351 122.714 191.337 1.00 17.98 ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 162.354 122.187 191.875 1.00 20.54 ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 164.500 122.230 191.414 1.00 17.05 ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 161.767 126.545 189.298 1.00 8.19  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 161.530 127.984 189.238 1.00 5.69  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 160.049 128.303 189.385 1.00 8.02  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 159.676 129.263 190.069 1.00 13.24 ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 162.078 128.550 187.928 1.00 8.39  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 162.121 130.071 187.789 1.00 5.04  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 163.442 130.509 187.186 1.00 5.32  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 160.962 130.567 186.944 1.00 6.84  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 159.186 127.504 188.755 1.00 7.63  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 157.750 127.726 188.880 1.00 8.22  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 157.263 127.425 190.291 1.00 12.62 ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 156.357 128.096 190.798 1.00 17.16 ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 157.000 126.882 187.853 1.00 8.41  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 157.324 127.372 186.147 1.00 29.09 ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 157.848 126.419 190.945 1.00 11.86 ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 157.510 126.155 192.340 1.00 4.75  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 157.927 127.317 193.233 1.00 6.96  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 157.187 127.708 194.143 1.00 14.12 ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 158.163 124.855 192.805 1.00 9.17  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 157.739 123.778 191.961 1.00 15.40 ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 157.771 124.547 194.238 1.00 11.57 ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 159.108 127.887 192.983 1.00 6.26  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 159.534 129.066 193.730 1.00 7.32  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 158.597 130.240 193.484 1.00 10.22 ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 158.290 131.007 194.403 1.00 11.29 ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 160.967 129.438 193.351 1.00 5.07  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 162.011 128.437 193.805 1.00 6.60  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 163.321 128.590 193.060 1.00 14.02 ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 163.423 129.508 192.221 1.00 12.61 ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 164.247 127.791 193.314 1.00 13.06 ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 158.140 130.399 192.241 1.00 7.69  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 157.201 131.470 191.923 1.00 3.42  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 155.869 131.275 192.639 1.00 5.39  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 155.264 132.241 193.113 1.00 8.33  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 156.997 131.545 190.411 1.00 2.65  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 158.181 132.152 189.695 1.00 3.82  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 159.089 132.693 190.325 1.00 5.04  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 158.181 132.066 188.372 1.00 7.64  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 155.393 130.031 192.719 1.00 4.34  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 154.172 129.751 193.470 1.00 1.85  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 154.366 130.023 194.958 1.00 8.82  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 153.461 130.537 195.627 1.00 16.36 ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 153.733 128.306 193.239 1.00 8.71  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 155.542 129.686 195.490 1.00 9.47  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 155.853 130.008 196.880 1.00 5.95  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 155.809 131.514 197.099 1.00 6.46  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 155.282 131.996 198.109 1.00 11.72 ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 157.220 129.417 197.269 1.00 6.42  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 157.133 127.895 197.380 1.00 8.35  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 157.721 130.032 198.563 1.00 7.85  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 158.470 127.203 197.273 1.00 9.10  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 156.373 132.280 196.162 1.00 4.82  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 156.326 133.735 196.262 1.00 1.48  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 154.892 134.246 196.206 1.00 5.55  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 154.514 135.142 196.969 1.00 11.38 ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 157.157 134.363 195.145 1.00 2.90  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 158.651 134.351 195.397 1.00 5.04  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 159.599 134.415 193.868 1.00 9.85  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 161.097 133.576 194.367 1.00 7.56  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 154.080 133.691 195.305 1.00 6.44  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 152.682 134.090 195.198 1.00 5.05  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 151.873 133.695 196.425 1.00 7.33  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 150.791 134.248 196.643 1.00 12.32 ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 152.050 133.476 193.948 1.00 6.31  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 152.493 134.047 192.601 1.00 5.99  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 152.004 133.170 191.461 1.00 6.19  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 151.994 135.468 192.435 1.00 4.89  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 152.352 132.733 197.209 1.00 4.03  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 151.684 132.385 198.457 1.00 5.23  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 152.148 133.245 199.630 1.00 9.82  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 151.329 133.642 200.466 1.00 14.67 ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 151.907 130.905 198.778 1.00 5.62  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 151.711 130.550 200.243 1.00 9.00  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 152.371 129.229 200.599 1.00 12.25 ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 153.781 129.134 200.044 1.00 14.17 ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 154.480 127.917 200.536 1.00 13.39 ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 153.442 133.557 199.699 1.00 7.75  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 154.044 134.203 200.858 1.00 3.88  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 154.385 135.669 200.617 1.00 5.53  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 155.269 136.207 201.292 1.00 11.10 ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 155.303 133.449 201.283 1.00 3.58  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 155.064 132.036 201.769 1.00 4.79  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 156.380 131.345 202.079 1.00 6.37  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 156.184 130.015 202.645 1.00 11.50 ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 155.840 129.778 203.903 1.00 14.00 ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 155.645 130.763 204.764 1.00 11.49 ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 155.692 128.520 204.309 1.00 10.57 ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 153.719 136.325 199.673 1.00 4.66  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 154.054 137.708 199.360 1.00 3.67  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 153.627 138.640 200.488 1.00 5.74  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 152.595 138.434 201.132 1.00 7.13  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 153.390 138.136 198.051 1.00 3.45  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 151.887 138.131 198.096 1.00 7.24  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 151.179 136.993 197.765 1.00 6.34  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 151.184 139.268 198.456 1.00 8.39  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 149.802 136.984 197.803 1.00 5.47  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 149.807 139.264 198.496 1.00 8.23  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 149.116 138.119 198.168 1.00 8.68  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 154.441 139.667 200.732 1.00 5.94  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 154.055 140.759 201.620 1.00 5.06  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 153.433 141.900 200.820 1.00 8.88  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 152.278 142.272 201.048 1.00 12.94 ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 155.263 141.250 202.422 1.00 5.20  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 155.521 140.414 203.660 1.00 12.88 ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 154.592 139.882 204.267 1.00 13.45 ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 156.785 140.300 204.044 1.00 15.01 ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 154.188 142.459 199.880 1.00 3.80  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 153.620 143.368 198.899 1.00 3.68  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 152.864 142.579 197.839 1.00 6.04  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 153.161 141.412 197.577 1.00 8.69  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 154.710 144.211 198.239 1.00 4.71  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 155.296 145.285 199.133 1.00 4.26  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 156.542 145.885 198.510 1.00 4.54  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 157.551 144.867 198.239 1.00 0.00  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 158.585 145.031 197.426 1.00 1.71  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 158.787 146.169 196.785 1.00 5.11  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 159.441 144.027 197.258 1.00 3.71  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 151.877 143.225 197.232 1.00 7.26  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 151.061 142.547 196.237 1.00 5.24  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 151.908 142.195 195.015 1.00 7.68  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 152.709 143.014 194.557 1.00 13.18 ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 149.877 143.422 195.837 1.00 7.64  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 148.859 143.572 196.942 1.00 11.88 ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 148.207 142.465 197.464 1.00 11.16 ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 148.559 144.818 197.474 1.00 12.01 ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 147.280 142.594 198.476 1.00 11.09 ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 147.633 144.958 198.485 1.00 10.65 ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 146.996 143.841 198.983 1.00 12.36 ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 146.071 143.973 199.994 1.00 14.80 ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 151.760 140.992 194.473 1.00 6.19  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 152.683 140.528 193.436 1.00 2.12  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 152.421 141.157 192.078 1.00 2.62  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 151.287 141.469 191.708 1.00 5.13  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 152.430 139.013 193.384 1.00 1.41  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 151.486 138.705 194.515 1.00 6.32  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 150.765 139.969 194.820 1.00 7.54  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 153.509 141.342 191.336 1.00 5.85  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 153.473 141.698 189.923 1.00 5.23  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 154.020 140.502 189.156 1.00 7.83  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 155.213 140.193 189.249 1.00 11.35 ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 154.285 142.960 189.638 1.00 2.19  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 153.995 143.698 188.328 1.00 2.09  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 154.342 145.167 188.460 1.00 8.94  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 154.749 143.089 187.159 1.00 5.06  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 153.154 139.833 188.404 1.00 8.30  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 153.495 138.593 187.718 1.00 3.84  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 153.908 138.917 186.292 1.00 7.36  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 153.228 139.681 185.597 1.00 14.23 ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 152.316 137.608 187.737 1.00 0.77  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 151.795 137.425 189.161 1.00 5.48  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 152.736 136.276 187.156 1.00 4.35  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 150.483 136.683 189.236 1.00 7.54  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 155.025 138.344 185.855 1.00 7.55  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 155.490 138.461 184.479 1.00 5.71  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 155.488 137.061 183.887 1.00 11.03 ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 156.265 136.199 184.315 1.00 14.73 ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 156.883 139.098 184.390 1.00 6.38  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 156.945 140.366 185.241 1.00 10.39 ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 157.231 139.406 182.946 1.00 6.89  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 158.344 140.893 185.446 1.00 7.03  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 154.617 136.829 182.906 1.00 8.67  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 154.511 135.529 182.247 1.00 11.63 ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 154.084 135.735 180.800 1.00 15.68 ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 152.883 135.855 180.512 1.00 20.35 ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 153.529 134.610 182.968 1.00 12.12 ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 153.677 133.159 182.547 1.00 21.51 ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 154.690 132.831 181.897 1.00 22.52 ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 152.778 132.350 182.854 1.00 23.45 ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 155.036 135.786 179.866 1.00 14.75 ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 154.655 135.856 178.446 1.00 17.57 ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 153.843 134.658 177.988 1.00 16.83 ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 152.976 134.804 177.118 1.00 18.44 ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 156.006 135.937 177.723 1.00 17.00 ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 157.005 135.412 178.702 1.00 18.59 ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 156.494 135.786 180.053 1.00 13.17 ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 154.095 133.476 178.553 1.00 18.35 ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 153.370 132.277 178.153 1.00 22.11 ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 151.921 132.287 178.620 1.00 22.96 ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 151.087 131.599 178.022 1.00 25.19 ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 154.077 131.033 178.693 1.00 23.13 ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 155.386 130.922 178.164 1.00 24.42 ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 151.602 133.045 179.667 1.00 21.27 ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 150.250 133.121 180.176 1.00 21.93 ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 149.839 132.001 181.104 1.00 23.13 ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 148.679 131.974 181.536 1.00 21.94 ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 150.744 131.074 181.428 1.00 23.66 ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 150.390 129.982 182.328 1.00 23.54 ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 150.193 130.467 183.758 1.00 25.09 ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 149.372 129.905 184.493 1.00 26.97 ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 151.460 128.891 182.284 1.00 23.61 ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 151.393 128.003 181.054 1.00 27.68 ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 152.735 127.396 180.701 1.00 29.42 ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 153.428 127.874 179.804 1.00 26.20 ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 153.110 126.335 181.408 1.00 27.15 ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 150.939 131.493 184.174 1.00 20.62 ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 150.789 132.018 185.529 1.00 16.03 ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 149.412 132.631 185.739 1.00 19.09 ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 148.823 132.489 186.816 1.00 20.79 ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 151.876 133.047 185.817 1.00 17.77 ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 148.890 133.331 184.730 1.00 20.84 ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 147.552 133.900 184.838 1.00 21.35 ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 146.504 132.810 185.021 1.00 23.93 ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 145.615 132.927 185.873 1.00 22.16 ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 147.242 134.742 183.599 1.00 23.15 ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 148.196 135.806 183.494 1.00 21.67 ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 145.844 135.324 183.679 1.00 24.31 ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 146.600 131.734 184.237 1.00 26.20 ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 145.662 130.626 184.377 1.00 23.55 ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 145.806 129.951 185.735 1.00 23.81 ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 144.806 129.569 186.355 1.00 25.35 ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 145.870 129.618 183.249 1.00 23.25 ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 144.859 128.484 183.230 1.00 26.52 ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 145.358 127.272 182.470 1.00 30.63 ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 146.555 127.244 182.114 1.00 31.52 ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 144.553 126.348 182.227 1.00 26.17 ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 147.044 129.796 186.212 1.00 21.39 ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 147.265 129.194 187.522 1.00 18.95 ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 146.646 130.039 188.629 1.00 20.76 ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 146.031 129.505 189.558 1.00 25.87 ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 148.763 129.003 187.760 1.00 19.08 ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 149.138 128.866 189.207 1.00 19.81 ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 148.856 127.705 189.904 1.00 21.68 ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 149.780 129.898 189.870 1.00 18.53 ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 149.204 127.577 191.233 1.00 21.86 ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 150.128 129.775 191.199 1.00 17.54 ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 149.840 128.614 191.881 1.00 19.39 ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 146.804 131.361 188.548 1.00 18.63 ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 146.214 132.247 189.547 1.00 19.37 ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 144.691 132.190 189.484 1.00 21.24 ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 144.017 132.136 190.521 1.00 21.79 ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 146.740 133.682 189.364 1.00 19.44 ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 148.145 133.808 189.953 1.00 18.02 ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 145.810 134.689 190.013 1.00 18.42 ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 148.191 133.613 191.450 1.00 16.74 ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 144.126 132.195 188.274 1.00 23.21 ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 142.674 132.134 188.137 1.00 19.79 ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 142.115 130.829 188.689 1.00 24.56 ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 141.057 130.820 189.327 1.00 28.05 ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 142.279 132.309 186.669 1.00 19.61 ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 142.532 133.703 186.122 1.00 24.31 ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 141.521 134.964 186.919 1.00 33.72 ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 139.888 134.252 186.733 1.00 25.58 ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 142.808 129.713 188.451 1.00 22.90 ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 142.334 128.428 188.957 1.00 21.03 ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 142.511 128.323 190.466 1.00 22.24 ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 141.666 127.742 191.156 1.00 24.94 ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 143.066 127.287 188.251 1.00 23.02 ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 142.721 127.196 186.779 1.00 26.82 ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 143.591 126.982 185.937 1.00 27.34 ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 141.442 127.356 186.461 1.00 26.82 ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 143.608 128.870 190.996 1.00 23.22 ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 143.885 128.753 192.425 1.00 23.93 ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 142.861 129.515 193.258 1.00 27.61 ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 142.424 129.031 194.308 1.00 28.21 ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 145.298 129.251 192.723 1.00 23.35 ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 145.793 128.916 194.117 1.00 24.73 ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 146.332 127.505 194.218 1.00 27.86 ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 146.463 126.843 193.169 1.00 30.43 ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 146.624 127.057 195.347 1.00 28.70 ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 142.469 130.707 192.810 1.00 26.25 ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 141.521 131.546 193.531 1.00 26.14 ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 140.116 131.468 192.950 1.00 28.92 ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 139.331 132.407 193.113 1.00 31.70 ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 142.006 132.997 193.543 1.00 25.00 ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 143.176 133.248 194.466 1.00 26.51 ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 144.472 132.941 194.074 1.00 26.98 ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 142.985 133.793 195.729 1.00 27.00 ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 145.543 133.169 194.914 1.00 26.47 ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 144.052 134.024 196.574 1.00 27.10 ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 145.328 133.710 196.162 1.00 27.41 ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 146.393 133.939 197.001 1.00 27.81 ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 139.784 130.369 192.268 1.00 34.26 ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 138.464 130.242 191.659 1.00 34.22 ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 137.367 130.169 192.716 1.00 36.37 ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 136.306 130.786 192.559 1.00 33.92 ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 138.425 129.013 190.752 1.00 32.80 ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 137.036 128.445 190.523 1.00 35.46 ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 137.098 127.139 189.749 1.00 35.49 ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 137.321 127.390 188.268 1.00 36.03 ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 136.169 128.095 187.644 1.00 36.95 ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 137.604 129.427 193.801 1.00 39.05 ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 136.589 129.275 194.837 1.00 39.33 ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 136.324 130.570 195.595 1.00 40.03 ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 135.295 130.678 196.269 1.00 41.77 ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 136.993 128.168 195.813 1.00 39.69 ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 138.407 128.338 196.341 1.00 41.87 ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 138.977 129.439 196.200 1.00 41.07 ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 138.953 127.360 196.894 1.00 41.21 ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 137.223 131.546 195.503 1.00 34.26 ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 137.030 132.849 196.122 1.00 33.85 ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 136.501 133.884 195.140 1.00 33.32 ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 136.452 135.072 195.474 1.00 35.60 ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 138.337 133.335 196.749 1.00 33.94 ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 138.904 132.399 197.803 1.00 33.68 ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 140.294 132.830 198.234 1.00 34.86 ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 140.336 134.241 198.599 1.00 38.31 ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 141.196 134.766 199.461 1.00 36.70 ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 142.107 134.025 200.068 1.00 35.35 ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 141.141 136.070 199.717 1.00 36.41 ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 136.113 133.458 193.938 1.00 32.28 ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 135.539 134.331 192.914 1.00 34.09 ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 136.514 135.446 192.527 1.00 31.47 ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 136.231 136.637 192.659 1.00 32.86 ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 134.194 134.905 193.370 1.00 33.19 ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 132.985 134.209 192.766 1.00 32.86 ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 132.883 132.768 193.235 1.00 34.19 ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 132.499 132.692 194.702 1.00 33.64 ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 132.250 131.292 195.137 1.00 32.06 ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 137.684 135.029 192.039 1.00 24.71 ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 138.661 135.982 191.534 1.00 24.31 ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 138.174 136.547 190.207 1.00 25.74 ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 137.540 135.846 189.405 1.00 25.69 ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 140.043 135.317 191.399 1.00 24.37 ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 141.108 136.352 191.035 1.00 20.67 ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 140.007 134.185 190.386 1.00 26.50 ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 142.519 135.833 191.137 1.00 23.08 ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 138.450 137.826 189.975 1.00 24.99 ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 137.962 138.536 188.801 1.00 23.17 ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 139.138 139.005 187.960 1.00 23.60 ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 140.048 139.664 188.472 1.00 25.10 ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 137.095 139.732 189.204 1.00 24.14 ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 135.969 139.273 189.962 1.00 24.89 ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 136.601 140.473 187.972 1.00 24.24 ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 139.115 138.665 186.675 1.00 22.94 ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 140.127 139.139 185.745 1.00 22.24 ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 139.752 140.516 185.215 1.00 22.88 ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 138.601 140.764 184.842 1.00 29.07 ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 140.297 138.153 184.590 1.00 22.64 ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 141.291 138.601 183.540 1.00 25.38 ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 141.307 137.662 182.346 1.00 26.65 ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 142.050 136.440 182.629 1.00 27.56 ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 141.590 135.215 182.420 1.00 29.39 ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 140.383 135.007 181.920 1.00 28.85 ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 142.360 134.173 182.718 1.00 26.28 ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 140.732 141.416 185.186 1.00 15.87 ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 140.495 142.804 184.819 1.00 20.54 ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 141.754 143.329 184.141 1.00 21.04 ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 142.831 142.741 184.254 1.00 27.66 ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 140.124 143.638 186.058 1.00 24.82 ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 139.015 143.026 186.726 1.00 28.18 ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 139.711 145.051 185.677 1.00 24.01 ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 141.605 144.427 183.401 1.00 17.74 ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 142.726 145.096 182.762 1.00 20.42 ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 142.710 146.573 183.124 1.00 21.95 ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 141.650 147.160 183.355 1.00 26.90 ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 142.685 144.932 181.238 1.00 25.34 ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 143.573 145.837 180.606 1.00 26.80 ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 143.905 147.169 183.180 1.00 23.23 ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 144.001 148.598 183.458 1.00 24.20 ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 143.360 149.428 182.355 1.00 27.27 ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 142.837 150.515 182.620 1.00 29.20 ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 145.463 149.010 183.638 1.00 21.90 ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 146.033 148.668 184.983 1.00 22.63 ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 145.600 149.325 186.121 1.00 23.64 ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 147.020 147.706 185.108 1.00 21.95 ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 146.129 149.017 187.359 1.00 21.97 ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 147.554 147.395 186.343 1.00 21.50 ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 147.106 148.051 187.469 1.00 20.74 ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 143.398 148.936 181.114 1.00 26.61 ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 142.822 149.673 179.998 1.00 28.21 ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 141.300 149.667 180.016 1.00 30.11 ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 140.683 150.542 179.400 1.00 32.71 ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 143.325 149.092 178.676 1.00 28.37 ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 144.840 148.932 178.559 1.00 26.82 ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 145.183 147.888 177.513 1.00 25.90 ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 145.489 150.263 178.223 1.00 26.89 ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 140.685 148.706 180.699 1.00 27.10 ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 139.232 148.660 180.780 1.00 28.84 ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 138.704 149.836 181.591 1.00 33.33 ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 139.276 150.213 182.617 1.00 31.70 ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 138.776 147.343 181.406 1.00 29.64 ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 139.057 146.148 180.518 1.00 35.10 ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 139.571 146.348 179.397 1.00 36.94 ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 138.767 145.010 180.941 1.00 33.55 ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 137.603 150.424 181.118 1.00 43.64 ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 136.984 151.524 181.849 1.00 43.40 ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 136.327 151.044 183.135 1.00 41.40 ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 136.308 151.777 184.131 1.00 41.48 ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 135.961 152.235 180.962 1.00 41.91 ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 136.607 152.983 179.813 1.00 44.86 ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 137.766 153.423 179.966 1.00 44.24 ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 135.956 153.130 178.757 1.00 45.42 ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 135.786 149.824 183.136 1.00 35.47 ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 135.137 149.283 184.322 1.00 37.41 ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 136.120 148.915 185.424 1.00 38.70 ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 135.680 148.642 186.547 1.00 38.47 ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 134.305 148.055 183.947 1.00 33.97 ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 137.425 148.912 185.129 1.00 34.44 ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 138.437 148.487 186.093 1.00 32.42 ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 138.220 149.137 187.453 1.00 32.72 ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 138.095 148.447 188.473 1.00 33.59 ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 139.833 148.815 185.558 1.00 29.92 ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 140.885 148.924 186.628 1.00 31.29 ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 141.235 147.822 187.392 1.00 30.80 ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 141.521 150.129 186.870 1.00 30.22 ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 142.199 147.924 188.375 1.00 28.49 ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 142.486 150.235 187.852 1.00 29.46 ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 142.825 149.131 188.606 1.00 27.86 ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 138.156 150.473 187.476 1.00 32.17 ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 137.874 151.215 188.700 1.00 33.25 ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 136.727 150.578 189.472 1.00 33.26 ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 136.902 150.126 190.612 1.00 34.79 ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 137.548 152.672 188.359 1.00 31.93 ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 138.763 153.562 188.172 1.00 31.69 ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 139.350 153.972 189.510 1.00 33.01 ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 138.333 154.491 190.415 1.00 35.86 ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 138.328 155.720 190.913 1.00 36.94 ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 139.272 156.593 190.604 1.00 34.89 ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 137.351 156.081 191.740 1.00 34.31 ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 135.561 150.482 188.826 1.00 33.46 ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 134.403 149.864 189.461 1.00 34.18 ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 134.757 148.483 189.993 1.00 33.72 ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 134.554 148.190 191.178 1.00 35.00 ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 133.242 149.791 188.465 1.00 35.06 ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 131.912 149.323 189.052 1.00 36.71 ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 131.738 147.812 188.948 1.00 35.22 ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 130.381 147.372 189.469 1.00 36.10 ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 130.218 145.893 189.402 1.00 34.47 ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 135.339 147.640 189.134 1.00 30.87 ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 135.750 146.310 189.570 1.00 30.54 ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 136.641 146.404 190.798 1.00 30.22 ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 136.375 145.765 191.823 1.00 30.21 ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 136.469 145.579 188.434 1.00 31.41 ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 135.572 145.328 187.242 1.00 34.95 ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 135.793 145.868 186.158 1.00 33.46 ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 134.551 144.501 187.433 1.00 36.35 ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 137.668 147.256 190.730 1.00 28.03 ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 138.560 147.414 191.871 1.00 28.39 ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 137.778 147.820 193.108 1.00 31.31 ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 137.955 147.234 194.183 1.00 30.52 ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 139.645 148.441 191.552 1.00 29.87 ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 140.453 148.977 192.732 1.00 28.64 ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 141.259 147.866 193.380 1.00 29.85 ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 141.362 150.106 192.280 1.00 27.90 ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 136.856 148.776 192.956 1.00 35.02 ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 136.054 149.204 194.094 1.00 31.96 ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 135.288 148.030 194.682 1.00 32.61 ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 135.267 147.842 195.904 1.00 32.28 ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 135.101 150.322 193.676 1.00 31.25 ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 134.224 150.837 194.802 1.00 36.20 ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 132.923 151.431 194.303 1.00 40.71 ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 132.732 151.498 193.071 1.00 40.46 ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 132.093 151.831 195.144 1.00 37.40 ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 134.698 147.195 193.822 1.00 33.11 ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 134.007 146.011 194.315 1.00 31.79 ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 134.965 145.123 195.094 1.00 33.57 ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 134.655 144.675 196.205 1.00 34.40 ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 133.379 145.245 193.152 1.00 32.21 ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 132.545 146.089 192.379 1.00 33.24 ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 136.164 144.904 194.546 1.00 31.29 ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 137.153 144.105 195.254 1.00 28.81 ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 137.559 144.764 196.561 1.00 31.18 ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 137.871 144.072 197.536 1.00 31.16 ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 138.375 143.872 194.367 1.00 27.33 ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 137.546 146.099 196.609 1.00 31.68 ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 137.887 146.776 197.852 1.00 29.04 ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 136.747 146.700 198.858 1.00 35.45 ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 136.975 146.861 200.062 1.00 36.89 ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 138.258 148.232 197.576 1.00 30.22 ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 139.535 148.472 196.769 1.00 32.10 ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 139.728 149.953 196.507 1.00 34.16 ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 140.743 147.892 197.481 1.00 29.31 ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 135.524 146.446 198.393 1.00 38.00 ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 134.376 146.436 199.291 1.00 36.51 ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 134.032 145.032 199.771 1.00 35.15 ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 133.896 144.801 200.977 1.00 35.28 ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 133.164 147.071 198.602 1.00 36.49 ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 133.012 148.558 198.866 1.00 35.37 ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 131.866 149.151 198.060 1.00 37.31 ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 131.974 150.599 197.925 1.00 38.37 ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 131.806 151.463 198.917 1.00 40.22 ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 131.502 151.064 200.142 1.00 35.85 ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 131.942 152.763 198.674 1.00 40.15 ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 133.885 144.088 198.845 1.00 31.87 ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 133.467 142.738 199.184 1.00 33.99 ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 134.632 141.810 199.503 1.00 35.73 ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 134.400 140.676 199.934 1.00 35.02 ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 132.636 142.147 198.039 1.00 36.00 ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 131.574 143.077 197.517 1.00 39.44 ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 130.843 143.875 198.381 1.00 35.26 ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 131.317 143.159 196.159 1.00 38.69 ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 129.873 144.732 197.901 1.00 33.82 ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 130.347 144.014 195.675 1.00 36.70 ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 129.624 144.802 196.547 1.00 35.26 ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 135.869 142.259 199.308 1.00 34.67 ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 137.022 141.450 199.650 1.00 31.84 ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 137.329 140.321 198.693 1.00 30.71 ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 138.019 139.370 199.075 1.00 31.41 ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 136.838 140.392 197.461 1.00 28.90 ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 137.178 139.308 196.554 1.00 28.84 ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 138.568 139.510 195.962 1.00 28.87 ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 139.023 140.646 195.801 1.00 28.23 ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 136.157 139.215 195.423 1.00 27.52 ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 134.749 139.000 195.928 1.00 30.97 ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 134.057 139.948 196.293 1.00 31.72 ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 134.315 137.746 195.953 1.00 29.57 ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 139.264 138.419 195.645 1.00 23.08 ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 140.538 138.543 194.931 1.00 16.60 ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 140.337 139.145 193.550 1.00 19.31 ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 139.299 138.964 192.912 1.00 26.78 ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 141.042 137.096 194.843 1.00 22.32 ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 139.842 136.247 195.097 1.00 27.24 ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 138.976 137.028 196.026 1.00 26.62 ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 141.351 139.873 193.095 1.00 15.57 ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 141.317 140.549 191.809 1.00 15.90 ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 142.629 140.314 191.078 1.00 14.86 ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 143.693 140.225 191.694 1.00 17.25 ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 141.066 142.054 191.984 1.00 14.29 ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 140.856 142.906 190.732 1.00 15.07 ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 139.510 142.603 190.101 1.00 17.78 ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 140.962 144.377 191.081 1.00 17.48 ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 142.543 140.202 189.754 1.00 13.27 ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 143.712 140.017 188.901 1.00 10.22 ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 143.644 141.043 187.780 1.00 14.34 ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 142.738 140.992 186.941 1.00 22.32 ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 143.772 138.597 188.344 1.00 13.80 ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 144.764 138.359 187.205 1.00 13.68 ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 146.194 138.401 187.712 1.00 14.75 ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 144.477 137.031 186.536 1.00 17.62 ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 144.597 141.969 187.764 1.00 11.34 ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 144.620 143.069 186.808 1.00 9.56  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 145.828 142.893 185.899 1.00 9.38  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 146.959 142.752 186.378 1.00 14.97 ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 144.658 144.432 187.519 1.00 12.32 ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 144.607 145.556 186.505 1.00 17.09 ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 143.517 144.544 188.507 1.00 15.47 ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 145.589 142.899 184.591 1.00 11.58 ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 146.651 142.773 183.611 1.00 14.11 ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 146.947 144.123 182.963 1.00 16.47 ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 146.369 145.153 183.311 1.00 18.51 ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 146.294 141.729 182.552 1.00 16.27 ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 145.564 140.517 183.085 1.00 18.35 ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 144.896 139.723 181.991 1.00 22.21 ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 144.912 140.114 180.824 1.00 22.55 ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 144.333 138.579 182.353 1.00 21.22 ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 147.869 144.099 181.998 1.00 19.75 ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 148.335 145.296 181.299 1.00 20.77 ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 148.923 146.306 182.286 1.00 24.63 ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 148.551 147.480 182.321 1.00 29.12 ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 147.212 145.916 180.462 1.00 20.65 ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 146.807 145.042 179.292 1.00 26.52 ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 147.663 144.778 178.422 1.00 28.40 ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 145.636 144.617 179.243 1.00 26.50 ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 149.864 145.816 183.098 1.00 18.12 ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 150.513 146.664 184.090 1.00 16.86 ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 151.416 147.698 183.428 1.00 20.83 ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 151.747 148.716 184.046 1.00 22.61 ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 151.286 145.788 185.096 1.00 16.24 ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 151.924 146.632 186.186 1.00 17.52 ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 150.358 144.764 185.707 1.00 18.97 ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 151.809 147.480 182.171 1.00 20.68 ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 152.527 148.516 181.438 1.00 21.59 ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 151.693 149.782 181.295 1.00 22.37 ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 152.251 150.857 181.056 1.00 22.79 ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 152.944 148.003 180.057 1.00 23.80 ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 151.901 147.149 179.351 1.00 23.34 ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 151.993 145.680 179.720 1.00 26.05 ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 152.430 145.372 180.848 1.00 29.30 ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 151.627 144.831 178.880 1.00 25.42 ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 150.375 149.673 181.441 1.00 20.99 ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 149.465 150.810 181.494 1.00 23.39 ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 148.916 150.992 182.906 1.00 24.36 ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 147.730 151.263 183.100 1.00 25.83 ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 148.327 150.638 180.493 1.00 24.86 ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 148.825 150.514 179.173 1.00 27.15 ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 149.785 150.824 183.902 1.00 21.55 ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 149.377 150.872 185.302 1.00 18.03 ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 148.700 152.198 185.627 1.00 19.18 ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 149.179 153.267 185.242 1.00 23.12 ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 150.597 150.661 186.199 1.00 17.58 ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 150.403 151.027 187.653 1.00 17.14 ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 149.713 150.186 188.514 1.00 19.32 ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 150.932 152.202 188.167 1.00 13.50 ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 149.543 150.514 189.845 1.00 17.49 ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 150.765 152.537 189.495 1.00 15.44 ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 150.072 151.690 190.329 1.00 18.93 ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 149.907 152.023 191.652 1.00 20.26 ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 147.575 152.118 186.337 1.00 18.84 ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 146.815 153.302 186.702 1.00 19.99 ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 147.184 153.706 188.119 1.00 21.68 ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 147.011 152.896 189.045 1.00 21.64 ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 145.319 153.031 186.599 1.00 20.93 ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 144.511 154.297 186.394 1.00 24.57 ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 144.535 154.835 185.268 1.00 24.85 ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 143.856 154.756 187.348 1.00 25.44 ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 147.690 154.923 188.341 1.00 20.52 ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 148.199 155.285 189.675 1.00 14.98 ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 147.140 155.305 190.766 1.00 17.29 ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 147.495 155.483 191.938 1.00 18.30 ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 148.788 156.686 189.457 1.00 15.60 ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 149.021 156.783 187.981 1.00 18.96 ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 147.926 155.986 187.351 1.00 20.77 ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 145.861 155.119 190.428 1.00 17.48 ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 144.807 155.144 191.435 1.00 19.00 ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 144.988 154.017 192.443 1.00 21.21 ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 144.427 154.068 193.542 1.00 21.97 ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 143.424 155.062 190.751 1.00 18.35 ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 143.190 153.674 190.160 1.00 19.56 ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 142.316 155.485 191.696 1.00 19.55 ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 145.776 152.998 192.094 1.00 18.45 ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 146.060 151.876 192.978 1.00 15.19 ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 147.165 152.173 193.983 1.00 13.84 ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 147.462 151.307 194.814 1.00 14.39 ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 146.454 150.650 192.153 1.00 14.90 ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 145.377 149.622 191.814 1.00 18.03 ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 145.953 148.542 190.918 1.00 18.71 ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 144.800 149.015 193.077 1.00 14.74 ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 147.785 153.353 193.922 1.00 11.36 ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 148.916 153.642 194.803 1.00 11.92 ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 148.579 153.500 196.284 1.00 15.32 ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 149.358 152.857 197.007 1.00 16.36 ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 149.471 155.034 194.487 1.00 13.02 ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 150.265 155.061 193.200 1.00 17.99 ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 150.399 154.046 192.518 1.00 16.46 ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 150.798 156.228 192.857 1.00 18.33 ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 147.480 154.060 196.805 1.00 17.29 ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 147.148 153.799 198.215 1.00 12.88 ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 146.891 152.332 198.513 1.00 15.27 ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 147.168 151.880 199.632 1.00 18.71 ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 145.891 154.650 198.444 1.00 15.72 ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 145.312 154.830 197.088 1.00 15.81 ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 146.501 154.980 196.196 1.00 17.67 ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 146.363 151.579 197.550 1.00 16.09 ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 146.071 150.167 197.779 1.00 14.86 ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 147.362 149.362 197.879 1.00 13.75 ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 147.519 148.518 198.769 1.00 15.11 ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 145.154 149.627 196.668 1.00 15.13 ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 144.798 148.176 196.934 1.00 13.66 ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 143.900 150.478 196.557 1.00 17.54 ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 148.301 149.605 196.965 1.00 10.13 ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 149.560 148.869 196.977 1.00 9.69  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 150.384 149.208 198.213 1.00 11.51 ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 150.998 148.326 198.825 1.00 16.31 ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 150.351 149.160 195.702 1.00 11.56 ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 149.709 148.680 194.399 1.00 9.34  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 150.641 148.917 193.226 1.00 8.85  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 149.333 147.215 194.501 1.00 9.62  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 150.409 150.486 198.596 1.00 14.59 ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 151.130 150.898 199.795 1.00 13.59 ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 150.426 150.478 201.075 1.00 13.72 ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 151.012 150.618 202.155 1.00 13.57 ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 151.327 152.414 199.795 1.00 9.92  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 152.530 152.844 198.991 1.00 12.69 ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 153.566 152.183 199.001 1.00 18.98 ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 152.404 153.963 198.292 1.00 14.56 ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 149.194 149.975 200.981 1.00 13.15 ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 148.395 149.589 202.143 1.00 11.37 ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 148.218 150.752 203.113 1.00 16.06 ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 148.270 150.574 204.333 1.00 21.56 ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 148.997 148.375 202.855 1.00 13.52 ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 148.440 147.049 202.371 1.00 16.04 ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 148.764 145.921 203.334 1.00 16.16 ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 148.747 144.624 202.672 1.00 18.12 ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 149.726 144.155 201.913 1.00 17.40 ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 150.828 144.855 201.696 1.00 12.91 ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 149.601 142.953 201.358 1.00 14.17 ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 148.011 151.950 202.572 1.00 19.83 ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 147.788 153.139 203.386 1.00 20.32 ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 146.323 153.202 203.795 1.00 21.96 ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 145.488 153.740 203.061 1.00 24.44 ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 148.195 154.388 202.609 1.00 19.50 ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 149.673 154.454 202.279 1.00 19.26 ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 149.994 155.536 201.269 1.00 25.23 ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 149.055 156.212 200.801 1.00 21.05 ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 151.188 155.709 200.945 1.00 26.69 ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 146.007 152.660 204.970 1.00 25.20 ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 144.639 152.573 205.459 1.00 28.48 ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 144.560 153.243 206.824 1.00 32.98 ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 145.560 153.405 207.525 1.00 34.79 ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 144.140 151.115 205.552 1.00 29.02 ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 144.103 150.476 204.174 1.00 28.65 ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 145.017 150.314 206.499 1.00 27.57 ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 143.344 153.636 207.192 1.00 39.97 ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 143.064 154.230 208.491 1.00 39.63 ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 142.047 153.358 209.209 1.00 41.04 ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 140.970 153.084 208.670 1.00 43.36 ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 142.542 155.664 208.340 1.00 37.55 ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 141.691 156.148 209.499 1.00 39.52 ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 141.281 157.602 209.319 1.00 41.39 ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 140.511 157.817 208.100 1.00 44.56 ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 140.860 158.650 207.129 1.00 43.41 ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 141.968 159.368 207.201 1.00 39.61 ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 140.076 158.767 206.061 1.00 41.76 ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 142.390 152.916 210.414 1.00 38.57 ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 141.523 152.054 211.213 1.00 40.25 ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 140.821 152.922 212.249 1.00 43.84 ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 141.380 153.221 213.307 1.00 44.46 ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 142.321 150.929 211.863 1.00 40.55 ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 142.872 149.918 210.874 1.00 43.69 ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 143.657 148.827 211.577 1.00 41.71 ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 144.168 147.835 210.639 1.00 40.52 ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 145.353 147.905 210.046 1.00 42.35 ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 146.172 148.922 210.258 1.00 42.00 ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 145.723 146.932 209.220 1.00 43.86 ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 139.591 153.328 211.940 1.00 47.35 ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 138.811 154.199 212.808 1.00 48.43 ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 137.430 153.599 213.024 1.00 47.40 ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 136.737 153.266 212.059 1.00 43.92 ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 138.686 155.607 212.211 1.00 47.13 ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 139.972 156.240 212.200 1.00 44.69 ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 137.717 156.452 213.026 1.00 45.34 ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 137.042 153.461 214.288 1.00 45.86 ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 135.699 153.014 214.630 1.00 43.51 ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 135.336 151.654 214.078 1.00 45.60 ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 134.215 151.464 213.591 1.00 44.83 ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 136.259 150.697 214.143 1.00 46.38 ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 136.008 149.394 213.565 1.00 45.89 ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 135.906 149.388 212.059 1.00 48.70 ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 135.438 148.404 211.482 1.00 47.29 ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 136.334 150.465 211.402 1.00 49.53 ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 136.272 150.592 209.953 1.00 46.53 ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 137.684 150.774 209.417 1.00 47.23 ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 138.406 151.676 209.857 1.00 48.58 ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 135.385 151.771 209.543 1.00 44.12 ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 133.897 151.521 209.721 1.00 44.57 ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 133.085 152.797 209.542 1.00 47.98 ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 133.326 153.442 208.256 1.00 47.13 ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 132.783 154.594 207.886 1.00 46.91 ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 131.964 155.261 208.683 1.00 46.54 ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 133.066 155.090 206.684 1.00 45.93 ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 138.075 149.917 208.478 1.00 39.76 ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 139.354 150.040 207.788 1.00 39.33 ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 139.074 150.789 206.489 1.00 39.18 ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 138.602 150.209 205.511 1.00 41.36 ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 139.995 148.674 207.535 1.00 36.66 ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 141.274 148.829 206.727 1.00 39.92 ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 140.274 147.968 208.851 1.00 37.01 ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 139.364 152.086 206.481 1.00 38.50 ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 139.040 152.949 205.356 1.00 38.85 ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 140.288 153.245 204.538 1.00 39.05 ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 141.351 153.547 205.090 1.00 42.06 ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 138.415 154.257 205.839 1.00 40.75 ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 137.215 154.121 206.777 1.00 43.41 ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 136.970 155.419 207.531 1.00 41.90 ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 135.979 153.700 206.002 1.00 42.12 ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 140.151 153.156 203.220 1.00 32.95 ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 141.211 153.493 202.284 1.00 32.31 ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 140.656 154.501 201.288 1.00 33.04 ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 139.516 154.374 200.831 1.00 35.29 ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 141.766 152.237 201.571 1.00 33.20 ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 142.959 152.598 200.687 1.00 32.18 ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 140.677 151.527 200.774 1.00 34.75 ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 143.823 151.413 200.340 1.00 29.91 ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 141.445 155.527 200.984 1.00 34.10 ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 141.006 156.592 200.084 1.00 36.69 ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 141.437 156.217 198.673 1.00 34.53 ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 142.599 156.383 198.294 1.00 33.02 ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 141.578 157.937 200.516 1.00 36.95 ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 140.941 158.357 201.729 1.00 34.05 ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 141.323 158.990 199.447 1.00 34.55 ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 140.494 155.691 197.895 1.00 35.74 ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 140.725 155.331 196.505 1.00 35.64 ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 140.302 156.518 195.650 1.00 36.07 ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 139.121 156.880 195.626 1.00 37.09 ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 139.931 154.077 196.133 1.00 35.72 ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 139.694 153.779 194.654 1.00 35.12 ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 140.986 153.298 194.030 1.00 34.80 ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 138.590 152.751 194.462 1.00 34.59 ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 141.262 157.125 194.965 1.00 36.60 ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 140.966 158.342 194.232 1.00 37.58 ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 140.508 159.429 195.186 1.00 39.60 ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 141.251 159.866 196.072 1.00 38.92 ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 139.266 159.875 195.011 1.00 47.42 ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 138.660 160.871 195.884 1.00 47.76 ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 137.595 160.276 196.798 1.00 46.67 ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 136.909 161.026 197.502 1.00 46.02 ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 138.056 162.001 195.048 1.00 49.10 ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 137.067 161.497 194.017 1.00 49.06 ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 137.442 160.618 193.210 1.00 46.68 ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 135.913 161.976 194.014 1.00 48.71 ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 137.441 158.955 196.812 1.00 47.28 ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 136.358 158.301 197.532 1.00 47.87 ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 136.925 157.441 198.652 1.00 47.75 ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 137.828 156.632 198.423 1.00 47.48 ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 135.513 157.449 196.579 1.00 47.62 ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 134.344 156.738 197.238 1.00 49.22 ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 133.791 155.616 196.382 1.00 49.83 ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 134.352 155.282 195.338 1.00 50.00 ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 132.683 155.029 196.817 1.00 47.02 ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 136.384 157.606 199.855 1.00 44.93 ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 136.795 156.817 201.011 1.00 43.99 ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 135.957 155.545 201.063 1.00 44.73 ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 134.728 155.611 201.154 1.00 45.87 ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 136.638 157.631 202.295 1.00 45.63 ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 137.335 156.994 203.476 1.00 46.98 ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 138.584 157.005 203.511 1.00 46.55 ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 136.632 156.491 204.377 1.00 45.94 ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 136.621 154.392 201.002 1.00 42.49 ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 135.956 153.102 200.866 1.00 40.37 ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 136.438 152.183 201.977 1.00 40.60 ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 137.641 152.111 202.249 1.00 42.43 ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 136.234 152.475 199.487 1.00 39.54 ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 135.659 153.361 198.382 1.00 40.82 ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 135.663 151.069 199.403 1.00 38.91 ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 136.101 152.969 197.002 1.00 41.17 ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 135.505 151.489 202.623 1.00 37.66 ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 135.881 150.487 203.609 1.00 37.68 ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 136.571 149.313 202.924 1.00 37.38 ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 136.150 148.863 201.854 1.00 35.35 ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 134.652 150.004 204.377 1.00 36.67 ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 135.010 149.364 205.703 1.00 40.22 ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 135.770 148.373 205.704 1.00 38.85 ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 134.531 149.852 206.747 1.00 41.63 ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 137.632 148.815 203.549 1.00 36.38 ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 138.446 147.745 202.987 1.00 32.98 ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 138.186 146.445 203.735 1.00 33.45 ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 138.232 146.412 204.969 1.00 34.29 ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 139.932 148.103 203.053 1.00 34.26 ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 140.909 147.038 202.553 1.00 35.00 ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 141.029 147.089 201.041 1.00 33.16 ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 142.271 147.213 203.205 1.00 33.89 ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 137.914 145.379 202.985 1.00 30.52 ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 137.670 144.075 203.584 1.00 30.71 ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 138.985 143.318 203.755 1.00 28.96 ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 139.870 143.411 202.900 1.00 32.46 ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 136.707 143.264 202.720 1.00 30.41 ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 136.615 141.924 203.172 1.00 30.50 ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 139.143 142.565 204.848 1.00 27.22 ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 140.425 141.886 205.094 1.00 27.29 ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 140.761 140.804 204.082 1.00 27.02 ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 141.934 140.424 203.979 1.00 26.71 ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 140.245 141.292 206.498 1.00 28.29 ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 138.769 141.140 206.651 1.00 31.16 ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 138.162 142.297 205.913 1.00 29.99 ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 139.785 140.297 203.337 1.00 26.15 ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 140.012 139.210 202.393 1.00 25.81 ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 140.473 139.693 201.024 1.00 27.09 ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 140.687 138.866 200.132 1.00 30.77 ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 138.740 138.373 202.240 1.00 26.90 ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 137.596 139.201 202.142 1.00 28.92 ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 140.626 141.000 200.836 1.00 21.39 ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 141.026 141.529 199.540 1.00 17.33 ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 142.470 141.164 199.219 1.00 19.74 ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 143.335 141.133 200.099 1.00 23.50 ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 140.854 143.046 199.512 1.00 16.86 ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 141.483 143.706 198.320 1.00 16.21 ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 140.930 143.563 197.059 1.00 20.60 ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 142.628 144.468 198.459 1.00 17.00 ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 141.510 144.170 195.961 1.00 18.44 ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 143.210 145.073 197.366 1.00 18.57 ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 142.650 144.925 196.117 1.00 17.73 ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 142.722 140.881 197.945 1.00 15.66 ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 144.067 140.634 197.438 1.00 14.18 ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 144.054 140.945 195.949 1.00 13.07 ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 143.060 140.699 195.263 1.00 17.83 ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 144.521 139.182 197.731 1.00 12.29 ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 143.511 138.190 197.198 1.00 15.83 ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 145.893 138.918 197.140 1.00 10.55 ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 145.150 141.517 195.458 1.00 8.93  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 145.260 141.917 194.061 1.00 6.01  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 146.547 141.352 193.479 1.00 10.36 ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 147.589 141.335 194.142 1.00 11.69 ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 145.199 143.453 193.903 1.00 7.35  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 145.160 143.840 192.423 1.00 11.74 ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 146.361 144.130 194.611 1.00 11.02 ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 144.914 145.305 192.190 1.00 10.82 ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 146.461 140.857 192.247 1.00 9.55  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 147.607 140.341 191.511 1.00 6.11  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 147.751 141.137 190.222 1.00 4.77  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 146.841 141.142 189.389 1.00 14.95 ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 147.441 138.853 191.194 1.00 8.90  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 147.294 137.982 192.405 1.00 7.59  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 148.410 137.501 193.067 1.00 7.47  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 146.040 137.634 192.876 1.00 8.54  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 148.278 136.695 194.179 1.00 10.34 ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 145.904 136.829 193.988 1.00 11.88 ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 147.024 136.360 194.640 1.00 12.68 ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 148.895 141.790 190.054 1.00 6.13  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 149.199 142.502 188.821 1.00 7.57  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 149.983 141.579 187.898 1.00 8.67  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 150.917 140.904 188.338 1.00 17.95 ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 149.995 143.775 189.114 1.00 9.05  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 149.444 144.708 190.192 1.00 7.09  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 150.247 145.995 190.235 1.00 9.19  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 147.977 145.002 189.953 1.00 8.27  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 149.591 141.530 186.629 1.00 4.81  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 150.214 140.621 185.678 1.00 7.77  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 150.504 141.331 184.365 1.00 8.35  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 149.752 142.213 183.943 1.00 15.44 ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 149.330 139.395 185.423 1.00 10.61 ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 148.097 139.768 184.842 1.00 16.26 ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 151.604 140.942 183.724 1.00 7.51  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 151.966 141.455 182.412 1.00 11.13 ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 152.484 140.309 181.555 1.00 13.85 ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 152.990 139.309 182.069 1.00 15.75 ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 153.021 142.569 182.502 1.00 10.40 ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 153.246 143.124 181.201 1.00 14.76 ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 154.331 142.032 183.050 1.00 11.05 ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 152.337 140.458 180.240 1.00 14.38 ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 152.801 139.462 179.286 1.00 10.56 ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 154.101 139.854 178.599 1.00 14.64 ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 154.564 139.125 177.718 1.00 19.35 ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 151.730 139.204 178.224 1.00 11.01 ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 150.484 138.511 178.737 1.00 13.44 ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 149.485 138.285 177.614 1.00 12.96 ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 149.076 139.533 176.982 1.00 14.32 ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 149.455 139.920 175.771 1.00 15.86 ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 150.257 139.176 175.028 1.00 19.27 ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 149.019 141.080 175.294 1.00 15.37 ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 154.696 140.982 178.972 1.00 13.04 ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 155.908 141.465 178.321 1.00 14.03 ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 157.102 141.267 179.242 1.00 17.17 ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 157.219 141.975 180.253 1.00 21.64 ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 155.762 142.939 177.946 1.00 16.47 ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 156.723 143.360 176.853 1.00 21.29 ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 157.392 142.480 176.274 1.00 21.69 ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 156.808 144.574 176.571 1.00 21.06 ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 158.004 140.326 178.951 1.00 18.80 ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 159.201 140.178 179.791 1.00 18.46 ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 160.161 141.351 179.697 1.00 22.35 ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 160.994 141.518 180.594 1.00 26.12 ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 159.844 138.890 179.262 1.00 19.39 ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 159.373 138.789 177.852 1.00 18.85 ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 157.988 139.372 177.829 1.00 17.81 ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 160.069 142.166 178.647 1.00 22.85 ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 160.999 143.263 178.419 1.00 23.24 ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 160.448 144.611 178.862 1.00 23.56 ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 161.057 145.643 178.566 1.00 26.95 ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 161.384 143.328 176.939 1.00 24.30 ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 160.320 143.932 176.195 1.00 23.43 ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 161.649 141.933 176.394 1.00 25.42 ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 159.312 144.631 179.559 1.00 22.19 ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 158.711 145.893 179.967 1.00 25.08 ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 159.552 146.533 181.064 1.00 25.55 ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 160.107 145.848 181.934 1.00 26.88 ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 157.256 145.675 180.420 1.00 24.54 ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 157.198 144.809 181.666 1.00 23.64 ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 156.562 147.008 180.659 1.00 24.82 ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 159.673 147.854 181.008 1.00 26.79 ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 160.385 148.625 182.016 1.00 27.32 ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 159.387 149.228 182.994 1.00 25.49 ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 158.286 149.629 182.604 1.00 25.95 ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 161.223 149.729 181.370 1.00 27.75 ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 162.343 150.259 182.249 1.00 29.18 ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 163.524 149.313 182.318 1.00 35.97 ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 164.006 148.880 181.249 1.00 33.61 ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 163.972 148.999 183.442 1.00 34.48 ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 159.775 149.288 184.265 1.00 16.91 ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 158.884 149.809 185.284 1.00 17.79 ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 159.551 150.949 186.045 1.00 21.41 ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 160.768 150.925 186.256 1.00 26.36 ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 158.476 148.708 186.272 1.00 16.81 ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 157.474 147.737 185.721 1.00 19.23 ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 156.217 148.163 185.334 1.00 18.54 ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 157.789 146.396 185.593 1.00 17.55 ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 155.294 147.272 184.827 1.00 17.27 ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 156.870 145.499 185.088 1.00 15.90 ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 155.623 145.938 184.704 1.00 17.03 ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 158.784 151.959 186.465 1.00 15.71 ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 159.374 153.040 187.247 1.00 14.64 ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 159.796 152.545 188.616 1.00 15.70 ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 159.254 151.549 189.126 1.00 16.75 ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 158.232 154.068 187.345 1.00 16.34 ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 156.993 153.269 187.157 1.00 17.30 ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 157.354 152.179 186.196 1.00 15.28 ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 160.772 153.201 189.251 1.00 16.01 ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 161.251 152.718 190.556 1.00 13.83 ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 160.173 152.655 191.623 1.00 13.22 ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 160.217 151.765 192.480 1.00 16.27 ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 162.346 153.729 190.923 1.00 12.79 ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 162.769 154.325 189.624 1.00 15.93 ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 161.534 154.371 188.780 1.00 17.52 ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 159.207 153.575 191.603 1.00 8.44  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 158.152 153.555 192.612 1.00 11.39 ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 157.262 152.324 192.467 1.00 13.97 ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 156.895 151.695 193.467 1.00 17.92 ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 157.338 154.847 192.543 1.00 10.41 ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 156.640 155.039 191.209 1.00 19.59 ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 156.818 154.197 190.303 1.00 20.97 ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 155.908 156.040 191.064 1.00 22.21 ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 156.907 151.961 191.232 1.00 11.67 ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 156.124 150.748 191.024 1.00 8.95  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 156.921 149.510 191.413 1.00 10.59 ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 156.370 148.573 192.001 1.00 18.30 ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 155.659 150.654 189.572 1.00 12.40 ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 154.734 149.478 189.256 1.00 11.80 ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 153.606 149.388 190.271 1.00 7.32  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 154.177 149.597 187.851 1.00 15.18 ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 158.217 149.487 191.094 1.00 7.43  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 159.063 148.376 191.518 1.00 7.00  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 159.105 148.272 193.035 1.00 9.62  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 159.184 147.169 193.589 1.00 14.13 ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 160.473 148.542 190.954 1.00 9.53  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 160.562 148.630 189.157 1.00 23.51 ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 159.061 149.413 193.725 1.00 5.99  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 159.043 149.398 195.182 1.00 5.25  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 157.704 148.920 195.726 1.00 7.04  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 157.665 148.255 196.766 1.00 10.94 ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 159.358 150.791 195.724 1.00 8.23  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 158.284 151.683 195.491 1.00 8.88  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 156.604 149.244 195.047 1.00 5.20  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 155.280 148.953 195.586 1.00 3.35  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 154.871 147.491 195.451 1.00 4.34  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 153.935 147.065 196.135 1.00 8.09  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 154.233 149.835 194.904 1.00 6.08  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 153.945 151.126 195.644 1.00 10.48 ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 152.861 151.924 194.951 1.00 11.32 ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 153.412 152.926 194.047 1.00 13.58 ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 153.737 154.159 194.409 1.00 13.93 ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 153.599 154.572 195.658 1.00 8.43  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 154.211 155.000 193.495 1.00 13.40 ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 155.536 146.714 194.596 1.00 4.69  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 155.145 145.334 194.339 1.00 2.61  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 156.363 144.429 194.445 1.00 6.32  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 157.509 144.869 194.337 1.00 10.54 ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 154.487 145.162 192.953 1.00 3.89  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 153.196 145.957 192.865 1.00 6.55  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 155.455 145.571 191.863 1.00 2.93  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 156.096 143.144 194.660 1.00 4.56  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 157.119 142.110 194.592 1.00 5.94  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 156.996 141.387 193.257 1.00 4.85  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 155.907 140.951 192.876 1.00 7.45  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 157.007 141.127 195.762 1.00 5.58  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 157.994 140.098 195.624 1.00 13.49 ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 155.626 140.496 195.836 1.00 2.54  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 158.105 141.297 192.532 1.00 3.04  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 158.078 140.736 191.191 1.00 0.81  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 158.115 139.216 191.242 1.00 6.69  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 158.809 138.622 192.070 1.00 16.76 ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 159.255 141.263 190.373 1.00 4.89  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 159.061 142.664 189.877 1.00 3.03  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 158.345 142.907 188.722 1.00 7.31  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 159.581 143.736 190.575 1.00 6.84  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 158.160 144.194 188.265 1.00 10.50 ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 159.399 145.024 190.124 1.00 8.56  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 158.687 145.254 188.969 1.00 7.87  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 157.347 138.588 190.355 1.00 6.68  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 157.326 137.138 190.198 1.00 5.94  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 157.497 136.877 188.707 1.00 6.72  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 156.538 136.996 187.937 1.00 9.85  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 156.037 136.505 190.730 1.00 1.61  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 156.114 135.002 190.625 1.00 2.70  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 155.792 136.921 192.170 1.00 4.19  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 158.710 136.528 188.296 1.00 4.22  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 159.050 136.366 186.888 1.00 4.35  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 158.926 134.897 186.505 1.00 8.06  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 159.599 134.040 187.089 1.00 10.85 ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 160.463 136.879 186.615 1.00 5.73  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 160.660 137.307 185.178 1.00 5.55  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 159.851 136.995 184.307 1.00 9.56  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 161.744 138.027 184.922 1.00 3.96  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 158.072 134.611 185.526 1.00 5.45  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 157.875 133.255 185.017 1.00 4.50  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 158.679 133.119 183.730 1.00 10.32 ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 158.162 133.299 182.628 1.00 18.07 ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 156.396 132.967 184.788 1.00 4.46  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 155.645 132.607 186.037 1.00 6.51  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 155.215 133.588 186.910 1.00 6.90  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 155.360 131.284 186.329 1.00 6.65  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 154.520 133.256 188.056 1.00 6.78  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 154.665 130.948 187.471 1.00 4.41  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 154.244 131.934 188.335 1.00 5.21  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 159.959 132.794 183.876 1.00 7.91  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 160.855 132.615 182.743 1.00 4.23  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 160.946 131.140 182.375 1.00 4.48  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 160.670 130.257 183.190 1.00 7.91  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 162.251 133.158 183.055 1.00 6.50  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 162.790 132.480 184.195 1.00 