data_9BMF
# 
_entry.id   9BMF 
# 
_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   9BMF         pdb_00009bmf 10.2210/pdb9bmf/pdb 
WWPDB D_1000283524 ?            ?                   
EMDB  EMD-44697    ?            ?                   
# 
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                        9BMF 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-1(phi motor) of full-length human dynein-1 in 5mM ATPVi' 
_pdbx_database_related.db_id          EMD-44697 
_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 'ADP ORTHOVANADATE'                  544.156    1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    2 ? ? ? ? 
5 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 'ADP ORTHOVANADATE'         AOV 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
5 '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  
AOV non-polymer         . 'ADP ORTHOVANADATE'         ? 'C10 H17 N5 O14 P2 V' 544.156 
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 AOV ? ? AOV ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
4 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 AOV 1 4701 4701 AOV AOV A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 4 ADP 1 4703 4703 ADP ADP A . 
E 4 ADP 1 4704 4704 ADP ADP A . 
F 5 MG  1 4705 4705 MG  MG  A . 
G 5 MG  1 4706 4707 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                   9BMF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BMF 
_struct.title                        'State-1(phi motor) of full-length human dynein-1 in 5mM ATPVi' 
_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        9BMF 
_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 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BMF 
_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 PRO A 1511 ? VAL A 1515 ? PRO A 1511 VAL A 1515 5 ? 5  
HELX_P HELX_P4   AA4 PHE A 1516 ? SER A 1554 ? PHE A 1516 SER A 1554 1 ? 39 
HELX_P HELX_P5   AA5 ASP A 1556 ? LEU A 1561 ? ASP A 1556 LEU A 1561 1 ? 6  
HELX_P HELX_P6   AA6 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P7   AA7 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P8   AA8 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 ASN A 1646 ? GLN A 1651 ? ASN A 1646 GLN A 1651 5 ? 6  
HELX_P HELX_P13  AB4 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P14  AB5 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P15  AB6 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P16  AB7 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P17  AB8 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P18  AB9 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P19  AC1 PRO A 1801 ? LYS A 1829 ? PRO A 1801 LYS A 1829 1 ? 29 
HELX_P HELX_P20  AC2 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P21  AC3 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P22  AC4 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P23  AC5 LYS A 1912 ? LEU A 1923 ? LYS A 1912 LEU A 1923 1 ? 12 
HELX_P HELX_P24  AC6 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P25  AC7 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P26  AC8 GLU A 1964 ? SER A 1986 ? GLU A 1964 SER A 1986 1 ? 23 
HELX_P HELX_P27  AC9 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P28  AD1 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P29  AD2 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P30  AD3 GLY A 2089 ? GLY A 2119 ? GLY A 2089 GLY A 2119 1 ? 31 
HELX_P HELX_P31  AD4 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P32  AD5 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P33  AD6 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P34  AD7 VAL A 2150 ? GLU A 2152 ? VAL A 2150 GLU A 2152 5 ? 3  
HELX_P HELX_P35  AD8 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P36  AD9 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P37  AE1 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P38  AE2 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P39  AE3 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P40  AE4 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P41  AE5 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P42  AE6 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P43  AE7 ASN A 2314 ? ASN A 2316 ? ASN A 2314 ASN A 2316 5 ? 3  
HELX_P HELX_P44  AE8 THR A 2352 ? SER A 2357 ? THR A 2352 SER A 2357 1 ? 6  
HELX_P HELX_P45  AE9 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P46  AF1 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P47  AF2 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P48  AF3 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P49  AF4 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P50  AF5 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P51  AF6 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P52  AF7 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P53  AF8 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P54  AF9 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P55  AG1 GLY A 2600 ? ARG A 2610 ? GLY A 2600 ARG A 2610 1 ? 11 
HELX_P HELX_P56  AG2 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P57  AG3 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P58  AG4 SER A 2724 ? VAL A 2731 ? SER A 2724 VAL A 2731 1 ? 8  
HELX_P HELX_P59  AG5 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P60  AG6 ARG A 2757 ? THR A 2764 ? ARG A 2757 THR A 2764 5 ? 8  
HELX_P HELX_P61  AG7 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P62  AG8 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P63  AG9 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P64  AH1 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P65  AH2 ASP A 2862 ? MET A 2867 ? ASP A 2862 MET A 2867 1 ? 6  
HELX_P HELX_P66  AH3 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P67  AH4 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P68  AH5 GLY A 2942 ? GLY A 2955 ? GLY A 2942 GLY A 2955 1 ? 14 
HELX_P HELX_P69  AH6 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P70  AH7 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P71  AH8 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P72  AH9 GLY A 3023 ? GLU A 3040 ? GLY A 3023 GLU A 3040 1 ? 18 
HELX_P HELX_P73  AI1 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P74  AI2 SER A 3072 ? SER A 3082 ? SER A 3072 SER A 3082 1 ? 11 
HELX_P HELX_P75  AI3 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P76  AI4 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P77  AI5 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P78  AI6 THR A 3172 ? LYS A 3242 ? THR A 3172 LYS A 3242 1 ? 71 
HELX_P HELX_P79  AI7 GLU A 3450 ? LEU A 3482 ? GLU A 3450 LEU A 3482 1 ? 33 
HELX_P HELX_P80  AI8 LEU A 3482 ? THR A 3495 ? LEU A 3482 THR A 3495 1 ? 14 
HELX_P HELX_P81  AI9 THR A 3495 ? THR A 3502 ? THR A 3495 THR A 3502 1 ? 8  
HELX_P HELX_P82  AJ1 THR A 3502 ? ALA A 3517 ? THR A 3502 ALA A 3517 1 ? 16 
HELX_P HELX_P83  AJ2 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P84  AJ3 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P85  AJ4 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P86  AJ5 ASP A 3570 ? LEU A 3580 ? ASP A 3570 LEU A 3580 1 ? 11 
HELX_P HELX_P87  AJ6 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P88  AJ7 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P89  AJ8 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P90  AJ9 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P91  AK1 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P92  AK2 PRO A 3689 ? ARG A 3695 ? PRO A 3689 ARG A 3695 1 ? 7  
HELX_P HELX_P93  AK3 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P94  AK4 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P95  AK5 ASP A 3763 ? TYR A 3801 ? ASP A 3763 TYR A 3801 1 ? 39 
HELX_P HELX_P96  AK6 TYR A 3801 ? SER A 3817 ? TYR A 3801 SER A 3817 1 ? 17 
HELX_P HELX_P97  AK7 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P98  AK8 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P99  AK9 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P100 AL1 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P101 AL2 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P102 AL3 ASP A 3879 ? GLY A 3894 ? ASP A 3879 GLY A 3894 1 ? 16 
HELX_P HELX_P103 AL4 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P104 AL5 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P105 AL6 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P106 AL7 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P107 AL8 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P108 AL9 SER A 3965 ? THR A 3969 ? SER A 3965 THR A 3969 5 ? 5  
HELX_P HELX_P109 AM1 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P110 AM2 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P111 AM3 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P112 AM4 ASP A 4026 ? GLU A 4034 ? ASP A 4026 GLU A 4034 1 ? 9  
HELX_P HELX_P113 AM5 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P114 AM6 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P115 AM7 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P116 AM8 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P117 AM9 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P118 AN1 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P119 AN2 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P120 AN3 GLU A 4175 ? LEU A 4194 ? GLU A 4175 LEU A 4194 1 ? 20 
HELX_P HELX_P121 AN4 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P122 AN5 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P123 AN6 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P124 AN7 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P125 AN8 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P126 AN9 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P127 AO1 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P128 AO2 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P129 AO3 ASN A 4326 ? MET A 4346 ? ASN A 4326 MET A 4346 1 ? 21 
HELX_P HELX_P130 AO4 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P131 AO5 THR A 4401 ? ASP A 4407 ? THR A 4401 ASP A 4407 1 ? 7  
HELX_P HELX_P132 AO6 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P133 AO7 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P134 AO8 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P135 AO9 ALA A 4501 ? ASN A 4506 ? ALA A 4501 ASN A 4506 1 ? 6  
HELX_P HELX_P136 AP1 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P137 AP2 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 2231 OG  ? ? ? 1_555 F MG . MG ? ? A SER 2231 A MG 4705 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc2 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 F MG . MG ? ? A GLU 2344 A MG 4705 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc3 metalc ? ? B AOV .    O3B ? ? ? 1_555 G MG . MG ? ? A AOV 4701 A MG 4706 1_555 ? ? ? ? ? ? ? 2.583 ? ? 
metalc4 metalc ? ? B AOV .    O3G ? ? ? 1_555 G MG . MG ? ? A AOV 4701 A MG 4706 1_555 ? ? ? ? ? ? ? 2.923 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.897 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 74.9  ? 
2 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 132.7 ? 
3 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 92.7  ? 
4 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 56.8  ? 
5 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 74.2  ? 
6 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 75.9  ? 
7 O3B ? B AOV .    ? A AOV 4701 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3G ? B AOV .    ? A AOV 4701 ? 1_555 62.7  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 3 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? parallel      
AC2 3 4 ? anti-parallel 
AC2 4 5 ? parallel      
AC2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 1476 ? 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 ? GLU A 2000 ? THR A 1998 GLU A 2000 
AA6 2 GLN A 2005 ? LYS A 2007 ? GLN A 2005 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB3 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB5 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 PRO A 3632 ? GLN A 3636 ? PRO A 3632 GLN A 3636 
AB6 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB6 4 TYR A 3586 ? ILE A 3590 ? TYR A 3586 ILE A 3590 
AB6 5 VAL A 3696 ? ASN A 3700 ? VAL A 3696 ASN A 3700 
AB7 1 VAL A 3653 ? THR A 3656 ? VAL A 3653 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? MET A 4128 ? ARG A 4123 MET A 4128 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC2 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 1476 ? N ASP A 1476 O ARG A 1488 ? O ARG A 1488 
AA2 1 2 N ILE A 1665 ? N ILE A 1665 O GLY A 1675 ? O GLY A 1675 
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 MET A 1861 ? N MET A 1861 O ALA A 1864 ? O ALA A 1864 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N GLY A 1955 ? N GLY A 1955 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N ILE A 2254 ? N ILE A 2254 O VAL A 2302 ? O VAL A 2302 
AA7 2 3 N ILE A 2301 ? N ILE A 2301 O MET A 2342 ? O MET A 2342 
AA7 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA7 4 5 N GLY A 2219 ? N GLY A 2219 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N LEU A 2659 ? N LEU A 2659 O GLN A 2707 ? O GLN A 2707 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB3 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N MET A 2994 ? N MET A 2994 O VAL A 3065 ? O VAL A 3065 
AB5 3 4 O VAL A 3064 ? O VAL A 3064 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 O PHE A 4125 ? O PHE A 4125 
AB8 3 4 O LEU A 4126 ? O LEU A 4126 N MET A 4043 ? N MET A 4043 
AB8 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB9 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O GLY A 4559 ? O GLY A 4559 
AC1 2 3 N PHE A 4558 ? N PHE A 4558 O LEU A 4590 ? O LEU A 4590 
AC1 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AC2 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O VAL A 4622 ? O VAL A 4622 N LEU A 4607 ? N LEU A 4607 
AC2 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
# 
_pdbx_entry_details.entry_id                   9BMF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    1835 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE1 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    1837 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 1643 ? ? -96.72  34.40   
2  1 ALA A 1862 ? ? 59.33   -123.09 
3  1 ASN A 2130 ? ? -94.42  56.65   
4  1 PHE A 2427 ? ? -91.90  56.88   
5  1 ASP A 2505 ? ? -99.84  34.10   
6  1 ASP A 2672 ? ? -69.28  -178.60 
7  1 VAL A 2838 ? ? -95.72  -61.47  
8  1 ASN A 2860 ? ? 35.44   48.86   
9  1 ASP A 2906 ? ? -91.01  54.00   
10 1 ALA A 3013 ? ? -93.21  -60.23  
11 1 LEU A 3115 ? ? 48.48   27.27   
12 1 LYS A 3608 ? ? 60.54   60.48   
13 1 SER A 3640 ? ? -103.67 40.38   
14 1 ASP A 3946 ? ? -99.02  34.01   
15 1 GLU A 4206 ? ? -94.93  54.67   
16 1 ASN A 4597 ? ? 35.00   47.17   
17 1 GLU A 4599 ? ? 63.13   177.44  
18 1 ALA A 4602 ? ? 67.44   -1.14   
19 1 THR A 4628 ? ? 53.90   -141.53 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMF 
_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                    9BMF 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.8 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               266214 
_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 ATPVi' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'state-1 (phi motor) of full-length human dynein-1 in 5mM ATPVi' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BMF 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             5000 
_em_imaging.calibrated_defocus_min          3000 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           45000 
_em_imaging.calibrated_magnification        45000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            30 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BMF 
_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                9BMF 
_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  
AOV PB     P  N N 56  
AOV O1B    O  N N 57  
AOV O2B    O  N N 58  
AOV O3B    O  N N 59  
AOV PA     P  N N 60  
AOV O1A    O  N N 61  
AOV O2A    O  N N 62  
AOV O3A    O  N N 63  
AOV "O5'"  O  N N 64  
AOV "C5'"  C  N N 65  
AOV "C4'"  C  N R 66  
AOV "O4'"  O  N N 67  
AOV "C3'"  C  N S 68  
AOV "O3'"  O  N N 69  
AOV "C2'"  C  N R 70  
AOV "O2'"  O  N N 71  
AOV "C1'"  C  N R 72  
AOV N9     N  Y N 73  
AOV C8     C  Y N 74  
AOV N7     N  Y N 75  
AOV C5     C  Y N 76  
AOV C6     C  Y N 77  
AOV N6     N  N N 78  
AOV N1     N  Y N 79  
AOV C2     C  Y N 80  
AOV N3     N  Y N 81  
AOV C4     C  Y N 82  
AOV VG     V  N N 83  
AOV O1G    O  N N 84  
AOV O2G    O  N N 85  
AOV O3G    O  N N 86  
AOV O4G    O  N N 87  
AOV H2B    H  N N 88  
AOV H2A    H  N N 89  
AOV "H5'1" H  N N 90  
AOV "H5'2" H  N N 91  
AOV "H4'"  H  N N 92  
AOV "H3'"  H  N N 93  
AOV "H1'"  H  N N 94  
AOV HA     H  N N 95  
AOV "H2'"  H  N N 96  
AOV HB     H  N N 97  
AOV H8     H  N N 98  
AOV H61N   H  N N 99  
AOV H62N   H  N N 100 
AOV H2     H  N N 101 
AOV H2G1   H  N N 102 
AOV H3G1   H  N N 103 
AOV H4G1   H  N N 104 
ARG N      N  N N 105 
ARG CA     C  N S 106 
ARG C      C  N N 107 
ARG O      O  N N 108 
ARG CB     C  N N 109 
ARG CG     C  N N 110 
ARG CD     C  N N 111 
ARG NE     N  N N 112 
ARG CZ     C  N N 113 
ARG NH1    N  N N 114 
ARG NH2    N  N N 115 
ARG OXT    O  N N 116 
ARG H      H  N N 117 
ARG H2     H  N N 118 
ARG HA     H  N N 119 
ARG HB2    H  N N 120 
ARG HB3    H  N N 121 
ARG HG2    H  N N 122 
ARG HG3    H  N N 123 
ARG HD2    H  N N 124 
ARG HD3    H  N N 125 
ARG HE     H  N N 126 
ARG HH11   H  N N 127 
ARG HH12   H  N N 128 
ARG HH21   H  N N 129 
ARG HH22   H  N N 130 
ARG HXT    H  N N 131 
ASN N      N  N N 132 
ASN CA     C  N S 133 
ASN C      C  N N 134 
ASN O      O  N N 135 
ASN CB     C  N N 136 
ASN CG     C  N N 137 
ASN OD1    O  N N 138 
ASN ND2    N  N N 139 
ASN OXT    O  N N 140 
ASN H      H  N N 141 
ASN H2     H  N N 142 
ASN HA     H  N N 143 
ASN HB2    H  N N 144 
ASN HB3    H  N N 145 
ASN HD21   H  N N 146 
ASN HD22   H  N N 147 
ASN HXT    H  N N 148 
ASP N      N  N N 149 
ASP CA     C  N S 150 
ASP C      C  N N 151 
ASP O      O  N N 152 
ASP CB     C  N N 153 
ASP CG     C  N N 154 
ASP OD1    O  N N 155 
ASP OD2    O  N N 156 
ASP OXT    O  N N 157 
ASP H      H  N N 158 
ASP H2     H  N N 159 
ASP HA     H  N N 160 
ASP HB2    H  N N 161 
ASP HB3    H  N N 162 
ASP HD2    H  N N 163 
ASP HXT    H  N N 164 
ATP PG     P  N N 165 
ATP O1G    O  N N 166 
ATP O2G    O  N N 167 
ATP O3G    O  N N 168 
ATP PB     P  N R 169 
ATP O1B    O  N N 170 
ATP O2B    O  N N 171 
ATP O3B    O  N N 172 
ATP PA     P  N R 173 
ATP O1A    O  N N 174 
ATP O2A    O  N N 175 
ATP O3A    O  N N 176 
ATP "O5'"  O  N N 177 
ATP "C5'"  C  N N 178 
ATP "C4'"  C  N R 179 
ATP "O4'"  O  N N 180 
ATP "C3'"  C  N S 181 
ATP "O3'"  O  N N 182 
ATP "C2'"  C  N R 183 
ATP "O2'"  O  N N 184 
ATP "C1'"  C  N R 185 
ATP N9     N  Y N 186 
ATP C8     C  Y N 187 
ATP N7     N  Y N 188 
ATP C5     C  Y N 189 
ATP C6     C  Y N 190 
ATP N6     N  N N 191 
ATP N1     N  Y N 192 
ATP C2     C  Y N 193 
ATP N3     N  Y N 194 
ATP C4     C  Y N 195 
ATP HOG2   H  N N 196 
ATP HOG3   H  N N 197 
ATP HOB2   H  N N 198 
ATP HOA2   H  N N 199 
ATP "H5'1" H  N N 200 
ATP "H5'2" H  N N 201 
ATP "H4'"  H  N N 202 
ATP "H3'"  H  N N 203 
ATP "HO3'" H  N N 204 
ATP "H2'"  H  N N 205 
ATP "HO2'" H  N N 206 
ATP "H1'"  H  N N 207 
ATP H8     H  N N 208 
ATP HN61   H  N N 209 
ATP HN62   H  N N 210 
ATP H2     H  N N 211 
CYS N      N  N N 212 
CYS CA     C  N R 213 
CYS C      C  N N 214 
CYS O      O  N N 215 
CYS CB     C  N N 216 
CYS SG     S  N N 217 
CYS OXT    O  N N 218 
CYS H      H  N N 219 
CYS H2     H  N N 220 
CYS HA     H  N N 221 
CYS HB2    H  N N 222 
CYS HB3    H  N N 223 
CYS HG     H  N N 224 
CYS HXT    H  N N 225 
GLN N      N  N N 226 
GLN CA     C  N S 227 
GLN C      C  N N 228 
GLN O      O  N N 229 
GLN CB     C  N N 230 
GLN CG     C  N N 231 
GLN CD     C  N N 232 
GLN OE1    O  N N 233 
GLN NE2    N  N N 234 
GLN OXT    O  N N 235 
GLN H      H  N N 236 
GLN H2     H  N N 237 
GLN HA     H  N N 238 
GLN HB2    H  N N 239 
GLN HB3    H  N N 240 
GLN HG2    H  N N 241 
GLN HG3    H  N N 242 
GLN HE21   H  N N 243 
GLN HE22   H  N N 244 
GLN HXT    H  N N 245 
GLU N      N  N N 246 
GLU CA     C  N S 247 
GLU C      C  N N 248 
GLU O      O  N N 249 
GLU CB     C  N N 250 
GLU CG     C  N N 251 
GLU CD     C  N N 252 
GLU OE1    O  N N 253 
GLU OE2    O  N N 254 
GLU OXT    O  N N 255 
GLU H      H  N N 256 
GLU H2     H  N N 257 
GLU HA     H  N N 258 
GLU HB2    H  N N 259 
GLU HB3    H  N N 260 
GLU HG2    H  N N 261 
GLU HG3    H  N N 262 
GLU HE2    H  N N 263 
GLU HXT    H  N N 264 
GLY N      N  N N 265 
GLY CA     C  N N 266 
GLY C      C  N N 267 
GLY O      O  N N 268 
GLY OXT    O  N N 269 
GLY H      H  N N 270 
GLY H2     H  N N 271 
GLY HA2    H  N N 272 
GLY HA3    H  N N 273 
GLY HXT    H  N N 274 
HIS N      N  N N 275 
HIS CA     C  N S 276 
HIS C      C  N N 277 
HIS O      O  N N 278 
HIS CB     C  N N 279 
HIS CG     C  Y N 280 
HIS ND1    N  Y N 281 
HIS CD2    C  Y N 282 
HIS CE1    C  Y N 283 
HIS NE2    N  Y N 284 
HIS OXT    O  N N 285 
HIS H      H  N N 286 
HIS H2     H  N N 287 
HIS HA     H  N N 288 
HIS HB2    H  N N 289 
HIS HB3    H  N N 290 
HIS HD1    H  N N 291 
HIS HD2    H  N N 292 
HIS HE1    H  N N 293 
HIS HE2    H  N N 294 
HIS HXT    H  N N 295 
ILE N      N  N N 296 
ILE CA     C  N S 297 
ILE C      C  N N 298 
ILE O      O  N N 299 
ILE CB     C  N S 300 
ILE CG1    C  N N 301 
ILE CG2    C  N N 302 
ILE CD1    C  N N 303 
ILE OXT    O  N N 304 
ILE H      H  N N 305 
ILE H2     H  N N 306 
ILE HA     H  N N 307 
ILE HB     H  N N 308 
ILE HG12   H  N N 309 
ILE HG13   H  N N 310 
ILE HG21   H  N N 311 
ILE HG22   H  N N 312 
ILE HG23   H  N N 313 
ILE HD11   H  N N 314 
ILE HD12   H  N N 315 
ILE HD13   H  N N 316 
ILE HXT    H  N N 317 
LEU N      N  N N 318 
LEU CA     C  N S 319 
LEU C      C  N N 320 
LEU O      O  N N 321 
LEU CB     C  N N 322 
LEU CG     C  N N 323 
LEU CD1    C  N N 324 
LEU CD2    C  N N 325 
LEU OXT    O  N N 326 
LEU H      H  N N 327 
LEU H2     H  N N 328 
LEU HA     H  N N 329 
LEU HB2    H  N N 330 
LEU HB3    H  N N 331 
LEU HG     H  N N 332 
LEU HD11   H  N N 333 
LEU HD12   H  N N 334 
LEU HD13   H  N N 335 
LEU HD21   H  N N 336 
LEU HD22   H  N N 337 
LEU HD23   H  N N 338 
LEU HXT    H  N N 339 
LYS N      N  N N 340 
LYS CA     C  N S 341 
LYS C      C  N N 342 
LYS O      O  N N 343 
LYS CB     C  N N 344 
LYS CG     C  N N 345 
LYS CD     C  N N 346 
LYS CE     C  N N 347 
LYS NZ     N  N N 348 
LYS OXT    O  N N 349 
LYS H      H  N N 350 
LYS H2     H  N N 351 
LYS HA     H  N N 352 
LYS HB2    H  N N 353 
LYS HB3    H  N N 354 
LYS HG2    H  N N 355 
LYS HG3    H  N N 356 
LYS HD2    H  N N 357 
LYS HD3    H  N N 358 
LYS HE2    H  N N 359 
LYS HE3    H  N N 360 
LYS HZ1    H  N N 361 
LYS HZ2    H  N N 362 
LYS HZ3    H  N N 363 
LYS HXT    H  N N 364 
MET N      N  N N 365 
MET CA     C  N S 366 
MET C      C  N N 367 
MET O      O  N N 368 
MET CB     C  N N 369 
MET CG     C  N N 370 
MET SD     S  N N 371 
MET CE     C  N N 372 
MET OXT    O  N N 373 
MET H      H  N N 374 
MET H2     H  N N 375 
MET HA     H  N N 376 
MET HB2    H  N N 377 
MET HB3    H  N N 378 
MET HG2    H  N N 379 
MET HG3    H  N N 380 
MET HE1    H  N N 381 
MET HE2    H  N N 382 
MET HE3    H  N N 383 
MET HXT    H  N N 384 
MG  MG     MG N N 385 
PHE N      N  N N 386 
PHE CA     C  N S 387 
PHE C      C  N N 388 
PHE O      O  N N 389 
PHE CB     C  N N 390 
PHE CG     C  Y N 391 
PHE CD1    C  Y N 392 
PHE CD2    C  Y N 393 
PHE CE1    C  Y N 394 
PHE CE2    C  Y N 395 
PHE CZ     C  Y N 396 
PHE OXT    O  N N 397 
PHE H      H  N N 398 
PHE H2     H  N N 399 
PHE HA     H  N N 400 
PHE HB2    H  N N 401 
PHE HB3    H  N N 402 
PHE HD1    H  N N 403 
PHE HD2    H  N N 404 
PHE HE1    H  N N 405 
PHE HE2    H  N N 406 
PHE HZ     H  N N 407 
PHE HXT    H  N N 408 
PRO N      N  N N 409 
PRO CA     C  N S 410 
PRO C      C  N N 411 
PRO O      O  N N 412 
PRO CB     C  N N 413 
PRO CG     C  N N 414 
PRO CD     C  N N 415 
PRO OXT    O  N N 416 
PRO H      H  N N 417 
PRO HA     H  N N 418 
PRO HB2    H  N N 419 
PRO HB3    H  N N 420 
PRO HG2    H  N N 421 
PRO HG3    H  N N 422 
PRO HD2    H  N N 423 
PRO HD3    H  N N 424 
PRO HXT    H  N N 425 
SER N      N  N N 426 
SER CA     C  N S 427 
SER C      C  N N 428 
SER O      O  N N 429 
SER CB     C  N N 430 
SER OG     O  N N 431 
SER OXT    O  N N 432 
SER H      H  N N 433 
SER H2     H  N N 434 
SER HA     H  N N 435 
SER HB2    H  N N 436 
SER HB3    H  N N 437 
SER HG     H  N N 438 
SER HXT    H  N N 439 
THR N      N  N N 440 
THR CA     C  N S 441 
THR C      C  N N 442 
THR O      O  N N 443 
THR CB     C  N R 444 
THR OG1    O  N N 445 
THR CG2    C  N N 446 
THR OXT    O  N N 447 
THR H      H  N N 448 
THR H2     H  N N 449 
THR HA     H  N N 450 
THR HB     H  N N 451 
THR HG1    H  N N 452 
THR HG21   H  N N 453 
THR HG22   H  N N 454 
THR HG23   H  N N 455 
THR HXT    H  N N 456 
TRP N      N  N N 457 
TRP CA     C  N S 458 
TRP C      C  N N 459 
TRP O      O  N N 460 
TRP CB     C  N N 461 
TRP CG     C  Y N 462 
TRP CD1    C  Y N 463 
TRP CD2    C  Y N 464 
TRP NE1    N  Y N 465 
TRP CE2    C  Y N 466 
TRP CE3    C  Y N 467 
TRP CZ2    C  Y N 468 
TRP CZ3    C  Y N 469 
TRP CH2    C  Y N 470 
TRP OXT    O  N N 471 
TRP H      H  N N 472 
TRP H2     H  N N 473 
TRP HA     H  N N 474 
TRP HB2    H  N N 475 
TRP HB3    H  N N 476 
TRP HD1    H  N N 477 
TRP HE1    H  N N 478 
TRP HE3    H  N N 479 
TRP HZ2    H  N N 480 
TRP HZ3    H  N N 481 
TRP HH2    H  N N 482 
TRP HXT    H  N N 483 
TYR N      N  N N 484 
TYR CA     C  N S 485 
TYR C      C  N N 486 
TYR O      O  N N 487 
TYR CB     C  N N 488 
TYR CG     C  Y N 489 
TYR CD1    C  Y N 490 
TYR CD2    C  Y N 491 
TYR CE1    C  Y N 492 
TYR CE2    C  Y N 493 
TYR CZ     C  Y N 494 
TYR OH     O  N N 495 
TYR OXT    O  N N 496 
TYR H      H  N N 497 
TYR H2     H  N N 498 
TYR HA     H  N N 499 
TYR HB2    H  N N 500 
TYR HB3    H  N N 501 
TYR HD1    H  N N 502 
TYR HD2    H  N N 503 
TYR HE1    H  N N 504 
TYR HE2    H  N N 505 
TYR HH     H  N N 506 
TYR HXT    H  N N 507 
VAL N      N  N N 508 
VAL CA     C  N S 509 
VAL C      C  N N 510 
VAL O      O  N N 511 
VAL CB     C  N N 512 
VAL CG1    C  N N 513 
VAL CG2    C  N N 514 
VAL OXT    O  N N 515 
VAL H      H  N N 516 
VAL H2     H  N N 517 
VAL HA     H  N N 518 
VAL HB     H  N N 519 
VAL HG11   H  N N 520 
VAL HG12   H  N N 521 
VAL HG13   H  N N 522 
VAL HG21   H  N N 523 
VAL HG22   H  N N 524 
VAL HG23   H  N N 525 
VAL HXT    H  N N 526 
# 
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  
AOV PB    O1B    doub N N 57  
AOV PB    O2B    sing N N 58  
AOV PB    O3B    sing N N 59  
AOV PB    O3A    sing N N 60  
AOV O3B   VG     sing N N 61  
AOV PA    O1A    doub N N 62  
AOV PA    O2A    sing N N 63  
AOV PA    O3A    sing N N 64  
AOV PA    "O5'"  sing N N 65  
AOV "O5'" "C5'"  sing N N 66  
AOV "C5'" "C4'"  sing N N 67  
AOV "C4'" "O4'"  sing N N 68  
AOV "C4'" "C3'"  sing N N 69  
AOV "O4'" "C1'"  sing N N 70  
AOV "C3'" "O3'"  sing N N 71  
AOV "C3'" "C2'"  sing N N 72  
AOV "C2'" "O2'"  sing N N 73  
AOV "C2'" "C1'"  sing N N 74  
AOV "C1'" N9     sing N N 75  
AOV N9    C8     sing Y N 76  
AOV N9    C4     sing Y N 77  
AOV C8    N7     doub Y N 78  
AOV N7    C5     sing Y N 79  
AOV C5    C6     sing Y N 80  
AOV C5    C4     doub Y N 81  
AOV C6    N6     sing N N 82  
AOV C6    N1     doub Y N 83  
AOV N1    C2     sing Y N 84  
AOV C2    N3     doub Y N 85  
AOV N3    C4     sing Y N 86  
AOV VG    O1G    doub N N 87  
AOV VG    O2G    sing N N 88  
AOV VG    O3G    sing N N 89  
AOV VG    O4G    sing N N 90  
AOV O2B   H2B    sing N N 91  
AOV O2A   H2A    sing N N 92  
AOV "C5'" "H5'1" sing N N 93  
AOV "C5'" "H5'2" sing N N 94  
AOV "C4'" "H4'"  sing N N 95  
AOV "C3'" "H3'"  sing N N 96  
AOV "C1'" "H1'"  sing N N 97  
AOV "O3'" HA     sing N N 98  
AOV "C2'" "H2'"  sing N N 99  
AOV "O2'" HB     sing N N 100 
AOV C8    H8     sing N N 101 
AOV N6    H61N   sing N N 102 
AOV N6    H62N   sing N N 103 
AOV C2    H2     sing N N 104 
AOV O2G   H2G1   sing N N 105 
AOV O3G   H3G1   sing N N 106 
AOV O4G   H4G1   sing N N 107 
ARG N     CA     sing N N 108 
ARG N     H      sing N N 109 
ARG N     H2     sing N N 110 
ARG CA    C      sing N N 111 
ARG CA    CB     sing N N 112 
ARG CA    HA     sing N N 113 
ARG C     O      doub N N 114 
ARG C     OXT    sing N N 115 
ARG CB    CG     sing N N 116 
ARG CB    HB2    sing N N 117 
ARG CB    HB3    sing N N 118 
ARG CG    CD     sing N N 119 
ARG CG    HG2    sing N N 120 
ARG CG    HG3    sing N N 121 
ARG CD    NE     sing N N 122 
ARG CD    HD2    sing N N 123 
ARG CD    HD3    sing N N 124 
ARG NE    CZ     sing N N 125 
ARG NE    HE     sing N N 126 
ARG CZ    NH1    sing N N 127 
ARG CZ    NH2    doub N N 128 
ARG NH1   HH11   sing N N 129 
ARG NH1   HH12   sing N N 130 
ARG NH2   HH21   sing N N 131 
ARG NH2   HH22   sing N N 132 
ARG OXT   HXT    sing N N 133 
ASN N     CA     sing N N 134 
ASN N     H      sing N N 135 
ASN N     H2     sing N N 136 
ASN CA    C      sing N N 137 
ASN CA    CB     sing N N 138 
ASN CA    HA     sing N N 139 
ASN C     O      doub N N 140 
ASN C     OXT    sing N N 141 
ASN CB    CG     sing N N 142 
ASN CB    HB2    sing N N 143 
ASN CB    HB3    sing N N 144 
ASN CG    OD1    doub N N 145 
ASN CG    ND2    sing N N 146 
ASN ND2   HD21   sing N N 147 
ASN ND2   HD22   sing N N 148 
ASN OXT   HXT    sing N N 149 
ASP N     CA     sing N N 150 
ASP N     H      sing N N 151 
ASP N     H2     sing N N 152 
ASP CA    C      sing N N 153 
ASP CA    CB     sing N N 154 
ASP CA    HA     sing N N 155 
ASP C     O      doub N N 156 
ASP C     OXT    sing N N 157 
ASP CB    CG     sing N N 158 
ASP CB    HB2    sing N N 159 
ASP CB    HB3    sing N N 160 
ASP CG    OD1    doub N N 161 
ASP CG    OD2    sing N N 162 
ASP OD2   HD2    sing N N 163 
ASP OXT   HXT    sing N N 164 
ATP PG    O1G    doub N N 165 
ATP PG    O2G    sing N N 166 
ATP PG    O3G    sing N N 167 
ATP PG    O3B    sing N N 168 
ATP O2G   HOG2   sing N N 169 
ATP O3G   HOG3   sing N N 170 
ATP PB    O1B    doub N N 171 
ATP PB    O2B    sing N N 172 
ATP PB    O3B    sing N N 173 
ATP PB    O3A    sing N N 174 
ATP O2B   HOB2   sing N N 175 
ATP PA    O1A    doub N N 176 
ATP PA    O2A    sing N N 177 
ATP PA    O3A    sing N N 178 
ATP PA    "O5'"  sing N N 179 
ATP O2A   HOA2   sing N N 180 
ATP "O5'" "C5'"  sing N N 181 
ATP "C5'" "C4'"  sing N N 182 
ATP "C5'" "H5'1" sing N N 183 
ATP "C5'" "H5'2" sing N N 184 
ATP "C4'" "O4'"  sing N N 185 
ATP "C4'" "C3'"  sing N N 186 
ATP "C4'" "H4'"  sing N N 187 
ATP "O4'" "C1'"  sing N N 188 
ATP "C3'" "O3'"  sing N N 189 
ATP "C3'" "C2'"  sing N N 190 
ATP "C3'" "H3'"  sing N N 191 
ATP "O3'" "HO3'" sing N N 192 
ATP "C2'" "O2'"  sing N N 193 
ATP "C2'" "C1'"  sing N N 194 
ATP "C2'" "H2'"  sing N N 195 
ATP "O2'" "HO2'" sing N N 196 
ATP "C1'" N9     sing N N 197 
ATP "C1'" "H1'"  sing N N 198 
ATP N9    C8     sing Y N 199 
ATP N9    C4     sing Y N 200 
ATP C8    N7     doub Y N 201 
ATP C8    H8     sing N N 202 
ATP N7    C5     sing Y N 203 
ATP C5    C6     sing Y N 204 
ATP C5    C4     doub Y N 205 
ATP C6    N6     sing N N 206 
ATP C6    N1     doub Y N 207 
ATP N6    HN61   sing N N 208 
ATP N6    HN62   sing N N 209 
ATP N1    C2     sing Y N 210 
ATP C2    N3     doub Y N 211 
ATP C2    H2     sing N N 212 
ATP N3    C4     sing Y N 213 
CYS N     CA     sing N N 214 
CYS N     H      sing N N 215 
CYS N     H2     sing N N 216 
CYS CA    C      sing N N 217 
CYS CA    CB     sing N N 218 
CYS CA    HA     sing N N 219 
CYS C     O      doub N N 220 
CYS C     OXT    sing N N 221 
CYS CB    SG     sing N N 222 
CYS CB    HB2    sing N N 223 
CYS CB    HB3    sing N N 224 
CYS SG    HG     sing N N 225 
CYS OXT   HXT    sing N N 226 
GLN N     CA     sing N N 227 
GLN N     H      sing N N 228 
GLN N     H2     sing N N 229 
GLN CA    C      sing N N 230 
GLN CA    CB     sing N N 231 
GLN CA    HA     sing N N 232 
GLN C     O      doub N N 233 
GLN C     OXT    sing N N 234 
GLN CB    CG     sing N N 235 
GLN CB    HB2    sing N N 236 
GLN CB    HB3    sing N N 237 
GLN CG    CD     sing N N 238 
GLN CG    HG2    sing N N 239 
GLN CG    HG3    sing N N 240 
GLN CD    OE1    doub N N 241 
GLN CD    NE2    sing N N 242 
GLN NE2   HE21   sing N N 243 
GLN NE2   HE22   sing N N 244 
GLN OXT   HXT    sing N N 245 
GLU N     CA     sing N N 246 
GLU N     H      sing N N 247 
GLU N     H2     sing N N 248 
GLU CA    C      sing N N 249 
GLU CA    CB     sing N N 250 
GLU CA    HA     sing N N 251 
GLU C     O      doub N N 252 
GLU C     OXT    sing N N 253 
GLU CB    CG     sing N N 254 
GLU CB    HB2    sing N N 255 
GLU CB    HB3    sing N N 256 
GLU CG    CD     sing N N 257 
GLU CG    HG2    sing N N 258 
GLU CG    HG3    sing N N 259 
GLU CD    OE1    doub N N 260 
GLU CD    OE2    sing N N 261 
GLU OE2   HE2    sing N N 262 
GLU OXT   HXT    sing N N 263 
GLY N     CA     sing N N 264 
GLY N     H      sing N N 265 
GLY N     H2     sing N N 266 
GLY CA    C      sing N N 267 
GLY CA    HA2    sing N N 268 
GLY CA    HA3    sing N N 269 
GLY C     O      doub N N 270 
GLY C     OXT    sing N N 271 
GLY OXT   HXT    sing N N 272 
HIS N     CA     sing N N 273 
HIS N     H      sing N N 274 
HIS N     H2     sing N N 275 
HIS CA    C      sing N N 276 
HIS CA    CB     sing N N 277 
HIS CA    HA     sing N N 278 
HIS C     O      doub N N 279 
HIS C     OXT    sing N N 280 
HIS CB    CG     sing N N 281 
HIS CB    HB2    sing N N 282 
HIS CB    HB3    sing N N 283 
HIS CG    ND1    sing Y N 284 
HIS CG    CD2    doub Y N 285 
HIS ND1   CE1    doub Y N 286 
HIS ND1   HD1    sing N N 287 
HIS CD2   NE2    sing Y N 288 
HIS CD2   HD2    sing N N 289 
HIS CE1   NE2    sing Y N 290 
HIS CE1   HE1    sing N N 291 
HIS NE2   HE2    sing N N 292 
HIS OXT   HXT    sing N N 293 
ILE N     CA     sing N N 294 
ILE N     H      sing N N 295 
ILE N     H2     sing N N 296 
ILE CA    C      sing N N 297 
ILE CA    CB     sing N N 298 
ILE CA    HA     sing N N 299 
ILE C     O      doub N N 300 
ILE C     OXT    sing N N 301 
ILE CB    CG1    sing N N 302 
ILE CB    CG2    sing N N 303 
ILE CB    HB     sing N N 304 
ILE CG1   CD1    sing N N 305 
ILE CG1   HG12   sing N N 306 
ILE CG1   HG13   sing N N 307 
ILE CG2   HG21   sing N N 308 
ILE CG2   HG22   sing N N 309 
ILE CG2   HG23   sing N N 310 
ILE CD1   HD11   sing N N 311 
ILE CD1   HD12   sing N N 312 
ILE CD1   HD13   sing N N 313 
ILE OXT   HXT    sing N N 314 
LEU N     CA     sing N N 315 
LEU N     H      sing N N 316 
LEU N     H2     sing N N 317 
LEU CA    C      sing N N 318 
LEU CA    CB     sing N N 319 
LEU CA    HA     sing N N 320 
LEU C     O      doub N N 321 
LEU C     OXT    sing N N 322 
LEU CB    CG     sing N N 323 
LEU CB    HB2    sing N N 324 
LEU CB    HB3    sing N N 325 
LEU CG    CD1    sing N N 326 
LEU CG    CD2    sing N N 327 
LEU CG    HG     sing N N 328 
LEU CD1   HD11   sing N N 329 
LEU CD1   HD12   sing N N 330 
LEU CD1   HD13   sing N N 331 
LEU CD2   HD21   sing N N 332 
LEU CD2   HD22   sing N N 333 
LEU CD2   HD23   sing N N 334 
LEU OXT   HXT    sing N N 335 
LYS N     CA     sing N N 336 
LYS N     H      sing N N 337 
LYS N     H2     sing N N 338 
LYS CA    C      sing N N 339 
LYS CA    CB     sing N N 340 
LYS CA    HA     sing N N 341 
LYS C     O      doub N N 342 
LYS C     OXT    sing N N 343 
LYS CB    CG     sing N N 344 
LYS CB    HB2    sing N N 345 
LYS CB    HB3    sing N N 346 
LYS CG    CD     sing N N 347 
LYS CG    HG2    sing N N 348 
LYS CG    HG3    sing N N 349 
LYS CD    CE     sing N N 350 
LYS CD    HD2    sing N N 351 
LYS CD    HD3    sing N N 352 
LYS CE    NZ     sing N N 353 
LYS CE    HE2    sing N N 354 
LYS CE    HE3    sing N N 355 
LYS NZ    HZ1    sing N N 356 
LYS NZ    HZ2    sing N N 357 
LYS NZ    HZ3    sing N N 358 
LYS OXT   HXT    sing N N 359 
MET N     CA     sing N N 360 
MET N     H      sing N N 361 
MET N     H2     sing N N 362 
MET CA    C      sing N N 363 
MET CA    CB     sing N N 364 
MET CA    HA     sing N N 365 
MET C     O      doub N N 366 
MET C     OXT    sing N N 367 
MET CB    CG     sing N N 368 
MET CB    HB2    sing N N 369 
MET CB    HB3    sing N N 370 
MET CG    SD     sing N N 371 
MET CG    HG2    sing N N 372 
MET CG    HG3    sing N N 373 
MET SD    CE     sing N N 374 
MET CE    HE1    sing N N 375 
MET CE    HE2    sing N N 376 
MET CE    HE3    sing N N 377 
MET OXT   HXT    sing N N 378 
PHE N     CA     sing N N 379 
PHE N     H      sing N N 380 
PHE N     H2     sing N N 381 
PHE CA    C      sing N N 382 
PHE CA    CB     sing N N 383 
PHE CA    HA     sing N N 384 
PHE C     O      doub N N 385 
PHE C     OXT    sing N N 386 
PHE CB    CG     sing N N 387 
PHE CB    HB2    sing N N 388 
PHE CB    HB3    sing N N 389 
PHE CG    CD1    doub Y N 390 
PHE CG    CD2    sing Y N 391 
PHE CD1   CE1    sing Y N 392 
PHE CD1   HD1    sing N N 393 
PHE CD2   CE2    doub Y N 394 
PHE CD2   HD2    sing N N 395 
PHE CE1   CZ     doub Y N 396 
PHE CE1   HE1    sing N N 397 
PHE CE2   CZ     sing Y N 398 
PHE CE2   HE2    sing N N 399 
PHE CZ    HZ     sing N N 400 
PHE OXT   HXT    sing N N 401 
PRO N     CA     sing N N 402 
PRO N     CD     sing N N 403 
PRO N     H      sing N N 404 
PRO CA    C      sing N N 405 
PRO CA    CB     sing N N 406 
PRO CA    HA     sing N N 407 
PRO C     O      doub N N 408 
PRO C     OXT    sing N N 409 
PRO CB    CG     sing N N 410 
PRO CB    HB2    sing N N 411 
PRO CB    HB3    sing N N 412 
PRO CG    CD     sing N N 413 
PRO CG    HG2    sing N N 414 
PRO CG    HG3    sing N N 415 
PRO CD    HD2    sing N N 416 
PRO CD    HD3    sing N N 417 
PRO OXT   HXT    sing N N 418 
SER N     CA     sing N N 419 
SER N     H      sing N N 420 
SER N     H2     sing N N 421 
SER CA    C      sing N N 422 
SER CA    CB     sing N N 423 
SER CA    HA     sing N N 424 
SER C     O      doub N N 425 
SER C     OXT    sing N N 426 
SER CB    OG     sing N N 427 
SER CB    HB2    sing N N 428 
SER CB    HB3    sing N N 429 
SER OG    HG     sing N N 430 
SER OXT   HXT    sing N N 431 
THR N     CA     sing N N 432 
THR N     H      sing N N 433 
THR N     H2     sing N N 434 
THR CA    C      sing N N 435 
THR CA    CB     sing N N 436 
THR CA    HA     sing N N 437 
THR C     O      doub N N 438 
THR C     OXT    sing N N 439 
THR CB    OG1    sing N N 440 
THR CB    CG2    sing N N 441 
THR CB    HB     sing N N 442 
THR OG1   HG1    sing N N 443 
THR CG2   HG21   sing N N 444 
THR CG2   HG22   sing N N 445 
THR CG2   HG23   sing N N 446 
THR OXT   HXT    sing N N 447 
TRP N     CA     sing N N 448 
TRP N     H      sing N N 449 
TRP N     H2     sing N N 450 
TRP CA    C      sing N N 451 
TRP CA    CB     sing N N 452 
TRP CA    HA     sing N N 453 
TRP C     O      doub N N 454 
TRP C     OXT    sing N N 455 
TRP CB    CG     sing N N 456 
TRP CB    HB2    sing N N 457 
TRP CB    HB3    sing N N 458 
TRP CG    CD1    doub Y N 459 
TRP CG    CD2    sing Y N 460 
TRP CD1   NE1    sing Y N 461 
TRP CD1   HD1    sing N N 462 
TRP CD2   CE2    doub Y N 463 
TRP CD2   CE3    sing Y N 464 
TRP NE1   CE2    sing Y N 465 
TRP NE1   HE1    sing N N 466 
TRP CE2   CZ2    sing Y N 467 
TRP CE3   CZ3    doub Y N 468 
TRP CE3   HE3    sing N N 469 
TRP CZ2   CH2    doub Y N 470 
TRP CZ2   HZ2    sing N N 471 
TRP CZ3   CH2    sing Y N 472 
TRP CZ3   HZ3    sing N N 473 
TRP CH2   HH2    sing N N 474 
TRP OXT   HXT    sing N N 475 
TYR N     CA     sing N N 476 
TYR N     H      sing N N 477 
TYR N     H2     sing N N 478 
TYR CA    C      sing N N 479 
TYR CA    CB     sing N N 480 
TYR CA    HA     sing N N 481 
TYR C     O      doub N N 482 
TYR C     OXT    sing N N 483 
TYR CB    CG     sing N N 484 
TYR CB    HB2    sing N N 485 
TYR CB    HB3    sing N N 486 
TYR CG    CD1    doub Y N 487 
TYR CG    CD2    sing Y N 488 
TYR CD1   CE1    sing Y N 489 
TYR CD1   HD1    sing N N 490 
TYR CD2   CE2    doub Y N 491 
TYR CD2   HD2    sing N N 492 
TYR CE1   CZ     doub Y N 493 
TYR CE1   HE1    sing N N 494 
TYR CE2   CZ     sing Y N 495 
TYR CE2   HE2    sing N N 496 
TYR CZ    OH     sing N N 497 
TYR OH    HH     sing N N 498 
TYR OXT   HXT    sing N N 499 
VAL N     CA     sing N N 500 
VAL N     H      sing N N 501 
VAL N     H2     sing N N 502 
VAL CA    C      sing N N 503 
VAL CA    CB     sing N N 504 
VAL CA    HA     sing N N 505 
VAL C     O      doub N N 506 
VAL C     OXT    sing N N 507 
VAL CB    CG1    sing N N 508 
VAL CB    CG2    sing N N 509 
VAL CB    HB     sing N N 510 
VAL CG1   HG11   sing N N 511 
VAL CG1   HG12   sing N N 512 
VAL CG1   HG13   sing N N 513 
VAL CG2   HG21   sing N N 514 
VAL CG2   HG22   sing N N 515 
VAL CG2   HG23   sing N N 516 
VAL OXT   HXT    sing N N 517 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BMF 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-1(phi motor) of full-length human dynein-1 in 5mM ATPVi' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 SerialEM  4 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ?         ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BMF 
_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  
V  
# 
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 ? 231.639 232.056 296.537 1.00 128.28 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 230.201 231.815 296.588 1.00 128.64 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 229.441 232.852 295.767 1.00 127.93 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 228.221 232.774 295.626 1.00 127.74 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 229.707 231.822 298.036 1.00 129.61 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 230.033 230.552 298.804 1.00 130.57 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 231.778 230.425 299.237 1.00 132.48 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 231.884 231.630 300.558 1.00 126.51 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 230.178 233.826 295.228 1.00 124.13 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 229.551 234.873 294.428 1.00 124.24 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 229.044 234.341 293.094 1.00 125.17 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 228.068 234.870 292.548 1.00 126.03 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 230.536 236.020 294.203 1.00 122.96 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 229.689 233.305 292.553 1.00 119.76 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 229.286 232.782 291.250 1.00 119.80 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 227.899 232.154 291.309 1.00 118.90 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 227.142 232.215 290.332 1.00 119.16 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 230.317 231.774 290.741 1.00 120.25 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 231.616 232.360 290.177 1.00 118.68 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 232.623 232.656 291.280 1.00 119.30 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 232.217 231.436 289.128 1.00 120.17 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 227.550 231.533 292.439 1.00 122.25 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 226.182 231.058 292.620 1.00 123.54 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 225.195 232.216 292.587 1.00 122.97 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 224.141 232.128 291.945 1.00 123.90 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 226.047 230.300 293.942 1.00 124.31 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 226.701 228.928 293.995 1.00 124.17 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 228.176 229.002 294.330 1.00 125.99 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 228.695 230.128 294.455 1.00 125.91 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 228.808 227.941 294.505 1.00 126.25 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 225.525 233.315 293.271 1.00 118.15 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 224.589 234.427 293.403 1.00 118.80 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 224.277 235.057 292.051 1.00 120.69 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 223.122 235.399 291.771 1.00 120.73 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 225.153 235.473 294.364 1.00 118.98 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 225.319 234.969 295.786 1.00 121.04 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 224.101 234.221 296.284 1.00 122.20 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 223.038 234.854 296.455 1.00 120.66 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 224.205 232.995 296.499 1.00 121.94 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 225.294 235.225 291.203 1.00 117.63 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 225.068 235.782 289.873 1.00 116.58 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 224.146 234.881 289.060 1.00 115.27 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 223.233 235.354 288.376 1.00 115.87 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 226.403 235.984 289.154 1.00 114.12 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 227.250 237.080 289.739 1.00 117.88 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 226.674 238.103 290.472 1.00 117.09 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 228.624 237.083 289.558 1.00 118.08 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 227.451 239.112 291.013 1.00 116.70 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 229.406 238.090 290.095 1.00 117.67 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 228.819 239.104 290.824 1.00 117.02 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 224.375 233.568 289.129 1.00 108.14 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 223.508 232.620 288.436 1.00 108.23 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 222.104 232.620 289.025 1.00 109.30 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 221.117 232.463 288.296 1.00 111.28 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 224.126 231.224 288.493 1.00 107.12 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 225.348 231.011 287.600 1.00 106.30 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 225.569 229.542 287.336 1.00 107.82 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 225.129 231.728 286.283 1.00 107.38 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 221.993 232.785 290.345 1.00 108.66 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 220.678 232.858 290.971 1.00 107.87 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 219.907 234.079 290.485 1.00 110.21 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 218.701 234.004 290.227 1.00 108.79 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 220.820 232.873 292.494 1.00 109.42 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 221.223 231.532 293.085 1.00 110.87 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 221.355 231.600 294.596 1.00 111.10 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 221.909 230.299 295.154 1.00 110.64 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 220.948 229.171 294.999 1.00 110.32 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 220.591 235.219 290.356 1.00 108.13 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 219.936 236.423 289.854 1.00 107.01 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 219.488 236.244 288.409 1.00 105.35 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 218.368 236.617 288.043 1.00 106.40 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 220.872 237.624 289.986 1.00 105.69 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 221.176 238.020 291.420 1.00 106.67 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 222.121 239.202 291.511 1.00 108.31 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 222.613 239.698 290.497 1.00 108.60 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 222.377 239.662 292.730 1.00 107.30 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 220.353 235.670 287.569 1.00 96.18  ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 220.001 235.456 286.167 1.00 93.52  ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 218.828 234.489 286.055 1.00 93.70  ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 217.900 234.698 285.265 1.00 97.86  ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 221.223 234.958 285.374 1.00 93.54  ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 222.352 235.989 285.428 1.00 93.19  ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 220.843 234.661 283.932 1.00 93.08  ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 223.578 235.595 284.634 1.00 93.75  ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 218.855 233.414 286.847 1.00 94.26  ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 217.791 232.416 286.782 1.00 94.68  ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 216.450 233.004 287.205 1.00 95.00  ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 215.425 232.775 286.553 1.00 95.26  ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 218.151 231.213 287.653 1.00 94.54  ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 217.521 229.908 287.198 1.00 93.74  ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 218.247 228.709 287.785 1.00 95.68  ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 219.221 228.150 286.855 1.00 95.91  ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 218.917 227.347 285.845 1.00 96.23  ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 217.668 226.984 285.602 1.00 94.11  ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 219.890 226.896 285.059 1.00 95.76  ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 216.437 233.767 288.301 1.00 99.50  ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 215.178 234.315 288.798 1.00 99.03  ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 214.644 235.410 287.883 1.00 99.75  ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 213.426 235.573 287.747 1.00 102.19 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 215.359 234.843 290.221 1.00 99.20  ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 215.661 233.760 291.244 1.00 103.73 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 214.496 232.809 291.448 1.00 104.61 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 213.335 233.252 291.320 1.00 102.59 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 214.742 231.619 291.733 1.00 103.28 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 215.538 236.179 287.256 1.00 94.00  ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 215.096 237.241 286.356 1.00 90.13  ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 214.361 236.657 285.156 1.00 90.15  ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 213.275 237.122 284.790 1.00 93.06  ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 216.291 238.111 285.921 1.00 89.33  ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 215.959 238.875 284.649 1.00 90.80  ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 216.667 239.080 287.029 1.00 90.71  ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 214.922 235.618 284.541 1.00 85.44  ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 214.348 235.053 283.328 1.00 86.31  ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 213.198 234.091 283.593 1.00 88.81  ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 212.476 233.745 282.652 1.00 92.19  ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 215.434 234.349 282.510 1.00 83.16  ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 216.461 235.299 281.982 1.00 83.60  ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 217.798 235.290 282.245 1.00 86.29  ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 216.231 236.410 281.107 1.00 86.03  ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 218.417 236.323 281.584 1.00 87.50  ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 217.476 237.026 280.879 1.00 85.70  ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 215.093 236.942 280.492 1.00 86.26  ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 217.616 238.146 280.063 1.00 85.76  ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 215.233 238.053 279.684 1.00 85.43  ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 216.485 238.643 279.476 1.00 85.97  ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 213.006 233.655 284.835 1.00 95.39  ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 211.844 232.851 285.182 1.00 96.98  ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 210.624 233.696 285.520 1.00 97.33  ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 209.529 233.144 285.671 1.00 97.63  ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 212.169 231.928 286.362 1.00 97.97  ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 213.136 230.822 285.987 1.00 101.50 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 214.052 230.499 286.744 1.00 100.13 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 212.935 230.234 284.814 1.00 99.69  ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 210.784 235.008 285.639 1.00 97.17  ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 209.696 235.913 285.992 1.00 96.06  ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 209.486 237.024 284.975 1.00 96.37  ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 208.384 237.572 284.896 1.00 98.61  ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 209.949 236.532 287.379 1.00 95.91  ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 211.157 237.302 287.348 1.00 95.67  ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 210.069 235.446 288.438 1.00 95.21  ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 210.511 237.375 284.201 1.00 91.46  ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 210.390 238.466 283.241 1.00 91.78  ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 209.434 238.092 282.119 1.00 93.36  ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 209.679 237.143 281.369 1.00 93.73  ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 211.765 238.822 282.672 1.00 91.38  ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 211.745 239.974 281.694 1.00 91.35  ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 211.615 241.284 282.136 1.00 91.12  ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 211.859 239.753 280.330 1.00 92.89  ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 211.596 242.340 281.244 1.00 90.90  ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 211.840 240.801 279.431 1.00 95.02  ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 211.709 242.092 279.893 1.00 93.91  ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 211.691 243.139 279.000 1.00 93.19  ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 208.350 238.851 282.003 1.00 91.71  ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 207.325 238.622 280.996 1.00 87.79  ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 207.380 239.722 279.947 1.00 89.65  ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 207.649 240.885 280.266 1.00 88.82  ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 205.932 238.576 281.628 1.00 86.62  ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 205.696 237.386 282.540 1.00 89.28  ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 204.312 237.394 283.157 1.00 92.39  ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 203.584 238.392 282.971 1.00 91.02  ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 203.951 236.404 283.827 1.00 93.68  ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 207.130 239.348 278.696 1.00 85.57  ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 207.091 240.320 277.611 1.00 82.09  ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 205.921 241.272 277.824 1.00 84.30  ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 204.771 240.837 277.946 1.00 87.14  ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 206.969 239.602 276.271 1.00 80.95  ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 208.256 238.965 275.747 1.00 82.19  ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 207.962 238.065 274.562 1.00 82.71  ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 209.269 240.034 275.373 1.00 81.99  ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 206.212 242.569 277.869 1.00 80.73  ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 205.185 243.572 278.117 1.00 82.33  ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 204.401 243.813 276.833 1.00 80.64  ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 204.976 244.199 275.810 1.00 82.73  ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 205.819 244.863 278.628 1.00 83.09  ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 204.795 245.933 278.948 1.00 85.82  ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 203.600 245.599 279.096 1.00 86.00  ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 205.188 247.113 279.059 1.00 84.85  ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 203.091 243.588 276.888 1.00 76.65  ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 202.226 243.663 275.720 1.00 76.55  ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 201.265 244.835 275.851 1.00 79.45  ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 200.744 245.107 276.938 1.00 79.23  ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 201.436 242.363 275.538 1.00 73.49  ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 202.224 241.054 275.428 1.00 74.22  ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 201.363 239.969 274.804 1.00 77.99  ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 203.500 241.245 274.625 1.00 77.31  ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 201.034 245.528 274.737 1.00 81.50  ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 200.110 246.653 274.674 1.00 81.01  ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 199.129 246.401 273.538 1.00 80.68  ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 199.539 246.037 272.430 1.00 82.20  ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 200.846 247.991 274.470 1.00 79.04  ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 199.852 249.125 274.281 1.00 79.88  ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 201.760 248.277 275.651 1.00 79.61  ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 197.840 246.588 273.814 1.00 80.70  ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 196.819 246.393 272.794 1.00 83.48  ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 196.985 247.409 271.671 1.00 81.04  ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 197.248 248.591 271.911 1.00 81.63  ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 195.426 246.511 273.414 1.00 81.80  ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 194.324 246.148 272.441 1.00 81.32  ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 194.252 245.018 271.960 1.00 81.58  ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 193.455 247.108 272.147 1.00 80.29  ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 196.829 246.941 270.435 1.00 73.94  ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 197.023 247.761 269.240 1.00 74.48  ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 195.727 247.761 268.433 1.00 79.28  ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 195.489 246.862 267.622 1.00 80.76  ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 198.202 247.243 268.414 1.00 73.46  ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 198.402 247.966 267.101 1.00 76.19  ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 198.908 249.259 267.067 1.00 73.93  ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 198.092 247.353 265.894 1.00 73.48  ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 199.094 249.922 265.870 1.00 71.89  ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 198.274 248.009 264.692 1.00 73.96  ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 198.776 249.293 264.686 1.00 73.79  ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 198.960 249.949 263.490 1.00 75.02  ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 194.892 248.777 268.666 1.00 79.89  ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 193.653 248.986 267.912 1.00 80.40  ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 192.735 247.768 267.982 1.00 84.51  ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 192.040 247.438 267.018 1.00 83.88  ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 193.950 249.357 266.457 1.00 78.39  ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 194.870 250.554 266.296 1.00 80.69  ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 195.196 250.844 264.845 1.00 82.66  ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 194.708 250.167 263.940 1.00 77.59  ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 196.026 251.854 264.615 1.00 83.37  ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 192.734 247.093 269.134 1.00 83.05  ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 191.886 245.924 269.376 1.00 81.59  ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 192.121 244.824 268.344 1.00 82.83  ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 191.216 244.048 268.030 1.00 82.56  ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 190.404 246.310 269.416 1.00 81.90  ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 190.131 247.473 270.349 1.00 83.14  ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 190.976 247.841 271.164 1.00 83.87  ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 188.945 248.058 270.233 1.00 83.11  ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 193.336 244.751 267.808 1.00 79.88  ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 193.713 243.732 266.836 1.00 79.22  ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 194.667 242.693 267.397 1.00 78.17  ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 194.507 241.503 267.121 1.00 75.27  ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 194.352 244.386 265.605 1.00 78.69  ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 194.404 243.487 264.380 1.00 79.90  ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 194.394 244.300 263.096 1.00 80.81  ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 194.414 243.398 261.872 1.00 80.39  ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 194.426 244.180 260.606 1.00 79.49  ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 195.652 243.116 268.182 1.00 77.48  ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 196.637 242.212 268.762 1.00 77.74  ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 197.307 242.928 269.930 1.00 79.51  ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 196.949 244.060 270.273 1.00 77.46  ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 197.649 241.760 267.705 1.00 75.89  ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 198.476 243.109 266.834 1.00 81.31  ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 198.283 242.265 270.543 1.00 80.39  ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 199.039 242.816 271.666 1.00 78.83  ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 200.507 242.887 271.257 1.00 75.94  ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 201.231 241.891 271.340 1.00 79.12  ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 198.847 241.973 272.923 1.00 80.52  ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 197.394 241.681 273.259 1.00 80.21  ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 196.921 242.513 274.442 1.00 80.45  ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 197.816 242.403 275.589 1.00 82.09  ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 197.887 241.347 276.389 1.00 83.79  ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 197.122 240.284 276.202 1.00 82.46  ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 198.747 241.360 277.404 1.00 79.66  ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 200.941 244.063 270.815 1.00 67.88  ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 202.319 244.255 270.391 1.00 67.54  ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 203.250 244.326 271.596 1.00 67.32  ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 202.857 244.741 272.690 1.00 72.39  ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 202.449 245.529 269.556 1.00 72.86  ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 201.594 245.592 268.289 1.00 69.18  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 201.851 246.887 267.537 1.00 69.77  ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 201.863 244.389 267.399 1.00 63.59  ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 204.499 243.915 271.382 1.00 62.42  ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 205.484 243.907 272.456 1.00 60.92  ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 205.999 245.321 272.689 1.00 66.88  ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 206.367 246.031 271.744 1.00 72.42  ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 206.631 242.941 272.128 1.00 62.08  ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 206.119 241.500 272.122 1.00 62.01  ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 207.770 243.100 273.125 1.00 67.63  ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 207.212 240.466 272.060 1.00 65.50  ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 206.025 245.736 273.954 1.00 73.72  ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 206.485 247.059 274.349 1.00 73.03  ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 207.557 246.902 275.419 1.00 75.59  ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 207.544 245.932 276.181 1.00 80.47  ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 205.301 247.916 274.851 1.00 73.03  ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 205.601 249.382 275.175 1.00 75.61  ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 206.096 249.590 276.601 1.00 78.64  ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 205.156 249.071 277.586 1.00 81.37  ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 204.082 249.722 278.014 1.00 78.82  ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 203.779 250.928 277.561 1.00 77.45  ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 203.294 249.150 278.920 1.00 75.67  ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 208.491 247.850 275.464 1.00 73.56  ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 209.583 247.786 276.417 1.00 74.74  ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 210.841 247.203 275.809 1.00 74.37  ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 211.440 246.275 276.361 1.00 73.39  ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 211.244 247.744 274.659 1.00 72.99  ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 212.338 247.150 273.899 1.00 67.97  ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 213.686 247.392 274.567 1.00 70.97  ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 214.515 246.479 274.652 1.00 71.13  ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 212.340 247.708 272.478 1.00 69.61  ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 211.221 247.175 271.658 1.00 67.02  ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 210.058 247.815 271.344 1.00 67.77  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 211.127 245.869 271.087 1.00 69.60  ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 209.258 246.997 270.588 1.00 70.20  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 209.890 245.794 270.418 1.00 70.25  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 211.974 244.758 271.067 1.00 70.71  ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 209.482 244.655 269.738 1.00 63.90  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 211.566 243.630 270.392 1.00 68.89  ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 210.333 243.587 269.737 1.00 64.54  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 213.926 248.619 275.035 1.00 79.15  ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 215.230 248.965 275.593 1.00 79.79  ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 215.540 248.141 276.837 1.00 81.72  ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 216.664 247.657 277.012 1.00 83.93  ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 215.280 250.461 275.904 1.00 83.29  ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 215.276 251.317 274.652 1.00 86.48  ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 215.775 250.845 273.608 1.00 86.27  ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 214.771 252.458 274.708 1.00 83.52  ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 214.552 247.979 277.720 1.00 82.61  ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 214.771 247.220 278.948 1.00 80.88  ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 215.075 245.755 278.655 1.00 80.29  ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 215.892 245.134 279.345 1.00 80.55  ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 213.555 247.349 279.865 1.00 81.33  ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 213.140 248.792 280.078 1.00 83.46  ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 213.963 249.577 280.595 1.00 83.46  ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 211.995 249.143 279.724 1.00 82.63  ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 214.415 245.181 277.647 1.00 76.78  ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 214.681 243.792 277.283 1.00 75.46  ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 216.103 243.621 276.763 1.00 75.04  ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 216.791 242.652 277.105 1.00 78.35  ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 213.666 243.319 276.241 1.00 73.73  ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 213.978 242.000 275.530 1.00 72.30  ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 213.972 240.834 276.507 1.00 72.01  ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 212.993 241.759 274.397 1.00 75.53  ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 216.564 244.560 275.934 1.00 70.34  ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 217.899 244.439 275.356 1.00 69.39  ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 218.978 244.710 276.396 1.00 75.10  ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 219.992 244.005 276.445 1.00 76.89  ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 218.045 245.392 274.171 1.00 74.26  ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 217.249 244.985 272.966 1.00 76.00  ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 217.305 243.688 272.486 1.00 70.71  ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 216.446 245.903 272.310 1.00 75.95  ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 216.572 243.313 271.377 1.00 70.46  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 215.712 245.534 271.201 1.00 73.46  ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 215.775 244.238 270.734 1.00 74.61  ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 218.778 245.730 277.234 1.00 83.09  ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 219.767 246.057 278.257 1.00 80.43  ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 219.916 244.920 279.259 1.00 80.76  ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 221.018 244.650 279.751 1.00 80.37  ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 219.376 247.355 278.964 1.00 81.16  ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 219.521 248.571 278.071 1.00 84.77  ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 220.495 248.698 277.328 1.00 83.31  ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 218.548 249.472 278.137 1.00 81.83  ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 218.810 244.246 279.582 1.00 79.22  ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 218.874 243.107 280.492 1.00 78.40  ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 219.722 241.985 279.903 1.00 76.65  ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 220.523 241.361 280.607 1.00 79.38  ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 217.462 242.611 280.808 1.00 78.80  ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 217.410 241.468 281.808 1.00 81.53  ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 217.982 241.885 283.153 1.00 80.66  ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 217.197 243.043 283.749 1.00 80.80  ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 217.765 243.487 285.051 1.00 78.94  ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 219.554 241.713 278.607 1.00 71.56  ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 220.355 240.682 277.953 1.00 71.86  ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 221.815 241.111 277.870 1.00 77.76  ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 222.726 240.313 278.122 1.00 79.45  ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 219.779 240.359 276.562 1.00 70.58  ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 220.653 239.341 275.848 1.00 75.51  ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 218.357 239.845 276.685 1.00 73.30  ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 222.061 242.374 277.512 1.00 78.48  ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 223.433 242.853 277.366 1.00 76.80  ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 224.181 242.804 278.693 1.00 82.13  ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 225.349 242.399 278.745 1.00 82.82  ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 223.437 244.274 276.800 1.00 80.68  ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 222.936 244.378 275.369 1.00 82.77  ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 223.018 245.806 274.855 1.00 81.02  ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 222.442 245.921 273.454 1.00 80.80  ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 223.271 245.201 272.449 1.00 81.57  ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 223.525 243.214 279.780 1.00 82.90  ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 224.191 243.214 281.078 1.00 79.99  ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 224.367 241.797 281.609 1.00 82.20  ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 225.320 241.516 282.346 1.00 87.11  ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 223.415 244.082 282.072 1.00 82.25  ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 222.275 243.379 282.790 1.00 85.49  ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 221.357 244.347 283.509 1.00 85.78  ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 221.017 245.394 282.920 1.00 85.11  ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 220.976 244.061 284.664 1.00 83.83  ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 223.458 240.887 281.248 1.00 81.36  ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 223.602 239.499 281.674 1.00 77.22  ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 224.671 238.780 280.862 1.00 79.34  ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 225.397 237.933 281.394 1.00 84.55  ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 222.260 238.776 281.570 1.00 77.50  ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 221.353 239.020 282.735 1.00 80.13  ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 220.141 238.380 282.882 1.00 80.05  ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 221.482 239.833 283.810 1.00 82.25  ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 219.562 238.789 283.997 1.00 84.75  ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 220.355 239.671 284.578 1.00 83.57  ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 224.779 239.098 279.569 1.00 80.77  ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 225.853 238.539 278.754 1.00 82.79  ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 227.208 239.008 279.269 1.00 83.86  ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 228.154 238.219 279.378 1.00 87.31  ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 225.647 238.908 277.273 1.00 81.24  ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 224.534 238.058 276.660 1.00 80.14  ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 226.939 238.737 276.489 1.00 80.26  ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 224.229 238.399 275.219 1.00 82.14  ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 227.321 240.297 279.597 1.00 84.23  ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 228.567 240.816 280.151 1.00 85.90  ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 228.864 240.199 281.512 1.00 88.60  ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 230.024 239.913 281.832 1.00 89.67  ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 228.499 242.340 280.254 1.00 87.22  ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 228.600 243.020 278.904 1.00 88.34  ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 229.179 242.476 277.964 1.00 87.64  ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 228.032 244.216 278.799 1.00 88.21  ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 227.828 239.994 282.331 1.00 86.55  ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 228.027 239.377 283.639 1.00 85.43  ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 228.552 237.953 283.504 1.00 87.22  ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 229.427 237.531 284.268 1.00 91.36  ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 226.721 239.395 284.432 1.00 86.63  ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 226.326 240.722 284.733 1.00 88.28  ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 228.023 237.195 282.540 1.00 88.59  ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 228.527 235.846 282.298 1.00 89.06  ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 229.974 235.901 281.823 1.00 90.72  ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 230.811 235.089 282.238 1.00 94.14  ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 227.622 235.110 281.292 1.00 88.05  ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 228.293 233.838 280.795 1.00 90.05  ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 226.275 234.794 281.925 1.00 87.09  ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 230.292 236.860 280.949 1.00 93.91  ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 231.670 237.023 280.496 1.00 94.73  ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 232.591 237.393 281.653 1.00 94.93  ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 233.714 236.885 281.750 1.00 93.51  ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 231.740 238.079 279.394 1.00 93.36  ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 231.068 237.640 278.226 1.00 93.60  ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 232.135 238.283 282.539 1.00 98.05  ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 232.911 238.593 283.735 1.00 100.47 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 233.027 237.373 284.637 1.00 99.83  ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 234.052 237.173 285.300 1.00 98.65  ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 232.276 239.762 284.488 1.00 97.82  ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 231.981 236.548 284.678 1.00 101.19 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 232.029 235.317 285.457 1.00 101.32 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 233.066 234.351 284.899 1.00 101.93 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 233.647 233.552 285.644 1.00 102.26 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 230.644 234.678 285.479 1.00 100.15 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 230.492 233.501 286.408 1.00 102.32 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 229.030 232.589 285.907 1.00 107.55 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 227.841 233.927 285.943 1.00 103.55 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 233.315 234.411 283.589 1.00 102.91 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 234.315 233.541 282.980 1.00 103.21 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 235.728 233.927 283.398 1.00 105.03 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 236.652 233.114 283.281 1.00 103.16 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 234.184 233.584 281.457 1.00 101.98 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 232.921 232.929 280.923 1.00 102.96 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 232.779 233.129 279.422 1.00 104.27 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 233.806 232.319 278.647 1.00 104.28 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 233.599 232.421 277.175 1.00 102.87 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 235.915 235.156 283.884 1.00 111.42 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 237.251 235.620 284.246 1.00 110.07 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 237.718 235.007 285.561 1.00 110.24 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 238.921 234.809 285.768 1.00 109.29 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 237.266 237.146 284.332 1.00 107.63 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 236.755 237.918 283.113 1.00 109.28 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 237.065 239.400 283.252 1.00 107.56 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 237.355 237.362 281.830 1.00 109.10 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 236.787 234.712 286.462 1.00 116.23 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 237.159 234.211 287.777 1.00 115.38 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 237.808 232.834 287.656 1.00 118.00 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 237.388 232.018 286.826 1.00 117.19 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 235.933 234.136 288.688 1.00 114.92 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 235.027 233.140 288.244 1.00 115.58 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 238.838 232.542 288.459 1.00 120.72 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 239.466 231.212 288.404 1.00 119.56 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 238.552 230.081 288.844 1.00 119.78 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 238.802 228.928 288.466 1.00 118.85 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 240.666 231.353 289.349 1.00 118.74 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 240.268 232.433 290.298 1.00 118.74 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 239.434 233.397 289.500 1.00 118.87 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 237.508 230.365 289.621 1.00 120.92 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 236.559 229.355 290.066 1.00 120.86 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 235.414 229.161 289.081 1.00 120.08 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 234.360 228.644 289.463 1.00 119.61 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 236.009 229.724 291.446 1.00 120.16 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 237.064 229.786 292.526 1.00 121.27 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 237.546 228.627 293.121 1.00 119.89 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 237.582 231.003 292.949 1.00 121.57 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 238.511 228.679 294.109 1.00 121.17 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 238.548 231.065 293.936 1.00 122.23 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 239.009 229.900 294.512 1.00 122.53 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 239.970 229.956 295.495 1.00 119.61 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 235.597 229.574 287.826 1.00 115.20 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 234.533 229.458 286.835 1.00 115.22 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 234.369 228.026 286.340 1.00 115.51 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 233.294 227.661 285.851 1.00 117.21 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 234.819 230.406 285.669 1.00 113.96 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 233.943 230.202 284.457 1.00 114.62 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 232.564 230.340 284.541 1.00 116.03 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 234.495 229.872 283.227 1.00 113.01 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 231.761 230.154 283.435 1.00 115.98 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 233.700 229.686 282.115 1.00 113.76 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 232.333 229.826 282.225 1.00 115.56 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 231.535 229.641 281.119 1.00 115.11 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 235.410 227.200 286.470 1.00 114.34 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 235.387 225.864 285.879 1.00 114.61 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 234.301 224.989 286.495 1.00 114.54 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 233.630 224.225 285.791 1.00 114.64 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 236.759 225.205 286.026 1.00 114.07 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 236.848 223.822 285.400 1.00 114.95 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 236.642 223.887 283.894 1.00 115.89 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 237.812 224.563 283.201 1.00 115.57 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 237.646 224.574 281.721 1.00 114.08 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 234.119 225.078 287.815 1.00 115.74 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 233.120 224.242 288.479 1.00 116.48 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 231.716 224.606 288.012 1.00 117.22 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 230.812 223.761 287.997 1.00 115.35 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 233.261 224.346 290.010 1.00 115.50 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 234.530 223.646 290.471 1.00 114.30 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 233.268 225.798 290.448 1.00 116.24 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 231.506 225.865 287.627 1.00 117.04 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 230.242 226.312 287.056 1.00 114.93 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 230.356 226.630 285.572 1.00 113.62 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 229.563 227.423 285.053 1.00 113.88 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 229.715 227.528 287.820 1.00 113.78 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 229.325 227.225 289.234 1.00 115.26 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 228.103 226.638 289.514 1.00 115.34 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 230.181 227.514 290.282 1.00 115.31 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 227.738 226.351 290.812 1.00 117.31 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 229.822 227.228 291.583 1.00 115.67 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 228.599 226.644 291.846 1.00 116.80 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 231.329 226.033 284.881 1.00 107.67 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 231.525 226.315 283.463 1.00 106.09 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 230.334 225.847 282.636 1.00 105.73 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 229.882 226.550 281.725 1.00 108.24 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 232.815 225.650 282.981 1.00 107.38 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 233.418 226.262 281.730 1.00 107.21 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 232.960 225.577 280.461 1.00 109.48 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 232.558 224.396 280.531 1.00 107.08 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 233.012 226.218 279.391 1.00 111.03 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 229.807 224.660 282.945 1.00 102.02 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 228.769 224.063 282.110 1.00 103.17 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 227.473 224.865 282.158 1.00 103.86 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 226.866 225.148 281.119 1.00 104.51 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 228.516 222.619 282.545 1.00 104.63 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 227.290 221.989 281.901 1.00 103.68 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 226.983 220.611 282.452 1.00 104.52 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 226.806 220.489 283.682 1.00 102.82 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 226.920 219.651 281.656 1.00 104.45 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 227.031 225.236 283.361 1.00 99.48  ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 225.739 225.903 283.495 1.00 99.64  ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 225.778 227.304 282.895 1.00 100.19 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 224.779 227.788 282.351 1.00 101.61 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 225.319 225.950 284.965 1.00 99.23  ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 223.905 226.469 285.149 1.00 100.32 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 222.973 225.869 284.574 1.00 99.83  ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 223.722 227.470 285.870 1.00 100.81 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 226.927 227.978 282.996 1.00 98.26  ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 227.054 229.306 282.405 1.00 95.92  ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 227.023 229.241 280.883 1.00 95.65  ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 226.557 230.179 280.226 1.00 98.37  ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 228.338 229.976 282.889 1.00 95.17  ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 227.524 228.147 280.304 1.00 93.04  ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 227.460 227.977 278.855 1.00 91.52  ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 226.015 227.929 278.377 1.00 90.54  ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 225.670 228.509 277.341 1.00 95.07  ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 228.201 226.708 278.434 1.00 93.85  ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 229.724 226.674 278.562 1.00 94.62  ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 230.249 225.321 278.109 1.00 92.42  ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 230.364 227.799 277.766 1.00 92.43  ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 225.157 227.224 279.117 1.00 86.43  ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 223.741 227.179 278.771 1.00 86.59  ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 223.116 228.565 278.858 1.00 86.59  ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 222.334 228.965 277.989 1.00 89.01  ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 223.009 226.196 279.686 1.00 89.03  ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 222.960 226.679 281.017 1.00 93.06  ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 223.453 229.316 279.910 1.00 86.94  ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 222.952 230.680 280.028 1.00 86.30  ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 223.535 231.576 278.944 1.00 87.27  ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 222.827 232.414 278.375 1.00 91.49  ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 223.257 231.238 281.418 1.00 86.88  ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 222.225 230.863 282.432 1.00 86.29  ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 222.412 230.109 283.553 1.00 86.69  ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 220.834 231.207 282.407 1.00 87.30  ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 221.228 229.971 284.234 1.00 91.00  ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 220.243 230.635 283.550 1.00 88.95  ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 220.033 231.947 281.532 1.00 86.73  ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 218.889 230.779 283.841 1.00 88.36  ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 218.689 232.088 281.822 1.00 87.46  ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 218.131 231.508 282.967 1.00 88.34  ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 224.826 231.414 278.643 1.00 87.17  ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 225.424 232.148 277.534 1.00 83.83  ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 224.765 231.803 276.207 1.00 83.73  ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 224.564 232.695 275.376 1.00 86.52  ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 226.927 231.865 277.464 1.00 86.28  ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 227.662 232.617 276.361 1.00 88.42  ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 227.660 234.121 276.565 1.00 92.44  ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 227.547 234.570 277.724 1.00 95.14  ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 227.772 234.856 275.561 1.00 91.32  ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 224.424 230.532 275.991 1.00 79.88  ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 223.713 230.145 274.779 1.00 77.21  ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 222.302 230.723 274.764 1.00 78.31  ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 221.855 231.273 273.752 1.00 83.75  ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 223.674 228.620 274.660 1.00 80.26  ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 223.101 228.153 273.337 1.00 81.50  ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 223.383 228.796 272.304 1.00 82.78  ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 222.366 227.143 273.330 1.00 80.41  ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 221.587 230.610 275.886 1.00 76.46  ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 220.206 231.083 275.939 1.00 75.60  ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 220.129 232.594 275.758 1.00 75.84  ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 219.244 233.102 275.061 1.00 79.42  ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 219.554 230.663 277.257 1.00 77.97  ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 219.120 229.206 277.297 1.00 81.20  ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 218.509 228.844 278.642 1.00 78.13  ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 219.566 228.740 279.727 1.00 79.70  ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 219.004 228.189 280.991 1.00 77.54  ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 221.049 233.331 276.386 1.00 70.81  ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 221.056 234.784 276.248 1.00 70.09  ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 221.316 235.198 274.805 1.00 70.30  ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 220.724 236.160 274.304 1.00 74.04  ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 222.101 235.394 277.184 1.00 72.63  ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 221.757 235.390 278.674 1.00 71.61  ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 222.935 235.889 279.492 1.00 73.90  ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 220.520 236.229 278.938 1.00 69.29  ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 222.214 234.483 274.125 1.00 66.95  ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 222.461 234.750 272.712 1.00 63.88  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 221.217 234.471 271.878 1.00 63.03  ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 220.895 235.219 270.947 1.00 70.30  ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 223.643 233.912 272.222 1.00 67.80  ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 224.967 234.387 272.787 1.00 70.91  ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 225.041 235.433 273.430 1.00 70.64  ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 226.021 233.614 272.553 1.00 68.12  ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 220.506 233.386 272.195 1.00 64.22  ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 219.270 233.069 271.486 1.00 64.03  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 218.202 234.126 271.739 1.00 64.35  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 217.450 234.497 270.831 1.00 67.35  ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 218.767 231.685 271.900 1.00 70.09  ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 219.716 230.548 271.559 1.00 67.52  ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 218.955 229.301 271.140 1.00 68.61  ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 217.889 228.967 272.078 1.00 70.13  ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 218.081 228.409 273.266 1.00 71.09  ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 219.292 228.096 273.697 1.00 70.91  ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 217.030 228.155 274.040 1.00 71.16  ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 218.113 234.616 272.979 1.00 64.96  ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 217.134 235.653 273.308 1.00 61.76  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 217.434 236.926 272.527 1.00 65.64  ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 216.538 237.554 271.950 1.00 65.25  ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 217.113 235.918 274.823 1.00 61.70  ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 216.539 234.713 275.569 1.00 65.21  ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 216.305 237.166 275.137 1.00 66.22  ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 216.613 234.838 277.074 1.00 66.45  ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 218.708 237.323 272.497 1.00 71.42  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 219.095 238.524 271.765 1.00 61.82  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 218.828 238.371 270.273 1.00 60.40  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 218.310 239.286 269.625 1.00 66.02  ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 220.569 238.840 272.019 1.00 64.73  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 221.067 240.079 271.294 1.00 67.35  ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 220.204 241.577 271.803 1.00 78.17  ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 221.134 242.017 273.267 1.00 68.75  ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 219.174 237.211 269.712 1.00 63.07  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 218.978 236.984 268.284 1.00 57.13  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 217.498 236.969 267.923 1.00 60.43  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 217.100 237.455 266.859 1.00 66.97  ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 219.649 235.675 267.866 1.00 58.95  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 216.667 236.400 268.798 1.00 59.18  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 215.239 236.303 268.512 1.00 56.63  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 214.588 237.680 268.460 1.00 55.90  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 213.829 237.987 267.533 1.00 64.02  ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 214.553 235.422 269.556 1.00 63.72  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 213.072 235.134 269.308 1.00 55.11  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 212.913 234.064 268.245 1.00 59.15  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 212.384 234.719 270.598 1.00 59.99  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 214.873 238.526 269.448 1.00 64.79  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 214.256 239.844 269.516 1.00 62.73  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 215.013 240.903 268.725 1.00 63.58  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 214.500 242.015 268.568 1.00 72.06  ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 214.108 240.278 270.975 1.00 63.88  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 213.204 239.386 271.778 1.00 66.23  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 211.838 239.381 271.549 1.00 64.15  ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 213.717 238.550 272.754 1.00 66.73  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 211.001 238.561 272.280 1.00 61.79  ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 212.885 237.727 273.489 1.00 69.03  ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 211.525 237.733 273.252 1.00 66.21  ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 216.210 240.594 268.225 1.00 61.15  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 216.860 241.470 267.259 1.00 61.57  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 216.143 241.477 265.918 1.00 64.60  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 216.289 242.440 265.158 1.00 69.94  ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 218.320 241.055 267.059 1.00 63.59  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 219.204 242.213 266.642 1.00 69.18  ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 219.299 243.196 267.406 1.00 65.22  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 219.806 242.140 265.550 1.00 70.50  ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 215.380 240.431 265.617 1.00 57.91  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 214.581 240.361 264.403 1.00 57.77  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 213.120 240.694 264.677 1.00 57.70  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 212.444 241.272 263.826 1.00 64.01  ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 214.723 238.964 263.759 1.00 55.87  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 213.974 238.900 262.437 1.00 59.56  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 216.191 238.615 263.567 1.00 61.06  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 212.626 240.346 265.868 1.00 62.73  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 211.228 240.602 266.198 1.00 58.63  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 210.938 242.098 266.224 1.00 65.40  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 209.825 242.529 265.900 1.00 72.30  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 210.883 239.972 267.548 1.00 61.79  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 209.440 240.116 267.939 1.00 67.35  ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 208.919 240.998 268.832 1.00 77.17  ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 208.346 239.306 267.498 1.00 65.24  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 207.563 240.823 268.941 1.00 77.77  ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 207.188 239.780 268.139 1.00 70.35  ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 208.232 238.233 266.615 1.00 74.68  ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 205.935 239.220 267.922 1.00 72.18  ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 206.990 237.682 266.397 1.00 80.84  ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 205.858 238.172 267.049 1.00 78.10  ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 211.928 242.906 266.616 1.00 60.86  ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 211.741 244.354 266.659 1.00 56.16  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 211.564 244.923 265.258 1.00 56.46  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 210.792 245.868 265.056 1.00 61.40  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 212.910 245.024 267.414 1.00 54.91  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 212.600 246.497 267.690 1.00 57.92  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 214.228 244.861 266.664 1.00 57.75  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 213.567 247.154 268.652 1.00 57.76  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 212.265 244.365 264.271 1.00 57.02  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 212.107 244.798 262.889 1.00 52.63  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 210.854 244.230 262.240 1.00 56.93  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 210.245 244.898 261.397 1.00 61.62  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 213.336 244.399 262.068 1.00 57.25  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 214.615 245.017 262.597 1.00 65.17  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 214.707 246.262 262.628 1.00 69.70  ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 215.529 244.257 262.980 1.00 61.66  ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 210.459 243.010 262.610 1.00 60.10  ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 209.261 242.408 262.035 1.00 55.00  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 208.010 243.118 262.536 1.00 59.70  ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 207.101 243.426 261.755 1.00 60.66  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 209.221 240.902 262.346 1.00 52.87  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 207.876 240.311 261.956 1.00 56.54  ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 210.346 240.188 261.624 1.00 55.61  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 207.939 243.387 263.841 1.00 56.57  ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 206.766 244.056 264.394 1.00 52.21  ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 206.634 245.474 263.852 1.00 55.52  ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 205.536 245.908 263.489 1.00 64.32  ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 206.836 244.070 265.921 1.00 54.95  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 205.758 244.921 266.573 1.00 55.91  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 205.695 244.740 268.074 1.00 58.06  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 205.344 243.669 268.568 1.00 61.96  ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 206.032 245.792 268.811 1.00 55.79  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 207.748 246.207 263.781 1.00 55.79  ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 207.702 247.587 263.307 1.00 51.89  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 207.232 247.656 261.859 1.00 50.35  ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 206.422 248.517 261.497 1.00 60.86  ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 209.076 248.238 263.457 1.00 57.09  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 209.145 249.662 262.930 1.00 60.80  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 210.539 250.244 263.095 1.00 57.14  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 211.553 249.434 262.431 1.00 60.44  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 211.732 249.382 261.118 1.00 65.27  ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 210.987 250.094 260.288 1.00 61.33  ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 212.686 248.597 260.624 1.00 61.57  ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 207.734 246.753 261.014 1.00 47.91  ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 207.315 246.742 259.617 1.00 41.82  ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 205.849 246.357 259.475 1.00 50.94  ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 205.182 246.796 258.533 1.00 57.28  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 208.198 245.791 258.809 1.00 47.05  ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 209.420 246.455 258.199 1.00 52.07  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 209.953 245.664 257.014 1.00 58.51  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 210.963 244.689 257.407 1.00 64.25  ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 212.203 244.994 257.768 1.00 66.57  ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 212.631 246.246 257.785 1.00 62.61  ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 213.036 244.017 258.116 1.00 61.72  ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 205.331 245.542 260.396 1.00 55.36  ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 203.929 245.143 260.321 1.00 49.76  ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 202.998 246.295 260.680 1.00 56.82  ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 201.887 246.387 260.147 1.00 63.34  ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 203.672 243.947 261.237 1.00 52.81  ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 202.288 243.391 261.109 1.00 55.04  ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 201.850 242.485 260.189 1.00 51.63  ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 201.154 243.719 261.921 1.00 57.06  ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 200.516 242.221 260.382 1.00 55.49  ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 200.065 242.967 261.439 1.00 57.60  ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 200.955 244.572 263.010 1.00 56.96  ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 198.796 243.042 262.008 1.00 55.72  ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 199.695 244.645 263.574 1.00 53.87  ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 198.632 243.885 263.073 1.00 53.14  ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 203.427 247.176 261.588 1.00 58.50  ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 202.543 248.233 262.077 1.00 53.10  ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 202.161 249.184 260.949 1.00 58.64  ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 200.981 249.497 260.752 1.00 61.08  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 203.196 248.985 263.251 1.00 54.74  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 202.304 250.127 263.704 1.00 60.29  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 203.451 248.038 264.406 1.00 54.03  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 203.150 249.659 260.188 1.00 53.62  ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 202.842 250.610 259.127 1.00 51.60  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 202.438 249.931 257.825 1.00 55.59  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 201.861 250.590 256.955 1.00 66.43  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 204.023 251.562 258.896 1.00 53.54  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 205.297 250.942 258.356 1.00 49.35  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 205.421 250.605 257.014 1.00 50.24  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 206.394 250.741 259.183 1.00 51.53  ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 206.586 250.055 256.519 1.00 47.60  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 207.564 250.192 258.696 1.00 54.33  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 207.655 249.852 257.363 1.00 52.77  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 208.817 249.307 256.872 1.00 61.02  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 202.722 248.638 257.667 1.00 56.86  ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 202.203 247.919 256.510 1.00 53.13  ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 200.728 247.585 256.686 1.00 55.36  ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 199.966 247.593 255.713 1.00 55.98  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 203.014 246.646 256.265 1.00 53.10  ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 204.239 246.795 255.361 1.00 53.88  ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 204.853 245.438 255.057 1.00 53.89  ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 203.872 247.521 254.079 1.00 57.31  ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 200.310 247.289 257.919 1.00 61.47  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 198.903 247.003 258.180 1.00 59.61  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 198.038 248.228 257.916 1.00 66.66  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 196.944 248.120 257.352 1.00 72.43  ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 198.727 246.513 259.618 1.00 58.80  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 197.343 245.967 259.924 1.00 66.58  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 196.455 246.984 260.612 1.00 71.92  ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 196.953 248.078 260.952 1.00 69.67  ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 195.258 246.690 260.814 1.00 71.39  ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 198.515 249.408 258.318 1.00 57.84  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 197.768 250.631 258.086 1.00 54.95  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 197.588 250.973 256.623 1.00 59.44  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 196.528 251.480 256.239 1.00 63.57  ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 198.599 250.711 255.795 1.00 56.11  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 198.489 250.990 254.368 1.00 56.40  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 197.509 250.033 253.700 1.00 63.18  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 196.710 250.440 252.849 1.00 67.00  ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 199.880 250.933 253.712 1.00 53.96  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 200.779 252.024 254.291 1.00 59.71  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 199.771 251.083 252.205 1.00 57.08  ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 202.228 251.886 253.908 1.00 59.26  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 197.542 248.758 254.076 1.00 64.19  ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 196.683 247.749 253.473 1.00 62.10  ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 195.294 247.696 254.096 1.00 64.00  ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 194.461 246.902 253.649 1.00 71.79  ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 197.343 246.370 253.566 1.00 60.38  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 198.442 246.156 252.564 1.00 58.19  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 198.151 246.001 251.220 1.00 60.34  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 199.765 246.110 252.967 1.00 57.12  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 199.159 245.804 250.297 1.00 60.52  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 200.777 245.914 252.048 1.00 58.13  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 200.474 245.760 250.712 1.00 59.58  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 195.025 248.512 255.110 1.00 70.36  ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 193.706 248.588 255.728 1.00 73.74  ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 193.101 249.980 255.666 1.00 72.84  ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 191.892 250.113 255.455 1.00 76.23  ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 193.778 248.130 257.194 1.00 73.98  ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 194.425 246.854 257.266 1.00 69.02  ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 192.383 248.016 257.791 1.00 74.87  ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 193.912 251.026 255.838 1.00 82.95  ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 193.381 252.378 255.785 1.00 87.76  ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 192.873 252.760 254.408 1.00 90.23  ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 191.833 253.412 254.280 1.00 89.93  ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 193.593 252.362 253.364 1.00 91.03  ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 193.225 252.678 251.990 1.00 92.07  ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 192.447 251.509 251.398 1.00 92.89  ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 192.944 250.378 251.369 1.00 95.02  ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 194.465 252.978 251.148 1.00 91.19  ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 195.245 251.811 250.954 1.00 92.61  ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 191.234 251.785 250.927 1.00 100.74 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 190.393 250.779 250.295 1.00 104.62 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 190.697 250.604 248.814 1.00 105.34 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 190.060 249.773 248.158 1.00 104.03 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 188.914 251.135 250.478 1.00 101.50 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 191.651 251.363 248.276 1.00 100.47 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 191.967 251.328 246.856 1.00 99.69  ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 193.211 250.508 246.536 1.00 100.27 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 193.452 250.208 245.361 1.00 104.04 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 192.139 252.763 246.335 1.00 100.29 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 192.330 252.825 244.835 1.00 104.27 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 191.341 252.629 244.099 1.00 104.23 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 193.469 253.085 244.395 1.00 102.24 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 193.994 250.124 247.547 1.00 91.80  ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 195.213 249.362 247.299 1.00 91.93  ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 194.916 247.931 246.866 1.00 91.07  ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 195.752 247.302 246.206 1.00 89.90  ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 196.116 249.386 248.549 1.00 89.09  ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 197.531 248.920 248.200 1.00 86.02  ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 195.522 248.537 249.664 1.00 89.55  ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 198.560 249.265 249.247 1.00 86.12  ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 193.742 247.395 247.210 1.00 91.30  ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 193.401 246.032 246.818 1.00 92.51  ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 193.210 245.880 245.314 1.00 93.28  ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 193.242 244.751 244.813 1.00 90.95  ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 192.140 245.564 247.551 1.00 93.46  ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 192.385 245.030 248.960 1.00 96.01  ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 192.701 246.119 249.971 1.00 96.01  ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 191.494 246.991 250.259 1.00 94.28  ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 191.807 248.009 251.299 1.00 92.18  ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 193.016 246.978 244.585 1.00 101.68 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 192.808 246.900 243.144 1.00 101.63 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 194.093 247.159 242.363 1.00 101.71 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 194.421 246.408 241.439 1.00 102.92 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 191.716 247.886 242.720 1.00 101.77 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 190.381 247.608 243.339 1.00 105.41 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 189.554 246.597 242.901 1.00 103.94 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 189.731 248.208 244.365 1.00 103.73 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 188.451 246.586 243.629 1.00 102.19 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 188.534 247.554 244.524 1.00 104.54 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 194.827 248.217 242.715 1.00 95.32  ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 196.081 248.510 242.026 1.00 95.56  ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 197.126 247.432 242.288 1.00 96.28  ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 197.885 247.064 241.385 1.00 95.31  ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 196.611 249.884 242.440 1.00 96.06  ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 196.017 251.129 241.768 1.00 100.30 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 196.285 251.101 240.270 1.00 96.43  ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 194.528 251.283 242.040 1.00 97.51  ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 197.180 246.912 243.513 1.00 92.26  ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 198.149 245.889 243.904 1.00 90.53  ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 197.394 244.714 244.511 1.00 90.95  ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 197.372 244.539 245.737 1.00 88.21  ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 199.183 246.453 244.879 1.00 88.13  ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 199.887 247.740 244.445 1.00 87.77  ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 200.837 248.221 245.525 1.00 85.11  ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 200.628 247.533 243.134 1.00 86.44  ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 196.758 243.885 243.677 1.00 89.68  ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 195.961 242.771 244.208 1.00 87.33  ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 196.813 241.658 244.795 1.00 86.90  ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 196.529 241.168 245.893 1.00 85.99  ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 195.175 242.279 242.982 1.00 86.75  ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 195.403 243.306 241.902 1.00 86.76  ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 196.716 243.938 242.208 1.00 86.19  ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 197.861 241.251 244.075 1.00 86.54  ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 198.680 240.131 244.530 1.00 83.55  ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 199.473 240.510 245.776 1.00 82.65  ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 199.646 239.692 246.686 1.00 83.74  ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 199.592 239.629 243.393 1.00 81.80  ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 198.752 239.121 242.233 1.00 84.42  ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 200.531 240.727 242.919 1.00 80.54  ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 199.960 241.752 245.842 1.00 83.53  ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 200.690 242.197 247.026 1.00 79.69  ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 199.795 242.199 248.259 1.00 79.84  ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 200.244 241.864 249.361 1.00 80.51  ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 201.290 243.583 246.786 1.00 77.62  ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 202.394 243.616 245.736 1.00 82.23  ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 201.867 243.685 244.317 1.00 86.45  ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 200.635 243.769 244.139 1.00 87.27  ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 202.688 243.655 243.376 1.00 82.42  ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 198.528 242.585 248.095 1.00 77.11  ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 197.587 242.511 249.208 1.00 76.99  ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 197.367 241.069 249.648 1.00 81.04  ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 197.280 240.785 250.849 1.00 80.76  ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 196.258 243.159 248.822 1.00 75.24  ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 196.505 244.426 248.200 1.00 78.79  ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 195.394 243.366 250.056 1.00 76.32  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 197.272 240.143 248.690 1.00 84.43  ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 197.048 238.740 249.026 1.00 80.43  ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 198.210 238.171 249.831 1.00 80.02  ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 198.002 237.409 250.783 1.00 82.33  ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 196.819 237.923 247.754 1.00 82.01  ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 195.575 238.320 246.977 1.00 83.80  ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 194.847 237.126 246.393 1.00 83.85  ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 194.651 236.114 247.065 1.00 83.62  ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 194.439 237.240 245.134 1.00 84.19  ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 199.444 238.519 249.457 1.00 77.24  ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 200.597 238.063 250.227 1.00 75.71  ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 200.566 238.614 251.646 1.00 74.35  ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 200.847 237.888 252.607 1.00 80.04  ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 201.899 238.463 249.531 1.00 70.77  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 201.964 238.115 248.056 1.00 73.65  ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 203.375 238.291 247.517 1.00 79.45  ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 203.572 239.604 246.912 1.00 83.77  ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 204.754 240.106 246.580 1.00 78.57  ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 205.873 239.430 246.780 1.00 78.78  ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 204.814 241.317 246.034 1.00 72.67  ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 200.223 239.895 251.799 1.00 65.15  ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 200.197 240.493 253.129 1.00 67.15  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 199.114 239.881 254.006 1.00 69.34  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 199.338 239.672 255.203 1.00 71.88  ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 200.002 242.005 253.033 1.00 64.95  ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 200.071 242.703 254.360 1.00 62.26  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 201.285 242.868 255.005 1.00 59.39  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 198.924 243.184 254.968 1.00 62.95  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 201.355 243.503 256.228 1.00 59.74  ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 198.988 243.821 256.192 1.00 62.57  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 200.206 243.981 256.822 1.00 64.57  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 197.941 239.590 253.438 1.00 72.64  ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 196.870 238.985 254.223 1.00 74.11  ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 197.297 237.631 254.776 1.00 76.10  ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 197.015 237.302 255.933 1.00 78.31  ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 195.605 238.848 253.374 1.00 79.13  ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 194.974 240.173 252.978 1.00 78.89  ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 194.484 240.966 254.173 1.00 80.77  ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 193.965 240.402 255.136 1.00 78.29  ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 194.649 242.283 254.118 1.00 78.84  ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 197.980 236.830 253.957 1.00 74.76  ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 198.517 235.561 254.439 1.00 75.18  ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 199.585 235.789 255.502 1.00 74.65  ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 199.627 235.087 256.518 1.00 80.44  ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 199.080 234.754 253.269 1.00 76.22  ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 198.190 234.769 252.166 1.00 77.41  ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 200.461 236.770 255.280 1.00 68.11  ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 201.519 237.056 256.244 1.00 68.70  ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 200.939 237.670 257.513 1.00 68.18  ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 201.372 237.349 258.626 1.00 71.63  ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 202.588 237.961 255.605 1.00 69.24  ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 203.338 237.196 254.513 1.00 71.68  ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 203.561 238.476 256.654 1.00 68.66  ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 203.970 238.084 253.473 1.00 72.06  ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 199.952 238.559 257.369 1.00 62.14  ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 199.339 239.173 258.543 1.00 61.98  ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 198.644 238.134 259.414 1.00 68.31  ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 198.760 238.173 260.643 1.00 72.73  ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 198.353 240.260 258.117 1.00 66.25  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 197.772 240.893 259.244 1.00 68.69  ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 197.925 237.193 258.795 1.00 74.37  ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 197.243 236.159 259.568 1.00 73.75  ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 198.239 235.296 260.332 1.00 74.74  ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 198.008 234.952 261.497 1.00 74.14  ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 196.380 235.293 258.651 1.00 72.09  ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 197.132 234.926 257.488 1.00 74.95  ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 195.129 236.049 258.228 1.00 73.07  ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 199.352 234.932 259.691 1.00 71.96  ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 200.398 234.198 260.395 1.00 70.60  ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 201.012 235.047 261.500 1.00 71.69  ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 201.304 234.544 262.591 1.00 73.54  ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 201.469 233.735 259.408 1.00 70.74  ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 202.563 232.889 260.037 1.00 75.55  ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 203.580 232.403 259.024 1.00 80.93  ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 203.445 232.743 257.830 1.00 76.99  ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 204.510 231.673 259.424 1.00 78.24  ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 201.224 236.338 261.232 1.00 69.02  ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 201.721 237.238 262.267 1.00 62.96  ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 200.710 237.387 263.399 1.00 68.21  ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 201.086 237.386 264.577 1.00 70.84  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 202.060 238.598 261.656 1.00 64.40  ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 202.693 239.560 262.622 1.00 71.74  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 204.042 239.470 262.924 1.00 69.94  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 201.944 240.562 263.217 1.00 67.60  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 204.630 240.355 263.808 1.00 62.12  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 202.527 241.451 264.101 1.00 65.04  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 203.872 241.348 264.396 1.00 64.95  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 199.423 237.514 263.063 1.00 74.75  ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 198.393 237.582 264.096 1.00 71.20  ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 198.244 236.249 264.818 1.00 72.91  ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 197.880 236.216 265.999 1.00 75.38  ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 197.058 238.019 263.492 1.00 76.11  ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 196.984 239.430 262.903 1.00 72.61  ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 195.928 239.501 261.812 1.00 71.79  ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 196.704 240.451 263.993 1.00 74.07  ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 198.504 235.139 264.123 1.00 75.13  ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 198.490 233.840 264.786 1.00 75.71  ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 199.584 233.754 265.841 1.00 74.87  ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 199.384 233.169 266.911 1.00 75.44  ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 198.645 232.720 263.758 1.00 74.17  ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 200.752 234.334 265.554 1.00 74.97  ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 201.838 234.332 266.527 1.00 72.44  ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 201.555 235.309 267.664 1.00 75.88  ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 202.154 235.211 268.741 1.00 79.23  ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 203.156 234.664 265.825 1.00 74.31  ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 204.467 234.622 266.611 1.00 76.47  ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 204.512 233.410 267.525 1.00 75.61  ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 205.638 234.596 265.646 1.00 74.77  ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 200.638 236.257 267.444 1.00 80.17  ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 200.243 237.167 268.516 1.00 79.13  ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 199.584 236.415 269.663 1.00 82.34  ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 199.943 236.608 270.830 1.00 84.73  ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 199.293 238.237 267.979 1.00 84.94  ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 199.899 239.190 266.967 1.00 88.67  ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 201.264 240.152 267.633 1.00 94.06  ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 202.646 239.271 266.929 1.00 81.94  ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 198.615 235.552 269.348 1.00 83.62  ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 197.914 234.811 270.391 1.00 82.19  ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 198.853 233.851 271.108 1.00 85.78  ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 198.769 233.686 272.331 1.00 85.81  ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 196.725 234.054 269.795 1.00 83.00  ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 195.477 234.902 269.556 1.00 85.84  ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 195.639 235.842 268.369 1.00 87.34  ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 194.358 236.608 268.087 1.00 85.82  ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 194.546 237.612 267.004 1.00 86.30  ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 199.756 233.210 270.363 1.00 82.45  ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 200.693 232.273 270.973 1.00 78.52  ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 201.606 232.976 271.970 1.00 78.68  ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 201.878 232.448 273.055 1.00 80.81  ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 201.509 231.575 269.885 1.00 74.52  ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 202.429 230.480 270.390 1.00 80.82  ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 203.242 229.892 269.251 1.00 82.40  ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 202.385 229.010 268.358 1.00 79.76  ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 203.193 228.334 267.306 1.00 80.13  ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 202.092 234.169 271.619 1.00 84.36  ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 202.895 234.947 272.557 1.00 84.68  ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 202.028 235.477 273.692 1.00 81.82  ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 202.449 235.500 274.855 1.00 84.45  ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 203.626 236.083 271.817 1.00 82.80  ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 204.311 237.015 272.805 1.00 81.97  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 204.638 235.509 270.838 1.00 82.31  ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 200.802 235.907 273.378 1.00 81.14  ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 199.925 236.464 274.403 1.00 85.21  ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 199.508 235.416 275.427 1.00 88.09  ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 199.292 235.750 276.598 1.00 86.18  ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 198.691 237.092 273.756 1.00 85.89  ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 198.007 237.932 274.669 1.00 85.42  ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 199.377 234.153 275.010 1.00 86.31  ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 199.027 233.097 275.954 1.00 85.11  ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 200.117 232.907 277.001 1.00 84.76  ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 199.824 232.737 278.191 1.00 84.48  ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 198.766 231.788 275.209 1.00 84.05  ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 197.443 231.745 274.462 1.00 83.82  ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 197.220 230.388 273.815 1.00 83.66  ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 198.107 230.207 272.594 1.00 83.80  ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 197.815 228.939 271.870 1.00 84.72  ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 201.380 232.935 276.580 1.00 89.01  ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 202.524 232.762 277.474 1.00 90.14  ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 203.489 233.917 277.249 1.00 88.67  ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 204.447 233.800 276.474 1.00 90.04  ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 203.209 231.416 277.244 1.00 89.33  ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 204.036 231.456 276.094 1.00 91.18  ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 203.267 235.057 277.913 1.00 84.44  ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 204.137 236.223 277.701 1.00 86.00  ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 205.544 236.063 278.257 1.00 88.75  ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 206.349 236.991 278.119 1.00 89.89  ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 203.387 237.350 278.425 1.00 84.10  ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 202.591 236.655 279.472 1.00 86.73  ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 202.196 235.328 278.888 1.00 86.02  ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 205.865 234.934 278.882 1.00 88.37  ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 207.203 234.726 279.417 1.00 85.16  ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 208.221 234.639 278.286 1.00 83.44  ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 207.970 234.020 277.248 1.00 87.42  ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 207.238 233.453 280.261 1.00 88.08  ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 208.480 233.195 281.114 1.00 91.13  ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 208.584 234.219 282.232 1.00 87.38  ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 208.454 231.783 281.678 1.00 88.07  ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 209.379 235.271 278.493 1.00 81.06  ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 210.417 235.286 277.466 1.00 81.86  ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 210.938 233.878 277.204 1.00 85.60  ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 211.155 233.486 276.051 1.00 85.17  ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 211.550 236.249 277.867 1.00 81.25  ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 212.813 235.957 277.071 1.00 81.45  ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 211.113 237.685 277.655 1.00 80.31  ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 211.153 233.097 278.264 1.00 84.45  ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 211.635 231.731 278.082 1.00 81.99  ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 210.620 230.883 277.325 1.00 84.50  ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 210.997 230.030 276.512 1.00 84.93  ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 211.962 231.104 279.436 1.00 81.61  ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 213.123 231.768 280.155 1.00 84.57  ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 214.662 231.672 279.221 1.00 89.38  ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 215.014 229.919 279.327 1.00 84.20  ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 209.328 231.097 277.582 1.00 87.09  ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 208.302 230.342 276.869 1.00 86.46  ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 208.286 230.686 275.384 1.00 84.42  ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 208.200 229.791 274.535 1.00 84.26  ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 206.930 230.596 277.494 1.00 86.92  ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 206.801 229.991 278.879 1.00 90.89  ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 207.465 228.968 279.146 1.00 90.43  ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 206.028 230.532 279.697 1.00 90.49  ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 208.370 231.977 275.047 1.00 80.90  ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 208.366 232.364 273.641 1.00 81.31  ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 209.689 232.033 272.965 1.00 79.63  ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 209.742 231.929 271.734 1.00 82.74  ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 208.035 233.860 273.476 1.00 77.03  ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 206.761 234.211 274.226 1.00 80.24  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 209.194 234.725 273.937 1.00 76.60  ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 210.765 231.867 273.738 1.00 74.16  ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 212.040 231.472 273.151 1.00 74.34  ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 212.040 230.001 272.756 1.00 76.59  ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 212.713 229.619 271.792 1.00 75.87  ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 213.179 231.760 274.129 1.00 71.21  ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 214.598 231.453 273.647 1.00 75.03  ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 215.104 232.556 272.731 1.00 74.13  ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 215.535 231.254 274.827 1.00 78.34  ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 211.290 229.170 273.475 1.00 82.45  ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 211.233 227.738 273.217 1.00 81.36  ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 210.149 227.356 272.219 1.00 81.16  ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 209.924 226.160 272.002 1.00 81.07  ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 211.019 226.975 274.528 1.00 79.40  ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 212.217 227.062 275.454 1.00 80.09  ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 212.080 227.367 276.638 1.00 80.41  ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 213.401 226.797 274.915 1.00 77.64  ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 209.465 228.335 271.621 1.00 76.54  ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 208.468 228.033 270.603 1.00 74.30  ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 209.138 227.336 269.427 1.00 76.45  ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 210.225 227.726 268.983 1.00 76.66  ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 207.748 229.318 270.161 1.00 74.82  ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 206.956 229.912 271.327 1.00 73.88  ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 206.830 229.047 268.980 1.00 76.41  ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 206.165 231.149 270.961 1.00 74.22  ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 208.490 226.286 268.925 1.00 82.25  ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 209.061 225.484 267.851 1.00 81.74  ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 209.246 226.319 266.591 1.00 82.75  ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 208.270 226.777 265.988 1.00 81.88  ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 208.163 224.281 267.566 1.00 82.04  ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 208.702 223.343 266.500 1.00 82.20  ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 207.855 222.096 266.342 1.00 83.93  ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 206.653 222.176 266.092 1.00 84.37  ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 208.480 220.934 266.490 1.00 83.43  ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 210.502 226.511 266.196 1.00 77.01  ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 210.810 227.256 264.987 1.00 73.00  ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 210.392 228.708 265.023 1.00 75.50  ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 210.025 229.266 263.984 1.00 79.24  ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 210.436 229.339 266.198 1.00 70.42  ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 210.089 230.754 266.288 1.00 65.32  ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 211.146 231.609 265.598 1.00 66.98  ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 210.827 232.623 264.965 1.00 73.13  ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 209.882 231.161 267.760 1.00 67.08  ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 211.130 230.882 268.587 1.00 68.74  ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 209.478 232.626 267.861 1.00 64.06  ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 212.417 231.216 265.703 1.00 64.20  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 213.487 231.969 265.056 1.00 60.23  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 213.358 231.918 263.539 1.00 64.71  ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 213.408 232.953 262.865 1.00 68.74  ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 214.847 231.430 265.499 1.00 64.43  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 216.035 232.149 264.879 1.00 64.31  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 216.216 233.551 265.422 1.00 65.90  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 216.073 233.787 266.621 1.00 71.07  ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 216.535 234.491 264.541 1.00 64.91  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 213.185 230.716 262.983 1.00 70.91  ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 213.095 230.581 261.533 1.00 68.08  ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 211.816 231.211 260.997 1.00 67.64  ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 211.790 231.721 259.871 1.00 73.18  ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 213.179 229.109 261.132 1.00 71.01  ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 214.519 228.462 261.433 1.00 72.72  ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 214.533 227.005 261.005 1.00 76.46  ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 214.444 226.865 259.556 1.00 78.34  ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 213.380 226.405 258.912 1.00 75.96  ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 212.289 226.030 259.559 1.00 76.18  ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 213.412 226.321 257.585 1.00 69.76  ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 210.739 231.174 261.785 1.00 64.57  ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 209.513 231.860 261.390 1.00 66.27  ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 209.739 233.364 261.305 1.00 68.14  ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 209.138 234.050 260.471 1.00 70.46  ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 208.389 231.536 262.374 1.00 62.41  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 207.209 232.252 262.055 1.00 65.84  ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 210.612 233.894 262.165 1.00 68.04  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 210.893 235.325 262.154 1.00 62.55  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 211.722 235.724 260.940 1.00 63.47  ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 211.470 236.762 260.318 1.00 69.70  ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 211.600 235.729 263.445 1.00 65.48  ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 210.611 236.213 264.493 1.00 59.06  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 211.304 236.532 265.805 1.00 67.78  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 209.918 237.430 263.921 1.00 63.78  ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 212.727 234.917 260.596 1.00 65.92  ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 213.566 235.242 259.447 1.00 66.22  ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 212.749 235.259 258.162 1.00 67.97  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 212.959 236.114 257.295 1.00 72.62  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 214.723 234.250 259.341 1.00 68.46  ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 215.446 233.997 260.655 1.00 65.83  ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 216.552 235.000 260.924 1.00 72.10  ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 217.404 234.724 261.795 1.00 71.82  ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 216.572 236.062 260.268 1.00 72.45  ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 211.813 234.319 258.022 1.00 65.17  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 210.933 234.319 256.859 1.00 65.55  ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 209.974 235.504 256.896 1.00 68.49  ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 209.745 236.160 255.874 1.00 74.59  ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 210.168 232.998 256.783 1.00 66.41  ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 209.163 232.921 255.646 1.00 70.55  ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 208.288 231.681 255.770 1.00 70.50  ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 207.889 231.415 257.148 1.00 71.08  ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 207.060 232.171 257.856 1.00 74.39  ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 206.483 233.242 257.335 1.00 74.76  ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 206.798 231.841 259.117 1.00 70.71  ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 209.407 235.799 258.071 1.00 62.89  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 208.508 236.944 258.188 1.00 59.14  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 209.235 238.249 257.893 1.00 60.79  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 208.689 239.135 257.227 1.00 63.37  ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 207.876 236.986 259.579 1.00 55.63  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 206.702 236.039 259.833 1.00 60.85  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 206.113 236.275 261.214 1.00 62.27  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 205.640 236.204 258.760 1.00 61.16  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 210.467 238.389 258.387 1.00 64.58  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 211.264 239.568 258.062 1.00 58.57  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 211.549 239.636 256.568 1.00 67.07  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 211.497 240.711 255.960 1.00 72.39  ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 212.568 239.559 258.860 1.00 58.30  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 211.858 238.489 255.960 1.00 70.72  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 212.125 238.456 254.526 1.00 65.50  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 210.864 238.758 253.725 1.00 66.74  ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 210.889 239.564 252.787 1.00 70.01  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 212.702 237.094 254.137 1.00 68.71  ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 213.134 237.037 252.687 1.00 77.80  ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 214.182 237.628 252.353 1.00 74.73  ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 212.427 236.397 251.880 1.00 78.99  ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 209.746 238.120 254.084 1.00 63.02  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 208.507 238.318 253.337 1.00 63.70  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 207.985 239.742 253.485 1.00 65.81  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 207.498 240.335 252.515 1.00 72.85  ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 207.452 237.308 253.789 1.00 64.00  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 207.715 235.839 253.453 1.00 63.89  ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 206.462 235.008 253.670 1.00 65.76  ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 208.219 235.693 252.026 1.00 64.62  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 208.064 240.306 254.693 1.00 59.55  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 207.638 241.689 254.887 1.00 58.97  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 208.506 242.647 254.083 1.00 59.47  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 208.022 243.673 253.591 1.00 62.69  ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 207.669 242.050 256.373 1.00 58.26  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 206.481 241.576 257.213 1.00 54.78  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 206.574 242.123 258.628 1.00 56.16  ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 205.168 241.982 256.565 1.00 56.20  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 209.795 242.332 253.945 1.00 60.81  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 210.657 243.144 253.103 1.00 61.31  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 210.265 243.086 251.640 1.00 66.00  ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 210.365 244.083 250.921 1.00 68.40  ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 209.816 241.917 251.177 1.00 66.97  ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 209.403 241.780 249.783 1.00 63.57  ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 208.213 242.677 249.469 1.00 65.91  ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 208.158 243.300 248.402 1.00 72.56  ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 209.070 240.321 249.474 1.00 70.05  ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 210.226 239.358 249.683 1.00 69.16  ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 211.320 239.568 248.651 1.00 68.75  ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 212.484 238.622 248.891 