10.36 ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 162.192 134.648 183.338 1.00 5.55  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 161.331 130.882 181.129 1.00 5.72  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 161.469 129.523 180.623 1.00 6.86  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 162.888 129.047 180.902 1.00 6.95  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 163.861 129.679 180.478 1.00 10.30 ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 161.150 129.450 179.123 1.00 7.07  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 161.274 128.022 178.626 1.00 6.73  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 159.758 129.993 178.850 1.00 12.63 ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 163.006 127.936 181.619 1.00 9.27  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 164.291 127.339 181.945 1.00 10.40 ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 164.572 126.158 181.025 1.00 10.05 ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 163.664 125.566 180.437 1.00 11.37 ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 164.329 126.889 183.407 1.00 9.10  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 163.346 125.868 183.619 1.00 10.04 ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 164.037 128.061 184.328 1.00 6.12  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 165.859 125.825 180.900 1.00 8.17  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 166.263 124.760 179.986 1.00 6.88  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 165.692 123.413 180.411 1.00 9.71  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 165.238 122.633 179.568 1.00 15.26 ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 167.787 124.694 179.899 1.00 7.21  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 168.401 125.844 179.122 1.00 7.87  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 169.914 125.765 179.089 1.00 10.72 ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 170.470 126.597 178.030 1.00 11.18 ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 170.603 126.215 176.766 1.00 14.71 ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 170.232 125.009 176.368 1.00 13.15 ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 171.120 127.062 175.883 1.00 10.07 ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 165.710 123.119 181.712 1.00 6.95  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 165.208 121.833 182.186 1.00 9.77  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 163.705 121.702 181.964 1.00 10.70 ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 163.226 120.646 181.532 1.00 13.08 ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 165.551 121.649 183.663 1.00 14.45 ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 164.864 122.592 184.467 1.00 20.48 ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 162.947 122.762 182.254 1.00 6.78  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 161.501 122.709 182.064 1.00 13.30 ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 161.145 122.544 180.593 1.00 13.42 ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 160.250 121.764 180.248 1.00 14.56 ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 160.851 123.968 182.636 1.00 13.29 ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 161.264 125.122 181.926 1.00 12.51 ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 161.834 123.270 179.711 1.00 7.25  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 161.572 123.135 178.282 1.00 7.01  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 161.970 121.756 177.773 1.00 10.57 ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 161.283 121.184 176.919 1.00 16.45 ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 162.307 124.224 177.507 1.00 9.02  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 161.995 124.246 176.013 1.00 9.06  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 160.515 124.489 175.774 1.00 6.02  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 162.829 125.293 175.327 1.00 7.07  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 163.081 121.212 178.274 1.00 7.22  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 163.469 119.857 177.899 1.00 4.42  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 162.405 118.853 178.312 1.00 11.32 ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 162.054 117.955 177.540 1.00 16.63 ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 164.811 119.496 178.530 1.00 4.46  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 166.017 119.998 177.768 1.00 8.16  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 167.305 119.824 178.542 1.00 13.42 ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 167.410 118.951 179.402 1.00 13.79 ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 168.295 120.655 178.239 1.00 14.64 ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 161.877 118.992 179.530 1.00 9.85  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 160.817 118.097 179.979 1.00 10.82 ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 159.566 118.248 179.123 1.00 12.17 ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 158.928 117.253 178.760 1.00 12.51 ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 160.496 118.359 181.451 1.00 13.73 ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 159.488 117.483 181.917 1.00 18.42 ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 159.205 119.489 178.783 1.00 11.16 ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 158.034 119.725 177.946 1.00 9.26  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 158.191 119.065 176.583 1.00 11.33 ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 157.276 118.388 176.096 1.00 14.91 ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 157.805 121.228 177.779 1.00 7.18  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 157.225 121.925 178.989 1.00 11.31 ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 157.088 123.417 178.775 1.00 16.53 ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 157.483 124.217 179.622 1.00 19.66 ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 156.532 123.800 177.632 1.00 9.16  ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 159.351 119.249 175.953 1.00 11.67 ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 159.574 118.689 174.626 1.00 8.27  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 159.640 117.167 174.668 1.00 9.34  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 159.135 116.495 173.762 1.00 15.31 ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 160.846 119.276 174.019 1.00 8.08  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 160.773 121.063 173.767 1.00 14.37 ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 160.259 116.605 175.709 1.00 8.87  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 160.306 115.155 175.842 1.00 14.05 ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 158.909 114.576 176.025 1.00 16.21 ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 158.567 113.556 175.414 1.00 16.44 ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 161.212 114.765 177.008 1.00 11.43 ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 161.306 113.276 177.343 1.00 13.39 ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 162.034 112.526 176.245 1.00 15.14 ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 162.006 113.080 178.675 1.00 15.72 ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 158.081 115.217 176.854 1.00 15.84 ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 156.714 114.745 177.034 1.00 16.37 ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 155.912 114.869 175.744 1.00 17.08 ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 155.113 113.985 175.414 1.00 23.29 ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 156.036 115.514 178.166 1.00 17.66 ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 156.690 115.265 179.509 1.00 20.74 ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 157.338 114.238 179.717 1.00 20.51 ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 156.525 116.204 180.431 1.00 18.70 ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 156.114 115.959 175.000 1.00 15.13 ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 155.395 116.136 173.742 1.00 13.56 ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 155.786 115.073 172.723 1.00 15.44 ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 154.920 114.509 172.040 1.00 17.95 ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 155.652 117.535 173.185 1.00 13.53 ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 154.751 117.916 172.022 1.00 18.50 ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 153.279 117.813 172.365 1.00 25.50 ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 152.874 118.342 173.422 1.00 24.33 ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 152.524 117.204 171.578 1.00 24.43 ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 157.082 114.776 172.608 1.00 16.56 ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 157.503 113.763 171.644 1.00 16.34 ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 157.073 112.372 172.098 1.00 16.64 ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 156.789 111.506 171.264 1.00 20.02 ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 159.020 113.839 171.381 1.00 13.11 ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 159.819 113.305 172.554 1.00 17.79 ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 159.367 113.079 170.111 1.00 12.33 ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 157.014 112.126 173.411 1.00 15.52 ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 156.474 110.858 173.887 1.00 18.80 ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 154.997 110.727 173.544 1.00 20.08 ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 154.546 109.661 173.112 1.00 24.45 ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 156.685 110.724 175.393 1.00 23.01 ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 158.071 110.285 175.860 1.00 23.27 ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 158.142 110.331 177.375 1.00 23.38 ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 158.389 108.893 175.343 1.00 20.20 ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 154.230 111.802 173.730 1.00 22.72 ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 152.808 111.765 173.407 1.00 22.76 ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 152.589 111.568 171.913 1.00 23.69 ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 151.658 110.865 171.501 1.00 24.14 ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 152.135 113.050 173.889 1.00 21.19 ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 150.645 113.121 173.612 1.00 22.80 ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 150.164 114.565 173.566 1.00 26.05 ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 150.601 115.337 174.801 1.00 26.19 ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 149.952 114.824 176.040 1.00 26.24 ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 153.438 112.179 171.085 1.00 23.09 ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 153.272 112.070 169.639 1.00 22.17 ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 153.706 110.699 169.132 1.00 24.70 ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 152.911 109.963 168.535 1.00 25.89 ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 154.063 113.176 168.940 1.00 19.24 ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 154.971 110.339 169.359 1.00 23.04 ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 155.522 109.133 168.748 1.00 21.73 ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 155.002 107.867 169.417 1.00 24.14 ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 154.654 106.898 168.733 1.00 33.06 ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 157.048 109.177 168.804 1.00 21.14 ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 157.677 110.014 167.708 1.00 21.24 ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 157.150 109.657 166.335 1.00 28.01 ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 157.398 108.521 165.880 1.00 29.83 ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 156.480 110.508 165.714 1.00 27.73 ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 154.942 107.849 170.747 1.00 24.14 ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 154.621 106.641 171.509 1.00 27.60 ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 153.511 106.954 172.503 1.00 27.87 ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 153.747 107.040 173.714 1.00 29.76 ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 155.867 106.108 172.216 1.00 24.54 ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 156.939 105.604 171.261 1.00 23.74 ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 158.175 105.136 172.003 1.00 26.09 ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 157.898 103.977 172.843 1.00 33.21 ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 157.963 102.719 172.428 1.00 30.62 ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 158.308 102.420 171.187 1.00 29.43 ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 157.677 101.740 173.279 1.00 27.91 ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 152.278 107.125 172.019 1.00 29.68 ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 151.195 107.577 172.912 1.00 31.11 ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 150.907 106.635 174.067 1.00 32.84 ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 150.551 107.103 175.156 1.00 34.30 ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 149.992 107.696 171.965 1.00 31.96 ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 150.309 106.784 170.828 1.00 31.14 ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 151.796 106.844 170.657 1.00 29.22 ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 151.042 105.321 173.868 1.00 34.78 ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 150.781 104.382 174.954 1.00 32.95 ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 151.778 104.564 176.093 1.00 36.94 ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 151.405 104.507 177.272 1.00 37.29 ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 150.816 102.947 174.431 1.00 32.39 ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 152.103 102.621 173.701 1.00 34.92 ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 152.292 103.122 172.573 1.00 37.13 ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 152.927 101.865 174.256 1.00 34.49 ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 153.051 104.788 175.761 1.00 35.65 ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 154.062 104.997 176.791 1.00 31.87 ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 153.782 106.279 177.565 1.00 33.06 ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 153.931 106.323 178.791 1.00 37.37 ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 155.468 105.004 176.165 1.00 32.76 ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 156.521 105.260 177.229 1.00 33.50 ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 155.733 103.689 175.455 1.00 30.82 ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 153.375 107.343 176.868 1.00 30.95 ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 153.045 108.590 177.553 1.00 31.17 ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 151.831 108.421 178.459 1.00 36.27 ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 151.796 108.961 179.573 1.00 39.67 ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 152.802 109.701 176.534 1.00 31.73 ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 152.356 110.996 177.181 1.00 35.92 ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 153.170 111.615 177.899 1.00 36.55 ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 151.191 111.395 176.974 1.00 36.62 ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 150.816 107.688 177.992 1.00 38.05 ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 149.647 107.428 178.827 1.00 37.42 ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 150.031 106.641 180.073 1.00 37.08 ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 149.571 106.949 181.181 1.00 38.55 ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 148.591 106.674 178.021 1.00 36.51 ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 147.331 106.343 178.798 1.00 38.78 ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 146.299 105.629 177.948 1.00 41.42 ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 146.586 105.368 176.761 1.00 40.53 ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 145.203 105.329 178.466 1.00 40.27 ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 150.882 105.626 179.910 1.00 35.04 ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 151.364 104.870 181.059 1.00 36.06 ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 152.136 105.766 182.016 1.00 36.35 ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 151.975 105.666 183.236 1.00 39.40 ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 152.235 103.705 180.589 1.00 36.59 ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 152.781 102.841 181.713 1.00 38.62 ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 153.902 101.938 181.224 1.00 37.07 ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 153.512 101.204 179.956 1.00 37.49 ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 152.301 100.362 180.148 1.00 38.72 ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 152.977 106.652 181.481 1.00 34.40 ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 153.755 107.547 182.331 1.00 35.66 ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 152.849 108.471 183.134 1.00 38.64 ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 153.067 108.680 184.333 1.00 40.83 ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 154.732 108.355 181.480 1.00 35.60 ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 155.689 109.221 182.276 1.00 38.54 ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 156.457 110.159 181.363 1.00 36.40 ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 155.572 111.104 180.694 1.00 39.27 ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 155.063 112.188 181.267 1.00 40.06 ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 155.346 112.504 182.518 1.00 38.39 ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 154.252 112.972 180.563 1.00 37.69 ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 151.820 109.029 182.492 1.00 37.24 ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 150.893 109.906 183.205 1.00 36.81 ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 150.125 109.147 184.281 1.00 39.45 ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 149.954 109.643 185.405 1.00 40.61 ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 149.928 110.561 182.217 1.00 37.59 ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 150.615 111.432 181.334 1.00 38.20 ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 149.655 107.939 183.956 1.00 38.11 ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 148.932 107.141 184.943 1.00 36.44 ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 149.819 106.798 186.133 1.00 38.32 ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 149.378 106.870 187.286 1.00 39.59 ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 148.384 105.870 184.296 1.00 38.20 ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 147.343 106.162 183.235 1.00 41.96 ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 147.003 107.348 183.043 1.00 41.20 ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 146.862 105.206 182.593 1.00 42.33 ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 151.073 106.425 185.876 1.00 36.76 ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 151.994 106.127 186.969 1.00 37.51 ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 152.313 107.365 187.794 1.00 39.29 ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 152.476 107.270 189.013 1.00 41.41 ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 153.278 105.495 186.437 1.00 36.30 ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 153.319 103.991 186.157 1.00 40.31 ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 152.147 103.477 185.338 1.00 39.04 ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 154.627 103.684 185.464 1.00 39.47 ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 152.435 108.529 187.154 1.00 38.48 ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 152.665 109.754 187.914 1.00 40.59 ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 151.503 110.031 188.859 1.00 39.66 ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 151.705 110.350 190.040 1.00 40.19 ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 152.881 110.930 186.965 1.00 39.92 ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 154.306 111.146 186.456 1.00 37.91 ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 154.404 112.469 185.719 1.00 38.18 ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 155.285 111.110 187.618 1.00 39.09 ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 150.273 109.893 188.360 1.00 38.45 ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 149.106 110.092 189.217 1.00 39.13 ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 149.075 109.073 190.351 1.00 39.95 ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 148.805 109.423 191.509 1.00 39.03 ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 147.828 110.015 188.385 1.00 39.78 ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 146.556 109.922 189.209 1.00 39.87 ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 145.326 110.132 188.344 1.00 40.44 ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 145.304 111.530 187.746 1.00 42.15 ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 145.737 112.567 188.723 1.00 40.28 ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 149.359 107.806 190.036 1.00 38.61 ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 149.346 106.763 191.055 1.00 39.80 ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 150.407 107.009 192.119 1.00 39.88 ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 150.152 106.823 193.312 1.00 40.72 ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 149.549 105.394 190.405 1.00 39.44 ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 148.302 104.548 190.141 1.00 41.61 ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 147.264 105.333 189.353 1.00 39.94 ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 148.676 103.271 189.409 1.00 40.65 ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 151.605 107.425 191.706 1.00 38.23 ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 152.677 107.689 192.659 1.00 37.89 ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 152.348 108.884 193.543 1.00 38.93 ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 152.628 108.863 194.747 1.00 39.18 ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 153.995 107.914 191.918 1.00 38.40 ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 154.620 106.643 191.365 1.00 39.48 ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 155.869 106.914 190.550 1.00 42.05 ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 156.243 108.067 190.329 1.00 39.74 ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 156.525 105.850 190.100 1.00 41.65 ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 151.758 109.933 192.967 1.00 39.30 ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 151.331 111.056 193.787 1.00 38.45 ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 150.299 110.648 194.821 1.00 39.85 ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 150.395 111.016 195.999 1.00 40.80 ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 149.305 109.860 194.397 1.00 43.20 ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 148.290 109.388 195.332 1.00 41.25 ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 148.900 108.511 196.418 1.00 42.87 ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 148.518 108.603 197.589 1.00 45.73 ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 147.194 108.631 194.583 1.00 41.73 ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 146.346 109.507 193.677 1.00 43.34 ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 145.510 108.698 192.706 1.00 46.76 ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 145.618 107.454 192.719 1.00 46.97 ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 144.743 109.307 191.930 1.00 44.89 ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 149.848 107.646 196.047 1.00 41.00 ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 150.472 106.760 197.024 1.00 39.99 ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 151.301 107.541 198.036 1.00 43.21 ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 151.279 107.229 199.232 1.00 46.04 ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 151.335 105.721 196.307 1.00 42.74 ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 150.544 104.731 195.501 1.00 46.22 ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 149.186 104.566 195.718 1.00 45.90 ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 151.156 103.973 194.517 1.00 44.55 ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 148.455 103.658 194.976 1.00 44.21 ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 150.430 103.066 193.769 1.00 43.93 ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 149.079 102.907 194.000 1.00 44.02 ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 152.042 108.554 197.578 1.00 41.36 ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 152.795 109.390 198.509 1.00 40.06 ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 151.861 110.141 199.449 1.00 39.18 ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 152.130 110.248 200.654 1.00 40.12 ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 153.685 110.365 197.740 1.00 40.76 ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 154.790 109.697 196.940 1.00 41.97 ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 155.610 108.732 197.771 1.00 42.15 ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 156.283 109.129 198.721 1.00 40.96 ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 155.556 107.452 197.418 1.00 40.62 ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 150.751 110.664 198.918 1.00 37.69 ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 149.772 111.334 199.768 1.00 37.71 ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 149.203 110.381 200.810 1.00 37.76 ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 149.052 110.745 201.983 1.00 41.29 ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 148.651 111.920 198.910 1.00 37.45 ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 147.391 112.391 199.638 1.00 38.91 ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 147.715 113.493 200.634 1.00 38.56 ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 146.337 112.852 198.644 1.00 38.66 ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 148.879 109.154 200.400 1.00 37.55 ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 148.300 108.185 201.324 1.00 39.59 ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 149.317 107.794 202.393 1.00 38.28 ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 148.968 107.643 203.567 1.00 38.36 ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 147.805 106.967 200.530 1.00 41.07 ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 147.479 105.673 201.288 1.00 41.79 ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 146.731 105.886 202.605 1.00 43.49 ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 145.560 106.742 202.454 1.00 43.68 ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 144.552 106.792 203.316 1.00 42.24 ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 144.528 106.027 204.395 1.00 41.10 ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 143.546 107.630 203.089 1.00 40.49 ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 150.588 107.644 202.006 1.00 37.86 ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 151.631 107.345 202.983 1.00 38.09 ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 151.776 108.468 204.002 1.00 40.85 ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 151.911 108.213 205.207 1.00 42.76 ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 152.962 107.100 202.270 1.00 37.56 ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 153.309 105.666 201.868 1.00 39.23 ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 154.764 105.575 201.432 1.00 40.28 ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 153.034 104.708 203.014 1.00 38.40 ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 151.759 109.720 203.536 1.00 39.02 ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 151.834 110.849 204.460 1.00 37.42 ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 150.638 110.868 205.402 1.00 38.51 ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 150.785 111.113 206.607 1.00 39.29 ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 151.919 112.160 203.678 1.00 37.10 ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 153.288 112.447 203.092 1.00 38.11 ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 153.353 113.856 202.528 1.00 36.58 ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 152.961 113.895 201.123 1.00 36.71 ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 151.819 114.399 200.679 1.00 37.07 ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 150.922 114.914 201.505 1.00 36.61 ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 151.569 114.386 199.373 1.00 36.58 ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 149.441 110.608 204.866 1.00 39.35 ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 148.247 110.572 205.703 1.00 39.12 ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 148.339 109.469 206.747 1.00 41.71 ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 147.948 109.667 207.901 1.00 41.04 ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 147.003 110.385 204.833 1.00 39.68 ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 146.626 111.611 204.018 1.00 41.06 ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 145.331 111.424 203.253 1.00 41.96 ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 145.178 110.475 202.487 1.00 42.89 ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 144.387 112.336 203.459 1.00 40.25 ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 148.852 108.299 206.361 1.00 45.10 ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 148.997 107.202 207.316 1.00 44.35 ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 149.996 107.548 208.410 1.00 43.68 ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 149.767 107.245 209.586 1.00 44.97 ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 149.420 105.923 206.596 1.00 42.68 ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 148.382 105.279 205.678 1.00 43.32 ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 148.836 103.898 205.248 1.00 44.79 ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 147.025 105.210 206.356 1.00 41.68 ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 151.119 108.171 208.043 1.00 44.22 ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 152.098 108.566 209.053 1.00 45.54 ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 151.495 109.562 210.034 1.00 47.80 ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 151.641 109.421 211.257 1.00 49.70 ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 153.339 109.153 208.381 1.00 45.64 ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 154.407 109.619 209.360 1.00 46.56 ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 155.066 108.467 210.095 1.00 49.77 ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 155.151 107.363 209.516 1.00 49.93 ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 155.498 108.662 211.250 1.00 50.27 ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 150.793 110.574 209.512 1.00 44.73 ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 150.173 111.567 210.384 1.00 43.77 ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 149.113 110.934 211.277 1.00 44.04 ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 149.024 111.252 212.469 1.00 45.35 ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 149.571 112.696 209.550 1.00 41.95 ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 148.671 113.636 210.336 1.00 42.19 ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 148.124 114.746 209.454 1.00 43.45 ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 149.247 115.588 208.868 1.00 43.73 ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 148.728 116.727 208.060 1.00 43.37 ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 148.301 110.032 210.721 1.00 43.00 ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 147.251 109.385 211.501 1.00 43.90 ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 147.836 108.506 212.599 1.00 45.44 ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 147.321 108.488 213.721 1.00 45.30 ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 146.343 108.569 210.583 1.00 43.41 ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 146.958 107.347 210.213 1.00 45.19 ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 148.903 107.765 212.296 1.00 43.57 ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 149.540 106.936 213.314 1.00 44.39 ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 150.141 107.793 214.422 1.00 48.24 ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 150.003 107.470 215.611 1.00 49.82 ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 150.607 106.052 212.666 1.00 44.27 ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 151.141 104.856 213.457 1.00 46.33 ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 151.442 103.701 212.516 1.00 47.50 ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 152.387 105.235 214.231 1.00 44.53 ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 150.802 108.894 214.052 1.00 48.59 ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 151.353 109.790 215.062 1.00 49.09 ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 150.250 110.374 215.937 1.00 47.15 ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 150.386 110.433 217.164 1.00 45.22 ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 152.158 110.903 214.393 1.00 47.11 ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 153.087 111.709 215.302 1.00 48.65 ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 153.913 110.784 216.181 1.00 46.78 ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 153.987 112.615 214.477 1.00 48.73 ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 149.141 110.794 215.324 1.00 46.14 ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 148.030 111.346 216.093 1.00 46.81 ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 147.419 110.297 217.011 1.00 48.66 ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 147.064 110.595 218.159 1.00 50.28 ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 146.976 111.920 215.146 1.00 45.91 ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 145.616 112.147 215.785 1.00 47.31 ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 144.492 112.152 214.771 1.00 49.13 ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 144.470 112.974 213.855 1.00 48.82 ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 143.548 111.230 214.928 1.00 48.55 ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 147.282 109.061 216.525 1.00 48.80 ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 146.718 107.996 217.345 1.00 48.73 ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 147.591 107.713 218.559 1.00 49.06 ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 147.080 107.532 219.670 1.00 48.61 ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 146.531 106.730 216.508 1.00 46.37 ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 148.912 107.672 218.372 1.00 48.50 ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 149.787 107.467 219.523 1.00 50.52 ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 149.882 108.700 220.412 1.00 51.78 ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 150.259 108.573 221.582 1.00 52.27 ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 151.182 107.033 219.075 1.00 51.34 ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 151.229 105.660 218.410 1.00 51.15 ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 152.613 105.364 217.876 1.00 50.64 ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 150.804 104.595 219.402 1.00 49.65 ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 149.566 109.886 219.892 1.00 52.42 ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 149.524 111.067 220.749 1.00 53.22 ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 148.261 111.121 221.599 1.00 52.80 ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 148.317 111.557 222.754 1.00 53.97 ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 149.638 112.339 219.907 1.00 51.30 ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 151.001 112.495 219.268 1.00 53.77 ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 152.003 112.007 219.789 1.00 52.28 ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 151.045 113.178 218.130 1.00 52.38 ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 147.124 110.689 221.059 1.00 52.57 ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 145.846 110.800 221.751 1.00 53.93 ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 145.490 109.565 222.570 1.00 53.75 ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 144.452 109.569 223.242 1.00 53.04 ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 144.723 111.087 220.748 1.00 53.16 ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 144.976 112.285 219.848 1.00 54.04 ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 145.560 113.466 220.597 1.00 55.49 ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 144.894 113.972 221.526 1.00 55.17 ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 146.684 113.890 220.258 1.00 53.05 ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 146.307 108.512 222.534 1.00 53.68 ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 146.019 107.327 223.331 1.00 54.48 ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 146.260 107.632 224.804 1.00 54.73 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 147.246 108.284 225.173 1.00 54.55 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 146.859 106.129 222.852 1.00 55.80 ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 148.346 106.427 222.954 1.00 55.07 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 146.506 104.876 223.641 1.00 54.81 ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 145.341 107.182 225.653 1.00 55.24 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 145.400 107.436 227.085 1.00 56.03 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 145.839 106.176 227.816 1.00 55.87 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 145.271 105.099 227.615 1.00 55.80 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 144.042 107.903 227.616 1.00 53.87 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 143.362 108.956 226.755 1.00 53.28 ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 144.240 110.185 226.577 1.00 54.87 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 144.454 110.912 227.895 1.00 54.56 ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 145.314 112.117 227.732 1.00 54.08 ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 146.850 106.318 228.669 1.00 55.38 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 147.371 105.192 229.416 1.00 56.00 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 148.371 104.369 228.631 1.00 57.04 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 149.463 104.847 228.308 1.00 55.20 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 148.009 103.127 228.318 1.00 65.35 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 148.876 102.222 227.580 1.00 65.77 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 148.120 101.656 226.385 1.00 66.05 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 146.887 101.610 226.368 1.00 65.85 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 149.393 101.083 228.472 1.00 65.78 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 149.865 101.542 229.845 1.00 64.63 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 149.901 100.397 230.845 1.00 64.96 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 148.599 99.764  231.023 1.00 67.13 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 148.357 98.787  231.885 1.00 65.59 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 149.307 98.307  232.671 1.00 63.73 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 147.131 98.277  231.960 1.00 64.96 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 148.884 101.231 225.377 1.00 63.12 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 148.279 100.694 224.161 1.00 64.63 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 147.565 99.379  224.449 1.00 63.94 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 146.512 99.089  223.870 1.00 61.65 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 149.344 100.534 223.061 1.00 63.01 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 150.124 101.838 222.881 1.00 62.15 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 148.700 100.115 221.749 1.00 62.28 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 151.192 101.768 221.814 1.00 61.23 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 148.123 98.562  225.347 1.00 64.64 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 147.500 97.283  225.673 1.00 64.96 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 146.147 97.468  226.347 1.00 65.11 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 145.293 96.576  226.275 1.00 65.49 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 148.423 96.459  226.573 1.00 65.33 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 149.768 95.998  226.006 1.00 64.29 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 150.855 97.021  226.285 1.00 63.51 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 150.145 94.648  226.587 1.00 62.59 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 145.932 98.608  227.007 1.00 66.93 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 144.681 98.827  227.726 1.00 67.67 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 143.487 98.852  226.781 1.00 67.57 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 142.437 98.271  227.080 1.00 67.94 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 144.757 100.129 228.525 1.00 68.00 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 145.629 100.007 229.756 1.00 68.41 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 145.435 99.045  230.528 1.00 68.03 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 146.506 100.873 229.953 1.00 66.94 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 143.624 99.517  225.638 1.00 61.70 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 142.537 99.673  224.678 1.00 62.61 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 142.848 98.829  223.447 1.00 62.43 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 143.870 99.039  222.784 1.00 61.89 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 142.347 101.141 224.305 1.00 63.24 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 141.090 101.379 223.494 1.00 62.48 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 139.988 101.076 223.998 1.00 61.78 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 141.204 101.868 222.351 1.00 61.25 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 141.965 97.876  223.144 1.00 61.53 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 142.146 97.041  221.962 1.00 62.14 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 141.822 97.784  220.673 1.00 61.09 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 142.336 97.413  219.613 1.00 60.77 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 141.283 95.783  222.069 1.00 61.19 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 141.808 94.804  223.100 1.00 61.99 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 142.878 95.073  223.686 1.00 62.05 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 141.151 93.766  223.324 1.00 60.21 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 140.976 98.816  220.740 1.00 57.11 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 140.668 99.598  219.547 1.00 59.10 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 141.912 100.302 219.018 1.00 58.26 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 142.135 100.358 217.803 1.00 56.54 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 139.566 100.612 219.853 1.00 57.33 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 138.437 99.936  220.419 1.00 56.22 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 139.132 101.328 218.583 1.00 57.11 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 142.738 100.840 219.918 1.00 56.27 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 143.996 101.458 219.508 1.00 57.91 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 144.897 100.429 218.837 1.00 58.72 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 145.547 100.715 217.823 1.00 59.28 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 144.683 102.119 220.717 1.00 58.35 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 143.942 103.395 221.120 1.00 57.28 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 146.141 102.428 220.410 1.00 57.34 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 144.013 104.498 220.088 1.00 56.03 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 144.947 99.215  219.390 1.00 56.38 ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 145.763 98.152  218.810 1.00 57.85 ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 145.288 97.826  217.398 1.00 57.02 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 146.090 97.689  216.466 1.00 55.76 ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 145.733 96.907  219.714 1.00 57.44 ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 146.492 97.171  221.015 1.00 57.12 ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 146.297 95.697  218.984 1.00 56.69 ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 146.519 95.987  221.957 1.00 56.62 ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 143.970 97.692  217.225 1.00 54.76 ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 143.426 97.378  215.907 1.00 56.85 ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 143.708 98.496  214.912 1.00 56.22 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 144.053 98.231  213.754 1.00 54.81 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 141.922 97.118  216.004 1.00 56.98 ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 141.282 98.229  216.645 1.00 55.43 ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 141.651 95.851  216.799 1.00 55.35 ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 143.562 99.751  215.342 1.00 55.38 ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 143.852 100.870 214.451 1.00 56.22 ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 145.320 100.885 214.046 1.00 55.92 ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 145.644 101.120 212.876 1.00 56.50 ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 143.469 102.196 215.109 1.00 56.63 ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 144.088 102.290 216.398 1.00 56.72 ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 141.959 102.303 215.259 1.00 54.10 ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 146.225 100.636 214.996 1.00 55.08 ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 147.646 100.601 214.668 1.00 57.44 ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 147.959 99.476  213.687 1.00 57.38 ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 148.724 99.669  212.732 1.00 56.30 ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 148.479 100.443 215.940 1.00 57.04 ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 148.511 101.622 216.914 1.00 57.60 ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 149.663 101.464 217.893 1.00 54.77 ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 148.615 102.943 216.169 1.00 56.14 ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 147.375 98.296  213.906 1.00 57.75 ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 147.612 97.177  212.997 1.00 57.97 ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 147.088 97.482  211.598 1.00 59.11 ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 147.759 97.193  210.599 1.00 59.36 ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 146.967 95.907  213.548 1.00 57.54 ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 147.649 95.352  214.790 1.00 58.15 ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 146.785 94.351  215.530 1.00 60.02 ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 145.649 94.707  215.906 1.00 59.11 ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 147.242 93.206  215.735 1.00 59.76 ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 145.892 98.069  211.507 1.00 57.23 ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 145.341 98.426  210.204 1.00 57.10 ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 146.202 99.471  209.508 1.00 56.40 ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 146.446 99.379  208.299 1.00 56.22 ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 143.907 98.932  210.361 1.00 54.25 ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 142.974 97.876  210.915 1.00 56.51 ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 143.391 96.755  211.206 1.00 55.46 ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 141.703 98.228  211.064 1.00 57.27 ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 146.670 100.475 210.255 1.00 51.99 ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 147.517 101.505 209.665 1.00 53.65 ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 148.821 100.915 209.148 1.00 54.46 ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 149.277 101.266 208.054 1.00 54.42 ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 147.793 102.608 210.686 1.00 52.80 ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 146.611 103.520 211.029 1.00 53.30 ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 147.013 104.557 212.064 1.00 51.33 ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 146.065 104.187 209.778 1.00 51.45 ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 149.433 100.009 209.914 1.00 55.80 ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 150.680 99.396  209.466 1.00 55.38 ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 150.461 98.511  208.243 1.00 56.24 ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 151.283 98.510  207.316 1.00 57.34 ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 151.314 98.605  210.607 1.00 54.00 ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 152.161 99.456  211.541 1.00 56.40 ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 153.388 100.014 210.831 1.00 56.50 ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 154.162 98.922  210.107 1.00 56.02 ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 155.459 99.415  209.571 1.00 56.97 ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 149.365 97.747  208.219 1.00 56.67 ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 149.072 96.921  207.053 1.00 57.91 ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 148.849 97.777  205.813 1.00 58.97 ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 149.354 97.460  204.726 1.00 59.14 ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 147.849 96.044  207.326 1.00 58.69 ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 147.513 95.078  206.201 1.00 59.61 ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 146.233 94.310  206.494 1.00 59.42 ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 146.216 93.758  207.843 1.00 61.71 ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 145.328 94.083  208.774 1.00 60.66 ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 144.365 94.956  208.534 1.00 58.72 ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 145.410 93.516  209.974 1.00 58.38 ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 148.101 98.875  205.958 1.00 50.12 ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 147.877 99.769  204.828 1.00 49.56 ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 149.180 100.410 204.372 1.00 49.19 ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 149.407 100.580 203.169 1.00 50.67 ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 146.847 100.835 205.203 1.00 48.88 ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 146.062 101.379 204.021 1.00 48.75 ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 144.866 102.211 204.447 1.00 51.25 ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 144.670 102.397 205.665 1.00 52.82 ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 144.121 102.678 203.560 1.00 49.34 ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 150.050 100.770 205.320 1.00 47.00 ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 151.346 101.333 204.960 1.00 47.63 ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 152.173 100.337 204.161 1.00 48.47 ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 152.790 100.701 203.154 1.00 49.61 ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 152.097 101.770 206.217 1.00 45.88 ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 152.188 99.073  204.586 1.00 48.41 ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 152.939 98.055  203.855 1.00 49.26 ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 152.375 97.851  202.451 1.00 50.67 ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 153.131 97.734  201.477 1.00 49.87 ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 152.939 96.740  204.629 1.00 47.94 ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 151.046 97.803  202.329 1.00 50.51 ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 150.439 97.601  201.014 1.00 50.63 ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 150.744 98.768  200.081 1.00 51.16 ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 151.100 98.566  198.910 1.00 51.38 ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 148.931 97.408  201.155 1.00 49.64 ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 148.526 95.961  201.349 1.00 53.35 ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 149.142 95.046  200.312 1.00 55.51 ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 148.791 95.169  199.119 1.00 56.38 ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 149.985 94.207  200.687 1.00 51.77 ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 150.614 99.998  200.584 1.00 45.83 ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 150.917 101.167 199.767 1.00 45.83 ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 152.395 101.196 199.409 1.00 45.11 ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 152.763 101.580 198.294 1.00 47.71 ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 150.478 102.450 200.489 1.00 44.55 ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 150.952 103.685 199.727 1.00 43.54 ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 148.968 102.460 200.633 1.00 44.82 ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 153.264 100.762 200.321 1.00 42.30 ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 154.678 100.667 199.994 1.00 44.68 ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 154.911 99.708  198.834 1.00 47.58 ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 155.613 100.048 197.877 1.00 50.78 ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 155.462 100.210 201.224 1.00 46.22 ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 155.119 101.028 202.347 1.00 47.13 ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 156.947 100.308 200.967 1.00 44.81 ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 154.298 98.522  198.886 1.00 47.98 ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 154.466 97.544  197.808 1.00 48.54 ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 153.982 98.101  196.470 1.00 49.78 ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 154.644 97.933  195.429 1.00 48.09 ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 153.719 96.255  198.162 1.00 48.20 ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 153.526 95.299  197.003 1.00 48.92 ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 152.334 94.374  197.251 1.00 48.44 ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 151.060 94.960  196.842 1.00 50.25 ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 150.737 95.291  195.597 1.00 50.94 ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 151.552 95.049  194.583 1.00 49.84 ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 149.561 95.865  195.363 1.00 49.43 ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 152.828 98.773  196.483 1.00 47.52 ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 152.380 99.480  195.288 1.00 47.60 ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 153.425 100.488 194.828 1.00 48.28 ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 153.622 100.684 193.622 1.00 49.43 ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 151.045 100.175 195.557 1.00 46.02 ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 149.938 99.254  196.045 1.00 47.33 ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 148.879 100.031 196.813 1.00 49.25 ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 148.101 99.125  197.753 1.00 49.89 ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 147.484 99.898  198.862 1.00 49.46 ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 154.107 101.132 195.778 1.00 46.75 ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 155.132 102.112 195.427 1.00 45.46 ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 156.293 101.459 194.683 1.00 45.50 ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 156.759 101.990 193.670 1.00 47.10 ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 155.609 102.871 196.677 1.00 45.83 ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 156.875 103.643 196.367 1.00 45.47 ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 154.528 103.837 197.132 1.00 44.14 ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 156.793 100.312 195.168 1.00 44.92 ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 157.890 99.679  194.422 1.00 48.28 ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 157.436 99.208  193.043 1.00 49.39 ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 158.201 99.303  192.072 1.00 48.20 ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 158.593 98.504  195.137 1.00 46.89 ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 159.434 98.784  196.400 1.00 48.49 ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 158.638 98.841  197.668 1.00 50.68 ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 157.441 98.581  197.567 1.00 49.59 ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 159.193 99.165  198.737 1.00 50.28 ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 156.222 98.662  192.927 1.00 48.25 ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 155.811 98.212  191.596 1.00 47.69 ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 155.682 99.395  190.633 1.00 48.99 ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 156.132 99.322  189.479 1.00 49.86 ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 154.517 97.396  191.670 1.00 47.03 ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 153.221 98.178  191.782 1.00 48.02 ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 152.102 97.353  192.377 1.00 49.91 ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 152.384 96.236  192.857 1.00 50.98 ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 150.941 97.815  192.361 1.00 48.62 ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 155.116 100.512 191.102 1.00 46.94 ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 155.064 101.703 190.264 1.00 47.38 ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 156.460 102.210 189.945 1.00 47.59 ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 156.697 102.719 188.847 1.00 49.75 ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 154.242 102.801 190.938 1.00 48.66 ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 154.711 103.001 192.278 1.00 48.91 ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 152.771 102.418 190.971 1.00 46.76 ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 157.403 102.066 190.881 1.00 44.47 ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 158.773 102.498 190.635 1.00 45.92 ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 159.426 101.681 189.529 1.00 46.87 ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 160.138 102.232 188.685 1.00 48.24 ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 159.591 102.404 191.921 1.00 46.97 ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 159.291 103.532 192.885 1.00 50.74 ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 158.459 104.399 192.543 1.00 51.37 ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 159.885 103.552 193.982 1.00 50.81 ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 159.209 100.365 189.517 1.00 45.41 ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 159.833 99.551  188.473 1.00 45.83 ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 159.196 99.834  187.112 1.00 44.48 ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 159.894 99.907  186.087 1.00 44.12 ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 159.800 98.052  188.840 1.00 45.76 ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 158.399 97.455  188.701 1.00 45.48 ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 160.353 97.835  190.240 1.00 43.94 ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 158.348 95.957  188.905 1.00 44.73 ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 157.873 100.027 187.072 1.00 42.49 ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 157.256 100.361 185.790 1.00 42.51 ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 157.714 101.745 185.324 1.00 41.55 ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 157.925 101.979 184.125 1.00 43.08 ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 155.723 100.250 185.875 1.00 41.96 ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 155.109 100.390 184.491 1.00 41.06 ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 155.322 98.919  186.486 1.00 40.98 ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 157.910 102.673 186.263 1.00 44.07 ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 158.476 103.973 185.922 1.00 43.89 ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 159.899 103.842 185.399 1.00 44.31 ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 160.303 104.585 184.503 1.00 45.34 ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 158.438 104.903 187.134 1.00 43.14 ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 158.162 106.351 186.783 1.00 45.31 ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 156.609 106.598 185.909 1.00 53.25 ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 156.612 108.377 185.740 1.00 44.47 ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 160.684 102.926 185.970 1.00 43.30 ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 162.031 102.689 185.464 1.00 44.19 ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 161.988 102.218 184.017 1.00 43.49 ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 162.791 102.656 183.183 1.00 43.29 ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 162.752 101.668 186.344 1.00 43.93 ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 163.954 101.008 185.688 1.00 45.79 ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 164.235 99.624  186.240 1.00 46.42 ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 164.675 99.475  187.381 1.00 46.54 ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 163.975 98.600  185.434 1.00 43.57 ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 161.041 101.331 183.701 1.00 41.06 ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 160.838 100.937 182.308 1.00 41.08 ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 160.496 102.148 181.440 1.00 41.48 ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 161.005 102.291 180.317 1.00 41.81 ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 159.740 99.877  182.226 1.00 40.07 ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 159.587 99.207  180.868 1.00 42.05 ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 158.701 99.989  179.920 1.00 46.38 ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 157.733 100.620 180.393 1.00 46.51 ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 158.966 99.963  178.700 1.00 43.87 ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 159.640 103.035 181.952 1.00 39.16 ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 159.262 104.226 181.194 1.00 37.84 ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 160.476 105.113 180.928 1.00 38.85 ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 160.639 105.653 179.827 1.00 40.14 ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 158.145 104.993 181.931 1.00 41.63 ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 157.975 106.385 181.346 1.00 39.70 ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 156.840 104.220 181.852 1.00 40.77 ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 161.341 105.291 181.930 1.00 38.47 ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 162.551 106.090 181.726 1.00 39.11 ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 163.494 105.432 180.727 1.00 38.31 ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 164.156 106.125 179.943 1.00 38.90 ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 163.281 106.349 183.047 1.00 38.19 ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 162.397 106.628 184.241 1.00 39.83 ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 161.790 108.016 184.206 1.00 44.14 ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 162.503 108.966 183.824 1.00 43.88 ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 160.601 108.155 184.561 1.00 43.84 ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 163.596 104.100 180.755 1.00 35.40 ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 164.389 103.420 179.735 1.00 35.30 ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 163.848 103.712 178.342 1.00 35.02 ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 164.618 103.868 177.387 1.00 37.26 ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 164.425 101.910 179.985 1.00 38.64 ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 163.098 101.377 179.925 1.00 40.20 ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 165.057 101.597 181.333 1.00 39.58 ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 162.523 103.779 178.206 1.00 34.01 ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 161.939 104.172 176.924 1.00 33.56 ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 162.297 105.617 176.580 1.00 31.89 ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 162.658 105.927 175.439 1.00 29.24 ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 160.415 103.960 176.939 1.00 33.68 ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 159.798 104.468 175.648 1.00 28.15 ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 160.094 102.493 177.139 1.00 35.44 ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 162.203 106.522 177.559 1.00 31.87 ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 162.372 107.952 177.304 1.00 28.98 ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 163.823 108.345 177.055 1.00 27.72 ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 164.078 109.450 176.549 1.00 30.85 ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 161.823 108.756 178.483 1.00 27.16 ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 160.444 108.507 178.672 1.00 29.35 ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 164.776 107.490 177.435 1.00 25.40 ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 166.181 107.799 177.193 1.00 28.02 ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 166.476 107.950 175.706 1.00 26.56 ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 167.391 108.690 175.328 1.00 27.38 ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 167.073 106.717 177.802 1.00 29.61 ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 167.231 106.801 179.314 1.00 31.18 ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 167.755 108.147 179.779 1.00 33.42 ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 166.982 109.062 180.070 1.00 31.86 ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 169.074 108.275 179.854 1.00 30.03 ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 165.723 107.255 174.852 1.00 23.92 ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 165.930 107.372 173.412 1.00 23.33 ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 165.562 108.760 172.906 1.00 23.78 ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 166.259 109.321 172.051 1.00 21.82 ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 165.122 106.302 172.679 1.00 24.16 ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 165.367 106.258 171.182 1.00 26.16 ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 164.378 105.366 170.454 1.00 29.59 ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 163.406 104.891 171.040 1.00 28.51 ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 164.624 105.134 169.171 1.00 26.73 ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 164.470 109.330 173.414 1.00 24.23 ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 163.981 110.622 172.951 1.00 18.14 ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 164.552 111.800 173.730 1.00 16.91 ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 164.291 112.948 173.356 1.00 18.99 ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 162.451 110.665 173.022 1.00 15.46 ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 161.766 109.675 172.110 1.00 16.09 ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 161.603 108.351 172.487 1.00 19.29 ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 161.284 110.065 170.869 1.00 18.62 ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 160.979 107.443 171.655 1.00 19.92 ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 160.658 109.165 170.030 1.00 20.06 ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 160.509 107.856 170.429 1.00 20.75 ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 159.887 106.955 169.595 1.00 25.09 ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 165.296 111.548 174.806 1.00 14.82 ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 165.928 112.648 175.537 1.00 15.08 ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 166.803 113.551 174.665 1.00 15.84 ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 166.701 114.787 174.802 1.00 16.54 ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 166.723 112.081 176.718 1.00 16.10 ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 167.344 113.104 177.669 1.00 13.71 ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 166.263 113.839 178.441 1.00 13.93 ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 168.319 112.427 178.617 1.00 13.98 ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 167.681 113.036 173.790 1.00 16.66 ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 168.513 113.948 172.983 1.00 12.40 ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 167.717 114.902 172.110 1.00 9.94  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 168.147 116.043 171.903 1.00 7.77  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 169.360 112.988 172.136 1.00 7.16  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 169.414 111.746 172.925 1.00 9.11  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 168.072 111.630 173.576 1.00 14.25 ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 166.570 114.468 171.584 1.00 8.27  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 165.747 115.368 170.785 1.00 5.71  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 165.227 116.527 171.627 1.00 10.32 ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 165.199 117.672 171.166 1.00 14.11 ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 164.590 114.599 170.152 1.00 4.71  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 163.539 115.449 169.440 1.00 6.41  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 164.158 116.216 168.284 1.00 8.09  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 162.410 114.575 168.953 1.00 10.63 ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 164.813 116.249 172.866 1.00 7.26  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 164.370 117.319 173.753 1.00 5.14  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 165.512 118.271 174.084 1.00 6.62  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 165.314 119.493 174.161 1.00 10.88 ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 163.779 116.727 175.030 1.00 7.81  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 164.797 116.201 175.862 1.00 14.77 ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 166.716 117.732 174.293 1.00 3.29  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 167.870 118.596 174.531 1.00 4.45  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 168.127 119.507 173.335 1.00 5.33  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 168.388 120.707 173.495 1.00 6.47  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 169.108 117.754 174.836 1.00 11.04 ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 168.778 116.746 175.798 1.00 10.66 ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 170.221 118.629 175.388 1.00 8.14  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 168.048 118.949 172.125 1.00 7.66  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 168.228 119.751 170.919 1.00 6.69  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 167.143 120.815 170.800 1.00 6.55  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 167.417 121.943 170.375 1.00 8.24  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 168.235 118.852 169.684 1.00 4.78  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 165.906 120.469 171.159 1.00 6.30  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 164.816 121.440 171.116 1.00 4.41  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 165.084 122.609 172.055 1.00 4.61  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 164.896 123.776 171.687 1.00 10.35 ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 163.497 120.761 171.479 1.00 0.66  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 162.889 119.584 170.262 1.00 12.15 ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 165.517 122.313 173.283 1.00 2.76  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 165.815 123.388 174.227 1.00 4.74  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 166.958 124.261 173.722 1.00 6.30  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 166.893 125.496 173.808 1.00 10.51 ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 166.151 122.811 175.601 1.00 7.84  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 167.523 122.471 175.689 1.00 13.55 ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 168.010 123.637 173.183 1.00 3.79  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 169.129 124.410 172.652 1.00 0.99  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 168.683 125.310 171.505 1.00 4.06  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 169.086 126.476 171.428 1.00 5.92  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 170.244 123.473 172.195 1.00 3.34  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 170.751 122.714 173.277 1.00 8.80  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 167.844 124.784 170.609 1.00 3.80  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 167.370 125.568 169.471 1.00 2.15  ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 166.530 126.745 169.944 1.00 1.89  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 166.688 127.874 169.460 1.00 3.16  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 166.585 124.669 168.497 1.00 1.82  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 167.542 123.787 167.697 1.00 2.83  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 165.734 125.508 167.560 1.00 2.89  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 166.843 122.871 166.723 1.00 4.44  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 165.623 126.508 170.897 1.00 2.37  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 164.787 127.602 171.380 1.00 0.00  ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 165.624 128.680 172.049 1.00 2.18  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 165.359 129.874 171.875 1.00 9.76  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 163.726 127.109 172.357 1.00 0.27  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 163.092 128.260 173.108 1.00 2.70  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 162.220 129.131 172.469 1.00 4.78  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 163.397 128.505 174.440 1.00 6.15  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 161.651 130.193 173.142 1.00 4.74  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 162.832 129.564 175.120 1.00 6.06  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 161.961 130.404 174.466 1.00 6.28  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 161.395 131.461 175.139 1.00 9.15  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 166.622 128.289 172.840 1.00 2.58  ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 167.407 129.309 173.526 1.00 1.53  ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 168.335 130.046 172.568 1.00 2.73  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 168.608 131.234 172.768 1.00 8.30  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 168.167 128.688 174.692 1.00 2.13  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 167.337 128.570 175.938 1.00 3.39  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 167.238 129.630 176.822 1.00 5.74  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 166.622 127.416 176.203 1.00 6.73  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 166.462 129.530 177.958 1.00 5.90  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 165.844 127.314 177.336 1.00 9.03  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 165.765 128.370 178.215 1.00 7.00  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 168.794 129.385 171.502 1.00 1.44  ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 169.498 130.106 170.445 1.00 1.34  ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 168.580 131.124 169.775 1.00 1.37  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 168.980 132.269 169.527 1.00 3.76  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 170.054 129.119 169.418 1.00 1.72  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 171.205 128.460 169.960 1.00 3.68  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 170.450 129.837 168.139 1.00 1.84  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 167.335 130.730 169.495 1.00 1.76  ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 166.381 131.663 168.901 1.00 0.00  ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 166.107 132.838 169.833 1.00 1.12  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 165.970 133.981 169.384 1.00 5.11  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 165.080 130.937 168.561 1.00 0.00  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 165.164 130.048 167.336 1.00 2.01  ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 163.723 128.984 167.148 1.00 13.44 ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 162.456 129.988 167.912 1.00 5.51  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 166.006 132.568 171.135 1.00 1.56  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 165.794 133.634 172.108 1.00 2.28  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 166.988 134.579 172.164 1.00 4.29  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 166.815 135.800 172.261 1.00 8.88  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 165.517 133.033 173.486 1.00 0.30  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 165.021 134.032 174.513 1.00 6.70  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 165.209 133.544 175.935 1.00 14.98 ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 165.342 132.317 176.129 1.00 15.82 ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 165.226 134.385 176.859 1.00 14.16 ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 168.206 134.038 172.108 1.00 5.94  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 169.403 134.870 172.101 1.00 4.19  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 169.615 135.589 170.776 1.00 4.85  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 170.447 136.499 170.716 1.00 5.82  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 170.632 134.021 172.425 1.00 6.38  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 170.454 133.308 173.636 1.00 10.77 ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 168.900 135.197 169.718 1.00 4.98  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 169.038 135.879 168.433 1.00 2.64  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 168.695 137.361 168.509 1.00 3.63  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 169.135 138.128 167.647 1.00 4.30  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 168.153 135.212 167.380 1.00 0.27  ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 168.770 134.077 166.567 1.00 0.41  ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 167.746 133.516 165.605 1.00 0.17  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 169.997 134.563 165.820 1.00 3.12  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 167.922 137.783 169.510 1.00 3.42  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 167.564 139.191 169.638 1.00 1.56  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 168.755 140.078 169.968 1.00 3.56  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 168.640 141.304 169.856 1.00 3.08  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 166.487 139.363 170.711 1.00 2.59  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 166.979 139.111 172.124 1.00 2.38  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 166.042 139.720 173.150 1.00 3.52  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 164.871 138.802 173.441 1.00 6.22  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 165.268 137.663 174.311 1.00 6.93  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 169.888 139.501 170.374 1.00 6.93  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 171.064 140.302 170.693 1.00 5.79  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 171.737 140.868 169.449 1.00 6.24  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 172.488 141.842 169.559 1.00 7.79  ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 172.069 139.471 171.489 1.00 7.35  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 171.480 138.769 172.699 1.00 4.42  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 171.015 139.736 173.766 1.00 8.81  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 169.888 139.647 174.249 1.00 14.21 ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 171.884 140.667 174.140 1.00 6.82  ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 171.489 140.285 168.275 1.00 3.76  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 172.120 140.748 167.043 1.00 4.04  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 171.202 141.628 166.203 1.00 7.18  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 171.680 142.261 165.248 1.00 10.48 ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 172.625 139.561 166.195 1.00 4.51  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 171.465 138.889 165.462 1.00 2.50  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 173.352 138.556 167.071 1.00 5.60  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 171.878 137.685 164.648 1.00 4.03  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 169.911 141.690 166.524 1.00 6.42  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 168.975 142.548 165.810 1.00 2.94  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 167.706 142.677 166.639 1.00 5.01  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 167.229 141.694 167.207 1.00 10.09 ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 168.648 141.991 164.421 1.00 2.94  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 168.219 143.036 163.437 1.00 3.85  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 166.958 143.591 163.443 1.00 7.49  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 168.883 143.625 162.417 1.00 4.58  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 166.865 144.477 162.469 1.00 5.27  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 168.019 144.517 161.831 1.00 5.89  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 167.167 143.899 166.700 1.00 3.68  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 165.960 144.136 167.484 1.00 2.68  ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 164.751 143.421 166.896 1.00 2.07  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 163.793 143.129 167.620 1.00 9.66  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 165.687 145.637 167.586 1.00 0.26  ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 165.535 146.320 166.256 1.00 4.56  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 164.309 146.359 165.614 1.00 5.76  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 166.620 146.929 165.648 1.00 7.45  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 164.169 146.984 164.393 1.00 5.03  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 166.483 147.557 164.427 1.00 7.00  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 165.257 147.584 163.800 1.00 5.57  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 164.772 143.136 165.595 1.00 2.57  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 163.639 142.518 164.923 1.00 2.17  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 163.524 141.024 165.190 1.00 3.90  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 162.481 140.438 164.886 1.00 8.45  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 163.736 142.759 163.414 1.00 1.59  ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 162.448 142.694 162.593 1.00 0.99  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 161.675 143.996 162.700 1.00 5.80  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 162.764 142.373 161.146 1.00 2.61  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 164.557 140.397 165.753 1.00 3.32  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 164.568 138.944 165.928 1.00 2.33  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 163.926 138.584 167.268 1.00 5.04  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 164.563 138.085 168.196 1.00 8.65  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 165.987 138.403 165.813 1.00 0.86  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 166.669 138.688 164.491 1.00 2.73  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 165.953 139.162 163.400 1.00 3.67  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 168.029 138.477 164.336 1.00 4.20  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 166.575 139.425 162.199 1.00 1.61  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 168.658 138.732 163.136 1.00 3.43  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 167.926 139.207 162.072 1.00 2.23  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 168.548 139.463 160.874 1.00 6.97  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 162.625 138.847 167.347 1.00 2.81  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 161.828 138.554 168.533 1.00 1.95  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 160.997 137.306 168.255 1.00 4.28  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 160.076 137.336 167.434 1.00 7.33  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 160.936 139.738 168.893 1.00 1.83  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 161.671 141.059 169.018 1.00 2.07  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 162.613 141.093 170.203 1.00 5.19  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 162.322 140.527 171.256 1.00 7.59  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 163.745 141.764 170.039 1.00 1.76  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 161.323 136.212 168.938 1.00 1.94  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 160.633 134.941 168.762 1.00 2.31  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 160.130 134.463 170.115 1.00 4.27  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 160.919 134.304 171.050 1.00 9.55  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 161.557 133.896 168.128 1.00 1.89  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 162.195 134.367 166.844 1.00 1.74  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 161.443 134.512 165.688 1.00 3.73  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 163.544 134.682 166.792 1.00 1.96  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 162.017 134.949 164.514 1.00 4.60  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 164.128 135.120 165.621 1.00 5.57  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 163.361 135.253 164.485 1.00 7.61  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 163.935 135.690 163.316 1.00 7.57  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 158.825 134.237 170.212 1.00 3.12  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 158.223 133.767 171.447 1.00 5.66  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 158.360 132.252 171.566 1.00 7.50  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 158.739 131.555 170.620 1.00 14.30 ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 156.753 134.175 171.512 1.00 7.19  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 155.996 133.506 170.520 1.00 4.22  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 158.050 131.739 172.758 1.00 3.56  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 158.057 130.295 172.958 1.00 2.08  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 156.983 129.612 172.125 1.00 4.55  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 157.172 128.473 171.686 1.00 13.14 ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 157.870 129.964 174.439 1.00 3.93  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 157.907 128.482 174.818 1.00 3.43  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 159.306 127.915 174.656 1.00 3.28  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 157.403 128.274 176.233 1.00 8.47  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 155.858 130.290 171.891 1.00 0.94  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 154.800 129.705 171.076 1.00 0.13  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 155.249 129.498 169.636 1.00 4.31  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 154.799 128.554 168.984 1.00 9.79  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 153.551 130.581 171.124 1.00 4.76  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 152.300 129.899 170.597 1.00 5.69  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 152.225 128.437 170.993 1.00 9.94  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 152.185 128.103 172.177 1.00 11.80 ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 152.202 127.557 170.000 1.00 8.80  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 156.134 130.356 169.128 1.00 3.89  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 156.666 130.165 167.782 1.00 0.25  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 157.447 128.858 167.684 1.00 4.23  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 157.240 128.056 166.761 1.00 8.80  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 157.547 131.357 167.405 1.00 0.60  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 158.104 131.288 166.014 1.00 5.87  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 157.299 130.933 164.947 1.00 10.64 ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 159.431 131.590 165.774 1.00 3.53  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 157.810 130.873 163.669 1.00 6.07  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 159.947 131.533 164.498 1.00 5.35  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 159.136 131.175 163.445 1.00 6.56  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 158.344 128.619 168.641 1.00 2.51  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 159.110 127.380 168.631 1.00 3.50  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 158.214 126.174 168.884 1.00 5.64  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 158.450 125.096 168.330 1.00 10.53 ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 160.231 127.435 169.666 1.00 1.06  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 160.954 126.135 169.825 1.00 4.79  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 161.847 125.706 168.861 1.00 6.83  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 160.725 125.329 170.926 1.00 2.55  