1.00 69.78  ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 212.102 237.202 248.660 1.00 69.92  ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 207.244 242.748 250.384 1.00 60.54  ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 206.096 243.627 250.188 1.00 60.57  ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 206.527 245.087 250.236 1.00 64.05  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 205.992 245.931 249.508 1.00 65.48  ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 205.011 243.323 251.236 1.00 57.75  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 204.662 241.836 251.225 1.00 62.56  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 203.768 244.160 250.979 1.00 61.39  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 203.606 241.460 252.231 1.00 63.68  ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 207.497 245.407 251.096 1.00 68.87  ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 207.937 246.790 251.247 1.00 65.98  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 208.521 247.335 249.949 1.00 67.25  ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 208.235 248.474 249.562 1.00 70.63  ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 208.960 246.886 252.379 1.00 68.28  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 209.113 248.277 252.962 1.00 66.78  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 210.505 248.535 253.499 1.00 72.54  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 211.360 247.649 253.493 1.00 76.28  ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 210.741 249.754 253.969 1.00 70.02  ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 209.340 246.537 249.260 1.00 69.05  ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 209.928 246.985 248.002 1.00 70.16  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 208.951 246.896 246.838 1.00 70.83  ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 209.236 247.438 245.765 1.00 74.03  ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 211.189 246.177 247.680 1.00 69.74  ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 212.449 246.622 248.423 1.00 72.82  ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 212.425 246.235 249.892 1.00 74.92  ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 213.725 246.603 250.586 1.00 74.94  ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 213.663 246.333 252.049 1.00 74.52  ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 207.810 246.232 247.022 1.00 66.45  ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 206.809 246.086 245.976 1.00 67.73  ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 205.763 247.194 246.005 1.00 67.51  ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 204.767 247.115 245.276 1.00 70.59  ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 206.129 244.719 246.084 1.00 70.18  ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 205.966 248.222 246.830 1.00 66.27  ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 205.024 249.328 246.959 1.00 65.46  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 205.565 250.615 246.346 1.00 66.81  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 205.073 251.702 246.664 1.00 69.17  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 204.668 249.551 248.430 1.00 63.35  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 203.666 248.574 249.048 1.00 61.84  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 203.894 248.453 250.542 1.00 60.60  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 202.245 249.022 248.765 1.00 64.48  ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 206.571 250.514 245.475 1.00 71.69  ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 207.166 251.711 244.901 1.00 69.13  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 206.196 252.506 244.048 1.00 69.20  ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 206.150 253.736 244.126 1.00 73.36  ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 205.411 251.817 243.216 1.00 73.24  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 204.447 252.510 242.367 1.00 74.07  ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 203.342 253.156 243.193 1.00 70.47  ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 202.877 254.254 242.866 1.00 73.75  ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 203.857 251.542 241.341 1.00 75.18  ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 204.802 251.194 240.202 1.00 75.18  ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 205.763 250.077 240.558 1.00 78.50  ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 205.625 249.500 241.657 1.00 74.81  ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 206.656 249.776 239.739 1.00 78.12  ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 202.903 252.487 244.262 1.00 60.65  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 201.873 253.062 245.122 1.00 62.46  ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 202.374 254.323 245.815 1.00 67.63  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 201.627 255.297 245.963 1.00 69.39  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 201.412 252.029 246.150 1.00 61.53  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 200.391 252.557 247.132 1.00 62.36  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 199.072 252.758 246.749 1.00 63.54  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 200.746 252.854 248.441 1.00 60.33  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 198.134 253.240 247.643 1.00 66.14  ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 199.816 253.337 249.341 1.00 61.71  ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 198.512 253.528 248.937 1.00 67.60  ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 197.582 254.008 249.830 1.00 66.66  ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 203.635 254.320 246.255 1.00 61.53  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 204.194 255.497 246.912 1.00 53.43  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 204.318 256.666 245.944 1.00 56.26  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 204.103 257.822 246.326 1.00 64.34  ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 205.552 255.160 247.524 1.00 51.56  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 205.532 254.184 248.700 1.00 52.71  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 206.933 253.989 249.249 1.00 59.07  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 204.588 254.673 249.787 1.00 52.49  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 204.671 256.386 244.687 1.00 57.35  ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 204.770 257.450 243.692 1.00 59.05  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 203.418 258.114 243.464 1.00 59.66  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 203.338 259.337 243.296 1.00 65.68  ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 205.325 256.894 242.381 1.00 62.30  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 206.814 256.591 242.416 1.00 65.25  ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 207.648 257.801 242.787 1.00 67.65  ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 207.634 258.791 242.025 1.00 60.87  ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 208.319 257.762 243.840 1.00 67.47  ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 202.344 257.322 243.447 1.00 60.21  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 201.004 257.891 243.348 1.00 64.91  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 200.666 258.722 244.580 1.00 64.39  ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 200.010 259.764 244.472 1.00 64.69  ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 199.976 256.777 243.153 1.00 63.92  ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 200.118 256.022 241.842 1.00 64.80  ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 199.080 254.918 241.728 1.00 69.57  ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 197.725 255.448 241.631 1.00 75.59  ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 196.814 255.350 242.589 1.00 74.57  ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 197.079 254.748 243.737 1.00 71.92  ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 195.606 255.870 242.391 1.00 68.37  ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 201.098 258.271 245.760 1.00 59.65  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 200.825 259.012 246.988 1.00 54.56  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 201.561 260.345 247.020 1.00 58.33  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 201.056 261.315 247.596 1.00 60.77  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 201.207 258.170 248.205 1.00 56.03  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 200.277 256.998 248.471 1.00 61.56  ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 198.814 257.386 248.401 1.00 67.79  ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 198.343 258.103 249.309 1.00 62.28  ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 198.133 256.973 247.438 1.00 64.84  ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 202.752 260.412 246.417 1.00 46.90  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 203.522 261.652 246.428 1.00 40.19  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 202.824 262.759 245.650 1.00 46.31  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 203.061 263.944 245.911 1.00 50.61  ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 204.918 261.406 245.858 1.00 39.50  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 205.831 260.609 246.772 1.00 39.33  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 207.208 260.437 246.158 1.00 41.34  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 207.755 259.109 246.406 1.00 45.36  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 208.403 258.759 247.508 1.00 42.40  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 208.612 259.620 248.490 1.00 47.91  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 208.854 257.514 247.628 1.00 48.00  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 201.970 262.400 244.689 1.00 53.77  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 201.258 263.415 243.920 1.00 48.76  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 200.225 264.146 244.767 1.00 49.01  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 200.005 265.347 244.570 1.00 54.43  ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 200.591 262.777 242.701 1.00 52.13  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 201.538 262.090 241.903 1.00 49.50  ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 199.579 263.446 245.702 1.00 48.48  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 198.570 264.082 246.544 1.00 50.67  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 199.189 265.158 247.427 1.00 54.36  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 198.664 266.274 247.529 1.00 60.63  ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 197.860 263.028 247.394 1.00 56.72  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 198.789 262.287 248.165 1.00 64.21  ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 200.305 264.841 248.076 1.00 45.04  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 201.050 265.803 248.889 1.00 39.85  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 202.426 265.984 248.268 1.00 43.46  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 203.306 265.122 248.442 1.00 51.27  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 201.163 265.332 250.337 1.00 47.22  ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 201.520 266.424 251.305 1.00 42.36  ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 200.738 267.561 251.406 1.00 42.53  ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 202.635 266.310 252.119 1.00 46.48  ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 201.062 268.566 252.297 1.00 44.30  ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 202.964 267.312 253.012 1.00 41.14  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 202.177 268.441 253.101 1.00 44.16  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 202.661 267.077 247.538 1.00 47.12  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 203.924 267.205 246.791 1.00 41.24  ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 205.164 267.204 247.667 1.00 47.27  ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 206.255 266.892 247.175 1.00 39.97  ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 203.756 268.539 246.052 1.00 42.26  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 202.716 269.282 246.827 1.00 44.52  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 201.780 268.239 247.343 1.00 44.74  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 205.037 267.547 248.951 1.00 41.88  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 206.193 267.525 249.838 1.00 28.17  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 206.679 266.109 250.118 1.00 36.65  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 207.779 265.938 250.654 1.00 46.63  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 205.863 268.238 251.149 1.00 38.30  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 205.552 269.715 250.981 1.00 32.92  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 205.480 270.424 252.321 1.00 32.07  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 205.264 271.857 252.168 1.00 37.95  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 206.134 272.788 252.533 1.00 34.77  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 207.296 272.472 253.080 1.00 41.71  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 205.831 274.069 252.344 1.00 38.32  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 205.886 265.092 249.770 1.00 44.27  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 206.326 263.711 249.934 1.00 37.16  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 207.433 263.339 248.958 1.00 37.51  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 208.079 262.301 249.138 1.00 48.95  ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 205.144 262.756 249.763 1.00 38.77  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 204.227 262.703 250.951 1.00 43.35  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 204.686 263.037 252.214 1.00 41.68  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 202.907 262.312 250.806 1.00 41.65  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 203.843 262.987 253.308 1.00 43.48  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 202.060 262.260 251.896 1.00 46.59  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 202.529 262.598 253.148 1.00 48.91  ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 207.662 264.156 247.926 1.00 34.50  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 208.716 263.871 246.959 1.00 38.15  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 210.100 263.884 247.591 1.00 40.92  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 211.025 263.271 247.047 1.00 48.06  ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 208.661 264.880 245.811 1.00 36.23  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 207.735 264.482 244.686 1.00 41.01  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 208.101 263.504 243.773 1.00 37.53  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 206.493 265.084 244.539 1.00 39.45  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 207.258 263.136 242.744 1.00 41.12  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 205.642 264.723 243.513 1.00 37.75  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 206.030 263.749 242.618 1.00 45.53  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 205.186 263.386 241.594 1.00 52.99  ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 210.264 264.567 248.721 1.00 38.32  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 211.539 264.648 249.418 1.00 34.46  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 211.614 263.693 250.601 1.00 46.00  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 212.507 263.829 251.443 1.00 49.44  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 211.790 266.085 249.876 1.00 38.63  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 211.393 267.117 248.860 1.00 38.88  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 211.967 267.123 247.600 1.00 38.45  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 210.437 268.072 249.160 1.00 28.95  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 211.601 268.067 246.660 1.00 31.43  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 210.066 269.019 248.224 1.00 32.48  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 210.649 269.017 246.974 1.00 35.53  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 210.696 262.733 250.681 1.00 50.26  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 210.656 261.742 251.748 1.00 38.89  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 210.966 260.383 251.140 1.00 43.72  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 210.417 260.028 250.090 1.00 49.32  ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 209.289 261.729 252.457 1.00 33.46  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 209.265 260.681 253.554 1.00 45.41  ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 208.974 263.102 253.021 1.00 42.34  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 211.846 259.629 251.793 1.00 51.20  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 212.242 258.334 251.285 1.00 47.28  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 211.101 257.334 251.289 1.00 52.22  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 210.044 257.540 251.887 1.00 53.19  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 211.331 256.220 250.590 1.00 59.42  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 210.293 255.204 250.444 1.00 49.99  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 209.899 254.615 251.793 1.00 53.16  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 208.711 254.513 252.115 1.00 59.51  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 210.767 254.104 249.494 1.00 54.61  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 210.291 254.317 248.071 1.00 62.84  ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 209.561 255.299 247.826 1.00 58.36  ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 210.646 253.499 247.195 1.00 68.72  ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 210.889 254.223 252.599 1.00 55.95  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 210.591 253.631 253.900 1.00 56.37  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 209.910 254.633 254.823 1.00 60.54  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 208.956 254.288 255.530 1.00 62.30  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 211.871 253.097 254.542 1.00 63.35  ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 211.644 252.390 255.869 1.00 62.69  ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 212.922 251.828 256.456 1.00 69.73  ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 213.992 252.008 255.838 1.00 73.33  ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 212.857 251.205 257.537 1.00 68.27  ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 210.390 255.878 254.836 1.00 55.01  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 209.783 256.893 255.690 1.00 45.51  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 208.369 257.229 255.232 1.00 50.30  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 207.482 257.458 256.062 1.00 53.00  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 210.656 258.147 255.716 1.00 54.28  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 212.071 257.861 256.178 1.00 64.30  ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 212.236 257.321 257.292 1.00 65.98  ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 213.018 258.176 255.428 1.00 60.53  ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 208.140 257.268 253.917 1.00 49.68  ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 206.797 257.530 253.409 1.00 43.71  ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 205.833 256.416 253.793 1.00 44.69  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 204.678 256.682 254.145 1.00 52.06  ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 206.829 257.711 251.892 1.00 45.98  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 205.518 258.188 251.264 1.00 42.54  ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 204.993 259.415 251.990 1.00 41.98  ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 205.702 258.476 249.785 1.00 41.69  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 206.285 255.161 253.725 1.00 46.95  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 205.446 254.048 254.159 1.00 43.48  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 205.088 254.179 255.633 1.00 45.30  ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 203.952 253.899 256.032 1.00 51.51  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 206.155 252.720 253.896 1.00 46.17  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 206.376 252.333 252.433 1.00 51.84  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 207.585 251.427 252.300 1.00 50.60  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 205.145 251.665 251.849 1.00 52.21  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 206.049 254.602 256.456 1.00 53.22  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 205.761 254.855 257.863 1.00 49.61  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 204.777 256.007 258.024 1.00 55.42  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 203.941 255.997 258.934 1.00 64.15  ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 207.058 255.144 258.618 1.00 48.63  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 206.930 255.082 260.130 1.00 61.86  ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 208.223 254.670 260.807 1.00 67.19  ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 209.257 255.330 260.568 1.00 64.40  ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 208.207 253.687 261.577 1.00 66.70  ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 204.868 257.015 257.155 1.00 54.82  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 203.972 258.165 257.252 1.00 50.27  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 202.540 257.761 256.919 1.00 53.59  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 201.600 258.091 257.652 1.00 52.68  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 204.465 259.308 256.346 1.00 53.21  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 205.706 259.967 256.950 1.00 49.38  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 203.366 260.337 256.134 1.00 53.85  ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 206.402 260.931 256.016 1.00 52.51  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 202.352 257.040 255.812 1.00 55.01  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 201.007 256.645 255.406 1.00 45.38  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 200.446 255.591 256.352 1.00 53.84  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 199.278 255.655 256.754 1.00 53.86  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 201.010 256.152 253.948 1.00 50.24  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 201.731 257.151 253.041 1.00 51.29  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 199.588 255.922 253.461 1.00 55.27  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 201.137 258.539 253.058 1.00 47.87  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 201.264 254.602 256.718 1.00 55.29  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 200.774 253.518 257.554 1.00 50.80  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 200.413 253.960 258.959 1.00 55.32  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 199.416 253.504 259.525 1.00 56.58  ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 201.215 254.852 259.542 1.00 63.71  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 201.011 255.319 260.907 1.00 59.52  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 200.253 256.641 260.958 1.00 63.13  ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 200.522 257.477 261.826 1.00 66.52  ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 202.351 255.444 261.631 1.00 61.26  ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 202.902 254.102 262.070 1.00 67.25  ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 203.931 253.647 261.572 1.00 64.82  ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 202.218 253.461 263.010 1.00 67.62  ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 199.316 256.850 260.030 1.00 76.39  ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 198.519 258.072 260.045 1.00 77.65  ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 197.684 258.168 261.315 1.00 78.31  ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 197.531 259.255 261.885 1.00 80.15  ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 197.625 258.130 258.806 1.00 73.46  ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 196.699 257.059 258.795 1.00 76.08  ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 197.126 257.043 261.768 1.00 79.29  ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 196.384 257.041 263.025 1.00 81.34  ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 197.296 257.358 264.204 1.00 83.84  ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 196.912 258.103 265.113 1.00 82.48  ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 195.694 255.691 263.225 1.00 80.23  ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 194.437 255.508 262.391 1.00 82.12  ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 193.809 254.145 262.630 1.00 82.21  ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 192.896 253.750 261.481 1.00 82.64  ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 192.105 252.528 261.794 1.00 82.49  ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 198.507 256.800 264.207 1.00 81.04  ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 199.486 257.067 265.261 1.00 80.71  ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 200.268 258.322 264.882 1.00 80.58  ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 201.400 258.273 264.395 1.00 83.19  ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 200.400 255.866 265.464 1.00 83.91  ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 199.632 254.600 265.792 1.00 88.84  ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 199.570 253.671 264.987 1.00 85.34  ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 199.041 254.558 266.981 1.00 84.62  ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 199.634 259.474 265.117 1.00 75.35  ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 200.235 260.755 264.754 1.00 77.35  ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 201.499 261.022 265.560 1.00 72.36  ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 202.387 261.756 265.110 1.00 72.96  ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 199.205 261.888 264.927 1.00 77.55  ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 198.117 261.778 263.873 1.00 72.03  ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 198.598 261.838 266.318 1.00 76.58  ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 201.604 260.442 266.758 1.00 70.50  ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 202.782 260.657 267.591 1.00 69.68  ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 204.050 260.097 266.961 1.00 69.62  ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 205.147 260.567 267.281 1.00 67.24  ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 202.570 260.037 268.973 1.00 68.10  ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 203.927 259.107 266.078 1.00 69.65  ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 205.085 258.538 265.402 1.00 71.23  ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 205.505 259.335 264.175 1.00 71.54  ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 206.509 258.988 263.545 1.00 69.49  ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 204.797 257.089 265.000 1.00 72.30  ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 204.675 256.128 266.172 1.00 73.26  ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 204.316 254.729 265.699 1.00 73.75  ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 205.480 254.077 264.971 1.00 72.70  ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 206.615 253.787 265.889 1.00 71.97  ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 204.764 260.383 263.823 1.00 69.36  ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 205.042 261.185 262.640 1.00 64.04  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 205.918 262.395 262.930 1.00 66.48  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 206.295 263.106 261.993 1.00 67.40  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 203.727 261.653 262.011 1.00 58.82  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 202.853 260.538 261.443 1.00 66.56  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 201.513 261.079 260.965 1.00 66.41  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 203.584 259.827 260.327 1.00 69.58  ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 206.252 262.643 264.197 1.00 53.93  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 206.956 263.865 264.564 1.00 50.58  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 208.391 263.894 264.054 1.00 51.13  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 208.972 264.979 263.946 1.00 60.41  ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 206.935 264.037 266.083 1.00 51.22  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 205.561 263.832 266.704 1.00 53.61  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 204.684 265.068 266.629 1.00 50.23  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 204.973 266.009 265.891 1.00 52.89  ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 203.599 265.067 267.394 1.00 51.74  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 208.975 262.741 263.739 1.00 49.15  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 210.351 262.678 263.266 1.00 51.46  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 210.471 262.838 261.757 1.00 52.71  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 211.589 262.793 261.232 1.00 56.15  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 210.999 261.358 263.697 1.00 53.61  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 210.418 260.125 263.027 1.00 54.74  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 211.201 258.878 263.407 1.00 54.56  ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 210.674 257.649 262.684 1.00 60.99  ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 211.491 256.439 262.979 1.00 57.10  ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 209.357 263.022 261.047 1.00 56.13  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 209.377 263.179 259.601 1.00 55.41  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 209.015 264.582 259.134 1.00 52.51  ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 209.125 264.862 257.936 1.00 57.06  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 208.424 262.170 258.943 1.00 54.36  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 208.749 260.742 259.252 1.00 54.23  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 209.910 260.134 258.826 1.00 51.39  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 208.064 259.801 259.945 1.00 53.68  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 209.927 258.881 259.243 1.00 52.70  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 208.818 258.653 259.924 1.00 53.23  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 208.587 265.467 260.038 1.00 51.35  ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 208.213 266.816 259.627 1.00 44.91  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 209.428 267.647 259.237 1.00 45.45  ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 209.300 268.597 258.456 1.00 48.67  ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 207.431 267.508 260.742 1.00 45.19  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 206.020 267.017 260.886 1.00 45.96  ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 205.044 267.402 259.982 1.00 48.45  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 205.670 266.171 261.923 1.00 48.67  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 203.745 266.951 260.111 1.00 51.25  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 204.373 265.717 262.057 1.00 50.90  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 203.409 266.107 261.150 1.00 48.98  ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 210.608 267.314 259.765 1.00 48.48  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 211.813 268.058 259.419 1.00 43.70  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 212.248 267.822 257.980 1.00 46.94  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 213.059 268.593 257.457 1.00 45.01  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 212.952 267.689 260.371 1.00 44.57  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 213.413 266.246 260.256 1.00 49.83  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 214.512 265.934 261.258 1.00 50.38  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 214.982 264.495 261.128 1.00 55.37  ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 216.054 264.170 262.108 1.00 53.91  ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 211.733 266.778 257.331 1.00 47.33  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 212.090 266.480 255.951 1.00 42.52  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 211.138 267.102 254.940 1.00 49.29  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 211.488 267.198 253.758 1.00 53.55  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 212.135 264.964 255.736 1.00 37.43  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 212.755 264.197 256.891 1.00 44.03  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 212.511 262.703 256.763 1.00 47.77  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 213.050 261.956 257.972 1.00 56.24  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 212.867 260.485 257.846 1.00 48.00  ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 209.950 267.528 255.371 1.00 48.14  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 208.969 268.116 254.470 1.00 38.59  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 208.872 269.630 254.583 1.00 43.21  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 208.427 270.276 253.628 1.00 51.21  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 207.582 267.514 254.725 1.00 41.96  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 207.537 266.000 254.654 1.00 41.15  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 205.874 265.350 254.897 1.00 54.88  ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 205.882 265.042 256.660 1.00 35.74  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 209.274 270.209 255.710 1.00 41.84  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 209.122 271.634 255.952 1.00 30.82  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 210.475 272.264 256.255 1.00 38.09  ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 211.409 271.599 256.712 1.00 37.58  ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 208.151 271.900 257.108 1.00 33.53  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 206.739 271.468 256.827 1.00 32.59  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 206.350 270.154 257.022 1.00 37.76  ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 205.800 272.378 256.370 1.00 38.50  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 205.053 269.754 256.765 1.00 41.30  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 204.501 271.984 256.111 1.00 34.33  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 204.127 270.670 256.309 1.00 36.97  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 210.568 273.569 255.986 1.00 44.27  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 211.824 274.284 256.187 1.00 41.02  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 212.203 274.354 257.661 1.00 45.49  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 213.371 274.157 258.016 1.00 50.14  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 211.729 275.688 255.593 1.00 39.67  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 211.238 274.633 258.533 1.00 40.50  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 211.545 274.829 259.936 1.00 35.15  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 210.588 274.157 260.898 1.00 40.02  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 210.741 274.282 262.116 1.00 50.31  ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 209.596 273.444 260.372 1.00 45.12  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 208.633 272.737 261.211 1.00 44.46  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 209.244 271.396 261.603 1.00 40.50  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 209.414 270.511 260.761 1.00 47.17  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 207.291 272.547 260.496 1.00 41.79  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 206.321 271.782 261.384 1.00 35.85  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 206.711 273.889 260.092 1.00 42.90  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 209.576 271.245 262.883 1.00 37.49  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 210.134 269.994 263.379 1.00 44.45  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 209.074 269.072 263.961 1.00 47.94  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 209.234 267.847 263.912 1.00 55.04  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 211.204 270.276 264.437 1.00 48.64  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 211.799 269.075 264.895 1.00 52.22  ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 207.997 269.631 264.508 1.00 44.02  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 206.914 268.834 265.064 1.00 40.52  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 205.650 269.679 265.086 1.00 44.32  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 205.703 270.908 265.004 1.00 53.73  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 207.251 268.329 266.471 1.00 44.40  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 207.262 269.394 267.405 1.00 48.37  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 204.513 269.001 265.197 1.00 45.36  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 203.219 269.662 265.275 1.00 49.91  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 202.722 269.598 266.713 1.00 47.98  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 203.161 268.774 267.521 1.00 51.92  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 202.189 269.043 264.308 1.00 49.05  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 201.946 267.573 264.652 1.00 48.48  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 202.652 269.193 262.868 1.00 50.16  ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 200.792 266.953 263.896 1.00 48.62  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 201.786 270.489 267.030 1.00 47.44  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 201.205 270.595 268.363 1.00 43.82  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 199.792 270.036 268.314 1.00 49.55  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 198.998 270.410 267.443 1.00 54.86  ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 201.208 272.047 268.868 1.00 48.87  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 202.597 272.664 268.698 1.00 45.37  ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 200.768 272.107 270.322 1.00 49.60  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 202.687 274.101 269.157 1.00 51.75  ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 199.480 269.142 269.248 1.00 59.26  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 198.195 268.464 269.292 1.00 58.36  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 197.605 268.581 270.690 1.00 62.11  ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 198.315 268.808 271.672 1.00 66.66  ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 198.331 266.986 268.902 1.00 60.22  ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 198.755 266.697 267.462 1.00 59.72  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 199.201 265.255 267.324 1.00 57.51  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 197.619 266.996 266.502 1.00 60.11  ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 196.287 268.421 270.768 1.00 64.76  ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 195.588 268.436 272.045 1.00 69.99  ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 195.782 267.088 272.739 1.00 74.33  ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 196.565 266.242 272.300 1.00 75.48  ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 194.115 268.775 271.838 1.00 66.82  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 193.490 267.989 270.703 1.00 67.99  ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 194.159 267.197 270.040 1.00 73.52  ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 192.201 268.205 270.473 1.00 68.10  ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 195.068 266.874 273.846 1.00 81.77  ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 195.190 265.611 274.567 1.00 82.24  ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 194.639 264.449 273.749 1.00 81.25  ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 195.132 263.320 273.850 1.00 80.15  ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 194.476 265.706 275.915 1.00 81.95  ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 194.975 266.835 276.803 1.00 83.97  ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 196.402 266.625 277.269 1.00 86.22  ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 196.807 265.456 277.443 1.00 84.71  ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 197.121 267.628 277.461 1.00 83.01  ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 193.615 264.707 272.932 1.00 81.07  ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 193.011 263.648 272.132 1.00 78.32  ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 193.914 263.270 270.960 1.00 81.75  ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 193.811 262.159 270.429 1.00 83.76  ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 191.628 264.116 271.657 1.00 78.56  ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 190.931 263.128 270.726 1.00 84.07  ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 191.306 261.939 270.678 1.00 82.54  ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 189.931 263.532 270.097 1.00 89.32  ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 194.836 264.161 270.579 1.00 79.62  ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 195.678 263.990 269.390 1.00 73.60  ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 194.818 263.872 268.131 1.00 74.22  ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 195.059 263.033 267.262 1.00 76.77  ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 196.620 262.788 269.526 1.00 73.49  ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 197.769 263.048 270.480 1.00 78.99  ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 197.847 264.105 271.104 1.00 79.54  ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 198.671 262.080 270.596 1.00 77.91  ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 193.803 264.731 268.041 1.00 70.21  ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 192.908 264.757 266.892 1.00 69.94  ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 192.802 266.116 266.219 1.00 73.39  ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 192.291 266.182 265.095 1.00 74.80  ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 191.498 264.303 267.298 1.00 72.76  ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 190.993 265.097 268.357 1.00 71.60  ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 193.245 267.195 266.859 1.00 67.18  ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 193.210 268.532 266.281 1.00 58.64  ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 194.612 269.118 266.355 1.00 58.93  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 195.232 269.119 267.424 1.00 63.56  ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 192.203 269.447 267.005 1.00 62.20  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 191.959 270.707 266.196 1.00 60.97  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 190.895 268.713 267.260 1.00 65.33  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 195.108 269.615 265.226 1.00 54.59  ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 196.444 270.196 265.151 1.00 48.48  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 196.352 271.644 265.616 1.00 53.96  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 195.869 272.513 264.886 1.00 59.81  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 197.021 270.101 263.734 1.00 48.46  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 198.474 270.550 263.725 1.00 52.81  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 196.893 268.682 263.204 1.00 47.94  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 196.819 271.905 266.838 1.00 51.12  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 196.749 273.252 267.393 1.00 51.52  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 197.805 274.178 266.805 1.00 44.47  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 197.584 275.392 266.736 1.00 47.27  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 196.885 273.201 268.916 1.00 52.53  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 195.904 272.287 269.651 1.00 49.43  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 196.052 272.441 271.155 1.00 49.42  ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 194.475 272.579 269.220 1.00 47.89  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 198.942 273.641 266.384 1.00 39.50  ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 199.990 274.484 265.844 1.00 35.79  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 201.198 273.667 265.443 1.00 35.75  ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 201.126 272.446 265.289 1.00 49.18  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 202.318 274.370 265.272 1.00 40.33  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 203.576 273.768 264.854 1.00 43.62  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 204.685 274.240 265.784 1.00 43.57  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 204.560 275.249 266.480 1.00 45.74  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 203.929 274.109 263.391 1.00 43.54  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 203.957 275.626 263.198 1.00 41.88  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 202.948 273.452 262.434 1.00 44.13  ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 204.292 276.057 261.795 1.00 39.37  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 205.783 273.489 265.784 1.00 43.91  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 206.951 273.808 266.588 1.00 42.40  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 208.213 273.597 265.763 1.00 43.65  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 208.233 272.820 264.805 1.00 52.72  ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 207.011 272.955 267.863 1.00 48.08  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 205.864 273.158 268.668 1.00 52.99  ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 209.269 274.305 266.146 1.00 42.21  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 210.566 274.190 265.499 1.00 45.64  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 211.514 273.360 266.358 1.00 53.91  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 211.175 272.913 267.456 1.00 59.43  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 211.158 275.576 265.229 1.00 48.41  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 211.477 276.240 266.439 1.00 55.65  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 212.724 273.151 265.833 1.00 61.03  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 213.724 272.379 266.563 1.00 62.10  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 214.136 273.085 267.849 1.00 67.44  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 214.327 272.442 268.888 1.00 68.80  ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 214.941 272.123 265.674 1.00 63.13  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 216.166 271.622 266.421 1.00 65.96  ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 217.311 271.310 265.470 1.00 68.03  ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 217.157 271.986 264.188 1.00 68.70  ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 217.803 273.092 263.843 1.00 69.17  ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 218.662 273.675 264.663 1.00 66.62  ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 217.583 273.624 262.644 1.00 68.22  ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 214.268 274.412 267.802 1.00 66.76  ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 214.693 275.178 268.967 1.00 59.57  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 213.608 275.297 270.028 1.00 64.22  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 213.887 275.809 271.117 1.00 67.55  ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 215.147 276.575 268.539 1.00 63.71  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 216.388 276.588 267.659 1.00 65.51  ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 216.062 276.418 266.188 1.00 66.41  ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 214.863 276.369 265.845 1.00 67.20  ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 217.006 276.332 265.374 1.00 66.99  ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 212.388 274.841 269.745 1.00 60.36  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 211.294 274.931 270.685 1.00 58.49  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 210.321 276.061 270.433 1.00 60.26  ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 209.313 276.155 271.145 1.00 58.45  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 210.589 276.922 269.455 1.00 55.14  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 209.657 277.990 269.123 1.00 54.10  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 208.377 277.406 268.538 1.00 56.07  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 208.414 276.515 267.685 1.00 57.49  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 210.303 278.960 268.135 1.00 58.71  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 209.494 280.214 267.861 1.00 54.55  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 210.178 281.133 266.871 1.00 58.15  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 210.330 280.737 265.696 1.00 56.41  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 210.575 282.247 267.270 1.00 60.98  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 207.237 277.915 268.998 1.00 52.45  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 205.937 277.367 268.638 1.00 55.32  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 205.076 278.434 267.981 1.00 54.01  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 205.071 279.593 268.408 1.00 56.41  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 205.212 276.804 269.867 1.00 50.85  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 206.078 275.923 270.751 1.00 58.29  ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 205.262 275.022 271.655 1.00 64.95  ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 205.731 273.907 271.965 1.00 62.43  ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 204.152 275.428 272.056 1.00 61.59  ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 204.350 278.033 266.943 1.00 47.87  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 203.398 278.894 266.250 1.00 47.98  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 202.017 278.284 266.446 1.00 47.81  ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 201.757 277.160 265.998 1.00 50.06  ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 203.734 279.039 264.761 1.00 41.62  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 202.706 279.918 264.067 1.00 41.69  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 205.131 279.604 264.586 1.00 40.43  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 201.130 279.018 267.110 1.00 43.62  ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 199.786 278.526 267.383 1.00 41.01  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 198.855 278.923 266.244 1.00 46.80  ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 198.735 280.108 265.917 1.00 53.81  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 199.276 279.075 268.713 1.00 46.16  ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 200.059 278.592 269.920 1.00 52.19  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 199.931 276.810 270.158 1.00 68.02  ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 201.123 276.561 271.470 1.00 58.82  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 198.196 277.932 265.647 1.00 48.65  ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 197.292 278.196 264.536 1.00 45.58  ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 196.098 279.022 264.999 1.00 44.22  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 195.542 278.792 266.076 1.00 47.84  ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 196.808 276.881 263.923 1.00 44.57  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 197.852 276.160 263.117 1.00 40.27  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 199.079 276.747 262.855 1.00 42.26  ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 197.604 274.891 262.621 1.00 34.99  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 200.036 276.082 262.114 1.00 44.51  ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 198.557 274.222 261.880 1.00 42.86  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 199.774 274.819 261.625 1.00 44.10  ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 195.711 280.000 264.176 1.00 48.59  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 194.507 280.771 264.468 1.00 46.02  ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 193.269 279.887 264.415 1.00 54.09  ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 192.388 279.982 265.278 1.00 57.31  ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 194.378 281.937 263.488 1.00 47.54  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 195.707 282.507 263.016 1.00 54.37  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 196.428 283.246 264.132 1.00 51.86  ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 195.732 284.554 264.470 1.00 49.41  ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 196.520 285.363 265.440 1.00 46.03  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 193.185 279.023 263.410 1.00 47.32  ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 192.114 278.034 263.297 1.00 46.33  ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 192.750 276.652 263.290 1.00 48.52  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 193.341 276.255 262.265 1.00 52.51  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 191.280 278.254 262.038 1.00 54.66  ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 192.083 277.997 260.880 1.00 54.96  ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 190.762 279.684 261.983 1.00 47.36  ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 192.671 275.901 264.389 1.00 55.42  ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 193.329 274.590 264.434 1.00 53.23  ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 192.752 273.631 263.403 1.00 53.87  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 191.568 273.683 263.063 1.00 50.79  ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 193.057 274.106 265.863 1.00 49.27  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 192.763 275.352 266.639 1.00 56.31  ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 192.052 276.253 265.677 1.00 51.90  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 193.612 272.748 262.905 1.00 58.89  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 193.237 271.779 261.881 1.00 55.72  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 192.806 270.490 262.568 1.00 58.00  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 193.559 269.919 263.364 1.00 60.21  ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 194.397 271.525 260.908 1.00 53.19  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 194.085 270.340 260.007 1.00 56.08  ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 194.680 272.771 260.083 1.00 52.47  ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 191.598 270.028 262.255 1.00 66.12  ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 191.043 268.828 262.867 1.00 68.26  ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 191.339 267.613 261.998 1.00 68.49  ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 191.043 267.611 260.799 1.00 69.45  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 189.535 268.979 263.072 1.00 65.93  ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 188.992 267.840 263.716 1.00 68.38  ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 191.923 266.581 262.609 1.00 62.26  ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 192.233 265.363 261.868 1.00 56.03  ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 191.016 264.446 261.788 1.00 61.84  ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 190.897 263.649 260.850 1.00 70.42  ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 193.438 264.648 262.502 1.00 58.16  ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 194.557 265.650 262.790 1.00 60.06  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 193.949 263.541 261.592 1.00 62.26  ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 195.819 265.018 263.333 1.00 61.79  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 190.100 264.535 262.756 1.00 68.44  ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 188.890 263.719 262.703 1.00 67.94  ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 188.034 264.078 261.495 1.00 68.27  ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 187.483 263.194 260.830 1.00 69.21  ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 188.085 263.879 263.992 1.00 66.22  ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 187.922 265.272 264.287 1.00 69.08  ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 188.794 263.197 265.151 1.00 68.93  ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 187.910 265.373 261.197 1.00 68.90  ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 187.137 265.801 260.038 1.00 69.53  ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 187.843 265.492 258.725 1.00 71.52  ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 187.176 265.352 257.695 1.00 71.35  ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 186.840 267.299 260.134 1.00 69.61  ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 185.686 267.766 259.264 1.00 72.68  ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 185.284 269.199 259.551 1.00 77.95  ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 185.173 269.560 260.742 1.00 71.53  ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 185.080 269.966 258.587 1.00 76.11  ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 189.169 265.378 258.739 1.00 67.60  ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 189.963 265.081 257.547 1.00 66.25  ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 190.893 263.914 257.854 1.00 66.82  ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 192.097 264.097 258.067 1.00 69.74  ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 190.744 266.314 257.093 1.00 60.57  ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 189.895 267.536 256.926 1.00 65.97  ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 189.306 267.874 255.726 1.00 64.80  ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 189.529 268.495 257.808 1.00 67.71  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 188.617 268.991 255.876 1.00 62.30  ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 188.736 269.389 257.130 1.00 65.10  ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 190.355 262.692 257.897 1.00 61.29  ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 191.177 261.539 258.303 1.00 60.87  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 192.357 261.262 257.387 1.00 64.43  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 193.383 260.756 257.860 1.00 66.99  ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 190.175 260.374 258.294 1.00 68.45  ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 188.821 261.018 258.338 1.00 66.45  ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 188.970 262.301 257.592 1.00 63.24  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 192.244 261.562 256.094 1.00 62.14  ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 193.320 261.253 255.161 1.00 59.26  ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 194.582 262.030 255.515 1.00 60.31  ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 194.531 263.221 255.831 1.00 61.80  ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 192.889 261.566 253.729 1.00 63.66  ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 191.780 260.666 253.210 1.00 62.44  ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 191.433 260.989 251.767 1.00 66.59  ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 190.270 260.142 251.279 1.00 69.83  ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 190.637 258.702 251.180 1.00 67.54  ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 195.723 261.338 255.452 1.00 62.49  ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 196.989 261.926 255.887 1.00 55.01  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 197.350 263.129 255.023 1.00 51.09  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 197.801 264.164 255.528 1.00 53.36  ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 198.103 260.861 255.884 1.00 54.76  ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 199.441 261.471 256.311 1.00 51.87  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 198.203 260.168 254.529 1.00 57.04  ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 199.476 261.920 257.751 1.00 52.76  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 197.154 263.017 253.708 1.00 57.69  ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 197.514 264.116 252.818 1.00 57.80  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 196.517 265.263 252.923 1.00 60.62  ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 196.866 266.420 252.660 1.00 63.34  ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 197.608 263.616 251.377 1.00 58.43  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 196.378 262.844 250.947 1.00 62.70  ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 196.085 261.774 251.478 1.00 63.43  ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 195.648 263.387 249.980 1.00 61.73  ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 195.272 264.964 253.299 1.00 57.97  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 194.250 266.004 253.358 1.00 54.66  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 194.496 266.959 254.520 1.00 58.75  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 194.436 268.183 254.355 1.00 65.81  ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 192.862 265.371 253.459 1.00 61.53  ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 191.726 266.329 253.139 1.00 67.12  ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 190.372 265.649 253.134 1.00 70.07  ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 190.058 264.956 252.143 1.00 67.84  ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 189.619 265.810 254.117 1.00 68.04  ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 194.775 266.419 255.711 1.00 50.90  ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 195.011 267.285 256.860 1.00 46.23  ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 196.429 267.842 256.881 1.00 45.51  ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 196.667 268.865 257.531 1.00 58.00  ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 194.700 266.542 258.165 1.00 44.62  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 195.718 265.523 258.595 1.00 47.61  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 195.662 264.176 258.389 1.00 50.55  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 196.915 265.762 259.349 1.00 50.27  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 196.760 263.565 258.942 1.00 51.35  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 197.544 264.516 259.539 1.00 52.95  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 197.521 266.910 259.870 1.00 50.17  ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 198.748 264.385 260.228 1.00 45.22  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 198.716 266.777 260.552 1.00 50.67  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 199.316 265.525 260.725 1.00 45.12  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 197.371 267.199 256.189 1.00 34.87  ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 198.703 267.780 256.051 1.00 41.78  ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 198.668 269.025 255.174 1.00 44.77  ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 199.385 269.997 255.436 1.00 59.41  ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 199.675 266.748 255.481 1.00 45.98  ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 200.500 265.959 256.498 1.00 37.16  ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 201.382 264.941 255.795 1.00 40.51  ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 201.336 266.899 257.351 1.00 43.92  ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 197.846 269.008 254.122 1.00 39.40  ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 197.685 270.193 253.286 1.00 44.45  ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 197.051 271.335 254.070 1.00 44.42  ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 197.440 272.498 253.914 1.00 56.29  ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 196.846 269.855 252.053 1.00 47.68  ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 197.454 268.769 251.343 1.00 49.65  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 196.744 271.059 251.129 1.00 51.03  ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 196.068 271.021 254.918 1.00 41.05  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 195.443 272.050 255.742 1.00 36.36  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 196.437 272.644 256.731 1.00 43.06  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 196.420 273.853 256.990 1.00 49.70  ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 194.235 271.471 256.477 1.00 43.90  ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 193.080 270.966 255.610 1.00 50.74  ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 191.834 270.760 256.452 1.00 47.70  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 192.803 271.927 254.465 1.00 50.31  ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 197.305 271.806 257.303 1.00 44.82  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 198.319 272.298 258.233 1.00 42.42  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 199.271 273.252 257.521 1.00 44.04  ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 199.616 274.320 258.042 1.00 47.39  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 199.072 271.119 258.877 1.00 38.27  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 200.408 271.578 259.443 1.00 37.44  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 198.221 270.480 259.962 1.00 42.96  ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 199.708 272.880 256.316 1.00 39.48  ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 200.588 273.750 255.542 1.00 35.60  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 199.890 275.056 255.181 1.00 34.18  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 200.486 276.136 255.265 1.00 43.04  ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 201.062 273.023 254.283 1.00 37.28  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 201.838 273.898 253.314 1.00 47.54  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 202.052 273.230 251.971 1.00 55.93  ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 201.050 272.856 251.326 1.00 55.22  ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 203.221 273.082 251.558 1.00 55.88  ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 198.622 274.975 254.768 1.00 37.16  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 197.874 276.184 254.439 1.00 33.54  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 197.652 277.052 255.672 1.00 38.88  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 197.786 278.279 255.608 1.00 45.01  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 196.538 275.816 253.795 1.00 42.33  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 195.724 277.014 253.335 1.00 50.85  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 194.344 276.599 252.849 1.00 51.24  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 194.424 275.433 251.877 1.00 50.58  ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 195.272 275.752 250.695 1.00 40.99  ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 197.310 276.433 256.804 1.00 42.56  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 197.110 277.198 258.031 1.00 37.14  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 198.426 277.775 258.538 1.00 39.63  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 198.435 278.794 259.237 1.00 41.92  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 196.457 276.319 259.097 1.00 40.29  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 195.966 277.076 260.320 1.00 46.50  ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 195.186 278.325 259.961 1.00 55.65  ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 194.190 278.213 259.216 1.00 53.75  ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 195.568 279.419 260.425 1.00 55.49  ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 199.545 277.132 258.199 1.00 44.46  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 200.855 277.660 258.568 1.00 31.82  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 201.090 279.032 257.949 1.00 44.63  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 201.529 279.968 258.627 1.00 52.02  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 201.946 276.684 258.130 1.00 40.62  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 203.351 277.105 258.505 1.00 40.11  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 204.573 275.894 257.976 1.00 62.38  ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 204.550 276.152 256.204 1.00 33.51  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 200.805 279.167 256.653 1.00 41.22  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 201.030 280.435 255.967 1.00 28.51  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 200.045 281.497 256.438 1.00 38.64  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 200.408 282.666 256.610 1.00 48.69  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 200.928 280.229 254.456 1.00 32.14  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 201.936 279.234 253.908 1.00 38.94  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 201.831 279.106 252.400 1.00 36.73  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 202.862 278.229 251.859 1.00 43.99  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 202.619 277.096 251.216 1.00 46.96  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 201.384 276.665 251.016 1.00 42.02  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 203.641 276.375 250.763 1.00 43.94  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 198.785 281.107 256.646 1.00 33.26  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 197.768 282.063 257.076 1.00 32.01  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 198.071 282.576 258.478 1.00 36.68  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 197.944 283.775 258.756 1.00 48.70  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 196.369 281.423 256.994 1.00 40.68  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 195.325 282.345 257.602 1.00 46.00  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 196.022 281.098 255.551 1.00 44.98  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 198.471 281.680 259.383 1.00 39.19  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 198.777 282.090 260.750 1.00 34.21  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 199.956 283.055 260.785 1.00 43.61  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 199.918 284.075 261.483 1.00 49.94  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 199.062 280.863 261.615 1.00 33.47  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 197.907 280.016 261.642 1.00 47.08  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 199.411 281.282 263.032 1.00 34.13  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 201.015 282.749 260.032 1.00 33.56  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 202.169 283.640 259.986 1.00 28.61  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 201.807 284.978 259.354 1.00 36.51  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 202.296 286.029 259.785 1.00 38.79  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 203.315 282.976 259.224 1.00 33.62  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 204.028 281.838 259.956 1.00 32.71  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 205.142 281.271 259.097 1.00 31.92  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 204.569 282.319 261.292 1.00 29.53  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 200.957 284.958 258.325 1.00 36.99  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 200.506 286.205 257.716 1.00 26.02  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 199.694 287.039 258.699 1.00 33.67  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 199.848 288.264 258.757 1.00 48.83  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 199.690 285.910 256.458 1.00 27.03  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 198.822 286.394 259.477 1.00 41.23  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 198.040 287.123 260.470 1.00 35.36  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 198.915 287.598 261.624 1.00 37.20  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 198.734 288.713 262.127 1.00 47.28  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 196.899 286.247 260.987 1.00 41.83  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 195.802 285.990 259.967 1.00 40.93  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 194.714 285.101 260.544 1.00 44.31  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 193.560 284.937 259.570 1.00 43.19  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 192.531 283.993 260.087 1.00 43.96  ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 199.863 286.766 262.060 1.00 38.32  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 200.751 287.164 263.148 1.00 33.07  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 201.676 288.297 262.722 1.00 36.10  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 202.007 289.172 263.531 1.00 44.31  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 201.561 285.964 263.635 1.00 32.99  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 200.825 284.952 264.515 1.00 36.43  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 201.700 283.738 264.778 1.00 37.88  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 200.389 285.596 265.821 1.00 42.98  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 202.111 288.294 261.460 1.00 38.70  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 202.961 289.374 260.969 1.00 37.90  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 202.228 290.708 261.002 1.00 40.77  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 202.810 291.735 261.369 1.00 50.07  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 203.446 289.062 259.553 1.00 39.31  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 204.160 290.198 258.817 1.00 37.67  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 205.542 290.436 259.406 1.00 33.39  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 204.252 289.901 257.329 1.00 42.37  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 200.947 290.713 260.625 1.00 33.09  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 200.171 291.949 260.645 1.00 32.32  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 200.061 292.504 262.059 1.00 39.66  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 200.174 293.716 262.275 1.00 47.72  ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 198.785 291.707 260.048 1.00 36.80  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 199.832 291.627 263.039 1.00 46.48  ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 199.813 292.064 264.431 1.00 42.11  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 201.188 292.551 264.873 1.00 44.92  