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 162.507 124.507 168.996 1.00 4.43  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 161.382 124.129 171.065 1.00 4.59  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 162.273 123.718 170.098 1.00 3.66  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 157.190 126.332 169.722 1.00 3.26  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 156.265 125.228 169.952 1.00 0.45  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 155.468 124.907 168.696 1.00 2.72  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 155.167 123.741 168.429 1.00 10.42 ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 155.336 125.550 171.122 1.00 3.10  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 155.994 125.576 172.503 1.00 4.09  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 154.954 125.774 173.589 1.00 4.50  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 156.794 124.308 172.746 1.00 3.20  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 155.118 125.927 167.908 1.00 4.09  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 154.477 125.687 166.618 1.00 5.02  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 155.419 124.964 165.664 1.00 8.81  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 154.995 124.063 164.930 1.00 12.21 ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 154.012 127.008 166.008 1.00 7.75  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 152.875 127.641 166.783 1.00 15.06 ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 152.349 126.988 167.708 1.00 13.83 ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 152.508 128.792 166.467 1.00 11.61 ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 156.696 125.350 165.656 1.00 7.95  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 157.679 124.649 164.830 1.00 4.77  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 157.756 123.179 165.235 1.00 7.38  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 157.744 122.276 164.388 1.00 13.56 ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 159.055 125.331 164.940 1.00 3.65  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 159.038 126.698 164.256 1.00 5.07  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 160.142 124.449 164.349 1.00 4.36  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 160.254 127.542 164.560 1.00 2.77  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 157.828 122.925 166.542 1.00 5.52  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 157.910 121.561 167.053 1.00 2.86  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 156.656 120.764 166.713 1.00 6.35  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 156.737 119.587 166.344 1.00 11.93 ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 158.138 121.602 168.563 1.00 4.92  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 158.650 120.319 169.167 1.00 8.84  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 159.511 119.491 168.463 1.00 12.24 ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 158.282 119.942 170.449 1.00 10.27 ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 159.982 118.320 169.017 1.00 11.12 ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 158.748 118.775 171.010 1.00 9.86  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 159.598 117.968 170.292 1.00 10.69 ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 160.066 116.805 170.852 1.00 16.49 ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 155.484 121.392 166.838 1.00 6.25  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 154.229 120.733 166.492 1.00 8.42  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 154.186 120.372 165.014 1.00 13.33 ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 153.746 119.277 164.646 1.00 20.71 ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 153.059 121.645 166.857 1.00 12.24 ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 151.712 121.044 166.600 1.00 16.41 ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 151.234 119.960 167.302 1.00 16.57 ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 150.743 121.377 165.715 1.00 17.25 ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 150.027 119.652 166.863 1.00 18.14 ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 149.706 120.495 165.899 1.00 18.97 ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 154.631 121.288 164.152 1.00 10.96 ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 154.673 121.004 162.721 1.00 10.90 ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 155.620 119.852 162.418 1.00 11.27 ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 155.316 118.991 161.585 1.00 17.36 ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 155.091 122.255 161.953 1.00 10.49 ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 155.387 121.971 160.495 1.00 12.22 ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 156.545 121.924 160.083 1.00 13.07 ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 154.339 121.785 159.705 1.00 12.62 ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 156.774 119.823 163.082 1.00 11.72 ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 157.739 118.756 162.841 1.00 9.16  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 157.194 117.416 163.325 1.00 12.35 ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 157.424 116.374 162.702 1.00 16.35 ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 159.082 119.103 163.507 1.00 7.76  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 160.014 117.908 163.497 1.00 10.16 ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 159.720 120.283 162.800 1.00 6.76  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 156.459 117.420 164.439 1.00 12.65 ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 155.991 116.161 165.013 1.00 13.87 ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 154.782 115.607 164.264 1.00 19.46 ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 154.749 114.418 163.930 1.00 22.92 ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 155.654 116.355 166.489 1.00 11.27 ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 156.825 116.306 167.468 1.00 10.38 ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 156.359 116.667 168.865 1.00 13.89 ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 157.469 114.932 167.453 1.00 13.06 ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 153.783 116.447 163.993 1.00 14.73 ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 152.499 115.971 163.492 1.00 14.49 ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 152.235 116.292 162.029 1.00 19.24 ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 151.566 115.506 161.356 1.00 25.61 ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 151.358 116.555 164.334 1.00 14.91 ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 151.445 116.209 165.802 1.00 17.39 ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 150.903 115.030 166.293 1.00 18.72 ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 152.089 117.052 166.694 1.00 17.88 ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 150.983 114.713 167.635 1.00 19.24 ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 152.175 116.744 168.034 1.00 18.26 ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 151.622 115.575 168.499 1.00 21.76 ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 151.712 115.268 169.837 1.00 23.66 ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 152.737 117.413 161.517 1.00 16.50 ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 152.520 117.807 160.126 1.00 18.81 ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 153.735 117.507 159.260 1.00 22.94 ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 154.081 118.283 158.365 1.00 22.98 ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 152.157 119.287 160.038 1.00 17.80 ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 151.041 119.721 160.971 1.00 22.45 ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 151.093 121.203 161.282 1.00 24.28 ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 151.902 121.915 160.652 1.00 22.63 ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 150.326 121.657 162.156 1.00 21.64 ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 154.398 116.377 159.507 1.00 22.08 ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 155.660 116.070 158.850 1.00 21.44 ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 155.396 115.208 157.622 1.00 27.10 ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 154.958 114.058 157.773 1.00 30.94 ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 156.595 115.352 159.808 1.00 20.24 ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 158.037 115.721 159.585 1.00 23.83 ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 158.334 116.813 159.103 1.00 23.50 ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 158.948 114.818 159.929 1.00 24.16 ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 155.638 115.705 156.405 1.00 30.23 ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 155.395 114.874 155.213 1.00 29.23 ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 156.331 113.684 155.091 1.00 29.82 ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 156.003 112.737 154.366 1.00 29.12 ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 155.592 115.856 154.048 1.00 29.95 ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 155.559 117.222 154.665 1.00 28.89 ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 156.092 117.057 156.049 1.00 29.25 ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 157.482 113.698 155.763 1.00 26.32 ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 158.425 112.590 155.677 1.00 25.56 ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 158.079 111.437 156.608 1.00 25.83 ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 158.757 110.405 156.564 1.00 28.12 ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 159.846 113.082 155.964 1.00 25.24 ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 160.251 114.238 155.072 1.00 27.39 ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 160.094 114.185 153.855 1.00 31.91 ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 160.775 115.294 155.681 1.00 22.68 ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 157.055 111.583 157.449 1.00 27.26 ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 156.595 110.514 158.327 1.00 29.39 ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 155.324 109.851 157.808 1.00 34.89 ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 154.546 109.301 158.594 1.00 35.61 ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 156.373 111.048 159.741 1.00 26.84 ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 157.607 111.545 160.493 1.00 26.76 ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 157.212 112.087 161.852 1.00 27.03 ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 158.627 110.433 160.633 1.00 27.66 ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 155.097 109.901 156.493 1.00 35.12 ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 153.861 109.367 155.929 1.00 33.64 ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 153.784 107.853 156.091 1.00 36.44 ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 152.775 107.323 156.572 1.00 36.17 ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 153.750 109.757 154.456 1.00 34.46 ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 153.157 111.136 154.221 1.00 37.41 ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 151.690 111.180 154.608 1.00 37.32 ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 150.915 112.131 153.712 1.00 35.55 ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 150.945 111.696 152.289 1.00 34.31 ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 154.837 107.142 155.700 1.00 33.64 ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 154.811 105.693 155.733 1.00 32.30 ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 155.868 105.067 156.617 1.00 32.52 ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 156.002 103.841 156.658 1.00 33.41 ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 156.627 105.894 157.331 1.00 33.71 ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 157.689 105.395 158.196 1.00 35.51 ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 157.076 104.886 159.493 1.00 33.59 ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 156.289 105.587 160.142 1.00 32.58 ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 158.732 106.490 158.465 1.00 33.00 ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 159.952 105.899 159.146 1.00 28.96 ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 159.122 107.176 157.168 1.00 32.10 ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 157.432 103.658 159.876 1.00 35.23 ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 156.928 103.052 161.098 1.00 36.03 ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 158.004 102.746 162.129 1.00 38.15 ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 157.673 102.628 163.313 1.00 36.84 ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 156.168 101.753 160.783 1.00 34.66 ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 155.639 101.201 161.995 1.00 34.61 ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 157.089 100.737 160.125 1.00 32.55 ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 159.264 102.609 161.723 1.00 36.50 ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 160.330 102.335 162.677 1.00 35.43 ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 160.514 103.524 163.609 1.00 37.53 ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 160.567 104.674 163.163 1.00 40.84 ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 161.634 102.027 161.941 1.00 37.26 ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 162.710 101.487 162.861 1.00 40.36 ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 162.393 101.153 164.022 1.00 40.36 ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 163.877 101.394 162.423 1.00 40.62 ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 160.610 103.246 164.911 1.00 33.56 ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 160.720 104.322 165.892 1.00 32.71 ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 162.019 105.100 165.724 1.00 32.85 ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 162.022 106.334 165.795 1.00 37.39 ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 160.609 103.753 167.305 1.00 33.62 ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 159.252 103.216 167.632 1.00 34.72 ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 158.098 103.947 167.454 1.00 36.12 ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 158.862 102.014 168.122 1.00 33.87 ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 157.057 103.223 167.821 1.00 35.74 ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 157.493 102.045 168.231 1.00 36.87 ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 163.133 104.399 165.503 1.00 27.61 ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 164.415 105.081 165.343 1.00 29.37 ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 164.447 105.913 164.066 1.00 31.59 ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 164.946 107.045 164.066 1.00 30.71 ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 165.557 104.065 165.346 1.00 30.20 ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 165.372 103.142 166.426 1.00 31.61 ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 166.892 104.769 165.514 1.00 28.80 ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 163.928 105.364 162.965 1.00 28.45 ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 163.879 106.111 161.713 1.00 28.19 ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 163.001 107.347 161.847 1.00 28.20 ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 163.365 108.434 161.376 1.00 28.97 ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 163.369 105.209 160.590 1.00 27.48 ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 163.896 105.564 159.212 1.00 29.93 ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 163.246 104.742 158.117 1.00 33.51 ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 163.042 103.538 158.268 1.00 31.66 ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 162.915 105.390 157.006 1.00 29.35 ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 161.843 107.200 162.493 1.00 25.13 ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 160.968 108.345 162.712 1.00 22.49 ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 161.640 109.390 163.591 1.00 21.28 ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 161.500 110.592 163.351 1.00 24.22 ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 159.648 107.889 163.332 1.00 21.65 ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 158.729 107.172 162.361 1.00 23.86 ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 157.373 106.894 162.981 1.00 24.20 ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 156.692 108.121 163.373 1.00 22.47 ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 155.604 108.595 162.780 1.00 26.80 ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 155.050 107.972 161.755 1.00 28.68 ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 155.061 109.722 163.230 1.00 26.91 ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 162.378 108.953 164.614 1.00 18.31 ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 163.076 109.897 165.482 1.00 20.89 ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 164.152 110.664 164.722 1.00 21.45 ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 164.298 111.881 164.893 1.00 21.00 ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 163.682 109.156 166.673 1.00 21.65 ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 164.394 110.008 167.721 1.00 21.12 ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 163.470 111.094 168.245 1.00 19.36 ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 164.899 109.137 168.857 1.00 20.73 ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 164.923 109.967 163.883 1.00 18.21 ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 165.947 110.643 163.091 1.00 20.36 ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 165.324 111.636 162.118 1.00 18.44 ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 165.820 112.761 161.958 1.00 18.49 ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 166.793 109.615 162.341 1.00 19.59 ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 166.025 108.945 161.357 1.00 21.30 ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 164.231 111.236 161.462 1.00 17.39 ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 163.530 112.141 160.556 1.00 16.93 ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 163.016 113.356 161.317 1.00 18.56 ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 163.096 114.489 160.832 1.00 21.32 ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 162.390 111.398 159.835 1.00 16.53 ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 162.953 110.462 158.768 1.00 17.44 ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 161.417 112.383 159.211 1.00 16.79 ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 161.907 109.593 158.111 1.00 19.13 ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 162.489 113.138 162.523 1.00 15.71 ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 161.956 114.234 163.320 1.00 11.40 ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 163.060 115.208 163.700 1.00 12.72 ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 162.872 116.424 163.646 1.00 15.30 ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 161.224 113.690 164.561 1.00 10.86 ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 159.839 113.176 164.178 1.00 13.10 ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 161.095 114.764 165.621 1.00 11.72 ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 159.168 112.381 165.265 1.00 12.90 ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 164.230 114.698 164.088 1.00 11.06 ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 165.334 115.586 164.452 1.00 9.00  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 165.809 116.399 163.248 1.00 11.79 ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 165.987 117.628 163.334 1.00 17.14 ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 166.485 114.771 165.039 1.00 8.96  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 166.017 114.019 166.163 1.00 11.84 ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 167.606 115.690 165.492 1.00 8.74  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 166.012 115.725 162.112 1.00 10.28 ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 166.447 116.415 160.900 1.00 7.85  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 165.450 117.495 160.500 1.00 10.37 ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 165.828 118.638 160.207 1.00 14.42 ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 166.619 115.400 159.770 1.00 8.83  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 167.134 115.977 158.466 1.00 14.35 ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 167.328 114.878 157.434 1.00 12.35 ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 168.062 115.386 156.204 1.00 11.86 ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 168.305 114.293 155.223 1.00 12.09 ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 164.162 117.152 160.505 1.00 7.44  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 163.137 118.104 160.110 1.00 8.47  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 162.966 119.204 161.144 1.00 6.90  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 162.607 120.327 160.787 1.00 10.82 ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 161.824 117.367 159.867 1.00 10.11 ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 161.727 116.821 158.459 1.00 20.41 ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 162.689 117.008 157.685 1.00 21.56 ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 160.708 116.186 158.130 1.00 23.20 ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 163.224 118.914 162.421 1.00 7.22  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 163.234 119.962 163.434 1.00 5.46  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 164.260 121.023 163.090 1.00 1.96  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 163.946 122.218 163.045 1.00 5.90  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 163.534 119.361 164.806 1.00 7.60  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 163.786 120.369 165.930 1.00 6.33  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 162.500 121.056 166.366 1.00 6.99  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 164.481 119.704 167.104 1.00 5.99  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 165.494 120.597 162.814 1.00 4.04  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 166.529 121.563 162.460 1.00 5.21  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 166.156 122.325 161.192 1.00 6.19  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 166.260 123.561 161.139 1.00 9.53  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 167.875 120.857 162.297 1.00 5.02  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 168.562 120.566 163.598 1.00 6.40  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 169.223 121.569 164.283 1.00 4.71  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 168.539 119.295 164.140 1.00 9.02  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 169.852 121.306 165.481 1.00 6.99  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 169.165 119.027 165.339 1.00 6.21  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 169.822 120.033 166.009 1.00 6.49  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 165.680 121.607 160.170 1.00 5.05  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 165.372 122.248 158.895 1.00 3.28  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 164.241 123.263 159.032 1.00 6.50  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 164.343 124.392 158.539 1.00 9.40  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 165.020 121.188 157.852 1.00 6.99  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 164.802 121.746 156.458 1.00 9.77  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 166.068 122.320 155.863 1.00 7.79  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 166.972 121.583 155.470 1.00 11.67 ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 166.141 123.642 155.790 1.00 5.75  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 163.151 122.878 159.701 1.00 3.49  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 161.992 123.754 159.825 1.00 0.00  ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 162.309 124.939 160.724 1.00 0.45  ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 161.869 126.066 160.463 1.00 8.26  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 160.777 122.958 160.336 1.00 2.63  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 159.633 123.891 160.691 1.00 3.54  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 160.328 121.952 159.291 1.00 5.54  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 163.070 124.715 161.801 1.00 3.09  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 163.489 125.829 162.640 1.00 3.12  ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 164.277 126.845 161.828 1.00 2.90  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 163.993 128.049 161.876 1.00 6.50  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 164.316 125.318 163.820 1.00 2.91  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 165.254 126.372 161.046 1.00 2.70  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 166.024 127.294 160.219 1.00 0.00  ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 165.131 128.028 159.232 1.00 2.78  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 165.229 129.248 159.085 1.00 8.46  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 167.131 126.561 159.470 1.00 1.18  ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 167.842 127.426 158.468 1.00 4.66  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 168.772 128.364 158.881 1.00 7.10  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 167.565 127.319 157.117 1.00 4.24  ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 169.418 129.168 157.967 1.00 4.87  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 168.207 128.121 156.199 1.00 4.17  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 169.136 129.045 156.625 1.00 3.98  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 164.248 127.300 158.543 1.00 5.60  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 163.411 127.928 157.526 1.00 3.00  ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 162.538 129.019 158.132 1.00 6.02  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 162.537 130.165 157.664 1.00 9.22  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 162.544 126.876 156.837 1.00 0.00  ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 163.351 125.911 156.000 1.00 6.58  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 164.573 126.023 155.910 1.00 12.81 ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 162.672 124.955 155.380 1.00 7.88  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 161.805 128.682 159.194 1.00 5.11  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 160.864 129.629 159.778 1.00 0.00  ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 161.577 130.823 160.395 1.00 3.56  ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 161.105 131.959 160.271 1.00 7.93  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 159.988 128.925 160.812 1.00 0.00  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 159.090 127.856 160.219 1.00 2.09  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 157.780 127.754 160.976 1.00 5.45  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 156.991 126.607 160.544 1.00 5.06  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 155.780 126.320 160.999 1.00 9.29  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 155.186 127.077 161.907 1.00 9.86  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 155.147 125.250 160.529 1.00 10.24 ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 162.707 130.601 161.070 1.00 5.91  ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 163.406 131.724 161.681 1.00 0.96  ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 164.052 132.606 160.618 1.00 7.49  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 163.967 133.837 160.683 1.00 14.43 ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 164.434 131.220 162.707 1.00 0.10  ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 165.311 132.361 163.178 1.00 2.19  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 163.723 130.578 163.883 1.00 2.75  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 164.695 131.999 159.616 1.00 3.83  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 165.425 132.762 158.616 1.00 0.00  ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 164.510 133.457 157.621 1.00 3.64  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 164.953 134.395 156.951 1.00 5.67  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 166.400 131.851 157.870 1.00 1.98  ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 163.253 133.024 157.497 1.00 9.68  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 162.315 133.780 156.676 1.00 5.86  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 162.075 135.177 157.231 1.00 1.31  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 161.678 136.072 156.477 1.00 6.02  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 160.990 133.029 156.550 1.00 7.79  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 160.956 132.034 155.405 1.00 7.98  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 161.433 132.671 154.109 1.00 9.04  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 161.423 131.728 152.997 1.00 7.06  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 161.960 131.968 151.808 1.00 10.73 ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 162.556 133.117 151.537 1.00 12.83 ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 161.898 131.029 150.868 1.00 9.71  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 162.312 135.384 158.524 1.00 0.00  ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 162.175 136.694 159.126 1.00 2.15  ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 163.489 137.261 159.619 1.00 2.81  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 163.539 137.919 160.661 1.00 4.02  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 164.565 137.012 158.875 1.00 4.28  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 165.888 137.513 159.211 1.00 1.46  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 166.541 138.110 157.975 1.00 3.87  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 166.230 137.729 156.844 1.00 5.36  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 166.790 136.407 159.778 1.00 2.26  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 166.387 135.906 161.150 1.00 7.43  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 167.740 135.083 162.010 1.00 10.87 ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 168.607 134.337 160.637 1.00 5.85  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 167.446 139.056 158.204 1.00 6.00  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 168.258 139.592 157.123 1.00 4.26  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 169.198 138.515 156.595 1.00 5.22  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 169.628 137.624 157.331 1.00 11.01 ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 169.054 140.805 157.600 1.00 2.73  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 168.233 142.014 158.044 1.00 0.78  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 169.131 143.062 158.672 1.00 3.38  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 167.467 142.600 156.873 1.00 2.35  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 169.518 138.605 155.303 1.00 2.41  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 170.259 137.531 154.650 1.00 1.32  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 171.662 137.367 155.224 1.00 5.07  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 172.230 136.271 155.159 1.00 12.34 ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 170.328 137.774 153.145 1.00 2.61  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 170.674 136.552 152.354 1.00 6.95  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 171.966 136.244 151.985 1.00 4.04  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 169.898 135.554 151.871 1.00 5.64  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 171.968 135.113 151.304 1.00 3.59  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 170.726 134.674 151.218 1.00 5.26  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 172.239 138.429 155.784 1.00 0.87  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 173.579 138.325 156.345 1.00 2.35  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 173.608 137.623 157.698 1.00 8.60  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 174.699 137.316 158.191 1.00 13.25 ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 174.217 139.711 156.465 1.00 2.19  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 173.584 140.611 157.505 1.00 2.55  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 172.664 141.643 156.892 1.00 10.86 ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 172.231 141.504 155.748 1.00 14.30 ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 172.365 142.691 157.649 1.00 11.97 ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 172.450 137.367 158.307 1.00 4.66  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 172.373 136.620 159.556 1.00 0.99  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 171.965 135.167 159.356 1.00 2.78  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 171.980 134.393 160.324 1.00 13.09 ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 171.395 137.301 160.518 1.00 1.95  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 171.715 138.764 160.733 1.00 8.10  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 172.887 139.079 161.019 1.00 11.65 ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 170.798 139.601 160.615 1.00 11.35 ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 171.600 134.784 158.131 1.00 0.00  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 171.274 133.389 157.856 1.00 3.45  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 172.470 132.491 158.128 1.00 3.00  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 172.320 131.402 158.692 1.00 9.12  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 170.813 133.226 156.408 1.00 6.15  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 169.498 133.876 156.110 1.00 1.72  ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 168.808 133.649 154.940 1.00 1.63  ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 168.749 134.747 156.825 1.00 2.07  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 167.691 134.351 154.947 1.00 3.33  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 167.630 135.027 156.080 1.00 4.17  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 173.666 132.929 157.734 1.00 3.30  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 174.859 132.122 157.958 1.00 4.34  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 175.152 131.999 159.448 1.00 3.54  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 175.563 130.936 159.924 1.00 7.33  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 176.056 132.700 157.179 1.00 6.67  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 177.288 131.810 157.350 1.00 5.55  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 176.346 134.134 157.597 1.00 7.48  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 177.035 130.352 157.041 1.00 6.33  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 174.928 133.070 160.213 1.00 5.15  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 175.139 133.002 161.656 1.00 4.54  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 174.187 132.004 162.301 1.00 5.16  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 174.600 131.155 163.105 1.00 11.74 ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 174.964 134.389 162.276 1.00 3.06  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 175.800 135.331 161.593 1.00 8.61  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 175.335 134.365 163.748 1.00 5.06  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 172.901 132.082 161.949 1.00 2.16  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 171.934 131.157 162.534 1.00 0.86  ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 172.214 129.719 162.111 1.00 4.34  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 172.075 128.791 162.916 1.00 10.78 ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 170.511 131.560 162.155 1.00 2.48  ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 169.455 130.789 162.892 1.00 6.69  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 169.512 130.658 164.268 1.00 4.92  ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 168.416 130.184 162.209 1.00 4.37  ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 168.547 129.945 164.950 1.00 2.46  ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 167.451 129.469 162.887 1.00 2.56  ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 167.516 129.350 164.258 1.00 0.40  ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 172.610 129.513 160.852 1.00 2.10  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 172.924 128.169 160.385 1.00 0.98  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 174.163 127.619 161.078 1.00 4.61  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 174.226 126.426 161.384 1.00 7.22  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 173.110 128.169 158.870 1.00 3.96  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 175.159 128.470 161.335 1.00 4.01  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 176.337 128.034 162.076 1.00 3.07  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 175.972 127.638 163.499 1.00 7.44  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 176.474 126.636 164.024 1.00 13.87 ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 177.389 129.144 162.085 1.00 3.28  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 178.190 129.264 160.801 1.00 7.20  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 179.418 127.967 160.603 1.00 15.10 ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 180.851 128.746 161.337 1.00 10.88 ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 175.098 128.416 164.142 1.00 7.89  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 174.657 128.066 165.490 1.00 3.22  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 173.896 126.743 165.500 1.00 2.12  ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 174.100 125.904 166.387 1.00 7.80  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 173.802 129.191 166.066 1.00 3.39  ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 174.543 130.515 166.257 1.00 4.02  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 173.564 131.650 166.458 1.00 3.80  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 175.517 130.430 167.419 1.00 3.16  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 173.018 126.534 164.516 1.00 0.00  ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 172.295 125.268 164.430 1.00 3.55  ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 173.243 124.106 164.156 1.00 5.30  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 173.055 123.002 164.683 1.00 7.71  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 171.220 125.345 163.346 1.00 6.34  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 169.995 126.207 163.651 1.00 3.13  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 168.910 125.960 162.622 1.00 2.77  ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 169.480 125.936 165.053 1.00 6.76  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 174.260 124.329 163.322 1.00 7.69  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 175.247 123.289 163.053 1.00 4.81  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 176.018 122.928 164.314 1.00 5.36  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 176.285 121.751 164.568 1.00 10.87 ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 176.202 123.743 161.950 1.00 5.38  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 176.384 123.930 165.116 1.00 4.53  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 177.041 123.649 166.390 1.00 4.15  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 176.122 122.869 167.322 1.00 7.52  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 176.564 121.941 168.013 1.00 10.82 ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 177.494 124.949 167.048 1.00 2.00  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 178.646 125.637 166.342 1.00 7.83  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 179.379 126.576 167.283 1.00 13.13 ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 180.045 125.850 168.357 1.00 18.04 ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 180.665 126.426 169.378 1.00 16.09 ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 180.721 127.741 169.500 1.00 15.14 ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 181.242 125.661 170.301 1.00 11.64 ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 174.838 123.236 167.357 1.00 9.64  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 173.881 122.522 168.203 1.00 4.39  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 173.785 121.060 167.786 1.00 3.41  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 173.785 120.157 168.629 1.00 9.69  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 172.506 123.216 168.158 1.00 2.94  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 172.548 124.536 168.926 1.00 3.07  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 171.429 122.310 168.726 1.00 3.27  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 171.275 125.335 168.821 1.00 3.25  ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 173.702 120.804 166.478 1.00 6.76  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 173.631 119.425 166.000 1.00 9.11  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 174.930 118.677 166.269 1.00 13.22 ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 174.911 117.482 166.586 1.00 13.59 ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 173.299 119.395 164.509 1.00 4.79  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 173.029 117.998 163.980 1.00 5.69  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 172.943 117.979 162.468 1.00 10.29 ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 172.394 116.657 161.965 1.00 11.81 ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 171.048 116.369 162.530 1.00 13.54 ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 176.068 119.361 166.138 1.00 14.22 ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 177.358 118.726 166.391 1.00 11.94 ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 177.489 118.310 167.847 1.00 15.85 ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 178.044 117.247 168.150 1.00 16.64 ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 178.487 119.676 165.995 1.00 9.85  ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 179.912 119.149 166.146 1.00 15.01 ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 180.078 117.852 165.377 1.00 18.63 ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 180.915 120.190 165.676 1.00 13.62 ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 176.990 119.138 168.769 1.00 16.31 ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 177.009 118.768 170.179 1.00 15.35 ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 176.145 117.547 170.467 1.00 15.79 ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 176.350 116.885 171.490 1.00 20.12 ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 176.549 119.944 171.041 1.00 12.53 ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 177.686 120.773 171.612 1.00 15.51 ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 177.161 121.885 172.502 1.00 20.94 ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 178.244 122.409 173.431 1.00 20.22 ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 177.733 122.625 174.813 1.00 16.72 ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 175.192 117.237 169.598 1.00 16.73 ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 174.317 116.097 169.763 1.00 20.82 ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 174.797 114.808 169.134 1.00 23.46 ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 174.058 113.819 169.144 1.00 26.09 ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 176.009 114.781 168.586 1.00 28.76 ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 176.561 113.586 167.958 1.00 31.71 ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 177.526 112.914 168.926 1.00 34.37 ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 178.492 113.538 169.382 1.00 31.35 ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 177.268 113.930 166.648 1.00 31.16 ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 176.360 114.625 165.780 1.00 27.96 ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 177.750 112.667 165.957 1.00 30.55 ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 177.259 111.645 169.240 1.00 41.33 ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 178.101 110.914 170.183 1.00 43.25 ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 179.471 110.634 169.582 1.00 44.55 ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 180.493 110.685 170.278 1.00 42.90 ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 177.399 109.615 170.624 1.00 43.30 ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 178.150 108.973 171.779 1.00 42.59 ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 175.957 109.898 171.007 1.00 42.87 ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 179.522 110.340 168.285 1.00 43.94 ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 180.759 109.966 167.633 1.00 43.61 ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 181.688 111.100 167.268 1.00 43.93 ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 182.769 110.847 166.731 1.00 43.44 ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 181.306 112.345 167.542 1.00 39.24 ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 182.150 113.476 167.203 1.00 37.18 ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 182.816 114.050 168.450 1.00 35.17 ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 182.220 114.057 169.531 1.00 34.99 ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 181.342 114.584 166.516 1.00 35.04 ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 180.997 114.298 165.066 1.00 35.00 ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 182.220 114.017 164.220 1.00 37.60 ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 183.151 114.849 164.223 1.00 34.66 ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 182.251 112.962 163.552 1.00 39.94 ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 184.051 114.531 168.333 1.00 33.67 ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 184.691 115.211 169.462 1.00 33.42 ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 184.026 116.548 169.747 1.00 33.97 ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 183.204 117.051 168.977 1.00 32.08 ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 186.141 115.393 169.002 1.00 31.80 ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 186.324 114.389 167.904 1.00 31.78 ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 184.993 114.290 167.229 1.00 33.81 ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 184.396 117.128 170.890 1.00 32.71 ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 183.773 118.377 171.316 1.00 33.38 ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 184.182 119.552 170.435 1.00 34.26 ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 183.375 120.462 170.214 1.00 33.52 ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 184.116 118.666 172.781 1.00 33.99 ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 183.577 119.937 173.160 1.00 33.34 ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 185.623 118.665 172.998 1.00 32.81 ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 185.417 119.551 169.925 1.00 33.60 ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 185.960 120.678 169.162 1.00 32.19 ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 185.837 121.982 169.943 1.00 31.66 ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 185.603 123.048 169.369 1.00 33.28 ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 185.288 120.807 167.792 1.00 28.34 ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 185.396 119.573 166.929 1.00 28.06 ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 186.628 119.117 166.488 1.00 27.91 ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 184.263 118.868 166.551 1.00 28.33 ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 186.730 117.991 165.697 1.00 29.97 ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 184.355 117.742 165.759 1.00 28.50 ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 185.589 117.308 165.335 1.00 30.90 ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 185.684 116.184 164.546 1.00 31.42 ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 185.990 121.900 171.265 1.00 32.19 ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 185.822 123.079 172.107 1.00 31.93 ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 186.949 124.078 171.875 1.00 32.46 ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 186.703 125.279 171.711 1.00 31.90 ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 185.757 122.655 173.577 1.00 34.16 ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 185.370 123.793 174.507 1.00 37.40 ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 185.177 124.930 174.029 1.00 39.53 ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 185.258 123.545 175.725 1.00 34.59 ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 188.193 123.596 171.846 1.00 32.70 ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 189.328 124.487 171.624 1.00 31.87 ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 189.299 125.085 170.224 1.00 31.75 ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 189.618 126.267 170.041 1.00 33.43 ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 190.638 123.736 171.859 1.00 31.32 ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 188.920 124.286 169.225 1.00 29.59 ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 188.884 124.779 167.850 1.00 25.57 ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 187.874 125.908 167.696 1.00 23.64 ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 188.180 126.953 167.112 1.00 27.94 ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 188.563 123.631 166.894 1.00 25.61 ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 189.742 122.713 166.610 1.00 29.25 ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 189.854 121.573 167.604 1.00 33.06 ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 189.394 121.735 168.755 1.00 31.58 ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 190.406 120.516 167.237 1.00 31.99 ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 186.667 125.725 168.233 1.00 21.64 ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 185.658 126.778 168.146 1.00 22.38 ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 186.015 127.972 169.021 1.00 22.00 ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 185.731 129.117 168.650 1.00 22.23 ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 184.288 126.224 168.526 1.00 22.75 ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 183.578 125.549 167.393 1.00 21.80 ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 183.375 126.209 166.195 1.00 20.15 ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 183.117 124.250 167.522 1.00 20.50 ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 182.726 125.591 165.149 1.00 21.31 ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 182.465 123.626 166.479 1.00 22.92 ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 182.269 124.297 165.291 1.00 25.52 ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 186.640 127.729 170.175 1.00 28.10 ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 187.091 128.834 171.012 1.00 27.12 ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 188.095 129.703 170.268 1.00 26.93 ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 188.023 130.935 170.323 1.00 30.47 ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 187.697 128.300 172.308 1.00 29.50 ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 187.474 129.197 173.513 1.00 33.44 ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 188.646 130.120 173.781 1.00 34.87 ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 189.718 129.970 173.191 1.00 33.57 ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 188.451 131.082 174.675 1.00 29.52 ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 189.037 129.076 169.560 1.00 24.32 ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 189.963 129.847 168.738 1.00 27.24 ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 189.233 130.546 167.598 1.00 29.19 ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 189.447 131.737 167.355 1.00 27.82 ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 191.071 128.949 168.191 1.00 26.62 ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 192.143 129.703 167.470 1.00 29.92 ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 193.057 130.502 168.122 1.00 30.45 ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 192.433 129.800 166.152 1.00 29.11 ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 193.870 131.049 167.238 1.00 31.44 ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 193.513 130.639 166.033 1.00 29.84 ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 188.341 129.827 166.912 1.00 28.21 ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 187.596 130.413 165.802 1.00 20.39 ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 186.825 131.652 166.231 1.00 22.36 ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 186.606 132.559 165.422 1.00 21.66 ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 186.646 129.368 165.215 1.00 16.12 ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 185.785 129.883 164.100 1.00 20.70 ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 186.342 130.262 162.892 1.00 22.85 ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 184.411 129.973 164.255 1.00 22.75 ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 185.549 130.731 161.864 1.00 18.77 ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 183.614 130.439 163.231 1.00 19.67 ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 184.184 130.819 162.034 1.00 17.86 ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 186.414 131.715 167.496 1.00 25.97 ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 185.646 132.850 167.990 1.00 23.10 ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 186.490 133.931 168.657 1.00 26.54 ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 186.081 135.096 168.653 1.00 26.38 ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 184.575 132.373 168.976 1.00 23.20 ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 183.384 131.650 168.348 1.00 22.78 ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 182.310 131.373 169.385 1.00 23.86 ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 182.821 132.458 167.191 1.00 19.80 ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 187.646 133.595 169.231 1.00 33.88 ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 188.417 134.576 169.993 1.00 35.06 ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 189.906 134.489 169.674 1.00 37.52 ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 190.754 134.618 170.562 1.00 37.93 ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 188.189 134.403 171.495 1.00 34.25 ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 186.821 134.849 171.977 1.00 34.73 ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 186.635 134.545 173.455 1.00 37.17 ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 185.297 134.046 173.749 1.00 38.41 ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 184.873 132.822 173.467 1.00 36.58 ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 185.661 131.934 172.882 1.00 31.93 ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 183.627 132.479 173.780 1.00 33.61 ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 190.250 134.268 168.404 1.00 42.06 ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 191.653 134.251 168.032 1.00 38.32 ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 192.301 135.620 168.023 1.00 40.49 ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 193.524 135.729 168.146 1.00 41.42 ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 191.502 136.678 167.877 1.00 44.38 ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 192.058 138.025 167.855 1.00 43.71 ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 192.440 138.532 169.239 1.00 44.78 ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 193.136 139.550 169.335 1.00 45.96 ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 191.071 138.990 167.187 1.00 46.06 ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 189.754 139.106 167.938 1.00 50.23 ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 189.586 138.563 169.029 1.00 50.62 ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 188.808 139.829 167.349 1.00 47.21 ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 192.010 137.857 170.304 1.00 47.42 ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 192.361 138.265 171.659 1.00 48.32 ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 193.723 137.748 172.103 1.00 47.98 ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 194.202 138.155 173.167 1.00 46.12 ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 191.287 137.796 172.643 1.00 47.68 ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 189.993 138.589 172.569 1.00 48.19 ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 188.907 138.019 173.461 1.00 49.29 ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 189.184 137.776 174.654 1.00 47.45 ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 187.779 137.817 172.968 1.00 48.62 ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 194.353 136.869 171.325 1.00 46.10 ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 195.677 136.344 171.657 1.00 45.86 ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 196.691 137.435 171.324 1.00 46.99 ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 197.015 137.663 170.158 1.00 45.77 ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 195.979 135.043 170.912 1.00 46.51 ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 194.913 133.991 171.228 1.00 45.11 ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 197.364 134.530 171.276 1.00 45.10 ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 195.166 132.648 170.582 1.00 43.05 ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 197.195 138.113 172.354 1.00 48.14 ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 198.115 139.225 172.150 1.00 47.36 ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 199.479 138.689 171.736 1.00 45.32 ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 200.024 137.772 172.364 1.00 41.73 ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 198.214 140.081 173.420 1.00 45.41 ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 199.240 141.190 173.237 1.00 43.59 ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 196.853 140.660 173.774 1.00 44.73 ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 200.036 139.262 170.673 1.00 43.47 ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 201.359 138.908 170.180 1.00 42.66 ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 202.297 140.098 170.324 1.00 45.05 ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 201.911 141.241 170.060 1.00 43.94 ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 201.300 138.466 168.715 1.00 43.42 ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 200.476 137.216 168.407 1.00 45.96 ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 200.558 136.880 166.928 1.00 44.71 ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 200.942 136.042 169.252 1.00 43.87 ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 203.528 139.826 170.748 1.00 48.95 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 204.528 140.868 170.912 1.00 48.51 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 205.167 141.205 169.565 1.00 49.11 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 204.839 140.625 168.526 1.00 49.60 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 205.580 140.437 171.930 1.00 46.05 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 204.990 140.168 173.189 1.00 45.98 ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 206.095 142.165 169.585 1.00 48.51 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 206.775 142.563 168.357 1.00 48.98 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 207.598 141.417 167.782 1.00 51.22 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 207.594 141.189 166.566 1.00 50.38 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 207.662 143.780 168.619 1.00 45.97 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 208.309 140.683 168.639 1.00 48.51 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 209.105 139.561 168.183 1.00 47.57 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 208.334 138.288 167.921 1.00 48.77 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 208.916 137.319 167.424 1.00 47.22 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 207.041 138.265 168.252 1.00 49.44 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 206.234 137.071 168.011 1.00 49.93 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 206.098 136.786 166.520 1.00 49.34 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 206.160 135.626 166.095 1.00 46.10 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 204.858 137.229 168.657 1.00 47.38 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 204.972 137.422 170.057 1.00 44.22 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 205.916 137.823 165.717 1.00 52.33 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 205.745 137.647 164.279 1.00 53.41 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 207.079 137.307 163.630 1.00 52.55 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 208.029 138.095 163.739 1.00 51.34 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 205.161 138.912 163.656 1.00 52.79 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 203.861 139.161 164.202 1.00 52.63 ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 205.051 138.761 162.147 1.00 51.60 ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 207.203 136.167 162.953 1.00 54.73 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 208.473 135.797 162.316 1.00 55.31 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 208.612 136.224 160.862 1.00 54.85 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 209.645 135.923 160.254 1.00 53.98 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 208.451 134.268 162.426 1.00 55.00 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 206.996 133.915 162.324 1.00 54.60 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 206.195 135.101 162.823 1.00 52.97 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 207.611 136.905 160.299 1.00 56.27 ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 207.640 137.390 158.919 1.00 55.98 ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 207.855 136.231 157.938 1.00 55.76 ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 208.870 136.130 157.244 1.00 54.36 ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 208.710 138.476 158.745 1.00 55.33 ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 208.558 139.306 157.480 1.00 56.16 ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 209.774 140.191 157.262 1.00 56.27 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 211.013 139.426 157.300 1.00 58.16 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 212.224 139.951 157.168 1.00 56.74 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 212.396 141.250 156.983 1.00 55.37 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 213.286 139.154 157.224 1.00 55.70 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 206.860 135.340 157.917 1.00 51.36 ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 206.897 134.201 157.011 1.00 50.58 ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 206.893 134.692 155.571 1.00 49.97 ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 206.181 135.643 155.215 1.00 48.62 ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 205.712 133.258 157.279 1.00 49.76 ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 205.684 132.828 158.747 1.00 49.63 ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 205.778 132.036 156.374 1.00 47.26 ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 204.632 133.531 159.570 1.00 50.52 ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 207.701 134.049 154.733 1.00 50.11 ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 207.791 134.428 153.329 1.00 48.67 ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 206.475 134.148 152.615 1.00 48.34 ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 205.838 133.113 152.832 1.00 46.59 ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 208.945 133.677 152.657 1.00 47.27 ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 209.356 134.199 151.281 1.00 48.70 ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 208.579 133.578 150.131 1.00 50.62 ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 207.599 132.862 150.332 1.00 50.56 ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 209.023 133.852 148.908 1.00 49.09 ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 206.072 135.081 151.755 1.00 41.17 ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 204.858 134.940 150.980 1.00 39.36 ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 203.581 135.290 151.706 1.00 40.86 ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 202.499 135.146 151.120 1.00 39.80 ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 203.660 135.746 152.954 1.00 40.04 ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 202.489 136.062 153.758 1.00 37.87 ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 202.524 137.522 154.185 1.00 36.28 ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 203.584 138.055 154.526 1.00 38.81 ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 202.399 135.166 155.002 1.00 37.23 ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 201.667 133.819 154.934 1.00 37.29 ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 201.990 133.044 153.668 1.00 36.11 ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 201.985 132.985 156.164 1.00 38.42 ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 201.358 138.159 154.160 1.00 34.43 ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 201.213 139.510 154.674 1.00 35.14 ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 201.423 139.509 156.189 1.00 33.95 ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 201.265 138.486 156.861 1.00 35.61 ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 199.832 140.064 154.299 1.00 35.78 ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 199.699 140.075 152.872 1.00 34.01 ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 199.635 141.487 154.801 1.00 36.47 ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 201.815 140.670 156.723 1.00 32.69 ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 202.103 140.787 158.152 1.00 37.49 ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 200.904 140.334 158.979 1.00 38.11 ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 201.048 139.579 159.950 1.00 35.71 ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 202.514 142.228 158.498 1.00 38.60 ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 202.580 142.417 160.006 1.00 37.69 ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 203.849 142.567 157.856 1.00 35.57 ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 199.705 140.785 158.607 1.00 37.80 ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 198.505 140.352 159.318 1.00 37.92 ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 198.276 138.856 159.152 1.00 36.72 ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 197.848 138.175 160.092 1.00 38.51 ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 197.289 141.144 158.833 1.00 36.52 ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 197.275 142.632 159.214 1.00 39.05 ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 197.181 142.909 160.717 1.00 41.70 ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 196.793 144.042 161.071 1.00 39.39 ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 197.474 142.022 161.545 1.00 42.55 ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 198.558 138.323 157.960 1.00 33.34 ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 198.475 136.880 157.763 1.00 34.16 ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 199.469 136.151 158.658 1.00 38.09 ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 199.155 135.095 159.214 1.00 36.73 ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 198.719 136.532 156.296 1.00 30.63 ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 197.564 136.874 155.374 1.00 31.98 ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 197.746 136.307 153.982 1.00 34.61 ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 198.752 135.665 153.690 1.00 38.07 ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 196.772 136.546 153.114 1.00 33.16 ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 200.674 136.706 158.811 1.00 41.20 ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 201.658 136.105 159.705 1.00 37.59 ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 201.174 136.115 161.150 1.00 38.10 ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 201.340 135.126 161.873 1.00 38.46 ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 202.994 136.838 159.582 1.00 37.74 ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 200.579 137.227 161.592 1.00 37.05 ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 200.048 137.286 162.952 1.00 40.07 ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 198.936 136.266 163.152 1.00 40.34 ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 198.864 135.608 164.198 1.00 38.60 ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 199.544 138.695 163.265 1.00 38.10 ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 200.570 139.790 163.043 1.00 39.47 ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 200.316 141.005 163.911 1.00 41.98 ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 199.335 140.992 164.683 1.00 41.60 ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 201.098 141.975 163.822 1.00 39.75 ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 198.058 136.122 162.157 1.00 37.94 ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 197.009 135.112 162.238 1.00 37.58 ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 197.602 133.710 162.303 1.00 39.21 ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 197.093 132.846 163.025 1.00 39.17 ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 196.061 135.242 161.048 1.00 36.44 ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 198.680 133.466 161.554 1.00 36.29 ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 199.341 132.165 161.591 1.00 37.10 ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 199.910 131.890 162.978 1.00 38.11 ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 199.763 130.785 163.516 1.00 37.27 ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 200.436 132.090 160.510 1.00 38.44 ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 201.387 130.939 160.791 1.00 38.76 ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 199.808 131.939 159.146 1.00 36.89 ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 200.571 132.884 163.577 1.00 38.87 ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 201.129 132.692 164.915 1.00 40.02 ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 200.021 132.436 165.927 1.00 42.41 ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 200.156 131.581 166.812 1.00 41.90 ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 202.003 133.892 165.324 1.00 41.15 ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 202.746 133.578 166.611 1.00 40.24 ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 203.004 134.207 164.237 1.00 40.88 ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 198.914 133.176 165.824 1.00 40.98 ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 197.799 132.952 166.739 1.00 38.09 ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 197.211 131.556 166.568 1.00 36.84 ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 196.890 130.885 167.555 1.00 37.00 ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 196.727 134.022 166.533 1.00 36.66 ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 197.145 135.403 167.000 1.00 37.69 ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 196.220 136.476 166.461 1.00 40.61 ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 196.836 137.795 166.498 1.00 40.76 ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 196.448 138.778 167.296 1.00 41.36 ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 195.444 138.626 168.145 1.00 42.07 ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 197.082 139.947 167.244 1.00 40.54 ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 197.072 131.101 165.322 1.00 32.71 ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 196.557 129.759 165.072 1.00 34.21 ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 197.524 128.686 165.557 1.00 38.06 ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 197.095 127.587 165.925 1.00 38.48 ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 196.267 129.581 163.581 1.00 32.45 ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 195.645 128.258 163.134 1.00 32.31 ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 194.306 128.038 163.813 1.00 31.66 ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 195.496 128.223 161.622 1.00 32.77 ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 198.823 128.986 165.567 1.00 40.01 ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 199.825 128.017 165.992 1.00 38.88 ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 199.707 127.642 167.463 1.00 40.10 ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 200.311 126.646 167.876 1.00 39.54 ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 201.227 128.560 165.710 1.00 38.56 ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 201.498 129.706 166.496 1.00 38.27 ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 198.959 128.410 168.259 1.00 40.07 ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 198.771 128.057 169.663 1.00 39.72 ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 198.041 126.729 169.816 1.00 40.93 ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 198.242 126.023 170.811 1.00 40.82 ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 198.010 129.168 170.386 1.00 39.73 ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 198.846 130.770 170.381 1.00 48.76 ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 197.193 126.376 168.854 1.00 39.87 ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 196.485 125.110 168.916 1.00 39.94 ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 197.455 123.946 168.726 1.00 41.65 ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 198.444 124.063 167.999 1.00 38.51 ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 195.393 125.054 167.851 1.00 38.82 ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 194.227 126.036 167.981 1.00 39.33 ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 192.996 125.490 167.272 1.00 37.75 ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 193.917 126.334 169.440 1.00 39.03 ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 197.199 122.811 169.383 1.00 44.61 ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 198.094 121.653 169.220 1.00 41.60 ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 198.181 121.143 167.792 1.00 40.11 ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 199.241 120.649 167.387 1.00 41.36 ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 197.479 120.603 170.156 1.00 39.99 ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 196.674 121.388 171.139 1.00 39.59 ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 196.144 122.561 170.379 1.00 41.10 ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 197.099 121.241 167.017 1.00 36.55 ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 197.111 120.716 165.657 1.00 38.80 ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 197.935 121.572 164.706 1.00 39.58 ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 198.381 121.069 163.669 1.00 39.07 ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 195.683 120.585 165.130 1.00 38.23 ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 198.150 122.847 165.030 1.00 37.59 ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 198.868 123.771 164.159 1.00 38.32 ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 200.181 124.231 164.785 1.00 42.16 ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 200.643 125.342 164.520 1.00 41.74 ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 197.991 124.975 163.815 1.00 36.88 ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 196.753 124.625 163.040 1.00 39.38 ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 196.827 124.324 161.690 1.00 38.69 ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 195.515 124.598 163.660 1.00 39.41 ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 195.689 124.004 160.975 1.00 36.56 ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 194.375 124.277 162.948 1.00 35.21 ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 194.464 123.980 161.605 1.00 35.26 ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 200.793 123.385 165.615 1.00 46.33 ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 202.022 123.778 166.299 1.00 46.27 ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 203.149 124.053 165.311 1.00 45.91 ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 203.911 125.014 165.479 1.00 45.97 ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 202.435 122.700 167.302 1.00 45.77 ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 202.359 121.279 166.763 1.00 45.77 ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 202.937 120.285 167.757 1.00 45.56 ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 204.445 120.434 167.875 1.00 44.60 ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 205.157 119.821 166.722 1.00 44.62 ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 203.270 123.226 164.275 1.00 45.42 ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 204.293 123.392 163.243 1.00 45.89 ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 203.707 123.943 161.949 1.00 45.09 ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 204.108 123.544 160.853 1.00 43.32 ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 205.008 122.068 162.989 1.00 46.94 ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 204.050 120.942 162.646 1.00 48.52 ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 202.825 121.127 162.812 1.00 47.90 ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 204.524 119.873 162.209 1.00 47.63 ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 202.744 124.861 162.058 1.00 38.80 ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 202.094 125.410 160.872 1.00 39.54 ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 203.068 126.218 160.022 1.00 41.38 ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 203.008 126.171 158.789 1.00 41.96 ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 200.899 126.267 161.280 1.00 37.53 ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 200.087 126.891 160.146 1.00 38.38 ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 199.324 125.824 159.383 1.00 37.13 ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 199.141 127.951 160.683 1.00 38.86 ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 203.962 126.977 160.662 1.00 40.28 ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 204.889 127.828 159.922 1.00 38.10 ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 205.817 126.987 159.054 1.00 38.92 ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 206.079 127.323 157.891 1.00 38.22 ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 205.681 128.724 160.892 1.00 38.80 ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 204.731 129.604 161.707 1.00 37.53 ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 206.683 129.581 160.135 1.00 38.57 ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 204.558 129.152 163.140 1.00 37.68 ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 206.336 125.887 159.605 1.00 39.76 ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 207.217 125.017 158.833 1.00 40.85 ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 206.486 124.401 157.646 1.00 42.12 ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 207.043 124.306 156.547 1.00 42.68 ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 207.798 123.928 159.733 1.00 38.46 ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 205.237 123.975 157.850 1.00 40.39 ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 204.459 123.412 156.751 1.00 41.47 ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 204.195 124.454 155.672 1.00 40.58 ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 204.253 124.148 154.475 1.00 40.96 ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 203.143 122.840 157.278 1.00 41.64 ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 203.281 121.502 157.982 1.00 41.20 ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 201.928 120.839 158.170 1.00 39.93 ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 202.065 119.477 158.826 1.00 40.70 ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 202.439 119.592 160.262 1.00 40.12 ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 203.890 125.688 156.076 1.00 37.91 ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 203.661 126.759 155.112 1.00 39.56 ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 204.924 127.033 154.308 1.00 42.42 ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 204.880 127.175 153.080 1.00 38.99 ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 203.162 128.027 155.832 1.00 40.31 ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 203.334 129.251 154.945 1.00 38.45 ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 201.713 127.865 156.253 1.00 38.99 ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 206.073 127.102 154.987 1.00 43.36 ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 207.324 127.398 154.297 1.00 41.69 ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 207.763 126.253 153.394 1.00 41.03 ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 208.395 126.491 152.360 1.00 41.25 ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 208.418 127.722 155.313 1.00 39.56 ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 208.246 129.067 155.998 1.00 42.70 ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 209.230 129.275 157.131 1.00 45.01 ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 209.996 128.375 157.477 1.00 43.85 ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 209.213 130.466 157.717 1.00 42.08 ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 207.442 125.012 153.763 1.00 40.09 ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 207.872 123.856 152.988 1.00 40.92 ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 207.007 123.596 151.761 1.00 42.84 ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 207.351 122.720 150.961 1.00 43.21 ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 207.885 122.608 153.874 1.00 40.50 ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 205.905 124.322 151.592 1.00 46.96 ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 204.995 124.120 150.468 1.00 47.60 ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 205.280 125.173 149.403 1.00 48.34 ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 205.106 126.372 149.642 1.00 48.96 ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 203.541 124.191 150.928 1.00 46.89 ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 203.007 122.849 151.381 1.00 48.39 ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 203.439 121.817 150.822 1.00 47.77 ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 202.155 122.823 152.293 1.00 47.27 ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 205.720 124.723 148.226 1.00 51.69 ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 205.933 125.637 147.111 1.00 52.39 ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 204.623 126.036 146.443 1.00 51.95 ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 204.512 127.154 145.925 1.00 49.83 ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 206.878 125.009 146.085 1.00 52.35 ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 206.447 123.638 145.589 1.00 52.16 ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 207.049 122.510 146.402 1.00 53.09 ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 207.829 122.795 147.335 1.00 52.06 ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 206.743 121.335 146.106 1.00 53.10 ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 203.628 125.151 146.447 1.00 48.34 ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 202.329 125.440 145.854 1.00 48.01 ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 201.422 126.238 146.780 1.00 46.90 ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 200.284 126.534 146.400 1.00 44.50 ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 201.630 124.139 145.452 1.00 46.56 ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 201.911 123.693 144.026 1.00 46.08 ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 203.302 123.116 143.860 1.00 47.38 ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 203.664 122.142 144.518 1.00 48.33 ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 204.091 123.716 142.976 1.00 48.12 ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 201.894 126.584 147.979 1.00 38.76 ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 201.068 127.341 148.914 1.00 37.00 ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 200.716 128.715 148.359 1.00 39.43 ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 199.594 129.200 148.547 1.00 39.64 ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 201.783 127.474 150.256 1.00 35.70 ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 200.952 128.127 151.316 1.00 35.36 ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 199.947 127.424 151.955 1.00 36.74 ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 201.169 129.447 151.667 1.00 34.05 ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 199.178 128.024 152.926 1.00 36.21 ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 200.403 130.051 152.638 1.00 34.68 ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 199.407 129.340 153.267 1.00 35.85 ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 201.667 129.365 147.687 1.00 35.09 ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 201.388 130.661 147.091 1.00 31.40 ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 200.315 130.602 146.022 1.00 32.33 ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 199.555 131.556 145.847 1.00 29.72 ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 200.246 129.490 145.288 1.00 33.33 ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 199.199 129.323 144.284 1.00 34.61 ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 197.830 129.268 144.949 1.00 35.45 ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 196.874 129.907 144.495 1.00 34.09 ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 199.466 128.065 143.438 1.00 34.29 ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 200.878 128.105 142.853 1.00 35.29 ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 198.432 127.938 142.331 1.00 29.49 ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 201.141 129.303 141.973 1.00 32.76 ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 197.713 128.500 146.037 1.00 32.46 ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 196.437 128.395 146.736 1.00 29.06 ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 196.053 129.714 147.394 1.00 29.12 ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 194.874 130.086 147.410 1.00 30.04 ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 196.497 127.276 147.777 1.00 29.13 ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 195.327 127.270 148.717 1.00 30.04 ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 194.102 126.720 148.492 1.00 28.25 ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 195.277 127.839 150.032 1.00 29.39 ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 193.289 126.909 149.584 1.00 26.38 ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 193.987 127.597 150.541 1.00 28.04 ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 196.196 128.532 150.825 1.00 29.69 ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 193.594 128.020 151.808 1.00 30.85 ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 195.802 128.951 152.081 1.00 27.17 ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 194.514 128.695 152.561 1.00 28.36 ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 197.035 130.434 147.943 1.00 28.83 ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 196.750 131.693 148.620 1.00 28.10 ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 196.181 132.746 147.678 1.00 30.17 ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 195.511 133.675 148.139 1.00 30.41 ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 198.018 132.225 149.290 1.00 28.20 ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 197.820 133.083 150.540 1.00 30.37 ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 197.064 132.311 151.607 1.00 31.71 ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 199.157 133.569 151.074 1.00 30.06 ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 196.433 132.627 146.376 1.00 35.96 ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 195.937 133.579 145.391 1.00 35.96 ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 194.790 133.021 144.559 1.00 36.33 ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 194.364 133.668 143.596 1.00 34.61 ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 197.076 134.031 144.474 1.00 34.07 ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 198.121 134.847 145.205 1.00 36.80 ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 197.770 135.918 145.742 1.00 37.23 ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 199.293 134.417 145.243 1.00 37.76 ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 194.281 131.842 144.902 1.00 31.55 ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 193.190 131.250 144.142 1.00 28.66 ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 191.890 132.010 144.384 1.00 30.42 ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 191.700 132.648 145.422 1.00 29.90 ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 193.017 129.778 144.513 1.00 29.11 ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 192.841 129.626 145.909 1.00 31.11 ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 190.993 131.940 143.398 1.00 30.98 ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 189.719 132.645 143.502 1.00 29.63 ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 188.866 132.086 144.633 1.00 30.01 ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 188.251 132.846 145.391 1.00 27.80 ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 188.968 132.565 142.174 1.00 26.32 ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 188.768 131.218 141.784 1.00 27.46 ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 188.816 130.762 144.766 1.00 27.04 ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 188.022 130.090 145.793 1.00 24.21 ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 188.919 129.107 146.532 1.00 24.12 ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 188.864 127.894 146.292 1.00 26.04 ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 186.812 129.384 145.184 1.00 26.67 ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 187.215 128.298 144.369 1.00 29.54 ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 189.771 129.599 147.435 1.00 22.32 ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 190.654 128.689 148.179 1.00 23.72 ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 189.911 127.683 149.039 1.00 27.30 ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 190.406 126.566 149.234 1.00 30.96 ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 191.500 129.643 149.031 1.00 24.88 ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 190.691 130.885 149.131 1.00 22.48 ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 189.966 131.004 147.830 1.00 24.24 ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 188.730 128.041 149.553 1.00 25.21 ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 188.012 127.163 150.470 1.00 21.61 ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 187.646 125.828 149.835 1.00 24.95 ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 187.414 124.853 150.558 1.00 24.37 ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 186.754 127.860 150.990 1.00 17.33 ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 185.567 127.798 150.047 1.00 21.48 ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 185.463 129.021 149.160 1.00 27.10 ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 186.193 130.002 149.410 1.00 28.31 ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 184.651 129.000 148.213 1.00 26.75 ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 187.586 125.761 148.504 1.00 28.58 ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 187.330 124.487 147.842 1.00 30.13 ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 188.505 123.529 147.989 1.00 32.76 ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 188.299 122.321 148.146 1.00 36.61 ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 187.024 124.715 146.363 1.00 29.36 ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 185.745 125.486 146.091 1.00 31.32 ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 184.510 124.764 146.587 1.00 37.00 ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 183.882 125.182 147.560 1.00 36.81 ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 184.154 123.672 145.920 1.00 34.80 ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 189.732 124.041 147.940 1.00 31.25 ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 190.939 123.221 147.879 1.00 31.62 ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 191.917 123.616 148.978 1.00 32.37 ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 193.102 123.850 148.732 1.00 33.36 ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 191.616 123.330 146.515 1.00 34.52 ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 192.285 124.594 146.411 1.00 37.01 ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 190.598 123.201 145.389 1.00 33.06 ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 191.430 123.704 150.208 1.00 33.51 ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 192.312 124.039 151.334 1.00 31.53 ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 193.329 122.917 151.523 1.00 31.96 ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 192.938 121.741 151.626 1.00 29.31 ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 191.495 124.258 152.606 1.00 27.33 ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 192.415 124.530 153.785 1.00 25.30 ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 190.522 125.405 152.420 1.00 27.26 ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 194.625 123.219 151.564 1.00 33.28 ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 195.621 122.156 151.728 1.00 32.50 ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 195.556 121.526 153.108 1.00 35.19 ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 195.155 122.154 154.090 1.00 35.45 ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 196.952 122.885 151.514 1.00 32.40 ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 196.662 124.299 151.881 1.00 31.23 ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 195.246 124.549 151.452 1.00 31.51 ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 195.967 120.260 153.172 1.00 37.84 ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 196.036 119.519 154.431 1.00 38.07 ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 197.242 120.031 155.212 1.00 37.11 ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 198.343 119.478 155.166 1.00 39.20 ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 196.126 118.022 154.164 1.00 38.44 ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 196.241 117.176 155.409 1.00 39.12 ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 195.223 117.152 156.351 1.00 37.34 ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 197.369 116.402 155.641 1.00 38.01 ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 195.325 116.376 157.489 1.00 39.13 ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 197.480 115.626 156.775 1.00 39.48 ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 196.457 115.617 157.695 1.00 41.12 ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 196.568 114.843 158.825 1.00 41.06 ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 197.022 121.120 155.949 1.00 33.64 ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 198.096 121.867 156.588 1.00 35.46 ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 198.134 121.667 158.101 1.00 37.74 ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 198.728 122.481 158.813 1.00 39.97 ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 197.962 123.351 156.249 1.00 35.74 ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 199.250 124.154 156.079 1.00 38.62 ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 200.162 123.477 155.072 1.00 39.98 ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 198.927 125.571 155.641 1.00 36.95 ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 197.516 120.604 158.606 1.00 34.48 ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 197.507 120.313 160.031 1.00 34.97 ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 197.952 118.876 160.262 1.00 38.42 ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 197.860 118.024 159.374 1.00 38.26 ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 196.122 120.544 160.654 1.00 34.04 ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 195.046 119.683 160.077 1.00 35.90 ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 194.662 118.449 160.514 1.00 36.32 ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 194.206 119.990 158.959 1.00 36.35 ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 193.639 117.968 159.736 1.00 36.90 ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 193.339 118.895 158.773 1.00 36.41 ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 194.103 121.085 158.096 1.00 34.98 ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 192.385 118.863 157.761 1.00 34.53 ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 193.156 121.051 157.092 1.00 35.85 ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 192.308 119.947 156.932 1.00 35.76 ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 198.437 118.617 161.471 1.00 43.83 ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 198.945 117.307 161.857 1.00 44.50 ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 198.024 116.689 162.899 1.00 46.20 ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 197.703 117.326 163.908 1.00 44.07 ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 200.368 117.411 162.407 1.00 43.66 ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 200.403 118.204 163.580 1.00 45.88 ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 197.604 115.450 162.653 1.00 50.37 ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 196.749 114.709 163.568 1.00 49.59 ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 197.297 113.303 163.747 1.00 50.54 ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 197.819 112.704 162.802 1.00 48.58 ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 195.306 114.647 163.054 1.00 48.50 ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 195.184 114.193 161.610 1.00 48.22 ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 193.862 114.590 160.982 1.00 50.34 ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 193.424 115.739 161.194 1.00 51.32 ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 193.265 113.753 160.272 1.00 47.52 ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 197.181 112.779 164.969 1.00 57.44 ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 197.638 111.421 165.238 1.00 57.84 ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 196.695 110.385 164.640 1.00 57.13 ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 197.135 109.299 164.247 1.00 55.90 ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 197.786 111.199 166.743 1.00 56.55 ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 198.884 112.031 167.393 1.00 57.56 ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 198.448 113.454 167.689 1.00 59.53 ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 197.268 113.781 167.446 1.00 57.87 ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 199.288 114.247 168.164 1.00 59.06 ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 195.406 110.701 164.562 1.00 53.07 ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 194.399 109.834 163.976 1.00 52.28 ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 193.623 110.609 162.923 1.00 51.73 ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 193.479 111.831 163.030 1.00 49.00 ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 193.435 109.301 165.050 1.00 50.45 ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 192.405 108.516 164.435 1.00 50.29 ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 192.803 110.448 165.826 1.00 50.00 ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 193.135 109.933 161.881 1.00 47.57 ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 192.369 110.637 160.847 1.00 46.60 ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 191.160 111.348 161.436 1.00 47.09 ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 190.481 110.833 162.326 1.00 44.92 ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 191.952 109.515 159.891 1.00 42.90 ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 193.020 108.490 160.047 1.00 44.98 ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 193.443 108.545 161.491 1.00 44.53 ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 190.901 112.548 160.928 1.00 40.05 ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 189.826 113.384 161.435 1.00 35.74 ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 188.540 113.142 160.656 1.00 34.84 ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 188.559 112.824 159.464 1.00 32.77 ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 190.208 114.863 161.359 1.00 33.52 ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 187.418 113.298 161.351 1.00 32.77 ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 186.115 113.162 160.731 1.00 31.46 ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 185.872 114.320 159.765 1.00 33.02 ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 186.523 115.363 159.857 1.00 31.10 ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 185.027 113.124 161.802 1.00 30.96 ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 184.797 114.448 162.299 1.00 30.54 ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 185.450 112.227 162.953 1.00 31.97 ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 184.950 114.150 158.810 1.00 31.68 ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 184.669 115.250 157.871 1.00 29.02 ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 184.281 116.548 158.553 1.00 25.56 ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 184.631 117.625 158.054 1.00 25.49 ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 183.521 114.698 157.009 1.00 26.71 ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 183.088 113.414 157.664 1.00 26.98 ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 184.269 112.909 158.414 1.00 26.90 ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 183.568 116.486 159.679 1.00 23.56 ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 183.274 117.701 160.434 1.00 24.86 ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 184.558 118.312 160.985 1.00 24.56 ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 184.749 119.533 160.939 1.00 26.23 ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 182.255 117.416 161.553 1.00 26.04 ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 180.912 116.962 160.974 1.00 21.59 ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 182.067 118.647 162.424 1.00 20.70 ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 180.784 115.467 160.776 1.00 24.81 ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 185.453 117.480 161.519 1.00 22.56 ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 186.728 117.992 161.995 1.00 23.36 ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 187.571 118.576 160.878 1.00 25.09 ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 188.236 119.601 161.056 1.00 26.49 ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 187.556 117.928 159.709 1.00 23.53 ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 188.249 118.479 158.552 1.00 21.90 ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 187.672 119.832 158.166 1.00 22.14 ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 188.419 120.766 157.855 1.00 25.43 ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 188.164 117.509 157.374 1.00 23.79 ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 189.274 116.479 157.330 1.00 27.94 ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 189.066 115.454 156.234 1.00 30.19 ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 188.017 115.417 155.593 1.00 26.20 ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 190.071 114.613 156.013 1.00 28.33 ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 186.344 119.958 158.183 1.00 19.05 ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 185.715 121.235 157.868 1.00 15.76 ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 186.099 122.303 158.882 1.00 17.79 ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 186.325 123.460 158.516 1.00 23.14 ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 184.197 121.073 157.806 1.00 15.98 ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 186.173 121.937 160.164 1.00 16.54 ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 186.554 122.903 161.192 1.00 16.45 ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 187.989 123.373 160.983 1.00 19.00 ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 188.289 124.570 161.086 1.00 26.35 ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 186.359 122.299 162.594 1.00 18.18 ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 184.877 122.042 162.860 1.00 19.71 ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 186.931 123.221 163.655 1.00 19.28 ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 184.566 121.660 164.282 1.00 19.46 ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 188.899 122.440 160.699 1.00 22.11 ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 190.289 122.824 160.467 1.00 18.85 ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 190.428 123.676 159.211 1.00 21.74 ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 191.205 124.638 159.189 1.00 25.54 ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 191.169 121.578 160.384 1.00 20.79 ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 191.446 120.952 161.716 1.00 25.88 ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 190.996 119.694 162.055 1.00 26.64 ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 192.121 121.414 162.795 1.00 25.60 ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 191.384 119.408 163.284 1.00 26.42 ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 192.070 120.434 163.756 1.00 26.03 ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 189.681 123.341 158.155 1.00 21.09 ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 189.687 124.163 156.950 1.00 16.90 ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 189.144 125.558 157.234 1.00 16.64 ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 189.647 126.549 156.699 1.00 18.80 ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 188.870 123.486 155.849 1.00 13.01 ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 189.487 122.211 155.310 1.00 16.40 ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 189.020 121.929 153.896 1.00 22.67 ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 189.359 120.577 153.471 1.00 24.02 ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 188.541 119.538 153.557 1.00 23.04 ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 187.318 119.660 154.047 1.00 21.34 ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 188.959 118.346 153.142 1.00 21.20 ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 188.105 125.649 158.067 1.00 18.35 ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 187.555 126.945 158.446 1.00 15.06 ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 188.579 127.775 159.208 1.00 15.88 ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 188.722 128.979 158.965 1.00 21.44 ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 186.293 126.738 159.281 1.00 13.48 ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 185.434 127.940 159.667 1.00 16.18 ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 184.841 128.602 158.439 1.00 19.86 ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 184.335 127.504 160.619 1.00 15.29 ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 189.306 127.143 160.131 1.00 17.18 ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 190.354 127.851 160.862 1.00 19.50 ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 191.456 128.327 159.923 1.00 19.57 ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 191.928 129.468 160.032 1.00 17.24 ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 190.933 126.950 161.951 1.00 19.69 ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 190.018 126.630 163.132 1.00 17.09 ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 190.680 125.632 164.061 1.00 21.98 ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 189.663 127.899 163.879 1.00 19.68 ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 191.875 127.469 158.990 1.00 19.32 ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 192.914 127.853 158.040 1.00 19.75 ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 192.456 129.000 157.150 1.00 20.34 ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 193.229 129.923 156.868 1.00 20.17 ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 193.319 126.649 157.192 1.00 18.66 ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 194.298 125.671 157.839 1.00 21.28 ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 194.497 124.457 156.950 1.00 21.25 ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 195.623 126.354 158.124 1.00 21.89 ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 191.205 128.956 156.691 1.00 20.86 ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 190.676 130.024 155.852 1.00 14.59 ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 190.602 131.330 156.631 1.00 13.52 ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 190.962 132.395 156.120 1.00 21.00 ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 189.306 129.620 155.277 1.00 15.21 ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 189.485 128.621 154.135 1.00 16.06 ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 188.547 130.837 154.793 1.00 17.54 ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 190.186 129.197 152.932 1.00 18.24 ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 190.147 131.269 157.884 1.00 12.42 ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 190.101 132.471 158.710 1.00 16.37 ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 191.495 133.055 158.904 1.00 20.49 ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 191.671 134.279 158.883 1.00 21.13 ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 189.456 132.151 160.058 1.00 18.19 ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 189.790 133.133 161.163 1.00 15.65 ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 188.976 132.892 162.415 1.00 19.75 ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 189.433 132.229 163.345 1.00 24.43 ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 187.767 133.434 162.448 1.00 19.66 ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 192.497 132.195 159.097 1.00 24.91 ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 193.861 132.685 159.275 1.00 20.55 ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 194.416 133.288 157.988 1.00 21.63 ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 195.076 134.332 158.022 1.00 26.72 ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 194.762 131.554 159.766 1.00 20.87 ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 194.157 132.652 156.846 1.00 19.88 ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 194.784 133.010 155.579 1.00 19.38 ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 193.916 133.907 154.705 1.00 21.52 ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 194.359 134.983 154.292 1.00 25.97 ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 195.151 131.739 154.805 1.00 22.93 ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 196.310 130.990 155.390 1.00 26.82 ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 197.515 131.629 155.621 1.00 24.39 ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 196.191 129.650 155.721 1.00 25.24 ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 198.581 130.944 156.159 1.00 22.62 ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 197.256 128.961 156.262 1.00 23.45 ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 198.451 129.609 156.485 1.00 24.67 ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 192.686 133.489 154.414 1.00 22.57 ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 191.816 134.173 153.458 1.00 17.32 ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 190.500 134.503 154.145 1.00 14.53 ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 189.481 133.837 153.914 1.00 18.99 ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 191.582 133.312 152.216 1.00 18.97 ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 192.833 133.037 151.400 1.00 20.36 ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 193.311 134.286 150.684 1.00 22.16 ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 192.273 134.854 149.832 1.00 21.91 ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 192.022 134.457 148.594 1.00 21.26 ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 192.715 133.486 148.025 1.00 22.05 ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 191.049 135.049 147.908 1.00 19.51 ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 190.484 135.524 155.007 1.00 13.11 ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 189.242 135.854 155.724 1.00 15.12 ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 188.092 136.237 154.807 1.00 18.62 ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 186.928 136.037 155.178 1.00 19.31 ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 189.657 137.021 156.630 1.00 12.02 ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 190.889 137.577 156.005 1.00 14.20 ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 191.591 136.422 155.372 1.00 17.25 ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 188.383 136.778 153.622 1.00 17.21 ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 187.315 137.174 152.709 1.00 13.68 ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 186.491 135.977 152.255 1.00 17.69 ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 185.296 136.119 151.969 1.00 20.93 ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 187.899 137.912 151.504 1.00 14.19 ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 188.918 137.085 150.748 1.00 19.05 ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 190.093 137.056 151.168 1.00 16.39 ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 188.547 136.470 149.728 1.00 22.07 ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 187.099 134.798 152.188 1.00 17.25 ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 186.390 133.574 151.847 1.00 14.01 ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 185.767 132.895 153.058 1.00 15.84 ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 185.086 131.877 152.893 1.00 19.96 ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 187.334 132.599 151.140 1.00 11.41 ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 188.020 133.185 149.926 1.00 12.12 ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 187.005 133.699 148.925 1.00 16.19 ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 186.139 132.633 148.436 1.00 19.68 ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 184.998 132.833 147.794 1.00 20.16 ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 184.549 134.052 147.548 1.00 19.11 ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 184.287 131.784 147.393 1.00 16.28 ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 185.969 133.449 154.258 1.00 14.06 ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 185.501 132.807 155.482 1.00 10.19 ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 184.024 132.449 155.396 1.00 12.62 ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 183.637 131.301 155.639 1.00 16.24 ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 185.761 133.723 156.679 1.00 8.14  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 185.351 133.188 158.051 1.00 8.65  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 186.194 131.988 158.425 1.00 11.87 ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 185.467 134.276 159.103 1.00 13.40 ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 183.189 133.421 155.013 1.00 12.84 ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 181.760 133.166 154.868 1.00 8.39  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 181.510 131.951 153.991 1.00 9.68  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 180.785 131.027 154.379 1.00 17.27 ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 181.063 134.394 154.284 1.00 8.18  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 180.678 135.516 155.245 1.00 11.85 ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 179.907 136.585 154.498 1.00 11.37 ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 179.864 134.972 156.405 1.00 10.18 ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 182.142 131.915 152.814 1.00 6.83  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 181.987 130.766 151.932 1.00 5.88  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 182.376 129.485 152.653 1.00 10.89 ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 181.610 128.513 152.676 1.00 15.15 ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 182.825 130.956 150.669 1.00 9.01  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 183.540 129.492 153.308 1.00 10.91 ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 183.962 128.315 154.054 1.00 8.70  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 182.958 127.986 155.147 1.00 8.86  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 182.640 126.812 155.376 1.00 13.57 ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 185.356 128.535 154.642 1.00 9.31  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 185.971 127.288 155.243 1.00 12.53 ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 186.169 125.951 154.053 1.00 22.03 ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 185.431 124.592 154.953 1.00 10.81 ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 182.418 129.016 155.806 1.00 7.33  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 181.390 128.788 156.812 1.00 4.81  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 180.231 128.003 156.222 1.00 5.30  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 179.762 127.027 156.821 1.00 12.27 ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 180.904 130.121 157.382 1.00 4.56  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 179.791 128.382 155.017 1.00 5.98  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 178.717 127.644 154.366 1.00 5.24  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 179.086 126.176 154.218 1.00 6.73  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 178.280 125.291 154.532 1.00 8.46  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 178.404 128.262 153.004 1.00 6.28  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 177.535 129.478 153.079 1.00 11.42 ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 178.015 130.713 153.455 1.00 10.08 ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 176.216 129.647 152.826 1.00 11.89 ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 177.030 131.593 153.430 1.00 10.59 ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 175.927 130.972 153.052 1.00 15.69 ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 180.323 125.900 153.793 1.00 7.55  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 180.766 124.519 153.666 1.00 7.50  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 180.622 123.780 154.987 1.00 9.35  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 180.140 122.641 155.019 1.00 12.32 ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 182.214 124.471 153.179 1.00 10.45 ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 182.470 125.252 151.904 1.00 11.32 ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 183.772 124.510 150.905 1.00 25.49 ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 182.836 123.289 149.989 1.00 14.11 ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 180.989 124.431 156.095 1.00 8.36  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 180.851 123.784 157.395 1.00 6.17  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 179.404 123.395 157.650 1.00 7.36  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 179.126 122.282 158.110 1.00 8.47  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 181.365 124.698 158.505 1.00 8.04  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 181.145 124.151 159.885 1.00 12.07 ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 181.925 123.115 160.366 1.00 13.10 ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 180.151 124.663 160.699 1.00 14.10 ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 181.719 122.608 161.633 1.00 12.76 ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 179.942 124.161 161.968 1.00 9.87  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 180.727 123.132 162.434 1.00 9.90  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 178.466 124.284 157.315 1.00 7.82  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 177.056 123.946 157.464 1.00 4.34  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 176.719 122.736 156.606 1.00 8.63  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 176.064 121.792 157.064 1.00 14.44 ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 176.174 125.159 157.119 1.00 5.62  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 174.704 124.800 157.239 1.00 5.50  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 176.517 126.332 158.019 1.00 5.99  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 177.206 122.724 155.362 1.00 4.77  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 176.959 121.583 154.489 1.00 5.47  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 177.581 120.311 155.047 1.00 10.16 ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 177.117 119.207 154.742 1.00 12.37 ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 177.499 121.869 153.088 1.00 12.97 ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 177.006 123.104 152.597 1.00 14.45 ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 178.623 120.443 155.868 1.00 10.62 ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 179.221 119.268 156.486 1.00 8.96  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 178.364 118.730 157.624 1.00 12.65 ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 178.383 117.523 157.892 1.00 17.37 ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 180.626 119.596 156.995 1.00 11.21 ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 181.310 120.392 156.020 1.00 15.48 ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 181.416 118.323 157.232 1.00 12.33 ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 177.601 119.597 158.290 1.00 9.07  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 176.814 119.202 159.451 1.00 4.78  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 175.342 119.001 159.121 1.00 7.80  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 174.741 118.002 159.528 1.00 10.37 ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 176.952 120.250 160.559 1.00 3.56  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 178.337 120.280 161.164 1.00 9.59  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 179.316 120.595 160.488 1.00 11.30 ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 178.430 119.953 162.446 1.00 14.82 ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 174.749 119.937 158.379 1.00 7.61  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 173.310 119.977 158.182 1.00 5.21  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 172.862 119.550 156.792 1.00 10.61 ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 171.682 119.235 156.615 1.00 16.50 ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 172.794 121.393 158.471 1.00 6.54  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 172.972 121.822 159.929 1.00 3.08  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 172.691 123.295 160.108 1.00 6.17  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 172.054 121.009 160.817 1.00 2.60  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 173.761 119.526 155.814 1.00 11.72 ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 173.398 119.121 154.470 1.00 12.27 ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 173.662 120.189 153.430 1.00 17.98 ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 173.699 121.381 153.748 1.00 19.41 ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 173.853 119.769 152.176 1.00 19.88 ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 174.114 120.724 151.105 1.00 18.84 ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 172.913 121.630 150.860 1.00 20.77 ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 173.073 122.835 150.629 1.00 22.02 ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 174.495 119.983 149.825 1.00 20.79 ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 175.856 119.311 149.875 1.00 25.12 ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 176.895 120.042 149.047 1.00 29.64 ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 176.530 121.015 148.355 1.00 26.84 ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 178.077 119.641 149.088 1.00 26.86 ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 171.704 121.072 150.903 1.00 16.68 ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 170.485 121.812 150.613 1.00 18.02 ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 169.821 122.374 151.864 1.00 18.13 ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 168.605 122.600 151.860 1.00 18.74 ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 169.501 120.923 149.851 1.00 17.86 ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 169.105 119.815 150.639 1.00 16.68 ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 170.586 122.597 152.934 1.00 14.14 ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 169.996 123.115 154.164 1.00 11.06 ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 169.533 124.557 153.997 1.00 15.41 ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 168.423 124.910 154.409 1.00 17.23 ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 170.996 123.004 155.313 1.00 4.10  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 170.412 123.333 156.652 1.00 3.48  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 169.614 122.421 157.317 1.00 7.69  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 170.649 124.561 157.242 1.00 5.88  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 169.074 122.722 158.546 1.00 8.01  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 170.108 124.869 158.470 1.00 5.45  ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 169.321 123.945 159.125 1.00 7.06  ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 170.368 125.402 153.398 1.00 11.39 ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 170.055 126.811 153.202 1.00 6.94  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 169.544 127.106 151.798 1.00 15.11 ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 169.433 128.277 151.424 1.00 18.51 ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 171.286 127.668 153.500 1.00 6.78  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 171.980 127.321 154.805 1.00 8.24  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 173.469 128.295 155.095 1.00 13.89 ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 172.766 129.919 155.352 1.00 6.05  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 169.231 126.071 151.015 1.00 12.33 ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 168.808 126.281 149.634 1.00 13.75 ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 167.443 126.950 149.546 1.00 17.92 ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 167.199 127.734 148.623 1.00 22.66 ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 168.794 124.951 148.882 1.00 18.54 ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 170.109 124.524 148.580 1.00 22.46 ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 166.544 126.658 150.490 1.00 16.94 ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 165.197 127.218 150.441 1.00 17.02 ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 165.210 128.733 150.586 1.00 13.41 ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 164.248 129.399 150.189 1.00 17.88 ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 164.307 126.563 151.519 1.00 16.18 ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 162.830 126.682 151.142 1.00 14.06 ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 164.565 127.182 152.879 1.00 13.52 ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 162.458 125.917 149.891 1.00 14.18 ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 166.280 129.300 151.142 1.00 9.49  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 166.390 130.747 151.251 1.00 13.03 ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 166.763 131.404 149.929 1.00 20.18 ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 166.621 132.624 149.797 1.00 22.06 ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 167.419 131.116 152.320 1.00 11.51 ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 166.914 130.958 153.742 1.00 12.84 ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 165.331 131.774 154.008 1.00 20.02 ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 164.339 130.403 154.587 1.00 9.92  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 167.236 130.626 148.954 1.00 21.63 ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 167.590 131.166 147.649 1.00 20.59 ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 166.411 131.216 146.686 1.00 21.95 ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 166.551 131.772 145.592 1.00 23.84 ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 168.719 130.340 147.029 1.00 20.28 ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 169.761 129.869 148.028 1.00 24.60 ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 170.754 128.896 147.422 1.00 30.03 ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 170.423 128.273 146.391 1.00 29.69 ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 171.864 128.752 147.977 1.00 28.29 ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 165.268 130.653 147.061 1.00 22.89 ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 164.064 130.617 146.250 1.00 23.44 ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 163.118 131.744 146.645 1.00 24.17 ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 163.150 132.218 147.785 1.00 23.26 ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 163.350 129.272 146.405 1.00 20.30 ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 164.211 128.073 146.044 1.00 21.48 ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 164.387 127.914 144.546 1.00 28.11 ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 163.438 128.065 143.778 1.00 26.84 ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 165.607 127.606 144.124 1.00 29.53 ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 162.275 132.207 145.721 1.00 25.81 ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 161.306 133.251 146.071 1.00 23.67 ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 160.357 132.782 147.163 1.00 25.04 ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 159.986 131.609 147.233 1.00 26.21 ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 160.565 133.508 144.753 1.00 22.01 ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 160.843 132.311 143.905 1.00 23.28 ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 162.208 131.849 144.295 1.00 25.07 ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 159.975 133.719 148.026 1.00 20.49 ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 159.106 133.397 149.150 1.00 17.86 ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 157.750 132.912 148.656 1.00 23.51 ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 157.136 133.530 147.781 1.00 29.05 ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 158.941 134.621 150.051 1.00 16.06 ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 157.968 134.501 151.224 1.00 18.78 ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 158.407 133.403 152.170 1.00 16.38 ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 157.859 135.826 151.957 1.00 17.24 ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 157.282 131.800 149.222 1.00 22.10 ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 155.998 131.210 148.852 1.00 22.31 ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 154.978 131.587 149.922 1.00 26.29 ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 154.718 130.846 150.868 1.00 30.09 ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 156.127 129.700 148.690 1.00 25.98 ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 154.856 129.060 148.170 1.00 30.58 ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 154.563 129.211 146.966 1.00 31.01 ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 154.152 128.407 148.966 1.00 29.92 ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 154.388 132.773 149.751 1.00 22.00 ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 153.469 133.299 150.754 1.00 22.35 ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 152.180 132.493 150.832 1.00 22.99 ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 151.553 132.437 151.897 1.00 27.54 ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 153.154 134.763 150.454 1.00 23.79 ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 153.918 135.809 151.263 1.00 23.30 ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 153.509 137.205 150.832 1.00 22.46 ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 153.677 135.612 152.749 1.00 19.66 ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 151.768 131.870 149.725 1.00 24.33 ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 150.473 131.193 149.691 1.00 27.38 ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 150.398 130.080 150.728 1.00 29.89 ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 149.493 130.064 151.572 1.00 31.49 ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 150.218 130.631 148.293 1.00 29.03 ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 150.204 131.697 147.335 1.00 30.30 ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 148.888 129.897 148.250 1.00 27.17 ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 151.355 129.151 150.691 1.00 27.62 ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 151.324 128.017 151.607 1.00 28.76 ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 151.514 128.462 153.051 1.00 28.80 ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 150.845 127.951 153.956 1.00 27.71 ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 152.393 126.997 151.219 1.00 27.54 ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 152.518 125.857 152.182 1.00 33.26 ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 151.459 125.036 152.504 1.00 34.88 ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 153.574 125.404 152.895 1.00 30.69 ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 151.859 124.126 153.373 1.00 31.18 ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 153.138 124.327 153.627 1.00 33.98 ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 152.421 129.411 153.285 1.00 23.14 ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 152.702 129.848 154.649 1.00 22.96 ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 151.477 130.511 155.262 1.00 22.89 ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 151.133 130.259 156.423 1.00 25.76 ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 153.923 130.783 154.671 1.00 20.75 ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 155.112 130.114 153.980 1.00 22.18 ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 154.280 131.140 156.097 1.00 20.15 ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 156.369 130.948 153.992 1.00 23.76 ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 150.799 131.369 154.498 1.00 22.87 ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 149.604 132.026 155.015 1.00 21.32 ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 148.476 131.016 155.203 1.00 24.39 ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 147.774 131.036 156.222 1.00 20.85 ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 149.188 133.182 154.088 1.00 20.52 ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 147.774 133.635 154.401 1.00 22.97 ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 150.159 134.341 154.229 1.00 20.33 ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 148.288 130.114 154.238 1.00 27.37 ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 147.185 129.173 154.330 1.00 27.56 ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 147.332 128.174 155.462 1.00 27.38 ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 146.348 127.805 156.106 1.00 28.07 ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 148.558 127.721 155.724 1.00 29.27 ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 148.785 126.619 156.649 1.00 31.06 ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 149.551 127.024 157.898 1.00 30.23 ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 149.114 126.717 159.013 1.00 29.92 ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 149.533 125.483 155.933 1.00 30.17 ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 148.868 125.171 154.703 1.00 31.80 ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 149.580 124.242 156.808 1.00 27.15 ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 150.684 127.704 157.749 1.00 23.35 ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 151.603 127.925 158.858 1.00 19.62 ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 151.267 129.145 159.702 1.00 21.07 ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 151.946 129.388 160.704 1.00 19.15 ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 153.035 128.054 158.331 1.00 17.30 ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 153.408 127.021 157.285 1.00 21.76 ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 154.826 127.191 156.782 1.00 24.61 ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 155.533 128.087 157.290 1.00 21.52 ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 155.234 126.431 155.881 1.00 25.74 ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 150.249 129.919 159.336 1.00 23.65 ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 149.886 131.132 160.061 1.00 21.02 ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 148.480 130.957 160.616 1.00 22.84 ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 147.537 130.692 159.860 1.00 24.35 ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 149.972 132.380 159.168 1.00 13.99 ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 149.310 133.562 159.848 1.00 13.61 ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 151.420 132.696 158.839 1.00 13.79 ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 148.344 131.099 161.930 1.00 17.19 ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 147.042 131.068 162.570 1.00 15.21 ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 146.334 132.411 162.394 1.00 17.83 ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 146.988 133.446 162.241 1.00 19.48 ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 147.185 130.748 164.054 1.00 17.06 ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 147.283 129.264 164.360 1.00 18.21 ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 148.094 129.013 165.620 1.00 19.06 ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 148.717 127.628 165.607 1.00 15.84 ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 149.638 127.450 164.453 1.00 16.24 ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 144.998 132.419 162.401 1.00 18.95 ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 144.281 133.695 162.250 1.00 18.49 ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 144.590 134.695 163.348 1.00 16.95 ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 144.537 135.908 163.102 1.00 14.82 ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 142.804 133.273 162.269 1.00 17.34 ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 142.794 131.930 162.915 1.00 16.00 ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 144.076 131.278 162.515 1.00 18.74 ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 144.908 134.228 164.553 1.00 16.82 ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 145.227 135.135 165.646 1.00 15.78 ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 146.604 135.764 165.496 1.00 19.86 ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 146.853 136.829 166.072 1.00 20.43 ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 145.137 134.394 166.981 1.00 16.18 ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 144.678 135.287 168.110 1.00 19.83 ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 144.359 136.455 167.897 1.00 21.14 ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 144.643 134.744 169.320 1.00 21.36 ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 147.501 135.135 164.739 1.00 17.79 ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 148.861 135.631 164.583 1.00 8.99  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 148.937 136.576 163.392 1.00 10.88 ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 148.674 136.147 162.260 1.00 13.84 ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 149.830 134.477 164.387 1.00 7.71  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 149.785 133.614 165.529 1.00 16.31 ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 151.242 134.991 164.200 1.00 4.34  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 149.277 137.848 163.590 1.00 8.39  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 149.439 138.750 162.447 1.00 5.18  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 150.660 138.387 161.617 1.00 8.52  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 151.622 137.791 162.108 1.00 16.42 ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 149.600 140.128 163.096 1.00 3.04  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 150.078 139.843 164.474 1.00 5.10  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 149.449 138.544 164.875 1.00 7.41  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 150.607 138.752 160.343 1.00 6.11  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 151.701 138.540 159.405 1.00 2.32  ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 152.450 139.862 159.302 1.00 2.21  ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 152.011 140.786 158.613 1.00 13.27 ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 151.189 138.067 158.041 1.00 4.46  ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 152.348 137.747 157.121 1.00 10.02 ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 150.281 136.860 158.206 1.00 3.90  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 153.581 139.963 159.997 1.00 3.61  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 154.354 141.200 160.065 1.00 3.06  ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 155.357 141.205 158.920 1.00 4.23  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 156.362 140.491 158.967 1.00 9.58  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 155.067 141.308 161.408 1.00 3.24  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 154.183 141.315 162.650 1.00 4.64  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 155.042 141.275 163.890 1.00 4.76  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 153.286 142.530 162.661 1.00 12.76 ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 155.096 142.012 157.900 1.00 5.02  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 155.927 142.043 156.701 1.00 4.47  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 156.842 143.257 156.795 1.00 6.92  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 156.447 144.377 156.462 1.00 11.53 ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 155.054 142.077 155.456 1.00 4.95  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 153.825 141.207 155.598 1.00 10.10 ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 153.167 140.622 154.039 1.00 22.07 ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 154.123 139.127 153.840 1.00 11.69 ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 158.069 143.028 157.253 1.00 5.09  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 159.038 144.091 157.465 1.00 4.19  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 159.977 144.153 156.272 1.00 6.54  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 160.576 143.141 155.894 1.00 11.86 ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 159.825 143.855 158.754 1.00 5.44  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 158.820 143.248 160.124 1.00 16.00 ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 160.102 145.333 155.679 1.00 8.06  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 160.882 145.506 154.464 1.00 7.68  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 161.918 146.603 154.652 1.00 8.69  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 161.685 147.589 155.354 1.00 10.74 ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 159.985 145.836 153.267 1.00 9.92  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 159.225 147.006 153.509 1.00 12.97 ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 163.069 146.415 154.015 1.00 11.10 ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 164.122 147.426 153.992 1.00 14.76 ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 163.622 148.595 153.152 1.00 22.58 ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 162.704 148.414 152.338 1.00 23.57 ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 165.436 146.850 153.444 1.00 12.29 ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 165.909 145.697 154.310 1.00 12.34 ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 165.257 146.401 152.005 1.00 11.58 ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 164.159 149.803 153.325 1.00 19.82 ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 163.702 150.931 152.506 1.00 16.02 ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 163.874 150.643 151.021 1.00 18.47 ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 164.871 150.059 150.592 1.00 19.31 ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 164.594 152.087 152.964 1.00 18.77 ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 164.984 151.724 154.354 1.00 19.95 ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 165.113 150.230 154.367 1.00 18.01 ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 162.883 151.063 150.238 1.00 18.69 ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 162.836 150.753 148.828 1.00 21.61 ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 162.090 149.483 148.480 1.00 18.58 ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 161.921 149.191 147.289 1.00 20.86 ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 161.644 148.720 149.473 1.00 12.90 ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 160.874 147.506 149.253 1.00 17.44 ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 159.541 147.613 149.978 1.00 21.46 ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 159.472 148.113 151.104 1.00 25.76 ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 161.643 146.267 149.724 1.00 13.09 ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 162.638 145.778 148.702 1.00 18.21 ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 163.812 146.478 148.461 1.00 15.80 ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 162.395 144.630 147.962 1.00 14.36 ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 164.719 146.044 147.519 1.00 14.92 ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 163.297 144.188 147.018 1.00 15.28 ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 164.458 144.899 146.801 1.00 19.36 ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 165.361 144.466 145.859 1.00 23.06 ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 158.481 147.151 149.317 1.00 16.76 ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 157.130 147.233 149.857 1.00 14.85 ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 156.423 145.917 149.583 1.00 19.22 ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 156.337 145.485 148.430 1.00 17.58 ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 156.363 148.405 149.236 1.00 13.51 ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 154.906 148.429 149.643 1.00 18.79 ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 154.624 148.364 150.858 1.00 20.28 ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 154.041 148.522 148.747 1.00 15.45 ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 155.921 145.284 150.640 1.00 15.97 ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 155.258 143.993 150.532 1.00 12.12 ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 153.757 144.108 150.315 1.00 18.29 ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 153.077 143.079 150.261 1.00 22.29 ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 155.533 143.156 151.783 1.00 13.42 ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 153.224 145.326 150.195 1.00 15.02 ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 151.792 145.489 149.969 1.00 12.74 ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 151.371 144.861 148.646 1.00 15.68 ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 150.310 144.230 148.557 1.00 15.41 ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 151.422 146.971 149.999 1.00 16.35 ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 151.796 147.563 151.230 1.00 21.18 ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 152.188 145.032 147.606 1.00 18.86 ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 151.891 144.398 146.334 1.00 21.01 ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 151.852 142.886 146.436 1.00 22.20 ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 151.033 142.233 145.787 1.00 23.46 ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 152.734 142.310 147.256 1.00 21.06 ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 152.724 140.865 147.460 1.00 19.86 ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 151.398 140.408 148.052 1.00 22.68 ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 150.807 139.424 147.596 1.00 23.18 ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 153.883 140.452 148.367 1.00 18.82 ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 155.236 140.639 147.752 1.00 20.69 ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 156.243 139.709 147.880 1.00 22.79 ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 155.749 141.651 147.014 1.00 22.28 ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 157.318 140.137 147.243 1.00 23.72 ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 157.044 141.313 146.710 1.00 23.93 ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 150.909 141.122 149.067 1.00 22.27 ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 149.653 140.740 149.707 1.00 18.35 ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 148.485 140.922 148.751 1.00 23.26 ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 147.570 140.092 148.707 1.00 24.41 ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 149.445 141.538 151.004 1.00 17.08 ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 148.307 140.944 151.808 1.00 18.24 ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 150.714 141.558 151.816 1.00 17.25 ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 148.480 142.016 147.985 1.00 20.08 ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 147.397 142.235 147.031 1.00 16.73 ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 147.376 141.147 145.963 1.00 24.25 ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 146.308 140.615 145.626 1.00 29.48 ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 147.529 143.617 146.397 1.00 21.83 ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 147.265 144.763 147.364 1.00 25.28 ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 147.954 146.051 146.953 1.00 31.21 ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 148.550 146.087 145.857 1.00 27.69 ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 147.901 147.027 147.730 1.00 29.91 ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 148.547 140.786 145.431 1.00 23.56 ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 148.615 139.714 144.445 1.00 23.00 ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 148.175 138.384 145.042 1.00 26.31 ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 147.452 137.617 144.398 1.00 27.07 ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 150.030 139.609 143.880 1.00 26.06 ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 150.452 140.854 143.127 1.00 28.23 ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 149.654 141.813 143.071 1.00 25.38 ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 151.578 140.872 142.590 1.00 29.34 ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 148.604 138.093 146.274 1.00 26.54 ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 148.210 136.846 146.920 1.00 25.83 ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 146.704 136.785 147.129 1.00 27.82 ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 146.081 135.741 146.906 1.00 31.02 ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 148.950 136.691 148.248 1.00 24.64 ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 148.466 135.593 149.195 1.00 24.96 ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 148.625 134.230 148.554 1.00 26.03 ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 149.220 135.659 150.511 1.00 25.69 ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 146.101 137.894 147.559 1.00 27.91 ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 144.653 137.931 147.729 1.00 26.14 ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 143.940 137.759 146.395 1.00 30.35 ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 142.881 137.123 146.326 1.00 31.83 ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 144.235 139.239 148.398 1.00 21.98 ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 144.503 138.324 145.324 1.00 30.47 ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 143.923 138.129 143.999 1.00 31.46 ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 143.989 136.668 143.573 1.00 34.71 ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 143.038 136.144 142.980 1.00 33.88 ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 144.631 139.021 142.981 1.00 28.85 ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 145.107 135.993 143.858 1.00 35.47 ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 145.258 134.598 143.450 1.00 36.42 ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 144.232 133.699 144.131 1.00 36.83 ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 143.646 132.820 143.489 1.00 38.97 ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 146.674 134.105 143.752 1.00 37.49 ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 147.772 134.845 143.010 1.00 38.87 ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 149.147 134.586 143.596 1.00 41.72 ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 149.237 133.837 144.591 1.00 41.88 ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 150.136 135.129 143.062 1.00 39.51 ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 144.004 133.898 145.426 1.00 35.94 ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 143.063 133.080 146.179 1.00 36.58 ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 141.628 133.576 146.074 1.00 36.04 ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 140.735 132.963 146.668 1.00 35.10 ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 143.475 133.016 147.654 1.00 35.78 ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 144.971 132.957 147.874 1.00 35.82 ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 145.507 131.544 147.818 1.00 38.82 ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 145.254 130.734 148.711 1.00 37.96 ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 146.245 131.233 146.760 1.00 37.80 ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 141.391 134.664 145.338 1.00 35.18 ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 140.058 135.250 145.192 1.00 37.42 ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 139.451 135.582 146.553 1.00 38.23 ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 138.259 135.376 146.791 1.00 39.38 ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 139.134 134.330 144.390 1.00 38.54 ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 139.757 133.874 143.086 1.00 41.14 ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 139.946 132.679 142.859 1.00 39.61 ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 140.081 134.826 142.219 1.00 41.09 ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 140.282 136.096 147.454 1.00 31.39 ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 139.861 136.488 148.791 1.00 28.69 ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 139.788 138.006 148.863 1.00 28.26 ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 140.754 138.693 148.514 1.00 32.40 ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 140.826 135.958 149.855 1.00 29.70 ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 141.139 134.588 149.580 1.00 33.53 ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 140.203 136.061 151.237 1.00 28.05 ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 138.648 138.524 149.309 1.00 26.85 ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 138.492 139.964 149.452 1.00 25.42 ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 139.386 140.473 150.574 1.00 22.83 ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 139.418 139.899 151.666 1.00 24.29 ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 137.032 140.314 149.733 1.00 24.20 ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 136.184 140.484 148.485 1.00 27.17 ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 135.840 139.161 147.829 1.00 31.43 ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 136.145 138.936 146.658 1.00 29.75 ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 135.202 138.275 148.586 1.00 30.43 ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 140.118 141.548 150.303 1.00 15.25 ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 141.061 142.118 151.255 1.00 14.19 ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 140.750 143.598 151.424 1.00 17.04 ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 140.526 144.309 150.439 1.00 21.35 ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 142.523 141.911 150.811 1.00 14.18 ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 143.484 142.586 151.790 1.00 13.22 ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 142.742 142.420 149.395 1.00 16.21 ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 144.931 142.278 151.528 1.00 13.31 ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 140.712 144.051 152.673 1.00 10.67 ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 140.536 145.461 152.996 1.00 8.59  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 141.902 146.055 153.308 1.00 8.82  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 142.540 145.669 154.294 1.00 16.64 ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 139.586 145.639 154.179 1.00 13.01 ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 138.276 145.191 153.813 1.00 16.83 ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 139.517 147.102 154.586 1.00 9.03  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 142.351 146.985 152.472 1.00 5.61  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 143.666 147.596 152.604 1.00 4.23  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 143.517 149.003 153.161 1.00 10.47 ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 142.758 149.813 152.617 1.00 15.19 ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 144.386 147.633 151.255 1.00 6.38  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 144.396 146.354 150.649 1.00 14.87 ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 144.238 149.288 154.241 1.00 4.76  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 144.165 150.574 154.923 1.00 3.35  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 145.582 151.079 155.151 1.00 7.75  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 146.448 150.323 155.603 1.00 15.75 ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 143.404 150.469 156.258 1.00 3.79  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 141.939 150.114 156.004 1.00 8.57  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 143.502 151.767 157.039 1.00 7.90  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 141.336 149.241 157.067 1.00 9.14  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 145.816 152.349 154.837 1.00 5.06  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 147.105 152.980 155.077 1.00 1.32  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 147.057 153.713 156.412 1.00 5.69  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 146.206 154.584 156.620 1.00 9.17  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 147.459 153.937 153.942 1.00 1.97  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 147.968 153.360 157.307 1.00 6.93  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 147.994 153.912 158.656 1.00 7.62  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 148.577 155.318 158.623 1.00 7.57  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 149.442 155.637 157.801 1.00 6.74  ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 148.792 152.974 159.586 1.00 4.33  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 148.078 151.628 159.707 1.00 6.35  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 148.998 153.587 160.962 1.00 6.60  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 146.609 151.746 160.042 1.00 3.59  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 148.097 156.173 159.526 1.00 9.26  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 148.626 157.516 159.639 1.00 8.12  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 147.627 158.576 160.051 1.00 11.52 ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 148.021 159.655 160.501 1.00 14.93 ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 146.336 158.290 159.916 1.00 14.60 ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 145.293 159.249 160.241 1.00 15.16 ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 144.312 158.644 161.239 1.00 20.50 ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 144.185 157.422 161.352 1.00 25.94 ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 144.553 159.709 158.979 1.00 12.37 ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 144.148 158.604 158.191 1.00 17.09 ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 143.629 159.522 161.979 1.00 15.33 ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 142.667 159.063 162.979 1.00 18.23 ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 141.514 158.306 162.333 1.00 18.57 ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 141.112 157.237 162.812 1.00 24.16 ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 142.143 160.248 163.788 1.00 20.37 ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 140.965 158.847 161.246 1.00 13.49 ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 139.999 158.099 160.450 1.00 18.93 ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 140.609 156.827 159.879 1.00 20.38 ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 139.903 155.830 159.696 1.00 23.51 ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 139.429 159.003 159.357 1.00 21.12 ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 140.431 159.386 158.297 1.00 24.74 ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 141.246 160.596 158.734 1.00 27.31 ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 141.224 160.918 159.938 1.00 28.05 ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 141.917 161.218 157.894 1.00 24.61 ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 141.918 156.824 159.622 1.00 18.20 ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 142.579 155.581 159.260 1.00 14.94 ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 142.519 154.551 160.372 1.00 15.30 ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 142.274 153.368 160.123 1.00 17.92 ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 142.730 154.988 161.617 1.00 17.71 ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 142.620 154.081 162.754 1.00 15.11 ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 141.193 153.575 162.922 1.00 13.94 ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 140.976 152.397 163.232 1.00 20.71 ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 143.089 154.780 164.028 1.00 16.42 ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 144.527 155.202 163.991 1.00 16.06 ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 145.513 154.314 163.605 1.00 15.00 ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 144.894 156.490 164.346 1.00 15.77 ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 146.837 154.702 163.570 1.00 16.33 ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 146.215 156.883 164.312 1.00 14.64 ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 147.189 155.987 163.925 1.00 15.16 ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 140.207 154.454 162.737 1.00 13.23 ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 138.812 154.032 162.823 1.00 16.44 ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 138.484 152.992 161.758 1.00 16.88 ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 137.831 151.981 162.045 1.00 18.23 ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 137.887 155.239 162.688 1.00 18.77 ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 137.934 156.147 163.897 1.00 22.48 ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 138.239 155.710 165.006 1.00 24.24 ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 137.633 157.423 163.690 1.00 18.54 ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 138.935 153.226 160.523 1.00 17.54 ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 138.711 152.256 159.457 1.00 14.53 ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 139.410 150.938 159.757 1.00 14.42 ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 138.859 149.866 159.490 1.00 18.62 ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 139.187 152.821 158.121 1.00 15.81 ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 138.374 153.996 157.617 1.00 20.36 ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 138.968 154.618 156.370 1.00 25.53 ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 140.091 154.298 155.979 1.00 20.23 ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 138.218 155.513 155.739 1.00 22.58 ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 140.625 150.996 160.305 1.00 13.97 ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 141.341 149.773 160.653 1.00 10.93 ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 140.585 148.978 161.707 1.00 13.23 ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 140.430 147.755 161.588 1.00 18.03 ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 142.750 150.110 161.139 1.00 11.54 ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 140.098 149.658 162.746 1.00 13.92 ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 139.356 148.975 163.801 1.00 10.86 ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 138.076 148.354 163.257 1.00 14.70 ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 137.758 147.196 163.554 1.00 18.52 ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 139.042 149.950 164.936 1.00 14.75 ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 140.285 150.401 165.675 1.00 23.40 ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 141.401 150.079 165.218 1.00 22.39 ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 140.146 151.080 166.716 1.00 25.49 ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 137.331 149.112 162.446 1.00 14.11 ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 136.093 148.586 161.882 1.00 10.44 ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 136.360 147.396 160.969 1.00 12.71 ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 135.637 146.394 161.014 1.00 17.01 ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 135.350 149.685 161.125 1.00 14.61 ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 134.820 150.803 162.004 1.00 18.26 ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 134.224 151.924 161.165 1.00 17.67 ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 134.316 153.262 161.882 1.00 18.32 ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 133.814 153.180 163.279 1.00 18.31 ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 137.397 147.486 160.132 1.00 12.63 ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 137.715 146.398 159.219 1.00 11.88 ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 138.137 145.147 159.975 1.00 14.10 ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 137.742 144.036 159.612 1.00 18.19 ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 138.807 146.831 158.245 1.00 11.61 ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 138.944 145.305 161.027 1.00 9.71  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 139.349 144.149 161.822 1.00 11.82 ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 138.138 143.516 162.494 1.00 14.78 ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 137.978 142.288 162.492 1.00 16.86 ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 140.423 144.554 162.847 1.00 11.62 ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 141.739 144.876 162.137 1.00 10.59 ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 140.630 143.452 163.870 1.00 13.84 ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 142.722 145.639 162.992 1.00 8.65  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 137.261 144.342 163.074 1.00 15.41 ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 136.081 143.813 163.751 1.00 11.99 ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 135.165 143.085 162.777 1.00 12.98 ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 134.556 142.068 163.129 1.00 16.26 ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 135.329 144.944 164.452 1.00 11.79 ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 136.029 145.414 165.708 1.00 13.34 ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 136.898 144.727 166.241 1.00 14.77 ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 135.653 146.593 166.188 1.00 14.03 ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 135.038 143.598 161.552 1.00 14.26 ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 134.206 142.928 160.559 1.00 13.96 ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 134.850 141.636 160.072 1.00 18.57 ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 134.164 140.621 159.899 1.00 19.89 ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 133.939 143.866 159.382 1.00 12.55 ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 133.395 145.100 159.867 1.00 17.84 ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 132.960 143.233 158.408 1.00 13.54 ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 136.167 141.649 159.855 1.00 18.35 ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 136.840 140.508 159.250 1.00 14.49 ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 137.025 139.350 160.222 1.00 14.53 ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 137.039 138.193 159.790 1.00 15.88 ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 138.194 140.938 158.687 1.00 12.17 ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 137.175 139.626 161.521 1.00 11.79 ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 137.313 138.528 162.472 1.00 12.14 ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 136.046 137.688 162.534 1.00 18.76 ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 136.084 136.546 163.001 1.00 22.18 ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 137.694 139.048 163.873 1.00 12.51 ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 139.065 139.694 163.841 1.00 16.48 ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 136.647 140.014 164.393 1.00 17.30 ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 134.920 138.227 162.071 1.00 19.00 ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 133.674 137.481 161.968 1.00 17.12 ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 133.409 136.965 160.561 1.00 16.98 ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 132.961 135.826 160.400 1.00 20.26 ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 132.498 138.353 162.419 1.00 15.92 ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 132.672 138.959 163.801 1.00 17.36 ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 131.341 139.399 164.381 1.00 19.73 ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 131.123 140.890 164.185 1.00 20.37 ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 131.945 141.698 165.125 1.00 20.66 ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 133.677 137.776 159.537 1.00 13.85 ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 133.437 137.359 158.161 1.00 16.17 ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 134.544 136.474 157.604 1.00 19.18 ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 134.306 135.751 156.631 1.00 18.99 ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 133.264 138.585 157.262 1.00 18.29 ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 134.474 139.313 157.155 1.00 19.68 ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 135.738 136.510 158.189 1.00 18.53 ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 136.843 135.715 157.698 1.00 17.16 ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 137.612 136.315 156.544 1.00 17.06 ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 138.356 135.590 155.876 1.00 18.34 ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 137.458 137.610 156.284 1.00 14.58 ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 138.170 138.258 155.197 1.00 15.06 ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 139.561 138.698 155.650 1.00 17.60 ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 139.901 138.669 156.836 1.00 20.35 ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 137.378 139.455 154.677 1.00 16.61 ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 136.108 139.085 153.930 1.00 18.98 ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 135.131 140.249 153.890 1.00 21.98 ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 135.357 141.120 152.742 1.00 24.08 ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 136.106 142.213 152.767 1.00 21.95 ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 136.723 142.604 153.870 1.00 17.79 ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 136.238 142.935 151.657 1.00 17.34 ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 140.373 139.109 154.681 1.00 17.16 ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 141.733 139.556 154.941 1.00 15.42 ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 141.766 141.064 155.145 1.00 17.33 ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 141.039 141.808 154.484 1.00 20.01 ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 142.658 139.172 153.785 1.00 17.63 ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 142.986 137.717 153.729 1.00 16.78 ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 142.454 136.726 154.497 1.00 16.63 ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 143.928 137.086 152.855 1.00 17.04 ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 143.004 135.516 154.155 1.00 16.61 ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 143.913 135.711 153.148 1.00 16.97 ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 144.781 137.552 151.851 1.00 18.75 ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 144.718 134.796 152.476 1.00 20.00 ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 145.579 136.644 151.185 1.00 18.55 ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 145.542 135.282 151.501 1.00 19.16 ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 142.615 141.512 156.065 1.00 13.02 ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 142.817 142.934 156.318 1.00 9.10  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 144.310 143.211 156.282 1.00 10.68 ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 145.080 142.556 156.993 1.00 18.48 ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 142.217 143.375 157.664 1.00 8.83  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 142.627 144.800 157.982 1.00 9.19  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 140.710 143.259 157.631 1.00 14.76 ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 144.719 144.177 155.466 1.00 4.89  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 146.107 144.610 155.401 1.00 3.01  ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 146.201 146.063 155.842 1.00 4.55  ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 145.402 146.901 155.414 1.00 11.48 ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 146.681 144.447 153.993 1.00 9.05  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 148.135 144.883 153.883 1.00 10.74 ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 148.795 144.842 152.208 1.00 19.78 ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 147.473 145.622 151.294 1.00 13.92 ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 147.164 146.346 156.713 1.00 4.85  ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 147.431 147.689 157.206 1.00 4.18  ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 148.868 148.044 156.854 1.00 5.05  ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 149.798 147.316 157.219 1.00 12.67 ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 147.191 147.779 158.713 1.00 7.66  ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 145.887 147.131 159.187 1.00 5.80  ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 145.795 147.117 160.697 1.00 7.97  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 144.688 147.845 158.590 1.00 8.43  ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 149.044 149.155 156.150 1.00 1.36  ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 150.335 149.530 155.597 1.00 1.73  ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 150.989 150.628 156.425 1.00 2.83  ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 150.316 151.487 156.997 1.00 9.70  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 150.192 149.991 154.147 1.00 5.58  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 149.235 149.156 153.321 1.00 2.02  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 148.881 149.855 152.026 1.00 5.85  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 147.587 149.320 151.450 1.00 12.44 ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 147.190 150.033 150.208 1.00 12.21 ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 152.322 150.585 156.470 1.00 4.56  ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 153.130 151.580 157.176 1.00 3.82  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 152.717 151.700 158.639 1.00 7.12  ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 152.602 152.799 159.183 1.00 13.93 ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 153.065 152.938 156.476 1.00 4.07  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 153.273 152.831 154.981 1.00 5.44  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 154.287 152.312 154.520 1.00 8.67  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 152.309 153.321 154.213 1.00 2.56  ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 152.492 150.554 159.285 1.00 5.15  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 152.097 150.543 160.688 1.00 6.29  ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 153.212 150.991 161.616 1.00 8.80  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 152.955 151.249 162.797 1.00 13.35 ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 151.608 149.142 161.107 1.00 4.20  ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 150.373 148.755 160.318 1.00 2.78  ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 152.710 148.117 160.917 1.00 4.93  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 154.444 151.099 161.116 1.00 5.76  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 155.554 151.568 161.933 1.00 2.65  ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 155.434 153.040 162.299 1.00 5.94  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 156.205 153.516 163.139 1.00 13.38 ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 156.881 151.320 161.213 1.00 2.58  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 157.034 152.093 159.940 1.00 8.38  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 156.456 151.697 158.754 1.00 9.66  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 157.704 153.237 159.667 1.00 8.84  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 156.761 152.563 157.806 1.00 3.93  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 157.517 153.507 158.333 1.00 4.04  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 154.500 153.768 161.688 1.00 5.71  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 154.298 155.178 161.993 1.00 7.99  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 153.429 155.403 163.223 1.00 14.17 ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 153.322 156.546 163.680 1.00 15.91 ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 153.673 155.885 160.788 1.00 0.78  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 154.487 155.837 159.495 1.00 2.11  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 153.616 156.173 158.299 1.00 4.83  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 155.678 156.777 159.574 1.00 3.79  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 152.807 154.357 163.764 1.00 11.37 ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 151.944 154.459 164.940 1.00 9.30  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 152.317 153.364 165.930 1.00 13.31 ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 151.643 152.330 166.013 1.00 19.02 ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 150.468 154.367 164.551 1.00 11.66 ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 153.396 153.556 166.697 1.00 13.80 ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 153.794 152.505 167.652 1.00 14.21 ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 152.819 152.319 168.803 1.00 14.95 ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 152.574 151.180 169.218 1.00 19.04 ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 155.172 152.978 168.139 1.00 11.79 ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 155.206 154.440 167.851 1.00 14.29 ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 154.377 154.649 166.626 1.00 12.09 ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 152.260 153.404 169.344 1.00 11.20 ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 151.290 153.258 170.421 1.00 16.32 ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 150.027 152.548 169.973 1.00 18.14 ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 149.515 151.660 170.664 1.00 19.47 ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 149.508 152.929 168.803 1.00 14.46 ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 148.383 152.197 168.243 1.00 13.26 ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 148.769 150.759 167.930 1.00 16.27 ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 147.919 149.869 167.972 1.00 21.70 ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 147.860 152.896 166.989 1.00 11.74 ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 146.808 152.103 166.286 1.00 12.73 ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 145.478 152.062 166.581 1.00 15.58 ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 147.000 151.216 