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 201.300 293.544 265.600 1.00 45.86  ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 199.330 290.928 265.331 1.00 43.54  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 197.944 290.411 264.985 1.00 50.00  ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 197.468 289.335 265.941 1.00 58.19  ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 198.310 288.541 266.411 1.00 55.76  ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 196.252 289.282 266.221 1.00 57.16  ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 202.246 291.856 264.447 1.00 44.71  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 203.600 292.278 264.794 1.00 34.23  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 203.942 293.619 264.157 1.00 34.26  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 204.603 294.459 264.778 1.00 42.26  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 204.606 291.209 264.369 1.00 34.60  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 205.935 291.648 264.582 1.00 43.09  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 203.508 293.833 262.912 1.00 50.66  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 203.754 295.109 262.244 1.00 44.15  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 203.052 296.241 262.982 1.00 45.05  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 203.616 297.327 263.165 1.00 45.67  ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 203.320 295.034 260.767 1.00 37.91  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 203.252 296.425 260.158 1.00 48.77  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 204.285 294.165 259.979 1.00 41.61  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 201.814 296.006 263.423 1.00 50.58  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 201.082 297.034 264.156 1.00 49.75  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 201.799 297.410 265.447 1.00 49.74  ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 201.871 298.592 265.806 1.00 57.38  ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 199.661 296.553 264.454 1.00 49.70  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 198.998 296.227 263.225 1.00 50.92  ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 198.870 297.632 265.176 1.00 42.89  ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 202.341 296.419 266.158 1.00 52.79  ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 203.034 296.701 267.411 1.00 52.16  ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 204.352 297.427 267.174 1.00 54.60  ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 204.694 298.358 267.913 1.00 60.96  ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 203.271 295.403 268.183 1.00 52.96  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 202.008 294.767 268.736 1.00 56.96  ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 202.297 293.772 269.842 1.00 64.17  ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 203.447 293.740 270.328 1.00 61.11  ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 201.375 293.021 270.225 1.00 63.27  ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 205.108 297.020 266.151 1.00 55.58  ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 206.428 297.605 265.932 1.00 54.48  ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 206.338 299.028 265.389 1.00 60.38  ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 207.318 299.780 265.476 1.00 64.25  ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 207.265 296.715 264.994 1.00 50.06  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 206.708 296.739 263.582 1.00 59.25  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 208.739 297.113 265.021 1.00 44.66  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 205.185 299.430 264.847 1.00 64.13  ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 205.022 300.809 264.399 1.00 64.30  ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 205.142 301.801 265.547 1.00 70.42  ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 205.500 302.961 265.315 1.00 76.27  ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 203.674 300.989 263.697 1.00 65.25  ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 203.582 300.342 262.321 1.00 67.66  ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 204.561 300.929 261.319 1.00 74.99  ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 204.994 302.086 261.505 1.00 74.56  ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 204.897 300.229 260.340 1.00 71.41  ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 204.845 301.375 266.776 1.00 73.45  ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 205.049 302.241 267.932 1.00 72.63  ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 206.537 302.473 268.167 1.00 69.72  ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 206.966 303.596 268.455 1.00 70.23  ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 204.364 301.644 269.174 1.00 71.29  ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 202.905 301.301 268.865 1.00 71.69  ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 204.453 302.607 270.347 1.00 67.95  ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 202.087 302.481 268.389 1.00 66.28  ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 207.346 301.416 268.053 1.00 69.19  ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 208.789 301.567 268.211 1.00 71.00  ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 209.372 302.448 267.114 1.00 73.16  ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 210.269 303.260 267.370 1.00 75.78  ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 209.464 300.196 268.220 1.00 72.11  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 208.848 299.225 269.184 1.00 70.72  ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 208.600 299.595 270.495 1.00 68.45  ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 208.519 297.943 268.781 1.00 66.52  ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 208.033 298.705 271.385 1.00 70.12  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 207.951 297.049 269.666 1.00 68.13  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 207.708 297.430 270.970 1.00 72.44  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 208.884 302.296 265.886 1.00 78.48  ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 209.265 303.213 264.832 1.00 75.31  ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 208.688 304.596 265.064 1.00 79.29  ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 207.670 304.768 265.736 1.00 78.90  ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 209.364 305.600 264.502 1.00 83.19  ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 208.988 307.005 264.674 1.00 87.87  ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 208.954 307.404 266.147 1.00 86.54  ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 208.170 308.268 266.549 1.00 87.48  ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 207.641 307.310 264.009 1.00 86.62  ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 207.586 306.997 262.523 1.00 84.18  ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 208.231 308.101 261.702 1.00 85.79  ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 208.366 307.699 260.242 1.00 85.04  ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 207.136 307.030 259.735 1.00 84.07  ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 209.799 306.779 266.963 1.00 86.95  ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 209.868 307.050 268.392 1.00 87.07  ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 211.288 307.454 268.760 1.00 88.94  ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 212.244 306.740 268.440 1.00 89.58  ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 209.434 305.831 269.209 1.00 84.29  ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 211.420 308.600 269.432 1.00 93.59  ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 212.739 309.070 269.842 1.00 92.92  ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 213.332 308.184 270.930 1.00 94.85  ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 214.536 307.902 270.922 1.00 94.97  ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 212.655 310.520 270.319 1.00 91.37  ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 211.783 310.601 271.453 1.00 91.51  ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 212.119 311.413 269.210 1.00 90.63  ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 212.507 307.736 271.873 1.00 90.64  ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 212.949 306.904 272.983 1.00 88.49  ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 212.165 305.600 272.990 1.00 89.38  ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 210.947 305.595 272.780 1.00 90.03  ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 212.773 307.628 274.321 1.00 90.58  ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 211.410 307.925 274.565 1.00 88.49  ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 212.867 304.496 273.233 1.00 80.06  ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 212.274 303.165 273.252 1.00 81.49  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 212.517 302.543 274.620 1.00 79.18  ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 213.661 302.485 275.086 1.00 77.61  ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 212.846 302.272 272.136 1.00 79.49  ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 212.438 302.812 270.765 1.00 79.41  ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 212.382 300.835 272.307 1.00 79.23  ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 213.105 302.107 269.613 1.00 78.69  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 211.448 302.084 275.254 1.00 73.70  ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 211.558 301.403 276.538 1.00 75.41  ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 212.122 300.005 276.319 1.00 74.47  ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 211.529 299.222 275.565 1.00 74.59  ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 210.188 301.334 277.210 1.00 75.42  ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 210.268 300.949 278.677 1.00 79.39  ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 211.378 300.665 279.169 1.00 76.80  ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 209.211 300.935 279.341 1.00 80.14  ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 213.257 299.652 276.931 1.00 75.15  ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 213.797 298.295 276.731 1.00 73.35  ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 212.846 297.193 277.163 1.00 73.51  ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 212.803 296.136 276.523 1.00 73.65  ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 215.081 298.305 277.573 1.00 69.30  ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 215.456 299.746 277.678 1.00 68.76  ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 214.161 300.496 277.732 1.00 72.62  ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 212.078 297.408 278.234 1.00 74.47  ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 211.147 296.383 278.695 1.00 72.50  ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 210.052 296.128 277.666 1.00 69.18  ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 209.685 294.976 277.407 1.00 72.44  ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 210.542 296.791 280.039 1.00 74.98  ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 211.353 296.291 281.217 1.00 75.82  ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 212.584 296.290 281.182 1.00 72.02  ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 210.667 295.863 282.270 1.00 74.32  ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 209.512 297.196 277.072 1.00 62.27  ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 208.484 297.030 276.049 1.00 66.08  ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 209.051 296.366 274.800 1.00 65.71  ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 208.402 295.503 274.197 1.00 62.51  ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 207.864 298.384 275.704 1.00 64.49  ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 207.357 298.997 276.896 1.00 67.89  ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 206.725 298.212 274.711 1.00 61.11  ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 210.262 296.757 274.396 1.00 60.17  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 210.869 296.179 273.201 1.00 54.63  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 211.161 294.694 273.387 1.00 56.75  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 210.926 293.890 272.477 1.00 60.01  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 212.147 296.938 272.844 1.00 52.93  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 212.582 296.760 271.408 1.00 54.88  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 211.768 297.170 270.361 1.00 56.52  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 213.806 296.184 271.099 1.00 52.37  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 212.161 297.009 269.046 1.00 56.94  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 214.207 296.019 269.788 1.00 55.20  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 213.381 296.433 268.766 1.00 55.87  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 213.777 296.271 267.458 1.00 57.35  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 211.677 294.313 274.557 1.00 54.53  ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 211.975 292.907 274.816 1.00 50.00  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 210.692 292.085 274.851 1.00 52.06  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 210.655 290.946 274.367 1.00 59.47  ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 212.782 292.765 276.120 1.00 52.36  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 214.183 293.354 275.945 1.00 54.86  ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 212.874 291.309 276.546 1.00 54.44  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 215.028 292.628 274.923 1.00 54.88  ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 209.619 292.647 275.415 1.00 45.04  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 208.343 291.939 275.448 1.00 51.60  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 207.831 291.660 274.040 1.00 57.77  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 207.328 290.566 273.759 1.00 61.06  ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 207.315 292.748 276.241 1.00 54.76  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 207.806 292.977 277.568 1.00 57.96  ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 205.992 292.002 276.320 1.00 52.68  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 207.952 292.639 273.141 1.00 52.55  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 207.539 292.433 271.756 1.00 38.86  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 208.399 291.376 271.073 1.00 37.18  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 207.896 290.575 270.277 1.00 48.63  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 207.598 293.757 270.993 1.00 43.03  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 207.527 293.608 269.504 1.00 47.37  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 206.413 293.358 268.758 1.00 48.22  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 208.615 293.716 268.578 1.00 46.88  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 206.741 293.295 267.425 1.00 46.10  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 208.087 293.512 267.288 1.00 46.54  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 209.984 293.961 268.715 1.00 43.61  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 208.879 293.547 266.144 1.00 46.73  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 210.769 293.994 267.577 1.00 42.73  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 210.214 293.789 266.309 1.00 47.24  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 209.702 291.365 271.365 1.00 39.58  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 210.593 290.368 270.777 1.00 43.04  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 210.200 288.967 271.228 1.00 48.16  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 210.130 288.033 270.420 1.00 54.22  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 212.057 290.687 271.131 1.00 38.75  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 212.534 291.926 270.373 1.00 43.28  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 212.956 289.499 270.827 1.00 37.79  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 213.879 292.438 270.833 1.00 46.75  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 209.933 288.798 272.526 1.00 49.35  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 209.576 287.483 273.047 1.00 50.64  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 208.202 287.034 272.568 1.00 49.24  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 207.939 285.829 272.488 1.00 53.61  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 209.621 287.496 274.575 1.00 48.20  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 211.031 287.394 275.117 1.00 53.29  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 211.875 286.745 274.465 1.00 57.20  ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 211.295 287.965 276.196 1.00 54.47  ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 207.317 287.981 272.251 1.00 44.21  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 205.946 287.626 271.896 1.00 39.05  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 205.871 286.970 270.522 1.00 44.36  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 205.132 285.997 270.334 1.00 46.79  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 205.059 288.869 271.946 1.00 39.36  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 203.617 288.626 271.536 1.00 44.50  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 202.777 289.878 271.718 1.00 46.05  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 201.357 289.668 271.222 1.00 46.68  ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 200.660 288.591 271.976 1.00 42.17  ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 206.625 287.479 269.554 1.00 48.08  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 206.511 287.051 268.168 1.00 43.78  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 207.699 286.188 267.763 1.00 40.69  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 208.752 286.189 268.407 1.00 44.10  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 206.389 288.261 267.237 1.00 39.18  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 205.121 289.052 267.459 1.00 41.43  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 203.913 288.627 266.924 1.00 40.83  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 205.129 290.215 268.217 1.00 41.63  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 202.750 289.342 267.129 1.00 35.67  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 203.970 290.937 268.427 1.00 41.82  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 202.784 290.496 267.881 1.00 37.86  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 201.628 291.212 268.088 1.00 47.33  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 207.510 285.447 266.674 1.00 39.89  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 208.509 284.498 266.209 1.00 37.93  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 209.726 285.220 265.636 1.00 42.58  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 209.670 286.395 265.266 1.00 51.05  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 207.908 283.561 265.161 1.00 34.08  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 207.018 282.476 265.745 1.00 39.09  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 205.645 282.989 266.132 1.00 45.49  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 205.233 284.071 265.715 1.00 50.46  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 204.929 282.214 266.937 1.00 41.44  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 210.837 284.484 265.557 1.00 34.84  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 212.111 285.085 265.171 1.00 32.40  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 212.055 285.656 263.760 1.00 42.05  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 212.563 286.754 263.503 1.00 50.71  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 213.232 284.053 265.291 1.00 37.64  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 211.445 284.923 262.826 1.00 43.79  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 211.372 285.412 261.453 1.00 30.39  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 210.403 286.582 261.334 1.00 32.33  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 210.535 287.417 260.432 1.00 41.06  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 210.974 284.277 260.506 1.00 32.75  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 209.480 284.016 260.413 1.00 33.52  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 209.135 282.993 259.350 1.00 37.44  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 209.402 281.803 259.508 1.00 39.78  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 208.538 283.454 258.257 1.00 35.36  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 209.420 286.661 262.235 1.00 37.74  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 208.461 287.759 262.184 1.00 29.95  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 209.011 289.011 262.855 1.00 28.04  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 208.694 290.132 262.442 1.00 42.09  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 207.143 287.335 262.831 1.00 32.36  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 206.427 286.155 262.171 1.00 34.90  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 205.119 285.860 262.882 1.00 40.52  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 206.189 286.425 260.694 1.00 31.78  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 209.826 288.844 263.899 1.00 29.63  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 210.433 289.996 264.564 1.00 32.32  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 211.374 290.723 263.610 1.00 39.60  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 211.360 291.956 263.514 1.00 44.87  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 211.158 289.557 265.849 1.00 25.35  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 211.939 290.714 266.439 1.00 42.85  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 210.156 289.043 266.867 1.00 36.37  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 212.205 289.968 262.889 1.00 37.73  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 213.110 290.578 261.919 1.00 32.12  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 212.323 291.184 260.765 1.00 34.08  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 212.628 292.288 260.298 1.00 46.80  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 214.136 289.543 261.424 1.00 33.61  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 215.083 290.173 260.415 1.00 28.55  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 214.905 288.961 262.596 1.00 34.48  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 211.298 290.473 260.289 1.00 24.25  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 210.501 290.969 259.171 1.00 28.99  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 209.770 292.255 259.534 1.00 29.66  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 209.669 293.173 258.712 1.00 38.08  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 209.508 289.896 258.725 1.00 32.75  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 208.961 289.985 257.301 1.00 34.54  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 210.092 290.065 256.291 1.00 33.85  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 208.069 288.789 257.018 1.00 40.22  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 209.246 292.337 260.759 1.00 27.38  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 208.546 293.544 261.186 1.00 23.91  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 209.489 294.739 261.240 1.00 29.14  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 209.105 295.859 260.883 1.00 37.55  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 207.890 293.316 262.547 1.00 34.25  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 207.138 292.116 262.552 1.00 49.63  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 210.725 294.523 261.695 1.00 28.11  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 211.701 295.607 261.729 1.00 27.46  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 212.032 296.095 260.324 1.00 37.43  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 212.188 297.301 260.098 1.00 46.70  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 212.967 295.152 262.453 1.00 28.90  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 212.152 295.171 259.368 1.00 36.35  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 212.424 295.561 257.988 1.00 22.52  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 211.267 296.359 257.400 1.00 23.10  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 211.483 297.349 256.692 1.00 38.07  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 212.705 294.322 257.140 1.00 26.03  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 213.880 293.496 257.626 1.00 25.75  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 214.038 292.198 256.861 1.00 33.33  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 213.109 291.397 256.778 1.00 45.69  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 215.220 291.984 256.296 1.00 33.17  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 210.031 295.937 257.676 1.00 22.74  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 208.866 296.656 257.167 1.00 22.14  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 208.789 298.049 257.780 1.00 26.29  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 208.517 299.036 257.085 1.00 37.64  ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 207.583 295.847 257.431 1.00 26.88  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 207.584 294.560 256.606 1.00 27.57  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 206.350 296.678 257.115 1.00 30.24  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 206.573 293.539 257.071 1.00 21.87  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 209.027 298.150 259.090 1.00 34.83  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 208.964 299.447 259.757 1.00 39.35  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 210.043 300.391 259.241 1.00 41.61  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 209.785 301.581 259.025 1.00 45.15  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 209.088 299.265 261.269 1.00 35.88  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 211.261 299.881 259.043 1.00 35.43  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 212.349 300.734 258.573 1.00 32.01  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 212.113 301.194 257.140 1.00 37.56  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 212.319 302.370 256.817 1.00 48.63  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 213.682 299.996 258.682 1.00 36.17  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 214.794 300.669 257.940 1.00 33.03  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 215.473 301.788 258.322 1.00 33.74  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 215.351 300.271 256.682 1.00 31.94  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 216.422 302.109 257.383 1.00 34.31  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 216.367 301.193 256.366 1.00 29.50  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 215.091 299.223 255.794 1.00 32.06  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 217.123 301.100 255.200 1.00 34.57  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 215.843 299.132 254.637 1.00 39.17  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 216.846 300.065 254.351 1.00 42.40  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 211.687 300.280 256.264 1.00 37.30  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 211.455 300.642 254.869 1.00 34.45  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 210.345 301.676 254.744 1.00 43.32  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 210.446 302.613 253.943 1.00 58.71  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 211.123 299.394 254.052 1.00 34.79  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 212.246 298.537 253.952 1.00 44.68  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 209.272 301.519 255.522 1.00 43.77  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 208.201 302.510 255.512 1.00 40.65  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 208.689 303.852 256.042 1.00 51.25  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 208.300 304.909 255.530 1.00 60.22  ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 207.013 302.006 256.331 1.00 47.59  ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 206.216 300.904 255.652 1.00 53.60  ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 204.930 300.577 256.386 1.00 65.06  ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 204.715 301.128 257.486 1.00 56.65  ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 204.135 299.769 255.863 1.00 63.41  ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 209.533 303.832 257.077 1.00 53.46  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 210.064 305.075 257.626 1.00 44.19  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 210.943 305.798 256.613 1.00 44.02  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 210.861 307.024 256.472 1.00 55.95  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 210.848 304.790 258.907 1.00 47.83  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 209.946 304.509 260.092 1.00 52.15  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 208.725 304.438 259.954 1.00 57.77  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 210.544 304.348 261.266 1.00 54.03  ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 211.797 305.058 255.903 1.00 44.55  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 212.648 305.674 254.889 1.00 46.61  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 211.807 306.200 253.734 1.00 45.90  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 212.035 307.309 253.237 1.00 50.22  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 213.714 304.675 254.406 1.00 42.78  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 214.512 305.266 253.255 1.00 45.85  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 214.636 304.291 255.549 1.00 43.40  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 210.821 305.416 253.289 1.00 47.29  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 209.971 305.848 252.184 1.00 42.22  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 209.182 307.098 252.551 1.00 47.23  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 209.012 308.000 251.722 1.00 58.73  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 209.027 304.716 251.777 1.00 43.49  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 208.452 304.859 250.379 1.00 54.56  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 209.355 304.268 249.315 1.00 54.33  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 210.391 303.673 249.677 1.00 53.40  ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 209.027 304.396 248.117 1.00 52.59  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 208.683 307.166 253.787 1.00 51.05  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 207.992 308.368 254.241 1.00 49.77  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 208.933 309.566 254.268 1.00 53.52  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 208.561 310.669 253.850 1.00 63.18  ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 207.382 308.131 255.624 1.00 53.86  ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 206.332 307.161 255.525 1.00 53.02  ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 206.814 309.423 256.192 1.00 55.20  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 210.162 309.367 254.753 1.00 52.99  ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 211.130 310.459 254.795 1.00 54.77  ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 211.482 310.942 253.394 1.00 61.65  ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 211.582 312.151 253.153 1.00 69.52  ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 212.387 310.017 255.543 1.00 59.84  ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 211.678 310.012 252.456 1.00 60.67  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 211.992 310.400 251.084 1.00 50.70  ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 210.817 311.116 250.429 1.00 59.55  ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 211.014 312.046 249.638 1.00 64.98  ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 212.398 309.172 250.270 1.00 49.65  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 213.695 308.482 250.697 1.00 53.73  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 214.110 307.438 249.676 1.00 58.56  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 214.801 309.503 250.903 1.00 55.38  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 209.590 310.690 250.736 1.00 64.69  ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 208.415 311.370 250.199 1.00 62.79  ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 208.341 312.809 250.692 1.00 65.54  ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 207.992 313.718 249.929 1.00 70.13  ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 207.147 310.604 250.576 1.00 62.91  ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 207.195 309.273 250.094 1.00 67.90  ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 208.658 313.035 251.969 1.00 71.04  ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 208.717 314.399 252.486 1.00 75.82  ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 209.830 315.191 251.813 1.00 77.67  ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 209.682 316.392 251.556 1.00 80.61  ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 208.910 314.378 254.002 1.00 74.97  ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 209.451 315.603 254.464 1.00 77.49  ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 210.956 314.536 251.519 1.00 75.01  ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 212.057 315.181 250.815 1.00 75.49  ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 211.788 315.348 249.326 1.00 81.99  ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 212.681 315.803 248.602 1.00 81.48  ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 213.348 314.386 251.015 1.00 77.04  ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 213.861 314.384 252.443 1.00 79.16  ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 215.336 313.371 252.660 1.00 81.00  ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 216.554 314.353 251.791 1.00 77.48  ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 210.593 314.998 248.854 1.00 96.71  ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 210.263 315.092 247.445 1.00 94.49  ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 210.232 316.512 246.917 1.00 98.86  ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 210.196 316.726 245.701 1.00 99.37  ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 210.243 317.492 247.820 1.00 106.41 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 210.266 318.885 247.418 1.00 106.48 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 211.610 319.397 246.951 1.00 108.58 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 211.697 320.540 246.493 1.00 106.69 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 212.658 318.582 247.057 1.00 111.25 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 213.974 318.972 246.592 1.00 109.33 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 214.793 319.715 247.627 1.00 110.37 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 215.766 319.176 248.163 1.00 108.07 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 214.408 320.954 247.916 1.00 110.31 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 215.112 321.800 248.855 1.00 109.23 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 214.662 321.688 250.294 1.00 112.18 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 215.093 322.493 251.127 1.00 111.41 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 213.812 320.717 250.617 1.00 110.42 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 213.307 320.565 251.973 1.00 109.22 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 214.413 320.066 252.902 1.00 108.39 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 215.562 319.854 252.501 1.00 108.25 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 212.113 319.613 251.989 1.00 108.65 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 210.891 320.199 251.311 1.00 109.12 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 210.738 321.438 251.325 1.00 109.11 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 210.082 319.420 250.765 1.00 107.10 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 214.052 319.870 254.168 1.00 102.47 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 214.996 319.388 255.163 1.00 102.12 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 215.250 317.894 254.966 1.00 102.77 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 214.816 317.280 253.987 1.00 100.32 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 214.477 319.678 256.570 1.00 99.69  ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 215.969 317.297 255.918 1.00 90.54  ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 216.353 315.890 255.842 1.00 86.96  ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 215.771 315.126 257.024 1.00 86.26  ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 216.422 315.000 258.072 1.00 80.49  ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 217.876 315.749 255.803 1.00 83.06  ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 214.547 314.600 256.912 1.00 85.31  ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 214.033 313.700 257.956 1.00 82.15  ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 214.728 312.350 257.990 1.00 80.58  ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 214.433 311.548 258.886 1.00 81.47  ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 212.549 313.547 257.592 1.00 77.83  ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 212.242 314.725 256.721 1.00 81.22  ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 213.500 314.980 255.952 1.00 82.16  ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 215.628 312.069 257.042 1.00 67.83  ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 216.380 310.819 257.078 1.00 64.49  ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 217.260 310.733 258.317 1.00 67.18  ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 217.599 309.630 258.761 1.00 70.50  ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 217.228 310.681 255.814 1.00 63.44  ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 216.615 309.895 254.654 1.00 60.76  ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 217.485 310.015 253.414 1.00 63.95  ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 216.421 308.437 255.036 1.00 62.78  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 217.645 311.880 258.882 1.00 64.58  ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 218.399 311.871 260.130 1.00 63.35  ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 217.563 311.302 261.269 1.00 64.92  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 218.089 310.616 262.153 1.00 70.21  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 218.876 313.284 260.465 1.00 65.73  ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 219.904 313.816 259.515 1.00 70.63  ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 221.145 313.237 259.361 1.00 67.21  ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 219.874 314.872 258.669 1.00 70.63  ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 221.836 313.914 258.461 1.00 64.89  ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 221.087 314.911 258.025 1.00 69.19  ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 216.258 311.583 261.267 1.00 61.60  ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 215.373 310.995 262.267 1.00 61.49  ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 215.301 309.481 262.114 1.00 62.83  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 215.262 308.749 263.110 1.00 70.39  ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 213.979 311.613 262.165 1.00 61.87  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 214.003 312.986 262.514 1.00 68.31  ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 215.272 308.994 260.871 1.00 57.17  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 215.271 307.553 260.636 1.00 52.19  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 216.572 306.932 261.128 1.00 54.92  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 216.569 305.881 261.781 1.00 59.91  ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 215.030 307.254 259.145 1.00 50.09  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 215.107 305.759 258.885 1.00 51.37  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 213.686 307.809 258.704 1.00 55.20  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 217.705 307.570 260.823 1.00 53.03  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 218.988 307.070 261.308 1.00 49.80  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 219.068 307.143 262.827 1.00 54.88  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 219.634 306.252 263.470 1.00 60.65  ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 220.135 307.855 260.672 1.00 51.44  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 221.543 307.330 260.960 1.00 52.35  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 221.701 305.903 260.461 1.00 53.11  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 222.595 308.237 260.340 1.00 53.06  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 218.516 308.206 263.417 1.00 52.31  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 218.502 308.318 264.872 1.00 51.60  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 217.685 307.198 265.502 1.00 54.95  ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 218.111 306.591 266.491 1.00 60.73  ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 217.953 309.682 265.288 1.00 55.85  ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 218.899 310.708 265.046 1.00 59.37  ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 216.511 306.902 264.937 1.00 56.50  ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 215.674 305.839 265.483 1.00 54.25  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 216.355 304.481 265.365 1.00 52.89  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 216.254 303.646 266.271 1.00 59.99  ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 214.318 305.822 264.777 1.00 52.80  ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 213.439 304.675 265.232 1.00 62.66  ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 213.000 303.856 264.425 1.00 63.05  ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 213.178 304.610 266.533 1.00 63.13  ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 217.045 304.239 264.248 1.00 46.66  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 217.763 302.979 264.076 1.00 48.21  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 218.873 302.851 265.111 1.00 49.85  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 219.062 301.787 265.714 1.00 52.54  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 218.308 302.869 262.639 1.00 45.47  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 219.346 301.763 262.543 1.00 46.74  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 217.172 302.624 261.659 1.00 41.49  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 219.622 303.933 265.339 1.00 46.19  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 220.723 303.883 266.296 1.00 47.39  ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 220.218 303.728 267.726 1.00 55.87  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 220.825 303.009 268.528 1.00 58.60  ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 221.593 305.132 266.161 1.00 48.35  ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 222.697 304.999 265.125 1.00 52.75  ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 223.294 306.335 264.730 1.00 63.45  ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 222.690 307.378 265.058 1.00 61.81  ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 224.367 306.342 264.091 1.00 61.94  ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 219.117 304.401 268.070 1.00 53.45  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 218.536 304.244 269.402 1.00 54.59  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 218.067 302.809 269.608 1.00 50.56  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 218.283 302.211 270.669 1.00 56.58  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 217.391 305.251 269.617 1.00 54.51  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 216.682 304.974 270.931 1.00 57.07  ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 217.930 306.670 269.610 1.00 51.71  ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 217.417 302.235 268.593 1.00 48.63  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 216.993 300.841 268.682 1.00 41.75  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 218.195 299.908 268.761 1.00 40.89  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 218.166 298.903 269.481 1.00 48.26  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 216.116 300.478 267.485 1.00 48.95  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 215.165 301.524 267.252 1.00 51.81  ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 215.368 299.182 267.754 1.00 45.01  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 219.262 300.224 268.022 1.00 42.30  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 220.454 299.382 268.039 1.00 40.80  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 221.146 299.426 269.396 1.00 38.28  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 221.694 298.415 269.850 1.00 43.40  ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 221.414 299.814 266.931 1.00 43.64  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 222.515 298.822 266.554 1.00 44.33  ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 221.918 297.477 266.175 1.00 39.34  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 223.367 299.373 265.422 1.00 40.59  ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 221.140 300.588 270.053 1.00 46.11  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 221.741 300.689 271.379 1.00 50.65  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 220.992 299.831 272.391 1.00 50.15  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 221.608 299.200 273.258 1.00 54.92  ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 221.776 302.148 271.833 1.00 49.27  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 222.903 302.932 271.190 1.00 57.51  ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 223.925 302.366 270.803 1.00 57.27  ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 222.721 304.242 271.072 1.00 55.52  ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 219.661 299.802 272.300 1.00 45.53  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 218.870 298.956 273.189 1.00 40.74  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 219.193 297.487 272.950 1.00 40.56  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 219.344 296.705 273.897 1.00 49.16  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 217.368 299.246 273.005 1.00 48.44  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 216.529 298.234 273.770 1.00 45.59  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 217.044 300.663 273.451 1.00 47.41  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 219.304 297.088 271.680 1.00 41.81  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 219.643 295.704 271.363 1.00 42.15  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 221.038 295.347 271.861 1.00 47.89  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 221.255 294.248 272.384 1.00 54.36  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 219.538 295.472 269.856 1.00 41.24  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 218.141 295.534 269.242 1.00 42.95  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 218.233 295.657 267.732 1.00 42.63  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 217.334 294.310 269.632 1.00 46.00  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 221.998 296.260 271.698 1.00 44.52  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 223.352 296.004 272.178 1.00 38.67  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 223.387 295.888 273.697 1.00 49.36  ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 224.114 295.051 274.244 1.00 60.40  ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 224.297 297.106 271.700 1.00 43.87  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 222.617 296.727 274.394 1.00 51.88  ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 222.563 296.648 275.850 1.00 51.40  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 221.944 295.334 276.311 1.00 52.68  ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 222.398 294.737 277.294 1.00 56.73  ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 221.779 297.835 276.409 1.00 56.26  ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 222.621 299.091 276.517 1.00 62.69  ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 223.823 299.034 276.181 1.00 61.91  ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 222.080 300.136 276.935 1.00 59.01  ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 220.901 294.873 275.617 1.00 53.82  ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 220.225 293.643 276.020 1.00 51.09  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 221.128 292.428 275.847 1.00 49.34  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 221.096 291.500 276.664 1.00 58.84  ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 218.933 293.470 275.223 1.00 52.74  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 218.059 294.567 275.425 1.00 54.41  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 221.931 292.408 274.782 1.00 45.94  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 222.822 291.277 274.544 1.00 52.71  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 223.902 291.206 275.617 1.00 54.28  ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 224.314 290.115 276.031 1.00 59.87  ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 223.420 291.364 273.128 1.00 45.78  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 224.562 290.376 272.961 1.00 53.78  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 222.343 291.100 272.095 1.00 46.42  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 224.368 292.363 276.094 1.00 55.14  ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 225.432 292.389 277.092 1.00 57.99  ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 225.046 291.673 278.379 1.00 61.39  ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 225.923 291.129 279.058 1.00 63.41  ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 225.829 293.833 277.397 1.00 59.13  ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 226.894 294.417 276.470 1.00 63.58  ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 226.971 295.929 276.613 1.00 63.24  ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 228.242 293.773 276.746 1.00 62.45  ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 223.765 291.658 278.731 1.00 71.40  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 223.284 290.917 279.887 1.00 72.24  ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 222.747 289.557 279.451 1.00 69.89  ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 222.514 289.299 278.268 1.00 71.80  ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 222.209 291.715 280.632 1.00 69.34  ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 220.937 291.944 279.838 1.00 69.49  ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 219.697 292.871 280.762 1.00 82.55  ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 219.170 291.640 281.952 1.00 71.77  ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 222.555 288.679 280.432 1.00 79.40  ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 222.129 287.316 280.144 1.00 81.70  ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 220.684 287.292 279.661 1.00 85.28  ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 219.813 287.953 280.234 1.00 84.72  ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 222.289 286.437 281.382 1.00 82.09  ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 223.732 286.234 281.804 1.00 84.32  ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 224.529 285.434 280.792 1.00 86.74  ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 223.937 284.561 280.123 1.00 82.46  ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 225.746 285.680 280.664 1.00 87.26  ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 220.436 286.527 278.608 1.00 71.59  ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 219.129 286.376 277.991 1.00 67.54  ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 218.850 284.902 277.751 1.00 65.60  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 219.779 284.089 277.684 1.00 62.26  ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 219.049 287.142 276.661 1.00 61.17  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 219.558 288.573 276.721 1.00 56.58  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 218.565 289.521 277.365 1.00 59.28  ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 217.476 289.118 277.773 1.00 62.11  ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 218.936 290.791 277.457 1.00 64.91  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 217.579 284.520 277.635 1.00 67.10  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 217.266 283.143 277.269 1.00 60.60  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 217.823 282.818 275.898 1.00 66.25  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 217.969 283.710 275.040 1.00 74.32  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 215.731 283.115 277.278 1.00 59.53  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 215.334 284.237 278.167 1.00 60.32  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 216.372 285.296 277.969 1.00 64.72  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 218.168 281.550 275.650 1.00 64.44  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 218.793 281.202 274.361 1.00 62.45  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 217.953 281.573 273.150 1.00 61.48  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 218.506 282.010 272.133 1.00 62.99  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 218.991 279.683 274.470 1.00 62.68  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 218.995 279.400 275.937 1.00 65.90  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 218.044 280.385 276.541 1.00 59.28  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 216.630 281.414 273.227 1.00 57.73  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 215.782 281.796 272.102 1.00 53.42  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 215.733 283.309 271.936 1.00 59.40  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 215.767 283.817 270.809 1.00 61.82  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 214.375 281.229 272.286 1.00 59.83  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 213.388 281.524 271.154 1.00 60.90  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 213.802 280.803 269.881 1.00 57.68  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 211.974 281.139 271.557 1.00 58.00  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 215.650 284.046 273.046 1.00 56.44  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 215.643 285.503 272.966 1.00 45.85  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 216.999 286.036 272.522 1.00 48.18  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 217.074 287.044 271.809 1.00 59.87  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 215.246 286.101 274.315 1.00 46.35  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 215.042 287.606 274.290 1.00 49.75  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 215.183 288.202 275.678 1.00 54.99  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 214.030 287.907 276.520 1.00 57.33  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 213.944 288.213 277.807 1.00 57.56  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 214.932 288.827 278.439 1.00 55.10  ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 212.840 287.897 278.477 1.00 55.12  ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 218.082 285.376 272.937 1.00 40.95  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 219.416 285.813 272.537 1.00 45.22  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 219.600 285.718 271.028 1.00 54.34  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 220.191 286.611 270.410 1.00 62.88  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 220.478 284.984 273.259 1.00 49.60  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 221.871 285.587 273.218 1.00 51.60  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 222.936 284.517 273.381 1.00 55.22  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 223.149 283.771 272.146 1.00 63.36  ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 223.170 282.448 272.064 1.00 61.94  ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 222.996 281.686 273.132 1.00 52.46  ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 223.370 281.875 270.881 1.00 56.22  ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 219.105 284.639 270.418 1.00 54.94  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 219.198 284.504 268.968 1.00 45.35  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 218.345 285.551 268.262 1.00 44.16  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 218.732 286.064 267.206 1.00 55.64  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 218.788 283.094 268.544 1.00 46.07  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 219.679 282.003 269.114 1.00 48.21  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 219.441 280.666 268.433 1.00 53.03  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 220.024 280.621 267.097 1.00 56.02  ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 219.731 279.706 266.183 1.00 58.09  ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 218.864 278.737 266.427 1.00 54.46  ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 220.322 279.766 264.993 1.00 55.29  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 217.179 285.874 268.825 1.00 38.54  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 216.347 286.927 268.252 1.00 37.17  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 217.052 288.276 268.303 1.00 41.11  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 216.980 289.060 267.349 1.00 45.27  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 215.007 286.997 268.985 1.00 41.03  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 214.064 285.848 268.674 1.00 38.21  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 212.753 286.000 269.426 1.00 39.11  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 211.816 284.838 269.146 1.00 45.84  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 210.544 284.959 269.908 1.00 46.21  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 217.732 288.569 269.415 1.00 37.24  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 218.470 289.823 269.523 1.00 34.95  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 219.611 289.882 268.515 1.00 40.27  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 219.858 290.929 267.906 1.00 49.68  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 219.003 289.999 270.945 1.00 42.11  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 217.970 290.167 272.060 1.00 37.36  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 218.609 289.917 273.415 1.00 42.42  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 217.340 291.548 272.011 1.00 40.69  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 220.323 288.766 268.331 1.00 40.39  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 221.419 288.737 267.369 1.00 37.17  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 220.910 288.935 265.946 1.00 41.70  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 221.563 289.598 265.132 1.00 47.12  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 222.188 287.422 267.489 1.00 38.61  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 222.968 287.279 268.784 1.00 45.37  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 223.483 285.871 269.003 1.00 55.67  ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 223.218 285.000 268.148 1.00 55.48  ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 224.152 285.634 270.030 1.00 51.36  ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 219.751 288.356 265.625 1.00 42.22  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 219.154 288.575 264.312 1.00 31.39  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 218.766 290.035 264.120 1.00 41.14  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 218.954 290.599 263.036 1.00 45.04  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 217.934 287.673 264.132 1.00 26.29  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 218.261 286.214 264.081 1.00 41.47  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 217.291 285.235 264.073 1.00 42.01  ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 219.449 285.567 264.034 1.00 42.70  ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 217.868 284.048 264.025 1.00 41.92  ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 219.177 284.221 264.000 1.00 45.26  ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 218.213 290.662 265.161 1.00 37.54  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 217.811 292.060 265.055 1.00 23.68  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 219.019 292.975 264.905 1.00 31.73  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 218.981 293.943 264.138 1.00 50.52  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 216.980 292.460 266.275 1.00 36.37  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 215.466 292.287 266.146 1.00 32.87  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 214.751 292.990 267.286 1.00 39.42  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 214.977 292.806 264.803 1.00 37.12  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 220.101 292.689 265.633 1.00 28.55  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 221.311 293.499 265.518 1.00 33.03  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 221.888 293.395 264.112 1.00 37.01  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 222.306 294.395 263.517 1.00 50.60  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 222.344 293.084 266.581 1.00 33.57  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 221.862 293.474 267.976 1.00 35.04  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 223.696 293.716 266.293 1.00 33.67  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 222.733 292.939 269.079 1.00 34.22  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 221.913 292.180 263.560 1.00 36.74  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 222.518 291.969 262.248 1.00 39.32  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 221.803 292.779 261.173 1.00 39.17  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 222.445 293.398 260.317 1.00 47.53  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 222.504 290.481 261.899 1.00 38.78  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 223.122 289.735 262.954 1.00 35.27  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 223.257 290.231 260.603 1.00 42.29  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 220.469 292.788 261.200 1.00 25.24  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 219.730 293.542 260.194 1.00 28.00  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 219.773 295.042 260.458 1.00 35.71  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 219.940 295.827 259.518 1.00 54.81  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 218.281 293.059 260.117 1.00 35.63  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 217.440 293.789 259.071 1.00 46.27  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 217.750 293.369 257.638 1.00 55.15  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 218.835 292.807 257.380 1.00 47.56  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 216.902 293.616 256.756 1.00 50.38  ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 219.624 295.462 261.718 1.00 29.97  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 219.628 296.891 262.017 1.00 26.06  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 220.986 297.523 261.744 1.00 27.37  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 221.061 298.726 261.468 1.00 34.43  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 219.207 297.134 263.465 1.00 31.33  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 217.725 297.455 263.672 1.00 29.57  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 216.850 296.230 263.457 1.00 33.60  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 217.499 298.045 265.050 1.00 28.07  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 222.065 296.743 261.827 1.00 32.46  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 223.364 297.236 261.380 1.00 33.87  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 223.332 297.509 259.882 1.00 39.65  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 223.833 298.537 259.410 1.00 47.71  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 224.476 296.239 261.757 1.00 30.22  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 225.706 296.453 260.891 1.00 36.45  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 224.832 296.378 263.228 1.00 29.99  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 222.732 296.597 259.113 1.00 28.16  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 222.563 296.826 257.682 1.00 19.82  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 221.656 298.021 257.418 1.00 34.73  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 221.927 298.828 256.521 1.00 49.56  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 222.005 295.570 257.014 1.00 29.17  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 221.613 295.770 255.584 1.00 39.16  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 222.515 296.140 254.610 1.00 39.75  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 220.416 295.651 254.963 1.00 39.36  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 221.890 296.241 253.450 1.00 39.53  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 220.616 295.950 253.637 1.00 38.25  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 220.571 298.149 258.186 1.00 36.10  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 219.685 299.300 258.030 1.00 27.66  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 220.408 300.598 258.361 1.00 33.38  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 220.220 301.614 257.682 1.00 39.75  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 218.447 299.137 258.911 1.00 27.18  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 217.635 297.887 258.626 1.00 34.28  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 216.377 297.809 259.466 1.00 39.12  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 216.250 298.496 260.479 1.00 39.10  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 215.439 296.968 259.049 1.00 39.41  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 221.231 300.587 259.412 1.00 42.99  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 222.006 301.774 259.759 1.00 38.29  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 223.005 302.120 258.662 1.00 37.02  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 223.187 303.295 258.327 1.00 43.45  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 222.721 301.556 261.092 1.00 40.62  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 223.561 302.732 261.554 1.00 43.30  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 224.533 302.311 262.643 1.00 43.02  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 225.507 301.341 262.159 1.00 49.91  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 226.361 300.686 262.933 1.00 52.33  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 226.388 300.871 264.243 1.00 48.70  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 227.209 299.824 262.380 1.00 48.76  ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 223.662 301.107 258.091 1.00 34.26  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 224.619 301.355 257.017 1.00 37.83  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 223.931 301.922 255.782 1.00 42.06  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 224.452 302.841 255.139 1.00 46.82  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 225.364 300.066 256.672 1.00 42.17  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 226.303 299.622 257.776 1.00 52.88  ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 226.504 300.397 258.735 1.00 51.46  ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 226.840 298.498 257.686 1.00 48.55  ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 222.763 301.381 255.428 1.00 39.48  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 222.031 301.879 254.267 1.00 36.84  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 221.574 303.314 254.496 1.00 38.62  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 221.676 304.162 253.600 1.00 50.36  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 220.847 300.949 253.945 1.00 36.03  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 219.904 301.607 252.951 1.00 41.24  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 221.351 299.626 253.401 1.00 32.91  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 221.066 303.611 255.694 1.00 35.16  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 220.599 304.963 255.985 1.00 32.45  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 221.744 305.968 255.937 1.00 39.61  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 221.567 307.095 255.460 1.00 52.22  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 219.906 305.001 257.346 1.00 44.72  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 219.017 303.882 257.462 1.00 40.04  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 219.109 306.285 257.499 1.00 41.53  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 222.923 305.583 256.432 1.00 43.73  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 224.093 306.448 256.306 1.00 38.01  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 224.457 306.667 254.843 1.00 48.39  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 224.820 307.781 254.446 1.00 55.60  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 225.278 305.855 257.067 1.00 41.02  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 225.115 305.834 258.577 1.00 48.39  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 226.339 305.227 259.244 1.00 44.29  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 226.208 305.173 260.694 1.00 48.09  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 227.109 304.640 261.507 1.00 55.42  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 228.218 304.087 261.043 1.00 51.73  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 226.892 304.660 262.819 1.00 53.29  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 224.376 305.612 254.029 1.00 49.00  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 224.654 305.753 252.603 1.00 40.80  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 223.652 306.686 251.935 1.00 45.53  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 224.024 307.499 251.081 1.00 52.85  ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 224.642 304.381 251.930 1.00 44.51  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 224.607 304.505 250.519 1.00 53.08  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 222.374 306.577 252.305 1.00 41.43  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 221.363 307.467 251.745 1.00 39.40  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 221.609 308.913 252.156 1.00 47.01  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 221.443 309.834 251.347 1.00 57.62  ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 219.968 307.015 252.178 1.00 41.82  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 219.469 305.691 251.598 1.00 47.69  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 217.993 305.499 251.905 1.00 45.35  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 219.720 305.626 250.100 1.00 45.22  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 221.997 309.133 253.413 1.00 51.61  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 222.263 310.488 253.883 1.00 48.73  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 223.510 311.054 253.215 1.00 50.82  ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 223.544 312.227 252.824 1.00 53.82  ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 222.381 310.500 255.418 1.00 44.17  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 221.012 310.265 256.058 1.00 43.80  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 222.978 311.811 255.904 1.00 54.53  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 221.041 310.231 257.568 1.00 51.64  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 224.551 310.230 253.066 1.00 55.17  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 225.807 310.710 252.499 1.00 56.39  ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 225.641 311.138 251.045 1.00 57.89  ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 226.192 312.162 250.626 1.00 65.06  ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 226.881 309.629 252.618 1.00 57.53  ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 228.267 310.081 252.194 1.00 61.09  ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 229.212 308.900 252.048 1.00 60.93  ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 230.655 309.360 251.923 1.00 61.79  ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 231.125 310.048 253.157 1.00 62.35  ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 224.887 310.371 250.262 1.00 61.27  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 224.736 310.638 248.838 1.00 62.88  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 223.597 311.601 248.525 1.00 62.60  ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 223.378 311.913 247.350 1.00 68.82  ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 224.530 309.326 248.075 1.00 65.05  ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 225.634 308.456 248.250 1.00 68.74  ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 222.871 312.070 249.540 1.00 63.99  ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 221.845 313.104 249.395 1.00 67.32  ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 220.751 312.677 248.411 1.00 68.17  ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 220.550 313.274 247.354 1.00 67.66  ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 222.476 314.434 248.970 1.00 68.10  ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 223.474 315.002 249.965 1.00 65.47  ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 222.784 315.459 251.240 1.00 69.06  ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 223.783 316.021 252.238 1.00 70.77  ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 224.379 317.302 251.764 1.00 66.17  ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 220.044 311.618 248.795 1.00 63.97  ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 218.874 311.147 248.061 1.00 63.83  ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 217.641 311.822 248.644 1.00 67.70  ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 217.373 311.716 249.847 1.00 73.11  ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 218.738 309.616 248.114 1.00 63.87  ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 219.927 308.928 247.436 1.00 63.78  ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 217.428 309.175 247.483 1.00 65.27  ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 221.090 308.653 248.346 1.00 64.48  ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 216.892 312.519 247.792 1.00 69.54  ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 215.666 313.193 248.193 1.00 72.23  ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 214.434 312.655 247.481 1.00 74.30  ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 213.330 313.156 247.717 1.00 75.17  ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 215.790 314.701 247.946 1.00 74.38  ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 