165.181 1.00 13.86 ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 144.828 151.212 165.722 1.00 14.33 ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 145.740 150.679 164.853 1.00 14.38 ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 148.115 150.826 164.432 1.00 14.36 ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 145.565 149.776 163.811 1.00 16.18 ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 147.937 149.928 163.401 1.00 14.38 ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 146.674 149.414 163.099 1.00 16.14 ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 150.046 150.509 167.630 1.00 11.13 ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 150.497 149.136 167.427 1.00 13.78 ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 150.423 148.330 168.720 1.00 17.45 ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 150.027 147.160 168.705 1.00 17.67 ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 151.917 149.125 166.865 1.00 11.25 ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 152.035 149.117 165.342 1.00 10.01 ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 153.467 148.836 164.921 1.00 12.18 ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 151.083 148.098 164.736 1.00 11.05 ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 150.805 148.938 169.847 1.00 15.45 ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 150.654 148.262 171.133 1.00 17.20 ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 149.186 147.984 171.436 1.00 18.64 ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 148.829 146.884 171.885 1.00 21.78 ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 151.275 149.102 172.249 1.00 15.76 ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 152.705 149.530 171.987 1.00 19.58 ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 153.329 150.678 173.231 1.00 35.86 ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 154.808 151.279 172.421 1.00 18.89 ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 148.323 148.972 171.191 1.00 17.01 ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 146.891 148.761 171.396 1.00 17.24 ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 146.368 147.640 170.506 1.00 16.22 ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 145.551 146.820 170.939 1.00 17.57 ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 146.121 150.054 171.131 1.00 18.36 ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 146.597 151.248 171.936 1.00 21.52 ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 145.967 152.546 171.471 1.00 25.89 ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 144.937 152.542 170.798 1.00 27.35 ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 146.582 153.667 171.830 1.00 21.87 ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 146.829 147.592 169.255 1.00 15.35 ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 146.393 146.559 168.325 1.00 16.13 ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 146.863 145.178 168.765 1.00 18.73 ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 146.123 144.200 168.639 1.00 20.60 ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 146.903 146.879 166.920 1.00 12.78 ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 146.837 145.760 165.882 1.00 13.36 ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 145.397 145.476 165.497 1.00 13.41 ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 147.660 146.126 164.662 1.00 16.88 ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 148.092 145.077 169.271 1.00 17.73 ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 148.571 143.797 169.783 1.00 13.71 ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 147.734 143.335 170.969 1.00 17.15 ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 147.357 142.159 171.059 1.00 19.47 ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 150.044 143.902 170.174 1.00 11.56 ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 150.700 142.572 170.502 1.00 14.97 ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 150.592 142.212 171.970 1.00 20.66 ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 150.890 143.078 172.818 1.00 22.64 ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 150.212 141.063 172.276 1.00 18.56 ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 147.424 144.255 171.888 1.00 19.43 ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 146.589 143.900 173.031 1.00 15.49 ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 145.202 143.457 172.580 1.00 16.58 ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 144.639 142.502 173.127 1.00 19.81 ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 146.495 145.077 173.998 1.00 15.92 ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 147.721 145.247 174.877 1.00 17.57 ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 147.863 146.680 175.359 1.00 21.37 ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 149.024 146.825 176.326 1.00 20.98 ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 150.274 146.224 175.787 1.00 20.63 ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 144.635 144.144 171.586 1.00 16.94 ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 143.344 143.740 171.037 1.00 16.34 ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 143.420 142.363 170.390 1.00 15.61 ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 142.501 141.549 170.532 1.00 19.89 ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 142.867 144.776 170.020 1.00 17.77 ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 141.515 144.471 169.404 1.00 18.73 ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 141.085 145.579 168.459 1.00 20.60 ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 139.729 145.289 167.847 1.00 19.59 ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 139.294 146.386 166.940 1.00 20.31 ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 144.508 142.090 169.669 1.00 18.05 ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 144.637 140.826 168.953 1.00 19.55 ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 144.790 139.655 169.911 1.00 21.08 ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 144.290 138.558 169.638 1.00 18.57 ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 145.825 140.890 167.996 1.00 17.33 ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 145.611 141.601 166.662 1.00 18.66 ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 146.951 141.937 166.032 1.00 18.09 ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 144.774 140.744 165.728 1.00 17.15 ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 145.485 139.861 171.034 1.00 21.89 ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 145.712 138.754 171.958 1.00 18.58 ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 144.399 138.195 172.495 1.00 22.04 ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 144.214 136.973 172.551 1.00 22.46 ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 146.608 139.198 173.112 1.00 18.00 ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 146.826 138.136 174.143 1.00 21.66 ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 147.685 137.075 173.951 1.00 20.83 ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 146.285 137.962 175.372 1.00 19.63 ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 147.670 136.299 175.020 1.00 16.30 ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 146.828 136.813 175.897 1.00 17.71 ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 143.477 139.068 172.890 1.00 22.72 ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 142.183 138.640 173.417 1.00 23.66 ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 141.146 138.653 172.295 1.00 25.53 ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 140.258 139.504 172.226 1.00 26.74 ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 141.764 139.534 174.580 1.00 23.48 ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 141.709 140.892 174.182 1.00 25.07 ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 141.279 137.675 171.404 1.00 28.41 ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 140.442 137.624 170.215 1.00 28.45 ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 140.403 136.196 169.688 1.00 30.49 ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 141.409 135.482 169.743 1.00 31.23 ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 140.971 138.582 169.143 1.00 26.31 ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 140.106 138.854 167.916 1.00 28.95 ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 138.822 139.555 168.322 1.00 27.93 ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 140.888 139.694 166.925 1.00 28.12 ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 139.242 135.792 169.177 1.00 34.38 ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 139.040 134.472 168.581 1.00 33.64 ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 138.438 134.671 167.197 1.00 34.11 ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 137.222 134.520 167.007 1.00 32.34 ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 138.149 133.592 169.455 1.00 33.45 ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 138.852 133.004 170.666 1.00 35.99 ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 138.515 131.541 170.879 1.00 38.52 ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 137.370 131.124 170.711 1.00 37.36 ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 139.518 130.753 171.249 1.00 35.36 ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 139.256 135.008 166.210 1.00 30.88 ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 138.740 135.361 164.886 1.00 26.47 ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 138.325 134.123 164.095 1.00 23.04 ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 138.507 132.985 164.521 1.00 25.90 ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 139.926 136.070 164.233 1.00 24.95 ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 141.118 135.457 164.871 1.00 26.84 ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 140.724 135.091 166.275 1.00 26.71 ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 137.755 134.377 162.920 1.00 19.24 ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 137.336 133.318 162.018 1.00 17.56 ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 138.551 132.545 161.511 1.00 23.49 ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 139.680 133.039 161.512 1.00 30.01 ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 136.543 133.907 160.850 1.00 18.56 ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 135.920 132.881 159.955 1.00 22.79 ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 136.549 132.395 158.828 1.00 22.08 ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 134.720 132.259 160.012 1.00 25.48 ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 135.766 131.515 158.234 1.00 21.68 ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 134.649 131.412 158.933 1.00 27.42 ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 138.303 131.304 161.081 1.00 19.65 ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 139.395 130.431 160.661 1.00 19.51 ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 140.160 130.999 159.473 1.00 20.59 ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 141.375 130.799 159.366 1.00 18.22 ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 138.854 129.042 160.325 1.00 18.94 ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 139.477 131.704 158.574 1.00 17.42 ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 140.102 132.238 157.372 1.00 17.92 ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 140.572 133.679 157.529 1.00 19.05 ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 141.076 134.255 156.560 1.00 19.79 ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 139.135 132.142 156.190 1.00 20.27 ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 138.728 130.453 155.696 1.00 31.85 ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 140.424 134.271 158.709 1.00 15.13 ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 140.851 135.648 158.912 1.00 13.36 ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 142.369 135.753 158.879 1.00 19.92 ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 143.079 134.922 159.451 1.00 23.46 ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 140.322 136.179 160.243 1.00 14.10 ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 140.924 137.494 160.656 1.00 17.01 ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 140.581 138.662 160.000 1.00 15.30 ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 141.828 137.562 161.701 1.00 18.76 ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 141.131 139.871 160.379 1.00 12.67 ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 142.379 138.768 162.081 1.00 15.34 ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 142.029 139.923 161.420 1.00 11.15 ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 142.867 136.780 158.196 1.00 18.56 ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 144.288 137.087 158.173 1.00 13.60 ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 144.471 138.589 158.311 1.00 11.31 ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 143.712 139.371 157.732 1.00 18.63 ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 144.958 136.595 156.885 1.00 15.83 ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 145.071 135.086 156.773 1.00 15.48 ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 145.937 134.503 157.875 1.00 14.53 ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 146.020 133.051 157.780 1.00 19.04 ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 145.072 132.216 158.182 1.00 18.53 ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 143.954 132.655 158.737 1.00 16.05 ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 145.249 130.908 158.025 1.00 20.03 ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 145.475 138.983 159.089 1.00 9.03  ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 145.813 140.388 159.290 1.00 10.42 ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 147.276 140.581 158.922 1.00 8.78  ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 148.168 140.120 159.639 1.00 15.45 ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 145.551 140.822 160.730 1.00 13.44 ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 146.026 142.233 161.074 1.00 6.53  ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 145.183 143.268 160.354 1.00 12.00 ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 145.989 142.462 162.568 1.00 9.41  ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 147.516 141.261 157.807 1.00 6.14  ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 148.858 141.587 157.353 1.00 4.78  ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 149.198 143.001 157.802 1.00 4.35  ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 148.378 143.911 157.662 1.00 10.31 ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 148.968 141.477 155.831 1.00 8.29  ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 148.528 140.150 155.284 1.00 7.29  ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 147.187 139.882 155.070 1.00 7.07  ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 149.456 139.172 154.977 1.00 6.90  ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 146.783 138.666 154.567 1.00 7.28  ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 149.055 137.954 154.474 1.00 8.83  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 147.718 137.701 154.269 1.00 9.78  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 150.390 143.174 158.358 1.00 2.25  ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 150.878 144.480 158.792 1.00 2.20  ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 152.187 144.730 158.059 1.00 7.01  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 153.217 144.146 158.406 1.00 13.00 ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 151.066 144.527 160.304 1.00 4.62  ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 149.857 144.144 161.155 1.00 5.59  ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 150.165 144.313 162.628 1.00 5.01  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 148.659 144.977 160.765 1.00 11.63 ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 152.153 145.585 157.041 1.00 8.21  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 153.338 145.859 156.239 1.00 9.69  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 154.025 147.104 156.782 1.00 1.85  ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 153.398 148.160 156.912 1.00 6.25  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 152.982 146.037 154.765 1.00 10.37 ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 152.105 147.156 154.613 1.00 11.41 ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 152.294 144.794 154.230 1.00 10.23 ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 155.309 146.978 157.102 1.00 3.54  ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 156.057 148.077 157.691 1.00 5.57  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 157.502 147.997 157.228 1.00 5.53  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 157.938 147.007 156.638 1.00 8.27  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 155.990 148.043 159.221 1.00 9.00  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 156.851 146.956 159.842 1.00 10.34 ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 156.248 146.405 161.444 1.00 24.06 ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 155.071 145.160 160.937 1.00 6.79  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 158.241 149.064 157.496 1.00 3.76  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 159.681 149.047 157.313 1.00 3.97  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 160.357 148.633 158.616 1.00 7.55  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 159.786 148.745 159.702 1.00 14.05 ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 160.189 150.414 156.852 1.00 5.37  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 160.459 151.396 157.975 1.00 9.72  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 161.125 152.664 157.486 1.00 15.95 ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 161.167 152.877 156.257 1.00 14.84 ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 161.610 153.447 158.330 1.00 14.88 ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 161.585 148.136 158.494 1.00 7.77  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 162.326 147.690 159.669 1.00 5.39  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 162.684 148.926 160.489 1.00 9.88  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 163.567 149.701 160.112 1.00 15.02 ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 163.572 146.891 159.279 1.00 6.19  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 163.169 145.620 158.527 1.00 4.81  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 164.383 146.537 160.513 1.00 7.30  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 164.337 144.760 158.111 1.00 5.34  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 161.993 149.111 161.616 1.00 7.62  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 162.095 150.314 162.420 1.00 7.07  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 162.175 149.898 163.884 1.00 10.41 ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 161.351 149.083 164.337 1.00 13.02 ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 160.885 151.223 162.178 1.00 11.09 ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 161.178 152.684 162.454 1.00 17.14 ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 162.302 153.056 162.783 1.00 21.49 ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 160.161 153.523 162.317 1.00 12.98 ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 163.141 150.416 164.646 1.00 11.24 ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 163.206 150.073 166.076 1.00 7.57  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 161.995 150.528 166.871 1.00 12.55 ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 161.757 149.995 167.961 1.00 16.00 ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 164.484 150.779 166.553 1.00 6.42  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 164.790 151.792 165.497 1.00 11.53 ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 164.313 151.195 164.217 1.00 10.57 ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 161.223 151.492 166.367 1.00 16.40 ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 160.038 151.959 167.075 1.00 15.21 ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 158.919 150.928 167.109 1.00 15.00 ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 157.982 151.087 167.898 1.00 20.25 ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 159.519 153.251 166.442 1.00 12.81 ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 160.460 154.438 166.578 1.00 14.50 ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 160.117 155.554 165.597 1.00 22.02 ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 158.679 155.465 165.101 1.00 23.51 ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 158.431 156.350 163.929 1.00 17.23 ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 158.986 149.893 166.280 1.00 11.17 ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 157.949 148.856 166.292 1.00 12.00 ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 157.984 148.132 167.634 1.00 10.39 ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 159.063 147.698 168.073 1.00 14.78 ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 158.158 147.880 165.133 1.00 12.70 ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 157.161 146.736 165.212 1.00 9.70  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 158.034 148.606 163.805 1.00 11.27 ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 156.853 147.990 168.325 1.00 8.70  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 156.870 147.383 169.659 1.00 8.60  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 157.349 145.940 169.624 1.00 10.05 ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 157.102 145.200 168.670 1.00 15.45 ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 155.408 147.476 170.111 1.00 12.34 ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 154.803 148.533 169.254 1.00 14.24 ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 155.508 148.453 167.944 1.00 13.73 ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 158.048 145.548 170.691 1.00 7.19  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 158.595 144.197 170.778 1.00 5.23  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 157.479 143.172 170.945 1.00 4.53  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 157.541 142.069 170.388 1.00 8.22  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 159.622 144.121 171.923 1.00 7.62  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 159.823 142.685 172.381 1.00 10.86 ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 160.942 144.734 171.485 1.00 7.68  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 156.440 143.514 171.713 1.00 5.18  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 155.357 142.565 171.949 1.00 7.85  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 154.612 142.241 170.660 1.00 8.00  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 154.174 141.103 170.458 1.00 9.13  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 154.401 143.107 173.013 1.00 8.81  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 153.870 144.484 172.677 1.00 14.82 ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 154.153 145.029 171.611 1.00 16.68 ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 153.091 145.056 173.586 1.00 14.25 ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 154.455 143.230 169.776 1.00 5.59  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 153.855 142.960 168.475 1.00 6.00  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 154.731 142.026 167.650 1.00 5.62  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 154.226 141.122 166.976 1.00 9.94  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 153.612 144.265 167.718 1.00 8.51  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 152.937 144.083 166.358 1.00 7.11  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 151.431 143.942 166.517 1.00 6.47  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 153.281 145.222 165.418 1.00 8.16  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 156.050 142.232 167.689 1.00 3.54  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 156.961 141.358 166.958 1.00 3.19  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 156.885 139.928 167.476 1.00 4.42  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 156.940 138.972 166.695 1.00 5.54  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 158.390 141.888 167.056 1.00 0.93  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 158.699 143.186 166.305 1.00 1.02  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 160.093 143.674 166.650 1.00 5.56  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 158.555 142.991 164.807 1.00 2.89  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 156.764 139.763 168.794 1.00 5.38  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 156.642 138.426 169.362 1.00 3.17  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 155.277 137.813 169.083 1.00 4.98  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 155.153 136.587 169.009 1.00 6.86  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 156.903 138.467 170.867 1.00 4.31  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 158.312 138.886 171.241 1.00 3.77  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 158.501 138.880 172.745 1.00 6.19  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 157.786 137.777 173.375 1.00 11.32 ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 158.370 136.747 173.972 1.00 13.23 ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 159.687 136.645 174.041 1.00 11.31 ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 157.614 135.795 174.509 1.00 8.85  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 154.243 138.644 168.930 1.00 5.80  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 152.898 138.119 168.719 1.00 3.73  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 152.711 137.605 167.297 1.00 3.14  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 151.993 136.624 167.078 1.00 5.77  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 151.860 139.194 169.039 1.00 5.16  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 153.342 138.253 166.320 1.00 1.47  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 153.176 137.898 164.929 1.00 3.94  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 154.352 137.110 164.368 1.00 5.90  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 155.362 136.877 165.025 1.00 13.60 ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 154.193 136.696 163.115 1.00 3.93  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 155.247 136.024 162.370 1.00 5.03  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 155.874 137.009 161.393 1.00 3.45  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 155.170 137.615 160.581 1.00 8.42  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 154.714 134.805 161.618 1.00 3.73  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 155.761 134.169 160.722 1.00 8.22  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 155.612 132.665 160.632 1.00 10.71 ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 156.541 132.104 159.660 1.00 13.26 ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 156.401 130.917 159.086 1.00 15.68 ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 155.378 130.131 159.372 1.00 13.97 ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 157.309 130.514 158.202 1.00 13.02 ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 157.193 137.152 161.470 1.00 0.12  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 157.925 138.189 160.756 1.00 1.62  ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 158.447 137.625 159.444 1.00 4.06  ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 159.024 136.532 159.412 1.00 9.65  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 159.078 138.738 161.614 1.00 2.96  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 158.536 139.298 162.928 1.00 4.84  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 159.849 139.802 160.856 1.00 2.27  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 159.576 139.429 164.006 1.00 4.12  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 158.223 138.364 158.359 1.00 4.61  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 158.796 138.069 157.053 1.00 0.43  ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 159.579 139.288 156.595 1.00 1.99  ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 159.019 140.385 156.500 1.00 8.48  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 157.712 137.715 156.035 1.00 4.24  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 156.933 136.489 156.386 1.00 5.55  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 157.420 135.234 156.074 1.00 8.57  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 155.716 136.591 157.032 1.00 6.22  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 156.704 134.104 156.397 1.00 12.32 ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 154.999 135.463 157.360 1.00 8.02  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 155.493 134.219 157.043 1.00 11.71 ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 160.861 139.097 156.308 1.00 1.68  ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 161.752 140.185 155.925 1.00 1.46  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 161.853 140.224 154.409 1.00 6.88  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 162.185 139.216 153.771 1.00 10.70 ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 163.140 140.026 156.569 1.00 1.33  ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 164.146 140.933 155.885 1.00 5.53  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 163.068 140.335 158.049 1.00 0.77  ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 161.562 141.385 153.833 1.00 6.15  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 161.654 141.611 152.398 1.00 4.76  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 162.844 142.519 152.125 1.00 5.33  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 162.949 143.605 152.703 1.00 8.97  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 160.363 142.214 151.854 1.00 6.31  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 159.204 141.264 151.877 1.00 3.33  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 158.384 141.182 152.984 1.00 3.38  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 158.942 140.445 150.793 1.00 6.65  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 157.325 140.305 153.009 1.00 3.69  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 157.880 139.566 150.813 1.00 8.77  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 157.071 139.497 151.921 1.00 7.69  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 163.732 142.067 151.251 1.00 2.95  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 165.004 142.730 151.009 1.00 8.05  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 165.486 142.316 149.628 1.00 12.37 ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 164.913 141.408 149.012 1.00 11.38 ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 166.031 142.366 152.096 1.00 6.49  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 166.186 140.875 152.315 1.00 9.23  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 167.337 140.539 153.234 1.00 15.20 ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 168.221 141.401 153.418 1.00 15.77 ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 167.358 139.414 153.771 1.00 18.45 ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 166.513 142.977 149.094 1.00 12.14 ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 167.036 142.588 147.781 1.00 7.90  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 167.455 141.130 147.769 1.00 12.49 ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 168.038 140.632 148.743 1.00 17.29 ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 168.242 143.517 147.592 1.00 11.38 ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 167.898 144.721 148.375 1.00 13.41 ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 167.106 144.246 149.560 1.00 12.25 ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 167.160 140.412 146.687 1.00 8.93  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 167.534 139.003 146.623 1.00 8.27  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 169.039 138.844 146.706 1.00 8.10  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 169.800 139.738 146.295 1.00 11.03 ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 166.990 138.552 145.258 1.00 8.39  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 166.578 139.792 144.545 1.00 10.49 ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 166.288 140.814 145.575 1.00 7.02  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 169.513 137.720 147.249 1.00 5.81  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 170.957 137.578 147.505 1.00 7.80  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 171.830 137.695 146.269 1.00 10.39 ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 172.955 138.201 146.371 1.00 15.25 ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 171.063 136.181 148.135 1.00 8.13  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 169.791 135.484 147.778 1.00 8.75  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 168.749 136.548 147.704 1.00 5.60  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 171.363 137.251 145.106 1.00 3.69  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 172.217 137.263 143.935 1.00 4.85  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 171.498 137.415 142.611 1.00 9.09  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 170.289 137.645 142.572 1.00 14.36 ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 172.252 137.293 141.515 1.00 8.90  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 171.668 137.429 140.182 1.00 7.58  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 170.650 136.324 139.932 1.00 9.61  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 169.547 136.573 139.435 1.00 15.81 ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 172.773 137.429 139.110 1.00 4.37  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 172.182 137.186 137.733 1.00 5.56  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 173.538 138.737 139.137 1.00 4.58  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 171.008 135.085 140.275 1.00 6.93  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 170.103 133.961 140.048 1.00 4.51  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 168.825 134.115 140.862 1.00 4.93  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 167.720 133.903 140.350 1.00 8.31  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 170.811 132.650 140.390 1.00 7.33  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 169.902 131.439 140.419 1.00 9.71  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 170.653 130.202 140.875 1.00 9.42  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 169.727 129.008 140.997 1.00 10.67 ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 170.475 127.762 141.313 1.00 12.91 ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 168.958 134.498 142.133 1.00 6.54  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 167.783 134.710 142.970 1.00 5.12  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 166.940 135.867 142.452 1.00 6.72  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 165.705 135.800 142.466 1.00 14.54 ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 168.208 134.957 144.416 1.00 4.67  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 167.589 136.938 141.990 1.00 6.16  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 166.855 138.074 141.442 1.00 6.79  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 166.056 137.674 140.209 1.00 8.76  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 164.884 138.042 140.073 1.00 8.87  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 167.823 139.207 141.106 1.00 6.55  ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 167.175 140.571 141.190 1.00 7.26  ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 166.115 140.803 140.611 1.00 9.59  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 167.812 141.485 141.908 1.00 7.24  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 166.672 136.913 139.301 1.00 7.95  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 165.969 136.490 138.097 1.00 3.38  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 164.843 135.519 138.427 1.00 7.11  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 163.778 135.563 137.803 1.00 10.99 ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 166.948 135.870 137.103 1.00 6.45  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 168.062 136.804 136.673 1.00 7.31  ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 168.770 136.354 135.083 1.00 10.33 ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 167.289 136.216 134.092 1.00 10.18 ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 165.058 134.632 139.403 1.00 11.79 ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 163.990 133.729 139.821 1.00 8.32  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 162.811 134.500 140.397 1.00 9.54  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 161.652 134.203 140.084 1.00 12.82 ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 164.524 132.724 140.840 1.00 6.41  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 165.354 131.565 140.290 1.00 7.67  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 165.776 130.638 141.414 1.00 13.18 ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 164.575 130.807 139.230 1.00 8.42  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 163.087 135.502 141.236 1.00 5.12  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 162.017 136.318 141.795 1.00 6.99  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 161.279 137.084 140.703 1.00 10.47 ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 160.046 137.183 140.727 1.00 12.59 ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 162.588 137.279 142.837 1.00 7.23  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 161.670 138.429 143.204 1.00 6.70  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 162.229 139.221 144.376 1.00 9.96  ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 162.854 138.355 145.369 1.00 17.07 ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 163.086 138.705 146.627 1.00 16.26 ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 162.756 139.902 147.083 1.00 14.30 ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 163.663 137.833 147.447 1.00 9.13  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 162.018 137.630 139.735 1.00 11.53 ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 161.383 138.351 138.637 1.00 7.64  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 160.488 137.432 137.817 1.00 8.08  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 159.353 137.792 137.482 1.00 13.91 ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 162.446 138.996 137.748 1.00 8.08  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 163.049 140.094 138.441 1.00 11.98 ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 161.828 139.499 136.456 1.00 4.50  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 160.976 136.230 137.494 1.00 8.83  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 160.179 135.304 136.698 1.00 8.85  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 158.983 134.776 137.477 1.00 11.69 ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 157.966 134.416 136.875 1.00 17.27 ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 161.052 134.151 136.207 1.00 6.17  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 161.748 134.433 134.907 1.00 7.77  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 161.024 134.553 133.732 1.00 10.37 ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 163.121 134.583 134.858 1.00 12.33 ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 161.660 134.814 132.537 1.00 10.18 ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 163.761 134.844 133.665 1.00 14.17 ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 163.030 134.958 132.503 1.00 15.41 ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 159.084 134.712 138.806 1.00 9.12  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 157.937 134.296 139.606 1.00 10.28 ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 156.889 135.398 139.687 1.00 11.10 ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 155.686 135.121 139.644 1.00 16.89 ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 158.391 133.885 141.005 1.00 11.60 ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 158.524 135.015 141.847 1.00 14.48 ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 157.326 136.655 139.808 1.00 8.41  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 156.376 137.754 139.955 1.00 9.35  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 155.569 137.976 138.679 1.00 11.84 ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 154.367 138.251 138.742 1.00 11.71 ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 157.109 139.033 140.354 1.00 10.43 ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 157.863 139.549 139.271 1.00 13.31 ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 156.209 137.869 137.524 1.00 13.52 ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 155.523 138.113 136.253 1.00 14.58 ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 154.657 136.901 135.919 1.00 16.80 ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 155.166 135.769 135.916 1.00 15.61 ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 156.530 138.390 135.143 1.00 15.74 ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 157.436 139.560 135.526 1.00 14.95 ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 155.810 138.689 133.839 1.00 13.69 ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 158.580 139.782 134.567 1.00 13.93 ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 153.366 137.090 135.646 1.00 18.75 ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 152.509 135.948 135.304 1.00 18.62 ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 152.962 135.268 134.022 1.00 17.92 ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 153.514 135.898 133.117 1.00 20.46 ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 151.122 136.581 135.140 1.00 16.75 ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 151.192 137.863 135.899 1.00 18.72 ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 152.602 138.343 135.747 1.00 18.84 ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 152.725 133.957 133.957 1.00 23.48 ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 153.134 133.176 132.793 1.00 26.32 ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 152.379 133.630 131.551 1.00 25.77 ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 152.955 133.746 130.462 1.00 24.37 ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 152.927 131.673 133.061 1.00 27.10 ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 153.251 130.860 131.818 1.00 25.57 ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 153.771 131.222 134.240 1.00 23.35 ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 151.076 133.891 131.692 1.00 25.48 ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 150.261 134.264 130.541 1.00 26.27 ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 150.713 135.580 129.924 1.00 27.02 ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 150.482 135.817 128.733 1.00 28.65 ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 148.790 134.346 130.949 1.00 25.23 ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 148.622 135.192 132.073 1.00 29.13 ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 151.350 136.449 130.711 1.00 20.56 ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 151.845 137.708 130.166 1.00 18.82 ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 153.059 137.487 129.272 1.00 20.33 ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 153.164 138.087 128.197 1.00 20.23 ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 152.184 138.674 131.300 1.00 17.27 ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 152.675 140.026 130.826 1.00 17.88 ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 153.158 140.876 131.984 1.00 18.56 ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 152.886 142.290 131.760 1.00 16.32 ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 153.074 143.241 132.665 1.00 17.35 ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 153.545 142.965 133.869 1.00 21.62 ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 152.783 144.499 132.351 1.00 15.34 ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 153.989 136.632 129.703 1.00 24.05 ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 155.188 136.375 128.912 1.00 21.95 ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 154.850 135.575 127.661 1.00 22.59 ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 155.375 135.845 126.574 1.00 21.37 ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 156.245 135.659 129.772 1.00 20.75 ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 156.580 136.496 131.007 1.00 19.75 ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 157.498 135.387 128.963 1.00 21.32 ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 157.510 135.804 131.975 1.00 22.60 ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 153.969 134.584 127.788 1.00 29.93 ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 153.638 133.691 126.677 1.00 32.74 ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 152.458 134.256 125.885 1.00 35.22 ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 151.355 133.707 125.858 1.00 36.94 ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 153.347 132.289 127.194 1.00 36.04 ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 154.781 131.438 127.894 1.00 49.38 ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 152.716 135.382 125.228 1.00 34.86 ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 151.736 136.022 124.366 1.00 31.67 ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 152.054 135.708 122.905 1.00 34.08 ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 152.892 134.855 122.597 1.00 36.36 ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 151.687 137.524 124.641 1.00 29.05 ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 150.739 137.900 125.769 1.00 29.40 ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 150.590 139.405 125.899 1.00 33.21 ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 149.820 139.981 124.723 1.00 31.50 ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 148.397 139.546 124.727 1.00 32.44 ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 151.365 136.395 121.991 1.00 37.26 ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 151.452 136.051 120.572 1.00 38.97 ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 152.869 136.111 120.012 1.00 40.53 ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 153.284 135.140 119.356 1.00 41.87 ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 150.496 136.941 119.770 1.00 40.70 ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 149.154 136.753 120.183 1.00 43.74 ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 153.655 137.173 120.211 1.00 36.27 ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 155.021 137.169 119.666 1.00 34.78 ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 155.923 136.240 120.466 1.00 35.44 ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 155.979 136.313 121.694 1.00 34.80 ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 155.465 138.633 119.785 1.00 28.83 ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 154.218 139.408 120.074 1.00 32.14 ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 153.343 138.471 120.833 1.00 31.95 ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 156.630 135.357 119.755 1.00 31.95 ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 157.549 134.437 120.414 1.00 31.64 ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 158.773 135.146 120.975 1.00 32.23 ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 159.451 134.591 121.847 1.00 32.45 ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 157.987 133.343 119.439 1.00 33.20 ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 156.840 132.452 119.008 1.00 35.72 ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 155.714 132.600 119.482 1.00 34.69 ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 157.120 131.520 118.107 1.00 34.56 ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 159.069 136.356 120.499 1.00 26.50 ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 160.217 137.122 120.965 1.00 25.05 ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 159.968 137.796 122.307 1.00 23.47 ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 160.920 138.297 122.922 1.00 26.96 ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 160.593 138.171 119.915 1.00 21.64 ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 161.270 137.605 118.671 1.00 24.31 ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 160.341 136.776 117.800 1.00 28.72 ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 159.115 136.797 118.034 1.00 33.07 ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 160.843 136.096 116.880 1.00 26.38 ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 158.716 137.817 122.768 1.00 18.69 ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 158.402 138.448 124.043 1.00 14.29 ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 159.099 137.738 125.196 1.00 15.31 ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 159.519 138.379 126.164 1.00 17.55 ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 156.889 138.467 124.255 1.00 18.02 ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 156.444 139.186 125.513 1.00 18.01 ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 154.932 139.257 125.593 1.00 18.01 ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 154.345 139.706 124.337 1.00 19.60 ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 153.605 140.797 124.206 1.00 15.79 ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 153.339 141.579 125.237 1.00 14.95 ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 153.118 141.111 123.009 1.00 16.25 ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 159.227 136.412 125.113 1.00 18.18 ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 159.915 135.672 126.165 1.00 14.65 ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 161.380 136.077 126.259 1.00 13.69 ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 161.907 136.279 127.361 1.00 17.13 ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 159.786 134.169 125.919 1.00 17.81 ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 162.054 136.210 125.117 1.00 12.32 ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 163.451 136.630 125.133 1.00 12.59 ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 163.591 138.067 125.615 1.00 12.61 ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 164.540 138.394 126.338 1.00 18.07 ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 164.069 136.469 123.745 1.00 12.68 ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 165.587 136.497 123.744 1.00 13.25 ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 166.135 135.858 122.483 1.00 15.61 ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 167.465 135.298 122.674 1.00 17.46 ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 167.780 134.033 122.438 1.00 19.76 ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 166.878 133.164 122.015 1.00 19.10 ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 169.031 133.629 122.632 1.00 22.43 ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 162.662 138.942 125.222 1.00 12.53 ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 162.704 140.317 125.709 1.00 5.85  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 162.525 140.369 127.222 1.00 8.38  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 163.222 141.121 127.913 1.00 14.89 ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 161.634 141.155 125.012 1.00 8.53  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 161.888 141.453 123.535 1.00 9.13  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 160.953 142.539 123.039 1.00 12.55 ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 163.333 141.851 123.324 1.00 11.20 ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 161.597 139.573 127.754 1.00 9.95  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 161.393 139.526 129.197 1.00 8.39  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 162.611 138.959 129.912 1.00 11.92 ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 162.966 139.421 131.000 1.00 17.56 ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 160.144 138.708 129.522 1.00 9.26  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 158.884 139.535 129.601 1.00 12.65 ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 158.351 140.135 128.470 1.00 11.38 ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 158.229 139.720 130.810 1.00 16.37 ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 157.202 140.892 128.539 1.00 7.19  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 157.079 140.476 130.887 1.00 16.71 ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 156.571 141.059 129.749 1.00 11.18 ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 155.426 141.812 129.825 1.00 12.72 ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 163.257 137.949 129.324 1.00 10.10 ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 164.476 137.416 129.921 1.00 5.59  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 165.583 138.464 129.950 1.00 9.75  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 166.306 138.584 130.945 1.00 16.43 ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 164.944 136.175 129.165 1.00 9.42  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 166.258 135.636 129.651 1.00 12.80 ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 166.307 134.752 130.713 1.00 14.22 ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 167.444 136.021 129.054 1.00 13.18 ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 167.512 134.262 131.163 1.00 15.87 ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 168.651 135.537 129.502 1.00 10.65 ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 168.685 134.656 130.556 1.00 14.61 ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 165.744 139.214 128.859 1.00 14.22 ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 166.753 140.268 128.833 1.00 9.57  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 166.445 141.344 129.864 1.00 7.84  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 167.352 141.859 130.529 1.00 14.56 ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 166.844 140.878 127.435 1.00 10.56 ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 167.610 140.068 126.391 1.00 10.70 ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 167.424 140.674 125.011 1.00 9.83  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 169.083 139.990 126.751 1.00 14.10 ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 165.167 141.693 130.013 1.00 4.58  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 164.767 142.655 131.032 1.00 7.25  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 165.080 142.144 132.433 1.00 9.52  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 165.568 142.897 133.284 1.00 12.08 ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 163.279 142.960 130.888 1.00 10.54 ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 162.728 144.183 131.611 1.00 12.19 ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 163.708 145.338 131.532 1.00 8.30  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 161.395 144.558 130.995 1.00 11.54 ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 164.800 140.864 132.691 1.00 6.43  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 165.091 140.285 133.998 1.00 5.94  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 166.587 140.276 134.277 1.00 10.95 ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 167.019 140.582 135.395 1.00 17.97 ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 164.521 138.870 134.081 1.00 7.11  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 167.393 139.920 133.276 1.00 7.32  ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 168.843 139.931 133.453 1.00 3.97  ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 169.354 141.341 133.718 1.00 7.90  ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 170.215 141.544 134.582 1.00 14.41 ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 169.531 139.334 132.227 1.00 5.30  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 171.023 139.443 132.281 1.00 9.58  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 171.791 140.445 131.766 1.00 11.46 ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 171.930 138.522 132.898 1.00 12.42 ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 173.117 140.203 132.018 1.00 13.02 ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 173.229 139.028 132.712 1.00 13.04 ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 171.768 137.316 133.586 1.00 11.30 ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 174.361 138.372 133.190 1.00 12.33 ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 172.891 136.667 134.059 1.00 9.67  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 174.170 137.196 133.859 1.00 10.04 ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 168.843 142.327 132.978 1.00 9.74  ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 169.252 143.711 133.194 1.00 6.02  ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 168.899 144.167 134.604 1.00 8.67  ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 169.723 144.777 135.298 1.00 18.79 ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 168.590 144.606 132.145 1.00 11.61 ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 168.869 146.069 132.326 1.00 12.07 ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 170.065 146.617 131.900 1.00 12.68 ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 167.926 146.901 132.905 1.00 10.11 ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 170.319 147.961 132.061 1.00 10.18 ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 168.177 148.245 133.066 1.00 9.80  ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 169.374 148.776 132.644 1.00 11.71 ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 167.679 143.863 135.050 1.00 5.70  ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 167.260 144.242 136.394 1.00 3.04  ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 168.133 143.580 137.450 1.00 8.26  ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 168.542 144.225 138.422 1.00 9.69  ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 165.792 143.873 136.600 1.00 6.60  ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 165.180 144.482 137.821 1.00 8.02  ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 164.945 145.834 137.942 1.00 4.22  ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 164.750 143.920 138.977 1.00 7.61  ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 164.400 146.081 139.118 1.00 7.31  ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 164.271 144.938 139.765 1.00 8.02  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 168.430 142.290 137.274 1.00 14.76 ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 169.267 141.581 138.235 1.00 7.29  ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 170.666 142.177 138.295 1.00 10.58 ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 171.211 142.383 139.385 1.00 16.30 ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 169.333 140.098 137.878 1.00 6.14  ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 171.257 142.467 137.134 1.00 12.39 ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 172.605 143.029 137.106 1.00 4.84  ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 172.629 144.386 137.793 1.00 4.75  ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 173.524 144.674 138.597 1.00 10.76 ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 173.120 143.121 135.657 1.00 7.58  ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 173.307 141.725 135.060 1.00 10.17 ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 174.420 143.901 135.600 1.00 8.92  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 173.961 140.737 135.991 1.00 11.74 ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 171.643 145.236 137.503 1.00 8.23  ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 171.616 146.572 138.096 1.00 6.23  ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 171.448 146.481 139.610 1.00 7.59  ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 172.174 147.130 140.379 1.00 12.18 ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 170.503 147.416 137.451 1.00 3.52  ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 170.768 147.601 135.955 1.00 9.09  ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 170.390 148.752 138.131 1.00 9.84  ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 172.189 147.974 135.619 1.00 10.89 ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 170.498 145.658 140.063 1.00 8.34  ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 170.236 145.554 141.495 1.00 6.49  ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 171.418 144.950 142.238 1.00 9.34  ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 171.699 145.331 143.380 1.00 11.41 ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 168.971 144.733 141.734 1.00 8.09  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 167.691 145.524 141.575 1.00 4.19  ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 166.538 144.911 142.332 1.00 8.43  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 166.157 143.768 142.083 1.00 13.88 ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 165.975 145.664 143.268 1.00 10.11 ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 172.123 144.000 141.619 1.00 6.99  ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 173.311 143.448 142.256 1.00 2.49  ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 174.454 144.451 142.272 1.00 6.74  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 175.244 144.471 143.221 1.00 13.07 ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 173.731 142.160 141.553 1.00 3.11  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 172.862 140.968 141.895 1.00 11.58 ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 172.647 140.816 143.386 1.00 20.06 ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 173.646 140.641 144.114 1.00 13.84 ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 171.480 140.873 143.828 1.00 19.01 ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 174.565 145.285 141.235 1.00 7.29  ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 175.555 146.355 141.258 1.00 0.70  ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 175.250 147.372 142.345 1.00 4.49  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 176.157 148.061 142.823 1.00 8.14  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 175.619 147.049 139.899 1.00 2.55  ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 176.318 146.249 138.825 1.00 3.94  ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 176.569 147.103 137.602 1.00 3.88  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 177.596 148.107 137.844 1.00 1.66  ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 178.801 148.090 137.292 1.00 2.77  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 179.161 147.135 136.451 1.00 2.32  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 179.665 149.055 137.589 1.00 4.88  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 173.980 147.487 142.745 1.00 6.68  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 173.634 148.394 143.834 1.00 4.78  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 174.329 148.036 145.144 1.00 6.70  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 174.503 148.913 145.996 1.00 5.67  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 172.122 148.411 144.051 1.00 7.30  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 171.321 149.409 143.218 1.00 8.29  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 169.834 149.217 143.456 1.00 7.77  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 171.742 150.829 143.545 1.00 6.28  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 174.722 146.771 145.329 1.00 9.74  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 175.347 146.362 146.584 1.00 6.79  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 176.696 147.044 146.787 1.00 9.71  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 177.023 147.466 147.902 1.00 10.24 ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 175.507 144.845 146.622 1.00 0.77  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 174.197 144.088 146.656 1.00 7.87  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 174.422 142.596 146.807 1.00 9.76  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 173.167 141.854 146.788 1.00 10.73 ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 172.334 141.763 147.816 1.00 12.16 ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 172.593 142.352 148.970 1.00 11.22 ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 171.212 141.063 147.680 1.00 11.25 ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 177.493 147.152 145.728 1.00 10.77 ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 178.793 147.817 145.784 1.00 5.90  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 178.555 149.295 145.507 1.00 8.84  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 178.596 149.753 144.365 1.00 11.57 ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 179.758 147.178 144.794 1.00 4.32  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 179.616 145.675 144.735 1.00 5.14  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 180.273 144.859 145.645 1.00 10.38 ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 178.805 145.070 143.785 1.00 7.49  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 180.139 143.486 145.601 1.00 12.73 ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 178.664 143.699 143.735 1.00 6.92  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 179.332 142.912 144.644 1.00 9.87  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 179.194 141.544 144.596 1.00 10.72 ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 178.300 150.045 146.579 1.00 8.11  ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 177.763 151.398 146.444 1.00 5.72  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 178.670 152.351 145.674 1.00 14.35 ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 178.159 153.071 144.799 1.00 23.44 ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 177.424 151.956 147.829 1.00 9.84  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 179.988 152.437 145.937 1.00 10.89 ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 180.796 153.425 145.210 1.00 1.02  ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 181.210 152.976 143.817 1.00 5.25  ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 181.406 153.814 142.932 1.00 12.28 ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 182.023 153.614 146.115 1.00 5.41  ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 181.677 152.947 147.414 1.00 14.70 ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 180.761 151.837 147.036 1.00 11.44 ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 181.350 151.669 143.600 1.00 5.08  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 181.841 151.156 142.324 1.00 6.26  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 180.723 150.717 141.387 1.00 10.87 ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 180.737 151.075 140.206 1.00 13.76 ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 182.810 149.991 142.557 1.00 3.74  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 184.278 150.376 142.724 1.00 2.99  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 184.537 150.927 144.116 1.00 9.81  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 185.173 149.186 142.439 1.00 10.50 ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 179.765 149.933 141.881 1.00 7.70  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 178.657 149.520 141.035 1.00 6.44  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 177.849 150.698 140.529 1.00 8.57  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 177.486 150.757 139.352 1.00 10.26 ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 177.564 151.652 141.409 1.00 3.92  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 176.913 152.902 141.051 1.00 4.73  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 177.645 154.017 141.789 1.00 8.00  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 178.743 153.819 142.312 1.00 13.28 ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 175.415 152.847 141.378 1.00 3.87  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 174.665 151.895 140.502 1.00 5.45  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 174.147 150.686 140.859 1.00 5.25  ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 174.359 152.068 139.115 1.00 8.13  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 173.532 150.099 139.783 1.00 1.59  ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 173.649 150.928 138.699 1.00 4.97  ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 174.612 153.081 138.185 1.00 8.37  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 173.193 150.772 137.395 1.00 4.16  ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 174.159 152.921 136.892 1.00 7.69  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 173.457 151.775 136.509 1.00 4.47  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 177.058 155.211 141.812 1.00 5.56  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 177.598 156.281 142.638 1.00 6.50  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 176.831 156.463 143.937 1.00 10.03 ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 177.387 157.007 144.897 1.00 16.07 ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 177.609 157.606 141.867 1.00 10.40 ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 178.611 157.602 140.867 1.00 12.98 ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 175.580 156.017 143.989 1.00 8.20  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 174.770 156.107 145.194 1.00 10.43 ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 173.737 154.993 145.156 1.00 10.14 ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 173.501 154.372 144.117 1.00 13.29 ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 174.106 157.480 145.321 1.00 8.24  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 173.308 157.896 144.104 1.00 8.05  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 172.645 159.246 144.317 1.00 14.40 ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 173.669 160.368 144.324 1.00 11.89 ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 174.313 160.543 142.994 1.00 11.00 ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 173.122 154.742 146.311 1.00 8.15  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 172.122 153.684 146.444 1.00 9.25  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 170.822 154.147 145.792 1.00 11.44 ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 169.905 154.655 146.439 1.00 12.51 ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 171.912 153.321 147.908 1.00 10.86 ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 172.984 152.417 148.486 1.00 11.20 ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 172.847 151.002 147.954 1.00 12.32 ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 173.439 149.989 148.920 1.00 11.82 ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 174.898 150.200 149.127 1.00 8.96  ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 170.752 153.973 144.476 1.00 7.51  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 169.531 154.275 143.748 1.00 3.66  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 168.424 153.307 144.142 1.00 8.00  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 168.674 152.160 144.520 1.00 12.50 ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 169.765 154.201 142.243 1.00 3.10  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 170.680 155.269 141.701 1.00 2.49  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 170.353 156.611 141.815 1.00 3.80  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 171.867 154.934 141.070 1.00 4.39  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 171.186 157.589 141.318 1.00 6.80  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 172.704 155.903 140.571 1.00 4.23  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 172.360 157.230 140.698 1.00 7.88  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 173.196 158.201 140.200 1.00 11.91 ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 167.188 153.782 144.050 1.00 9.66  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 166.028 152.965 144.404 1.00 5.45  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 165.513 152.177 143.203 1.00 6.65  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 164.333 152.224 142.864 1.00 14.20 ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 164.933 153.847 144.990 1.00 8.76  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 165.366 154.648 146.208 1.00 8.27  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 165.623 153.775 147.420 1.00 16.09 ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 165.016 152.688 147.509 1.00 19.51 ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 166.432 154.174 148.283 1.00 14.52 ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 166.409 151.442 142.547 1.00 5.69  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 166.015 150.548 141.465 1.00 4.01  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 165.231 149.382 142.052 1.00 5.66  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 165.811 148.491 142.681 1.00 8.37  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 167.244 150.050 140.711 1.00 4.28  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 167.985 151.126 139.972 1.00 8.17  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 167.318 151.984 139.116 1.00 7.35  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 169.352 151.277 140.130 1.00 5.83  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 168.002 152.971 138.433 1.00 6.13  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 170.039 152.258 139.445 1.00 3.38  ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 169.363 153.108 138.599 1.00 3.15  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 163.917 149.381 141.852 1.00 4.68  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 163.081 148.394 142.502 1.00 6.48  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 162.030 147.762 141.617 1.00 2.98  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 162.167 147.730 140.392 1.00 5.82  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 160.966 147.251 142.241 1.00 4.08  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 159.927 146.546 141.500 1.00 2.79  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 159.165 147.473 140.565 1.00 2.75  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 158.739 147.043 139.489 1.00 8.86  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 158.965 145.865 142.474 1.00 5.15  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 157.908 144.999 141.811 1.00 7.17  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 158.480 143.722 141.225 1.00 16.21 ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 159.584 143.314 141.643 1.00 10.35 ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 157.823 143.127 140.346 1.00 17.88 ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 158.981 148.737 140.954 1.00 3.74  ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 158.231 149.666 140.113 1.00 3.87  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 158.920 149.878 138.772 1.00 4.94  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 158.259 149.941 137.728 1.00 7.97  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 158.047 150.996 140.841 1.00 2.68  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 159.297 151.593 141.134 1.00 7.08  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 160.250 149.993 138.781 1.00 3.27  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 160.989 150.139 137.532 1.00 0.00  ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 160.827 148.910 136.649 1.00 1.23  ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 160.666 149.031 135.430 1.00 8.62  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 162.465 150.395 137.825 1.00 2.78  ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 162.705 151.746 138.457 1.00 5.47  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 161.923 152.679 138.182 1.00 9.75  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 163.674 151.879 139.231 1.00 8.29  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 160.868 147.718 137.246 1.00 1.78  ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 160.692 146.496 136.469 1.00 1.26  ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 159.295 146.423 135.863 1.00 1.90  ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 159.137 146.039 134.699 1.00 6.39  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 160.965 145.275 137.344 1.00 2.21  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 160.774 143.907 136.691 1.00 3.49  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 161.779 143.696 135.572 1.00 0.38  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 160.893 142.812 137.732 1.00 9.11  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 158.270 146.785 136.638 1.00 2.48  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 156.909 146.783 136.109 1.00 0.78  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 156.754 147.787 134.976 1.00 4.89  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 156.122 147.491 133.956 1.00 8.16  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 155.908 147.079 137.225 1.00 2.16  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 155.990 146.134 138.408 1.00 4.98  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 154.701 146.143 139.209 1.00 6.10  ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 154.960 146.111 140.643 1.00 14.37 ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 154.915 147.173 141.436 1.00 14.41 ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 154.622 148.374 140.966 1.00 9.73  ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 155.173 147.027 142.733 1.00 7.77  ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 157.323 148.986 135.137 1.00 3.18  ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 157.243 149.989 134.079 1.00 0.00  ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 157.962 149.522 132.820 1.00 1.79  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 157.473 149.725 131.703 1.00 5.88  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 157.825 151.313 134.570 1.00 0.00  ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 157.199 151.725 135.772 1.00 4.99  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 159.130 148.896 132.981 1.00 0.51  ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 159.868 148.392 131.829 1.00 0.00  ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 159.105 147.277 131.126 1.00 1.76  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 159.084 147.215 129.893 1.00 9.23  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 161.249 147.913 132.265 1.00 0.00  ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 158.478 146.382 131.894 1.00 3.23  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 157.668 145.328 131.293 1.00 3.28  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 156.479 145.910 130.540 1.00 5.54  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 156.142 145.447 129.444 1.00 9.79  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 157.197 144.349 132.366 1.00 5.20  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 158.504 143.324 133.073 1.00 16.19 ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 155.831 146.927 131.113 1.00 5.21  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 154.718 147.575 130.428 1.00 4.20  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 155.175 148.230 129.133 1.00 4.91  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 154.489 148.146 128.110 1.00 7.66  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 154.063 148.608 131.346 1.00 3.97  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 153.432 147.982 132.571 1.00 10.01 ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 153.190 146.759 132.559 1.00 15.69 ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 153.176 148.714 133.551 1.00 8.75  ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 156.333 148.894 129.160 1.00 4.20  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 156.869 149.513 127.952 1.00 4.09  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 157.186 148.469 126.888 1.00 5.52  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 156.884 148.663 125.702 1.00 11.06 ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 158.117 150.325 128.296 1.00 1.45  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 157.747 151.462 129.086 1.00 3.89  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 158.822 150.794 127.037 1.00 3.62  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 157.794 147.353 127.297 1.00 6.28  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 158.115 146.286 126.353 1.00 5.78  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 156.841 145.739 125.724 1.00 8.81  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 156.761 145.555 124.505 1.00 12.29 ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 158.924 145.178 127.050 1.00 4.55  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 158.823 143.873 126.278 1.00 5.26  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 160.376 145.598 127.204 1.00 4.29  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 155.821 145.489 126.548 1.00 7.35  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 154.550 144.991 126.029 1.00 3.87  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 153.935 145.977 125.047 1.00 6.03  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 153.503 145.596 123.952 1.00 8.58  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 153.584 144.720 127.181 1.00 6.59  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 153.827 143.385 127.845 1.00 16.38 ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 154.468 142.516 127.220 1.00 19.97 ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 153.374 143.203 128.993 1.00 16.82 ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 153.901 147.259 125.421 1.00 9.12  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 153.277 148.270 124.577 1.00 9.62  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 153.966 148.355 123.223 1.00 9.12  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 153.313 148.300 122.175 1.00 14.51 ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 153.311 149.629 125.278 1.00 6.52  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 152.472 149.592 126.438 1.00 8.34  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 152.826 150.724 124.346 1.00 6.75  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 155.295 148.459 123.222 1.00 5.17  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 155.993 148.653 121.957 1.00 7.64  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 156.073 147.375 121.133 1.00 11.88 ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 156.117 147.446 119.899 1.00 16.94 ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 157.381 149.237 122.217 1.00 8.96  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 157.294 150.673 122.614 1.00 9.11  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 157.254 151.173 123.881 1.00 8.60  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 157.193 151.799 121.735 1.00 8.08  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 157.150 152.542 123.847 1.00 7.19  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 157.112 152.950 122.540 1.00 8.69  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 157.174 151.945 120.346 1.00 7.14  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 157.012 154.229 122.003 1.00 9.85  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 157.075 153.216 119.815 1.00 9.36  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 156.996 154.341 120.641 1.00 9.31  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 156.062 146.203 121.773 1.00 10.98 ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 156.020 144.962 121.010 1.00 12.18 ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 154.661 144.769 120.351 1.00 16.16 ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 154.584 144.345 119.192 1.00 19.00 ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 156.355 143.777 121.915 1.00 12.80 ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 156.957 142.561 121.215 1.00 13.46 ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 158.088 142.983 120.292 1.00 14.22 ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 157.447 141.553 122.236 1.00 15.64 ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 153.574 145.075 121.067 1.00 12.08 ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 152.255 145.007 120.450 1.00 12.35 ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 152.088 146.074 119.375 1.00 20.21 ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 151.360 145.861 118.400 1.00 24.06 ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 151.165 145.146 121.513 1.00 15.94 ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 151.284 144.102 122.605 1.00 22.82 ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 152.202 143.259 122.523 1.00 24.27 ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 150.464 144.124 123.545 1.00 23.46 ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 152.746 147.223 119.539 1.00 21.20 ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 152.707 148.254 118.508 1.00 20.40 ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 153.416 147.770 117.247 1.00 20.32 ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 152.874 147.872 116.141 1.00 20.52 ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 153.334 149.543 119.063 1.00 18.34 ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 153.454 150.673 118.032 1.00 25.33 ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 153.572 150.436 116.813 1.00 26.04 ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 153.433 151.841 118.471 1.00 25.18 ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 154.628 147.230 117.395 1.00 21.43 ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 155.379 146.791 116.223 1.00 24.70 ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 154.796 145.515 115.627 1.00 25.53 ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 154.655 145.405 114.404 1.00 25.39 ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 156.848 146.587 116.584 1.00 24.48 ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 157.346 147.761 117.238 1.00 25.41 ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 157.663 146.331 115.333 1.00 22.31 ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 154.454 144.542 116.468 1.00 27.96 ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 153.906 143.268 116.016 1.00 29.96 ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 152.390 143.317 116.157 1.00 35.40 ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 151.860 143.266 117.271 1.00 37.40 ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 154.495 142.107 116.812 1.00 27.93 ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 151.692 143.410 115.024 1.00 39.75 ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 150.236 143.519 115.013 1.00 37.44 ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 149.590 142.136 115.130 1.00 37.87 ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 148.888 141.658 114.240 1.00 40.86 ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 149.773 144.243 113.755 1.00 39.30 ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 150.540 145.519 113.450 1.00 39.19 ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 150.431 146.514 114.593 1.00 39.64 ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 148.999 146.987 114.786 1.00 41.42 ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 148.880 147.948 115.919 1.00 38.41 ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 149.846 141.492 116.266 1.00 38.22 ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 149.297 140.177 116.526 1.00 38.49 ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 149.982 139.039 115.809 1.00 40.81 ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 149.469 137.914 115.838 1.00 42.36 ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 151.118 139.289 115.163 1.00 40.21 ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 151.827 138.232 114.460 1.00 38.36 ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 152.454 137.257 115.450 1.00 39.71 ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 152.781 137.609 116.586 1.00 39.67 ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 152.906 138.824 113.554 1.00 38.01 ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 152.388 139.857 112.567 1.00 39.13 ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 153.307 139.979 111.366 1.00 39.73 ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 154.463 140.822 111.645 1.00 43.46 ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 154.510 142.128 111.426 1.00 41.68 ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 153.476 142.782 110.923 1.00 39.23 ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 155.622 142.797 111.716 1.00 39.63 ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 152.614 136.009 115.005 1.00 42.01 ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 153.186 134.989 115.876 1.00 41.00 ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 154.690 135.171 116.034 1.00 40.59 ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 155.242 134.923 117.112 1.00 39.72 ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 152.869 133.595 115.333 1.00 38.29 ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 152.672 132.543 116.411 1.00 40.50 ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 151.687 132.974 117.479 1.00 43.26 ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 150.629 133.527 117.179 1.00 40.83 ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 152.031 132.723 118.737 1.00 42.56 ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 155.371 135.600 114.973 1.00 36.92 ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 156.811 135.805 114.999 1.00 35.77 ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 157.147 137.166 114.412 1.00 35.43 ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 156.534 137.597 113.431 1.00 37.00 ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 157.547 134.706 114.223 1.00 36.61 ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 157.271 133.322 114.771 1.00 39.27 ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 156.203 132.754 114.547 1.00 40.46 ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 158.238 132.768 115.494 1.00 35.74 ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 158.122 137.835 115.018 1.00 31.90 ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 158.617 139.124 114.549 1.00 29.78 ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 160.129 139.028 114.411 1.00 26.74 ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 160.806 138.514 115.308 1.00 28.17 ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 158.220 140.271 115.502 1.00 28.31 ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 158.940 141.566 115.121 1.00 25.68 ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 158.499 139.899 116.951 1.00 27.29 ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 158.470 142.771 115.896 1.00 27.48 ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 160.651 139.499 113.284 1.00 23.23 ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 162.086 139.440 113.057 1.00 23.89 ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 162.814 140.293 114.095 1.00 26.22 ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 162.335 141.374 114.455 1.00 28.10 ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 162.428 139.922 111.647 1.00 25.91 ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 163.828 139.988 111.454 1.00 27.89 ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 163.961 139.835 114.602 1.00 22.23 ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 164.679 140.625 115.617 1.00 20.11 ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 165.115 141.993 115.125 1.00 22.37 ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 165.305 142.901 115.944 1.00 22.97 ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 165.882 139.737 115.961 1.00 21.88 ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 165.459 138.359 115.583 1.00 23.21 ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 164.591 138.524 114.374 1.00 22.31 ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 165.285 142.171 113.812 1.00 23.38 ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 165.601 143.494 113.283 1.00 24.67 ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 164.434 144.458 113.451 1.00 24.16 ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 164.648 145.666 113.598 1.00 26.09 ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 165.990 143.396 111.809 1.00 24.25 ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 167.317 142.700 111.599 1.00 27.19 ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 168.180 142.778 112.496 1.00 29.38 ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 167.499 142.077 110.533 1.00 30.57 ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 163.204 143.949 113.428 1.00 17.30 ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 162.025 144.798 113.504 1.00 19.89 ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 161.654 145.185 114.929 1.00 21.21 ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 160.806 146.066 115.108 1.00 24.97 ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 160.836 144.100 112.840 1.00 23.66 ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 161.068 143.725 111.386 1.00 22.31 ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 161.048 144.948 110.483 1.00 25.89 ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 162.439 145.263 109.949 1.00 25.65 ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 162.426 146.426 109.020 1.00 24.06 ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 162.257 144.559 115.934 1.00 16.46 ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 161.928 144.895 117.323 1.00 16.48 ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 162.355 146.330 117.606 1.00 16.42 ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 163.486 146.720 117.257 1.00 18.12 ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 162.612 143.914 118.291 1.00 14.16 ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 161.986 142.524 118.164 1.00 15.07 ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 162.522 144.409 119.725 1.00 11.02 ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 162.581 141.500 119.094 1.00 15.50 ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 161.506 147.159 118.219 1.00 14.56 ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 161.889 148.556 118.465 1.00 10.88 ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 162.949 148.683 119.545 1.00 10.01 ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 162.650 149.077 120.676 1.00 14.56 ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 160.570 149.207 118.894 1.00 9.40  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 159.784 148.090 119.483 1.00 9.03  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 160.138 146.872 118.680 1.00 11.74 ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 164.195 148.349 119.203 1.00 7.59  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 165.276 148.415 120.181 1.00 4.72  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 165.520 149.844 120.642 1.00 6.70  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 165.758 150.088 121.832 1.00 8.76  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 166.552 147.823 119.586 1.00 7.54  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 166.428 146.381 119.234 1.00 8.88  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 166.416 145.842 117.982 1.00 10.81 ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 166.298 145.286 120.145 1.00 10.40 ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 166.287 144.478 118.056 1.00 14.64 ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 166.213 144.111 119.375 1.00 12.83 ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 166.245 145.183 121.538 1.00 10.26 ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 166.078 142.852 119.949 1.00 11.68 ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 166.111 143.932 122.105 1.00 7.95  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 166.031 142.785 121.314 1.00 9.25  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 165.472 150.801 119.713 1.00 8.08  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 165.721 152.193 120.069 1.00 3.95  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 164.681 152.704 121.055 1.00 4.70  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 165.020 153.402 122.017 1.00 5.32  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 165.739 153.060 118.812 1.00 7.00  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 166.676 152.570 117.869 1.00 12.01 ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 163.411 152.361 120.837 1.00 5.32  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 162.352 152.813 121.735 1.00 3.27  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 162.574 152.293 123.149 1.00 2.87  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 162.541 153.063 124.117 1.00 6.12  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 160.992 152.365 121.205 1.00 4.75  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 162.809 150.987 123.285 1.00 5.34  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 163.011 150.399 124.605 1.00 4.76  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 164.245 150.979 125.281 1.00 4.56  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 164.206 151.351 126.461 1.00 8.79  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 163.128 148.879 124.489 1.00 4.18  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 162.036 148.158 123.701 1.00 3.69  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 162.292 146.662 123.688 1.00 5.34  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 160.667 148.464 124.280 1.00 4.45  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 165.354 151.070 124.543 1.00 2.19  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 166.593 151.571 125.128 1.00 0.44  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 166.441 153.014 125.587 1.00 3.69  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 166.849 153.367 126.699 1.00 6.92  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 167.737 151.441 124.124 1.00 1.76  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 168.357 150.060 124.076 1.00 5.96  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 169.525 150.015 123.111 1.00 6.38  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 169.062 150.196 121.678 1.00 6.61  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 170.141 149.875 120.705 1.00 11.77 ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 165.844 153.864 124.750 1.00 2.70  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 165.685 155.267 125.109 1.00 1.32  ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 164.722 155.438 126.277 1.00 2.46  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 164.975 156.242 127.181 1.00 8.47  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 165.207 156.069 123.901 1.00 5.22  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 165.982 155.709 122.752 1.00 9.54  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 165.356 157.559 124.156 1.00 4.19  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 163.616 154.691 126.286 1.00 1.94  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 162.656 154.838 127.372 1.00 1.92  ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 163.213 154.320 128.692 1.00 3.60  ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 162.888 154.865 129.752 1.00 9.12  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 161.350 154.130 127.020 1.00 0.26  ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 160.456 154.908 126.052 1.00 0.54  ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 159.140 154.197 125.844 1.00 4.60  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 160.220 156.319 126.558 1.00 3.05  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 164.047 153.281 128.656 1.00 1.64  ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 164.656 152.796 129.887 1.00 0.00  ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 165.794 153.695 130.355 1.00 0.00  ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 165.991 153.856 131.563 1.00 3.06  ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 165.158 151.367 129.695 1.00 1.37  ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 164.048 150.357 129.493 1.00 0.00  ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 164.656 148.680 129.259 1.00 7.94  ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 163.116 147.820 128.960 1.00 10.46 ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 166.550 154.283 129.425 1.00 2.40  ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 167.669 155.143 129.791 1.00 2.41  ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 167.222 156.528 130.235 1.00 4.67  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 167.933 157.180 131.005 1.00 8.36  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 168.636 155.269 128.615 1.00 0.00  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 166.071 156.999 129.759 1.00 4.68  ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 165.627 158.359 130.030 1.00 2.99  ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 164.440 158.446 130.976 1.00 6.75  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 164.310 159.444 131.684 1.00 7.54  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 165.259 159.065 128.720 1.00 3.75  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 166.365 159.082 127.676 1.00 4.84  ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 167.450 160.092 127.986 1.00 12.08 ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 167.188 161.290 128.080 1.00 18.20 ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 168.678 159.613 128.140 1.00 11.08 ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 163.574 157.435 131.007 1.00 5.76  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 162.328 157.517 131.759 1.00 1.83  ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 162.242 156.508 132.893 1.00 2.65  ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 161.971 156.893 134.036 1.00 5.34  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 161.132 157.331 130.811 1.00 1.29  ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 161.082 158.362 129.843 1.00 5.92  ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 162.462 155.226 132.615 1.00 4.88  ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 162.171 154.189 133.601 1.00 3.22  ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 163.302 154.068 134.614 1.00 2.96  ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 163.111 154.295 135.814 1.00 7.64  ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 161.896 152.848 132.900 1.00 0.00  ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 160.733 152.993 131.920 1.00 0.00  ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 161.596 151.772 133.923 1.00 0.00  ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 160.678 151.912 130.876 1.00 0.00  ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 164.495 153.710 134.148 1.00 3.26  ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 165.632 153.552 135.045 1.00 3.18  ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 166.481 154.808 135.146 1.00 3.59  ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 167.046 155.079 136.210 1.00 8.45  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 166.505 152.379 134.591 1.00 1.99  ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 165.902 151.021 134.866 1.00 1.86  ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 166.090 150.391 136.085 1.00 1.40  ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 165.145 150.368 133.902 1.00 3.97  ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 165.542 149.150 136.341 1.00 3.23  ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 164.594 149.128 134.148 1.00 0.86  ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 164.796 148.523 135.368 1.00 2.68  ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 164.249 147.289 135.618 1.00 6.05  ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 166.582 155.582 134.068 1.00 2.09  ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 167.363 156.801 134.092 1.00 1.09  ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 166.709 157.968 134.792 1.00 4.40  ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 167.363 158.994 134.993 1.00 10.60 ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 165.433 157.841 135.158 1.00 2.64  ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 164.787 158.900 135.914 1.00 0.00  ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 165.393 159.085 137.291 1.00 5.28  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 165.584 160.214 137.749 1.00 9.29  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 165.711 157.980 137.969 1.00 9.01  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 166.329 158.059 139.285 1.00 4.85  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 167.782 158.506 139.219 1.00 6.38  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 168.316 158.979 140.227 1.00 10.30 ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 166.247 156.703 139.986 1.00 4.07  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 164.933 155.976 139.785 1.00 7.09  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 164.947 154.631 140.485 1.00 7.30  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 163.618 154.040 140.561 1.00 9.66  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 162.692 154.386 141.445 1.00 10.09 ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 162.919 155.321 142.352 1.00 7.94  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 161.512 153.773 141.421 1.00 9.00  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 168.427 158.368 138.066 1.00 5.12  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 169.852 158.653 137.941 1.00 2.97  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 170.056 160.162 137.883 1.00 5.13  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 169.496 160.843 137.020 1.00 6.56  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 170.443 157.966 136.703 1.00 3.21  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 171.834 158.494 136.423 1.00 7.67  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 170.470 156.460 136.898 1.00 1.68  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 170.869 160.684 138.804 1.00 6.56  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 171.218 162.100 138.840 1.00 9.42  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 172.702 162.329 138.579 1.00 11.60 ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 173.222 163.408 138.878 1.00 13.45 ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 170.806 162.718 140.178 1.00 6.26  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 171.342 161.949 141.371 1.00 11.38 ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 172.287 161.148 141.205 1.00 11.61 ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 170.810 162.142 142.484 1.00 14.34 ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 173.392 161.335 138.027 1.00 10.81 ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 174.821 161.403 137.772 1.00 6.41  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 175.082 161.164 136.293 1.00 8.89  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 174.451 160.303 135.672 1.00 11.86 ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 175.576 160.372 138.619 1.00 3.01  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 177.072 160.605 138.634 1.00 10.04 ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 177.717 160.656 137.587 1.00 15.58 ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 177.635 160.742 139.827 1.00 13.38 ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 176.010 161.938 135.729 1.00 7.21  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 176.357 161.774 134.320 1.00 7.13  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 176.986 160.411 134.060 1.00 7.12  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 176.665 159.750 133.066 1.00 9.07  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 177.298 162.896 133.887 1.00 8.81  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 178.185 162.555 132.704 1.00 11.61 ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 179.131 163.682 132.342 1.00 16.42 ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 179.931 163.510 131.399 1.00 15.55 ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 179.077 164.739 133.004 1.00 15.37 ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 177.878 159.970 134.947 1.00 4.73  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 178.572 158.705 134.746 1.00 4.13  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 177.696 157.504 135.072 1.00 8.59  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 177.835 156.452 134.439 1.00 17.52 ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 179.858 158.694 135.569 1.00 6.33  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 180.752 159.861 135.282 1.00 10.15 ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 181.641 159.819 134.223 1.00 10.49 ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 180.677 161.013 136.044 1.00 7.14  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 182.453 160.895 133.942 1.00 8.67  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 181.487 162.091 135.767 1.00 8.03  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 182.376 162.031 134.716 1.00 11.19 ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 176.782 157.636 136.035 1.00 5.39  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 175.783 156.595 136.237 1.00 4.07  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 174.894 156.452 135.009 1.00 5.07  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 174.552 155.334 134.604 1.00 10.27 ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 174.941 156.905 137.473 1.00 4.65  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 175.708 156.715 138.761 1.00 10.83 ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 176.712 155.974 138.755 1.00 13.57 ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 175.308 157.316 139.777 1.00 12.28 ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 174.513 157.578 134.403 1.00 1.48  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 173.754 157.532 133.159 1.00 0.00  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 174.559 156.872 132.050 1.00 4.18  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 174.018 156.090 131.261 1.00 12.63 ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 173.334 158.943 132.751 1.00 4.27  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 172.432 158.996 131.533 1.00 6.12  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 171.087 158.350 131.781 1.00 6.39  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 170.424 158.631 132.779 1.00 8.81  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 170.672 157.477 130.871 1.00 7.34  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 175.857 157.176 131.972 1.00 5.75  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 176.705 156.554 130.961 1.00 5.02  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 176.789 155.045 131.159 1.00 6.09  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 176.731 154.280 130.193 1.00 10.71 ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 178.098 157.182 130.995 1.00 6.41  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 179.155 156.406 130.232 1.00 9.06  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 180.498 157.112 130.285 1.00 10.55 ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 181.188 156.878 131.548 1.00 13.87 ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 182.383 157.367 131.848 1.00 13.03 ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 183.054 158.125 130.997 1.00 9.60  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 182.921 157.084 133.030 1.00 13.21 ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 176.920 154.599 132.409 1.00 3.47  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 176.969 153.167 132.693 1.00 0.30  ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 175.648 152.484 132.356 1.00 7.25  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 175.635 151.384 131.787 1.00 14.92 ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 177.333 152.947 134.161 1.00 1.27  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 177.336 151.507 134.668 1.00 4.37  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 178.304 150.673 133.856 1.00 8.11  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 177.698 151.473 136.139 1.00 5.17  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 174.528 153.118 132.710 1.00 4.69  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 173.222 152.560 132.377 1.00 1.30  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 173.041 152.455 130.868 1.00 1.05  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 172.537 151.445 130.362 1.00 5.74  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 172.121 153.421 132.998 1.00 5.37  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 170.678 152.919 132.935 1.00 9.21  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 170.417 151.901 134.029 1.00 7.68  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 169.718 154.085 133.051 1.00 6.16  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 173.460 153.487 130.133 1.00 1.32  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 173.402 153.437 128.676 1.00 2.37  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 174.291 152.331 128.129 1.00 4.40  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 173.917 151.644 127.174 1.00 5.81  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 173.810 154.787 128.088 1.00 1.99  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 172.853 155.900 128.459 1.00 5.83  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 171.792 155.653 129.028 1.00 9.15  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 173.225 157.132 128.141 1.00 6.41  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 175.479 152.157 128.708 1.00 6.17  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 176.372 151.089 128.267 1.00 6.19  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 175.705 149.731 128.414 1.00 7.37  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 175.708 148.917 127.483 1.00 9.93  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 177.675 151.137 129.067 1.00 6.13  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 178.393 152.334 128.746 1.00 12.62 ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 178.540 149.929 128.747 1.00 8.32  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 175.096 149.481 129.577 1.00 4.17  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 174.392 148.218 129.783 1.00 2.36  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 173.240 148.056 128.799 1.00 4.11  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 173.034 146.969 128.244 1.00 8.34  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 173.880 148.125 131.219 1.00 3.67  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 174.910 147.651 132.198 1.00 6.10  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 175.597 146.470 131.980 1.00 10.66 ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 175.184 148.380 133.339 1.00 1.17  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 176.543 146.028 132.880 1.00 9.84  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 176.127 147.943 134.240 1.00 6.52  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 176.809 146.766 134.011 1.00 10.52 ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 172.475 149.126 128.572 1.00 6.31  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 171.305 149.025 127.704 1.00 2.80  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 171.697 148.738 126.258 1.00 4.81  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 171.084 147.885 125.607 1.00 7.50  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 170.476 150.304 127.801 1.00 3.65  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 169.566 150.363 129.027 1.00 1.51  ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 169.238 151.796 129.387 1.00 0.00  ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 168.297 149.565 128.789 1.00 3.86  ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 172.709 149.436 125.733 1.00 5.40  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 173.172 149.136 124.382 1.00 3.30  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 173.868 147.785 124.295 1.00 6.63  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 173.872 147.178 123.221 1.00 10.65 ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 174.112 150.226 123.857 1.00 4.90  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 173.731 151.649 124.221 1.00 9.02  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 172.417 152.084 123.609 1.00 16.32 ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 172.165 151.745 122.434 1.00 14.10 ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 171.636 152.769 124.303 1.00 13.32 ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 174.462 147.303 125.389 1.00 9.91  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 175.067 145.977 125.359 1.00 8.56  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 174.008 144.884 125.299 1.00 8.13  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 174.180 143.884 124.592 1.00 10.76 ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 175.963 145.786 126.580 1.00 7.33  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 177.255 145.049 126.294 1.00 9.34  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 178.043 144.823 127.574 1.00 14.06 ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 177.219 144.226 128.618 1.00 13.91 ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 176.870 142.947 128.660 1.00 13.02 ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 177.268 142.092 127.733 1.00 11.31 ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 176.106 142.515 129.658 1.00 10.96 ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 172.904 145.056 126.024 1.00 6.60  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 171.922 143.986 126.171 1.00 8.92  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 170.810 144.052 125.129 1.00 9.68  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 170.473 143.033 124.518 1.00 11.55 ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 171.321 144.022 127.578 1.00 7.44  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 172.200 143.456 128.692 1.00 7.74  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 171.545 143.662 130.044 1.00 8.29  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 172.483 141.984 128.450 1.00 10.79 ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 170.228 145.230 124.915 1.00 9.80  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 169.037 145.369 124.077 1.00 4.81  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 169.459 145.720 122.652 1.00 10.20 ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 169.361 146.861 122.204 1.00 14.36 ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 168.091 146.411 124.662 1.00 2.54  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 167.510 146.018 125.989 1.00 9.26  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 168.163 146.336 127.167 1.00 8.97  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 166.316 145.324 126.057 1.00 9.25  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 167.634 145.974 128.387 1.00 5.82  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 165.783 144.959 127.276 1.00 4.63  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 166.443 145.285 128.441 1.00 6.77  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 169.932 144.704 121.934 1.00 11.37 ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 170.272 144.829 120.525 1.00 9.68  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 169.804 143.580 119.793 1.00 11.88 ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 169.345 142.611 120.401 1.00 14.48 ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 171.776 145.037 120.310 1.00 11.87 ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 172.512 144.133 121.141 1.00 17.24 ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 172.173 146.467 120.633 1.00 11.54 ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 169.922 143.614 118.465 1.00 14.96 ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 169.545 142.456 117.661 1.00 18.06 ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 170.464 141.273 117.932 1.00 21.27 ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 170.023 140.118 117.917 1.00 23.05 ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 169.564 142.813 116.177 1.00 19.69 ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 168.864 144.047 115.969 1.00 20.07 ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 168.900 141.718 115.363 1.00 19.72 ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 171.746 141.542 118.192 1.00 19.29 ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 172.703 140.466 118.412 1.00 18.94 ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 172.393 139.670 119.671 1.00 18.80 ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 172.946 138.579 119.852 1.00 24.38 ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 174.122 141.032 118.484 1.00 19.57 ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 174.545 141.872 117.277 1.00 21.29 ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 174.961 141.042 116.058 1.00 22.12 ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 173.892 140.202 115.531 1.00 26.62 ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 174.018 139.396 114.485 1.00 28.18 ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 175.159 139.296 113.823 1.00 24.75 ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 172.973 138.672 114.093 1.00 23.61 ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 171.528 140.186 120.546 1.00 16.32 ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 171.072 139.416 121.694 1.00 17.33 ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 170.244 138.204 121.292 1.00 18.61 ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 170.033 137.317 122.123 1.00 21.90 ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 170.262 140.304 122.636 1.00 16.72 ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 168.984 140.582 122.094 1.00 20.68 ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 169.772 138.150 120.048 1.00 16.55 ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 169.047 136.998 119.535 1.00 20.30 ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 169.961 135.992 118.848 1.00 24.39 ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 169.471 134.998 118.303 1.00 20.45 ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 167.949 137.451 118.572 1.00 17.29 ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 166.695 137.899 119.261 1.00 17.79 ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 166.648 139.111 119.925 1.00 18.20 ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 165.569 137.100 119.255 1.00 19.42 ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 165.496 139.519 120.564 1.00 15.83 ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 164.417 137.505 119.892 1.00 19.35 ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 164.380 138.715 120.547 1.00 16.90 ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 171.269 136.229 118.861 1.00 28.27 ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 172.213 135.274 118.307 1.00 26.84 ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 172.338 134.057 119.217 1.00 33.41 ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 171.945 134.073 120.385 1.00 30.35 ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 173.587 135.918 118.122 1.00 25.20 ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 173.654 136.815 116.908 1.00 27.89 ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 172.741 136.741 116.058 1.00 28.78 ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 174.626 137.590 116.802 1.00 27.45 ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 172.902 132.987 118.659 1.00 41.66 ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 173.170 131.788 119.441 1.00 40.29 ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 174.456 131.893 120.248 1.00 40.43 ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 174.692 131.053 121.124 1.00 43.27 ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 173.233 130.566 118.523 1.00 39.76 ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 174.344 130.648 117.647 1.00 41.49 ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 175.286 132.900 119.979 1.00 33.81 ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 176.578 133.055 120.634 1.00 35.55 ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 176.660 134.323 121.481 1.00 36.85 ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 177.752 134.710 121.904 1.00 35.21 ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 177.694 133.020 119.585 1.00 38.41 ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 177.621 134.121 118.524 1.00 40.07 ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 178.336 135.401 118.921 1.00 42.42 ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 179.221 135.347 119.800 1.00 39.35 ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 178.011 136.463 118.352 1.00 41.46 ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 175.525 134.962 121.755 1.00 30.27 ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 175.528 136.193 122.535 1.00 25.13 ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 176.027 135.936 123.952 1.00 23.57 ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 175.664 134.943 124.586 1.00 25.66 ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 174.125 136.798 122.573 1.00 23.23 ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 174.061 138.136 123.251 1.00 23.14 ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 174.730 139.227 122.726 1.00 24.06 ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 173.333 138.301 124.415 1.00 22.15 ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 174.672 140.457 123.349 1.00 22.63 ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 173.272 139.529 125.042 1.00 23.01 ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 173.941 140.608 124.509 1.00 22.07 ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 176.865 136.843 124.448 1.00 24.72 ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 177.477 136.727 125.768 1.00 24.41 ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 176.823 137.733 126.705 1.00 22.50 ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 177.005 138.944 126.549 1.00 25.62 ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 178.983 136.963 125.693 1.00 23.91 ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 179.650 136.408 124.449 1.00 27.71 ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 179.695 134.894 124.480 1.00 27.88 ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 180.620 134.352 123.403 1.00 27.73 ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 182.013 134.851 123.568 1.00 26.96 ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 176.059 137.229 127.678 1.00 16.69 ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 175.508 138.107 128.704 1.00 16.60 ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 176.614 138.715 129.557 1.00 20.63 ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 176.565 139.903 129.896 1.00 24.00 ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 174.516 137.338 129.574 1.00 14.34 ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 173.191 136.974 128.907 1.00 14.51 ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 172.362 136.093 129.820 1.00 19.02 ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 172.425 138.229 128.535 1.00 17.17 ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 177.616 137.916 129.914 1.00 21.63 ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 178.794 138.391 130.619 1.00 22.83 ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 180.022 137.750 129.993 1.00 28.26 ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 179.955 136.636 129.470 1.00 28.96 ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 178.732 138.071 132.117 1.00 20.38 ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 181.145 138.462 130.045 1.00 42.09 ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 182.377 138.031 129.399 1.00 43.35 ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 183.483 137.887 130.432 1.00 44.31 ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 183.733 138.813 131.212 1.00 45.27 ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 182.798 139.023 128.311 1.00 43.32 ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 181.925 138.820 126.741 1.00 50.29 ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 184.146 136.730 130.425 1.00 47.00 ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 185.297 136.454 131.285 1.00 46.74 ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 184.953 136.679 132.759 1.00 45.29 ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 185.509 137.545 133.435 1.00 47.06 ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 186.507 137.295 130.863 1.00 47.62 ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 187.470 136.582 129.924 1.00 48.40 ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 186.833 136.297 128.575 1.00 48.71 ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 186.532 137.583 127.826 1.00 47.41 ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 185.861 137.322 126.522 1.00 47.46 ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 184.007 135.875 133.247 1.00 37.91 ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 183.577 135.998 134.636 1.00 35.65 ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 184.683 135.554 135.586 1.00 38.83 ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 184.864 136.134 136.662 1.00 38.18 ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 182.274 135.212 134.864 1.00 32.76 ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 181.108 135.924 134.200 1.00 32.36 ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 182.406 133.804 134.324 1.00 36.65 ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 185.436 134.520 135.214 1.00 48.12 ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 186.578 134.069 136.003 1.00 49.70 ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 187.827 133.930 135.141 1.00 51.64 ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 188.686 133.086 135.408 1.00 50.76 ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 186.265 132.755 136.719 1.00 48.61 ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 185.656 131.715 135.800 1.00 50.21 ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 186.274 131.399 134.762 1.00 50.30 ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 184.561 131.209 136.121 1.00 50.10 ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 187.941 134.752 134.099 1.00 54.60 ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 189.092 134.763 133.230 1.00 55.98 ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 188.989 133.857 132.019 1.00 57.08 ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 189.554 134.179 130.968 1.00 56.42 ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 188.284 132.733 132.136 1.00 63.52 ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 188.187 131.773 131.039 1.00 64.50 ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 186.769 131.657 130.494 1.00 65.05 ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 186.557 131.886 129.299 1.00 63.32 ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 188.700 130.402 131.497 1.00 62.54 ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 190.031 130.451 132.182 1.00 65.03 ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 190.186 130.882 133.481 1.00 64.78 ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 191.270 130.126 131.743 1.00 65.65 ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 191.462 130.819 133.815 1.00 65.24 ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 192.142 130.362 132.778 1.00 65.88 ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 185.793 131.316 131.327 1.00 54.33 ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 184.448 131.058 130.839 1.00 50.39 ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 183.612 132.333 130.851 1.00 48.96 ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 183.992 133.354 131.427 1.00 48.58 ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 183.766 129.971 131.672 1.00 49.52 ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 183.739 130.240 133.165 1.00 49.99 ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 182.549 129.558 133.821 1.00 51.42 ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 181.318 130.449 133.816 1.00 51.05 ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 180.249 129.932 134.714 1.00 48.90 ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 182.460 132.260 130.190 1.00 41.91 ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 181.560 133.395 130.060 1.00 38.76 ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 180.121 132.901 130.093 1.00 35.72 ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 179.836 131.737 129.807 1.00 37.25 ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 181.838 134.181 128.773 1.00 37.52 ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 181.888 133.294 127.545 1.00 40.00 ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 181.762 132.060 127.693 1.00 38.26 ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 182.060 133.831 126.432 1.00 42.51 ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 179.213 133.806 130.448 1.00 25.35 ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 177.799 133.466 130.566 1.00 22.28 ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 177.154 133.553 129.189 1.00 24.75 ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 177.190 134.602 128.539 1.00 29.65 ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 177.093 134.386 131.570 1.00 19.89 ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 177.725 134.242 132.955 1.00 20.33 ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 175.612 134.070 131.627 1.00 21.18 ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 177.119 135.143 134.000 1.00 20.67 ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 176.559 132.449 128.747 1.00 24.97 ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 175.988 132.354 127.412 1.00 22.89 ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 174.514 132.736 127.415 1.00 22.61 ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 173.786 132.495 128.382 1.00 24.45 ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 176.145 130.938 126.858 1.00 24.65 ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 177.576 130.532 126.561 1.00 25.19 ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 178.141 131.240 125.350 1.00 29.34 ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 179.158 131.925 125.438 1.00 30.66 ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 177.481 131.081 124.209 1.00 27.31 ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 174.083 133.338 126.318 1.00 17.87 ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 172.668 133.614 126.117 1.00 16.57 ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 171.917 132.304 125.917 1.00 21.57 ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 172.370 131.448 125.146 1.00 23.09 ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 172.482 134.525 124.907 1.00 22.93 ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 171.088 135.099 124.736 1.00 20.68 ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 170.626 136.274 126.015 1.00 21.03 ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 168.845 136.163 125.918 1.00 18.95 ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 170.785 132.097 126.589 1.00 23.86 ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 170.017 130.865 126.374 1.00 19.01 ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 169.531 130.764 124.937 1.00 22.83 ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 169.182 131.763 124.305 1.00 27.03 ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 168.847 130.994 127.355 1.00 16.38 ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 169.266 132.030 128.335 1.00 19.26 ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 170.174 132.963 127.609 1.00 21.63 ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 169.511 129.539 124.421 1.00 28.74 ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 169.080 129.280 123.057 1.00 31.23 ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 167.584 129.020 122.946 1.00 33.49 ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 167.084 128.832 121.832 1.00 33.16 ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 169.853 128.092 122.476 1.00 33.76 ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 171.254 128.471 122.037 1.00 37.23 ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 171.419 129.554 121.439 1.00 37.03 ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 172.191 127.683 122.291 1.00 35.42 ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 166.862 129.005 124.064 1.00 30.69 ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 165.441 128.743 124.018 1.00 29.65 ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 164.646 129.925 123.495 1.00 29.78 ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 165.130 131.052 123.394 1.00 28.41 ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 163.389 129.647 123.149 1.00 31.87 ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 162.460 130.653 122.658 1.00 32.42 ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 161.183 130.704 123.488 1.00 34.45 ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 160.231 131.382 123.109 1.00 35.89 ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 162.130 130.432 121.169 1.00 31.72 ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 161.444 129.080 120.972 1.00 30.88 ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 163.389 130.523 120.322 1.00 34.18 ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 160.880 128.882 119.585 1.00 34.55 ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 161.147 129.997 124.614 1.00 31.87 ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 159.976 129.949 125.474 1.00 27.91 ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 160.380 130.306 126.897 1.00 28.54 ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 161.536 130.151 127.293 1.00 33.08 ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 159.315 128.564 125.444 1.00 30.73 ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 158.924 128.094 124.053 1.00 32.17 ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 158.957 126.575 123.947 1.00 31.63 ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 158.417 125.917 125.132 1.00 34.92 ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 157.134 125.899 125.466 1.00 33.47 ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 156.213 126.484 124.716 1.00 31.22 ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 156.763 125.273 126.579 1.00 32.33 ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 159.400 130.790 127.665 1.00 25.01 ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 159.674 131.230 129.030 1.00 23.52 ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 160.203 130.089 129.887 1.00 26.05 ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 161.072 130.297 130.743 1.00 30.78 ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 158.408 131.821 129.651 1.00 25.30 ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 158.456 131.927 131.166 1.00 24.33 ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 157.072 132.081 131.764 1.00 29.42 ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 157.122 132.186 133.217 1.00 29.57 ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 157.257 131.155 134.037 1.00 31.00 ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 157.355 129.916 133.582 1.00 29.58 ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 157.295 131.369 135.350 1.00 27.51 ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 159.692 128.875 129.670 1.00 30.69 ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 160.116 127.736 130.475 1.00 27.86 ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 161.601 127.454 130.296 1.00 28.76 ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 162.304 127.147 131.267 1.00 28.56 ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 159.287 126.503 130.113 1.00 27.89 ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 157.871 126.516 130.674 1.00 32.17 ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 156.952 127.469 129.931 1.00 37.41 ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 157.124 127.630 128.705 1.00 34.05 ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 156.057 128.058 130.574 1.00 34.54 ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 162.100 127.553 129.062 1.00 29.55 ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 163.520 127.321 128.818 1.00 26.99 ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 164.382 128.369 129.514 1.00 26.98 ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 165.437 128.043 130.068 1.00 28.99 ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 163.797 127.305 127.314 1.00 24.16 ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 162.815 126.460 126.521 1.00 27.84 ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 163.231 126.282 125.075 1.00 34.03 ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 164.295 125.676 124.832 1.00 33.81 ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 162.497 126.749 124.181 1.00 31.97 ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 163.952 129.631 129.496 1.00 22.69 ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 164.707 130.675 130.185 1.00 19.99 ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 164.692 130.467 131.695 1.00 20.86 ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 165.710 130.673 132.366 1.00 25.74 ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 164.155 132.050 129.819 1.00 18.94 ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 164.377 132.428 128.385 1.00 19.90 ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 165.658 132.580 127.885 1.00 20.15 ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 163.307 132.632 127.534 1.00 18.86 ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 165.867 132.925 126.567 1.00 20.26 ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 163.509 132.976 126.215 1.00 17.14 ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 164.791 133.124 125.730 1.00 19.79 ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 163.548 130.058 132.248 1.00 17.16 ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 163.479 129.778 133.680 1.00 19.79 ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 164.402 128.620 134.040 1.00 22.31 ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 165.108 128.661 135.055 1.00 21.53 ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 162.023 129.501 134.101 1.00 22.80 ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 161.972 128.985 135.528 1.00 19.98 ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 161.188 130.761 133.964 1.00 22.73 ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 164.413 127.570 133.213 1.00 22.16 ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 165.325 126.456 133.449 1.00 21.08 ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 166.777 126.909 133.379 1.00 21.60 ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 167.603 126.499 134.202 1.00 25.46 ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 165.063 125.337 132.442 1.00 21.02 ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 163.732 124.631 132.635 1.00 26.36 ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 163.540 123.475 131.674 1.00 28.40 ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 163.370 123.674 130.471 1.00 26.40 ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 163.565 122.257 132.201 1.00 26.95 ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 167.107 127.764 132.411 1.00 19.30 ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 168.465 128.289 132.314 1.00 16.54 ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 168.845 129.058 133.571 1.00 15.66 ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 169.974 128.944 134.062 1.00 16.35 ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 168.593 129.181 131.079 1.00 17.46 ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 169.965 129.739 130.870 1.00 22.08 ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 170.957 129.206 130.103 1.00 21.42 ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 170.495 130.949 131.426 1.00 21.47 ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 172.073 130.003 130.150 1.00 22.86 ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 171.815 131.081 130.955 1.00 19.91 ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 169.983 131.932 132.278 1.00 16.57 ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 172.629 132.152 131.308 1.00 15.52 ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 170.793 132.995 132.628 1.00 15.41 ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 172.101 133.097 132.142 1.00 14.78 ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 167.914 129.853 134.103 1.00 16.07 ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 168.174 130.574 135.347 1.00 17.63 ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 168.405 129.598 136.493 1.00 18.74 ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 169.309 129.788 137.317 1.00 16.74 ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 167.020 131.546 135.656 1.00 13.13 ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 167.228 132.197 137.012 1.00 8.70  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 166.915 132.601 134.577 1.00 14.75 ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 167.599 128.536 136.564 1.00 21.61 ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 167.720 127.585 137.666 1.00 18.32 ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 169.034 126.813 137.620 1.00 20.37 ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 169.511 126.351 138.660 1.00 22.02 ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 166.539 126.615 137.656 1.00 16.82 ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 165.201 127.268 137.946 1.00 19.36 ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 164.740 127.035 139.369 1.00 27.76 ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 165.548 126.547 140.186 1.00 26.80 ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 163.567 127.342 139.673 1.00 29.88 ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 169.631 126.664 136.440 1.00 20.31 ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 170.904 125.970 136.294 1.00 16.54 ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 172.107 126.893 136.439 1.00 18.11 ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 173.233 126.467 136.165 1.00 19.72 ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 170.968 125.247 134.945 1.00 16.93 ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 170.426 123.815 134.879 1.00 19.22 ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 168.908 123.770 134.886 1.00 19.36 ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 170.973 123.109 133.650 1.00 21.43 ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 171.901 128.140 136.848 1.00 17.60 ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 173.023 129.038 137.067 1.00 18.56 ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 173.879 128.533 138.228 1.00 20.21 ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 173.342 128.076 139.243 1.00 19.60 ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 172.534 130.455 137.359 1.00 17.59 ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 172.273 131.356 136.151 1.00 12.22 ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 172.002 132.781 136.597 1.00 14.99 ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 173.442 131.309 135.184 1.00 15.66 ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 175.202 128.590 138.106 1.00 20.83 ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 176.063 128.126 139.198 1.00 16.82 ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 175.938 129.007 140.428 1.00 19.09 ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 175.624 130.197 140.345 1.00 21.59 ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 177.474 128.208 138.601 1.00 19.59 ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 177.272 128.279 137.119 1.00 21.71 ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 175.977 128.993 136.923 1.00 19.24 ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 176.187 128.399 141.589 1.00 26.14 ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 176.195 129.143 142.844 1.00 29.66 ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 177.432 130.015 142.997 1.00 28.89 ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 177.477 130.842 143.916 1.00 29.11 ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 176.096 128.177 144.026 1.00 29.61 ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 175.672 128.865 145.310 1.00 35.04 ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 175.068 129.956 145.229 1.00 34.29 ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 175.947 128.319 146.398 1.00 36.53 ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 178.426 129.859 142.123 1.00 22.30 ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 179.675 130.616 142.213 1.00 21.42 ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 179.506 131.939 141.473 1.00 19.16 ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 179.991 132.135 140.357 1.00 19.49 ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 180.833 129.802 141.652 1.00 24.57 ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 180.594 129.520 140.268 1.00 23.51 ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 180.979 128.493 142.410 1.00 23.08 ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 178.798 132.865 142.114 1.00 13.59 ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 178.624 134.202 141.568 1.00 8.94  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 179.726 135.120 142.069 1.00 12.32 ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 180.077 135.108 143.252 1.00 18.49 ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 177.261 134.784 141.944 1.00 11.86 ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 176.918 136.045 141.162 1.00 11.90 ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 176.070 137.018 141.950 1.00 9.74  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 174.974 136.685 142.390 1.00 16.04 ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 176.574 138.233 142.127 1.00 4.08  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 180.265 135.919 141.162 1.00 9.99  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 181.322 136.876 141.437 1.00 11.34 ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 180.914 138.227 140.873 1.00 12.09 ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 180.052 138.304 139.992 1.00 16.50 ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 182.652 136.422 140.816 1.00 12.38 ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 182.428 135.969 139.476 1.00 13.71 ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 183.260 135.293 141.631 1.00 11.24 ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 181.502 139.317 141.372 1.00 7.75  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 181.161 140.640 140.822 1.00 8.50  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 181.478 140.786 139.344 1.00 5.97  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 180.937 141.692 138.700 1.00 10.81 ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 181.994 141.611 141.675 1.00 7.38  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 182.950 140.766 142.445 1.00 9.77  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 182.330 139.422 142.584 1.00 7.13  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 182.334 139.929 138.782 1.00 3.94  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 182.581 139.962 137.346 1.00 6.15  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 181.351 139.566 136.540 1.00 11.97 ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 181.307 139.832 135.334 1.00 14.83 ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 183.750 139.050 136.989 1.00 11.36 ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 183.597 137.774 137.585 1.00 17.25 ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 180.363 138.927 137.171 1.00 10.45 ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 179.075 138.729 136.514 1.00 7.04  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 178.429 140.060 136.169 1.00 10.70 ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 177.707 140.165 135.171 1.00 14.02 ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 178.138 137.920 137.412 1.00 4.54  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 178.460 136.465 137.512 1.00 10.07 ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 179.695 135.891 137.467 1.00 11.94 ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 177.525 135.393 137.684 1.00 12.40 ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 179.588 134.528 137.596 1.00 14.36 ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 178.267 134.197 137.732 1.00 13.17 ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 176.135 135.331 137.802 1.00 10.46 ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 177.662 132.953 137.891 1.00 13.10 ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 175.538 134.095 137.959 1.00 10.07 ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 176.300 132.924 138.003 1.00 12.07 ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 178.677 141.083 136.981 1.00 8.47  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 178.083 142.399 136.825 1.00 1.94  ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 178.950 143.343 136.005 1.00 6.00  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 178.586 144.511 135.842 1.00 11.14 ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 177.829 143.013 138.203 1.00 2.60  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 177.323 142.042 139.268 1.00 1.63  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 177.248 142.724 140.620 1.00 5.12  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 175.979 141.469 138.879 1.00 5.93  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 180.083 142.869 135.495 1.00 5.54  ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 181.047 143.719 134.837 1.00 4.83  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 182.057 144.356 135.763 1.00 4.61  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 183.002 144.990 135.280 1.00 10.88 ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 181.892 144.203 137.071 1.00 2.85  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 182.787 144.779 138.059 1.00 1.21  ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 184.050 143.935 138.202 1.00 5.65  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 184.079 142.770 137.801 1.00 6.95  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 182.073 144.885 139.401 1.00 1.75  ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 181.174 146.102 139.600 1.00 2.62  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 180.104 145.802 140.626 1.00 3.20  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 181.995 147.304 140.020 1.00 9.50  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 185.119 144.507 138.753 1.00 10.48 ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 186.296 143.692 139.075 1.00 7.94  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 185.978 142.668 140.154 1.00 8.33  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 185.131 142.885 141.023 1.00 7.84  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 187.320 144.721 139.565 1.00 7.50  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 186.510 145.896 139.987 1.00 5.74  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 185.343 145.931 139.054 1.00 9.36  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 186.679 141.535 140.087 1.00 8.20  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 186.392 140.421 140.984 1.00 9.31  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 186.718 140.727 142.438 1.00 11.68 ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 186.200 140.046 143.329 1.00 16.84 ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 187.157 139.177 140.534 1.00 11.23 ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 186.301 138.231 139.722 1.00 12.96 ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 185.076 138.275 139.791 1.00 9.54  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 186.944 137.368 138.946 1.00 14.00 ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 187.557 141.722 142.706 1.00 9.52  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 187.932 142.061 144.072 1.00 10.84 ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 186.995 143.074 144.713 1.00 12.94 ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 187.156 143.376 145.902 1.00 18.18 ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 189.370 142.590 144.107 1.00 12.48 ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 189.615 143.690 143.094 1.00 15.58 ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 188.681 144.218 142.495 1.00 20.57 ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 190.879 144.036 142.895 1.00 18.24 ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 186.013 143.587 143.967 1.00 10.50 ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 185.135 144.627 144.499 1.00 12.86 ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 184.356 144.145 145.714 1.00 14.39 ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 183.958 144.955 146.558 1.00 14.85 ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 184.177 145.109 143.413 1.00 9.43  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 184.128 142.838 145.824 1.00 15.27 ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 183.453 142.280 146.985 1.00 14.35 ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 184.409 141.916 148.111 1.00 15.53 ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 183.979 141.871 149.271 1.00 19.64 ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 182.659 141.032 146.586 1.00 13.47 ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 183.529 139.866 146.149 1.00 12.03 ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 182.738 138.594 145.934 1.00 19.26 ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 181.501 138.627 146.101 1.00 22.21 ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 183.353 137.561 145.598 1.00 19.45 ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 185.688 141.690 147.793 1.00 18.24 ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 186.632 141.101 148.741 1.00 17.91 ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 186.554 141.772 150.105 1.00 15.68 ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 186.160 141.146 151.098 1.00 20.10 ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 188.052 141.191 148.178 1.00 20.53 ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 189.144 140.917 149.201 1.00 20.58 ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 190.511 140.855 148.545 1.00 21.16 ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 190.606 139.768 147.580 1.00 24.79 ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 191.523 138.811 147.621 1.00 24.55 ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 192.449 138.778 148.565 1.00 19.83 ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 191.514 137.863 146.686 1.00 24.47 ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 186.872 143.067 150.157 1.00 14.56 ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 186.877 143.784 151.429 1.00 17.60 ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 185.528 143.641 152.113 1.00 18.70 ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 185.445 143.250 153.287 1.00 21.21 ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 187.247 145.262 151.209 1.00 21.14 ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 186.841 146.098 152.414 1.00 19.17 ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 188.735 145.401 150.932 1.00 21.21 ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 184.447 143.887 151.367 1.00 19.76 ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 183.107 143.736 151.921 1.00 16.11 ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 182.943 142.365 152.555 1.00 12.76 ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 182.586 142.249 153.734 1.00 18.07 ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 182.062 143.953 150.827 1.00 17.59 ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 180.595 143.892 151.255 1.00 20.01 ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 180.278 144.996 152.251 1.00 19.66 ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 179.680 143.973 150.044 1.00 19.51 ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 183.281 141.313 151.801 1.00 11.88 ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 183.149 139.959 152.321 1.00 13.91 ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 183.889 139.825 153.640 1.00 16.18 ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 183.327 139.350 154.637 1.00 22.74 ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 183.673 138.948 151.301 1.00 14.27 ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 182.739 138.577 150.151 1.00 12.51 ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 183.314 137.421 149.352 1.00 14.05 ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 181.356 138.231 150.672 1.00 15.45 ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 185.134 140.313 153.681 1.00 15.93 ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 185.917 140.225 154.906 1.00 14.81 ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 185.146 140.822 156.071 1.00 14.30 ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 184.929 140.159 157.093 1.00 18.27 ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 187.259 140.935 154.729 1.00 16.50 ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 187.951 140.380 153.603 1.00 16.13 ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 188.116 140.768 155.972 1.00 16.63 ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 184.649 142.050 155.891 1.00 11.46 ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 183.899 142.701 156.958 1.00 13.72 ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 182.747 141.818 157.403 1.00 13.45 ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 182.592 141.532 158.598 1.00 15.30 ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 183.387 144.063 156.487 1.00 16.19 ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 184.494 144.874 156.078 1.00 18.92 ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 182.642 144.763 157.609 1.00 15.38 ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 181.975 141.309 156.439 1.00 13.07 ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 180.834 140.474 156.782 1.00 10.09 ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 181.275 139.284 157.616 1.00 12.82 ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 180.676 138.994 158.660 1.00 18.31 ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 180.116 140.015 155.515 1.00 11.12 ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 179.186 141.057 154.920 1.00 15.51 ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 178.363 140.512 153.772 1.00 19.39 ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 178.861 140.343 152.660 1.00 21.62 ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 177.091 140.235 154.036 1.00 17.30 ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 182.367 138.629 157.213 1.00 13.15 ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 182.850 137.499 157.985 1.00 12.02 ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 183.134 137.890 159.419 1.00 15.18 ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 182.659 137.242 160.358 1.00 15.39 ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 183.839 139.009 159.605 1.00 15.13 ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 184.126 139.475 160.956 1.00 13.50 ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 182.827 139.705 161.707 1.00 15.75 ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 182.671 139.271 162.857 1.00 18.44 ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 184.993 140.745 160.913 1.00 12.83 ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 185.122 141.345 162.301 1.00 14.09 ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 186.362 140.429 160.335 1.00 14.96 ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 181.848 140.328 161.042 1.00 13.66 ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 180.565 140.569 161.686 1.00 10.39 ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 179.965 139.267 162.188 1.00 10.98 ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 179.508 139.190 163.337 1.00 17.15 ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 179.610 141.267 160.720 1.00 15.22 ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 179.566 142.768 160.929 1.00 21.78 ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 180.247 143.262 161.851 1.00 22.91 ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 178.847 143.454 160.170 1.00 20.95 ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 180.020 138.213 161.367 1.00 9.69  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 179.475 136.931 161.796 1.00 10.31 ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 180.123 136.492 163.098 1.00 13.52 ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 179.430 136.150 164.065 1.00 15.48 ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 179.675 135.877 160.706 1.00 9.27  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 179.353 134.462 161.158 1.00 11.43 ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 179.945 133.195 160.023 1.00 27.00 ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 181.706 133.511 160.047 1.00 16.30 ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 181.455 136.577 163.165 1.00 17.73 ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 182.159 136.207 164.387 1.00 15.86 ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 181.612 137.004 165.559 1.00 11.74 ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 181.239 136.439 166.597 1.00 15.27 ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 183.675 136.415 164.221 1.00 17.72 ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 184.240 135.425 163.204 1.00 13.29 ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 184.381 136.269 165.557 1.00 19.80 ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 183.786 134.008 163.428 1.00 15.57 ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 181.488 138.323 165.382 1.00 9.46  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 180.941 139.158 166.443 1.00 11.57 ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 179.576 138.644 166.873 1.00 16.17 ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 179.329 138.426 168.065 1.00 20.29 ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 180.854 140.611 165.977 1.00 12.52 ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 182.097 141.055 165.467 1.00 19.69 ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 178.698 138.384 165.903 1.00 16.87 ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 177.386 137.849 166.237 1.00 12.08 ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 177.526 136.500 166.927 1.00 13.72 ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 176.913 136.257 167.973 1.00 17.28 ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 176.529 137.740 164.977 1.00 9.02  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 176.300 139.071 164.280 1.00 10.22 ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 175.645 138.881 162.924 1.00 11.04 ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 175.716 140.153 162.096 1.00 11.39 ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 175.214 141.333 162.849 1.00 12.41 ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 178.386 135.632 166.386 1.00 13.19 ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 178.588 134.327 167.001 1.00 10.95 ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 179.212 134.450 168.380 1.00 17.26 ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 179.109 133.515 169.181 1.00 23.32 ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 179.455 133.450 166.097 1.00 12.44 ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 178.691 132.806 164.954 1.00 10.49 ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 179.513 131.341 164.306 1.00 22.21 ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 178.882 130.085 165.413 1.00 15.85 ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 179.849 135.581 168.676 1.00 18.03 ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 180.369 135.823 170.010 1.00 16.85 ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 179.387 136.583 170.886 1.00 17.24 ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 179.496 136.520 172.117 1.00 22.29 ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 181.689 136.592 169.932 1.00 15.14 ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 182.626 136.463 171.132 1.00 17.59 ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 183.116 135.034 171.261 1.00 19.92 ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 183.793 137.423 170.998 1.00 21.04 ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 178.431 137.291 170.286 1.00 16.58 ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 177.486 138.075 171.070 1.00 17.80 ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 176.375 137.220 171.664 1.00 17.98 ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 175.615 137.713 172.506 1.00 19.91 ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 176.884 139.186 170.208 1.00 17.50 ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 176.436 140.410 170.988 1.00 15.15 ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 175.886 141.483 170.065 1.00 17.93 ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 176.805 141.716 168.875 1.00 19.68 ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 176.146 142.527 167.816 1.00 17.89 ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 176.265 135.960 171.249 1.00 15.43 ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 175.209 135.070 171.709 1.00 16.59 ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 175.727 133.946 172.597 1.00 21.35 ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 174.981 133.006 172.888 1.00 24.24 ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 174.457 134.491 170.510 1.00 16.18 ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 173.826 135.546 169.618 1.00 14.99 ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 173.069 134.839 168.148 1.00 21.68 ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 171.906 133.704 168.898 1.00 13.17 ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 176.981 134.017 173.033 1.00 27.27 ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 177.547 132.986 173.895 1.00 25.97 ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 177.223 133.256 175.361 1.00 25.51 ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 176.543 134.229 175.689 1.00 23.25 ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 179.062 132.896 173.702 1.00 20.89 ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 179.485 132.451 172.313 1.00 23.73 ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 178.967 131.071 171.961 1.00 29.66 ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 178.081 130.924 171.120 1.00 29.13 ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 179.520 130.050 172.603 1.00 27.41 ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 190.947 163.072 187.222 1.00 52.12 ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 190.214 161.941 186.657 1.00 54.08 ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 190.965 161.266 185.513 1.00 54.90 ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 191.859 161.874 184.925 1.00 54.04 ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 188.920 162.590 186.159 1.00 54.29 ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 188.775 163.880 186.992 1.00 55.26 ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 190.020 164.033 187.839 1.00 51.84 ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 190.604 160.018 185.209 1.00 51.93 ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 191.280 159.290 184.141 1.00 52.01 ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 190.998 159.917 182.782 1.00 54.61 ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 191.918 160.155 181.988 1.00 51.08 ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 190.853 157.822 184.157 1.00 49.15 ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 189.723 160.199 182.496 1.00 59.99 ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 189.379 160.793 181.209 1.00 58.71 ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 189.944 162.200 181.079 1.00 57.16 ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 190.319 162.612 179.977 1.00 56.44 ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 187.861 160.790 181.007 1.00 55.83 ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 187.106 161.816 181.805 1.00 58.52 ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 186.451 161.614 182.986 1.00 59.24 ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 186.898 163.193 181.464 1.00 59.74 ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 185.865 162.782 183.409 1.00 59.85 ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 186.124 163.766 182.492 1.00 59.85 ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 187.299 163.998 180.394 1.00 58.50 ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 185.744 165.106 182.481 1.00 57.99 ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 186.921 165.328 180.386 1.00 58.04 ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 186.150 165.867 181.421 1.00 57.24 ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 190.022 162.945 182.184 1.00 56.21 ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 190.622 164.274 182.139 1.00 57.76 ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 192.085 164.198 181.717 1.00 57.88 ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 192.535 164.958 180.853 1.00 54.86 ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 190.488 164.954 183.501 1.00 57.18 ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 190.879 166.422 183.502 1.00 56.53 ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 189.891 167.407 184.644 1.00 64.06 ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 188.322 167.448 183.783 1.00 57.86 ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 192.842 163.272 182.311 1.00 56.53 ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 194.251 163.124 181.956 1.00 55.29 ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 194.413 162.631 180.524 1.00 55.36 ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 195.298 163.100 179.793 1.00 54.55 ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 194.943 162.173 182.933 1.00 54.50 ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 195.607 162.856 184.124 1.00 54.23 ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 194.609 163.650 184.954 1.00 56.20 ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 195.220 164.230 186.143 1.00 57.85 ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 194.558 164.918 187.064 1.00 56.84 ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 193.259 165.135 186.963 1.00 56.30 ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 195.220 165.399 188.114 1.00 53.71 ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 193.571 161.682 180.104 1.00 49.69 ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 193.640 161.189 178.733 1.00 48.94 ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 193.365 162.306 177.733 1.00 48.40 ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 194.079 162.445 176.731 1.00 45.45 ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 192.649 160.042 178.536 1.00 48.93 ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 192.834 159.067 179.569 1.00 48.22 ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 192.859 159.382 177.181 1.00 48.77 ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 192.341 163.121 177.996 1.00 47.79 ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 192.027 164.233 177.108 1.00 45.49 ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 193.130 165.282 177.126 1.00 44.99 ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 193.424 165.890 176.093 1.00 44.40 ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 190.686 164.851 177.498 1.00 44.00 ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 190.130 165.916 176.550 1.00 45.62 ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 189.754 165.297 175.215 1.00 43.50 ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 188.933 166.608 177.177 1.00 46.08 ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 193.751 165.510 178.285 1.00 44.10 ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 194.869 166.445 178.352 1.00 44.28 ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 196.016 165.986 177.464 1.00 45.52 ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 196.560 166.770 176.675 1.00 47.35 ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 195.340 166.596 179.799 1.00 44.96 ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 196.420 167.617 179.981 1.00 46.14 ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 197.708 167.428 179.532 1.00 44.83 ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 196.402 168.837 180.567 1.00 46.74 ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 198.439 168.487 179.830 1.00 45.06 ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 197.669 169.357 180.460 1.00 48.04 ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 196.396 164.711 177.577 1.00 44.33 ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 197.481 164.193 176.749 1.00 44.79 ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 197.119 164.245 175.271 1.00 44.90 ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 197.947 164.627 174.434 1.00 44.40 ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 197.834 162.765 177.165 1.00 45.06 ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 196.696 161.913 176.977 1.00 47.72 ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 198.268 162.722 178.622 1.00 43.19 ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 195.881 163.872 174.931 1.00 40.67 ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 195.462 163.884 173.533 1.00 40.62 ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 195.479 165.296 172.961 1.00 39.43 ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 195.945 165.511 171.836 1.00 37.64 ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 194.069 163.271 173.402 1.00 40.01 ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 194.033 162.012 174.081 1.00 41.12 ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 193.722 163.055 171.941 1.00 38.57 ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 194.986 166.275 173.722 1.00 37.95 ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 194.957 167.650 173.243 1.00 38.78 ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 196.362 168.227 173.122 1.00 39.99 ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 196.651 168.967 172.176 1.00 40.69 ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 194.096 168.509 174.168 1.00 37.39 ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 197.249 167.901 174.065 1.00 41.46 ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 198.632 168.356 173.952 1.00 41.70 ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 199.306 167.766 172.720 1.00 42.33 ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 200.007 168.473 171.985 1.00 42.26 ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 199.408 167.992 175.217 1.00 39.36 ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 198.764 168.499 176.373 1.00 41.76 ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 199.093 166.471 172.467 1.00 41.16 ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 199.677 165.847 171.285 1.00 40.83 ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 199.116 166.457 170.006 1.00 42.75 ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 199.856 166.686 169.042 1.00 41.16 ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 199.439 164.338 171.318 1.00 40.01 ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 199.946 163.641 170.070 1.00 43.96 ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 199.254 163.581 169.053 1.00 44.20 ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 201.161 163.110 170.141 1.00 43.47 ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 197.807 166.725 169.979 1.00 37.80 ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 197.204 167.350 168.807 1.00 35.52 ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 197.766 168.747 168.576 1.00 38.38 ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 198.047 169.128 167.435 1.00 41.75 ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 195.687 167.403 168.964 1.00 36.10 ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 195.019 166.090 168.733 1.00 38.26 ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 195.578 164.969 168.197 1.00 40.79 ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 193.661 165.755 169.040 1.00 37.68 ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 194.652 163.956 168.146 1.00 40.57 ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 193.468 164.413 168.659 1.00 38.54 ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 192.593 166.459 169.598 1.00 37.46 ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 192.249 163.764 168.816 1.00 38.70 ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 191.384 165.812 169.756 1.00 38.39 ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 191.222 164.479 169.369 1.00 38.95 ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 197.936 169.525 169.647 1.00 39.39 ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 198.531 170.849 169.511 1.00 39.92 ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 199.960 170.755 168.998 1.00 40.51 ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 200.413 171.616 168.235 1.00 38.27 ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 198.487 171.587 170.849 1.00 38.79 ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 197.206 172.364 171.154 1.00 39.61 ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 197.333 173.108 172.473 1.00 39.04 ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 196.882 173.324 170.022 1.00 39.74 ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 200.690 169.717 169.415 1.00 45.06 ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 202.025 169.493 168.869 1.00 45.49 ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 201.969 169.179 167.378 1.00 45.53 ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 202.797 169.666 166.602 1.00 45.57 ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 202.721 168.363 169.628 1.00 45.64 ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 202.986 168.675 171.067 1.00 48.20 ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 202.726 167.781 172.083 1.00 49.53 ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 203.486 169.784 171.661 1.00 46.83 ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 203.056 168.324 173.241 1.00 47.65 ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 203.519 169.540 173.014 1.00 48.76 ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 200.998 168.363 166.959 1.00 41.46 ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 200.911 167.969 165.555 1.00 39.98 ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 200.490 169.135 164.670 1.00 38.49 ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 201.094 169.381 163.620 1.00 37.54 ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 199.935 166.803 165.396 1.00 38.78 ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 200.326 165.472 166.039 1.00 39.95 ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 199.190 164.472 165.908 1.00 37.76 ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 201.601 164.928 165.414 1.00 41.35 ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 199.453 169.858 165.072 1.00 35.72 ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 198.904 170.929 164.230 1.00 34.95 ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 199.895 172.085 164.168 1.00 36.54 ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 200.495 172.435 165.198 1.00 36.93 ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 197.549 171.388 164.775 1.00 34.16 ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 196.582 170.207 164.867 1.00 36.15 ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 196.950 172.467 163.894 1.00 33.56 ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 195.220 170.576 165.409 1.00 33.06 ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 200.108 172.701 162.997 1.00 37.10 ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 200.962 173.895 162.931 1.00 34.68 ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 200.374 175.074 163.692 1.00 37.49 ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 199.281 174.971 164.257 1.00 40.13 ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 201.048 174.185 161.426 1.00 34.68 ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 200.744 172.878 160.772 1.00 35.80 ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 199.739 172.213 161.658 1.00 37.56 ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 201.085 176.204 163.713 1.00 38.71 ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 200.688 177.339 164.529 1.00 37.53 ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 200.453 178.631 163.759 1.00 39.98 ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 199.714 179.488 164.255 1.00 41.37 ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 201.741 177.610 165.615 1.00 37.30 ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 202.220 176.362 166.339 1.00 39.02 ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 203.133 176.677 167.507 1.00 41.08 ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 203.399 177.841 167.804 1.00 40.08 ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 203.621 175.638 168.174 1.00 37.80 ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 201.044 178.803 162.578 1.00 41.70 ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 200.989 180.073 161.868 1.00 44.24 ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 200.481 179.874 160.447 1.00 41.75 ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 200.793 178.872 159.798 1.00 41.86 ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 202.368 180.748 161.825 1.00 42.78 ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 203.323 179.854 161.241 1.00 43.07 ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 202.825 181.122 163.228 1.00 39.58 ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 199.691 180.840 159.975 1.00 37.04 ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 199.245 180.861 158.584 1.00 40.26 ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 198.870 182.299 158.246 1.00 42.22 ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 197.841 182.795 158.715 1.00 41.57 ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 198.069 179.916 158.368 1.00 40.42 ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 197.562 179.796 156.929 1.00 38.66 ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 198.715 179.536 155.975 1.00 38.00 ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 196.521 178.698 156.817 1.00 36.93 ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 199.696 182.956 157.437 1.00 41.94 ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 199.517 184.369 157.131 1.00 41.43 ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 198.622 184.556 155.914 1.00 42.45 ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 198.784 183.875 154.897 1.00 42.95 ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 200.871 185.037 156.885 1.00 40.89 ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 201.578 184.383 155.847 1.00 42.25 ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 197.683 185.493 156.023 1.00 48.40 ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 196.761 185.779 154.932 1.00 49.18 ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 197.503 186.345 153.727 1.00 49.75 ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 198.544 186.995 153.853 1.00 49.99 ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 195.692 186.774 155.383 1.00 47.52 ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 194.562 186.151 156.141 1.00 49.61 ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 193.411 186.840 156.460 1.00 48.39 ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 194.406 184.905 156.649 1.00 49.70 ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 192.595 186.046 157.128 1.00 47.24 ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 193.175 184.866 157.256 1.00 48.16 ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 196.953 186.087 152.543 1.00 47.98 ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 197.519 186.633 151.319 1.00 47.73 ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 197.284 188.139 151.252 1.00 49.69 ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 196.299 188.663 151.777 1.00 48.73 ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 196.913 185.945 150.098 1.00 47.30 ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 197.271 184.471 149.893 1.00 48.14 ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 197.092 184.069 148.438 1.00 47.15 ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 198.692 184.184 150.355 1.00 48.59 ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 198.205 188.835 150.591 1.00 50.17 ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 198.197 190.292 150.534 1.00 51.14 ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 197.528 190.764 149.252 1.00 48.86 ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 197.879 190.313 148.158 1.00 48.01 ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 199.620 190.847 150.619 1.00 49.94 ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 199.720 192.184 151.331 1.00 49.03 ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 201.036 192.877 151.018 1.00 48.76 ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 200.976 193.592 149.679 1.00 48.43 ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 202.053 194.611 149.546 1.00 47.63 ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 196.572 191.680 149.390 1.00 48.24 ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 195.864 192.224 148.241 1.00 49.45 ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 196.734 193.239 147.511 1.00 49.40 ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 197.361 194.099 148.135 1.00 49.91 ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 194.554 192.878 148.682 1.00 48.03 ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 193.559 191.930 149.328 1.00 46.97 ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 193.024 190.939 148.312 1.00 47.50 ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 192.014 190.050 148.874 1.00 49.97 ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 190.710 190.285 148.844 1.00 49.40 ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 190.218 191.378 148.286 1.00 44.87 ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 189.879 189.400 149.385 1.00 48.40 ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 196.769 193.135 146.185 1.00 44.77 ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 197.494 194.069 145.337 1.00 45.34 ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 196.654 194.333 144.096 1.00 44.75 ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 195.825 193.506 143.707 1.00 43.18 ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 198.883 193.524 144.953 1.00 45.89 ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 199.544 193.040 146.128 1.00 45.83 ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 199.744 194.612 144.326 1.00 40.42 ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 196.869 195.499 143.480 1.00 45.09 ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 196.046 195.908 142.343 1.00 43.43 ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 196.182 194.920 141.191 1.00 44.17 ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 195.210 194.641 140.480 1.00 42.90 ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 196.403 197.344 141.914 1.00 41.44 ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 196.023 198.328 143.008 1.00 40.53 ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 197.885 197.461 141.592 1.00 41.64 ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 197.381 194.377 140.982 1.00 44.50 ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 197.595 193.400 139.924 1.00 42.88 ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 197.411 191.963 140.393 1.00 43.49 ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 197.250 191.071 139.553 1.00 43.40 ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 198.993 193.572 139.317 1.00 44.20 ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 200.143 193.297 140.272 1.00 45.33 ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 200.703 191.899 140.116 1.00 46.50 ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 200.417 191.254 139.085 1.00 47.28 ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 201.442 191.447 141.016 1.00 45.52 ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 197.431 191.717 141.706 1.00 42.80 ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 197.165 190.375 142.212 1.00 41.27 ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 195.706 189.981 142.019 1.00 41.33 ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 195.410 188.804 141.791 1.00 38.91 ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 197.543 190.284 143.691 1.00 40.49 ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 199.038 190.178 143.904 1.00 41.93 ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 199.824 190.749 143.152 1.00 41.97 ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 199.437 189.453 144.941 1.00 40.21 ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 194.788 190.946 142.111 1.00 41.46 ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 193.366 190.646 141.976 1.00 41.50 ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 193.047 190.147 140.573 1.00 42.90 ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 192.180 189.283 140.397 1.00 43.25 ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 192.524 191.883 142.342 1.00 37.35 ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 192.872 192.363 143.749 1.00 40.74 ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 191.048 191.557 142.282 1.00 36.56 ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 192.840 191.269 144.782 1.00 41.73 ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 193.735 190.669 139.556 1.00 41.34 ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 193.497 190.236 138.184 1.00 40.28 ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 193.889 188.784 137.944 1.00 40.65 ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 193.516 188.228 136.907 1.00 38.46 ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 194.251 191.143 137.212 1.00 41.43 ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 193.892 192.615 137.330 1.00 42.72 ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 194.799 193.477 136.466 1.00 42.95 ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 195.184 194.763 137.179 1.00 41.74 ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 196.226 195.521 136.433 1.00 42.00 ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 194.626 188.163 138.863 1.00 41.93 ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 195.040 186.775 138.705 1.00 41.74 ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 194.018 185.856 139.361 1.00 40.01 ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 193.852 185.911 140.588 1.00 40.10 ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 196.408 186.554 139.323 1.00 40.50 ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 197.052 185.261 138.866 1.00 42.24 ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 196.518 184.627 137.934 1.00 42.92 ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 198.094 184.881 139.438 1.00 44.04 ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 193.313 185.014 138.601 1.00 38.43 ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 192.347 184.095 139.227 1.00 40.34 ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 192.983 183.121 140.202 1.00 40.27 ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 192.349 182.749 141.202 1.00 40.13 ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 191.731 183.366 138.024 1.00 36.43 ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 192.754 183.494 136.942 1.00 34.32 ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 193.386 184.833 137.141 1.00 35.00 ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 194.221 182.697 139.941 1.00 38.00 ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 194.898 181.783 140.854 1.00 40.04 ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 195.063 182.413 142.229 1.00 39.91 ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 194.847 181.757 143.254 1.00 39.20 ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 196.252 181.375 140.275 1.00 39.13 ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 196.762 179.986 140.651 1.00 40.35 ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 195.870 178.909 140.055 1.00 36.80 ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 198.193 179.810 140.181 1.00 39.76 ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 195.440 183.693 142.269 1.00 39.09 ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 195.494 184.404 143.542 1.00 40.81 ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 194.103 184.571 144.139 1.00 41.45 ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 193.934 184.478 145.360 1.00 41.13 ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 196.167 185.762 143.356 1.00 41.53 ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 196.693 186.354 144.630 1.00 41.75 ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 195.892 187.165 145.414 1.00 41.67 ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 197.988 186.098 145.043 1.00 41.21 ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 196.372 187.708 146.587 1.00 41.96 ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 198.473 186.638 146.215 1.00 42.45 ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 197.665 187.445 146.987 1.00 43.64 ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 193.097 184.819 143.296 1.00 39.45 ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 191.733 184.981 143.791 1.00 38.71 ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 191.225 183.715 144.469 1.00 38.97 ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 190.351 183.786 145.341 1.00 36.49 ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 190.800 185.373 142.645 1.00 34.55 ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 191.020 186.776 142.115 1.00 33.20 ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 189.855 187.223 141.249 1.00 34.99 ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 189.834 186.535 139.964 1.00 34.62 ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 189.960 187.140 138.790 1.00 36.32 ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 190.120 188.449 138.701 1.00 37.24 ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 189.921 186.410 137.679 1.00 34.78 ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 191.748 182.555 144.078 1.00 38.37 ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 191.393 181.299 144.725 1.00 41.50 ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 192.277 181.000 145.934 1.00 40.30 ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 191.782 180.551 146.980 1.00 40.70 ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 191.482 180.158 143.708 1.00 41.98 ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 191.613 178.798 144.324 1.00 39.82 ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 190.527 178.185 144.918 1.00 37.27 ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 192.825 178.130 144.300 1.00 36.84 ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 190.647 176.930 145.481 1.00 38.07 ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 192.951 176.880 144.864 1.00 38.67 ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 191.859 176.277 145.451 1.00 39.55 ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 193.581 181.255 145.814 1.00 34.69 ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 194.493 180.952 146.908 1.00 37.98 ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 194.253 181.853 148.111 1.00 42.67 ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 194.487 181.432 149.248 1.00 43.77 ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 195.941 181.062 146.432 1.00 41.37 ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 196.464 179.806 145.795 1.00 44.23 ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 196.301 178.580 146.416 1.00 42.85 ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 197.120 179.852 144.576 1.00 43.05 ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 196.780 177.421 145.832 1.00 41.10 ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 197.602 178.697 143.989 1.00 40.33 ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 197.431 177.482 144.618 1.00 40.41 ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 193.789 183.087 147.893 1.00 45.40 ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 193.469 183.951 149.025 1.00 45.70 ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 192.305 183.387 149.831 1.00 45.45 ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 192.341 183.388 151.066 1.00 44.45 ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 193.174 185.375 148.548 1.00 42.81 ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 191.935 185.534 147.684 1.00 43.56 ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 191.746 186.955 147.200 1.00 48.15 ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 192.598 187.810 147.520 1.00 50.22 ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 190.744 187.219 146.502 1.00 47.53 ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 191.273 182.880 149.151 1.00 37.82 ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 190.173 182.217 149.846 1.00 36.55 ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 190.671 180.992 150.598 1.00 38.03 ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 190.287 180.751 151.752 1.00 40.52 ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 189.088 181.816 148.847 1.00 35.06 ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 188.182 182.939 148.394 1.00 35.30 ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 187.041 182.384 147.562 1.00 34.14 ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 186.501 181.156 148.133 1.00 36.59 ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 185.437 180.515 147.667 1.00 35.86 ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 184.776 180.955 146.609 1.00 33.32 ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 185.029 179.408 148.277 1.00 36.23 ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 191.524 180.198 149.944 1.00 36.72 ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 192.065 179.004 150.586 1.00 39.71 ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 192.794 179.358 151.876 1.00 37.87 ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 192.532 178.775 152.935 1.00 38.76 ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 193.005 178.277 149.627 1.00 40.46 ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 192.294 177.435 148.592 1.00 39.33 ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 191.289 176.485 149.203 1.00 41.39 ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 191.673 175.720 150.112 1.00 40.51 ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 190.116 176.501 148.776 1.00 41.55 ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 193.707 180.327 151.804 1.00 36.68 ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 194.505 180.694 152.968 1.00 39.03 ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 193.634 181.332 154.042 1.00 40.63 ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 193.852 181.115 155.238 1.00 40.76 ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 195.666 181.614 152.549 1.00 41.02 ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 196.434 182.081 153.769 1.00 42.47 ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 196.593 180.886 151.593 1.00 40.34 ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 192.633 182.121 153.644 1.00 42.66 ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 191.746 182.738 154.624 1.00 43.44 ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 190.989 181.682 155.419 1.00 44.21 ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 190.971 181.712 156.658 1.00 41.97 ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 190.772 183.684 153.921 1.00 41.84 ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 190.262 184.818 154.792 1.00 43.44 ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 189.594 185.898 153.956 1.00 42.43 ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 190.490 186.349 152.813 1.00 42.92 ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 189.831 187.381 151.967 1.00 42.59 ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 190.365 180.729 154.720 1.00 41.82 ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 189.641 179.670 155.416 1.00 41.44 ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 190.579 178.831 156.273 1.00 40.02 ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 190.245 178.480 157.413 1.00 40.02 ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 188.893 178.789 154.416 1.00 39.42 ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 187.767 179.494 153.684 1.00 43.02 ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 186.872 178.400 152.564 1.00 53.22 ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 188.057 178.234 151.232 1.00 40.44 ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 191.763 178.509 155.746 1.00 35.53 ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 192.708 177.718 156.515 1.00 35.62 ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 193.150 178.414 157.786 1.00 35.24 ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 193.206 177.803 158.853 1.00 33.75 ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 193.465 179.708 157.689 1.00 36.69 ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 193.902 180.459 158.860 1.00 36.14 ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 192.786 180.583 159.888 1.00 38.56 ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 193.028 180.436 161.092 1.00 38.33 ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 194.400 181.841 158.442 1.00 37.18 ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 191.557 180.856 159.437 1.00 37.20 ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 190.444 180.958 160.373 1.00 36.57 ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 190.223 179.639 161.105 1.00 36.24 ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 190.097 179.609 162.339 1.00 34.96 ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 189.176 181.385 159.632 1.00 36.34 ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 188.049 181.843 160.543 1.00 35.99 ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 188.086 183.348 160.753 1.00 37.50 ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 187.330 183.751 162.008 1.00 37.10 ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 187.795 182.993 163.204 1.00 35.10 ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 190.193 178.530 160.360 1.00 36.58 ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 189.979 177.230 160.985 1.00 33.21 ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 191.129 176.871 161.919 1.00 31.76 ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 190.907 176.314 163.001 1.00 34.60 ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 189.797 176.155 159.915 1.00 33.89 ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 189.336 174.777 160.397 1.00 34.61 ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 188.271 174.906 161.474 1.00 33.07 ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 188.823 173.951 159.230 1.00 34.09 ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 192.363 177.179 161.517 1.00 30.66 ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 193.517 176.891 162.361 1.00 31.33 ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 193.453 177.667 163.666 1.00 34.14 ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 193.708 177.112 164.741 1.00 35.47 ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 194.805 177.215 161.603 1.00 32.75 ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 196.103 177.257 162.407 1.00 33.52 ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 196.443 175.880 162.927 1.00 35.51 ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 197.233 177.798 161.552 1.00 32.65 ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 193.106 178.956 163.596 1.00 35.27 ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 192.997 179.758 164.809 1.00 35.49 ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 191.905 179.216 165.722 1.00 35.89 ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 192.105 179.084 166.936 1.00 36.74 ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 192.729 181.219 164.448 1.00 36.14 ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 192.193 182.060 165.593 1.00 37.77 ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 191.423 183.275 165.114 1.00 40.66 ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 191.444 183.610 163.931 1.00 38.51 ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 190.737 183.941 166.035 1.00 38.55 ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 190.744 178.877 165.151 1.00 32.76 ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 189.654 178.353 165.970 1.00 31.06 ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 190.039 177.038 166.637 1.00 33.02 ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 189.796 176.846 167.835 1.00 35.00 ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 188.395 178.175 165.123 1.00 34.38 ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 187.954 179.461 164.455 1.00 39.24 ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 188.330 180.546 164.947 1.00 36.91 ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 187.230 179.386 163.441 1.00 39.68 ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 190.651 176.124 165.880 1.00 32.09 ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 191.013 174.821 166.430 1.00 28.43 ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 192.083 174.969 167.503 1.00 33.43 ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 192.025 174.311 168.550 1.00 35.63 ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 191.464 173.876 165.300 1.00 27.43 ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 192.124 172.635 165.875 1.00 31.32 ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 190.279 173.493 164.433 1.00 31.48 ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 193.077 175.829 167.267 1.00 37.50 ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 194.127 176.031 168.259 1.00 37.41 ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 193.565 176.635 169.538 1.00 36.98 ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 193.932 176.215 170.642 1.00 36.83 ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 195.230 176.915 167.681 1.00 36.39 ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 196.169 176.184 166.737 1.00 35.63 ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 197.490 176.920 166.594 1.00 38.79 ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 198.342 176.740 167.762 1.00 40.71 ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 199.044 175.645 168.017 1.00 39.76 ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 199.026 174.605 167.197 1.00 38.02 ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 199.784 175.589 169.119 1.00 37.03 ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 192.667 177.618 169.415 1.00 36.92 ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 192.052 178.202 170.602 1.00 38.05 ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 191.228 177.169 171.362 1.00 35.81 ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 191.286 177.104 172.597 1.00 34.01 ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 191.188 179.399 170.211 1.00 36.76 ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 190.562 180.123 171.391 1.00 38.83 ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 191.596 180.715 172.326 1.00 40.72 ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 191.844 180.189 173.411 1.00 38.28 ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 192.208 181.817 171.910 1.00 41.32 ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 190.459 176.348 170.641 1.00 30.15 ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 189.650 175.327 171.301 1.00 31.78 ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 190.522 174.311 172.028 1.00 34.24 ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 190.224 173.926 173.166 1.00 35.85 ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 188.755 174.628 170.278 1.00 33.45 ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 187.646 175.522 169.768 1.00 37.49 ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 187.593 176.701 170.179 1.00 38.62 ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 186.824 175.048 168.955 1.00 36.96 ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 191.606 173.866 171.391 1.00 34.31 ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 192.484 172.888 172.028 1.00 33.96 ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 193.202 173.490 173.231 1.00 35.82 ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 193.393 172.813 174.247 1.00 32.35 ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 193.484 172.343 171.013 1.00 36.36 ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 192.935 171.290 170.048 1.00 35.55 ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 194.044 170.734 169.172 1.00 36.02 ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 192.239 170.175 170.812 1.00 33.35 ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 193.609 174.759 173.135 1.00 40.39 ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 194.220 175.422 174.282 1.00 38.68 ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 193.236 175.529 175.438 1.00 39.64 ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 193.606 175.320 176.600 1.00 39.01 ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 194.731 176.805 173.878 1.00 34.90 ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 191.974 175.848 175.140 1.00 39.89 ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 190.954 175.890 176.183 1.00 37.46 ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 190.751 174.517 176.811 1.00 35.53 ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 190.583 174.405 178.031 1.00 39.97 ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 189.640 176.420 175.611 1.00 38.15 ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 189.699 177.901 175.296 1.00 41.91 ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 190.741 178.528 175.578 1.00 41.84 ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 188.703 178.438 174.767 1.00 40.53 ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 190.756 173.462 175.994 1.00 32.73 ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 190.603 172.108 176.527 1.00 34.50 ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 191.764 171.758 177.451 1.00 37.21 ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 191.565 171.192 178.533 1.00 36.58 ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 190.466 171.092 175.377 1.00 36.74 ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 190.555 169.674 175.910 1.00 34.79 ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 189.149 171.294 174.655 1.00 37.19 ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 192.992 172.084 177.039 1.00 38.86 ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 194.154 171.815 177.886 1.00 38.25 ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 194.056 172.601 179.186 1.00 40.56 ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 194.374 172.088 180.266 1.00 40.18 ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 195.459 172.132 177.132 1.00 36.06 ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 196.657 171.945 178.046 1.00 36.68 ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 195.595 171.248 175.912 1.00 39.87 ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 193.614 173.858 179.105 1.00 42.72 ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 193.456 174.674 180.304 1.00 38.80 ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 192.425 174.072 181.252 1.00 38.97 ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 192.623 174.061 182.472 1.00 39.03 ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 193.064 176.097 179.907 1.00 38.21 ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 193.168 177.117 181.021 1.00 41.67 ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 192.925 178.533 180.535 1.00 43.81 ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 192.721 178.765 179.343 1.00 41.46 ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 192.943 179.487 181.458 1.00 41.81 ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 191.315 173.568 180.706 1.00 36.71 ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 190.305 172.911 181.533 1.00 38.02 ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 190.874 171.662 182.190 1.00 40.62 ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 190.660 171.418 183.384 1.00 41.55 ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 189.056 172.579 180.697 1.00 35.37 ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 188.075 171.780 181.527 1.00 34.48 ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 188.395 173.849 180.209 1.00 36.67 ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 191.603 170.849 181.421 1.00 44.62 ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 192.108 169.586 181.950 1.00 44.49 ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 193.076 169.802 183.105 1.00 43.29 ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 193.213 168.932 183.972 1.00 44.36 ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 192.772 168.783 180.835 1.00 44.60 ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 191.620 168.146 179.595 1.00 48.66 ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 193.753 170.946 183.138 1.00 43.44 ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 194.609 171.310 184.258 1.00 42.87 ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 193.861 172.063 185.350 1.00 44.51 ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 194.458 172.381 186.383 1.00 45.25 ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 195.792 172.150 183.765 1.00 43.13 ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 196.860 171.345 183.049 1.00 43.39 ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 197.688 172.188 182.102 1.00 45.62 ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 197.847 173.398 182.363 1.00 45.62 ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 198.181 171.638 181.094 1.00 44.81 ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 192.579 172.355 185.146 1.00 40.64 ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 191.781 173.038 186.144 1.00 38.25 ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 192.005 174.526 186.245 1.00 38.95 ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 191.489 175.150 187.181 1.00 39.19 ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 192.759 175.123 185.319 1.00 43.71 ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 193.025 176.556 185.397 1.00 46.55 ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 191.771 177.373 185.112 1.00 47.23 ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 191.573 178.441 185.705 1.00 48.70 ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 194.145 176.938 184.431 1.00 45.78 ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 195.482 176.287 184.733 1.00 44.69 ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 196.472 176.528 183.605 1.00 45.95 ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 197.890 176.197 184.033 1.00 46.84 ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 198.848 176.310 182.899 1.00 46.21 ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 190.915 176.897 184.211 1.00 40.48 ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 189.711 177.620 183.833 1.00 40.04 ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 188.490 176.729 184.016 1.00 39.94 ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 188.581 175.498 184.004 1.00 35.89 ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 189.783 178.124 182.384 1.00 39.94 ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 189.489 177.068 181.336 1.00 37.45 ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 189.482 177.668 179.940 1.00 39.51 ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 188.339 178.656 179.774 1.00 41.22 ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 188.288 179.228 178.402 1.00 38.05 ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 187.341 177.374 184.195 1.00 40.52 ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 186.087 176.682 184.436 1.00 38.00 ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 185.459 176.226 183.120 1.00 36.00 ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 185.688 176.805 182.056 1.00 35.66 ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 185.117 177.588 185.194 1.00 37.81 ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 184.078 176.851 186.018 1.00 36.86 ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 184.731 176.037 187.119 1.00 38.90 ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 183.697 175.497 188.090 1.00 38.21 ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 184.227 175.413 189.478 1.00 35.20 ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 184.655 175.170 183.209 1.00 31.23 ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 183.971 174.636 182.040 1.00 32.13 ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 182.755 175.491 181.702 1.00 34.26 ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 181.973 175.852 182.586 1.00 35.09 ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 183.539 173.190 182.282 1.00 29.83 ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 184.627 172.169 182.016 1.00 35.00 ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 184.079 170.822 181.593 1.00 35.62 ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 183.659 170.640 180.450 1.00 34.10 ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 184.084 169.865 182.512 1.00 33.08 ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 182.602 175.812 180.424 1.00 29.08 ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 181.444 176.521 179.906 1.00 21.84 ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 180.578 175.555 179.104 1.00 23.47 ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 180.913 174.381 178.932 1.00 28.00 ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 181.876 177.716 179.055 1.00 21.11 ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 182.416 177.246 177.813 1.00 23.43 ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 182.933 178.529 179.783 1.00 22.24 ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 179.444 176.061 178.616 1.00 22.52 ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 178.546 175.227 177.822 1.00 21.67 ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 179.222 174.758 176.540 1.00 22.83 ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 179.193 173.568 176.205 1.00 24.25 ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 177.262 175.994 177.506 1.00 22.00 ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 176.306 176.037 178.678 1.00 19.42 ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 176.239 175.101 179.474 1.00 21.75 ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 175.557 177.126 178.792 1.00 12.29 ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 179.848 175.687 175.813 1.00 26.64 ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 180.568 175.312 174.601 1.00 26.61 ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 181.747 174.406 174.923 1.00 25.80 ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 182.016 173.444 174.195 1.00 28.88 ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 181.045 176.558 173.858 1.00 29.07 ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 181.985 176.244 172.718 1.00 28.70 ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 181.518 175.664 171.548 1.00 27.80 ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 183.343 176.515 172.816 1.00 29.34 ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 182.372 175.368 170.505 1.00 30.13 ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 184.207 176.222 171.779 1.00 27.68 ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 183.715 175.649 170.625 1.00 31.67 ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 184.569 175.356 169.588 1.00 33.09 ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 182.469 174.704 176.004 1.00 26.91 ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 183.583 173.851 176.403 1.00 28.19 ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 183.097 172.465 176.803 1.00 28.56 ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 183.736 171.460 176.473 1.00 31.62 ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 184.358 174.503 177.547 1.00 25.88 ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 185.418 175.512 177.105 1.00 27.05 ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 186.235 175.989 178.289 1.00 28.60 ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 186.314 174.905 176.039 1.00 28.61 ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 181.968 172.390 177.512 1.00 24.01 ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 181.405 171.093 177.870 1.00 23.45 ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 181.039 170.296 176.624 1.00 25.79 ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 181.340 169.100 176.527 1.00 30.40 ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 180.178 171.281 178.763 1.00 25.34 ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 180.480 171.296 180.250 1.00 25.38 ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 179.198 171.361 181.065 1.00 24.46 ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 178.616 172.698 181.069 1.00 25.70 ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 178.965 173.663 181.908 1.00 25.54 ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 179.895 173.476 182.829 1.00 29.74 ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 178.364 174.847 181.821 1.00 19.38 ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 180.392 170.947 175.654 1.00 25.88 ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 180.020 170.258 174.421 1.00 30.28 ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 181.251 169.783 173.658 1.00 30.00 ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 181.292 168.645 173.172 1.00 28.53 ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 179.171 171.178 173.544 1.00 27.81 ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 178.045 171.650 174.295 1.00 28.87 ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 178.675 170.434 172.314 1.00 27.40 ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 182.266 170.643 173.545 1.00 28.25 ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 183.479 170.277 172.822 1.00 27.98 ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 184.197 169.118 173.499 1.00 28.69 ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 184.662 168.190 172.828 1.00 33.53 ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 184.399 171.490 172.708 1.00 29.19 ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 185.777 171.264 172.091 1.00 28.88 ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 185.646 170.962 170.612 1.00 30.45 ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 186.655 172.479 172.314 1.00 30.36 ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 184.295 169.153 174.830 1.00 28.01 ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 184.943 168.068 175.558 1.00 29.44 ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 184.162 166.773 175.383 1.00 31.62 ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 184.746 165.702 175.180 1.00 33.32 ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 185.103 168.448 177.041 1.00 30.21 ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 186.286 169.405 177.215 1.00 29.25 ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 185.284 167.207 177.899 1.00 29.92 ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 186.378 170.018 178.593 1.00 29.66 ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 182.830 166.850 175.445 1.00 32.65 ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 182.015 165.659 175.241 1.00 32.38 ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 182.242 165.069 173.857 1.00 34.95 ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 182.363 163.848 173.709 1.00 33.09 ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 180.538 165.994 175.444 1.00 30.48 ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 179.670 164.758 175.549 1.00 34.54 ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 179.302 164.157 174.540 1.00 35.34 ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 179.335 164.372 176.775 1.00 33.25 ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 182.310 165.918 172.830 1.00 38.21 ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 182.573 165.417 171.483 1.00 34.08 ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 183.965 164.803 171.378 1.00 31.95 ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 184.151 163.791 170.694 1.00 35.10 ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 182.401 166.537 170.458 1.00 33.02 ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 181.007 167.136 170.424 1.00 34.71 ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 180.747 167.936 169.166 1.00 39.94 ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 180.620 167.321 168.085 1.00 40.52 ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 180.670 169.179 169.253 1.00 38.35 ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 184.956 165.402 172.042 1.00 30.03 ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 186.326 164.911 171.920 1.00 32.37 ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 186.521 163.584 172.648 1.00 37.11 ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 187.278 162.725 172.180 1.00 39.97 ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 187.309 165.958 172.442 1.00 33.51 ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 187.461 167.223 171.593 1.00 34.93 ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 188.661 168.037 172.051 1.00 33.82 ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 187.577 166.870 170.120 1.00 34.79 ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 185.863 163.400 173.796 1.00 35.71 ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 186.049 162.171 174.567 1.00 34.56 ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 185.569 160.957 173.782 1.00 35.95 ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 186.239 159.918 173.748 1.00 34.59 ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 185.348 162.275 175.934 1.00 34.64 ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 185.451 160.958 176.680 1.00 35.08 ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 185.985 163.370 176.766 1.00 36.44 ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 184.411 161.066 173.133 1.00 37.50 ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 183.871 159.955 172.358 1.00 36.14 ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 184.522 159.814 170.989 1.00 35.08 ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 184.083 158.973 170.197 1.00 34.11 ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 182.351 160.096 172.188 1.00 34.65 ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 181.627 160.893 173.267 1.00 34.63 ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 181.834 160.317 174.663 1.00 35.85 ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 180.743 160.771 175.616 1.00 34.21 ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 180.836 160.085 176.932 1.00 33.59 ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 185.550 160.605 170.694 1.00 32.75 ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 186.192 160.546 169.392 1.00 33.68 ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 185.295 160.976 168.253 1.00 37.72 ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 185.332 160.367 167.175 1.00 41.01 ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 184.487 162.012 168.464 1.00 35.05 ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 183.560 162.521 167.463 1.00 34.14 ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 184.047 163.893 167.024 1.00 36.54 ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 184.370 164.741 167.864 1.00 40.45 ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 182.124 162.591 168.012 1.00 34.22 ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 181.487 161.202 168.015 1.00 35.91 ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 181.280 163.559 167.196 1.00 33.54 ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 180.236 161.109 168.859 1.00 36.41 ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 184.112 164.104 165.714 1.00 37.72 ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 184.565 165.376 165.175 1.00 35.24 ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 183.601 166.489 165.570 1.00 35.38 ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 182.395 166.376 165.306 1.00 35.02 ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 184.680 165.297 163.655 1.00 33.81 ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 185.079 166.593 162.950 1.00 34.36 ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 186.493 166.992 163.335 1.00 35.76 ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 184.947 166.447 161.444 1.00 34.25 ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 184.075 167.559 166.210 1.00 35.58 ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 183.178 168.664 166.559 1.00 36.00 ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 182.581 169.310 165.317 1.00 36.27 ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 183.237 169.432 164.280 1.00 38.36 ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 184.093 169.636 167.314 1.00 35.43 ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 185.221 168.791 167.804 1.00 34.53 ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 185.427 167.744 166.757 1.00 34.57 ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 181.318 169.725 165.433 1.00 40.01 ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 180.643 170.356 164.305 1.00 44.02 ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 181.248 171.712 163.973 1.00 44.89 ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 181.182 172.154 162.820 1.00 46.37 ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 179.149 170.499 164.596 1.00 43.36 ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 178.401 169.177 164.649 1.00 43.45 ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 178.394 168.498 163.288 1.00 45.76 ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 179.424 167.469 163.187 1.00 48.05 ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 179.934 167.032 162.045 1.00 47.03 ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 179.540 167.517 160.878 1.00 44.55 ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 180.866 166.082 162.072 1.00 44.26 ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 181.831 172.390 164.963 1.00 38.68 ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 182.486 173.667 164.701 1.00 38.25 ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 183.703 173.489 163.802 1.00 40.97 ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 183.965 174.326 162.930 1.00 42.60 ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 182.885 174.333 166.017 1.00 38.02 ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 183.552 175.560 165.786 1.00 40.91 ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 184.459 172.408 164.001 1.00 37.04 ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 185.682 172.207 163.228 1.00 35.31 ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 185.386 171.791 161.793 1.00 36.64 ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 186.159 172.115 160.886 1.00 38.29 ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 186.566 171.162 163.908 1.00 31.52 ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 187.069 171.570 165.258 1.00 33.91 ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 186.805 172.734 165.917 1.00 35.97 ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 187.929 170.810 166.117 1.00 34.87 ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 187.443 172.747 167.132 1.00 35.75 ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 188.140 171.578 167.280 1.00 34.73 ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 188.537 169.557 166.016 1.00 34.53 ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 188.936 171.132 168.331 1.00 33.31 ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 189.328 169.117 167.062 1.00 35.91 ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 189.519 169.902 168.203 1.00 34.87 ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 184.286 171.078 161.567 1.00 37.81 ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 183.963 170.546 160.245 1.00 37.67 ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 183.497 171.688 159.350 1.00 38.57 ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 182.330 172.082 159.379 1.00 40.94 ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 182.901 169.459 160.351 1.00 38.09 ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 182.556 168.959 159.070 1.00 40.02 ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 184.415 172.221 158.545 1.00 36.42 ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 184.113 173.289 157.600 1.00 36.40 ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 184.199 172.833 156.153 1.00 36.79 ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 183.262 173.048 155.378 1.00 36.96 ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 185.059 174.476 157.826 1.00 37.11 ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 184.813 175.207 159.109 1.00 38.97 ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 185.682 176.154 159.606 1.00 39.12 ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 183.794 175.130 159.998 1.00 38.07 ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 185.209 176.628 160.745 1.00 40.02 ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 184.065 176.023 161.005 1.00 40.37 ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 185.305 172.204 155.762 1.00 36.35 ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 185.449 171.699 154.409 1.00 36.53 ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 184.769 170.338 154.274 1.00 36.70 ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 184.364 169.711 155.257 1.00 37.81 ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 186.925 171.610 154.023 1.00 34.03 ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 187.796 170.898 155.035 1.00 31.95 ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 187.895 169.513 155.045 1.00 33.06 ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 188.524 171.612 155.975 1.00 33.85 ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 188.691 168.862 155.966 1.00 35.53 ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 189.323 170.969 156.899 1.00 34.92 ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 189.402 169.594 156.890 1.00 35.09 ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 190.196 168.947 157.807 1.00 35.00 ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 184.640 169.882 153.030 1.00 36.14 ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 183.980 168.611 152.766 1.00 35.78 ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 184.832 167.460 153.287 1.00 37.57 ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 186.034 167.386 153.018 1.00 38.11 ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 183.720 168.444 151.272 1.00 37.31 ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 182.879 169.510 150.812 1.00 38.02 ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 183.031 167.118 151.002 1.00 36.92 ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 184.200 166.559 154.032 1.00 41.23 ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 184.897 165.473 154.714 1.00 40.85 ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 184.109 164.187 154.490 1.00 40.25 ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 182.879 164.242 154.334 1.00 40.17 ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 185.065 165.794 156.210 1.00 40.84 ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 183.712 165.818 156.911 1.00 41.43 ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 186.004 164.821 156.888 1.00 37.42 ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 184.757 163.021 154.429 1.00 37.34 ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 183.996 161.769 154.433 1.00 36.40 ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 183.176 161.638 155.707 1.00 41.16 ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 183.571 162.100 156.779 1.00 39.99 ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 185.082 160.693 154.350 1.00 34.89 ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 186.207 161.365 153.653 1.00 37.25 ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 186.174 162.803 154.091 1.00 37.48 ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 182.008 161.005 155.573 1.00 42.49 ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 181.069 160.928 156.689 1.00 40.63 ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 181.677 160.196 157.879 1.00 38.52 ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 181.571 160.650 159.023 1.00 38.96 ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 179.778 160.245 156.239 1.00 35.74 ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 182.321 159.060 157.628 1.00 36.53 ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 182.901 158.274 158.697 1.00 36.33 ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 184.362 158.562 158.972 1.00 40.64 ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 185.203 157.667 158.849 1.00 42.44 ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 184.686 159.797 159.344 1.00 43.54 ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 186.048 160.175 159.698 1.00 43.28 ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 186.114 160.523 161.177 1.00 41.28 ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 185.324 161.339 161.665 1.00 39.76 ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 186.541 161.354 158.857 1.00 41.65 ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 188.036 161.602 159.001 1.00 41.75 ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 188.696 162.892 157.930 1.00 49.49 ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 189.201 161.931 156.508 1.00 42.31 ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 187.058 159.908 161.882 1.00 39.82 ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 187.238 160.160 163.302 1.00 40.68 ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 187.936 161.499 163.524 1.00 39.78 ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 188.356 162.180 162.585 1.00 41.15 ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 188.038 159.033 163.951 1.00 39.64 ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 189.270 158.848 163.243 1.00 37.95 ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 187.246 157.736 163.926 1.00 38.53 ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 188.053 161.878 164.796 1.00 38.02 ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 188.674 163.154 165.134 1.00 38.51 ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 190.180 163.106 164.890 1.00 36.73 ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 190.786 164.108 164.494 1.00 37.44 ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 188.328 163.547 166.583 1.00 37.85 ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 188.925 162.561 167.576 1.00 37.80 ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 188.789 164.967 166.875 1.00 36.96 ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 190.808 161.949 165.110 1.00 33.90 ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 192.250 161.835 164.901 1.00 35.64 ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 192.589 161.924 163.417 1.00 37.73 ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 193.543 162.609 163.018 1.00 37.24 ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 192.773 160.529 165.527 1.00 37.27 ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 193.001 160.713 167.029 1.00 36.67 ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 194.054 160.075 164.847 1.00 36.85 ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 193.337 159.430 167.755 1.00 35.40 ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 191.816 161.232 162.576 1.00 38.54 ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 192.028 161.316 161.135 1.00 35.80 ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 191.818 162.737 160.636 1.00 34.86 ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 192.580 163.228 159.793 1.00 37.18 ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 191.091 160.351 160.411 1.00 36.40 ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 191.353 158.883 160.694 1.00 37.52 ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 190.478 157.969 159.861 1.00 37.89 ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 189.254 158.109 159.843 1.00 37.67 ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 191.101 157.029 159.160 1.00 34.90 ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 190.786 163.416 161.145 1.00 33.56 ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 190.552 164.799 160.754 1.00 34.12 ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 191.695 165.697 161.201 1.00 34.72 ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 192.085 166.615 160.479 1.00 35.25 ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 189.227 165.304 161.324 1.00 33.16 ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 188.883 166.689 160.861 1.00 31.79 ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 188.104 167.024 159.793 1.00 32.05 ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 189.312 167.925 161.448 1.00 34.52 ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 188.019 168.390 159.679 1.00 33.86 ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 188.753 168.966 160.683 1.00 33.34 ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 190.113 168.251 162.546 1.00 35.48 ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 188.968 170.309 160.980 1.00 31.89 ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 190.326 169.585 162.838 1.00 34.23 ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 189.755 170.597 162.060 1.00 32.55 ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 192.237 165.454 162.396 1.00 32.21 ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 193.358 166.259 162.877 1.00 32.12 ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 194.571 166.078 161.973 1.00 34.13 ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 195.239 167.052 161.605 1.00 36.75 ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 193.682 165.908 164.341 1.00 32.87 ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 195.097 166.333 164.692 1.00 32.22 ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 192.685 166.572 165.274 1.00 35.66 ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 194.871 164.834 161.594 1.00 31.14 ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 196.011 164.593 160.710 1.00 30.09 ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 195.801 165.233 159.341 1.00 34.46 ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 196.713 165.873 158.794 1.00 37.29 ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 196.256 163.091 160.571 1.00 32.32 ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 196.500 162.497 161.834 1.00 33.97 ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 194.604 165.074 158.770 1.00 34.02 ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 194.319 165.671 157.470 1.00 33.89 ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 194.398 167.190 157.536 1.00 35.90 ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 194.928 167.832 156.623 1.00 38.24 ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 192.943 165.226 156.979 1.00 35.28 ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 192.895 165.029 155.478 1.00 38.00 ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 193.866 165.417 154.795 1.00 38.64 ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 191.886 164.488 154.980 1.00 37.19 ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 193.877 167.780 158.614 1.00 31.16 ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 193.937 169.226 158.783 1.00 30.56 ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 195.372 169.702 158.931 1.00 33.07 ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 195.732 170.766 158.420 1.00 36.60 ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 193.104 169.638 159.997 1.00 30.07 ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 193.012 171.121 160.191 1.00 31.10 ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 192.515 171.934 159.189 1.00 30.86 ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 193.419 171.702 161.381 1.00 31.26 ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 192.427 173.298 159.367 1.00 31.36 ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 193.333 173.065 161.563 1.00 32.31 ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 192.837 173.864 160.556 1.00 34.54 ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 196.205 168.937 159.638 1.00 30.66 ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 197.615 169.292 159.749 1.00 30.22 ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 198.286 169.295 158.383 1.00 32.79 ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 199.040 170.219 158.055 1.00 36.09 ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 198.324 168.326 160.696 1.00 32.84 ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 197.587 168.157 161.893 1.00 35.53 ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 198.014 168.273 157.567 1.00 34.22 ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 198.590 168.238 156.224 1.00 35.09 ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 198.103 169.413 155.381 1.00 35.81 ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 198.892 170.053 154.668 1.00 37.18 ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 198.253 166.912 155.543 1.00 33.39 ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 199.339 166.402 154.611 1.00 36.78 ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 198.829 165.359 153.638 1.00 39.36 ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 197.878 164.630 153.991 1.00 41.06 ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 199.379 165.268 152.521 1.00 35.76 ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 196.805 169.717 155.454 1.00 30.31 ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 196.254 170.833 154.692 1.00 28.88 ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 196.865 172.157 155.130 1.00 30.07 ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 197.167 173.017 154.295 1.00 36.49 ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 194.733 170.874 154.842 1.00 30.29 ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 194.017 169.669 154.264 1.00 30.87 ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 192.518 169.760 154.485 1.00 30.11 ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 191.829 168.561 154.023 1.00 29.50 ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 190.886 168.551 153.092 1.00 30.48 ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 190.491 169.664 152.496 1.00 31.31 ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 190.324 167.395 152.750 1.00 32.06 ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 197.053 172.340 156.437 1.00 29.47 ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 197.627 173.584 156.940 1.00 32.07 ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 199.090 173.700 156.532 1.00 33.16 ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 199.570 174.793 156.223 1.00 34.88 ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 197.443 173.683 158.465 1.00 30.86 ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 195.967 173.884 158.806 1.00 30.00 ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 198.251 174.836 159.033 1.00 33.22 ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 195.300 174.973 158.000 1.00 30.14 ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 199.823 172.583 156.520 1.00 30.62 ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 201.198 172.624 156.025 1.00 29.41 ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 201.242 173.040 154.559 1.00 29.40 ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 202.067 173.878 154.163 1.00 30.57 ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 201.867 171.263 156.215 1.00 28.42 ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 202.177 170.918 157.661 1.00 30.32 ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 202.620 169.470 157.795 1.00 31.90 ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 202.384 168.947 159.202 1.00 32.96 ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 202.894 169.889 160.237 1.00 33.25 ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 200.355 172.472 153.740 1.00 28.76 ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 200.315 172.855 152.331 1.00 30.89 ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 199.957 174.328 152.170 1.00 31.13 ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 200.534 175.030 151.332 1.00 33.44 ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 199.323 171.978 151.570 1.00 31.53 ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 199.257 172.287 150.085 1.00 32.91 ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 198.039 171.689 149.416 1.00 32.83 ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 198.158 170.889 148.491 1.00 33.03 ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 196.858 172.076 149.882 1.00 32.63 ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 199.003 174.815 152.967 1.00 32.19 ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 198.614 176.218 152.886 1.00 31.10 ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 199.742 177.134 153.346 1.00 36.10 ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 199.916 178.230 152.803 1.00 36.04 ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 197.352 176.459 153.712 1.00 31.29 ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 196.051 175.989 153.062 1.00 32.52 ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 194.860 176.336 153.938 1.00 34.39 ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 195.894 176.595 151.676 1.00 33.30 ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 200.511 176.707 154.351 1.00 35.41 ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 201.684 177.469 154.764 1.00 32.47 ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 202.692 177.567 153.631 1.00 35.09 ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 203.247 178.644 153.378 1.00 35.99 ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 202.335 176.825 155.988 1.00 32.01 ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 201.554 176.962 157.280 1.00 34.69 ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 202.301 176.381 158.463 1.00 36.61 ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 202.919 175.321 158.364 1.00 35.25 ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 202.251 177.075 159.594 1.00 38.32 ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 202.945 176.455 152.939 1.00 36.67 ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 203.862 176.496 151.804 1.00 35.34 ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 203.339 177.414 150.705 1.00 33.60 ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 204.103 178.180 150.104 1.00 33.40 ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 204.094 175.086 151.263 1.00 33.77 ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 204.794 174.187 152.260 1.00 36.15 ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 205.030 174.578 153.402 1.00 35.61 ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 205.132 172.977 151.833 1.00 34.89 ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 202.032 177.357 150.437 1.00 34.78 ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 201.440 178.195 149.397 1.00 33.85 ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 201.581 179.671 149.754 1.00 37.65 ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 201.948 180.500 148.914 1.00 39.92 ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 199.968 177.808 149.173 1.00 36.11 ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 199.872 176.452 148.471 1.00 37.84 ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 199.248 178.878 148.368 1.00 37.07 ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 198.510 175.806 148.572 1.00 36.44 ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 201.289 180.020 151.009 1.00 40.18 ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 201.393 181.412 151.438 1.00 40.22 ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 202.842 181.883 151.439 1.00 39.28 ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 203.122 183.043 151.112 1.00 39.92 ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 200.770 181.584 152.823 1.00 39.86 ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 200.652 182.955 153.161 1.00 38.51 ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 203.774 181.003 151.810 1.00 36.23 ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 205.188 181.349 151.752 1.00 38.51 ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 205.625 181.634 150.321 1.00 39.57 ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 206.373 182.585 150.069 1.00 36.68 ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 206.025 180.220 152.354 1.00 37.45 ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 207.536 180.440 152.433 1.00 36.92 ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 207.862 181.617 153.337 1.00 38.42 ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 208.231 179.175 152.914 1.00 34.27 ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 205.169 180.813 149.372 1.00 41.67 ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 205.486 181.066 147.971 1.00 40.38 ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 204.861 182.369 147.487 1.00 39.76 ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 205.495 183.135 146.751 1.00 40.45 ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 205.022 179.893 147.107 1.00 40.19 ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 203.614 182.634 147.884 1.00 40.69 ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 202.933 183.848 147.441 1.00 41.98 ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 203.612 185.102 147.980 1.00 43.28 ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 203.787 186.082 147.248 1.00 40.28 ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 201.466 183.812 147.866 1.00 40.00 ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 203.991 185.092 149.259 1.00 41.96 ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 204.642 186.261 149.843 1.00 39.82 ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 206.051 186.442 149.294 1.00 42.17 ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 206.500 187.574 149.082 1.00 40.19 ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 204.667 186.143 151.366 1.00 36.82 ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 206.763 185.342 149.060 1.00 42.95 ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 208.129 185.381 148.541 1.00 41.00 ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 208.089 184.977 147.069 1.00 42.01 ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 208.285 183.812 146.719 1.00 40.69 ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 209.041 184.469 149.351 1.00 41.64 ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 208.858 184.670 150.742 1.00 43.87 ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 207.836 185.954 146.203 1.00 44.78 ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 207.848 185.712 144.773 1.00 45.23 ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 206.630 186.234 144.038 1.00 48.23 ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 206.748 186.752 142.924 1.00 49.53 ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 205.454 186.109 144.646 1.00 44.20 ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 204.240 186.607 144.029 1.00 44.19 ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 203.431 185.553 143.300 1.00 46.20 ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 203.347 184.405 143.745 1.00 46.79 ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 202.828 185.938 142.172 1.00 50.43 ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 201.932 185.042 141.448 1.00 50.36 ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 202.679 183.975 140.655 1.00 49.06 ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 202.136 182.885 140.436 1.00 50.04 ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 201.031 185.848 140.511 1.00 47.52 ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 203.903 184.265 140.207 1.00 50.33 ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 204.654 183.284 139.428 1.00 51.18 ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 204.937 182.030 140.246 1.00 50.93 ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 204.802 180.905 139.744 1.00 51.73 ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 205.953 183.903 138.914 1.00 52.67 ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 206.665 184.790 139.925 1.00 53.21 ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 207.841 185.515 139.291 1.00 51.42 ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 208.632 186.298 140.325 1.00 51.28 ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 209.757 187.057 139.710 1.00 51.50 ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 205.326 182.201 141.511 1.00 48.01 ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 205.493 181.045 142.383 1.00 49.83 ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 204.177 180.306 142.584 1.00 49.70 ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 204.153 179.074 142.542 1.00 50.24 ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 206.079 181.475 143.728 1.00 48.92 ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 207.303 182.362 143.610 1.00 51.31 ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 208.568 181.573 143.329 1.00 53.71 ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 208.546 180.335 143.492 1.00 51.60 ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 209.583 182.190 142.945 1.00 52.41 ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 203.077 181.039 142.778 1.00 44.02 ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 201.776 180.393 142.912 1.00 44.31 ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 201.451 179.552 141.684 1.00 42.87 ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 200.785 178.514 141.790 1.00 44.56 ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 200.687 181.441 143.142 1.00 45.47 ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 200.641 182.092 144.523 1.00 47.29 ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 199.311 182.794 144.728 1.00 46.06 ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 200.873 181.051 145.606 1.00 45.26 ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 201.910 179.985 140.511 1.00 38.16 ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 201.691 179.199 139.303 1.00 38.57 ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 202.619 177.992 139.248 1.00 40.12 ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 202.235 176.930 138.744 1.00 41.32 ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 201.876 180.076 138.064 1.00 38.08 ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 201.336 179.462 136.783 1.00 39.49 ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 202.428 178.765 135.988 1.00 38.23 ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 201.847 177.981 134.826 1.00 37.56 ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 202.898 177.226 134.095 1.00 37.67 ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 203.841 178.129 139.757 1.00 39.10 ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 204.862 177.107 139.568 1.00 38.31 ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 204.939 176.084 140.700 1.00 37.86 ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 205.801 175.200 140.649 1.00 37.79 ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 206.233 177.765 139.383 1.00 38.80 ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 207.149 176.956 138.485 1.00 40.75 ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 206.746 175.939 137.923 1.00 41.58 ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 208.391 177.406 138.347 1.00 39.27 ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 204.077 176.168 141.709 1.00 35.25 ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 204.102 175.216 142.817 1.00 37.54 ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 203.143 174.068 142.544 1.00 36.20 ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 202.062 174.255 141.971 1.00 33.40 ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 203.776 175.906 144.158 1.00 36.87 ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 202.367 176.507 144.135 1.00 34.52 ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 204.858 176.908 144.540 1.00 36.33 ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 201.891 176.993 145.479 1.00 34.68 ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 203.551 172.868 142.947 1.00 30.53 ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 202.697 171.693 142.859 1.00 28.11 ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 201.713 171.684 144.020 1.00 28.81 ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 202.057 172.057 145.146 1.00 31.35 ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 203.539 170.417 142.875 1.00 29.04 ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 204.540 170.339 141.766 1.00 30.82 ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 204.579 171.247 140.730 1.00 31.81 ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 205.547 169.463 141.535 1.00 29.98 ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 205.563 170.933 139.907 1.00 30.25 ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 206.166 169.855 140.373 1.00 31.77 ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 200.485 171.254 143.747 1.00 26.62 ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 199.404 171.303 144.721 1.00 26.46 ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 198.808 169.911 144.878 1.00 26.64 ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 198.770 169.128 143.923 1.00 27.54 ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 198.324 172.326 144.308 1.00 23.82 ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 197.590 171.860 143.063 1.00 26.75 ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 197.356 172.579 145.450 1.00 25.72 ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 198.373 169.597 146.095 1.00 27.66 ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 197.628 168.376 146.368 1.00 25.40 ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 196.142 168.712 146.394 1.00 28.74 ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 195.683 169.444 147.276 1.00 31.30 ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 198.069 167.755 147.693 1.00 25.00 ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 197.167 166.263 148.163 1.00 38.20 ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 195.394 168.180 145.422 1.00 26.99 ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 193.980 168.522 145.308 1.00 26.84 ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 193.186 168.071 146.525 1.00 28.26 ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 192.154 168.668 146.848 1.00 29.51 ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 193.393 167.912 144.035 1.00 26.96 ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 193.558 168.722 142.749 1.00 27.69 ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 192.673 168.164 141.649 1.00 26.24 ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 193.262 170.193 142.987 1.00 29.37 ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 193.642 167.019 147.206 1.00 31.73 ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 192.965 166.592 148.418 1.00 30.92 ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 193.075 167.610 149.536 1.00 30.28 ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 192.131 167.803 150.306 1.00 31.77 ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 194.226 168.278 149.638 1.00 28.89 ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 194.424 169.265 150.683 1.00 29.90 ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 193.662 170.554 150.473 1.00 31.17 ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 193.433 171.291 151.439 1.00 32.86 ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 193.265 170.848 149.239 1.00 31.24 ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 192.508 172.059 148.969 1.00 31.19 ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 191.070 171.905 149.444 1.00 31.49 ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 190.462 170.841 149.301 1.00 36.83 ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 192.537 172.384 147.478 1.00 31.92 ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 193.915 172.714 146.905 1.00 33.08 ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 193.777 173.261 145.503 1.00 32.00 ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 194.643 173.704 147.797 1.00 33.92 ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 190.527 172.978 150.021 1.00 31.04 ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 189.152 172.935 150.505 1.00 33.78 ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 188.162 172.789 149.355 1.00 35.25 ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 187.185 172.040 149.466 1.00 38.60 ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 188.847 174.184 151.330 1.00 36.29 ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 189.763 174.367 152.509 1.00 37.15 ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 190.156 173.281 153.269 1.00 33.76 ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 190.228 175.625 152.853 1.00 36.66 ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 190.998 173.444 154.352 1.00 32.18 ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 191.070 175.792 153.935 1.00 36.62 ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 191.455 174.701 154.685 1.00 35.12 ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 188.389 173.493 148.250 1.00 32.02 ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 187.526 173.376 147.077 1.00 33.66 ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 188.417 173.166 145.854 1.00 33.60 ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 188.805 174.140 145.193 1.00 34.32 ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 186.617 174.607 146.923 1.00 35.03 ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 185.795 174.516 145.646 1.00 34.69 ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 185.710 174.763 148.132 1.00 33.83 ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 188.801 171.925 145.547 1.00 29.97 ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 189.687 171.690 144.390 1.00 28.42 ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 189.096 172.108 143.052 1.00 29.92 ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 189.847 172.529 142.159 1.00 34.61 ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 189.940 170.176 144.445 1.00 30.50 ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 188.861 169.623 145.318 1.00 31.25 ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 188.534 170.691 146.303 1.00 28.97 ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 187.777 171.988 142.869 1.00 27.43 ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 187.180 172.412 141.607 1.00 28.83 ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 187.368 173.906 141.383 1.00 32.07 ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 187.500 174.353 140.235 1.00 34.01 ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 185.697 172.039 141.567 1.00 25.88 ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 184.851 172.667 142.660 1.00 28.56 ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 184.677 171.753 143.856 1.00 31.93 ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 185.488 170.819 144.013 1.00 32.93 ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 183.728 171.969 144.638 1.00 30.72 ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 187.405 174.690 142.462 1.00 29.38 ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 187.755 176.099 142.330 1.00 28.46 ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 189.180 176.260 141.824 1.00 30.55 ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 189.466 177.173 141.045 1.00 35.95 ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 187.571 176.819 143.664 1.00 28.60 ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 190.094 175.381 142.251 1.00 28.54 ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 191.456 175.426 141.723 1.00 28.14 ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 191.488 175.101 140.237 1.00 26.92 ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 192.235 175.724 139.475 1.00 33.10 ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 192.359 174.459 142.486 1.00 27.83 ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 193.760 174.381 141.920 1.00 24.77 ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 194.691 175.373 142.186 1.00 28.56 ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 194.147 173.318 141.115 1.00 27.50 ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 195.969 175.309 141.671 1.00 27.34 ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 195.423 173.247 140.593 1.00 28.71 ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 196.329 174.245 140.875 1.00 27.27 ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 197.604 174.177 140.361 1.00 28.65 ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 190.704 174.109 139.812 1.00 22.96 ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 190.658 173.771 138.391 1.00 25.64 ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 190.124 174.948 137.586 1.00 27.32 ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 190.667 175.302 136.529 1.00 28.09 ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 189.816 172.502 138.168 1.00 28.53 ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 190.323 171.367 139.057 1.00 28.03 ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 189.850 172.089 136.707 1.00 26.84 ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 191.778 171.029 138.838 1.00 25.58 ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 189.058 175.585 138.081 1.00 29.56 ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 188.519 176.763 137.410 1.00 29.12 ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 189.530 177.905 137.399 1.00 29.17 ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 189.621 178.653 136.420 1.00 32.72 ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 187.219 177.199 138.088 1.00 32.08 ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 186.263 176.134 138.013 1.00 31.26 ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 186.642 178.429 137.407 1.00 32.02 ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 190.297 178.057 138.481 1.00 26.22 ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 191.305 179.109 138.538 1.00 29.14 ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 192.405 178.880 137.512 1.00 28.48 ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 192.848 179.823 136.852 1.00 32.51 ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 191.893 179.195 139.946 1.00 29.04 ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 192.864 177.636 137.369 1.00 28.52 ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 193.864 177.333 136.347 1.00 29.57 ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 193.308 177.575 134.949 1.00 27.92 ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 194.000 178.118 134.076 1.00 30.94 ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 