216.265 315.024 246.542 1.00 78.69  ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 216.552 314.080 245.777 1.00 74.58  ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 216.352 316.223 246.204 1.00 81.57  ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 214.589 311.654 246.619 1.00 63.94  ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 213.487 311.088 245.854 1.00 60.45  ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 213.391 309.596 246.133 1.00 62.10  ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 214.412 308.903 246.182 1.00 67.07  ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 213.675 311.334 244.355 1.00 61.99  ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 212.363 311.351 243.598 1.00 67.89  ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 211.288 311.356 244.197 1.00 72.94  ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 212.445 311.358 242.273 1.00 64.93  ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 212.163 309.107 246.316 1.00 55.29  ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 211.947 307.681 246.526 1.00 51.76  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 212.183 306.859 245.266 1.00 55.66  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 212.326 305.636 245.365 1.00 61.29  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 210.530 307.435 247.045 1.00 50.28  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 212.227 307.493 244.097 1.00 52.13  ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 212.475 306.804 242.839 1.00 51.54  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 213.953 306.745 242.478 1.00 53.79  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 214.300 306.171 241.441 1.00 55.35  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 211.696 307.479 241.705 1.00 47.92  ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 210.205 307.620 241.971 1.00 52.63  ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 209.553 306.271 242.235 1.00 60.41  ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 209.682 305.348 241.032 1.00 59.40  ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 209.142 303.989 241.312 1.00 57.13  ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 214.825 307.328 243.298 1.00 48.81  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 216.257 307.269 243.038 1.00 47.36  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 216.754 305.834 243.153 1.00 44.71  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 216.325 305.085 244.034 1.00 53.50  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 217.005 308.174 244.015 1.00 50.99  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 218.405 308.004 243.900 1.00 58.78  ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 217.664 305.451 242.254 1.00 38.14  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 218.114 304.063 242.218 1.00 35.94  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 218.951 303.704 243.438 1.00 48.31  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 219.055 302.523 243.788 1.00 55.56  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 218.903 303.789 240.939 1.00 32.35  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 219.088 302.328 240.652 1.00 37.43  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 218.002 301.532 240.328 1.00 35.98  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 220.340 301.744 240.725 1.00 37.33  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 218.164 300.186 240.069 1.00 37.01  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 220.507 300.397 240.468 1.00 36.58  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 219.418 299.618 240.139 1.00 41.24  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 219.561 304.696 244.093 1.00 43.38  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 220.295 304.418 245.324 1.00 43.83  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 219.371 303.865 246.401 1.00 48.63  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 219.805 303.111 247.279 1.00 55.63  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 221.007 305.680 245.815 1.00 47.89  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 222.135 306.159 244.910 1.00 49.83  ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 221.645 306.989 243.739 1.00 58.18  ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 220.428 307.249 243.659 1.00 59.11  ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 222.480 307.381 242.897 1.00 60.94  ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 218.091 304.230 246.348 1.00 39.79  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 217.084 303.643 247.222 1.00 36.96  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 216.364 302.475 246.558 1.00 47.15  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 215.958 301.529 247.241 1.00 56.96  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 216.072 304.710 247.650 1.00 43.76  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 214.890 304.170 248.402 1.00 44.69  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 213.575 304.320 248.074 1.00 37.05  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 214.915 303.400 249.612 1.00 46.98  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 212.780 303.691 249.000 1.00 41.24  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 213.578 303.119 249.955 1.00 40.48  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 215.937 302.922 250.438 1.00 44.57  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 213.236 302.380 251.085 1.00 44.70  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 215.596 302.188 251.560 1.00 43.14  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 214.257 301.925 251.873 1.00 44.95  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 216.201 302.523 245.233 1.00 41.89  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 215.518 301.443 244.530 1.00 27.26  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 216.355 300.170 244.491 1.00 33.51  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 215.800 299.067 244.549 1.00 43.34  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 215.157 301.882 243.111 1.00 27.28  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 214.020 302.896 242.976 1.00 39.12  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 213.508 302.935 241.547 1.00 39.12  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 212.891 302.578 243.943 1.00 41.54  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 217.681 300.296 244.393 1.00 31.09  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 218.534 299.113 244.354 1.00 27.59  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 218.542 298.362 245.678 1.00 41.01  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 218.906 297.182 245.703 1.00 49.34  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 219.963 299.502 243.972 1.00 34.47  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 220.407 300.616 244.726 1.00 39.16  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 218.153 299.012 246.770 1.00 39.38  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 218.050 298.341 248.053 1.00 37.09  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 216.784 297.493 248.104 1.00 44.46  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 215.824 297.715 247.360 1.00 38.68  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 218.041 299.358 249.195 1.00 38.96  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 219.170 300.374 249.143 1.00 40.07  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 220.538 299.735 249.265 1.00 49.74  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 220.738 298.816 250.058 1.00 48.65  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 221.491 300.223 248.480 1.00 42.29  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 216.789 296.507 248.995 1.00 46.44  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 215.606 295.683 249.209 1.00 39.90  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 214.644 296.416 250.134 1.00 43.07  ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 215.030 296.853 251.224 1.00 47.27  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 215.986 294.323 249.785 1.00 33.49  ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 214.803 293.383 249.917 1.00 42.66  ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 215.248 291.774 250.581 1.00 70.88  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 216.123 291.074 249.187 1.00 35.78  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 213.396 296.551 249.698 1.00 28.15  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 212.389 297.322 250.407 1.00 27.73  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 211.166 296.455 250.667 1.00 34.90  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 210.808 295.596 249.856 1.00 38.04  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 211.999 298.570 249.606 1.00 33.41  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 213.183 299.229 248.912 1.00 31.08  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 212.756 300.363 248.000 1.00 33.15  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 211.903 299.901 246.912 1.00 31.36  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 212.336 299.245 245.844 1.00 32.22  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 213.615 298.941 245.690 1.00 44.66  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 211.465 298.882 244.907 1.00 39.29  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 210.528 296.688 251.811 1.00 41.98  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 209.377 295.910 252.249 1.00 23.56  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 208.179 296.834 252.401 1.00 35.92  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 208.269 297.868 253.072 1.00 48.00  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 209.661 295.188 253.571 1.00 26.19  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 210.852 294.269 253.524 1.00 32.52  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 212.143 294.774 253.552 1.00 35.15  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 210.679 292.897 253.456 1.00 33.64  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 213.234 293.930 253.509 1.00 30.01  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 211.767 292.048 253.415 1.00 39.26  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 213.046 292.566 253.441 1.00 34.17  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 207.063 296.460 251.781 1.00 43.42  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 205.835 297.241 251.818 1.00 43.59  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 204.702 296.375 252.344 1.00 43.63  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 204.517 295.242 251.887 1.00 55.07  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 205.490 297.788 250.430 1.00 41.91  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 206.591 298.620 249.815 1.00 49.16  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 206.736 299.962 250.141 1.00 51.12  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 207.489 298.065 248.914 1.00 42.48  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 207.740 300.728 249.584 1.00 50.85  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 208.497 298.824 248.352 1.00 40.14  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 208.618 300.154 248.691 1.00 47.39  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 209.619 300.915 248.134 1.00 50.91  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 203.949 296.909 253.302 1.00 46.12  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 202.835 296.206 253.921 1.00 51.25  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 201.544 296.952 253.619 1.00 55.69  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 201.475 298.174 253.788 1.00 56.17  ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 203.036 296.079 255.433 1.00 48.61  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 202.246 294.968 256.059 1.00 44.11  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 202.617 293.647 255.872 1.00 47.15  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 201.135 295.242 256.838 1.00 46.46  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 201.893 292.622 256.447 1.00 47.86  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 200.407 294.221 257.415 1.00 50.09  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 200.787 292.909 257.219 1.00 52.35  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 200.528 296.218 253.173 1.00 69.98  ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 199.226 296.795 252.838 1.00 71.24  ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 198.159 296.193 253.740 1.00 74.49  ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 197.651 295.093 253.458 1.00 76.19  ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 198.886 296.553 251.369 1.00 72.76  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 197.752 297.433 250.880 1.00 78.49  ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 197.315 298.320 251.643 1.00 79.40  ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 197.298 297.237 249.734 1.00 76.17  ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 197.790 296.865 254.835 1.00 81.42  ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 196.740 296.319 255.711 1.00 82.57  ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 195.372 296.247 255.054 1.00 83.05  ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 194.516 295.493 255.534 1.00 82.64  ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 196.735 297.289 256.901 1.00 80.69  ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 197.296 298.560 256.353 1.00 79.43  ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 198.308 298.154 255.322 1.00 80.19  ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 195.137 296.999 253.979 1.00 84.53  ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 193.839 297.002 253.318 1.00 86.82  ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 193.647 295.824 252.372 1.00 84.22  ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 192.548 295.661 251.831 1.00 88.72  ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 193.642 298.311 252.551 1.00 86.63  ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 193.689 299.553 253.425 1.00 87.91  ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 192.522 299.585 254.398 1.00 86.56  ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 192.471 300.901 255.155 1.00 87.92  ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 193.608 301.039 256.106 1.00 87.69  ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 194.676 295.009 252.158 1.00 76.27  ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 194.547 293.860 251.272 1.00 78.58  ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 193.698 292.781 251.933 1.00 83.01  ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 193.945 292.396 253.080 1.00 80.02  ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 195.927 293.309 250.917 1.00 76.28  ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 195.899 292.134 249.954 1.00 77.77  ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 195.851 292.570 248.504 1.00 81.76  ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 196.446 293.580 248.127 1.00 80.06  ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 195.142 291.807 247.680 1.00 80.70  ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 192.689 292.297 251.204 1.00 88.43  ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 191.809 291.267 251.748 1.00 87.07  ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 192.561 289.964 251.991 1.00 88.27  ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 192.354 289.303 253.015 1.00 88.38  ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 190.627 291.034 250.808 1.00 89.38  ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 191.108 290.586 249.535 1.00 89.77  ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 189.835 292.320 250.622 1.00 87.77  ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 193.435 289.580 251.064 1.00 76.59  ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 194.214 288.357 251.206 1.00 74.20  ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 195.418 288.626 252.101 1.00 71.61  ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 196.279 289.445 251.763 1.00 73.37  ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 194.658 287.847 249.837 1.00 69.80  ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 195.089 286.394 249.869 1.00 74.94  ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 194.906 285.741 250.917 1.00 75.14  ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 195.609 285.905 248.844 1.00 74.64  ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 195.475 287.938 253.244 1.00 57.27  ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 196.583 288.136 254.173 1.00 60.21  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 197.899 287.671 253.562 1.00 62.82  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 198.969 288.179 253.917 1.00 62.83  ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 196.297 287.422 255.507 1.00 59.84  ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 195.129 288.085 256.221 1.00 59.86  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 196.015 285.946 255.274 1.00 57.58  ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 197.850 286.707 252.641 1.00 50.82  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 199.064 286.208 252.008 1.00 51.87  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 199.659 287.192 251.010 1.00 55.41  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 200.797 286.990 250.573 1.00 62.55  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 198.780 284.877 251.310 1.00 51.99  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 198.452 283.686 252.215 1.00 51.32  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 198.408 282.398 251.409 1.00 56.31  ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 199.455 283.576 253.352 1.00 51.46  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 198.927 288.244 250.640 1.00 53.82  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 199.406 289.231 249.680 1.00 52.35  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 199.606 290.607 250.303 1.00 53.01  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 199.821 291.581 249.572 1.00 55.33  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 198.438 289.333 248.497 1.00 57.09  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 198.096 287.998 247.858 1.00 56.68  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 199.178 287.510 246.918 1.00 61.10  ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 199.922 288.304 246.343 1.00 62.62  ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 199.273 286.195 246.756 1.00 61.46  ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 199.540 290.716 251.632 1.00 52.76  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 199.695 292.015 252.277 1.00 51.93  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 201.125 292.530 252.185 1.00 52.86  ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 201.338 293.735 252.013 1.00 52.09  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 199.257 291.933 253.738 1.00 49.96  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 197.768 291.708 253.928 1.00 51.53  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 197.328 291.916 255.362 1.00 58.90  ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 197.871 291.309 256.285 1.00 61.49  ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 196.339 292.781 255.558 1.00 58.66  ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 202.111 291.644 252.293 1.00 40.51  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 203.515 292.029 252.282 1.00 36.25  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 204.099 291.824 250.891 1.00 43.94  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 203.919 290.762 250.286 1.00 40.83  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 204.310 291.223 253.310 1.00 31.62  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 205.832 291.337 253.212 1.00 27.97  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 206.285 292.766 253.466 1.00 35.77  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 206.502 290.383 254.180 1.00 36.52  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 204.794 292.843 250.391 1.00 38.43  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 205.476 292.782 249.105 1.00 31.04  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 206.931 293.170 249.311 1.00 33.16  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 207.219 294.209 249.914 1.00 42.05  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 204.812 293.707 248.081 1.00 42.53  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 205.576 293.784 246.891 1.00 47.88  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 207.842 292.339 248.816 1.00 33.26  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 209.273 292.608 248.901 1.00 26.15  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 209.759 293.025 247.520 1.00 30.46  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 209.595 292.284 246.545 1.00 40.19  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 210.042 291.382 249.413 1.00 30.82  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 209.342 290.788 250.636 1.00 27.56  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 211.478 291.754 249.743 1.00 25.50  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 210.011 289.546 251.175 1.00 35.09  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 210.358 294.210 247.435 1.00 37.25  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 210.764 294.792 246.162 1.00 27.67  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 212.249 295.113 246.209 1.00 32.45  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 212.723 295.730 247.168 1.00 51.42  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 209.952 296.053 245.853 1.00 27.88  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 208.457 295.892 246.065 1.00 42.15  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 207.668 297.103 245.612 1.00 51.35  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 208.230 298.062 245.083 1.00 51.10  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 206.357 297.067 245.820 1.00 43.55  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 212.977 294.691 245.178 1.00 26.64  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 214.392 295.004 245.021 1.00 30.26  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 214.636 295.356 243.563 1.00 41.36  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 214.415 294.521 242.679 1.00 48.84  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 215.274 293.827 245.450 1.00 29.01  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 216.766 294.099 245.355 1.00 35.10  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 217.726 293.101 246.508 1.00 53.68  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 219.277 293.994 246.514 1.00 32.26  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 215.086 296.585 243.317 1.00 40.63  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 215.282 297.123 241.963 1.00 39.23  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 213.924 297.073 241.265 1.00 40.87  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 212.957 297.656 241.782 1.00 41.91  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 216.415 296.381 241.263 1.00 34.35  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 213.795 296.409 240.119 1.00 35.45  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 212.521 296.282 239.427 1.00 33.40  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 211.855 294.934 239.672 1.00 49.53  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 210.880 294.604 238.991 1.00 53.07  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 212.709 296.503 237.925 1.00 38.70  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 213.466 295.371 237.260 1.00 51.23  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 214.632 295.124 237.565 1.00 51.65  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 212.803 294.675 236.344 1.00 50.35  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 212.356 294.153 240.626 1.00 45.19  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 211.846 292.814 240.901 1.00 33.29  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 210.812 292.899 242.017 1.00 35.58  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 211.079 293.470 243.079 1.00 43.05  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 212.985 291.868 241.274 1.00 30.26  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 209.635 292.331 241.774 1.00 49.44  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 208.541 292.329 242.736 1.00 35.71  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 208.340 290.912 243.256 1.00 39.57  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 208.232 289.968 242.467 1.00 47.47  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 207.254 292.846 242.092 1.00 39.59  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 207.353 294.265 241.556 1.00 48.23  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 207.558 295.272 242.670 1.00 53.13  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 207.489 296.696 242.144 1.00 50.60  ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 208.655 297.021 241.276 1.00 48.85  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 208.290 290.764 244.579 1.00 34.56  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 208.181 289.456 245.205 1.00 30.15  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 207.111 289.469 246.287 1.00 34.59  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 206.767 290.515 246.844 1.00 40.46  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 209.516 289.005 245.814 1.00 24.21  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 210.606 288.810 244.804 1.00 36.45  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 210.544 287.771 243.892 1.00 33.99  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 211.694 289.663 244.769 1.00 38.86  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 211.546 287.588 242.961 1.00 39.17  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 212.698 289.484 243.841 1.00 34.68  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 212.625 288.446 242.936 1.00 40.48  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 206.587 288.281 246.572 1.00 41.63  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 205.635 288.062 247.648 1.00 44.43  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 206.227 287.094 248.664 1.00 47.23  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 206.918 286.137 248.304 1.00 46.79  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 204.312 287.507 247.112 1.00 38.28  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 203.240 288.570 246.989 1.00 51.98  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 203.286 289.596 247.668 1.00 55.58  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 202.265 288.330 246.120 1.00 50.15  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 205.954 287.352 249.940 1.00 37.78  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 206.444 286.492 251.008 1.00 26.32  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 205.696 285.165 250.972 1.00 30.19  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 204.461 285.141 251.003 1.00 42.04  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 206.272 287.171 252.365 1.00 31.65  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 207.265 286.713 253.409 1.00 25.41  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 208.588 287.127 253.365 1.00 28.13  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 206.880 285.864 254.437 1.00 29.19  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 209.498 286.711 254.317 1.00 34.36  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 207.783 285.442 255.392 1.00 26.46  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 209.091 285.868 255.327 1.00 32.73  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 209.996 285.452 256.276 1.00 40.17  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 206.444 284.062 250.905 1.00 22.94  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 205.825 282.748 250.882 1.00 24.63  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 205.260 282.313 252.216 1.00 34.11  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 204.460 281.373 252.260 1.00 42.90  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 205.664 282.974 253.303 1.00 39.55  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 205.164 282.694 254.649 1.00 32.01  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 205.436 281.254 255.074 1.00 33.03  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 204.673 280.666 255.844 1.00 42.65  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 203.672 283.021 254.765 1.00 35.40  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 203.380 284.493 254.790 1.00 34.29  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 203.814 285.280 255.843 1.00 33.21  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 202.684 285.093 253.755 1.00 39.26  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 203.554 286.635 255.866 1.00 31.73  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 202.419 286.448 253.774 1.00 42.08  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 202.855 287.220 254.831 1.00 32.79  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 206.525 280.677 254.573 1.00 33.88  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 206.988 279.381 255.047 1.00 28.57  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 207.612 279.544 256.426 1.00 39.88  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 208.427 280.446 256.642 1.00 47.71  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 208.003 278.790 254.070 1.00 31.34  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 208.553 277.431 254.472 1.00 37.61  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 207.531 276.321 254.341 1.00 53.61  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 206.612 276.453 253.506 1.00 57.47  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 207.648 275.315 255.071 1.00 48.86  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 207.229 278.677 257.361 1.00 40.54  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 207.789 278.745 258.707 1.00 36.77  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 209.243 278.298 258.664 1.00 43.40  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 209.538 277.135 258.374 1.00 50.18  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 206.986 277.889 259.679 1.00 36.04  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 207.527 277.948 261.089 1.00 40.82  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 207.751 279.167 261.714 1.00 39.45  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 207.826 276.788 261.791 1.00 36.41  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 208.251 279.230 262.998 1.00 36.62  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 208.325 276.842 263.078 1.00 35.01  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 208.535 278.066 263.676 1.00 39.59  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 209.032 278.126 264.957 1.00 51.25  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 210.151 279.224 258.951 1.00 30.78  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 211.581 278.974 258.869 1.00 31.49  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 212.200 278.623 260.214 1.00 33.80  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 213.389 278.295 260.264 1.00 43.08  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 212.280 280.200 258.282 1.00 42.15  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 211.868 280.533 256.848 1.00 38.42  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 212.465 281.856 256.425 1.00 37.28  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 212.282 279.423 255.894 1.00 33.94  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 211.426 278.670 261.294 1.00 44.80  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 212.001 278.449 262.611 1.00 44.80  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 212.994 279.544 262.938 1.00 50.19  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 212.730 280.734 262.731 1.00 50.70  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 214.153 279.148 263.455 1.00 53.54  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 215.244 280.068 263.755 1.00 50.80  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 216.432 279.648 262.902 1.00 45.98  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 216.929 278.522 263.028 1.00 51.41  ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 215.604 280.070 265.247 1.00 48.21  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 216.621 281.159 265.543 1.00 45.27  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 214.356 280.255 266.095 1.00 45.40  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 216.889 280.548 262.036 1.00 42.61  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 217.995 280.280 261.130 1.00 50.27  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 219.111 281.288 261.360 1.00 53.91  ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 218.861 282.451 261.691 1.00 52.06  ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 217.545 280.334 259.665 1.00 52.03  ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 216.198 279.683 259.400 1.00 50.82  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 216.324 278.234 258.975 1.00 55.27  ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 217.340 277.587 259.227 1.00 57.14  ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 215.288 277.716 258.326 1.00 49.24  ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 220.349 280.834 261.176 1.00 56.13  ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 221.511 281.701 261.342 1.00 56.00  ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 221.526 282.741 260.229 1.00 54.18  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 221.868 282.431 259.084 1.00 54.63  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 222.792 280.873 261.334 1.00 57.83  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 223.052 280.188 262.661 1.00 63.90  ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 223.076 280.885 263.697 1.00 65.26  ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 223.235 278.952 262.668 1.00 62.67  ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 221.156 283.975 260.562 1.00 51.38  ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 221.133 285.043 259.572 1.00 54.60  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 222.551 285.473 259.221 1.00 52.80  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 223.412 285.592 260.098 1.00 48.07  ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 220.331 286.234 260.092 1.00 43.50  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 218.828 286.090 259.929 1.00 40.76  ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 218.099 287.299 260.487 1.00 52.41  ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 218.407 288.551 259.681 1.00 50.06  ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 217.815 288.495 258.316 1.00 54.01  ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 222.791 285.707 257.935 1.00 42.36  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 224.096 286.151 257.476 1.00 39.94  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 224.252 287.655 257.675 1.00 44.06  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 223.277 288.396 257.824 1.00 43.10  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 224.299 285.800 256.002 1.00 42.40  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 224.084 284.348 255.575 1.00 40.25  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 224.621 284.132 254.172 1.00 29.84  ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 224.743 283.389 256.554 1.00 43.53  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 225.503 288.101 257.673 1.00 48.71  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 225.805 289.526 257.718 1.00 37.64  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 225.610 290.107 256.326 1.00 41.58  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 226.174 289.606 255.345 1.00 43.14  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 227.233 289.766 258.230 1.00 28.85  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 227.588 291.240 258.134 1.00 31.91  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 227.373 289.271 259.660 1.00 34.69  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 224.807 291.166 256.233 1.00 41.91  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 224.443 291.753 254.944 1.00 40.92  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 225.605 292.610 254.449 1.00 38.97  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 225.636 293.834 254.594 1.00 39.55  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 223.155 292.557 255.069 1.00 45.72  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 222.494 292.878 253.742 1.00 47.94  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 221.785 291.684 253.135 1.00 42.51  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 221.648 290.638 253.769 1.00 44.03  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 221.330 291.834 251.897 1.00 37.44  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 226.582 291.938 253.850 1.00 38.63  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 227.760 292.591 253.305 1.00 40.39  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 227.474 293.146 251.913 1.00 43.40  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 226.485 292.773 251.276 1.00 52.38  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 228.924 291.607 253.250 1.00 37.65  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 228.645 290.583 252.287 1.00 42.08  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 229.143 290.969 254.611 1.00 34.01  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 228.316 294.065 251.425 1.00 41.52  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 228.141 294.545 250.042 1.00 40.34  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 228.145 293.433 249.006 1.00 36.20  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 227.424 293.529 248.005 1.00 37.37  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 229.328 295.498 249.863 1.00 40.40  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 229.559 296.039 251.227 1.00 41.25  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 229.258 294.910 252.182 1.00 41.33  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 228.944 292.382 249.209 1.00 38.50  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 228.892 291.238 248.303 1.00 32.87  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 227.535 290.550 248.370 1.00 34.33  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 227.005 290.100 247.347 1.00 49.85  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 230.011 290.250 248.628 1.00 34.28  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 230.113 289.052 247.679 1.00 32.56  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 230.275 289.516 246.240 1.00 42.50  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 231.254 288.132 248.078 1.00 30.60  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 226.960 290.452 249.571 1.00 37.33  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 225.618 289.897 249.708 1.00 37.65  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 224.589 290.773 249.004 1.00 35.40  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 223.649 290.263 248.382 1.00 48.29  ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 225.266 289.732 251.187 1.00 39.71  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 226.304 288.996 251.846 1.00 44.24  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 223.953 288.986 251.345 1.00 39.89  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 224.748 292.097 249.092 1.00 34.62  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 223.866 292.999 248.359 1.00 34.70  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 224.002 292.796 246.856 1.00 38.39  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 223.004 292.808 246.127 1.00 43.88  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 224.169 294.450 248.732 1.00 41.17  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 224.006 294.716 250.212 1.00 53.96  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 223.621 293.780 250.942 1.00 56.53  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 224.262 295.858 250.647 1.00 49.59  ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 225.234 292.616 246.374 1.00 43.75  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 225.437 292.301 244.964 1.00 34.93  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 224.809 290.960 244.609 1.00 37.78  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 224.227 290.804 243.530 1.00 43.29  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 226.931 292.303 244.638 1.00 30.90  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 227.249 292.402 243.157 1.00 36.68  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 228.731 292.181 242.903 1.00 44.29  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 229.054 292.191 241.482 1.00 44.58  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 230.055 292.877 240.947 1.00 43.90  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 230.854 293.626 241.689 1.00 45.43  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 230.260 292.808 239.635 1.00 42.26  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 224.926 289.975 245.504 1.00 33.07  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 224.270 288.691 245.281 1.00 28.46  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 222.755 288.838 245.285 1.00 38.67  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 222.066 288.263 244.435 1.00 45.01  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 224.715 287.683 246.341 1.00 37.58  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 224.050 286.017 246.113 1.00 44.64  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 222.219 289.607 246.234 1.00 38.80  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 220.775 289.810 246.296 1.00 24.01  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 220.267 290.524 245.049 1.00 29.20  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 219.226 290.161 244.493 1.00 42.39  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 220.413 290.595 247.557 1.00 32.54  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 220.261 289.741 248.797 1.00 32.95  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 221.015 288.588 248.971 1.00 34.63  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 219.373 290.098 249.801 1.00 29.84  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 220.877 287.808 250.103 1.00 36.52  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 219.229 289.327 250.936 1.00 36.82  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 219.983 288.185 251.083 1.00 40.24  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 219.842 287.416 252.215 1.00 46.47  ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 220.995 291.545 244.594 1.00 34.69  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 220.574 292.286 243.409 1.00 26.66  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 220.605 291.404 242.166 1.00 30.35  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 219.682 291.436 241.345 1.00 36.46  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 221.459 293.517 243.220 1.00 37.39  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 221.164 294.388 241.997 1.00 34.44  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 219.858 295.144 242.179 1.00 34.35  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 222.312 295.348 241.735 1.00 27.10  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 221.664 290.607 242.011 1.00 39.25  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 221.821 289.811 240.797 1.00 23.35  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 220.800 288.681 240.725 1.00 35.02  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 220.204 288.446 239.668 1.00 42.94  ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 223.242 289.254 240.715 1.00 31.03  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 224.185 290.323 240.860 1.00 34.67  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 223.467 288.567 239.378 1.00 32.56  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 220.583 287.970 241.835 1.00 29.34  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 219.656 286.842 241.810 1.00 23.93  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 218.211 287.305 241.672 1.00 28.00  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 217.404 286.641 241.011 1.00 43.64  ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 219.830 285.981 243.060 1.00 27.53  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 221.250 285.491 243.292 1.00 34.56  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 221.928 284.632 241.859 1.00 50.51  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 223.616 285.227 241.869 1.00 32.59  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 217.860 288.436 242.290 1.00 19.78  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 216.510 288.965 242.124 1.00 19.44  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 216.262 289.426 240.693 1.00 35.65  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 215.135 289.318 240.196 1.00 38.15  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 216.260 290.112 243.103 1.00 21.65  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 217.338 291.053 243.029 1.00 41.97  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 216.140 289.583 244.525 1.00 20.96  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 217.292 289.948 240.022 1.00 36.42  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 217.160 290.273 238.606 1.00 26.88  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 216.931 289.016 237.777 1.00 33.98  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 216.145 289.026 236.822 1.00 38.69  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 218.400 291.021 238.119 1.00 26.87  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 218.475 292.469 238.572 1.00 31.24  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 217.310 293.297 238.072 1.00 37.52  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 217.148 293.497 236.868 1.00 43.58  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 216.490 293.785 238.995 1.00 31.35  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 217.619 287.925 238.121 1.00 38.68  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 217.401 286.660 237.428 1.00 26.43  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 215.993 286.132 237.672 1.00 25.43  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 215.364 285.576 236.765 1.00 47.87  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 218.444 285.634 237.869 1.00 19.18  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 215.485 286.288 238.898 1.00 21.41  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 214.138 285.820 239.208 1.00 29.08  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 213.086 286.582 238.412 1.00 28.86  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 212.121 285.988 237.917 1.00 38.73  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 213.872 285.948 240.707 1.00 31.48  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 214.655 285.005 241.621 1.00 25.31  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 214.199 285.161 243.060 1.00 25.92  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 214.507 283.565 241.162 1.00 29.68  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 213.250 287.902 238.284 1.00 35.77  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 212.306 288.688 237.495 1.00 27.50  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 212.369 288.323 236.018 1.00 36.69  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 211.335 288.302 235.341 1.00 47.87  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 212.567 290.181 237.689 1.00 41.39  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 211.408 291.072 237.266 1.00 45.44  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 210.261 291.067 238.260 1.00 55.82  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 210.373 290.396 239.308 1.00 54.47  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 209.241 291.736 237.992 1.00 50.75  ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 213.563 288.039 235.502 1.00 37.34  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 213.713 287.530 234.146 1.00 39.00  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 213.352 286.056 234.035 1.00 42.51  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 213.401 285.504 232.931 1.00 53.44  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 215.145 287.751 233.654 1.00 37.69  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 213.008 285.414 235.152 1.00 36.03  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 212.656 284.000 235.250 1.00 41.09  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 213.812 283.085 234.875 1.00 32.62  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 213.588 281.907 234.571 1.00 44.82  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 211.418 283.657 234.412 1.00 45.41  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 210.104 283.888 235.150 1.00 38.28  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 209.851 285.368 235.390 1.00 40.99  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 208.620 285.614 236.130 1.00 46.30  ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 208.250 286.802 236.590 1.00 49.02  ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 208.986 287.882 236.385 1.00 46.30  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 207.116 286.908 237.276 1.00 52.70  ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 215.039 283.591 234.889 1.00 27.51  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 216.226 282.769 234.737 1.00 34.89  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 216.653 282.220 236.095 1.00 42.58  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 216.106 282.575 237.141 1.00 52.19  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 217.361 283.575 234.107 1.00 34.39  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 217.172 284.049 232.665 1.00 40.85  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 218.465 284.641 232.130 1.00 47.25  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 216.695 282.910 231.780 1.00 37.42  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 217.644 281.335 236.070 1.00 32.24  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 218.202 280.812 237.297 1.00 34.29  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 219.383 281.626 237.792 1.00 34.45  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 219.913 282.491 237.098 1.00 48.12  ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 219.790 281.337 239.023 1.00 24.49  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 220.949 281.971 239.626 1.00 23.82  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 222.137 281.025 239.621 1.00 35.14  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 222.004 279.844 239.938 1.00 42.92  ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 223.300 281.557 239.253 1.00 33.68  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 224.526 280.769 239.136 1.00 24.03  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 225.687 281.484 239.819 1.00 29.49  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 226.614 281.961 239.155 1.00 41.36  ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 224.849 280.492 237.668 1.00 31.86  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 226.072 279.790 237.539 1.00 53.53  ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 225.676 281.568 241.150 1.00 27.71  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 226.845 282.115 241.851 1.00 28.00  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 228.013 281.143 241.774 1.00 29.09  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 227.866 279.951 242.053 1.00 41.50  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 226.348 282.295 243.290 1.00 23.47  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 225.252 281.301 243.431 1.00 27.35  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 224.597 281.197 242.084 1.00 25.66  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 229.177 281.658 241.389 1.00 19.92  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 230.366 280.838 241.216 1.00 23.78  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 231.563 281.523 241.861 1.00 32.06  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 231.589 282.743 242.040 1.00 44.57  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 230.652 280.557 239.732 1.00 32.66  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 231.038 281.777 238.942 1.00 28.39  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 230.068 282.601 238.399 1.00 34.66  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 232.371 282.091 238.731 1.00 28.11  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 230.419 283.721 237.671 1.00 37.43  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 232.727 283.210 238.004 1.00 35.87  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 231.750 284.025 237.473 1.00 37.61  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 232.558 280.713 242.209 1.00 30.70  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 233.761 281.201 242.837 1.00 25.48  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 234.501 280.099 243.565 1.00 30.18  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 234.171 278.915 243.446 1.00 44.01  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 235.526 280.468 244.334 1.00 33.39  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 236.266 279.459 245.104 1.00 35.78  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 235.477 278.952 246.301 1.00 35.01  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 234.330 279.356 246.517 1.00 41.50  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 237.533 280.207 245.537 1.00 29.89  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 237.146 281.642 245.532 1.00 33.16  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 236.125 281.809 244.446 1.00 30.71  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 236.086 278.067 247.084 1.00 38.63  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 235.400 277.449 248.209 1.00 33.69  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 235.344 278.391 249.404 1.00 44.59  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 236.298 279.122 249.685 1.00 50.78  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 236.096 276.148 248.605 1.00 34.23  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 234.215 278.365 250.109 1.00 41.68  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 234.077 279.128 251.333 1.00 33.55  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 233.802 280.602 251.153 1.00 26.19  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 234.138 281.397 252.036 1.00 44.90  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 233.199 280.998 250.035 1.00 22.56  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 232.884 282.397 249.780 1.00 33.99  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 231.443 282.757 250.116 1.00 27.87  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 231.041 283.904 249.902 1.00 36.81  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 233.174 282.748 248.318 1.00 24.05  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 232.406 281.899 247.457 1.00 38.69  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 234.650 282.570 248.013 1.00 25.71  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 230.661 281.815 250.636 1.00 30.23  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 229.298 282.103 251.035 1.00 27.47  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 228.336 282.242 249.874 1.00 32.58  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 227.606 283.233 249.781 1.00 40.79  ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 228.321 281.253 248.981 1.00 29.96  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 227.449 281.291 247.811 1.00 23.81  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 226.118 280.593 248.080 1.00 29.08  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 225.051 281.167 247.843 1.00 33.64  ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 228.159 280.661 246.608 1.00 22.57  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 229.454 281.356 246.236 1.00 29.02  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 229.981 280.878 244.898 1.00 39.21  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 230.460 279.442 244.973 1.00 26.83  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 231.562 279.273 245.958 1.00 23.05  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 226.168 279.354 248.573 1.00 28.57  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 224.932 278.628 248.848 1.00 28.49  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 224.240 279.164 250.096 1.00 21.90  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 223.011 279.088 250.210 1.00 36.50  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 225.213 277.131 248.985 1.00 28.06  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 223.992 276.436 249.269 1.00 36.97  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 226.210 276.865 250.093 1.00 34.65  ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 225.009 279.705 251.044 1.00 30.21  ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 224.399 280.346 252.204 1.00 23.64  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 223.670 281.620 251.801 1.00 33.17  ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 222.604 281.934 252.345 1.00 43.14  ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 225.460 280.644 253.263 1.00 32.20  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 226.015 279.410 253.957 1.00 45.96  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 224.927 278.496 254.485 1.00 51.40  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 224.080 278.969 255.271 1.00 43.65  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 224.920 277.303 254.116 1.00 45.07  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 224.233 282.372 250.852 1.00 28.28  ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 223.566 283.574 250.363 1.00 21.78  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 222.267 283.233 249.644 1.00 28.54  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 221.268 283.947 249.785 1.00 34.05  ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 224.502 284.353 249.440 1.00 26.71  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 225.601 284.883 250.159 1.00 38.31  ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 222.265 282.151 248.860 1.00 34.11  ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 221.043 281.723 248.186 1.00 24.97  ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 219.984 281.326 249.206 1.00 33.54  ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 218.807 281.685 249.074 1.00 35.09  ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 221.346 280.574 247.207 1.00 31.08  ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 220.059 280.036 246.605 1.00 28.01  ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 222.291 281.046 246.114 1.00 29.30  ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 220.383 280.578 250.237 1.00 29.92  ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 219.450 280.239 251.307 1.00 17.83  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 218.986 281.487 252.046 1.00 27.03  ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 217.805 281.613 252.385 1.00 39.69  ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 220.095 279.252 252.278 1.00 26.24  ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 220.375 277.883 251.685 1.00 29.78  ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 220.526 276.834 252.773 1.00 36.14  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 221.534 277.267 253.824 1.00 29.87  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 221.634 276.283 254.937 1.00 29.23  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 219.905 282.422 252.305 1.00 28.47  ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 219.536 283.650 253.000 1.00 17.79  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 218.532 284.463 252.191 1.00 25.54  ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 217.569 285.002 252.747 1.00 33.89  ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 220.783 284.480 253.300 1.00 13.53  ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 218.745 284.566 250.877 1.00 31.14  ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 217.777 285.251 250.026 1.00 24.12  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 216.448 284.507 249.998 1.00 27.01  ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 215.379 285.128 250.031 1.00 35.20  ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 218.336 285.408 248.613 1.00 23.84  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 217.363 285.951 247.564 1.00 28.23  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 216.981 287.389 247.875 1.00 29.59  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 217.959 285.842 246.173 1.00 29.56  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 216.495 283.175 249.930 1.00 32.28  ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 215.265 282.401 249.968 1.00 20.75  ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 214.534 282.536 251.288 1.00 25.97  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 213.308 282.668 251.320 1.00 43.57  ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 215.275 282.500 252.398 1.00 34.15  ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 214.662 282.736 253.700 1.00 24.30  ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 214.173 284.171 253.835 1.00 29.60  ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 213.202 284.429 254.555 1.00 46.86  ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 215.649 282.402 254.818 1.00 24.35  ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 216.135 280.986 254.794 1.00 38.10  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 215.480 279.986 254.108 1.00 42.84  ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 217.211 280.402 255.372 1.00 41.22  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 216.132 278.848 254.264 1.00 39.58  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 217.186 279.073 255.026 1.00 43.39  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 214.832 285.114 253.157 1.00 33.83  ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 214.385 286.502 253.193 1.00 31.64  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 213.020 286.667 252.538 1.00 35.33  ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 212.209 287.484 252.990 1.00 37.10  ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 215.416 287.400 252.511 1.00 30.54  ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 215.016 288.858 252.436 1.00 29.75  ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 215.051 289.542 253.787 1.00 48.46  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 216.095 290.028 254.222 1.00 48.61  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 213.906 289.586 254.458 1.00 44.82  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 212.747 285.905 251.483 1.00 33.68  ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 211.468 285.951 250.790 1.00 25.67  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 210.459 284.958 251.353 1.00 27.19  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 209.373 284.806 250.785 1.00 39.19  ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 211.669 285.693 249.294 1.00 32.36  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 212.715 286.556 248.585 1.00 27.00  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 212.772 286.220 247.105 1.00 25.86  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 212.422 288.032 248.789 1.00 22.62  ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 210.791 284.285 252.450 1.00 35.10  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 209.896 283.300 253.032 1.00 27.46  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 209.685 282.080 252.164 1.00 27.82  ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 208.570 281.545 252.112 1.00 37.97  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 210.729 281.623 251.484 1.00 33.11  ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 210.644 280.497 250.569 1.00 31.38  ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 211.209 279.236 251.211 1.00 36.31  ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 212.021 279.287 252.138 1.00 44.67  ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 211.397 280.799 249.270 1.00 17.48  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 210.845 281.974 248.482 1.00 26.03  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 209.610 281.579 247.690 1.00 36.17  ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 209.240 282.595 246.712 1.00 40.85  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 208.643 283.742 247.007 1.00 36.23  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 208.319 284.052 248.252 1.00 34.33  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 208.361 284.597 246.029 1.00 39.79  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 210.761 278.093 250.700 1.00 34.30  ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 211.289 276.795 251.101 1.00 31.93  ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 212.473 276.479 250.194 1.00 28.77  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 212.296 276.188 249.008 1.00 43.77  ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 210.205 275.723 251.007 1.00 34.66  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 210.623 274.374 251.532 1.00 34.67  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 211.722 274.240 252.364 1.00 39.66  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 209.905 273.239 251.195 1.00 31.40  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 212.100 273.000 252.843 1.00 40.16  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 210.277 271.998 251.673 1.00 25.79  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 211.375 271.878 252.498 1.00 34.48  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 213.680 276.549 250.745 1.00 22.37  ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 214.905 276.336 249.985 1.00 31.67  ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 215.432 274.945 250.305 1.00 38.08  ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 215.667 274.614 251.473 1.00 48.43  ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 215.956 277.412 250.300 1.00 26.78  ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 217.225 277.162 249.502 1.00 25.53  ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 215.400 278.792 250.005 1.00 26.48  ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 215.617 274.132 249.270 1.00 24.10  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 216.147 272.784 249.408 1.00 27.52  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 217.536 272.726 248.790 1.00 27.52  ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 217.727 273.136 247.641 1.00 37.27  ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 215.232 271.755 248.743 1.00 32.88  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 213.960 271.365 249.497 1.00 25.92  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 212.874 272.407 249.302 1.00 39.69  ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 213.477 269.998 249.056 1.00 29.32  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 218.496 272.216 249.553 1.00 29.78  ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 219.878 272.089 249.108 1.00 26.98  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 220.095 270.672 248.603 1.00 34.83  ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 219.811 269.700 249.313 1.00 44.64  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 220.859 272.428 250.243 1.00 31.79  ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 222.250 271.914 249.916 1.00 39.66  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 220.886 273.928 250.486 1.00 30.82  ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 220.588 270.552 247.373 1.00 19.24  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 220.919 269.266 246.772 1.00 26.45  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 222.412 269.236 246.485 1.00 33.26  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 222.918 270.074 245.731 1.00 47.62  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 220.122 269.033 245.486 1.00 27.31  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 218.633 269.126 245.666 1.00 33.86  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 217.912 268.047 246.146 1.00 33.77  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 217.955 270.293 245.354 1.00 36.63  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 216.543 268.128 246.309 1.00 28.18  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 216.586 270.380 245.517 1.00 29.43  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 215.880 269.296 245.996 1.00 29.14  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 223.114 268.275 247.081 1.00 40.45  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 224.532 268.079 246.803 1.00 30.14  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 224.656 267.194 245.571 1.00 40.16  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 224.450 265.978 245.644 1.00 48.46  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 225.241 267.463 248.006 1.00 36.92  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 226.750 267.569 247.909 1.00 39.19  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 227.286 268.090 246.932 1.00 42.08  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 227.443 267.075 248.928 1.00 48.69  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 224.994 267.802 244.439 1.00 43.40  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 224.963 267.122 243.154 1.00 40.16  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 226.255 266.357 242.901 1.00 41.86  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 227.345 266.815 243.252 1.00 47.66  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 224.726 268.132 242.031 1.00 37.28  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 223.052 268.807 241.974 1.00 47.75  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 226.120 265.183 242.287 1.00 50.56  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 227.256 264.388 241.842 1.00 46.44  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 226.894 263.777 240.492 1.00 48.40  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 225.862 264.103 239.898 1.00 51.04  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 227.638 263.331 242.888 1.00 46.75  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 226.620 262.216 242.993 1.00 54.51  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 225.411 262.515 243.070 1.00 61.47  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 227.029 261.036 243.004 1.00 54.17  ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 227.751 262.881 239.998 1.00 51.37  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 227.542 262.298 238.677 1.00 55.67  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 226.346 261.357 238.620 1.00 52.21  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 225.931 260.983 237.518 1.00 54.34  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 228.800 261.556 238.222 1.00 50.70  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 229.091 260.281 238.994 1.00 49.98  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 230.031 260.508 240.159 1.00 62.05  ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 230.467 261.661 240.359 1.00 59.63  ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 230.338 259.531 240.874 1.00 62.21  ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 225.783 260.967 239.765 1.00 47.37  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 224.636 260.068 239.776 1.00 42.39  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 223.309 260.792 239.589 1.00 48.93  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 222.272 260.128 239.487 1.00 52.82  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 224.601 259.270 241.083 1.00 43.39  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 224.444 260.166 242.189 1.00 47.80  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 225.888 258.478 241.255 1.00 47.36  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 223.312 262.125 239.544 1.00 48.52  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 222.099 262.901 239.285 1.00 46.74  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 221.851 262.908 237.779 1.00 49.19  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 222.203 263.844 237.057 1.00 53.67  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 222.232 264.316 239.835 1.00 46.46  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 221.947 264.430 241.306 1.00 50.83  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 222.810 263.881 242.238 1.00 49.98  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 220.823 265.101 241.757 1.00 48.97  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 222.553 263.990 243.592 1.00 45.22  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 220.561 265.214 243.109 1.00 50.42  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 221.428 264.659 244.028 1.00 46.30  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 221.229 261.835 237.299 1.00 49.01  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 220.984 261.676 235.872 1.00 46.16  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 219.742 262.470 235.467 1.00 48.59  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 219.207 263.275 236.234 1.00 53.67  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 220.868 260.195 235.514 1.00 44.26  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 219.944 259.436 236.446 1.00 55.79  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 219.196 260.081 237.206 1.00 62.65  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 219.966 258.188 236.415 1.00 56.40  ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 219.276 262.249 234.235 1.00 48.20  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 218.123 262.984 233.725 1.00 45.58  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 216.868 262.686 234.536 1.00 47.68  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 216.091 263.596 234.849 1.00 46.78  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 217.908 262.641 232.250 1.00 44.62  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 216.847 263.466 231.574 1.00 45.58  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 217.176 264.649 230.936 1.00 42.23  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 215.526 263.050 231.560 1.00 49.23  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 216.207 265.405 230.306 1.00 45.29  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 214.553 263.802 230.932 1.00 41.92  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 214.894 264.981 230.304 1.00 46.53  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 216.651 261.416 234.884 1.00 44.72  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 215.428 261.042 235.588 1.00 42.56  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 215.425 261.561 237.021 1.00 46.11  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 214.393 262.037 237.509 1.00 46.54  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 215.256 259.524 235.565 1.00 48.09  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 215.292 258.924 234.171 1.00 47.60  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 213.907 258.642 233.626 1.00 55.34  ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 213.096 257.978 234.272 1.00 55.09  ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 213.627 259.148 232.431 1.00 56.48  ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 216.562 261.470 237.715 1.00 44.83  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 216.628 261.958 239.089 1.00 38.43  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 216.433 263.467 239.151 1.00 43.48  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 215.709 263.972 240.016 1.00 53.35  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 217.959 261.564 239.727 1.00 38.73  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 217.076 264.204 238.243 1.00 39.84  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 216.927 265.655 238.228 1.00 31.81  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 215.512 266.060 237.833 1.00 36.12  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 214.962 267.024 238.377 1.00 35.62  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 217.953 266.277 237.281 1.00 39.36  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 219.394 266.120 237.745 1.00 45.54  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 219.895 267.321 238.992 1.00 62.27  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 219.013 268.775 238.441 1.00 37.51  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 214.912 265.340 236.883 1.00 44.35  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 213.550 265.652 236.481 1.00 36.39  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 212.540 265.408 237.585 1.00 43.35  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 211.616 266.203 237.778 1.00 47.46  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 212.696 264.305 238.320 1.00 41.31  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 211.802 264.032 239.441 1.00 32.75  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 211.963 265.079 240.535 1.00 36.83  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 210.986 265.456 241.194 1.00 44.61  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 212.062 262.630 239.991 1.00 40.14  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 211.104 262.209 241.091 1.00 41.95  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 211.368 260.782 241.538 1.00 39.03  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 210.650 260.454 242.763 1.00 40.41  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 211.111 260.685 243.985 1.00 47.07  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 212.293 261.245 244.183 1.00 45.44  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 210.368 260.346 245.033 1.00 49.74  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 213.191 265.555 240.747 1.00 36.45  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 213.419 266.631 241.708 1.00 36.43  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 212.720 267.905 241.251 1.00 32.73  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 212.091 268.608 242.053 1.00 41.81  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 214.930 266.848 241.915 1.00 28.83  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 215.501 265.763 242.829 1.00 28.60  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 215.202 268.225 242.496 1.00 25.45  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 217.003 265.822 242.981 1.00 25.13  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 212.810 268.218 239.955 1.00 35.09  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 212.116 269.388 239.424 1.00 19.74  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 210.607 269.253 239.576 1.00 25.11  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 209.915 270.238 239.861 1.00 31.19  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 212.482 269.598 237.955 1.00 29.77  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 213.895 270.058 237.738 1.00 28.27  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 214.541 270.829 238.687 1.00 34.73  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 214.572 269.728 236.576 1.00 35.33  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 215.839 271.256 238.486 1.00 32.95  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 215.869 270.152 236.369 1.00 37.78  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 216.502 270.919 237.325 1.00 33.19  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 210.077 268.043 239.382 1.00 41.03  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 208.639 267.824 239.528 1.00 32.31  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 208.199 268.139 240.952 1.00 35.41  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 207.173 268.793 241.175 1.00 39.31  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 208.273 266.384 239.127 1.00 30.56  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 206.881 266.027 239.623 1.00 34.86  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 208.363 266.215 237.619 1.00 40.77  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 208.972 267.680 241.937 1.00 29.96  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 208.666 268.015 243.318 1.00 28.30  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 208.776 269.502 243.594 1.00 38.65  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 207.944 270.074 244.302 1.00 51.29  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 209.804 270.148 243.040 1.00 36.06  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 209.967 271.585 243.235 1.00 21.16  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 208.865 272.369 242.531 1.00 31.77  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 208.409 273.400 243.040 1.00 38.17  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 211.343 272.029 242.741 1.00 30.38  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 212.548 271.522 243.536 1.00 28.49  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 213.847 271.972 242.889 1.00 29.71  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 212.476 271.985 244.982 1.00 34.43  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 208.435 271.905 241.354 1.00 35.65  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 207.357 272.583 240.639 1.00 30.62  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 206.066 272.579 241.447 1.00 43.54  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 205.404 273.614 241.581 1.00 48.24  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 207.123 271.918 239.281 1.00 33.12  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 208.352 272.273 238.007 1.00 50.41  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 205.693 271.421 241.995 1.00 43.77  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 204.408 271.303 242.675 1.00 36.24  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 204.443 271.944 244.058 1.00 40.72  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 203.468 272.579 244.476 1.00 43.86  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 204.009 269.832 242.768 1.00 42.13  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 203.810 269.164 241.418 1.00 40.54  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 203.600 267.668 241.532 1.00 52.39  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 203.577 267.115 242.631 1.00 58.38  ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 203.447 267.004 240.393 1.00 48.99  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 205.552 271.785 244.784 1.00 34.36  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 205.654 272.372 246.117 1.00 34.04  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 205.720 273.891 246.031 1.00 43.05  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 205.059 274.601 246.799 1.00 40.52  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 206.870 271.796 246.866 1.00 30.65  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 207.162 272.610 248.116 1.00 32.78  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 206.631 270.343 247.228 1.00 33.19  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 206.505 274.414 245.094 1.00 40.39  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 206.767 275.838 245.041 1.00 28.03  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 207.968 276.188 245.890 1.00 38.06  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 207.922 277.113 246.706 1.00 44.07  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 209.053 275.445 245.701 1.00 30.00  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 210.236 275.545 246.538 1.00 18.60  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 211.459 275.864 245.689 1.00 27.56  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 211.525 275.532 244.502 1.00 44.64  ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 210.465 274.246 247.320 1.00 20.49  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 212.431 276.517 246.317 1.00 23.84  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 213.675 276.858 245.644 1.00 24.80  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 214.623 275.667 245.645 1.00 18.51  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 214.759 274.962 246.649 1.00 27.99  ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 214.344 278.052 246.323 1.00 29.47  ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 213.690 279.363 246.025 1.00 30.77  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 212.413 279.563 245.592 1.00 38.39  ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 214.284 280.660 246.136 1.00 30.35  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 212.174 280.906 245.428 1.00 36.11  ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 213.308 281.601 245.755 1.00 33.29  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 215.548 281.118 246.520 1.00 30.06  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 213.555 282.970 245.749 1.00 30.52  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 215.791 282.478 246.511 1.00 28.07  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 214.800 283.388 246.129 1.00 32.03  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 215.279 275.446 244.510 1.00 27.65  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 216.246 274.373 244.402 1.00 33.27  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 217.666 274.883 244.286 1.00 27.79  ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 218.050 275.445 243.256 1.00 38.58  ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 218.456 274.695 245.339 1.00 20.42  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 219.849 275.135 245.370 1.00 27.11  ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 220.726 273.919 245.098 1.00 28.48  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 221.053 273.157 246.011 1.00 41.60  ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 220.183 275.785 246.708 1.00 30.26  ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 221.749 276.684 246.731 1.00 48.52  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 221.106 273.739 243.835 1.00 30.72  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 221.891 272.582 243.411 1.00 22.25  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 223.368 272.946 243.492 1.00 32.32  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 223.968 273.379 242.506 1.00 44.32  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 221.499 272.151 242.003 1.00 26.55  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 220.071 271.706 241.881 1.00 25.20  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 219.060 272.627 241.665 1.00 27.42  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 219.739 270.366 241.982 1.00 26.84  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 217.745 272.220 241.553 1.00 34.49  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 218.426 269.953 241.871 1.00 30.46  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 217.428 270.882 241.656 1.00 31.13  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 223.957 272.768 244.670 1.00 31.57  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 225.374 273.035 244.850 1.00 24.51  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 226.207 271.965 244.158 1.00 34.84  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 225.786 270.813 244.020 1.00 48.89  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 225.728 273.096 246.335 1.00 39.20  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 224.790 273.988 247.116 1.00 51.20  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 224.505 275.105 246.640 1.00 48.32  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 224.345 273.577 248.206 1.00 48.74  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 227.405 272.363 243.726 1.00 47.50  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 228.301 271.490 242.969 1.00 43.08  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 227.602 270.941 241.728 1.00 47.11  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 227.706 269.757 241.399 1.00 51.28  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 228.835 270.356 243.846 1.00 47.45  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 229.742 270.818 244.975 1.00 53.44  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 231.043 271.410 244.474 1.00 62.19  ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 231.532 270.967 243.414 1.00 61.41  ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 231.578 272.318 245.143 1.00 60.06  ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 226.874 271.820 241.034 1.00 46.56  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 226.117 271.402 239.858 1.00 37.90  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 227.030 270.930 238.736 1.00 35.49  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 226.641 270.065 237.943 1.00 43.05  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 225.232 272.550 239.372 1.00 36.82  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 224.168 272.127 238.401 1.00 46.06  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 223.196 271.212 238.772 1.00 40.45  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 224.138 272.645 237.117 1.00 43.13  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 222.215 270.823 237.880 1.00 37.25  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 223.160 272.259 236.221 1.00 37.88  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 222.197 271.347 236.603 1.00 40.01  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 228.242 271.480 238.650 1.00 37.55  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 229.172 271.097 237.595 1.00 32.28  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 229.754 269.704 237.792 1.00 35.57  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 230.433 269.206 236.888 1.00 45.53  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 230.299 272.125 237.492 1.00 34.57  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 230.900 272.468 238.838 1.00 42.26  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 230.465 271.963 239.873 1.00 47.77  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 231.906 273.334 238.833 1.00 38.74  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 229.513 269.066 238.939 1.00 44.40  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 229.977 267.699 239.145 1.00 47.51  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 229.158 266.677 238.368 1.00 49.71  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 229.537 265.501 238.338 1.00 50.36  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 229.974 267.359 240.637 1.00 34.24  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 231.071 268.072 241.416 1.00 39.29  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 231.078 267.700 242.892 1.00 38.61  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 231.440 266.306 243.117 1.00 45.32  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 230.650 265.412 243.694 1.00 46.05  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 229.448 265.739 244.140 1.00 46.30  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 231.079 264.161 243.835 1.00 35.73  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 228.055 267.088 237.748 1.00 41.57  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 227.334 266.212 236.838 1.00 32.47  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 228.156 265.967 235.577 1.00 45.80  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 229.067 266.726 235.237 1.00 53.65  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 225.983 266.815 236.452 1.00 32.83  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 224.762 266.557 237.335 1.00 35.79  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 224.873 267.320 238.633 1.00 45.20  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 223.486 266.935 236.599 1.00 36.55  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 227.823 264.886 234.880 1.00 45.85  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 228.447 264.610 233.596 1.00 48.85  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 228.029 265.659 232.571 1.00 53.49  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 226.942 266.238 232.651 1.00 56.25  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 228.070 263.213 233.107 1.00 49.10  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 228.870 262.095 233.754 1.00 51.00  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 228.127 260.774 233.762 1.00 63.36  ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 226.879 260.792 233.761 1.00 61.49  ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 228.792 259.717 233.769 1.00 62.64  ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 228.914 265.907 231.602 1.00 44.98  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 228.625 266.905 230.577 1.00 40.90  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 227.384 266.531 229.778 1.00 47.86  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 226.567 267.397 229.444 1.00 47.55  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 229.829 267.075 229.650 1.00 41.48  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 231.061 267.643 230.332 1.00 53.69  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 232.159 267.997 229.350 1.00 60.65  ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 231.957 267.799 228.133 1.00 58.24  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 233.225 268.474 229.794 1.00 58.12  ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 227.229 265.245 229.457 1.00 49.09  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 226.018 264.797 228.779 1.00 43.54  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 224.796 264.959 229.675 1.00 51.12  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 223.705 265.291 229.196 1.00 53.32  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 226.178 263.344 228.329 1.00 41.10  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 226.589 262.384 229.432 1.00 46.45  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 226.849 260.992 228.881 1.00 48.12  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 226.721 259.964 229.908 1.00 53.84  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 225.694 259.132 230.012 1.00 52.76  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 224.685 259.171 229.158 1.00 49.32  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 225.681 258.237 230.995 1.00 49.81  ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 224.957 264.723 230.980 1.00 49.62  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 223.852 264.929 231.911 1.00 41.92  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 223.509 266.407 232.048 1.00 43.85  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 222.329 266.769 232.127 1.00 48.55  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 224.193 264.327 233.273 1.00 41.77  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 224.344 262.813 233.274 1.00 51.65  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 222.835 261.944 232.797 1.00 60.76  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 223.204 261.493 231.105 1.00 44.05  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 224.524 267.275 232.085 1.00 30.31  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 224.264 268.709 232.156 1.00 29.23  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 223.532 269.196 230.913 1.00 40.44  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 222.615 270.021 231.006 1.00 51.76  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 225.573 269.476 232.342 1.00 30.93  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 226.300 269.297 233.676 1.00 33.84  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 227.779 269.616 233.528 1.00 29.67  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 225.668 270.164 234.750 1.00 40.16  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 223.929 268.703 229.738 1.00 40.03  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 223.241 269.076 228.507 1.00 34.63  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 221.795 268.597 228.515 1.00 39.37  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 220.885 269.340 228.130 1.00 47.13  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 223.987 268.510 227.299 1.00 34.45  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 223.236 268.678 226.110 1.00 42.05  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 221.563 267.359 228.958 1.00 35.44  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 220.207 266.819 228.981 1.00 34.67  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 219.329 267.564 229.979 1.00 47.62  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 218.146 267.809 229.715 1.00 46.65  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 220.245 265.327 229.305 1.00 36.98  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 219.890 267.929 231.135 1.00 42.54  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 219.123 268.640 232.152 1.00 31.85  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 218.692 270.013 231.648 1.00 33.63  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 217.630 270.520 232.034 1.00 41.66  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 219.946 268.729 233.454 1.00 35.90  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 219.443 269.846 234.357 1.00 39.24  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 219.911 267.397 234.189 1.00 39.83  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 219.482 270.622 230.758 1.00 42.14  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 219.162 271.958 230.261 1.00 36.68  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 217.798 271.992 229.582 1.00 38.90  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 217.129 273.032 229.572 1.00 49.26  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 220.250 272.430 229.297 1.00 28.28  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 220.185 271.723 228.071 1.00 34.83  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 217.371 270.868 229.003 1.00 44.90  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 216.047 270.808 228.393 1.00 42.38  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 214.953 270.953 229.444 1.00 39.04  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 213.947 271.638 229.222 1.00 45.89  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 215.885 269.500 227.619 1.00 48.47  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 214.592 269.406 226.827 1.00 55.91  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 214.521 268.156 225.972 1.00 60.92  ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 215.434 267.331 225.981 1.00 54.35  ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 213.432 268.010 225.226 1.00 58.23  ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 215.132 270.310 230.601 1.00 45.50  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 214.136 270.405 231.664 1.00 39.86  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 214.120 271.795 232.286 1.00 42.39  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 213.055 272.315 232.637 1.00 45.12  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 214.404 269.345 232.730 1.00 33.65  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 214.684 267.969 232.164 1.00 40.79  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 215.248 267.016 233.196 1.00 45.66  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 216.298 267.271 233.785 1.00 52.93  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 214.555 265.907 233.416 1.00 40.24  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 215.295 272.407 232.444 1.00 39.58  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 215.359 273.761 232.987 1.00 37.36  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 214.708 274.749 232.027 1.00 40.88  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 214.026 275.691 232.449 1.00 48.73  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 216.820 274.142 233.293 1.00 39.76  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 216.900 275.557 233.844 1.00 44.05  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 217.433 273.149 234.267 1.00 39.15  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 214.907 274.549 230.722 1.00 37.35  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 214.376 275.483 229.734 1.00 38.98  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 212.851 275.493 229.726 1.00 48.11  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 212.235 276.563 229.664 1.00 54.17  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 214.916 275.138 228.347 1.00 40.22  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 214.803 276.267 227.339 1.00 43.21  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 215.592 275.996 226.074 1.00 46.66  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 215.361 275.002 225.387 1.00 55.04  ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 216.531 276.881 225.761 1.00 48.41  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 212.221 274.316 229.785 1.00 40.66  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 210.763 274.271 229.730 1.00 42.88  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 210.135 274.762 231.028 1.00 50.80  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 209.035 275.325 231.007 1.00 56.59  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 210.282 272.856 229.407 1.00 47.00  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 210.948 271.558 230.465 1.00 65.51  ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 210.807 274.551 232.163 1.00 48.07  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 210.322 275.102 233.425 1.00 42.83  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 210.335 276.624 233.377 1.00 46.91  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 209.375 277.283 233.796 1.00 55.01  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 211.159 274.565 234.601 1.00 40.81  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 210.796 273.109 234.894 1.00 48.48  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 210.958 275.421 235.841 1.00 40.76  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 211.816 272.391 235.742 1.00 41.46  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 211.421 277.204 232.861 1.00 43.69  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 211.511 278.657 232.755 1.00 39.36  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 210.469 279.207 231.789 1.00 40.89  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 209.893 280.274 232.032 1.00 53.86  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 212.918 279.061 232.320 1.00 38.25  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 213.967 278.900 233.407 1.00 39.80  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 215.365 279.212 232.918 1.00 47.98  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 215.551 279.686 231.797 1.00 44.48  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 216.359 278.945 233.757 1.00 40.80  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 210.221 278.499 230.683 1.00 42.47  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 209.189 278.930 229.746 1.00 51.39  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 207.813 278.915 230.399 1.00 54.58  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 207.006 279.827 230.186 1.00 56.25  ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 209.204 278.042 228.502 1.00 54.18  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 210.378 278.298 227.572 1.00 57.55  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 210.572 277.186 226.560 1.00 64.30  ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 209.777 276.222 226.574 1.00 58.21  ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 211.519 277.275 225.751 1.00 61.15  ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 207.524 277.880 231.192 1.00 54.28  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 206.270 277.848 231.938 1.00 51.31  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 206.207 278.983 232.952 1.00 53.25  ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 205.156 279.606 233.135 1.00 62.72  ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 206.104 276.496 232.630 1.00 55.29  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 207.324 279.261 233.628 1.00 50.39  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 207.359 280.380 234.562 1.00 49.16  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 207.180 281.708 233.837 1.00 54.99  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 206.503 282.613 234.341 1.00 62.61  ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 208.672 280.368 235.346 1.00 47.60  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 208.751 279.394 236.522 1.00 48.07  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 210.166 279.330 237.073 1.00 47.55  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 207.765 279.786 237.611 1.00 48.15  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 207.785 281.846 232.655 1.00 57.19  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 207.683 283.096 231.909 1.00 53.87  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 206.251 283.369 231.465 1.00 62.20  ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 205.769 284.503 231.569 1.00 69.19  ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 208.622 283.064 230.703 1.00 53.87  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 209.212 284.416 230.343 1.00 64.01  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 210.479 284.262 229.522 1.00 66.34  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 211.599 283.799 230.333 1.00 59.30  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 212.310 282.710 230.076 1.00 59.04  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 212.043 281.940 229.035 1.00 61.74  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 213.315 282.387 230.885 1.00 57.49  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 205.553 282.345 230.967 1.00 78.75  ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 204.170 282.538 230.547 1.00 77.53  ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 203.231 282.722 231.732 1.00 75.93  ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 202.120 283.231 231.553 1.00 82.23  ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 203.703 281.363 229.683 1.00 76.27  ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 203.630 280.033 230.411 1.00 81.06  ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 203.227 278.892 229.498 1.00 82.31  ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 203.026 279.137 228.290 1.00 79.07  ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 203.109 277.749 229.988 1.00 80.06  ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 203.651 282.319 232.933 1.00 76.37  ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 202.850 282.583 234.123 1.00 80.84  ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 202.888 284.057 234.503 1.00 85.33  ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 201.963 284.552 235.156 1.00 84.92  ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 203.340 281.720 235.287 1.00 83.90  ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 202.550 281.899 236.546 1.00 86.06  ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 201.288 281.373 236.714 1.00 90.54  ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 202.842 282.551 237.695 1.00 85.15  ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 200.837 281.689 237.915 1.00 88.58  ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 201.761 282.405 238.530 1.00 89.25  ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 203.941 284.769 234.104 1.00 93.25  ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 204.096 286.182 234.421 1.00 89.45  ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 203.331 287.095 233.473 1.00 92.09  ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 203.296 288.308 233.706 1.00 92.77  ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 205.578 286.562 234.408 1.00 83.41  ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 206.013 286.875 233.097 1.00 86.11  ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 202.733 286.554 232.420 1.00 104.21 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 201.998 287.383 231.474 1.00 106.30 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 200.759 287.964 232.146 1.00 109.13 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 199.968 287.214 232.731 1.00 105.23 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 201.602 286.569 230.245 1.00 106.50 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 202.703 286.511 229.205 1.00 106.51 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 203.141 285.432 228.806 1.00 107.50 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 203.158 287.677 228.759 1.00 104.72 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 200.559 289.284 232.097 1.00 122.39 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 199.363 289.869 232.726 1.00 120.89 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 198.059 289.402 232.106 1.00 120.96 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 197.019 289.461 232.774 1.00 119.37 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 199.567 291.378 232.534 1.00 118.56 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 200.497 291.492 231.369 1.00 118.57 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 201.404 290.301 231.448 1.00 118.74 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 198.076 288.944 230.852 1.00 123.57 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 196.854 288.447 230.229 1.00 123.52 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 196.370 287.161 230.887 1.00 125.37 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 195.168 286.869 230.862 1.00 123.80 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 197.079 288.225 228.734 1.00 123.73 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 198.396 287.534 228.439 1.00 124.25 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 198.601 286.379 228.810 1.00 123.31 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 199.298 288.242 227.768 1.00 121.78 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 197.279 286.385 231.471 1.00 122.43 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 196.897 285.143 232.128 1.00 122.54 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 196.061 285.427 233.370 1.00 122.42 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 196.371 286.325 234.158 1.00 119.85 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 198.141 284.337 232.502 1.00 120.14 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 197.918 283.330 233.609 1.00 120.43 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 197.238 282.144 233.369 1.00 120.25 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 198.392 283.565 234.894 1.00 118.84 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 197.034 281.220 234.377 1.00 120.25 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 198.192 282.647 235.908 1.00 119.20 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 197.512 281.477 235.644 1.00 121.68 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 197.311 280.561 236.651 1.00 121.01 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 194.994 284.652 233.541 1.00 124.42 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 194.109 284.760 234.692 1.00 123.08 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 194.183 283.470 235.495 1.00 123.08 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 194.158 282.376 234.921 1.00 121.24 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 192.667 285.038 234.258 1.00 122.95 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 192.174 284.059 233.211 1.00 123.30 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 192.837 283.925 232.162 1.00 121.65 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 191.122 283.425 233.438 1.00 121.49 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 194.276 283.601 236.820 1.00 125.86 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 194.398 282.427 237.677 1.00 127.06 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 193.154 281.548 237.640 1.00 125.64 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 193.232 280.369 238.002 1.00 123.93 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 194.696 282.855 239.115 1.00 125.71 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 196.040 283.545 239.286 1.00 124.82 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 196.365 283.779 240.752 1.00 125.39 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 195.374 284.735 241.394 1.00 124.83 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 195.681 284.961 242.834 1.00 125.44 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 192.012 282.090 237.213 1.00 127.27 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 190.805 281.284 237.075 1.00 126.64 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 190.848 280.369 235.858 1.00 126.46 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 190.017 279.460 235.759 1.00 124.01 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 189.573 282.187 236.994 1.00 125.41 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 189.704 283.081 235.881 1.00 124.55 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 189.421 282.996 238.273 1.00 123.29 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 191.785 280.585 234.939 1.00 123.44 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 191.920 279.746 233.756 1.00 122.68 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 192.700 278.481 234.116 1.00 122.86 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 192.921 278.167 235.289 1.00 121.64 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 192.584 280.528 232.626 1.00 120.64 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 193.946 280.787 232.917 1.00 120.65 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 193.118 277.735 233.099 1.00 114.30 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 193.878 276.518 233.335 1.00 112.65 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 195.221 276.857 233.978 1.00 114.20 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 195.850 277.858 233.614 1.00 113.10 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 194.096 275.759 232.025 1.00 108.15 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 195.689 276.055 234.932 1.00 103.56 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 196.966 276.357 235.586 1.00 99.60  ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 198.142 276.113 234.653 1.00 99.22  ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 198.064 275.356 233.683 1.00 95.50  ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 197.001 275.403 236.786 1.00 97.95  ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 195.956 274.367 236.529 1.00 96.92  ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 195.134 274.753 235.338 1.00 99.52  ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 199.251 276.783 234.965 1.00 84.25  ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 200.453 276.667 234.150 1.00 80.82  ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 201.069 275.289 234.344 1.00 77.42  ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 201.318 274.855 235.477 1.00 77.76  ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 201.452 277.778 234.503 1.00 80.04  ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 200.820 279.153 234.279 1.00 83.55  ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 202.719 277.629 233.683 1.00 79.24  ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 200.406 279.408 232.848 1.00 82.85  ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 201.319 274.595 233.237 1.00 70.49  ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 201.895 273.260 233.258 1.00 68.95  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 203.088 273.203 232.317 1.00 68.90  ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 203.180 273.972 231.356 1.00 68.18  ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 200.868 272.190 232.853 1.00 74.31  ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 200.374 272.473 231.538 1.00 74.71  ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 199.705 272.161 233.833 1.00 69.70  ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 204.005 272.282 232.605 1.00 61.97  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 205.183 272.065 231.781 1.00 63.00  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 205.413 270.570 231.612 1.00 64.77  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 204.965 269.755 232.422 1.00 64.49  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 206.429 272.728 232.386 1.00 58.83  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 207.194 271.797 233.730 1.00 64.33  ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 206.120 270.219 230.541 1.00 68.09  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 206.397 268.826 230.210 1.00 65.60  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 207.647 268.383 230.962 1.00 65.07  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 208.757 268.827 230.654 1.00 65.55  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 206.563 268.658 228.701 1.00 67.16  ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 206.624 267.213 228.219 1.00 67.64  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 208.011 266.610 228.330 1.00 72.02  ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 209.000 267.368 228.246 1.00 75.09  ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 208.114 265.377 228.500 1.00 69.96  ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 207.464 267.511 231.952 1.00 51.15  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 208.566 266.950 232.724 1.00 49.97  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 208.389 265.442 232.793 1.00 54.42  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 207.404 264.958 233.362 1.00 54.02  ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 208.622 267.548 234.133 1.00 55.51  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 209.475 268.804 234.319 1.00 52.08  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 209.164 269.467 235.651 1.00 46.61  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 210.954 268.471 234.217 1.00 51.70  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 209.344 264.707 232.220 1.00 58.10  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 209.329 263.243 232.213 1.00 59.55  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 208.035 262.703 231.603 1.00 58.07  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 207.363 261.841 232.174 1.00 57.02  ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 209.548 262.685 233.622 1.00 60.68  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 210.856 263.081 234.310 1.00 57.43  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 210.961 262.426 235.678 1.00 55.81  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 212.051 262.715 233.445 1.00 53.21  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 207.691 263.227 230.424 1.00 61.82  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 206.514 262.791 229.667 1.00 63.48  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 205.232 262.934 230.486 1.00 63.95  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 204.345 262.080 230.437 1.00 68.39  ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 206.680 261.355 229.166 1.00 62.39  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 207.942 261.165 228.348 1.00 64.73  ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 208.805 260.360 228.697 1.00 67.74  ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 208.055 261.908 227.254 1.00 60.40  ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 205.132 264.024 231.243 1.00 58.06  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 203.949 264.285 232.048 1.00 58.81  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 203.713 265.786 232.118 1.00 64.20  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 204.630 266.589 231.931 1.00 70.16  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 204.083 263.700 233.459 1.00 61.99  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 203.523 262.295 233.608 1.00 65.83  ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 203.633 261.809 235.043 1.00 67.00  ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 202.916 260.484 235.235 1.00 67.13  ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 203.713 259.536 236.060 1.00 67.58  ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 202.464 266.154 232.393 1.00 64.76  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 202.080 267.551 232.562 1.00 62.81  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 202.128 267.881 234.049 1.00 64.28  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 201.293 267.406 234.826 1.00 69.95  ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 200.691 267.806 231.982 1.00 63.03  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 200.659 267.902 230.465 1.00 67.31  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 201.612 268.950 229.926 1.00 67.52  ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 201.493 270.134 230.239 1.00 64.67  ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 202.565 268.519 229.108 1.00 64.33  ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 203.102 268.695 234.445 1.00 59.85  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 203.348 269.022 235.845 1.00 61.43  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 203.038 270.495 236.062 1.00 58.94  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 203.557 271.358 235.343 1.00 62.28  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 204.796 268.700 236.251 1.00 60.18  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 205.073 269.184 237.665 1.00 58.88  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 205.060 267.207 236.129 1.00 62.47  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 202.192 270.780 237.049 1.00 58.08  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 201.884 272.160 237.396 1.00 57.59  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 203.119 272.850 237.962 1.00 60.24  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 203.853 272.280 238.773 1.00 64.47  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 200.739 272.206 238.408 1.00 54.38  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 200.367 273.605 238.871 1.00 61.24  ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 199.494 273.563 240.116 1.00 64.38  ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 200.089 272.656 241.182 1.00 65.71  ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 201.281 273.268 241.832 1.00 63.31  ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 203.345 274.087 237.531 1.00 61.27  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 204.504 274.870 237.943 1.00 53.41  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 204.015 275.978 238.864 1.00 55.73  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 203.241 276.849 238.449 1.00 65.99  ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 205.263 275.445 236.740 1.00 50.51  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 206.479 276.228 237.208 1.00 56.79  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 205.672 274.332 235.792 1.00 53.09  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 204.462 275.946 240.115 1.00 52.14  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 204.118 277.005 241.050 1.00 53.27  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 204.937 278.257 240.742 1.00 58.98  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 206.097 278.156 240.331 1.00 62.28  ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 204.370 276.549 242.487 1.00 56.66  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 204.130 277.595 243.412 1.00 61.95  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 204.364 279.451 240.926 1.00 53.56  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 205.120 280.684 240.653 1.00 53.89  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 206.311 280.900 241.572 1.00 56.89  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 207.189 281.703 241.231 1.00 56.34  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 204.071 281.787 240.843 1.00 55.85  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 203.049 281.182 241.748 1.00 56.10  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 202.987 279.734 241.366 1.00 50.79  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 206.375 280.219 242.713 1.00 50.01  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 207.434 280.435 243.689 1.00 45.47  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 208.671 279.583 243.437 1.00 52.64  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 209.629 279.669 244.210 1.00 52.81  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 206.908 280.165 245.102 1.00 49.74  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 205.776 281.095 245.489 1.00 59.19  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 205.373 281.925 244.647 1.00 56.10  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 205.288 280.997 246.635 1.00 56.89  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 208.676 278.766 242.387 1.00 51.05  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 209.830 277.923 242.109 1.00 42.95  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 211.012 278.756 241.627 1.00 40.34  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 210.845 279.759 240.929 1.00 44.04  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 209.486 276.865 241.062 1.00 34.74  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 210.630 275.903 240.786 1.00 45.33  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 210.235 274.592 239.625 1.00 79.72  ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 211.823 273.774 239.496 1.00 44.92  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 212.214 278.329 242.006 1.00 32.92  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 213.443 278.932 241.518 1.00 22.49  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 214.542 277.880 241.534 1.00 23.91  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 214.556 276.991 242.390 1.00 34.37  ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 213.850 280.147 242.357 1.00 27.05  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 215.460 277.986 240.578 1.00 25.19  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 216.579 277.060 240.447 1.00 26.84  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 217.868 277.854 240.600 1.00 28.56  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 218.103 278.814 239.856 1.00 31.91  ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 216.555 276.314 239.103 1.00 33.11  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 215.183 275.683 238.862 1.00 35.13  ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 217.645 275.255 239.062 1.00 26.64  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 215.056 274.997 237.520 1.00 26.00  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 218.697 277.455 241.560 1.00 27.88  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 219.999 278.067 241.788 1.00 18.58  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 221.066 276.984 241.769 1.00 26.58  ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 220.866 275.901 242.327 1.00 41.31  ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 220.038 278.825 243.118 1.00 27.18  ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 219.216 280.082 243.125 1.00 31.21  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 217.836 280.026 243.214 1.00 18.98  ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 219.826 281.321 243.037 1.00 35.70  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 217.082 281.183 243.219 1.00 28.98  ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 219.077 282.479 243.041 1.00 30.79  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 217.703 282.410 243.132 1.00 31.08  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 222.191 277.275 241.123 1.00 27.40  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 223.299 276.335 240.999 1.00 25.89  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 224.559 276.998 241.541 1.00 31.10  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 224.893 278.128 241.163 1.00 42.83  ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 223.481 275.865 239.546 1.00 27.77  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 223.640 277.055 238.597 1.00 31.06  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 222.300 275.009 239.116 1.00 28.46  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 224.072 276.665 237.202 1.00 33.88  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 225.245 276.303 242.444 1.00 35.53  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 226.487 276.789 243.029 1.00 36.84  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 227.649 275.934 242.540 1.00 38.47  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 227.613 274.705 242.638 1.00 46.01  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 226.412 276.754 244.557 1.00 47.12  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 225.442 277.706 245.012 1.00 37.86  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 227.762 277.077 245.171 1.00 43.76  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 228.680 276.590 242.010 1.00 33.32  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 229.731 275.871 241.307 1.00 32.01  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 231.098 276.436 241.658 1.00 34.11  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 231.237 277.616 241.990 1.00 41.13  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 229.530 275.945 239.791 1.00 36.36  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 228.298 275.228 239.287 1.00 45.73  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 228.185 275.318 237.498 1.00 49.37  ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 227.694 277.024 237.277 1.00 29.17  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 232.107 275.571 241.577 1.00 37.17  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 233.507 275.977 241.591 1.00 32.18  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 234.106 275.657 240.230 1.00 43.38  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 234.335 274.476 239.925 1.00 42.02  ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 234.279 275.260 242.698 1.00 31.32  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 233.684 275.495 244.069 1.00 36.08  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 233.281 274.555 244.751 1.00 37.23  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 233.625 276.756 244.481 1.00 40.52  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 234.366 276.655 239.380 1.00 43.99  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 234.756 276.343 237.992 1.00 46.51  ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 236.069 275.585 237.867 1.00 47.80  ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 236.116 274.537 237.210 1.00 40.88  ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 234.831 277.733 237.341 1.00 44.35  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 233.939 278.591 238.183 1.00 33.89  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 234.148 278.096 239.581 1.00 40.09  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 237.139 276.082 238.480 1.00 43.08  ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 238.458 275.526 238.273 1.00 42.62  ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 238.853 274.363 239.152 1.00 46.10  ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 239.995 273.901 239.064 1.00 49.82  ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 237.955 273.866 239.997 1.00 47.83  ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 238.311 272.784 240.899 1.00 40.38  ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 238.310 271.444 240.166 1.00 41.26  ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 237.690 271.279 239.112 1.00 45.41  ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 237.352 272.732 242.089 1.00 36.12  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 237.606 273.787 243.143 1.00 38.59  ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 238.471 274.847 242.902 1.00 39.25  ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 236.982 273.721 244.381 1.00 45.44  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 238.704 275.810 243.862 1.00 45.25  ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 237.209 274.680 245.347 1.00 45.58  ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 238.071 275.722 245.082 1.00 48.55  ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 238.301 276.680 246.041 1.00 51.24  ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 239.020 270.480 240.745 1.00 42.97  ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 239.124 269.153 240.161 1.00 41.23  ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 237.851 268.351 240.406 1.00 42.84  ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 237.140 268.556 241.393 1.00 49.19  ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 240.327 268.405 240.733 1.00 42.60  ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 237.572 267.424 239.491 1.00 43.23  ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 236.399 266.584 239.588 1.00 44.29  ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 235.121 267.192 239.056 1.00 51.93  ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 234.056 266.578 239.207 1.00 54.41  ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 235.183 268.369 238.443 1.00 44.85  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 234.007 269.036 237.909 1.00 40.80  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 234.057 269.053 236.386 1.00 45.62  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 235.132 269.025 235.781 1.00 44.86  ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 233.899 270.467 238.439 1.00 43.13  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 233.526 270.563 239.909 1.00 40.89  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 234.766 270.692 240.771 1.00 38.63  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 234.450 271.035 242.152 1.00 40.40  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 234.461 270.174 243.160 1.00 45.68  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 234.780 268.902 242.980 1.00 42.54  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 234.148 270.600 244.380 1.00 45.12  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 232.880 269.101 235.772 1.00 47.73  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 232.752 269.092 234.325 1.00 44.77  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 232.592 270.516 233.798 1.00 51.69  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 232.591 271.494 234.549 1.00 50.62  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 231.574 268.213 233.901 1.00 47.52  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 231.585 266.977 234.592 1.00 55.44  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 232.455 270.628 232.479 1.00 58.84  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 232.253 271.903 231.806 1.00 52.74  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 230.810 271.994 231.329 1.00 56.62  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 230.316 271.085 230.654 1.00 59.27  ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 233.214 272.060 230.626 1.00 50.97  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 234.573 272.582 231.048 1.00 58.54  ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 234.693 273.701 231.547 1.00 55.47  ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 235.606 271.772 230.850 1.00 56.66  ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 230.144 273.086 231.681 1.00 44.85  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 228.740 273.241 231.336 1.00 45.25  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 228.588 273.590 229.857 1.00 49.66  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 229.395 274.348 229.310 1.00 52.54  ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 228.086 274.324 232.193 1.00 40.76  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 227.701 273.953 233.626 1.00 43.24  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 228.930 273.798 234.504 1.00 40.58  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 226.753 274.993 234.201 1.00 42.24  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 227.573 273.053 229.186 1.00 45.30  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 227.293 273.478 227.812 1.00 40.25  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 226.823 274.922 227.771 1.00 48.19  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 226.287 275.456 228.745 1.00 51.60  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 226.188 272.518 227.357 1.00 34.80  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 225.586 271.994 228.618 1.00 40.80  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 226.693 271.956 229.622 1.00 44.00  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 227.041 275.559 226.618 1.00 43.83  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 226.681 276.966 226.469 1.00 43.15  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 225.175 277.172 226.568 1.00 46.52  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 224.714 278.175 227.125 1.00 54.93  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 227.213 277.505 225.142 1.00 54.21  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 228.709 277.746 225.170 1.00 61.86  ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 229.290 277.754 226.275 1.00 53.88  ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 229.303 277.926 224.086 1.00 62.20  ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 224.388 276.238 226.026 1.00 39.27  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 222.937 276.382 226.078 1.00 44.44  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 222.407 276.251 227.500 1.00 43.29  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 221.330 276.772 227.809 1.00 49.74  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 222.270 275.357 225.159 1.00 42.92  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 222.269 273.961 225.745 1.00 42.33  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 223.307 273.450 226.162 1.00 46.95  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 221.100 273.334 225.776 1.00 41.22  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 223.132 275.549 228.373 1.00 34.81  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 222.757 275.511 229.782 1.00 36.90  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 223.157 276.794 230.500 1.00 40.53  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 222.432 277.268 231.382 1.00 49.58  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 223.392 274.298 230.463 1.00 36.34  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 223.155 274.150 231.968 1.00 35.31  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 221.670 274.032 232.274 1.00 37.22  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 223.915 272.954 232.516 1.00 38.16  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 224.304 277.370 230.132 1.00 42.48  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 224.797 278.558 230.821 1.00 37.15  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 223.942 279.784 230.528 1.00 39.00  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 223.854 280.688 231.368 1.00 46.10  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 226.254 278.816 230.436 1.00 37.05  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 227.243 277.905 231.145 1.00 36.78  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 228.674 278.375 230.952 1.00 37.31  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 229.209 277.965 229.591 1.00 45.23  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 230.675 278.197 229.481 1.00 43.87  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 223.310 279.841 229.354 1.00 40.31  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 222.457 280.976 229.022 1.00 41.08  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 221.151 280.979 229.805 1.00 38.98  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 220.432 281.983 229.771 1.00 44.88  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 222.159 280.993 227.522 1.00 41.28  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 221.307 279.830 227.046 1.00 45.12  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 221.129 279.846 225.537 1.00 49.70  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 220.213 280.976 225.097 1.00 52.39  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 219.953 280.938 223.631 1.00 52.45  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 220.830 279.892 230.501 1.00 29.40  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 219.622 279.804 231.310 1.00 34.25  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 219.823 280.312 232.731 1.00 41.19  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 218.860 280.340 233.505 1.00 51.46  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 219.122 278.357 231.355 1.00 37.15  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 218.743 277.709 230.023 1.00 40.03  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 218.551 276.212 230.198 1.00 33.43  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 217.491 278.350 229.450 1.00 39.78  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 221.041 280.710 233.092 1.00 37.32  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 221.360 281.143 234.444 1.00 18.44  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 222.109 282.466 234.398 1.00 29.24  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 222.920 282.698 233.497 1.00 34.53  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 222.210 280.096 235.175 1.00 28.86  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 221.498 278.798 235.423 1.00 32.46  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 220.760 278.607 236.579 1.00 30.14  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 221.569 277.766 234.503 1.00 28.35  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 220.104 277.414 236.811 1.00 24.90  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 220.916 276.571 234.730 1.00 33.46  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 220.182 276.395 235.885 1.00 33.35  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 221.834 283.329 235.373 1.00 39.16  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 222.585 284.565 235.550 1.00 28.03  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 223.709 284.309 236.545 1.00 37.73  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 223.453 283.964 237.704 1.00 48.14  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 221.677 285.694 236.034 1.00 30.97  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 220.884 286.368 234.927 1.00 42.18  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 221.666 287.519 234.313 1.00 38.48  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 221.317 288.805 234.905 1.00 44.19  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 220.222 289.493 234.615 1.00 53.47  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 219.336 289.046 233.740 1.00 43.11  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 220.011 290.661 235.214 1.00 45.06  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 224.948 284.480 236.096 1.00 30.74  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 226.118 284.129 236.886 1.00 38.71  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 226.649 285.343 237.635 1.00 38.29  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 226.634 286.464 237.117 1.00 48.67  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 227.219 283.547 235.996 1.00 38.05  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 227.776 284.543 235.157 1.00 39.74  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 227.113 285.110 238.861 1.00 25.26  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 227.767 286.132 239.667 1.00 35.24  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 229.050 285.557 240.244 1.00 38.47  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 229.059 284.427 240.741 1.00 41.09  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 226.865 286.627 240.798 1.00 35.54  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 227.484 287.764 241.614 1.00 37.74  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 227.516 289.057 240.812 1.00 41.37  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 226.756 287.953 242.924 1.00 34.42  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 230.126 286.336 240.184 1.00 33.94  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 231.425 285.912 240.693 1.00 31.90  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 231.519 286.270 242.171 1.00 43.59  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 231.688 287.441 242.526 1.00 54.49  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 232.552 286.563 239.897 1.00 34.92  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 231.409 285.259 243.034 1.00 33.46  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 231.555 285.438 244.477 1.00 35.08  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 232.935 284.916 244.869 1.00 40.05  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 233.113 283.757 245.243 1.00 43.69  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 230.437 284.720 245.225 1.00 38.50  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 229.148 285.516 245.333 1.00 35.20  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 227.952 284.752 246.443 1.00 40.67  ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 228.019 285.874 247.836 1.00 38.07  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 233.928 285.799 244.773 1.00 36.78  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 235.323 285.427 244.983 1.00 39.16  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 235.900 285.983 246.279 1.00 44.71  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 236.574 285.258 247.016 1.00 50.43  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 236.173 285.895 243.796 1.00 39.21  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 235.781 287.220 243.418 1.00 42.50  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 235.989 284.961 242.613 1.00 45.75  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 235.653 287.258 246.574 1.00 44.31  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 236.214 287.896 247.761 1.00 49.09  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 235.097 288.322 248.702 1.00 50.31  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 234.506 289.397 248.517 1.00 50.21  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 237.071 289.103 247.369 1.00 47.99  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 238.363 288.747 246.654 1.00 48.34  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 239.083 289.996 246.174 1.00 54.33  ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 239.659 290.782 247.341 1.00 55.48  ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 240.466 291.947 246.884 1.00 48.07  ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 234.766 287.527 249.715 1.00 47.95  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 233.760 287.956 250.690 1.00 42.76  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 234.251 289.128 251.522 1.00 46.14  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 235.442 289.265 251.814 1.00 51.41  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 233.556 286.708 251.558 1.00 35.95  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 234.834 285.953 251.433 1.00 40.19  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 235.325 286.203 250.036 1.00 41.36  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 233.304 289.982 251.910 1.00 52.54  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 233.603 291.136 252.757 1.00 53.95  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 233.748 290.631 254.190 1.00 52.01  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 232.872 290.792 255.042 1.00 60.35  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 232.518 292.195 252.626 1.00 52.11  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 232.533 292.873 251.270 1.00 60.56  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 233.635 293.097 250.728 1.00 63.08  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 231.443 293.172 250.739 1.00 59.49  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 234.895 290.000 254.447 1.00 50.09  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 235.099 289.300 255.711 1.00 46.20  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 235.285 290.268 256.872 1.00 52.33  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 235.013 289.920 258.027 1.00 55.69  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 236.300 288.366 255.591 1.00 44.70  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 237.610 289.085 255.338 1.00 62.12  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 238.736 288.090 255.213 1.00 62.12  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 238.967 287.430 256.490 1.00 71.08  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 239.681 286.326 256.649 1.00 66.72  ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 240.272 285.731 255.625 1.00 50.48  ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 239.794 285.799 257.864 1.00 66.73  ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 235.768 291.480 256.593 1.00 51.47  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 235.960 292.457 257.660 1.00 43.75  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 234.631 292.830 258.305 1.00 46.08  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 234.524 292.914 259.533 1.00 47.22  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 236.669 293.698 257.116 1.00 54.04  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 236.340 294.979 257.864 1.00 50.03  ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 237.083 295.094 259.180 1.00 54.65  ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 238.306 294.971 259.229 1.00 53.54  ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 236.343 295.332 260.257 1.00 50.91  ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 233.600 293.046 257.486 1.00 45.35  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 232.292 293.398 258.027 1.00 38.19  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 231.643 292.206 258.720 1.00 40.56  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 230.907 292.377 259.699 1.00 41.53  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 231.393 293.934 256.913 1.00 39.72  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 229.993 294.388 257.331 1.00 47.06  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 230.078 295.651 258.171 1.00 45.04  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 229.114 294.610 256.114 1.00 43.19  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 231.903 290.992 258.229 1.00 39.85  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 231.335 289.797 258.851 1.00 27.74  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 231.839 289.653 260.281 1.00 37.71  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 231.066 289.382 261.207 1.00 50.71  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 231.660 288.547 258.014 1.00 34.96  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 231.053 288.661 256.616 1.00 30.35  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 231.162 287.292 258.712 1.00 39.28  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 231.490 287.565 255.670 1.00 31.04  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 233.145 289.835 260.482 1.00 34.47  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 233.714 289.718 261.821 1.00 27.55  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 233.186 290.810 262.743 1.00 31.38  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 232.893 290.558 263.917 1.00 43.54  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 235.240 289.763 261.748 1.00 38.36  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 233.062 292.034 262.228 1.00 42.87  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 232.647 293.155 263.066 1.00 34.92  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 231.205 292.991 263.532 1.00 38.59  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 230.890 293.223 264.705 1.00 47.14  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 232.833 294.469 262.302 1.00 40.56  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 232.620 295.730 263.131 1.00 46.49  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 231.168 296.159 263.198 1.00 57.30  ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 230.393 295.911 262.275 1.00 63.28  ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 230.793 296.808 264.294 1.00 49.67  ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 230.310 292.594 262.625 1.00 37.41  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 228.896 292.489 262.976 1.00 32.06  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 228.653 291.309 263.910 1.00 39.37  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 227.904 291.420 264.888 1.00 49.94  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 228.033 292.399 261.705 1.00 31.22  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 226.571 292.200 262.068 1.00 34.34  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 228.205 293.656 260.870 1.00 39.15  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 229.274 290.159 263.626 1.00 29.50  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 229.072 288.990 264.479 1.00 35.43  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 229.575 289.238 265.895 1.00 47.28  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 228.883 288.923 266.870 1.00 58.82  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 229.762 287.763 263.885 1.00 38.51  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 229.169 287.265 262.582 1.00 44.31  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 230.108 285.871 261.931 1.00 60.18  ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 229.676 284.599 263.115 1.00 46.80  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 230.774 289.807 266.030 1.00 43.17  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 231.300 290.097 267.360 1.00 36.32  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 230.461 291.149 268.072 1.00 36.50  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 230.284 291.077 269.293 1.00 47.68  ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 232.757 290.546 267.264 1.00 38.34  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 233.773 289.468 266.882 1.00 34.30  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 235.191 289.993 267.029 1.00 35.23  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 233.572 288.213 267.717 1.00 40.55  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 229.944 292.130 267.330 1.00 41.85  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 229.054 293.122 267.923 1.00 38.72  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 227.757 292.484 268.407 1.00 41.91  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 227.249 292.833 269.479 1.00 45.80  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 228.765 294.228 266.909 1.00 41.16  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 227.921 295.360 267.446 1.00 46.62  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 228.380 296.162 268.481 1.00 46.45  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 226.669 295.631 266.912 1.00 44.35  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 227.614 297.199 268.973 1.00 49.04  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 225.895 296.666 267.397 1.00 40.22  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 226.373 297.447 268.427 1.00 46.29  ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 225.607 298.480 268.915 1.00 50.39  ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 227.207 291.547 267.631 1.00 39.43  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 225.955 290.906 268.019 1.00 35.55  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 226.157 289.904 269.149 1.00 42.48  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 225.203 289.584 269.867 1.00 54.06  ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 225.318 290.220 266.811 1.00 39.88  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 226.166 289.211 266.290 1.00 41.11  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 227.377 289.395 269.320 1.00 50.17  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 227.655 288.436 270.382 1.00 48.14  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 227.942 289.095 271.724 1.00 54.00  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 228.032 288.388 272.733 1.00 58.48  ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 228.830 287.537 269.988 1.00 44.06  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 228.486 286.498 268.933 1.00 47.64  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 229.701 285.729 268.451 1.00 59.06  ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 230.830 286.015 268.851 1.00 59.51  ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 229.475 284.747 267.587 1.00 53.91  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 228.084 290.417 271.767 1.00 47.58  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 228.300 291.128 273.009 1.00 43.74  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 229.700 291.661 273.237 1.00 50.92  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 230.012 292.055 274.366 1.00 60.57  ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 230.551 291.686 272.214 1.00 47.49  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 231.907 292.192 272.370 1.00 47.02  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 231.911 293.715 272.301 1.00 54.82  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 231.379 294.304 271.356 1.00 53.89  ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 232.822 291.613 271.291 1.00 48.82  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 233.182 290.170 271.508 1.00 50.38  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 232.270 289.164 271.237 1.00 49.39  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 234.435 289.820 271.981 1.00 50.14  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 232.600 287.837 271.435 1.00 48.55  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 234.771 288.495 272.181 1.00 45.75  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 233.852 287.503 271.908 1.00 49.06  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 232.515 294.351 273.309 1.00 62.95  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 232.599 295.808 273.319 1.00 60.69  ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 233.628 296.326 272.324 1.00 66.58  ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 233.466 297.425 271.783 1.00 67.58  ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 232.929 296.309 274.725 1.00 64.02  ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 232.078 295.699 275.821 1.00 67.48  ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 230.655 296.227 275.749 1.00 67.87  ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 230.484 297.453 276.518 1.00 72.43  ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 230.332 297.499 277.835 1.00 71.07  ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 230.318 296.399 278.568 1.00 68.18  ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 230.189 298.680 278.430 1.00 67.23  ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 234.684 295.557 272.069 1.00 64.66  ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 235.755 295.950 271.156 1.00 58.84  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 235.637 295.245 269.813 1.00 60.71  ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 236.642 294.841 269.223 1.00 63.13  ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 237.117 295.676 271.787 1.00 59.72  ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 237.240 294.278 272.076 1.00 64.94  ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 237.275 296.468 273.076 1.00 60.15  ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 234.408 295.083 269.315 1.00 62.23  ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 234.194 294.342 268.075 1.00 56.78  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 234.909 294.997 266.901 1.00 60.85  ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 235.518 294.307 266.075 1.00 67.15  ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 232.697 294.221 267.790 1.00 48.57  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 234.844 296.327 266.804 1.00 64.34  ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 235.519 297.022 265.711 1.00 58.89  ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 237.029 296.831 265.788 1.00 61.70  ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 237.691 296.602 264.769 1.00 66.65  ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 235.161 298.509 265.735 1.00 65.05  ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 233.677 298.789 265.905 1.00 68.32  ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 233.328 299.240 267.310 1.00 69.03  ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 232.625 300.263 267.449 1.00 63.40  ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 233.756 298.572 268.274 1.00 66.62  ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 237.593 296.927 266.993 1.00 58.29  ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 239.030 296.734 267.159 1.00 56.82  ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 239.412 295.284 266.884 1.00 59.88  ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 240.401 295.010 266.194 1.00 62.91  ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 239.468 297.179 268.566 1.00 57.60  ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 240.946 296.893 268.780 1.00 56.51  ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 239.169 298.656 268.770 1.00 58.63  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 238.640 294.335 267.421 1.00 57.78  ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 238.953 292.924 267.220 1.00 51.94  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 238.821 292.526 265.755 1.00 50.47  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 239.650 291.770 265.234 1.00 59.26  ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 238.051 292.056 268.097 1.00 56.42  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 238.315 292.114 269.603 1.00 54.23  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 237.319 291.248 270.354 1.00 54.35  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 239.740 291.691 269.914 1.00 58.90  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 237.784 293.020 265.075 1.00 48.31  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 237.611 292.704 263.660 1.00 52.44  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 238.753 293.266 262.825 1.00 56.43  ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 239.220 292.615 261.884 1.00 58.36  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 236.270 293.237 263.159 1.00 51.60  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 239.216 294.473 263.154 1.00 62.11  ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 240.345 295.057 262.442 1.00 59.80  ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 241.655 294.349 262.760 1.00 60.31  ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 242.665 294.617 262.100 1.00 62.94  ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 240.462 296.545 262.774 1.00 57.66  ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 239.415 297.382 262.069 1.00 62.58  ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 239.417 297.497 260.843 1.00 65.09  ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 238.510 297.971 262.841 1.00 62.67  ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 241.666 293.467 263.757 1.00 59.28  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 242.858 292.712 264.118 1.00 57.04  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 242.819 291.263 263.654 1.00 58.73  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 243.848 290.738 263.218 1.00 65.68  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 243.065 292.741 265.636 1.00 56.09  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 243.801 293.968 266.142 1.00 55.83  ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 243.940 293.943 267.655 1.00 58.30  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 244.876 295.036 268.140 1.00 59.24  ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 246.180 295.002 267.424 1.00 63.83  ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 241.664 290.607 263.731 1.00 52.47  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 241.575 289.193 263.380 1.00 49.64  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 241.476 288.995 261.871 1.00 53.03  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 241.990 288.009 261.337 1.00 60.79  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 240.392 288.534 264.122 1.00 49.14  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 240.471 287.011 264.008 1.00 52.33  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 239.053 289.051 263.608 1.00 53.26  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 241.816 286.447 264.397 1.00 51.37  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 240.813 289.911 261.163 1.00 51.85  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 240.698 289.782 259.710 1.00 54.43  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 242.053 289.891 259.017 1.00 59.46  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 242.363 289.029 258.179 1.00 59.38  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 239.664 290.786 259.170 1.00 56.09  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 239.705 290.828 257.654 1.00 55.29  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 238.274 290.420 259.662 1.00 55.83  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 242.892 290.898 259.294 1.00 57.55  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 244.243 290.881 258.711 1.00 55.27  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 245.077 289.700 259.167 1.00 54.15  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 245.932 289.226 258.408 1.00 61.12  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 244.845 292.211 259.184 1.00 54.69  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 243.670 293.080 259.438 1.00 58.93  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 242.650 292.155 260.025 1.00 56.78  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 244.850 289.211 260.389 1.00 52.02  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 245.672 288.132 260.929 1.00 49.31  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 245.568 286.873 260.080 1.00 49.66  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 246.579 286.217 259.803 1.00 56.77  ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 245.267 287.842 262.375 1.00 48.36  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 245.824 286.558 262.915 1.00 50.50  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 247.155 286.466 263.281 1.00 59.35  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 245.015 285.444 263.065 1.00 51.21  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 247.672 285.286 263.780 1.00 54.99  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 245.525 284.261 263.564 1.00 51.05  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 246.855 284.182 263.922 1.00 55.33  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 244.353 286.518 259.657 1.00 52.35  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 244.188 285.358 258.789 1.00 51.48  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 244.842 285.589 257.433 1.00 54.26  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 245.447 284.673 256.864 1.00 64.04  ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 242.706 285.037 258.616 1.00 52.34  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 242.142 284.168 259.702 1.00 50.79  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 241.928 284.676 260.972 1.00 49.67  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 241.828 282.843 259.455 1.00 51.48  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 241.408 283.880 261.972 1.00 53.98  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 241.311 282.043 260.453 1.00 51.65  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 241.100 282.562 261.712 1.00 55.85  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 244.716 286.804 256.893 1.00 58.50  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 245.377 287.128 255.633 1.00 54.24  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 246.892 287.043 255.765 1.00 61.88  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 247.573 286.532 254.868 1.00 65.25  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 244.954 288.520 255.165 1.00 57.90  ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 245.534 288.927 253.824 1.00 61.89  ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 244.970 290.260 253.366 1.00 62.99  ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 245.615 290.709 252.068 1.00 64.55  ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 247.062 291.001 252.255 1.00 64.04  ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 247.439 287.542 256.877 1.00 61.91  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 248.875 287.421 257.108 1.00 53.95  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 249.289 285.962 257.248 1.00 57.09  ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 250.341 285.557 256.742 1.00 65.76  ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 249.280 288.219 258.348 1.00 60.78  ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 249.099 289.736 258.265 1.00 63.71  ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 249.107 290.350 259.653 1.00 62.37  ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 250.178 290.361 257.392 1.00 62.67  ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 248.474 285.157 257.935 1.00 58.66  ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 248.775 283.735 258.068 1.00 60.38  ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 248.762 283.037 256.714 1.00 56.96  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 249.604 282.174 256.443 1.00 58.38  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 247.778 283.073 259.018 1.00 58.70  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 248.011 283.493 260.755 1.00 74.02  ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 247.806 283.393 255.853 1.00 59.03  ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 247.736 282.779 254.532 1.00 61.88  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 248.969 283.111 253.701 1.00 66.28  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 249.477 282.259 252.962 1.00 66.89  ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 246.465 283.233 253.813 1.00 62.75  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 246.411 282.763 252.374 1.00 69.16  ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 246.385 281.535 252.149 1.00 68.90  ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 246.395 283.622 251.467 1.00 70.63  ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 249.465 284.342 253.809 1.00 70.60  ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 250.577 284.806 252.991 1.00 65.49  ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 251.944 284.535 253.607 1.00 67.94  ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 252.958 284.744 252.932 1.00 72.51  ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 250.432 286.307 252.720 1.00 66.13  ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 249.150 286.680 251.992 1.00 72.12  ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 248.931 288.179 251.927 1.00 75.13  ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 249.345 288.883 252.872 1.00 72.58  ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 248.344 288.653 250.932 1.00 72.94  ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 252.006 284.076 254.856 1.00 62.90  ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 253.274 283.829 255.534 1.00 59.26  ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 253.541 282.352 255.782 1.00 62.92  ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 254.667 281.887 255.582 1.00 70.14  ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 253.319 284.591 256.866 1.00 57.43  ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 254.574 284.333 257.685 1.00 63.43  ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 254.917 285.484 258.607 1.00 68.76  ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 254.981 286.636 258.182 1.00 65.59  ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 255.140 285.177 259.880 1.00 68.15  ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 252.533 281.601 256.218 1.00 63.93  ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 252.731 280.197 256.539 1.00 59.77  ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 253.048 279.393 255.281 1.00 61.93  ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 252.677 279.760 254.162 1.00 62.90  ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 251.495 279.626 257.233 1.00 54.75  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 251.132 280.268 258.573 1.00 55.44  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 250.002 279.515 259.245 1.00 56.39  ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 252.344 280.322 259.479 1.00 55.95  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 253.754 278.283 255.482 1.00 55.58  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 254.138 277.428 254.369 1.00 56.05  ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 252.905 276.819 253.711 1.00 50.54  ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 251.886 276.567 254.359 1.00 59.27  ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 255.080 276.322 254.847 1.00 56.33  ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 254.387 275.367 255.631 1.00 58.52  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 253.006 276.587 252.406 1.00 50.34  ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 251.890 276.057 251.630 1.00 54.00  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 251.751 274.566 251.912 1.00 57.94  ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 252.624 273.772 251.547 1.00 56.51  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 252.103 276.318 250.142 1.00 60.28  ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 251.096 275.695 249.365 1.00 63.52  ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 250.652 274.185 252.560 1.00 56.01  ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 250.357 272.793 252.860 1.00 46.84  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 248.975 272.445 252.327 1.00 53.90  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 248.096 273.304 252.224 1.00 58.15  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 250.426 272.508 254.368 1.00 42.05  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 251.668 273.058 255.048 1.00 49.98  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 252.887 272.184 254.829 1.00 51.81  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 252.776 271.046 254.374 1.00 57.57  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 254.061 272.713 255.154 1.00 50.82  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 248.795 271.167 251.985 1.00 51.40  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 247.544 270.722 251.382 1.00 47.15  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 246.370 270.781 252.350 1.00 44.70  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 245.219 270.816 251.903 1.00 47.96  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 247.701 269.299 250.845 1.00 47.71  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 248.102 268.408 251.870 1.00 55.63  ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 246.628 270.793 253.658 1.00 44.17  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 245.573 270.817 254.664 1.00 40.28  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 245.429 272.185 255.322 1.00 44.91  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 244.960 272.274 256.461 1.00 52.92  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 245.826 269.745 255.724 1.00 42.84  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 247.092 269.945 256.497 1.00 38.29  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 248.333 269.631 255.988 1.00 41.76  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 247.308 270.428 257.744 1.00 38.57  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 249.260 269.912 256.887 1.00 47.55  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 248.664 270.397 257.961 1.00 43.00  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 245.824 273.250 254.632 1.00 49.94  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 245.773 274.600 255.178 1.00 40.84  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 244.609 275.366 254.565 1.00 49.47  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 244.439 275.375 253.342 1.00 45.42  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 247.084 275.344 254.919 1.00 44.99  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 248.127 275.130 255.989 1.00 40.54  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 247.945 274.180 256.984 1.00 41.34  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 249.291 275.884 256.008 1.00 42.00  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 248.896 273.983 257.964 1.00 43.64  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 250.246 275.695 256.984 1.00 40.56  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 250.045 274.743 257.960 1.00 41.08  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 250.996 274.552 258.934 1.00 53.42  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 243.813 276.005 255.419 1.00 51.98  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 242.705 276.838 254.966 1.00 48.37  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 242.496 277.957 255.972 1.00 48.20  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 242.182 277.693 257.137 1.00 52.22  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 241.424 276.022 254.802 1.00 50.68  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 240.284 276.845 254.240 1.00 57.70  ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 240.342 277.205 253.046 1.00 55.89  ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 239.338 277.144 254.997 1.00 61.00  ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 242.668 279.196 255.524 1.00 47.73  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 242.463 280.379 256.349 1.00 45.17  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 241.443 281.309 255.706 1.00 53.64  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 241.563 282.534 255.763 1.00 65.39  ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 243.783 281.103 256.598 1.00 49.31  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 244.861 280.214 257.144 1.00 56.39  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 244.926 279.936 258.499 1.00 53.08  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 245.805 279.650 256.303 1.00 53.88  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 245.914 279.114 259.005 1.00 52.25  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 246.795 278.828 256.803 1.00 50.64  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 246.848 278.560 258.155 1.00 49.77  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 240.422 280.727 255.086 1.00 36.46  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 239.388 281.489 254.422 1.00 39.59  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 238.299 281.924 255.380 1.00 39.13  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 238.504 282.054 256.590 1.00 41.91  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 237.112 282.159 254.816 1.00 28.10  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 235.989 282.615 255.626 1.00 35.08  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 235.514 281.538 256.593 1.00 44.23  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 235.074 281.857 257.703 1.00 53.10  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 234.843 283.068 254.723 1.00 26.20  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 233.671 283.777 255.402 1.00 36.02  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 234.157 284.980 256.194 1.00 42.37  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 232.631 284.191 254.374 1.00 42.54  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 235.587 280.264 256.194 1.00 36.26  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 235.163 279.186 257.083 1.00 34.73  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 236.047 279.104 258.321 1.00 38.00  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 235.549 278.890 259.432 1.00 40.13  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 235.163 277.854 256.338 1.00 36.00  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 233.788 277.409 255.886 1.00 38.96  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 233.879 276.474 254.700 1.00 37.29  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 232.562 276.136 254.177 1.00 33.39  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 232.346 275.630 252.972 1.00 32.34  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 233.344 275.378 252.141 1.00 34.72  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 231.099 275.373 252.590 1.00 37.03  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 237.361 279.260 258.148 1.00 37.99  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 238.254 279.291 259.301 1.00 36.32  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 237.947 280.486 260.195 1.00 40.53  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 237.960 280.370 261.426 1.00 45.98  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 239.710 279.320 258.838 1.00 40.36  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 237.673 281.644 259.591 1.00 42.50  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 237.281 282.813 260.371 1.00 34.45  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 235.922 282.608 261.028 1.00 36.96  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 235.710 283.023 262.173 1.00 48.04  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 237.268 284.054 259.480 1.00 37.06  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 237.029 285.395 260.176 1.00 41.23  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 238.274 285.839 260.924 1.00 41.70  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 236.603 286.447 259.166 1.00 41.21  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 234.988 281.973 260.316 1.00 31.26  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 233.656 281.742 260.868 1.00 28.53  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 233.719 280.855 262.105 1.00 34.17  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 233.031 281.107 263.101 1.00 44.07  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 232.754 281.117 259.803 1.00 33.89  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 231.293 280.987 260.203 1.00 33.15  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 230.593 282.332 260.231 1.00 32.06  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 229.114 282.168 260.537 1.00 38.78  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 228.431 281.315 259.526 1.00 44.28  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 234.541 279.804 262.058 1.00 33.09  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 234.676 278.919 263.210 1.00 36.68  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 235.293 279.647 264.398 1.00 36.49  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 234.894 279.425 265.547 1.00 41.15  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 235.510 277.694 262.836 1.00 40.08  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 236.831 278.065 262.485 1.00 49.97  ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 236.276 280.513 264.141 1.00 32.14  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 236.907 281.267 265.220 1.00 34.65  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 235.907 282.219 265.866 1.00 40.30  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 235.830 282.320 267.097 1.00 50.78  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 238.146 282.015 264.694 1.00 37.77  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 238.604 283.061 265.697 1.00 33.21  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 239.267 281.034 264.394 1.00 42.04  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 235.127 282.931 265.049 1.00 40.21  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 234.144 283.864 265.592 1.00 35.15  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 233.061 283.137 266.380 1.00 36.31  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 232.633 283.613 267.438 1.00 45.09  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 233.524 284.691 264.466 1.00 36.47  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 234.483 285.579 263.672 1.00 32.34  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 233.820 286.071 262.397 1.00 30.17  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 234.964 286.746 264.519 1.00 40.06  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 232.599 281.991 265.876 1.00 36.07  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 231.608 281.205 266.606 1.00 40.06  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 232.188 280.715 267.926 1.00 40.59  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 231.527 280.767 268.971 1.00 43.27  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 231.104 280.038 265.736 1.00 40.20  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 230.339 279.032 266.580 1.00 41.55  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 230.229 280.561 264.608 1.00 35.23  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 233.434 280.235 267.902 1.00 38.11  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 234.084 279.799 269.133 1.00 30.69  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 234.281 280.963 270.096 1.00 39.43  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 234.195 280.789 271.316 1.00 48.41  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 235.423 279.135 268.812 1.00 36.69  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 235.261 278.086 267.875 1.00 49.33  ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 234.547 282.160 269.565 1.00 40.32  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 234.743 283.325 270.422 1.00 34.46  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 233.492 283.631 271.235 1.00 39.44  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 233.580 283.960 272.424 1.00 44.69  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 235.146 284.535 269.580 1.00 41.61  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 232.317 283.534 270.610 1.00 43.02  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 231.082 283.725 271.353 1.00 40.12  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 230.863 282.644 272.393 1.00 48.10  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 230.356 282.907 273.486 1.00 53.08  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 231.238 281.406 272.062 1.00 50.02  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 231.102 280.311 273.017 1.00 45.71  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 232.100 280.446 274.159 1.00 51.92  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 231.764 280.188 275.321 1.00 58.02  ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 231.278 278.970 272.304 1.00 45.14  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 230.109 278.632 271.402 1.00 52.00  ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 229.036 279.225 271.509 1.00 57.14  ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 230.311 277.675 270.504 1.00 45.65  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 233.336 280.843 273.849 1.00 50.53  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 234.346 281.012 274.889 1.00 45.70  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 233.977 282.167 275.811 1.00 51.27  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 234.156 282.087 277.032 1.00 61.89  ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 235.736 281.208 274.256 1.00 48.86  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 236.737 281.677 275.299 1.00 52.10  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 236.208 279.917 273.608 1.00 47.24  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 233.457 283.259 275.246 1.00 52.34  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 233.037 284.385 276.074 1.00 49.43  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 231.891 283.993 276.997 1.00 51.81  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 231.852 284.408 278.161 1.00 63.81  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 232.635 285.567 275.193 1.00 50.98  ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 232.478 286.874 275.954 1.00 54.32  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 232.087 288.011 275.029 1.00 53.73  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 230.610 287.953 274.682 1.00 54.25  ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 229.749 288.173 275.876 1.00 54.25  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 230.943 283.198 276.494 1.00 53.99  ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 229.814 282.783 277.321 1.00 57.44  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 230.263 281.898 278.476 1.00 59.08  ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 229.823 282.088 279.616 1.00 65.86  ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 228.774 282.058 276.469 1.00 57.96  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 227.753 282.976 275.823 1.00 58.36  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 226.566 282.187 275.296 1.00 62.51  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 226.837 281.599 273.990 1.00 65.13  ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 226.836 282.272 272.848 1.00 63.24  ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 226.576 283.569 272.810 1.00 63.29  ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 227.100 281.628 271.715 1.00 57.70  ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 231.139 280.927 278.207 1.00 61.26  ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 231.582 280.040 279.277 1.00 65.13  ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 232.461 280.782 280.275 1.00 68.82  ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 232.446 280.472 281.472 1.00 74.58  ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 232.315 278.825 278.703 1.00 63.41  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 233.625 279.133 278.000 1.00 70.47  ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 234.267 277.898 277.400 1.00 73.54  ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 233.676 276.804 277.514 1.00 73.33  ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 235.365 278.020 276.817 1.00 69.86  ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 233.234 281.762 279.806 1.00 65.05  ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 234.013 282.583 280.727 1.00 65.33  ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 233.105 283.446 281.593 1.00 70.79  ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 233.334 283.579 282.800 1.00 74.28  ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 235.007 283.445 279.949 1.00 64.40  ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 235.970 284.236 280.819 1.00 70.55  ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 236.940 285.057 279.974 1.00 78.74  ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 237.827 284.222 279.171 1.00 78.75  ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 238.961 283.693 279.610 1.00 74.34  ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 239.384 283.894 280.847 1.00 73.67  ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 239.688 282.942 278.787 1.00 68.88  ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 232.065 284.034 280.997 1.00 70.70  ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 231.113 284.825 281.772 1.00 67.54  ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 230.368 283.941 282.765 1.00 71.80  ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 230.181 284.315 283.930 1.00 77.69  ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 230.149 285.572 280.829 1.00 69.14  ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 230.853 286.771 280.191 1.00 69.54  ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 228.894 286.017 281.561 1.00 72.18  ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 229.994 287.525 279.192 1.00 69.59  ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 229.923 282.760 282.322 1.00 78.38  ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 229.303 281.812 283.244 1.00 77.08  ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 230.298 281.329 284.288 1.00 78.50  ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 229.928 281.098 285.444 1.00 83.42  ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 228.707 280.626 282.487 1.00 77.14  ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 227.547 280.986 281.568 1.00 80.82  ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 226.335 281.530 282.318 1.00 84.04  ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 226.020 282.721 282.257 1.00 83.75  ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 225.644 280.645 283.027 1.00 81.73  ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 231.564 281.167 283.904 1.00 81.03  ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 232.572 280.823 284.898 1.00 78.58  ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 232.734 281.924 285.940 1.00 79.95  ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 232.616 281.663 287.140 1.00 84.50  ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 233.911 280.540 284.226 1.00 83.35  ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 234.995 280.172 285.220 1.00 82.10  ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 236.345 280.291 284.582 1.00 83.93  ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 236.827 281.723 284.575 1.00 86.21  ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 236.930 282.312 285.938 1.00 81.89  ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 232.962 283.166 285.504 1.00 86.11  ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 233.279 284.241 286.445 1.00 85.38  ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 232.128 284.466 287.416 1.00 87.08  ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 232.341 284.773 288.595 1.00 91.38  ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 233.640 285.531 285.684 1.00 86.35  ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 234.901 285.324 284.840 1.00 88.35  ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 233.835 286.700 286.651 1.00 85.74  ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 235.162 286.458 283.868 1.00 90.40  ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 230.892 284.325 286.936 1.00 91.80  ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 229.730 284.438 287.812 1.00 91.33  ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 229.761 283.388 288.920 1.00 94.81  ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 229.243 283.618 290.019 1.00 99.33  ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 228.452 284.321 286.978 1.00 92.48  ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 227.155 284.522 287.745 1.00 94.77  ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 226.064 285.147 286.880 1.00 96.64  ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 225.903 284.426 285.552 1.00 96.10  ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 225.075 285.220 284.602 1.00 94.82  ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 230.343 282.217 288.640 1.00 97.38  ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 230.301 281.121 289.607 1.00 95.71  ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 231.260 281.334 290.781 1.00 97.76  ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 230.906 281.034 291.927 1.00 101.29 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 230.557 279.788 288.906 1.00 95.83  ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 229.404 279.410 287.970 1.00 96.46  ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 229.577 278.057 287.312 1.00 95.56  ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 230.659 278.029 286.338 1.00 99.07  ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 231.781 277.336 286.473 1.00 99.48  ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 232.030 276.621 287.559 1.00 97.77  ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 232.673 277.353 285.487 1.00 98.90  ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 232.483 281.826 290.531 1.00 101.36 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 233.325 282.200 291.670 1.00 101.84 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 232.700 283.334 292.472 1.00 103.05 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 232.733 283.315 293.707 1.00 105.14 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 234.762 282.575 291.263 1.00 101.74 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 235.677 281.461 290.719 1.00 101.74 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 235.504 281.165 289.264 1.00 104.29 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 234.718 281.857 288.609 1.00 106.07 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 236.142 280.223 288.762 1.00 104.84 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 232.109 284.321 291.795 1.00 103.65 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 231.555 285.465 292.512 1.00 103.98 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 230.432 285.049 293.454 1.00 106.01 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 230.319 285.582 294.565 1.00 108.95 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 231.055 286.520 291.527 1.00 104.43 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 232.132 287.419 290.942 1.00 103.99 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 231.483 288.514 290.109 1.00 104.79 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 232.434 289.662 289.818 1.00 104.06 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 233.674 289.204 289.145 1.00 105.28 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 229.582 284.113 293.031 1.00 104.41 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 228.513 283.657 293.912 1.00 105.57 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 229.046 282.729 294.998 1.00 107.93 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 228.497 282.684 296.105 1.00 106.56 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 227.401 282.992 293.095 1.00 105.76 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 227.821 281.759 292.306 1.00 106.60 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 227.764 280.483 293.119 1.00 108.32 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 227.063 280.465 294.153 1.00 107.81 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 228.434 279.503 292.729 1.00 108.50 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 230.110 281.976 294.703 1.00 108.30 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 230.742 281.158 295.734 1.00 106.75 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 231.584 281.999 296.689 1.00 107.03 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 231.510 281.817 297.909 1.00 107.41 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 231.601 280.066 295.093 1.00 106.06 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 230.852 278.776 294.797 1.00 106.31 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 231.628 277.845 293.883 1.00 107.58 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 232.498 277.107 294.391 1.00 107.38 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 231.368 277.848 292.662 1.00 107.58 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 232.386 282.925 296.158 1.00 112.20 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 233.239 283.758 296.999 1.00 113.13 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 232.457 284.824 297.755 1.00 113.28 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 232.877 285.219 298.849 1.00 113.21 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 234.337 284.398 296.139 1.00 112.25 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 235.086 285.560 296.773 1.00 112.55 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 236.310 285.924 295.950 1.00 113.80 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 236.083 287.089 295.103 1.00 115.69 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 236.169 287.074 293.780 1.00 115.08 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 236.476 285.970 293.120 1.00 113.70 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 235.940 288.195 293.102 1.00 111.77 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 231.320 285.266 297.226 1.00 117.58 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 230.513 286.268 297.892 1.00 117.16 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 229.138 286.403 297.275 1.00 119.47 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 228.522 285.403 296.896 1.00 118.28 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 228.644 287.637 297.163 1.00 127.39 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 227.335 287.910 296.562 1.00 126.92 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 227.481 289.167 295.707 1.00 125.42 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 227.332 290.288 296.199 1.00 125.66 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 226.257 288.070 297.627 1.00 126.14 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 225.839 286.767 298.293 1.00 126.30 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 224.824 286.977 299.400 1.00 127.25 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 223.700 287.430 299.099 1.00 127.21 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 225.150 286.689 300.570 1.00 126.41 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 227.772 288.969 294.423 1.00 118.04 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 227.948 290.083 293.495 1.00 118.92 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 227.667 289.578 292.087 1.00 121.19 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 228.501 288.883 291.500 1.00 120.43 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 229.353 290.669 293.597 1.00 118.78 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 226.502 289.922 291.552 1.00 118.96 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 226.108 289.539 290.197 1.00 117.50 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 225.761 290.829 289.463 1.00 116.81 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 224.626 291.311 289.511 1.00 116.85 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 224.937 288.552 290.183 1.00 115.18 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 224.634 288.112 288.758 1.00 115.50 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 225.243 287.348 291.062 1.00 113.61 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 226.747 291.400 288.774 1.00 116.48 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 226.559 292.611 287.980 1.00 116.79 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 227.118 292.354 286.589 1.00 118.15 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 228.320 292.110 286.434 1.00 118.94 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 227.240 293.815 288.632 1.00 115.67 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 227.083 295.084 287.818 1.00 116.89 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 225.936 295.424 287.460 1.00 116.93 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 228.106 295.744 287.537 1.00 115.84 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 226.248 292.407 285.578 1.00 107.75 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 226.683 292.125 284.214 1.00 105.74 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 227.597 293.222 283.685 1.00 107.73 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 228.504 292.950 282.889 1.00 108.44 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 225.467 291.950 283.304 1.00 104.49 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 224.489 290.883 283.773 1.00 106.18 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 224.996 289.472 283.539 1.00 108.16 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 226.033 289.309 282.862 1.00 108.27 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 224.357 288.523 284.039 1.00 107.76 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 227.371 294.467 284.108 1.00 113.01 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 228.202 295.561 283.630 1.00 112.87 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 229.646 295.437 284.074 1.00 112.99 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 230.571 295.629 283.282 1.00 112.28 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 229.859 295.112 285.352 1.00 118.35 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 231.220 294.980 285.864 1.00 118.93 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 231.949 293.816 285.205 1.00 118.25 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 233.142 293.916 284.894 1.00 116.53 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 231.196 294.808 287.383 1.00 118.44 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 232.558 294.941 288.044 1.00 118.85 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 232.505 294.699 289.540 1.00 120.74 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 231.422 294.340 290.047 1.00 120.36 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 233.546 294.870 290.208 1.00 120.24 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 231.250 292.699 284.991 1.00 109.86 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 231.869 291.542 284.349 1.00 110.12 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 232.256 291.872 282.913 1.00 109.04 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 233.350 291.524 282.453 1.00 108.15 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 230.925 290.327 284.418 1.00 107.96 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 230.728 289.887 285.870 1.00 108.49 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 231.468 289.178 283.583 1.00 106.59 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 229.682 288.808 286.042 1.00 108.04 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 231.366 292.551 282.185 1.00 110.04 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 231.636 292.870 280.786 1.00 109.63 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 232.817 293.823 280.645 1.00 109.64 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 233.646 293.660 279.742 1.00 109.22 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 230.387 293.460 280.133 1.00 106.54 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 232.908 294.829 281.519 1.00 104.97 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 234.005 295.788 281.432 1.00 104.90 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 235.348 295.117 281.696 1.00 104.81 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 236.318 295.330 280.960 1.00 102.58 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 233.777 296.941 282.411 1.00 105.18 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 232.559 297.796 282.099 1.00 104.00 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 232.778 298.715 280.913 1.00 105.96 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 233.947 298.932 280.533 1.00 105.41 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 231.778 299.222 280.362 1.00 104.48 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 235.423 294.301 282.742 1.00 107.07 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 236.654 293.588 283.082 1.00 108.17 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 236.647 292.189 282.469 1.00 106.79 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 236.782 291.172 283.149 1.00 105.97 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 236.830 293.532 284.597 1.00 108.37 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 236.765 294.902 285.241 1.00 108.37 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 235.791 295.635 285.072 1.00 110.45 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 237.807 295.256 285.984 1.00 106.40 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 236.487 292.156 281.149 1.00 93.17  ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 236.469 290.914 280.389 1.00 91.11  ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 237.554 290.965 279.324 1.00 90.41  ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 237.489 291.818 278.423 1.00 92.40  ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 235.101 290.685 279.745 1.00 91.78  ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 234.776 289.245 279.342 1.00 91.08  ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 235.102 288.279 280.471 1.00 88.64  ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 233.321 289.125 278.927 1.00 89.90  ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 238.558 290.092 279.374 1.00 80.89  ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 239.613 290.100 278.340 1.00 78.73  ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 239.117 289.528 277.014 1.00 79.15  ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 239.345 288.374 276.652 1.00 81.60  ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 240.708 289.238 278.973 1.00 79.09  ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 239.970 288.293 279.858 1.00 78.66  ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 238.771 289.038 280.381 1.00 79.55  ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 238.400 290.371 276.265 1.00 72.31  ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 237.873 289.950 274.971 1.00 68.66  ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 238.998 289.619 274.000 1.00 67.97  ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 238.845 288.754 273.130 1.00 71.76  ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 236.972 291.040 274.391 1.00 68.55  ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 235.748 291.353 275.232 1.00 71.96  ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 234.955 292.522 274.685 1.00 73.44  ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 235.415 293.147 273.707 1.00 72.04  ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 233.871 292.814 275.232 1.00 74.41  ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 240.137 290.301 274.132 1.00 66.67  ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 241.263 290.033 273.245 1.00 68.54  ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 241.922 288.701 273.587 1.00 69.57  ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 242.462 288.022 272.706 1.00 70.11  ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 242.261 291.188 273.319 1.00 71.19  ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 243.441 291.081 272.373 1.00 75.37  ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 244.354 292.289 272.458 1.00 75.60  ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 244.125 293.198 273.256 1.00 71.58  ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 245.394 292.306 271.636 1.00 76.85  ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 241.888 288.310 274.865 1.00 67.91  ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 242.341 286.974 275.241 1.00 62.87  ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 241.384 285.906 274.726 1.00 63.88  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 241.811 284.813 274.338 1.00 65.57  ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 242.486 286.868 276.759 1.00 68.60  ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 243.604 287.707 277.352 1.00 72.72  ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 243.769 287.484 278.843 1.00 74.68  ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 242.963 286.728 279.424 1.00 76.29  ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 244.705 288.065 279.432 1.00 69.61  ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 240.083 286.204 274.729 1.00 59.16  ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 239.085 285.242 274.269 1.00 55.76  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 239.286 284.924 272.793 1.00 56.15  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 239.207 283.762 272.375 1.00 60.77  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 237.667 285.777 274.547 1.00 58.19  ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 237.381 285.769 276.050 1.00 55.86  ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 236.625 284.971 273.788 1.00 59.92  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 236.131 286.523 276.438 1.00 56.18  ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 239.551 285.951 271.981 1.00 57.67  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 239.723 285.740 270.547 1.00 55.78  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 240.939 284.868 270.256 1.00 53.36  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 240.899 284.014 269.363 1.00 64.28  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 239.842 287.086 269.834 1.00 54.53  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 239.597 287.081 268.326 1.00 55.57  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 238.154 286.716 268.020 1.00 55.97  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 239.945 288.435 267.736 1.00 57.79  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 242.031 285.074 270.994 1.00 53.42  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 243.230 284.267 270.789 1.00 54.42  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 242.972 282.815 271.176 1.00 55.33  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 243.470 281.888 270.526 1.00 61.61  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 244.413 284.869 271.569 1.00 56.72  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 244.965 286.090 270.832 1.00 58.67  ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 245.514 283.840 271.773 1.00 51.96  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 246.090 286.782 271.561 1.00 64.04  ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 242.183 282.593 272.230 1.00 54.66  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 241.866 281.230 272.646 1.00 55.75  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 241.136 280.477 271.542 1.00 55.99  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 241.424 279.304 271.278 1.00 63.45  ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 241.031 281.251 273.927 1.00 58.19  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 240.720 279.870 274.481 1.00 57.28  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 239.704 279.902 275.603 1.00 62.53  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 239.796 280.723 276.515 1.00 61.84  ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 238.736 278.995 275.551 1.00 65.14  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 240.182 281.139 270.885 1.00 47.82  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 239.482 280.511 269.769 1.00 43.94  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 240.425 280.260 268.599 1.00 48.55  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 240.326 279.230 267.922 1.00 56.95  ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 238.306 281.383 269.335 1.00 45.68  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 237.519 281.755 270.451 1.00 54.16  ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 241.339 281.197 268.339 1.00 48.99  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 242.296 281.027 267.248 1.00 45.59  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 243.215 279.845 267.528 1.00 46.63  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 243.467 279.008 266.653 1.00 51.18  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 243.094 282.325 267.030 1.00 40.65  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 244.352 282.052 266.218 1.00 46.43  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 242.230 283.370 266.348 1.00 42.84  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 243.726 279.756 268.758 1.00 53.30  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 244.641 278.674 269.107 1.00 56.28  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 243.932 277.325 269.094 1.00 57.71  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 244.503 276.313 268.672 1.00 64.05  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 245.271 278.942 270.474 1.00 56.42  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 246.474 280.291 270.486 1.00 69.98  ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 242.682 277.289 269.559 1.00 49.23  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 241.957 276.025 269.624 1.00 48.74  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 241.556 275.525 268.241 1.00 50.24  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 241.206 274.350 268.086 1.00 57.42  ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 240.721 276.174 270.512 1.00 47.55  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 241.023 276.185 272.001 1.00 55.04  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 239.797 276.483 272.841 1.00 60.42  ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 238.691 276.578 272.269 1.00 63.41  ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 239.939 276.622 274.075 1.00 54.17  ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 241.593 276.393 267.230 1.00 49.45  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 241.109 276.022 265.905 1.00 44.71  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 242.214 275.958 264.857 1.00 47.01  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 242.147 275.119 263.951 1.00 55.28  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 240.028 277.007 265.449 1.00 48.99  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 239.112 277.242 266.526 1.00 42.55  ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 239.255 276.443 264.269 1.00 51.02  ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 243.231 276.814 264.956 1.00 45.75  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 244.291 276.894 263.955 1.00 52.50  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 245.546 276.118 264.334 1.00 56.28  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 246.210 275.564 263.453 1.00 61.97  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 244.665 278.358 263.698 1.00 53.08  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 243.567 279.206 263.067 1.00 52.78  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 243.058 278.630 261.434 1.00 77.13  ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 241.521 277.795 261.810 1.00 60.18  ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 245.892 276.076 265.624 1.00 44.13  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 247.130 275.404 266.038 1.00 44.46  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 247.145 273.924 265.683 1.00 49.51  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 248.176 273.444 265.188 1.00 51.67  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 247.403 275.670 267.525 1.00 52.90  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 248.572 274.828 268.014 1.00 50.29  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 247.678 277.147 267.752 1.00 47.16  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 246.081 273.138 265.906 1.00 44.11  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 246.172 271.700 265.594 1.00 41.14  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 246.528 271.396 264.148 1.00 45.67  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 247.183 270.379 263.886 1.00 57.63  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 244.772 271.180 265.947 1.00 43.23  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 244.293 272.101 266.994 1.00 37.92  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 244.823 273.451 266.612 1.00 40.22  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 246.121 272.240 263.200 1.00 39.08  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 246.434 271.995 261.798 1.00 33.91  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 247.862 272.379 261.432 1.00 40.11  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 248.343 271.975 260.368 1.00 45.60  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 245.456 272.757 260.899 1.00 38.73  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 245.945 274.133 260.476 1.00 40.93  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 245.086 274.715 259.367 1.00 42.82  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 243.805 275.315 259.918 1.00 44.13  ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 243.122 276.176 258.915 1.00 48.68  ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 248.548 273.136 262.285 1.00 49.03  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 249.861 273.659 261.935 1.00 42.20  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 250.924 272.569 261.979 1.00 40.63  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 250.911 271.698 262.853 1.00 45.53  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 250.250 274.793 262.882 1.00 38.57  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 249.404 276.064 262.825 1.00 37.48  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 249.952 277.098 263.792 1.00 50.08  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 249.358 276.614 261.411 1.00 34.77  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 251.852 272.628 261.026 1.00 46.75  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 253.033 271.772 261.031 1.00 48.45  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 254.023 272.334 262.041 1.00 48.86  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 253.841 273.445 262.550 1.00 51.73  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 253.661 271.662 259.630 1.00 45.78  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 252.664 271.071 258.646 1.00 42.93  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 254.142 273.020 259.157 1.00 51.99  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 255.074 271.567 262.342 1.00 59.06  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 256.008 271.962 263.394 1.00 61.75  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 256.686 273.290 263.078 1.00 63.73  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 256.858 274.133 263.966 1.00 59.80  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 257.051 270.866 263.605 1.00 60.41  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 257.079 273.498 261.820 1.00 65.05  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 257.792 274.716 261.455 1.00 63.79  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 256.890 275.942 261.394 1.00 63.60  ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 257.393 277.066 261.490 1.00 62.54  ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 258.494 274.534 260.107 1.00 62.70  ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 257.550 274.345 258.933 1.00 64.55  ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 258.283 274.104 257.628 1.00 74.50  ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 259.531 274.061 257.645 1.00 77.10  ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 257.611 273.957 256.586 1.00 71.18  ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 255.580 275.758 261.238 1.00 60.87  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 254.659 276.880 261.112 1.00 53.11  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 254.094 277.354 262.444 1.00 51.95  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 253.473 278.421 262.487 1.00 57.20  ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 253.506 276.513 260.172 1.00 48.07  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 253.923 276.511 258.715 1.00 58.98  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 254.970 277.110 258.395 1.00 60.14  ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 253.206 275.908 257.891 1.00 59.67  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 254.279 276.591 263.524 1.00 53.94  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 253.807 277.039 264.835 1.00 57.62  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 254.503 278.317 265.291 1.00 62.38  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 253.808 279.244 265.740 1.00 65.74  ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 253.926 275.897 265.861 1.00 57.00  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 253.122 274.681 265.403 1.00 56.78  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 253.457 276.360 267.232 1.00 57.49  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 253.284 273.472 266.295 1.00 58.80  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 255.838 278.441 265.226 1.00 65.28  ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 256.453 279.721 265.622 1.00 64.72  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 255.996 280.900 264.780 1.00 64.71  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 255.882 282.017 265.299 1.00 67.49  ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 257.956 279.453 265.455 1.00 65.76  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 258.092 277.981 265.561 1.00 65.70  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 256.864 277.428 264.914 1.00 63.85  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 255.738 280.683 263.489 1.00 59.52  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 255.329 281.782 262.619 1.00 59.87  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 253.972 282.339 263.033 1.00 66.57  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 253.780 283.559 263.094 1.00 75.48  ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 255.297 281.315 261.164 1.00 62.57  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 256.578 280.718 260.579 1.00 63.46  ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 256.468 280.607 259.066 1.00 61.48  ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 257.786 281.548 260.967 1.00 65.65  ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 253.012 281.455 263.318 1.00 56.89  ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 251.686 281.914 263.723 1.00 61.56  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 251.722 282.560 265.103 1.00 62.23  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 251.041 283.565 265.340 1.00 64.84  ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 250.693 280.752 263.692 1.00 59.36  ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 249.216 281.090 263.921 1.00 59.62  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 248.331 280.265 263.003 1.00 59.85  ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 248.822 280.864 265.373 1.00 60.09  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 252.503 281.996 266.026 1.00 57.21  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 252.615 282.588 267.355 1.00 58.77  ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 253.292 283.951 267.296 1.00 64.73  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 252.920 284.867 268.039 1.00 69.53  ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 253.371 281.645 268.290 1.00 61.26  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 252.480 280.697 269.040 1.00 65.98  ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 252.038 279.525 268.448 1.00 65.55  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 252.079 280.980 270.334 1.00 66.03  ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 251.216 278.653 269.135 1.00 64.16  ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 251.257 280.111 271.026 1.00 64.25  ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 250.825 278.946 270.425 1.00 65.06  ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 254.291 284.103 266.424 1.00 66.52  ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 254.884 285.418 266.208 1.00 65.31  ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 253.871 286.380 265.601 1.00 66.13  ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 253.835 287.563 265.957 1.00 72.29  ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 256.117 285.299 265.312 1.00 63.41  ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 257.160 284.602 265.971 1.00 68.29  ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 253.043 285.888 264.675 1.00 58.27  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 251.992 286.722 264.100 1.00 58.69  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 250.978 287.139 265.158 1.00 61.67  ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 250.525 288.289 265.174 1.00 67.36  ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 251.301 285.978 262.958 1.00 60.57  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 252.005 286.010 261.600 1.00 65.72  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 251.148 285.341 260.539 1.00 68.21  ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 252.334 287.439 261.202 1.00 68.07  ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 250.607 286.215 266.048 1.00 62.63  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 249.663 286.547 267.110 1.00 61.43  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 250.237 287.596 268.053 1.00 61.54  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 249.525 288.510 268.485 1.00 66.94  ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 