194.341 175.888 136.485 1.00 28.31 ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 193.212 175.006 136.474 1.00 32.68 ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 195.103 175.702 137.784 1.00 25.57 ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 192.054 177.176 134.722 1.00 31.59 ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 191.416 177.391 133.428 1.00 31.61 ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 191.343 178.879 133.099 1.00 34.76 ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 191.690 179.306 131.989 1.00 35.09 ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 190.024 176.759 133.458 1.00 33.08 ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 189.428 176.361 132.124 1.00 34.01 ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 187.913 176.476 132.163 1.00 34.39 ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 187.305 176.308 130.850 1.00 35.61 ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 186.737 175.183 130.438 1.00 38.21 ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 186.683 174.111 131.212 1.00 35.26 ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 186.208 175.131 129.219 1.00 38.74 ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 190.923 179.687 134.075 1.00 34.95 ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 190.834 181.130 133.880 1.00 31.54 ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 192.211 181.754 133.696 1.00 31.47 ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 192.366 182.699 132.916 1.00 35.11 ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 190.106 181.770 135.063 1.00 32.33 ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 189.788 183.248 134.889 1.00 35.41 ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 188.818 183.514 133.758 1.00 36.32 ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 187.961 182.688 133.451 1.00 35.75 ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 188.944 184.679 133.133 1.00 35.35 ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 193.217 181.252 134.413 1.00 31.28 ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 194.576 181.760 134.258 1.00 31.27 ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 195.078 181.541 132.839 1.00 29.74 ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 195.627 182.455 132.210 1.00 31.35 ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 195.498 181.080 135.275 1.00 30.92 ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 196.970 181.406 135.142 1.00 30.99 ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 197.787 180.698 134.268 1.00 29.58 ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 197.550 182.410 135.903 1.00 32.51 ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 199.130 180.988 134.148 1.00 29.86 ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 198.895 182.708 135.790 1.00 31.91 ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 199.679 181.994 134.911 1.00 31.74 ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 201.018 182.285 134.795 1.00 33.90 ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 194.887 180.330 132.310 1.00 31.66 ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 195.314 180.048 130.942 1.00 31.48 ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 194.537 180.907 129.952 1.00 33.78 ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 195.112 181.471 129.011 1.00 36.42 ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 195.167 178.547 130.630 1.00 35.10 ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 195.445 178.285 129.159 1.00 36.28 ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 196.105 177.736 131.504 1.00 33.86 ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 193.220 181.029 130.153 1.00 35.85 ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 192.410 181.830 129.241 1.00 37.65 ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 192.852 183.288 129.234 1.00 38.06 ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 192.947 183.910 128.172 1.00 39.53 ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 190.933 181.719 129.619 1.00 37.16 ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 193.126 183.852 130.414 1.00 35.34 ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 193.590 185.232 130.494 1.00 36.55 ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 194.964 185.392 129.857 1.00 38.08 ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 195.221 186.388 129.169 1.00 38.23 ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 193.616 185.691 131.950 1.00 35.95 ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 194.215 187.069 132.158 1.00 35.30 ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 194.210 187.488 133.612 1.00 38.05 ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 193.719 186.762 134.475 1.00 38.88 ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 194.758 188.663 133.892 1.00 36.71 ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 195.861 184.428 130.077 1.00 37.30 ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 197.190 184.511 129.483 1.00 36.25 ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 197.118 184.466 127.962 1.00 37.30 ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 197.908 185.127 127.277 1.00 36.76 ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 198.074 183.385 130.013 1.00 34.88 ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 196.178 183.697 127.416 1.00 41.43 ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 196.044 183.552 125.973 1.00 42.86 ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 194.848 184.307 125.402 1.00 43.52 ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 194.553 184.163 124.211 1.00 42.02 ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 195.957 182.073 125.604 1.00 42.80 ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 197.197 181.302 126.006 1.00 43.25 ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 198.302 181.843 126.015 1.00 41.84 ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 197.019 180.031 126.345 1.00 44.36 ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 194.161 185.107 126.221 1.00 47.28 ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 193.052 185.955 125.771 1.00 48.61 ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 191.967 185.141 125.064 1.00 48.64 ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 191.515 185.482 123.969 1.00 51.11 ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 193.558 187.086 124.874 1.00 49.12 ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 192.492 187.930 124.473 1.00 49.17 ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 191.549 184.055 125.700 1.00 48.37 ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 190.492 183.194 125.184 1.00 49.08 ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 189.370 183.087 126.212 1.00 49.91 ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 189.477 183.578 127.338 1.00 51.29 ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 191.039 181.808 124.831 1.00 49.67 ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 192.110 181.831 123.789 1.00 52.31 ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 192.235 182.718 122.761 1.00 50.53 ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 193.212 180.923 123.672 1.00 51.49 ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 193.347 182.422 122.011 1.00 50.92 ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 193.964 181.322 122.550 1.00 50.74 ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 193.635 179.812 124.406 1.00 49.99 ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 195.115 180.650 122.145 1.00 48.88 ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 194.779 179.147 124.005 1.00 50.29 ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 195.505 179.568 122.884 1.00 49.01 ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 188.285 182.433 125.812 1.00 49.08 ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 187.157 182.179 126.692 1.00 52.68 ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 187.304 180.813 127.351 1.00 50.86 ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 188.040 179.944 126.876 1.00 50.77 ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 185.834 182.249 125.924 1.00 52.77 ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 184.735 181.968 126.774 1.00 51.11 ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 186.595 180.636 128.467 1.00 46.19 ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 186.673 179.373 129.196 1.00 46.72 ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 186.157 178.213 128.355 1.00 48.53 ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 186.786 177.152 128.296 1.00 49.63 ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 185.890 179.472 130.506 1.00 49.03 ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 186.381 180.472 131.553 1.00 48.56 ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 185.538 181.740 131.518 1.00 44.49 ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 186.361 179.846 132.939 1.00 45.94 ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 185.023 178.403 127.677 1.00 48.52 ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 184.411 177.320 126.915 1.00 48.46 ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 185.234 176.908 125.701 1.00 50.54 ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 184.950 175.861 125.111 1.00 50.63 ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 183.002 177.718 126.478 1.00 47.43 ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 182.048 177.953 127.634 1.00 48.53 ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 180.652 178.316 127.173 1.00 49.23 ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 180.094 177.583 126.328 1.00 49.31 ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 180.114 179.335 127.653 1.00 46.23 ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 186.235 177.696 125.317 1.00 54.01 ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 187.126 177.347 124.222 1.00 54.16 ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 188.351 176.572 124.686 1.00 53.06 ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 189.210 176.247 123.860 1.00 53.46 ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 187.574 178.613 123.484 1.00 55.12 ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 186.442 179.562 123.124 1.00 56.15 ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 186.937 180.954 122.789 1.00 57.87 ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 188.160 181.191 122.885 1.00 57.07 ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 186.105 181.812 122.427 1.00 56.61 ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 188.451 176.267 125.977 1.00 47.24 ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 189.609 175.595 126.548 1.00 47.11 ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 189.226 174.189 126.986 1.00 45.81 ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 188.244 174.006 127.714 1.00 47.55 ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 190.164 176.381 127.737 1.00 43.86 ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 190.992 177.623 127.412 1.00 45.37 ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 191.624 178.184 128.674 1.00 43.76 ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 192.057 177.298 126.378 1.00 47.00 ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 190.004 173.205 126.547 1.00 41.19 ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 189.828 171.818 126.943 1.00 41.44 ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 191.056 171.349 127.708 1.00 42.52 ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 192.159 171.887 127.544 1.00 47.32 ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 189.581 170.911 125.731 1.00 41.43 ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 191.061 170.459 124.807 1.00 50.33 ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 190.853 170.335 128.544 1.00 32.80 ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 191.859 169.882 129.491 1.00 30.71 ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 192.555 168.625 128.984 1.00 35.85 ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 191.905 167.662 128.567 1.00 39.67 ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 191.223 169.612 130.857 1.00 31.90 ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 192.125 169.063 131.961 1.00 33.20 ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 193.339 169.950 132.132 1.00 33.91 ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 191.357 168.948 133.265 1.00 32.99 ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 193.884 168.648 129.026 1.00 36.06 ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 194.730 167.519 128.676 1.00 36.40 ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 195.512 167.098 129.911 1.00 35.58 ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 195.990 167.944 130.672 1.00 36.87 ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 195.686 167.881 127.535 1.00 34.95 ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 196.741 166.828 127.237 1.00 36.90 ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 197.851 167.352 126.346 1.00 40.76 ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 197.546 167.818 125.229 1.00 40.95 ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 199.027 167.299 126.764 1.00 40.07 ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 195.635 165.790 130.116 1.00 33.52 ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 196.257 165.233 131.309 1.00 32.51 ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 197.516 164.484 130.901 1.00 33.38 ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 197.478 163.633 130.002 1.00 32.80 ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 195.288 164.309 132.065 1.00 31.70 ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 196.016 163.571 133.168 1.00 32.53 ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 194.141 165.118 132.634 1.00 31.98 ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 198.630 164.802 131.557 1.00 31.13 ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 199.903 164.123 131.325 1.00 29.55 ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 200.389 163.557 132.652 1.00 31.45 ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 200.679 164.312 133.582 1.00 34.06 ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 200.931 165.081 130.724 1.00 31.14 ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 201.992 164.362 129.916 1.00 35.06 ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 201.723 163.854 128.827 1.00 34.63 ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 203.211 164.326 130.440 1.00 33.70 ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 200.475 162.236 132.747 1.00 31.68 ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 200.874 161.567 133.979 1.00 34.09 ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 202.346 161.197 133.842 1.00 36.41 ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 202.706 160.289 133.088 1.00 39.65 ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 200.003 160.342 134.269 1.00 33.23 ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 200.464 159.659 135.546 1.00 30.78 ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 198.546 160.752 134.379 1.00 30.94 ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 203.200 161.903 134.579 1.00 40.32 ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 204.634 161.660 134.563 1.00 42.10 ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 205.177 161.756 135.982 1.00 45.03 ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 204.530 162.298 136.881 1.00 43.73 ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 205.377 162.653 133.655 1.00 42.08 ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 204.938 163.986 133.940 1.00 42.26 ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 205.133 162.334 132.189 1.00 39.80 ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 206.378 161.214 136.168 1.00 51.53 ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 207.040 161.292 137.462 1.00 51.53 ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 207.374 162.742 137.793 1.00 51.01 ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 207.650 163.551 136.904 1.00 50.18 ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 208.311 160.440 137.456 1.00 51.85 ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 208.008 159.136 136.946 1.00 51.63 ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 208.875 160.298 138.862 1.00 49.24 ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 207.333 163.074 139.089 1.00 49.32 ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 207.616 164.440 139.514 1.00 52.86 ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 209.029 164.866 139.141 1.00 53.03 ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 209.256 166.036 138.810 1.00 49.89 ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 207.403 164.574 141.023 1.00 49.15 ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 207.631 165.904 141.452 1.00 49.22 ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 209.991 163.941 139.191 1.00 52.71 ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 211.364 164.277 138.827 1.00 52.83 ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 211.474 164.609 137.344 1.00 52.98 ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 212.081 165.618 136.966 1.00 51.88 ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 212.297 163.126 139.195 1.00 52.31 ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 212.164 162.653 140.631 1.00 54.27 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 212.967 161.398 140.911 1.00 55.87 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 213.865 161.396 141.753 1.00 54.78 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 212.644 160.321 140.203 1.00 54.34 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 210.892 163.772 136.489 1.00 47.45 ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 210.938 163.997 135.058 1.00 47.55 ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 209.740 164.758 134.529 1.00 48.25 ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 209.052 164.287 133.620 1.00 46.47 ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 209.481 165.938 135.087 1.00 47.84 ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 208.335 166.750 134.701 1.00 48.38 ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 208.780 168.181 134.446 1.00 48.14 ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 209.578 168.734 135.211 1.00 46.47 ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 207.251 166.720 135.780 1.00 46.62 ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 208.265 168.775 133.372 1.00 48.22 ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 208.519 170.167 133.030 1.00 49.82 ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 207.188 170.884 132.868 1.00 48.78 ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 206.320 170.428 132.115 1.00 46.92 ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 209.344 170.283 131.744 1.00 48.73 ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 208.695 169.561 130.691 1.00 49.77 ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 210.740 169.719 131.954 1.00 46.50 ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 207.028 172.003 133.571 1.00 45.15 ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 205.788 172.770 133.559 1.00 43.25 ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 205.931 173.919 132.566 1.00 42.43 ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 206.745 174.825 132.768 1.00 43.31 ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 205.460 173.292 134.957 1.00 40.98 ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 204.892 172.285 135.959 1.00 42.06 ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 204.264 173.003 137.142 1.00 40.27 ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 203.885 171.361 135.292 1.00 39.14 ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 205.137 173.880 131.502 1.00 40.19 ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 205.120 174.946 130.514 1.00 40.91 ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 204.090 176.000 130.923 1.00 40.48 ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 203.627 176.035 132.066 1.00 40.11 ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 204.853 174.379 129.121 1.00 40.00 ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 203.651 173.461 129.082 1.00 41.97 ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 202.521 173.949 129.281 1.00 40.74 ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 203.836 172.249 128.850 1.00 42.28 ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 203.736 176.884 129.988 1.00 38.28 ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 202.855 178.002 130.315 1.00 39.28 ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 201.478 177.526 130.762 1.00 39.46 ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 200.911 178.062 131.721 1.00 39.06 ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 202.732 178.938 129.112 1.00 37.57 ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 200.921 176.525 130.085 1.00 38.57 ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 199.576 176.048 130.373 1.00 39.56 ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 199.560 174.820 131.277 1.00 38.46 ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 198.486 174.267 131.531 1.00 38.84 ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 198.833 175.743 129.071 1.00 39.08 ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 199.747 174.710 127.902 1.00 49.56 ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 200.713 174.389 131.777 1.00 33.76 ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 200.818 173.170 132.567 1.00 34.02 ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 200.791 173.497 134.055 1.00 35.22 ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 201.504 174.396 134.513 1.00 38.10 ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 202.097 172.408 132.224 1.00 36.04 ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 201.998 171.788 130.956 1.00 39.71 ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 199.968 172.764 134.800 1.00 31.68 ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 199.892 172.880 136.250 1.00 28.55 ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 200.079 171.508 136.878 1.00 29.36 ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 199.516 170.520 136.402 1.00 33.62 ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 198.555 173.477 136.693 1.00 29.68 ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 198.319 174.871 136.194 1.00 32.04 ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 198.757 175.963 136.921 1.00 30.98 ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 197.665 175.089 134.995 1.00 31.07 ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 198.542 177.246 136.464 1.00 30.05 ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 197.450 176.371 134.533 1.00 30.94 ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 197.889 177.450 135.269 1.00 30.68 ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 200.870 171.452 137.946 1.00 25.83 ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 201.159 170.193 138.612 1.00 24.04 ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 200.177 169.905 139.737 1.00 25.54 ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 199.797 170.795 140.494 1.00 27.89 ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 199.770 168.640 139.832 1.00 25.90 ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 198.830 168.177 140.843 1.00 24.39 ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 199.342 166.861 141.407 1.00 23.09 ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 199.707 165.956 140.647 1.00 26.91 ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 197.410 168.005 140.266 1.00 20.94 ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 196.539 167.208 141.216 1.00 21.61 ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 196.785 169.360 139.984 1.00 24.06 ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 199.370 166.755 142.731 1.00 19.73 ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 199.825 165.564 143.428 1.00 22.06 ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 198.679 164.936 144.210 1.00 24.84 ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 197.677 165.584 144.521 1.00 26.88 ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 200.980 165.888 144.384 1.00 23.83 ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 200.534 166.825 145.372 1.00 24.76 ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 202.150 166.485 143.627 1.00 24.13 ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 198.840 163.653 144.527 1.00 25.86 ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 197.901 162.947 145.372 1.00 25.80 ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 196.759 162.258 144.658 1.00 27.80 ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 195.954 161.593 145.322 1.00 30.07 ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 196.653 162.395 143.338 1.00 23.57 ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 195.580 161.737 142.607 1.00 19.09 ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 195.773 160.225 142.635 1.00 19.74 ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 196.873 159.725 142.382 1.00 22.04 ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 195.533 162.235 141.165 1.00 20.27 ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 195.215 163.717 140.954 1.00 21.10 ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 194.942 163.993 139.486 1.00 20.71 ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 194.034 164.144 141.809 1.00 17.61 ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 194.702 159.500 142.945 1.00 20.44 ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 194.724 158.043 143.002 1.00 19.35 ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 193.802 157.498 141.922 1.00 14.16 ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 192.608 157.807 141.912 1.00 21.28 ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 194.288 157.540 144.381 1.00 19.28 ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 195.113 158.081 145.535 1.00 19.99 ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 196.511 157.488 145.538 1.00 21.91 ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 197.288 157.917 146.771 1.00 20.88 ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 197.628 159.365 146.737 1.00 19.68 ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 194.352 156.690 141.022 1.00 9.27  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 193.574 156.058 139.967 1.00 12.64 ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 192.967 154.771 140.509 1.00 17.60 ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 193.689 153.902 141.008 1.00 25.08 ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 194.455 155.778 138.750 1.00 14.36 ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 193.771 155.248 137.494 1.00 13.53 ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 192.760 156.250 136.979 1.00 13.03 ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 194.809 154.949 136.435 1.00 18.12 ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 191.648 154.649 140.412 1.00 11.27 ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 190.910 153.527 140.971 1.00 10.09 ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 190.476 152.602 139.845 1.00 14.72 ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 189.639 152.978 139.015 1.00 21.30 ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 189.693 154.018 141.752 1.00 10.19 ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 190.023 154.989 142.867 1.00 11.82 ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 190.377 154.292 144.160 1.00 20.00 ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 191.400 154.587 144.778 1.00 20.51 ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 189.529 153.360 144.582 1.00 20.61 ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 191.041 151.396 139.822 1.00 12.04 ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 190.656 150.372 138.877 1.00 12.05 ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 191.549 150.227 137.665 1.00 16.03 ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 191.260 149.381 136.809 1.00 20.38 ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 192.618 151.010 137.561 1.00 17.19 ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 193.470 150.965 136.382 1.00 16.62 ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 194.862 151.460 136.748 1.00 19.34 ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 195.078 152.044 137.814 1.00 22.86 ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 192.880 151.793 135.236 1.00 14.80 ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 195.807 151.204 135.849 1.00 21.13 ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 197.173 151.693 135.959 1.00 21.20 ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 197.509 152.540 134.742 1.00 25.43 ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 197.141 152.199 133.614 1.00 26.96 ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 198.185 150.546 136.076 1.00 23.15 ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 198.248 149.832 134.835 1.00 24.19 ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 197.800 149.595 137.191 1.00 22.28 ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 198.211 153.645 134.974 1.00 32.40 ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 198.620 154.551 133.911 1.00 32.10 ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 200.094 154.329 133.604 1.00 34.57 ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 200.954 154.587 134.452 1.00 36.99 ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 198.364 156.006 134.306 1.00 30.03 ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 198.599 157.190 132.964 1.00 43.26 ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 200.381 153.851 132.394 1.00 35.45 ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 201.746 153.654 131.924 1.00 37.67 ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 201.898 154.373 130.594 1.00 37.54 ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 201.125 154.121 129.663 1.00 39.93 ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 202.073 152.165 131.776 1.00 37.22 ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 202.095 151.438 133.106 1.00 38.80 ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 202.498 151.998 134.125 1.00 38.29 ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 201.656 150.186 133.103 1.00 37.37 ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 202.889 155.262 130.508 1.00 38.99 ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 203.133 156.060 129.306 1.00 40.66 ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 201.866 156.784 128.860 1.00 39.72 ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 201.520 156.804 127.675 1.00 36.69 ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 203.699 155.200 128.176 1.00 40.63 ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 205.117 154.742 128.450 1.00 42.55 ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 205.947 155.511 128.937 1.00 42.90 ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 205.404 153.485 128.135 1.00 41.90 ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 201.160 157.371 129.827 1.00 36.61 ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 199.928 158.123 129.600 1.00 36.40 ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 198.822 157.266 128.994 1.00 38.27 ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 197.870 157.797 128.412 1.00 38.22 ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 200.179 159.354 128.719 1.00 36.99 ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 199.475 160.588 129.232 1.00 37.34 ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 199.974 161.705 129.092 1.00 40.11 ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 198.311 160.396 129.837 1.00 35.39 ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 198.919 155.945 129.118 1.00 34.41 ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 197.904 155.032 128.616 1.00 29.66 ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 197.355 154.198 129.761 1.00 31.79 ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 198.109 153.724 130.615 1.00 32.85 ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 198.466 154.122 127.521 1.00 30.68 ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 198.816 154.850 126.237 1.00 34.10 ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 199.195 153.879 125.135 1.00 33.77 ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 199.839 154.602 123.966 1.00 33.07 ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 198.887 155.535 123.306 1.00 29.66 ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 196.038 154.023 129.775 1.00 27.52 ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 195.367 153.313 130.851 1.00 25.37 ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 195.258 151.828 130.536 1.00 26.76 ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 194.985 151.437 129.399 1.00 28.28 ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 193.973 153.888 131.094 1.00 23.33 ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 193.914 155.252 131.777 1.00 22.65 ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 192.537 155.469 132.358 1.00 21.76 ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 194.979 155.364 132.849 1.00 22.91 ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 195.475 151.005 131.558 1.00 19.37 ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 195.320 149.562 131.453 1.00 19.79 ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 194.490 149.082 132.631 1.00 18.73 ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 194.713 149.516 133.765 1.00 21.52 ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 196.679 148.857 131.432 1.00 23.91 ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 197.527 149.415 130.444 1.00 25.66 ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 193.534 148.196 132.364 1.00 19.68 ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 192.693 147.669 133.429 1.00 18.90 ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 193.536 146.894 134.432 1.00 18.47 ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 194.432 146.131 134.059 1.00 22.02 ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 191.596 146.775 132.849 1.00 17.20 ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 190.359 147.510 132.328 1.00 13.63 ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 189.347 146.528 131.768 1.00 15.37 ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 189.740 148.362 133.422 1.00 13.26 ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 193.248 147.096 135.713 1.00 15.75 ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 194.056 146.538 136.785 1.00 18.17 ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 193.169 145.847 137.808 1.00 21.43 ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 191.987 146.165 137.960 1.00 22.68 ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 194.889 147.623 137.476 1.00 19.00 ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 195.388 147.169 138.721 1.00 22.30 ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 193.764 144.887 138.512 1.00 22.35 ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 193.118 144.217 139.628 1.00 23.02 ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 193.472 144.845 140.969 1.00 23.98 ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 193.048 144.335 142.010 1.00 28.15 ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 193.488 142.731 139.637 1.00 24.36 ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 192.923 141.985 138.444 1.00 27.88 ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 193.653 141.327 137.705 1.00 29.50 ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 191.613 142.086 138.251 1.00 25.37 ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 194.238 145.931 140.968 1.00 20.31 ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 194.580 146.644 142.188 1.00 20.10 ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 193.520 147.691 142.500 1.00 23.20 ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 192.939 148.304 141.601 1.00 29.29 ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 195.952 147.308 142.064 1.00 19.69 ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 193.271 147.890 143.795 1.00 20.66 ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 192.231 148.824 144.217 1.00 20.85 ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 192.603 150.252 143.835 1.00 19.37 ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 191.776 151.005 143.310 1.00 19.17 ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 191.973 148.691 145.728 1.00 21.99 ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 191.508 147.273 146.067 1.00 21.70 ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 190.948 149.715 146.187 1.00 18.70 ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 190.283 146.830 145.300 1.00 19.85 ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 193.851 150.644 144.089 1.00 22.71 ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 194.292 152.005 143.829 1.00 18.57 ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 195.698 151.998 143.250 1.00 21.85 ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 196.474 151.064 143.466 1.00 26.85 ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 194.264 152.861 145.101 1.00 20.30 ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 192.934 153.100 145.527 1.00 22.96 ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 196.013 153.056 142.508 1.00 21.13 ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 197.343 153.283 141.962 1.00 22.02 ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 197.682 154.757 142.127 1.00 24.11 ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 196.953 155.621 141.633 1.00 28.68 ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 197.417 152.884 140.485 1.00 21.77 ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 197.295 151.461 140.367 1.00 23.45 ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 198.738 153.328 139.877 1.00 22.57 ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 198.778 155.043 142.823 1.00 26.69 ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 199.154 156.421 143.105 1.00 23.80 ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 199.771 157.055 141.865 1.00 25.01 ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 200.786 156.570 141.353 1.00 25.35 ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 200.126 156.479 144.281 1.00 25.53 ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 199.160 158.131 141.384 1.00 23.33 ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 199.719 158.879 140.266 1.00 25.01 ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 200.846 159.771 140.767 1.00 31.26 ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 200.622 160.578 141.678 1.00 32.16 ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 198.642 159.717 139.590 1.00 23.72 ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 197.468 158.957 138.970 1.00 23.77 ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 196.527 159.911 138.255 1.00 23.32 ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 197.967 157.883 138.020 1.00 26.81 ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 202.061 159.657 140.222 1.00 33.99 ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 203.186 160.447 140.739 1.00 32.95 ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 202.953 161.946 140.649 1.00 33.14 ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 202.997 162.653 141.661 1.00 32.30 ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 204.359 160.011 139.851 1.00 36.45 ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 203.941 158.698 139.270 1.00 33.42 ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 202.461 158.789 139.102 1.00 31.88 ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 202.701 162.440 139.441 1.00 32.12 ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 202.427 163.855 139.229 1.00 32.50 ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 201.574 164.006 137.982 1.00 34.01 ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 201.945 163.517 136.911 1.00 36.91 ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 203.723 164.660 139.088 1.00 32.77 ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 203.541 166.167 138.893 1.00 31.92 ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 203.043 166.815 140.166 1.00 31.18 ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 204.841 166.806 138.448 1.00 36.15 ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 200.440 164.682 138.122 1.00 27.92 ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 199.508 164.894 137.025 1.00 27.24 ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 199.637 166.331 136.542 1.00 28.73 ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 199.471 167.270 137.326 1.00 27.84 ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 198.074 164.599 137.464 1.00 29.23 ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 197.976 163.236 137.896 1.00 30.63 ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 197.107 164.831 136.321 1.00 27.64 ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 199.932 166.504 135.259 1.00 28.17 ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 200.042 167.819 134.650 1.00 28.06 ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 198.758 168.111 133.890 1.00 30.90 ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 198.379 167.356 132.986 1.00 36.72 ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 201.250 167.892 133.718 1.00 29.82 ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 202.546 167.422 134.346 1.00 31.37 ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 203.716 167.510 133.391 1.00 34.93 ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 203.737 168.354 132.496 1.00 34.93 ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 204.696 166.635 133.574 1.00 35.71 ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 198.091 169.194 134.272 1.00 26.88 ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 196.876 169.655 133.619 1.00 28.64 ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 197.244 170.774 132.656 1.00 30.58 ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 197.855 171.768 133.061 1.00 38.05 ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 195.857 170.145 134.647 1.00 30.99 ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 195.732 169.346 135.944 1.00 30.11 ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 194.808 170.058 136.913 1.00 27.16 ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 195.227 167.943 135.657 1.00 30.61 ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 196.887 170.603 131.386 1.00 32.72 ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 197.139 171.587 130.345 1.00 34.25 ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 195.805 172.067 129.799 1.00 36.53 ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 194.901 171.260 129.573 1.00 39.81 ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 197.986 170.994 129.217 1.00 34.07 ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 199.388 170.600 129.628 1.00 36.31 ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 200.166 170.051 128.447 1.00 37.45 ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 199.736 170.649 127.190 1.00 37.65 ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 200.553 170.979 126.198 1.00 38.98 ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 201.858 170.778 126.281 1.00 37.36 ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 200.047 171.523 125.094 1.00 37.76 ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 195.678 173.369 129.593 1.00 33.79 ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 194.470 173.949 129.021 1.00 33.13 ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 194.806 174.425 127.615 1.00 37.11 ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 195.597 175.359 127.444 1.00 41.60 ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 193.944 175.085 129.892 1.00 33.30 ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 193.396 174.611 131.199 1.00 35.66 ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 194.008 174.671 132.415 1.00 36.44 ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 192.126 173.986 131.420 1.00 37.82 ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 193.197 174.132 133.382 1.00 35.55 ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 192.036 173.704 132.796 1.00 35.34 ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 191.058 173.642 130.588 1.00 37.14 ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 190.919 173.094 133.360 1.00 33.50 ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 189.950 173.035 131.150 1.00 35.64 ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 189.889 172.769 132.522 1.00 34.10 ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 194.212 173.781 126.610 1.00 40.88 ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 194.543 174.061 125.220 1.00 43.71 ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 193.273 174.416 124.460 1.00 46.99 ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 192.162 174.053 124.850 1.00 46.80 ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 195.264 172.875 124.542 1.00 43.80 ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 196.583 172.588 125.238 1.00 45.09 ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 194.382 171.644 124.549 1.00 42.23 ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 193.454 175.144 123.361 1.00 53.80 ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 192.321 175.572 122.552 1.00 54.54 ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 191.571 174.365 122.005 1.00 54.58 ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 192.178 173.415 121.501 1.00 53.67 ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 192.800 176.463 121.405 1.00 54.61 ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 191.677 177.081 120.588 1.00 55.20 ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 190.992 178.199 121.357 1.00 56.48 ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 190.044 178.983 120.464 1.00 56.49 ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 188.874 178.167 120.040 1.00 55.51 ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 190.245 174.402 122.114 1.00 54.13 ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 189.422 173.290 121.659 1.00 55.32 ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 189.479 173.169 120.142 1.00 57.76 ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 189.378 174.166 119.422 1.00 58.21 ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 187.978 173.475 122.118 1.00 54.65 ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 187.743 173.148 123.581 1.00 55.26 ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 186.484 172.339 123.801 1.00 56.91 ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 186.260 171.326 123.138 1.00 58.06 ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 185.652 172.778 124.738 1.00 54.62 ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 189.643 171.938 119.657 1.00 52.65 ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 189.618 171.647 118.230 1.00 51.24 ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 188.385 170.851 117.824 1.00 50.83 ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 188.269 170.467 116.657 1.00 50.66 ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 190.888 170.898 117.818 1.00 51.69 ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 190.960 169.651 118.522 1.00 52.47 ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 192.122 171.727 118.137 1.00 48.26 ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 187.478 170.592 118.769 1.00 53.31 ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 186.209 169.882 118.560 1.00 54.32 ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 186.348 168.719 117.576 1.00 55.28 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 185.554 168.549 116.648 1.00 55.09 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 185.093 170.851 118.142 1.00 53.16 ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 185.432 171.671 116.906 1.00 54.96 ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 185.835 171.137 115.873 1.00 56.00 ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 185.269 172.984 117.013 1.00 53.86 ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 187.368 167.893 117.808 1.00 55.26 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 187.603 166.692 117.021 1.00 55.89 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 186.969 165.452 117.644 1.00 57.02 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 187.242 164.335 117.189 1.00 56.32 ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 189.104 166.468 116.825 1.00 57.84 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 189.757 166.439 118.100 1.00 56.97 ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 189.705 167.579 115.975 1.00 55.13 ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 186.143 165.631 118.668 1.00 59.64 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 185.463 164.536 119.386 1.00 58.15 ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 186.545 163.637 119.995 1.00 57.43 ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 187.574 164.145 120.466 1.00 56.43 ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 184.486 163.836 118.460 1.00 56.02 ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 183.375 164.734 117.943 1.00 56.40 ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 182.446 164.019 116.983 1.00 59.63 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 181.863 162.988 117.376 1.00 61.65 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 182.299 164.488 115.834 1.00 58.57 ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 186.353 162.323 120.006 1.00 55.81 ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 187.297 161.395 120.608 1.00 54.06 ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 187.981 160.562 119.532 1.00 52.98 ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 187.517 160.465 118.393 1.00 51.88 ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 186.592 160.484 121.621 1.00 52.82 ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 185.717 161.224 122.621 1.00 53.70 ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 186.481 162.345 123.310 1.00 54.06 ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 185.534 163.297 124.023 1.00 52.51 ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 186.263 164.417 124.678 1.00 51.52 ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 189.102 159.953 119.915 1.00 49.84 ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 189.891 159.116 119.022 1.00 50.69 ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 189.474 157.651 119.072 1.00 51.98 ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 190.270 156.777 118.709 1.00 49.94 ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 191.379 159.250 119.356 1.00 48.45 ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 192.298 159.199 118.145 1.00 48.95 ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 193.724 158.858 118.551 1.00 52.22 ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 194.251 159.828 119.597 1.00 51.75 ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 195.678 159.565 119.930 1.00 48.06 ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 188.253 157.364 119.527 1.00 47.40 ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 187.678 156.029 119.671 1.00 45.76 ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 188.429 155.168 120.679 1.00 46.20 ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 188.098 153.985 120.830 1.00 43.96 ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 187.596 155.277 118.334 1.00 42.52 ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 189.426 155.715 121.376 1.00 40.54 ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 190.162 154.997 122.407 1.00 37.96 ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 190.402 155.891 123.616 1.00 37.10 ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 191.367 155.696 124.361 1.00 38.34 ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 191.486 154.460 121.865 1.00 37.72 ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 192.356 155.520 121.505 1.00 37.55 ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 189.536 156.879 123.819 1.00 30.40 ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 189.663 157.845 124.903 1.00 30.51 ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 188.493 157.658 125.856 1.00 29.79 ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 187.332 157.644 125.430 1.00 29.25 ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 189.717 159.287 124.368 1.00 31.04 ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 189.493 160.283 125.493 1.00 28.83 ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 191.045 159.547 123.681 1.00 30.19 ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 188.801 157.515 127.141 1.00 22.53 ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 187.806 157.375 128.195 1.00 20.54 ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 187.781 158.660 129.009 1.00 18.35 ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 188.833 159.232 129.325 1.00 21.15 ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 188.096 156.161 129.099 1.00 20.22 ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 187.785 154.872 128.368 1.00 24.41 ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 189.542 156.170 129.566 1.00 20.02 ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 186.577 159.123 129.329 1.00 13.25 ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 186.389 160.278 130.201 1.00 10.81 ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 186.193 159.757 131.620 1.00 15.05 ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 185.104 159.315 131.990 1.00 22.00 ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 185.204 161.121 129.743 1.00 12.89 ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 185.456 161.621 128.425 1.00 18.16 ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 184.992 162.295 130.687 1.00 13.81 ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 187.249 159.805 132.403 1.00 12.49 ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 187.209 159.324 133.778 1.00 10.41 ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 186.787 160.442 134.718 1.00 10.83 ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 187.320 161.556 134.627 1.00 17.14 ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 188.563 158.785 134.213 1.00 13.89 ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 189.040 157.470 133.604 1.00 12.30 ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 190.088 156.860 134.507 1.00 12.26 ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 187.882 156.510 133.394 1.00 11.85 ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 185.837 160.187 135.612 1.00 8.12  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 185.529 161.163 136.656 1.00 8.14  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 186.668 161.278 137.653 1.00 12.32 ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 187.417 160.330 137.893 1.00 15.58 ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 184.273 160.587 137.317 1.00 9.50  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 184.368 159.125 137.075 1.00 10.88 ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 185.027 158.964 135.736 1.00 10.22 ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 186.793 162.466 138.238 1.00 14.98 ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 187.736 162.739 139.310 1.00 12.20 ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 186.918 163.303 140.456 1.00 10.91 ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 186.445 164.449 140.385 1.00 14.24 ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 188.839 163.714 138.885 1.00 12.47 ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 189.867 163.857 139.994 1.00 12.75 ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 189.495 163.247 137.602 1.00 9.72  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 186.738 162.495 141.497 1.00 11.99 ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 185.972 162.838 142.685 1.00 14.25 ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 186.897 163.371 143.772 1.00 17.15 ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 188.119 163.415 143.623 1.00 21.72 ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 185.207 161.619 143.207 1.00 12.22 ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 184.269 160.979 142.211 1.00 11.17 ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 182.997 161.490 141.997 1.00 12.58 ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 184.650 159.852 141.498 1.00 12.35 ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 182.136 160.903 141.092 1.00 12.47 ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 183.796 159.258 140.593 1.00 12.35 ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 182.542 159.787 140.394 1.00 13.81 ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 181.687 159.198 139.490 1.00 14.39 ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 186.291 163.765 144.891 1.00 15.59 ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 187.070 164.313 145.994 1.00 14.24 ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 187.640 163.212 146.881 1.00 21.26 ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 188.815 163.258 147.257 1.00 29.27 ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 186.211 165.274 146.814 1.00 14.10 ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 186.887 165.859 148.052 1.00 19.25 ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 188.108 166.668 147.657 1.00 24.86 ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 185.908 166.715 148.827 1.00 22.00 ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 186.828 162.215 147.222 1.00 21.48 ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 187.250 161.161 148.135 1.00 18.35 ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 186.662 159.837 147.660 1.00 18.92 ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 186.085 159.744 146.571 1.00 20.87 ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 186.837 161.502 149.573 1.00 17.14 ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 185.427 162.043 149.662 1.00 20.67 ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 184.648 161.935 148.717 1.00 22.61 ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 185.095 162.642 150.798 1.00 23.26 ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 186.810 158.803 148.491 1.00 17.88 ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 186.366 157.465 148.121 1.00 15.64 ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 184.850 157.337 148.092 1.00 17.05 ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 184.334 156.401 147.473 1.00 18.88 ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 186.948 156.422 149.079 1.00 16.28 ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 186.483 156.570 150.503 1.00 19.34 ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 186.896 157.638 151.283 1.00 20.67 ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 185.626 155.635 151.062 1.00 18.95 ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 186.466 157.769 152.588 1.00 21.92 ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 185.193 155.762 152.365 1.00 18.96 ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 185.614 156.830 153.129 1.00 22.74 ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 184.126 158.246 148.746 1.00 18.58 ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 182.670 158.174 148.752 1.00 16.24 ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 182.073 158.429 147.375 1.00 17.46 ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 180.918 158.056 147.140 1.00 19.94 ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 182.094 159.170 149.760 1.00 15.73 ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 182.380 160.507 149.330 1.00 18.53 ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 182.701 158.946 151.134 1.00 17.02 ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 182.829 159.050 146.469 1.00 15.32 ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 182.372 159.354 145.113 1.00 11.84 ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 181.090 160.180 145.119 1.00 15.76 ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 180.229 160.015 144.252 1.00 18.93 ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 182.179 158.075 144.290 1.00 6.78  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 183.431 157.226 144.164 1.00 7.04  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 183.370 156.342 142.934 1.00 7.61  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 184.493 155.415 142.870 1.00 8.38  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 184.802 154.688 141.805 1.00 10.45 ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 184.093 154.758 140.690 1.00 10.17 ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 185.850 153.873 141.859 1.00 9.22  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 180.959 161.078 146.093 1.00 13.71 ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 179.776 161.921 146.198 1.00 15.51 ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 179.953 163.270 145.520 1.00 18.99 ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 179.002 163.782 144.918 1.00 17.97 ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 179.408 162.136 147.668 1.00 14.73 ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 181.144 163.856 145.600 1.00 20.36 ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 181.435 165.145 144.987 1.00 18.67 ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 182.355 164.924 143.794 1.00 16.38 ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 183.468 164.416 143.952 1.00 20.40 ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 182.080 166.097 145.994 1.00 18.46 ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 181.130 166.500 147.102 1.00 23.49 ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 180.027 166.996 146.791 1.00 24.59 ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 181.484 166.317 148.285 1.00 20.47 ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 181.887 165.307 142.610 1.00 13.42 ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 182.666 165.177 141.383 1.00 10.54 ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 183.479 166.450 141.189 1.00 15.06 ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 182.919 167.519 140.927 1.00 16.83 ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 181.750 164.922 140.190 1.00 9.12  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 182.425 164.974 138.820 1.00 13.57 ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 183.283 163.745 138.615 1.00 12.22 ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 181.391 165.098 137.716 1.00 17.46 ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 184.802 166.337 141.315 1.00 14.72 ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 185.658 167.511 141.170 1.00 14.80 ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 185.736 167.928 139.707 1.00 16.41 ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 185.405 169.065 139.351 1.00 21.02 ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 187.053 167.246 141.759 1.00 15.54 ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 186.934 166.766 143.205 1.00 16.45 ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 187.901 168.502 141.700 1.00 18.10 ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 186.066 167.649 144.070 1.00 16.80 ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 186.161 167.017 138.836 1.00 15.73 ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 186.211 167.328 137.405 1.00 12.44 ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 186.302 166.028 136.611 1.00 14.84 ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 186.001 164.948 137.126 1.00 18.77 ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 187.351 168.305 137.075 1.00 14.14 ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 188.732 167.766 137.325 1.00 17.69 ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 189.210 167.600 138.613 1.00 20.12 ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 189.570 167.466 136.266 1.00 15.50 ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 190.486 167.123 138.838 1.00 18.39 ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 190.845 166.990 136.486 1.00 14.59 ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 191.303 166.816 137.772 1.00 14.37 ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 186.653 166.138 135.332 1.00 13.78 ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 186.781 164.982 134.455 1.00 14.34 ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 188.112 165.041 133.721 1.00 18.97 ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 188.649 166.121 133.463 1.00 22.36 ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 185.643 164.912 133.430 1.00 14.14 ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 185.663 166.087 132.612 1.00 19.13 ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 184.301 164.822 134.129 1.00 13.97 ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 188.641 163.865 133.382 1.00 15.94 ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 189.887 163.759 132.636 1.00 16.03 ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 189.661 162.869 131.424 1.00 20.89 ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 188.763 162.024 131.410 1.00 23.81 ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 191.041 163.207 133.500 1.00 19.60 ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 191.329 164.134 134.655 1.00 18.20 ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 190.698 161.820 134.011 1.00 20.01 ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 190.485 163.064 130.398 1.00 24.73 ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 190.450 162.249 129.191 1.00 22.69 ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 191.739 161.445 129.113 1.00 25.34 ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 192.833 162.017 129.133 1.00 29.76 ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 190.276 163.115 127.946 1.00 23.34 ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 188.872 163.666 127.811 1.00 28.38 ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 188.227 163.917 128.850 1.00 26.35 ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 188.410 163.847 126.665 1.00 33.39 ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 191.609 160.123 129.022 1.00 28.13 ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 192.756 159.224 129.030 1.00 27.58 ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 192.674 158.280 127.843 1.00 28.03 ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 191.619 157.696 127.587 1.00 31.32 ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 192.809 158.412 130.327 1.00 27.26 ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 193.639 159.036 131.408 1.00 28.63 ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 195.016 159.101 131.292 1.00 29.34 ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 193.042 159.543 132.549 1.00 27.29 ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 195.781 159.669 132.289 1.00 29.28 ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 193.803 160.110 133.549 1.00 26.04 ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 195.173 160.173 133.421 1.00 26.55 ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 193.781 158.118 127.129 1.00 31.42 ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 193.843 157.122 126.072 1.00 32.97 ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 194.110 155.749 126.674 1.00 34.61 ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 194.963 155.598 127.552 1.00 36.67 ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 194.929 157.474 125.056 1.00 34.02 ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 194.999 156.521 123.876 1.00 35.76 ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 196.049 156.925 122.860 1.00 40.95 ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 196.738 157.942 123.087 1.00 40.96 ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 196.188 156.224 121.836 1.00 41.55 ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 193.372 154.751 126.208 1.00 32.17 ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 193.489 153.398 126.736 1.00 32.23 ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 194.533 152.634 125.935 1.00 32.00 ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 194.706 152.842 124.730 1.00 32.60 ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 192.124 152.677 126.726 1.00 32.81 ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 191.578 152.577 125.301 1.00 34.52 ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 191.137 153.400 127.626 1.00 29.59 ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 190.286 151.810 125.204 1.00 33.06 ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 195.242 151.741 126.615 1.00 35.18 ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 196.340 151.000 126.015 1.00 37.89 ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 195.849 149.703 125.382 1.00 40.71 ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 194.753 149.217 125.669 1.00 39.80 ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 197.414 150.691 127.060 1.00 36.58 ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 196.690 149.147 124.517 1.00 49.27 ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 196.461 147.857 123.838 1.00 49.28 ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 195.107 147.934 123.122 1.00 47.72 ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 194.806 148.949 122.476 1.00 45.78 ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 196.596 146.717 124.829 1.00 47.44 ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 195.451 146.688 125.690 1.00 46.78 ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 197.856 146.884 125.670 1.00 44.59 ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 194.282 146.897 123.214 1.00 48.62 ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 192.977 146.853 122.566 1.00 50.79 ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 191.868 146.670 123.594 1.00 51.48 ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 190.948 145.870 123.410 1.00 53.41 ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 192.929 145.745 121.516 1.00 50.92 ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 193.628 144.464 121.934 1.00 50.61 ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 193.777 143.513 120.756 1.00 52.15 ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 194.508 144.179 119.600 1.00 51.90 ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 194.608 143.283 118.416 1.00 51.32 ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 191.948 147.410 124.695 1.00 36.81 ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 190.911 147.347 125.711 1.00 33.44 ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 189.644 148.047 125.223 1.00 34.92 ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 189.643 148.782 124.231 1.00 36.55 ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 191.400 147.969 127.017 1.00 34.34 ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 192.753 147.458 127.473 1.00 39.48 ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 192.912 147.499 128.978 1.00 38.81 ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 192.876 148.607 129.549 1.00 38.74 ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 193.076 146.422 129.588 1.00 33.24 ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 188.549 147.802 125.938 1.00 33.01 ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 187.242 148.335 125.583 1.00 29.47 ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 186.870 149.445 126.554 1.00 27.16 ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 186.869 149.213 127.772 1.00 29.00 ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 186.194 147.222 125.614 1.00 28.07 ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 184.956 147.559 124.811 1.00 30.88 ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 184.920 148.637 124.181 1.00 31.23 ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 184.013 146.741 124.809 1.00 30.94 ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 186.572 150.657 126.078 1.00 21.48 ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 186.144 151.722 127.006 1.00 22.11 ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 184.900 151.363 127.800 1.00 23.16 ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 184.736 151.837 128.935 1.00 22.47 ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 185.901 152.923 126.075 1.00 21.24 ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 185.844 152.354 124.682 1.00 25.53 ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 186.717 151.147 124.696 1.00 23.83 ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 184.015 150.539 127.235 1.00 20.78 ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 182.861 150.069 127.988 1.00 18.16 ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 183.288 149.270 129.213 1.00 17.49 ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 182.619 149.322 130.252 1.00 20.57 ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 181.970 149.214 127.090 1.00 20.43 ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 181.309 149.949 125.941 1.00 18.87 ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 180.207 149.149 125.199 1.00 19.83 ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 180.600 147.881 124.577 1.00 24.12 ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 180.908 146.747 125.201 1.00 25.56 ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 180.706 146.587 126.500 1.00 17.67 ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 181.373 145.725 124.489 1.00 22.66 ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 184.389 148.521 129.111 1.00 17.67 ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 184.920 147.816 130.274 1.00 15.55 ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 185.381 148.791 131.348 1.00 15.99 ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 185.214 148.534 132.545 1.00 21.52 ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 186.065 146.894 129.858 1.00 17.06 ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 185.605 145.885 128.975 1.00 21.20 ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 185.982 149.909 130.938 1.00 15.15 ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 186.354 150.940 131.900 1.00 12.60 ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 185.122 151.526 132.575 1.00 10.56 ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 185.127 151.779 133.786 1.00 11.29 ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 187.158 152.039 131.205 1.00 14.64 ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 188.618 151.722 131.058 1.00 15.57 ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 189.055 150.831 130.094 1.00 16.04 ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 189.554 152.316 131.886 1.00 14.86 ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 190.396 150.538 129.958 1.00 15.26 ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 190.895 152.027 131.755 1.00 16.40 ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 191.316 151.138 130.791 1.00 17.43 ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 184.056 151.757 131.804 1.00 13.98 ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 182.832 152.295 132.393 1.00 11.92 ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 182.209 151.309 133.372 1.00 10.67 ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 181.735 151.704 134.443 1.00 12.13 ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 181.828 152.660 131.297 1.00 10.63 ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 182.355 153.604 130.240 1.00 10.67 ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 183.426 154.450 130.496 1.00 11.64 ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 181.778 153.649 128.979 1.00 9.69  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 183.908 155.308 129.528 1.00 11.59 ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 182.251 154.503 128.006 1.00 13.49 ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 183.316 155.330 128.284 1.00 15.13 ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 183.786 156.183 127.312 1.00 17.49 ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 182.207 150.021 133.026 1.00 11.72 ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 181.515 149.018 133.830 1.00 7.95  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 182.267 148.667 135.106 1.00 8.36  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 181.640 148.287 136.101 1.00 13.29 ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 181.283 147.757 133.000 1.00 6.93  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 180.080 147.842 132.084 1.00 8.56  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 180.024 146.698 131.098 1.00 17.22 ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 180.737 145.695 131.314 1.00 18.32 ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 179.269 146.796 130.109 1.00 19.85 ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 183.592 148.776 135.103 1.00 6.76  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 184.398 148.421 136.264 1.00 6.01  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 184.545 149.565 137.256 1.00 9.62  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 185.216 149.396 138.279 1.00 15.66 ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 185.780 147.941 135.817 1.00 4.54  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 185.768 146.567 135.177 1.00 8.77  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 187.149 146.154 134.716 1.00 12.38 ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 188.086 146.048 135.827 1.00 12.76 ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 188.921 145.034 136.005 1.00 13.88 ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 188.965 144.019 135.159 1.00 12.23 ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 189.736 145.043 137.055 1.00 15.10 ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 183.941 150.716 136.984 1.00 5.44  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 184.005 151.840 137.900 1.00 6.57  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 185.382 152.447 138.058 1.00 10.13 ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 185.749 152.861 139.165 1.00 14.16 ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 186.157 152.509 136.976 1.00 8.98  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 187.459 153.160 137.020 1.00 6.49  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 187.259 154.659 137.185 1.00 8.95  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 186.468 155.278 136.459 1.00 12.43 ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 188.264 152.839 135.753 1.00 6.90  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 189.640 153.470 135.825 1.00 11.57 ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 188.372 151.337 135.561 1.00 13.49 ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 187.967 155.253 138.140 1.00 7.47  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 187.782 156.670 138.431 1.00 8.76  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 189.093 157.241 138.957 1.00 10.44 ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 190.131 156.576 138.944 1.00 17.16 ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 186.627 156.872 139.420 1.00 9.96  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 189.047 158.491 139.412 1.00 7.88  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 190.188 159.156 140.027 1.00 7.90  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 189.714 159.835 141.303 1.00 14.98 ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 188.644 160.455 141.327 1.00 17.96 ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 190.844 160.179 139.075 1.00 9.23  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 192.046 160.832 139.736 1.00 12.86 ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 191.256 159.515 137.772 1.00 10.49 ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 190.502 159.711 142.367 1.00 14.17 ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 190.200 160.314 143.654 1.00 14.29 ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 191.250 161.361 143.990 1.00 16.70 ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 192.448 161.141 143.781 1.00 20.23 ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 190.145 159.261 144.762 1.00 16.16 ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 189.233 158.058 144.526 1.00 13.67 ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 189.172 157.192 145.771 1.00 15.85 ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 187.841 158.501 144.109 1.00 14.62 ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 190.796 162.501 144.512 1.00 17.93 ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 191.724 163.560 144.890 1.00 20.84 ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 192.507 163.205 146.148 1.00 23.19 ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 193.609 163.722 146.354 1.00 26.60 ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 190.972 164.876 145.088 1.00 21.38 ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 190.416 165.656 143.555 1.00 36.74 ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 191.962 162.335 146.993 1.00 25.38 ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 192.647 161.927 148.215 1.00 28.60 ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 192.329 160.482 148.575 1.00 26.76 ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 191.359 159.906 148.082 1.00 27.45 ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 192.273 162.835 149.402 1.00 29.67 ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 193.048 162.467 150.550 1.00 31.09 ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 190.796 162.702 149.735 1.00 25.87 ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . ADP B 2 .    ? 162.343 174.631 141.391 1.00 0.03  ? 4701 ADP A PB    1 
HETATM 23595 O  O1B   . ADP B 2 .    ? 163.338 174.861 142.477 1.00 0.73  ? 4701 ADP A O1B   1 
HETATM 23596 O  O2B   . ADP B 2 .    ? 162.709 173.477 140.527 1.00 1.20  ? 4701 ADP A O2B   1 
HETATM 23597 O  O3B   . ADP B 2 .    ? 160.935 174.554 141.903 1.00 0.36  ? 4701 ADP A O3B   1 
HETATM 23598 P  PA    . ADP B 2 .    ? 161.473 176.530 139.312 1.00 0.07  ? 4701 ADP A PA    1 
HETATM 23599 O  O1A   . ADP B 2 .    ? 160.872 175.406 138.553 1.00 0.10  ? 4701 ADP A O1A   1 
HETATM 23600 O  O2A   . ADP B 2 .    ? 160.569 177.542 139.920 1.00 11.38 ? 4701 ADP A O2A   1 
HETATM 23601 O  O3A   . ADP B 2 .    ? 162.425 175.920 140.441 1.00 0.72  ? 4701 ADP A O3A   1 
HETATM 23602 O  "O5'" . ADP B 2 .    ? 162.545 177.257 138.386 1.00 1.64  ? 4701 ADP A "O5'" 1 
HETATM 23603 C  "C5'" . ADP B 2 .    ? 163.468 178.213 138.945 1.00 0.68  ? 4701 ADP A "C5'" 1 
HETATM 23604 C  "C4'" . ADP B 2 .    ? 163.658 179.341 137.964 1.00 0.84  ? 4701 ADP A "C4'" 1 
HETATM 23605 O  "O4'" . ADP B 2 .    ? 164.250 178.813 136.752 1.00 2.06  ? 4701 ADP A "O4'" 1 
HETATM 23606 C  "C3'" . ADP B 2 .    ? 162.378 180.051 137.510 1.00 0.86  ? 4701 ADP A "C3'" 1 
HETATM 23607 O  "O3'" . ADP B 2 .    ? 162.624 181.428 137.274 1.00 9.72  ? 4701 ADP A "O3'" 1 
HETATM 23608 C  "C2'" . ADP B 2 .    ? 162.067 179.341 136.194 1.00 0.35  ? 4701 ADP A "C2'" 1 
HETATM 23609 O  "O2'" . ADP B 2 .    ? 161.220 180.090 135.354 1.00 1.76  ? 4701 ADP A "O2'" 1 
HETATM 23610 C  "C1'" . ADP B 2 .    ? 163.476 179.191 135.641 1.00 0.82  ? 4701 ADP A "C1'" 1 
HETATM 23611 N  N9    . ADP B 2 .    ? 163.603 178.153 134.628 1.00 0.92  ? 4701 ADP A N9    1 
HETATM 23612 C  C8    . ADP B 2 .    ? 163.765 176.813 134.859 1.00 0.23  ? 4701 ADP A C8    1 
HETATM 23613 N  N7    . ADP B 2 .    ? 163.860 176.107 133.765 1.00 0.11  ? 4701 ADP A N7    1 
HETATM 23614 C  C5    . ADP B 2 .    ? 163.763 177.039 132.744 1.00 0.16  ? 4701 ADP A C5    1 
HETATM 23615 C  C6    . ADP B 2 .    ? 163.795 176.914 131.346 1.00 0.17  ? 4701 ADP A C6    1 
HETATM 23616 N  N6    . ADP B 2 .    ? 163.942 175.757 130.713 1.00 0.22  ? 4701 ADP A N6    1 
HETATM 23617 N  N1    . ADP B 2 .    ? 163.669 178.042 130.615 1.00 0.27  ? 4701 ADP A N1    1 
HETATM 23618 C  C2    . ADP B 2 .    ? 163.525 179.204 131.257 1.00 0.30  ? 4701 ADP A C2    1 
HETATM 23619 N  N3    . ADP B 2 .    ? 163.480 179.440 132.562 1.00 0.25  ? 4701 ADP A N3    1 
HETATM 23620 C  C4    . ADP B 2 .    ? 163.606 178.305 133.264 1.00 0.29  ? 4701 ADP A C4    1 
HETATM 23621 P  PG    . ATP C 3 .    ? 168.747 195.322 163.905 1.00 18.91 ? 4702 ATP A PG    1 
HETATM 23622 O  O1G   . ATP C 3 .    ? 169.273 194.240 163.026 1.00 25.02 ? 4702 ATP A O1G   1 
HETATM 23623 O  O2G   . ATP C 3 .    ? 167.305 195.611 163.670 1.00 31.29 ? 4702 ATP A O2G   1 
HETATM 23624 O  O3G   . ATP C 3 .    ? 169.070 195.117 165.341 1.00 28.02 ? 4702 ATP A O3G   1 
HETATM 23625 P  PB    . ATP C 3 .    ? 169.107 197.561 162.211 1.00 8.75  ? 4702 ATP A PB    1 
HETATM 23626 O  O1B   . ATP C 3 .    ? 170.022 197.191 161.112 1.00 30.88 ? 4702 ATP A O1B   1 
HETATM 23627 O  O2B   . ATP C 3 .    ? 167.635 197.478 162.024 1.00 28.96 ? 4702 ATP A O2B   1 
HETATM 23628 O  O3B   . ATP C 3 .    ? 169.474 196.664 163.471 1.00 25.36 ? 4702 ATP A O3B   1 
HETATM 23629 P  PA    . ATP C 3 .    ? 168.745 200.431 162.630 1.00 16.64 ? 4702 ATP A PA    1 
HETATM 23630 O  O1A   . ATP C 3 .    ? 167.322 200.259 163.024 1.00 32.10 ? 4702 ATP A O1A   1 
HETATM 23631 O  O2A   . ATP C 3 .    ? 169.040 201.074 161.330 1.00 28.64 ? 4702 ATP A O2A   1 
HETATM 23632 O  O3A   . ATP C 3 .    ? 169.500 199.028 162.698 1.00 20.57 ? 4702 ATP A O3A   1 
HETATM 23633 O  "O5'" . ATP C 3 .    ? 169.501 201.218 163.788 1.00 31.03 ? 4702 ATP A "O5'" 1 
HETATM 23634 C  "C5'" . ATP C 3 .    ? 170.926 201.385 163.713 1.00 26.46 ? 4702 ATP A "C5'" 1 
HETATM 23635 C  "C4'" . ATP C 3 .    ? 171.314 202.496 164.652 1.00 29.48 ? 4702 ATP A "C4'" 1 
HETATM 23636 O  "O4'" . ATP C 3 .    ? 171.967 203.544 163.895 1.00 34.38 ? 4702 ATP A "O4'" 1 
HETATM 23637 C  "C3'" . ATP C 3 .    ? 170.148 203.221 165.317 1.00 29.19 ? 4702 ATP A "C3'" 1 
HETATM 23638 O  "O3'" . ATP C 3 .    ? 170.608 204.079 166.346 1.00 34.70 ? 4702 ATP A "O3'" 1 
HETATM 23639 C  "C2'" . ATP C 3 .    ? 169.710 204.109 164.165 1.00 29.06 ? 4702 ATP A "C2'" 1 
HETATM 23640 O  "O2'" . ATP C 3 .    ? 168.843 205.136 164.586 1.00 30.70 ? 4702 ATP A "O2'" 1 
HETATM 23641 C  "C1'" . ATP C 3 .    ? 171.074 204.619 163.718 1.00 29.03 ? 4702 ATP A "C1'" 1 
HETATM 23642 N  N9    . ATP C 3 .    ? 171.105 204.999 162.327 1.00 28.99 ? 4702 ATP A N9    1 
HETATM 23643 C  C8    . ATP C 3 .    ? 170.510 204.355 161.281 1.00 31.06 ? 4702 ATP A C8    1 
HETATM 23644 N  N7    . ATP C 3 .    ? 170.693 204.971 160.139 1.00 28.18 ? 4702 ATP A N7    1 
HETATM 23645 C  C5    . ATP C 3 .    ? 171.440 206.093 160.466 1.00 26.99 ? 4702 ATP A C5    1 
HETATM 23646 C  C6    . ATP C 3 .    ? 171.949 207.150 159.697 1.00 26.51 ? 4702 ATP A C6    1 
HETATM 23647 N  N6    . ATP C 3 .    ? 171.784 207.252 158.384 1.00 28.24 ? 4702 ATP A N6    1 
HETATM 23648 N  N1    . ATP C 3 .    ? 172.648 208.107 160.348 1.00 27.69 ? 4702 ATP A N1    1 
HETATM 23649 C  C2    . ATP C 3 .    ? 172.809 207.999 161.670 1.00 24.95 ? 4702 ATP A C2    1 
HETATM 23650 N  N3    . ATP C 3 .    ? 172.375 207.053 162.493 1.00 26.23 ? 4702 ATP A N3    1 
HETATM 23651 C  C4    . ATP C 3 .    ? 171.687 206.123 161.816 1.00 27.46 ? 4702 ATP A C4    1 
HETATM 23652 P  PB    . ADP D 2 .    ? 169.547 186.863 192.947 1.00 1.42  ? 4703 ADP A PB    1 
HETATM 23653 O  O1B   . ADP D 2 .    ? 168.243 187.118 192.307 1.00 2.50  ? 4703 ADP A O1B   1 
HETATM 23654 O  O2B   . ADP D 2 .    ? 169.735 185.437 193.259 1.00 7.54  ? 4703 ADP A O2B   1 
HETATM 23655 O  O3B   . ADP D 2 .    ? 170.673 187.421 192.180 1.00 6.87  ? 4703 ADP A O3B   1 
HETATM 23656 P  PA    . ADP D 2 .    ? 168.662 187.566 195.636 1.00 9.87  ? 4703 ADP A PA    1 
HETATM 23657 O  O1A   . ADP D 2 .    ? 168.192 188.914 196.035 1.00 2.20  ? 4703 ADP A O1A   1 
HETATM 23658 O  O2A   . ADP D 2 .    ? 167.644 186.510 195.421 1.00 4.42  ? 4703 ADP A O2A   1 
HETATM 23659 O  O3A   . ADP D 2 .    ? 169.558 187.664 194.325 1.00 5.22  ? 4703 ADP A O3A   1 
HETATM 23660 O  "O5'" . ADP D 2 .    ? 169.705 187.054 196.718 1.00 11.70 ? 4703 ADP A "O5'" 1 
HETATM 23661 C  "C5'" . ADP D 2 .    ? 170.697 187.984 197.172 1.00 4.23  ? 4703 ADP A "C5'" 1 
HETATM 23662 C  "C4'" . ADP D 2 .    ? 171.187 187.537 198.520 1.00 2.69  ? 4703 ADP A "C4'" 1 
HETATM 23663 O  "O4'" . ADP D 2 .    ? 172.372 188.298 198.850 1.00 2.70  ? 4703 ADP A "O4'" 1 
HETATM 23664 C  "C3'" . ADP D 2 .    ? 170.212 187.756 199.679 1.00 4.96  ? 4703 ADP A "C3'" 1 
HETATM 23665 O  "O3'" . ADP D 2 .    ? 170.258 186.672 200.586 1.00 7.97  ? 4703 ADP A "O3'" 1 
HETATM 23666 C  "C2'" . ADP D 2 .    ? 170.771 188.999 200.363 1.00 3.34  ? 4703 ADP A "C2'" 1 
HETATM 23667 O  "O2'" . ADP D 2 .    ? 170.449 189.049 201.732 1.00 8.78  ? 4703 ADP A "O2'" 1 
HETATM 23668 C  "C1'" . ADP D 2 .    ? 172.262 188.817 200.146 1.00 3.08  ? 4703 ADP A "C1'" 1 
HETATM 23669 N  N9    . ADP D 2 .    ? 172.989 190.072 200.150 1.00 2.26  ? 4703 ADP A N9    1 
HETATM 23670 C  C8    . ADP D 2 .    ? 174.012 190.416 199.312 1.00 4.47  ? 4703 ADP A C8    1 
HETATM 23671 N  N7    . ADP D 2 .    ? 174.465 191.622 199.522 1.00 6.36  ? 4703 ADP A N7    1 
HETATM 23672 C  C5    . ADP D 2 .    ? 173.692 192.107 200.564 1.00 1.77  ? 4703 ADP A C5    1 
HETATM 23673 C  C6    . ADP D 2 .    ? 173.687 193.332 201.248 1.00 5.58  ? 4703 ADP A C6    1 
HETATM 23674 N  N6    . ADP D 2 .    ? 174.510 194.338 200.979 1.00 6.48  ? 4703 ADP A N6    1 
HETATM 23675 N  N1    . ADP D 2 .    ? 172.787 193.481 202.244 1.00 9.11  ? 4703 ADP A N1    1 
HETATM 23676 C  C2    . ADP D 2 .    ? 171.958 192.470 202.513 1.00 5.44  ? 4703 ADP A C2    1 
HETATM 23677 N  N3    . ADP D 2 .    ? 171.872 191.282 201.937 1.00 2.59  ? 4703 ADP A N3    1 
HETATM 23678 C  C4    . ADP D 2 .    ? 172.774 191.158 200.957 1.00 1.44  ? 4703 ADP A C4    1 
HETATM 23679 P  PB    . ADP E 2 .    ? 158.219 157.322 198.985 1.00 11.52 ? 4704 ADP A PB    1 
HETATM 23680 O  O1B   . ADP E 2 .    ? 159.606 157.883 198.960 1.00 10.27 ? 4704 ADP A O1B   1 
HETATM 23681 O  O2B   . ADP E 2 .    ? 157.170 158.376 198.984 1.00 11.77 ? 4704 ADP A O2B   1 
HETATM 23682 O  O3B   . ADP E 2 .    ? 157.988 156.283 197.938 1.00 9.47  ? 4704 ADP A O3B   1 
HETATM 23683 P  PA    . ADP E 2 .    ? 156.716 156.248 201.185 1.00 4.68  ? 4704 ADP A PA    1 
HETATM 23684 O  O1A   . ADP E 2 .    ? 156.887 156.782 202.560 1.00 0.99  ? 4704 ADP A O1A   1 
HETATM 23685 O  O2A   . ADP E 2 .    ? 155.540 156.689 200.387 1.00 6.80  ? 4704 ADP A O2A   1 
HETATM 23686 O  O3A   . ADP E 2 .    ? 158.054 156.572 200.380 1.00 10.92 ? 4704 ADP A O3A   1 
HETATM 23687 O  "O5'" . ADP E 2 .    ? 156.723 154.653 201.242 1.00 13.06 ? 4704 ADP A "O5'" 1 
HETATM 23688 C  "C5'" . ADP E 2 .    ? 155.542 154.002 201.773 1.00 9.74  ? 4704 ADP A "C5'" 1 
HETATM 23689 C  "C4'" . ADP E 2 .    ? 155.957 152.822 202.615 1.00 8.24  ? 4704 ADP A "C4'" 1 
HETATM 23690 O  "O4'" . ADP E 2 .    ? 157.259 153.077 203.178 1.00 7.35  ? 4704 ADP A "O4'" 1 
HETATM 23691 C  "C3'" . ADP E 2 .    ? 155.108 152.546 203.858 1.00 7.74  ? 4704 ADP A "C3'" 1 
HETATM 23692 O  "O3'" . ADP E 2 .    ? 153.988 151.718 203.569 1.00 12.16 ? 4704 ADP A "O3'" 1 
HETATM 23693 C  "C2'" . ADP E 2 .    ? 156.091 151.859 204.816 1.00 11.88 ? 4704 ADP A "C2'" 1 
HETATM 23694 O  "O2'" . ADP E 2 .    ? 155.887 150.466 204.899 1.00 13.30 ? 4704 ADP A "O2'" 1 
HETATM 23695 C  "C1'" . ADP E 2 .    ? 157.465 152.159 204.219 1.00 5.57  ? 4704 ADP A "C1'" 1 
HETATM 23696 N  N9    . ADP E 2 .    ? 158.397 152.762 205.159 1.00 7.36  ? 4704 ADP A N9    1 
HETATM 23697 C  C8    . ADP E 2 .    ? 159.151 153.881 204.933 1.00 10.49 ? 4704 ADP A C8    1 
HETATM 23698 N  N7    . ADP E 2 .    ? 159.924 154.199 205.939 1.00 14.99 ? 4704 ADP A N7    1 
HETATM 23699 C  C5    . ADP E 2 .    ? 159.683 153.214 206.881 1.00 11.17 ? 4704 ADP A C5    1 
HETATM 23700 C  C6    . ADP E 2 .    ? 160.208 152.993 208.165 1.00 9.69  ? 4704 ADP A C6    1 
HETATM 23701 N  N6    . ADP E 2 .    ? 161.110 153.781 208.740 1.00 6.19  ? 4704 ADP A N6    1 
HETATM 23702 N  N1    . ADP E 2 .    ? 159.756 151.916 208.844 1.00 9.82  ? 4704 ADP A N1    1 
HETATM 23703 C  C2    . ADP E 2 .    ? 158.844 151.133 208.261 1.00 9.21  ? 4704 ADP A C2    1 
HETATM 23704 N  N3    . ADP E 2 .    ? 158.279 151.243 207.064 1.00 8.57  ? 4704 ADP A N3    1 
HETATM 23705 C  C4    . ADP E 2 .    ? 158.745 152.319 206.412 1.00 8.34  ? 4704 ADP A C4    1 
HETATM 23706 MG MG    . MG  F 4 .    ? 159.282 174.375 142.485 1.00 30.00 ? 4705 MG  A MG    1 
HETATM 23707 MG MG    . MG  G 4 .    ? 165.612 197.026 162.267 1.00 10.72 ? 4706 MG  A MG    1 
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