249.279 285.287 267.886 1.00 60.03  ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 248.098 284.475 267.350 1.00 62.07  ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 247.901 283.215 268.176 1.00 62.49  ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 246.832 285.316 267.343 1.00 55.41  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 251.523 287.477 268.390 1.00 65.70  ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 252.148 288.448 269.282 1.00 66.45  ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 252.203 289.832 268.648 1.00 66.01  ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 251.993 290.841 269.331 1.00 68.36  ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 253.549 287.977 269.671 1.00 67.11  ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 253.503 286.704 270.292 1.00 69.90  ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 252.490 289.905 267.348 1.00 67.97  ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 252.557 291.201 266.682 1.00 67.68  ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 251.175 291.790 266.428 1.00 70.23  ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 250.992 293.004 266.564 1.00 75.25  ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 253.333 291.076 265.370 1.00 66.75  ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 254.808 290.802 265.593 1.00 76.32  ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 255.343 291.234 266.635 1.00 78.25  ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 255.432 290.154 264.728 1.00 74.12  ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 250.198 290.960 266.066 1.00 66.97  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 248.832 291.445 265.906 1.00 64.00  ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 248.194 291.779 267.252 1.00 64.37  ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 247.504 292.797 267.374 1.00 71.26  ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 247.982 290.420 265.133 1.00 62.10  ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 246.514 290.807 265.166 1.00 62.42  ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 248.462 290.308 263.698 1.00 62.73  ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 248.432 290.957 268.277 1.00 64.88  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 247.864 291.143 269.611 1.00 63.00  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 249.019 291.284 270.596 1.00 69.07  ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 249.418 290.307 271.247 1.00 71.25  ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 246.955 289.977 269.999 1.00 59.67  ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 245.823 289.737 269.040 1.00 66.22  ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 244.688 290.529 269.072 1.00 68.71  ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 245.889 288.708 268.116 1.00 69.64  ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 243.644 290.305 268.194 1.00 65.34  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 244.848 288.478 267.237 1.00 65.67  ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 243.725 289.279 267.276 1.00 60.60  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 249.582 292.484 270.730 1.00 74.20  ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 250.737 292.658 271.618 1.00 73.38  ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 250.332 292.647 273.083 1.00 73.65  ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 249.289 293.182 273.465 1.00 73.94  ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 251.297 294.022 271.203 1.00 73.42  ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 250.110 294.762 270.686 1.00 73.39  ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 249.211 293.736 270.046 1.00 71.16  ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 251.174 292.025 273.906 1.00 82.07  ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 250.969 292.001 275.337 1.00 84.53  ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 249.936 291.014 275.828 1.00 86.34  ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 249.669 290.973 277.036 1.00 85.71  ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 249.348 290.217 274.942 1.00 87.45  ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 248.295 289.276 275.301 1.00 86.43  ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 248.840 287.864 275.147 1.00 85.58  ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 249.344 287.496 274.079 1.00 85.92  ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 247.041 289.486 274.438 1.00 82.14  ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 245.978 288.466 274.795 1.00 83.24  ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 246.514 290.895 274.625 1.00 82.34  ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 248.734 287.074 276.210 1.00 92.81  ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 249.238 285.711 276.236 1.00 93.68  ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 248.090 284.732 276.442 1.00 94.81  ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 247.082 285.053 277.078 1.00 94.04  ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 250.282 285.534 277.343 1.00 94.40  ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 249.723 285.682 278.749 1.00 94.87  ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 250.163 286.967 279.421 1.00 98.51  ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 249.938 288.061 278.904 1.00 98.26  ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 250.792 286.841 280.584 1.00 95.74  ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 248.249 283.535 275.886 1.00 86.71  ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 247.269 282.467 276.016 1.00 87.77  ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 247.863 281.306 276.798 1.00 88.41  ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 248.917 280.776 276.430 1.00 87.11  ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 246.791 281.984 274.645 1.00 88.06  ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 245.897 280.770 274.723 1.00 88.50  ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 244.727 280.792 275.469 1.00 88.29  ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 246.240 279.588 274.079 1.00 83.10  ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 243.916 279.680 275.556 1.00 87.84  ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 245.431 278.471 274.155 1.00 85.98  ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 244.270 278.523 274.895 1.00 89.29  ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 243.460 277.413 274.978 1.00 89.15  ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 247.181 280.912 277.870 1.00 90.37  ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 247.538 279.738 278.654 1.00 92.16  ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 246.461 278.686 278.446 1.00 91.55  ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 245.296 278.911 278.793 1.00 91.98  ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 247.678 280.082 280.138 1.00 93.30  ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 248.501 281.305 280.401 1.00 95.15  ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 248.023 282.386 281.109 1.00 94.01  ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 249.771 281.616 280.051 1.00 94.04  ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 248.963 283.311 281.184 1.00 92.99  ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 250.034 282.869 280.550 1.00 93.27  ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 246.846 277.546 277.880 1.00 75.70  ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 245.889 276.479 277.621 1.00 77.24  ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 245.419 275.880 278.939 1.00 76.89  ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 246.212 275.284 279.676 1.00 76.42  ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 246.517 275.405 276.737 1.00 75.80  ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 245.536 274.344 276.270 1.00 75.41  ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 246.175 273.408 275.260 1.00 76.44  ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 245.220 272.438 274.738 1.00 76.61  ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 245.493 271.555 273.789 1.00 73.95  ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 246.692 271.485 273.234 1.00 71.40  ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 244.540 270.721 273.384 1.00 74.35  ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 244.134 276.049 279.241 1.00 86.50  ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 243.565 275.479 280.445 1.00 87.51  ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 243.705 273.973 280.472 1.00 88.90  ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 243.328 273.292 279.514 1.00 89.93  ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 244.249 273.439 281.562 1.00 92.35  ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 244.485 272.006 281.643 1.00 92.44  ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 243.166 271.263 281.802 1.00 94.22  ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 242.416 271.501 282.753 1.00 93.52  ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 245.417 271.685 282.811 1.00 89.15  ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 245.735 270.204 282.956 1.00 91.79  ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 246.872 269.942 283.924 1.00 95.33  ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 247.996 270.425 283.669 1.00 95.01  ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 246.642 269.254 284.940 1.00 93.25  ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 242.885 270.361 280.863 1.00 77.68  ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 241.721 269.482 280.958 1.00 74.26  ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 242.080 268.299 281.855 1.00 72.92  ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 242.321 267.176 281.408 1.00 77.60  ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 241.270 269.040 279.572 1.00 72.08  ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 240.728 270.177 278.718 1.00 74.19  ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 240.133 269.654 277.099 1.00 93.36  ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 241.677 269.346 276.246 1.00 75.70  ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 242.116 268.590 283.159 1.00 70.91  ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 242.642 267.637 284.133 1.00 68.50  ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 241.893 266.313 284.079 1.00 70.40  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 242.472 265.280 283.727 1.00 76.88  ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 242.573 268.233 285.540 1.00 75.14  ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 243.438 269.372 285.622 1.00 77.64  ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 243.004 267.203 286.574 1.00 71.48  ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 240.590 266.333 284.379 1.00 62.08  ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 239.835 265.092 284.539 1.00 60.30  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 239.926 264.214 283.297 1.00 61.48  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 239.834 262.985 283.388 1.00 64.23  ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 238.376 265.403 284.869 1.00 64.48  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 240.107 264.827 282.126 1.00 53.68  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 240.313 264.043 280.914 1.00 50.82  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 241.681 263.371 280.906 1.00 54.72  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 241.828 262.276 280.351 1.00 61.89  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 240.146 264.934 279.682 1.00 49.42  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 240.352 264.279 278.315 1.00 52.68  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 239.302 263.209 278.071 1.00 51.70  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 240.321 265.322 277.212 1.00 54.73  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 242.689 264.001 281.517 1.00 57.17  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 244.049 263.475 281.425 1.00 48.89  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 244.209 262.170 282.199 1.00 57.18  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 244.849 261.234 281.706 1.00 63.87  ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 245.058 264.519 281.903 1.00 51.85  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 245.138 265.743 281.002 1.00 54.45  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 246.121 266.771 281.534 1.00 60.20  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 247.502 266.368 281.296 1.00 65.55  ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 248.244 266.802 280.285 1.00 64.88  ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 247.777 267.679 279.412 1.00 53.56  ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 249.485 266.347 280.148 1.00 68.41  ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 243.652 262.080 283.412 1.00 57.99  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 243.689 260.797 284.112 1.00 65.20  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 242.872 259.747 283.372 1.00 59.47  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 243.208 258.558 283.403 1.00 63.69  ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 243.201 260.924 285.558 1.00 61.52  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 244.096 261.741 286.482 1.00 61.00  ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 243.855 263.225 286.376 1.00 68.35  ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 242.942 263.615 285.628 1.00 70.31  ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 244.576 263.999 287.040 1.00 67.76  ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 241.790 260.163 282.710 1.00 50.79  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 241.045 259.230 281.873 1.00 43.57  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 241.901 258.734 280.716 1.00 47.86  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 241.881 257.543 280.384 1.00 55.97  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 239.766 259.888 281.355 1.00 50.64  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 238.705 260.122 282.420 1.00 56.08  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 238.503 258.923 283.327 1.00 62.34  ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 238.380 257.793 282.811 1.00 61.52  ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 238.465 259.112 284.561 1.00 59.21  ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 242.662 259.635 280.089 1.00 45.56  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 243.589 259.220 279.041 1.00 43.07  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 244.694 258.335 279.603 1.00 47.10  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 245.090 257.347 278.973 1.00 55.80  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 244.189 260.445 278.351 1.00 43.64  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 243.239 261.346 277.560 1.00 46.01  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 243.973 262.576 277.057 1.00 45.61  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 242.612 260.587 276.405 1.00 46.17  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 245.208 258.678 280.787 1.00 48.28  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 246.301 257.912 281.378 1.00 49.69  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 245.874 256.480 281.677 1.00 47.73  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 246.623 255.530 281.422 1.00 55.05  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 246.795 258.605 282.648 1.00 49.60  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 248.122 258.078 283.169 1.00 52.11  ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 248.713 259.011 284.213 1.00 56.02  ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 250.084 258.536 284.665 1.00 55.68  ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 250.725 259.498 285.604 1.00 53.43  ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 244.670 256.306 282.226 1.00 49.68  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 244.180 254.962 282.515 1.00 45.53  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 243.927 254.177 281.233 1.00 52.57  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 244.247 252.985 281.155 1.00 63.11  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 242.910 255.037 283.362 1.00 48.03  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 243.135 255.583 284.763 1.00 55.41  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 241.877 255.482 285.609 1.00 59.18  ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 240.845 256.516 285.191 1.00 62.19  ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 239.653 256.502 286.082 1.00 54.28  ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 243.349 254.826 280.220 1.00 41.65  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 243.092 254.148 278.951 1.00 40.88  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 244.403 253.770 278.272 1.00 42.81  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 244.544 252.666 277.732 1.00 52.87  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 242.212 255.028 278.043 1.00 43.54  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 242.195 254.484 276.624 1.00 42.45  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 240.799 255.105 278.596 1.00 45.59  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 245.384 254.677 278.291 1.00 45.73  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 246.681 254.378 277.692 1.00 42.93  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 247.364 253.217 278.404 1.00 44.08  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 248.034 252.396 277.767 1.00 53.79  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 247.571 255.621 277.718 1.00 42.93  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 247.107 256.899 276.530 1.00 60.30  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 247.212 253.138 279.727 1.00 46.29  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 247.796 252.032 280.479 1.00 49.28  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 247.187 250.698 280.066 1.00 54.25  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 247.898 249.694 279.941 1.00 58.20  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 247.610 252.265 281.978 1.00 54.55  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 248.250 251.208 282.862 1.00 56.70  ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 249.763 251.211 282.776 1.00 64.79  ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 250.392 252.269 282.743 1.00 66.35  ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 250.357 250.024 282.743 1.00 56.54  ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 245.870 250.667 279.849 1.00 51.64  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 245.204 249.413 279.512 1.00 49.39  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 245.499 248.976 278.083 1.00 51.61  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 245.452 247.777 277.783 1.00 48.02  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 243.697 249.547 279.723 1.00 50.12  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 243.304 249.920 281.141 1.00 55.29  ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 241.805 249.910 281.349 1.00 63.04  ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 241.066 249.993 280.346 1.00 62.57  ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 241.365 249.823 282.514 1.00 58.84  ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 245.800 249.920 277.192 1.00 54.67  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 246.106 249.614 275.801 1.00 45.07  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 247.605 249.563 275.535 1.00 42.65  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 248.022 249.589 274.372 1.00 51.48  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 245.435 250.628 274.874 1.00 42.99  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 243.917 250.555 274.873 1.00 47.09  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 243.157 251.815 273.834 1.00 57.11  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 243.597 251.219 272.204 1.00 46.83  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 248.419 249.499 276.591 1.00 43.79  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 249.874 249.390 276.483 1.00 44.59  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 250.478 250.567 275.723 1.00 44.55  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 251.467 250.415 275.003 1.00 52.60  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 250.284 248.067 275.829 1.00 43.46  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 249.745 246.850 276.542 1.00 51.01  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 250.205 246.499 277.803 1.00 52.38  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 248.769 246.056 275.955 1.00 44.50  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 249.710 245.389 278.459 1.00 48.61  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 248.269 244.945 276.602 1.00 40.75  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 248.743 244.615 277.853 1.00 50.74  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 248.245 243.507 278.499 1.00 56.06  ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 249.891 251.748 275.880 1.00 45.48  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 250.374 252.955 275.229 1.00 41.92  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 251.166 253.808 276.212 1.00 46.27  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 251.034 253.682 277.432 1.00 44.29  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 249.211 253.762 274.647 1.00 41.67  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 248.390 253.094 273.541 1.00 31.73  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 247.646 254.140 272.732 1.00 40.49  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 249.272 252.248 272.635 1.00 36.63  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 251.998 254.685 275.659 1.00 52.83  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 252.854 255.551 276.456 1.00 47.51  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 252.174 256.897 276.667 1.00 44.27  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 251.749 257.544 275.704 1.00 51.86  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 254.209 255.745 275.777 1.00 43.36  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 254.832 254.471 275.576 1.00 44.66  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 255.114 256.613 276.635 1.00 46.52  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 252.073 257.312 277.925 1.00 50.06  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 251.460 258.578 278.296 1.00 50.96  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 252.517 259.507 278.875 1.00 55.72  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 253.365 259.082 279.666 1.00 60.28  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 250.331 258.365 279.309 1.00 52.87  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 249.619 259.637 279.709 1.00 57.81  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 248.525 260.096 278.990 1.00 55.19  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 250.038 260.375 280.808 1.00 58.50  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 247.871 261.257 279.350 1.00 51.35  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 249.391 261.537 281.175 1.00 52.66  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 248.309 261.972 280.443 1.00 53.11  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 247.664 263.129 280.806 1.00 57.58  ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 252.463 260.771 278.481 1.00 52.21  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 253.429 261.749 278.951 1.00 50.48  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 252.792 263.109 279.100 1.00 59.16  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 251.788 263.421 278.451 1.00 60.91  ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 253.384 263.928 279.966 1.00 73.40  ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 252.898 265.272 280.245 1.00 67.42  ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 253.933 266.284 279.778 1.00 71.48  ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 255.087 266.245 280.218 1.00 75.39  ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 252.616 265.455 281.739 1.00 67.36  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 251.318 264.804 282.172 1.00 72.17  ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 250.431 264.613 281.314 1.00 72.13  ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 251.184 264.483 283.371 1.00 76.74  ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 253.519 267.190 278.896 1.00 76.64  ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 254.399 268.240 278.422 1.00 78.64  ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 255.583 267.745 277.617 1.00 75.40  ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 255.422 267.264 276.491 1.00 76.04  ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 256.781 267.861 278.185 1.00 77.57  ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 258.013 267.498 277.497 1.00 80.58  ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 258.451 266.064 277.764 1.00 82.57  ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 259.510 265.656 277.275 1.00 79.63  ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 259.139 268.458 277.895 1.00 78.08  ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 258.960 269.877 277.380 1.00 78.95  ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 259.570 270.083 276.006 1.00 83.33  ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 259.251 269.301 275.086 1.00 83.31  ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 260.371 271.028 275.847 1.00 82.79  ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 257.674 265.293 278.520 1.00 68.99  ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 258.023 263.907 278.788 1.00 62.77  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 257.838 263.063 277.527 1.00 64.29  ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 257.433 263.549 276.468 1.00 65.49  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 257.180 263.357 279.936 1.00 61.99  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 257.291 264.147 281.229 1.00 66.50  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 256.225 263.761 282.235 1.00 69.61  ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 255.458 262.815 281.958 1.00 67.80  ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 256.152 264.405 283.303 1.00 70.49  ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 258.144 261.773 277.648 1.00 61.05  ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 257.958 260.850 276.535 1.00 61.02  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 256.465 260.668 276.297 1.00 58.01  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 255.716 260.301 277.209 1.00 61.16  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 258.647 259.508 276.814 1.00 60.81  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 258.183 258.459 275.819 1.00 54.32  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 260.158 259.669 276.759 1.00 56.79  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 256.028 260.918 275.065 1.00 46.07  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 254.624 260.863 274.728 1.00 47.04  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 253.848 262.132 274.996 1.00 46.73  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 252.627 262.143 274.796 1.00 55.99  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 254.511 263.201 275.441 1.00 43.07  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 253.802 264.440 275.716 1.00 43.61  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 253.192 265.058 274.473 1.00 47.53  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 252.086 265.602 274.518 1.00 55.36  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 253.908 264.991 273.348 1.00 51.63  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 253.373 265.527 272.100 1.00 47.35  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 252.143 264.751 271.648 1.00 46.84  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 251.180 265.339 271.142 1.00 54.74  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 254.449 265.507 271.015 1.00 48.42  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 255.751 266.178 271.416 1.00 52.03  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 256.874 266.392 270.022 1.00 78.28  ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 255.839 267.324 268.896 1.00 52.85  ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 252.160 263.426 271.813 1.00 40.92  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 251.016 262.616 271.406 1.00 36.90  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 249.790 262.918 272.258 1.00 38.94  ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 248.667 262.968 271.743 1.00 45.86  ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 251.368 261.132 271.479 1.00 45.86  ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 250.276 260.242 270.978 1.00 46.52  ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 249.955 259.991 269.677 1.00 34.55  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 249.350 259.490 271.772 1.00 40.04  ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 248.890 259.126 269.610 1.00 39.05  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 248.500 258.804 270.883 1.00 34.12  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 249.159 259.330 273.147 1.00 33.02  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 247.476 257.971 271.324 1.00 41.28  ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 248.142 258.502 273.582 1.00 31.39  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 247.314 257.833 272.674 1.00 39.44  ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 249.982 263.114 273.564 1.00 41.68  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 248.860 263.447 274.435 1.00 39.63  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 248.293 264.813 274.074 1.00 41.59  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 247.073 265.018 274.091 1.00 47.42  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 249.290 263.380 275.911 1.00 42.05  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 248.138 263.779 276.820 1.00 46.26  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 249.778 261.984 276.253 1.00 39.32  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 249.164 265.765 273.732 1.00 44.12  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 248.695 267.082 273.313 1.00 39.57  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 247.858 266.988 272.044 1.00 44.20  ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 246.856 267.698 271.898 1.00 56.03  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 249.882 268.022 273.106 1.00 44.19  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 250.353 268.723 274.371 1.00 56.77  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 249.300 269.642 274.960 1.00 66.03  ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 248.496 270.204 274.187 1.00 69.99  ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 249.278 269.804 276.198 1.00 57.95  ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 248.257 266.119 271.113 1.00 42.67  ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 247.472 265.921 269.899 1.00 29.85  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 246.103 265.333 270.217 1.00 31.51  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 245.103 265.690 269.582 1.00 45.00  ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 248.232 265.022 268.925 1.00 25.72  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 249.302 265.743 268.124 1.00 36.52  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 248.708 266.875 267.306 1.00 34.65  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 249.715 267.993 267.101 1.00 39.81  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 249.233 268.995 266.111 1.00 32.61  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 246.040 264.421 271.190 1.00 41.81  ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 244.755 263.866 271.607 1.00 36.81  ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 243.877 264.954 272.211 1.00 38.57  ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 242.674 265.029 271.934 1.00 44.88  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 244.970 262.699 272.590 1.00 32.03  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 243.641 262.222 273.152 1.00 37.58  ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 245.702 261.558 271.905 1.00 33.21  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 244.464 265.815 273.048 1.00 35.95  ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 243.709 266.926 273.618 1.00 35.18  ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 243.245 267.893 272.537 1.00 38.68  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 242.112 268.388 272.582 1.00 47.83  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 244.555 267.655 274.661 1.00 40.08  ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 245.074 266.809 275.821 1.00 45.67  ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 245.963 267.644 276.717 1.00 49.10  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 243.915 266.226 276.608 1.00 37.55  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 244.108 268.183 271.561 1.00 32.75  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 243.699 269.029 270.445 1.00 34.97  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 242.585 268.372 269.643 1.00 37.29  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 241.652 269.047 269.193 1.00 42.01  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 244.896 269.334 269.546 1.00 28.57  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 245.920 270.264 270.166 1.00 36.49  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 247.161 270.408 269.312 1.00 35.30  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 247.258 269.820 268.236 1.00 38.86  ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 248.119 271.193 269.788 1.00 43.86  ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 242.668 267.054 269.451 1.00 41.67  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 241.628 266.341 268.718 1.00 35.67  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 240.297 266.410 269.458 1.00 34.14  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 239.232 266.480 268.833 1.00 34.71  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 242.057 264.889 268.499 1.00 31.32  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 241.312 263.995 267.505 1.00 37.48  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 242.261 262.920 267.019 1.00 38.51  ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 240.067 263.362 268.097 1.00 42.33  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 240.340 266.384 270.792 1.00 29.71  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 239.118 266.490 271.584 1.00 34.33  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 238.465 267.855 271.409 1.00 37.89  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 237.236 267.965 271.344 1.00 46.97  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 239.425 266.223 273.057 1.00 37.80  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 238.271 266.517 273.989 1.00 42.22  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 237.049 265.877 273.836 1.00 39.54  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 238.405 267.434 275.021 1.00 37.32  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 235.992 266.144 274.685 1.00 43.46  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 237.355 267.707 275.876 1.00 37.40  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 236.151 267.059 275.703 1.00 48.95  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 235.102 267.328 276.552 1.00 49.63  ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 239.276 268.913 271.343 1.00 43.10  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 238.726 270.254 271.178 1.00 36.49  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 238.038 270.408 269.828 1.00 40.29  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 237.012 271.090 269.720 1.00 54.01  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 239.831 271.297 271.343 1.00 45.09  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 240.444 271.326 272.733 1.00 50.92  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 241.419 272.472 272.919 1.00 54.57  ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 242.439 272.552 272.234 1.00 51.40  ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 241.110 273.365 273.850 1.00 48.68  ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 238.590 269.786 268.785 1.00 35.64  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 237.990 269.887 267.458 1.00 35.84  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 236.644 269.171 267.420 1.00 41.00  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 235.727 269.585 266.700 1.00 45.77  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 238.961 269.347 266.392 1.00 35.28  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 240.298 270.083 266.476 1.00 36.59  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 238.383 269.531 265.002 1.00 38.24  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 240.199 271.562 266.179 1.00 32.03  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 236.500 268.088 268.191 1.00 40.21  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 235.216 267.395 268.258 1.00 32.86  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 234.125 268.312 268.796 1.00 36.33  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 232.992 268.301 268.301 1.00 41.30  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 235.323 266.144 269.132 1.00 33.65  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 235.928 266.482 270.386 1.00 51.43  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 236.152 265.072 268.451 1.00 30.06  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 234.448 269.109 269.816 1.00 36.16  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 233.467 270.013 270.402 1.00 36.34  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 233.119 271.171 269.477 1.00 41.58  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 232.067 271.795 269.653 1.00 48.66  ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 233.989 270.553 271.734 1.00 38.35  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 234.641 269.502 272.616 1.00 32.64  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 234.615 269.874 274.084 1.00 47.85  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 233.617 269.664 274.773 1.00 49.04  ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 235.717 270.432 274.572 1.00 47.10  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 233.971 271.473 268.504 1.00 35.44  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 233.777 272.613 267.614 1.00 34.90  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 233.182 272.190 266.278 1.00 41.67  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 232.170 272.737 265.840 1.00 50.05  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 235.111 273.368 267.417 1.00 35.16  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 235.627 273.899 268.756 1.00 44.01  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 234.940 274.502 266.420 1.00 37.35  ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 237.027 274.465 268.687 1.00 45.56  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 233.796 271.214 265.616 1.00 38.48  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 233.404 270.802 264.276 1.00 37.79  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 232.741 269.432 264.312 1.00 36.05  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 233.171 268.542 265.054 1.00 36.56  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 234.615 270.758 263.339 1.00 33.09  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 235.365 272.073 263.294 1.00 46.58  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 236.411 272.225 263.924 1.00 46.68  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 234.836 273.030 262.541 1.00 48.94  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 231.687 269.270 263.510 1.00 39.37  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 231.096 267.950 263.324 1.00 36.70  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 231.851 267.141 262.278 1.00 32.05  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 231.638 265.929 262.163 1.00 35.54  ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 229.623 268.076 262.930 1.00 36.51  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 229.391 268.893 261.698 1.00 34.96  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 229.578 270.258 261.662 1.00 37.71  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 228.987 268.537 260.455 1.00 35.23  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 229.299 270.707 260.451 1.00 37.58  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 228.938 269.683 259.700 1.00 36.51  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 232.724 267.789 261.511 1.00 29.96  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 233.559 267.103 260.547 1.00 25.13  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 235.033 267.278 260.847 1.00 31.40  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 235.557 268.393 260.782 1.00 35.66  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 235.712 266.185 261.178 1.00 36.72  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 237.119 266.216 261.542 1.00 35.68  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 237.949 265.501 260.488 1.00 41.45  ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 237.448 264.663 259.735 1.00 49.30  ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 237.373 265.557 262.902 1.00 29.77  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 237.037 266.321 264.179 1.00 35.65  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 235.535 266.434 264.394 1.00 39.24  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 237.717 265.660 265.360 1.00 46.09  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 239.234 265.841 260.447 1.00 31.93  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 240.182 265.150 259.583 1.00 36.92  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 241.520 265.062 260.297 1.00 34.10  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 241.994 266.053 260.860 1.00 43.86  ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 240.326 265.860 258.236 1.00 42.01  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 241.206 265.119 257.253 1.00 44.87  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 241.330 265.982 255.684 1.00 82.67  ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 239.693 265.701 255.015 1.00 33.04  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 242.120 263.875 260.274 1.00 39.79  ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 243.401 263.609 260.922 1.00 32.22  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 244.443 263.419 259.827 1.00 38.27  ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 244.496 262.369 259.182 1.00 55.96  ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 243.295 262.380 261.817 1.00 34.97  ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 242.381 262.564 263.011 1.00 32.57  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 242.348 261.096 264.048 1.00 38.17  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 241.352 260.022 263.021 1.00 47.97  ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 245.276 264.434 259.623 1.00 28.81  ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 246.264 264.448 258.552 1.00 26.55  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 247.637 264.207 259.161 1.00 33.03  ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 248.016 264.871 260.133 1.00 46.96  ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 246.231 265.774 257.773 1.00 30.29  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 247.299 265.783 256.692 1.00 33.82  ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 244.853 266.004 257.175 1.00 37.65  ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 248.374 263.256 258.598 1.00 24.42  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 249.705 262.953 259.065 1.00 19.48  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 250.261 261.698 258.430 1.00 27.59  ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 249.521 260.779 258.067 1.00 47.55  ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 251.585 261.631 258.291 1.00 32.93  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 252.205 260.460 257.664 1.00 36.89  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 251.904 259.182 258.434 1.00 37.29  ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 251.469 259.203 259.587 1.00 45.93  ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 253.702 260.789 257.698 1.00 38.75  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 253.758 262.277 257.775 1.00 42.37  ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 252.569 262.684 258.593 1.00 33.42  ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 252.138 258.054 257.766 1.00 41.61  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 251.846 256.756 258.356 1.00 38.92  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 252.671 256.542 259.618 1.00 41.99  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 253.835 256.944 259.704 1.00 49.82  ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 252.124 255.638 257.349 1.00 37.11  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 251.714 254.381 257.857 1.00 43.08  ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 252.055 255.897 260.604 1.00 31.73  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 252.719 255.672 261.877 1.00 30.08  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 252.980 256.932 262.673 1.00 41.61  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 254.072 257.096 263.231 1.00 49.68  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 252.001 257.832 262.733 1.00 44.01  ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 252.108 259.050 263.522 1.00 35.44  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 251.188 259.055 264.734 1.00 34.12  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 251.142 260.058 265.455 1.00 46.64  ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 251.816 260.275 262.648 1.00 30.13  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 250.670 260.065 261.843 1.00 39.80  ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 250.458 257.972 264.979 1.00 32.35  ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 249.572 257.883 266.119 1.00 29.61  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 248.158 258.369 265.892 1.00 38.16  ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 247.451 258.627 266.873 1.00 48.99  ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 247.724 258.508 264.637 1.00 34.16  ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 246.384 259.021 264.366 1.00 19.21  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 245.310 258.065 264.870 1.00 28.01  ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 244.359 258.483 265.540 1.00 39.26  ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 246.212 259.274 262.868 1.00 32.36  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 247.208 260.252 262.277 1.00 31.26  ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 246.910 260.510 260.812 1.00 38.20  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 247.053 259.242 259.989 1.00 32.65  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 248.477 258.848 259.819 1.00 28.61  ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 245.439 256.776 264.546 1.00 45.77  ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 244.422 255.806 264.943 1.00 30.08  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 244.359 255.662 266.458 1.00 33.04  ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 243.272 255.602 267.043 1.00 42.61  ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 244.699 254.455 264.285 1.00 33.78  ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 244.999 254.610 262.909 1.00 39.85  ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 245.521 255.607 267.112 1.00 38.89  ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 245.542 255.450 268.562 1.00 36.34  ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 244.996 256.688 269.261 1.00 37.19  ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 244.449 256.596 270.365 1.00 49.29  ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 246.964 255.149 269.037 1.00 27.11  ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 247.435 253.722 268.781 1.00 42.92  ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 246.504 252.458 269.669 1.00 59.00  ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 245.407 251.863 268.384 1.00 39.17  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 245.138 257.858 268.634 1.00 31.58  ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 244.674 259.094 269.257 1.00 29.04  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 243.158 259.102 269.411 1.00 38.21  ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 242.634 259.377 270.496 1.00 52.90  ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 245.140 260.300 268.441 1.00 29.18  ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 242.433 258.800 268.331 1.00 27.86  ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 240.976 258.833 268.402 1.00 25.01  ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 240.418 257.610 269.119 1.00 33.17  ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 239.351 257.694 269.737 1.00 45.68  ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 240.380 258.966 266.997 1.00 35.70  ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 240.465 257.733 266.144 1.00 35.49  ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 241.387 257.473 265.175 1.00 27.93  ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 239.563 256.618 266.146 1.00 38.44  ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 241.133 256.256 264.591 1.00 32.67  ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 240.018 255.711 265.169 1.00 33.73  ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 238.424 256.293 266.888 1.00 38.73  ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 239.375 254.503 264.915 1.00 31.41  ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 237.789 255.093 266.635 1.00 34.14  ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 238.264 254.213 265.657 1.00 35.08  ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 241.111 256.472 269.043 1.00 34.46  ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 240.664 255.287 269.770 1.00 30.70  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 240.750 255.504 271.276 1.00 38.24  ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 239.832 255.142 272.021 1.00 41.63  ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 241.494 254.071 269.359 1.00 28.63  ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 241.100 253.453 268.030 1.00 33.22  ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 241.839 252.144 267.815 1.00 36.57  ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 241.749 251.670 266.439 1.00 42.51  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 240.758 250.927 265.966 1.00 48.56  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 239.741 250.563 266.729 1.00 40.85  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 240.790 250.537 264.695 1.00 46.18  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 241.855 256.090 271.741 1.00 38.41  ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 242.014 256.351 273.169 1.00 32.49  ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 241.019 257.405 273.633 1.00 38.30  ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 240.390 257.265 274.689 1.00 49.30  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 243.466 256.763 273.477 1.00 26.72  ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 243.560 257.424 274.840 1.00 32.49  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 244.377 255.551 273.416 1.00 35.47  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 240.855 258.475 272.851 1.00 32.92  ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 239.924 259.533 273.231 1.00 25.40  ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 238.492 259.018 273.286 1.00 26.81  ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 237.740 259.356 274.207 1.00 46.66  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 240.029 260.704 272.258 1.00 28.26  ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 239.121 261.883 272.607 1.00 35.66  ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 239.551 262.525 273.917 1.00 32.74  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 239.104 262.896 271.486 1.00 28.09  ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 238.097 258.201 272.308 1.00 28.13  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 236.742 257.658 272.295 1.00 28.33  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 236.474 256.821 273.537 1.00 32.10  ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 235.387 256.886 274.123 1.00 40.15  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 236.522 256.827 271.031 1.00 30.46  ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 235.095 256.331 270.789 1.00 30.26  ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 234.110 257.485 270.792 1.00 34.79  ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 235.016 255.560 269.486 1.00 30.88  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 237.457 256.021 273.954 1.00 44.40  ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 237.258 255.173 275.122 1.00 38.90  ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 237.350 255.992 276.405 1.00 42.19  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 236.623 255.733 277.371 1.00 51.33  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 238.283 254.040 275.124 1.00 42.07  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 238.153 253.084 276.294 1.00 48.13  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 236.851 252.300 276.163 1.00 44.81  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 236.720 251.210 277.211 1.00 48.75  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 236.594 251.765 278.582 1.00 53.16  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 238.241 256.988 276.431 1.00 34.28  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 238.367 257.849 277.603 1.00 29.96  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 237.129 258.717 277.795 1.00 33.07  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 236.677 258.918 278.929 1.00 50.26  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 239.617 258.719 277.486 1.00 25.71  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 236.574 259.251 276.704 1.00 38.58  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 235.350 260.041 276.813 1.00 35.38  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 234.189 259.188 277.305 1.00 39.73  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 233.274 259.695 277.964 1.00 48.53  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 235.011 260.683 275.468 1.00 38.09  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 235.896 261.843 275.010 1.00 37.74  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 235.289 262.531 273.797 1.00 38.77  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 236.105 262.834 276.142 1.00 44.15  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 234.204 257.893 276.985 1.00 45.44  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 233.178 256.991 277.496 1.00 44.28  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 233.258 256.871 279.012 1.00 45.32  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 232.228 256.857 279.697 1.00 48.59  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 233.317 255.621 276.833 1.00 44.77  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 232.613 254.491 277.559 1.00 47.92  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 232.611 253.206 276.758 1.00 58.54  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 232.601 252.119 277.373 1.00 63.52  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 232.622 253.283 275.512 1.00 55.56  ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 234.473 256.785 279.557 1.00 47.64  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 234.627 256.729 281.007 1.00 47.54  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 234.323 258.076 281.650 1.00 46.21  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 233.673 258.138 282.700 1.00 51.36  ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 236.041 256.283 281.372 1.00 48.39  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 236.268 254.785 281.365 1.00 53.26  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 237.753 254.473 281.291 1.00 50.20  ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 238.012 253.196 280.640 1.00 58.38  ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 238.924 252.321 281.039 1.00 58.28  ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 239.697 252.556 282.087 1.00 56.66  ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 239.065 251.180 280.370 1.00 51.88  ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 234.791 259.166 281.037 1.00 45.69  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 234.659 260.482 281.653 1.00 45.59  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 233.209 260.951 281.676 1.00 48.94  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 232.756 261.531 282.670 1.00 49.54  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 235.537 261.492 280.914 1.00 45.81  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 235.456 262.947 281.379 1.00 47.35  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 236.112 263.111 282.740 1.00 52.72  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 236.096 263.873 280.356 1.00 40.53  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 232.466 260.711 280.597 1.00 49.25  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 231.110 261.226 280.468 1.00 53.88  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 230.034 260.161 280.639 1.00 55.26  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 228.856 260.512 280.761 1.00 58.12  ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 230.933 261.907 279.105 1.00 50.69  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 232.024 262.909 278.769 1.00 50.11  ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 231.883 263.475 277.370 1.00 56.16  ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 231.017 262.985 276.615 1.00 61.56  ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 232.637 264.408 277.026 1.00 54.66  ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 230.400 258.882 280.652 1.00 45.03  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 229.416 257.828 280.774 1.00 47.59  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 228.621 257.546 279.520 1.00 54.02  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 227.628 256.813 279.588 1.00 57.09  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 229.021 258.101 278.381 1.00 54.21  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 228.319 257.915 277.117 1.00 52.92  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 229.074 256.875 276.302 1.00 55.61  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 230.277 257.023 276.054 1.00 62.85  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 228.192 259.238 276.345 1.00 50.18  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 227.660 258.988 274.944 1.00 50.41  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 227.294 260.207 277.098 1.00 51.62  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 228.372 255.823 275.887 1.00 51.58  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 228.997 254.763 275.107 1.00 45.48  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 229.481 255.300 273.767 1.00 47.11  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 228.767 256.040 273.084 1.00 52.94  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 228.009 253.615 274.894 1.00 50.12  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 228.578 252.432 274.125 1.00 53.99  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 229.693 251.725 274.873 1.00 59.10  ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 229.717 251.797 276.120 1.00 61.18  ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 230.547 251.098 274.213 1.00 54.69  ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 230.701 254.924 273.392 1.00 36.61  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 231.277 255.370 272.139 1.00 40.86  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 231.339 254.279 271.091 1.00 43.28  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 232.020 253.266 271.278 1.00 45.36  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 230.632 254.475 269.982 1.00 33.21  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 230.594 253.519 268.881 1.00 29.40  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 231.314 254.134 267.691 1.00 36.67  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 231.018 255.268 267.295 1.00 41.14  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 229.150 253.138 268.513 1.00 31.62  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 229.143 252.060 267.442 1.00 35.67  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 228.395 252.673 269.748 1.00 39.51  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 232.258 253.389 267.124 1.00 31.47  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 233.051 253.844 265.992 1.00 26.10  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 232.766 252.969 264.781 1.00 40.34  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 232.785 251.737 264.880 1.00 45.61  ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 234.544 253.815 266.321 1.00 22.63  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 232.502 253.606 263.644 1.00 34.45  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 232.301 252.918 262.373 1.00 21.82  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 233.449 253.298 261.448 1.00 22.62  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 233.477 254.408 260.907 1.00 44.94  ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 230.951 253.281 261.759 1.00 28.01  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 229.803 253.166 262.712 1.00 35.15  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 229.040 252.024 262.823 1.00 35.25  ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 229.287 254.051 263.598 1.00 33.89  ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 228.104 252.209 263.736 1.00 32.63  ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 228.232 253.431 264.222 1.00 39.04  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 234.392 252.379 261.267 1.00 23.37  ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 235.570 252.609 260.440 1.00 34.22  ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 235.264 252.119 259.033 1.00 33.30  ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 234.921 250.947 258.834 1.00 42.64  ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 236.807 251.906 261.017 1.00 31.33  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 236.969 252.254 262.497 1.00 29.21  ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 238.052 252.298 260.239 1.00 25.43  ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 238.011 251.428 263.204 1.00 33.35  ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 235.389 253.015 258.058 1.00 30.36  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 235.054 252.731 256.669 1.00 30.59  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 236.265 253.050 255.806 1.00 37.13  ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 236.875 254.114 255.957 1.00 37.55  ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 233.830 253.543 256.203 1.00 31.77  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 232.576 253.103 256.961 1.00 32.69  ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 233.631 253.409 254.702 1.00 35.21  ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 231.415 254.063 256.826 1.00 32.57  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 236.620 252.126 254.916 1.00 42.09  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 237.628 252.400 253.901 1.00 34.53  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 236.921 252.838 252.624 1.00 47.03  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 236.444 251.994 251.855 1.00 47.37  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 238.506 251.176 253.646 1.00 39.05  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 239.888 251.546 253.141 1.00 52.48  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 239.987 252.456 252.291 1.00 46.77  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 240.875 250.931 253.593 1.00 54.43  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 236.826 254.146 252.372 1.00 42.87  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 236.042 254.620 251.220 1.00 31.01  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 236.601 254.193 249.876 1.00 38.46  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 235.838 254.124 248.905 1.00 37.01  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 236.081 256.144 251.378 1.00 36.32  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 237.342 256.400 252.132 1.00 26.46  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 237.508 255.248 253.071 1.00 31.58  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 237.900 253.909 249.782 1.00 41.73  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 238.506 253.545 248.511 1.00 31.58  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 238.648 252.042 248.321 1.00 33.95  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 238.973 251.604 247.212 1.00 42.41  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 239.881 254.207 248.371 1.00 43.39  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 239.855 255.712 248.581 1.00 41.03  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 239.277 256.437 247.376 1.00 28.62  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 240.174 256.304 246.161 1.00 35.94  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 239.630 257.037 244.987 1.00 40.33  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 238.417 251.247 249.367 1.00 36.49  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 238.404 249.797 249.220 1.00 36.94  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 237.153 249.296 248.515 1.00 38.20  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 237.108 248.125 248.124 1.00 47.56  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 238.528 249.128 250.589 1.00 31.79  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 236.144 250.150 248.348 1.00 39.11  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 234.900 249.802 247.678 1.00 36.31  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 234.585 250.888 246.657 1.00 44.83  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 235.117 251.997 246.709 1.00 53.38  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 233.728 249.634 248.668 1.00 39.47  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 233.459 250.951 249.400 1.00 32.10  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 234.015 248.516 249.658 1.00 45.09  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 232.189 250.948 250.216 1.00 37.04  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 233.708 250.551 245.718 1.00 39.57  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 233.280 251.515 244.719 1.00 38.87  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 232.389 252.578 245.356 1.00 42.64  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 231.839 252.396 246.445 1.00 49.88  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 232.537 250.818 243.579 1.00 39.97  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 231.271 250.348 244.006 1.00 49.14  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 232.260 253.709 244.658 1.00 43.96  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 231.432 254.797 245.167 1.00 37.01  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 229.966 254.389 245.252 1.00 42.01  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 229.234 254.879 246.120 1.00 51.01  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 231.596 256.037 244.287 1.00 35.46  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 230.783 257.237 244.743 1.00 41.49  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 231.044 258.449 243.870 1.00 43.19  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 230.015 259.536 244.125 1.00 41.76  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 230.292 260.762 243.328 1.00 46.62  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 229.523 253.491 244.369 1.00 39.18  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 228.150 253.000 244.438 1.00 43.81  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 227.904 252.228 245.728 1.00 45.88  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 226.820 252.315 246.315 1.00 49.68  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 227.843 252.126 243.222 1.00 44.77  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 227.788 252.919 241.932 1.00 56.27  ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 227.435 254.116 241.983 1.00 56.40  ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 228.096 252.345 240.867 1.00 54.67  ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 228.897 251.463 246.182 1.00 35.71  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 228.767 250.700 247.415 1.00 33.18  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 228.994 251.539 248.665 1.00 34.02  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 228.751 251.046 249.772 1.00 42.41  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 229.742 249.520 247.410 1.00 36.66  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 229.405 248.461 246.408 1.00 38.39  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 228.151 247.897 246.316 1.00 45.22  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 230.159 247.858 245.459 1.00 39.81  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 228.146 246.995 245.351 1.00 40.82  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 229.352 246.952 244.815 1.00 46.43  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 229.450 252.782 248.521 1.00 29.72  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 229.702 253.659 249.658 1.00 23.61  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 228.524 254.566 249.982 1.00 32.20  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 228.191 254.744 251.157 1.00 41.95  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 230.946 254.514 249.399 1.00 25.95  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 231.303 255.552 250.464 1.00 35.42  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 231.666 254.874 251.775 1.00 31.94  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 232.440 256.441 249.984 1.00 32.21  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 227.880 255.140 248.965 1.00 26.17  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 226.748 256.032 249.169 1.00 29.03  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 225.416 255.436 248.744 1.00 34.66  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 224.378 255.855 249.266 1.00 40.05  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 226.962 257.346 248.406 1.00 28.82  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 228.120 258.164 248.920 1.00 34.00  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 228.094 258.710 250.196 1.00 31.31  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 229.242 258.382 248.135 1.00 35.91  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 229.152 259.456 250.672 1.00 32.07  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 230.305 259.126 248.603 1.00 32.42  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 230.254 259.660 249.872 1.00 37.94  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 231.310 260.403 250.343 1.00 51.78  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 225.418 254.482 247.826 1.00 43.07  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 224.200 253.890 247.310 1.00 36.29  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 224.044 254.148 245.822 1.00 43.01  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 224.749 254.958 245.218 1.00 46.57  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 223.090 253.429 245.236 1.00 49.32  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 222.835 253.535 243.809 1.00 52.01  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 221.335 253.592 243.566 1.00 47.54  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 220.540 253.072 244.354 1.00 50.28  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 223.456 252.365 243.033 1.00 55.74  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 223.283 252.573 241.626 1.00 55.30  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 222.809 251.046 243.433 1.00 50.62  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 220.958 254.244 242.471 1.00 53.50  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 219.575 254.321 242.023 1.00 50.96  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 219.418 253.409 240.815 1.00 59.42  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 220.188 253.511 239.854 1.00 57.95  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 219.190 255.759 241.674 1.00 54.07  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 217.707 256.129 241.761 1.00 56.73  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 217.085 255.583 243.034 1.00 56.47  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 217.530 257.636 241.681 1.00 54.49  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 218.436 252.520 240.869 1.00 74.43  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 218.252 251.554 239.794 1.00 67.87  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 217.827 252.270 238.518 1.00 72.66  ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 216.859 253.040 238.537 1.00 76.34  ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 217.212 250.508 240.187 1.00 65.55  ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 217.204 249.316 239.252 1.00 74.22  ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 218.156 248.510 239.306 1.00 75.30  ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 216.244 249.185 238.463 1.00 79.37  ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 218.526 252.063 237.400 1.00 77.24  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 218.128 252.737 236.154 1.00 77.04  ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 216.739 252.356 235.672 1.00 76.79  ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 216.062 253.183 235.049 1.00 74.43  ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 219.212 252.300 235.158 1.00 75.04  ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 219.762 251.031 235.722 1.00 73.51  ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 219.687 251.177 237.211 1.00 73.59  ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 216.292 251.129 235.941 1.00 83.92  ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 215.016 250.648 235.419 1.00 84.04  ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 213.873 250.861 236.410 1.00 81.02  ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 212.893 251.544 236.098 1.00 81.07  ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 215.135 249.167 235.044 1.00 81.91  ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 216.013 248.943 233.830 1.00 85.37  ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 215.941 249.687 232.852 1.00 86.20  ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 216.851 247.914 233.886 1.00 86.06  ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 213.985 250.281 237.606 1.00 78.96  ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 212.907 250.355 238.584 1.00 79.14  ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 212.957 251.613 239.442 1.00 78.58  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 212.013 251.855 240.202 1.00 80.83  ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 212.930 249.123 239.494 1.00 80.84  ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 214.279 248.834 239.880 1.00 78.80  ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 212.348 247.917 238.771 1.00 80.59  ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 214.022 252.411 239.335 1.00 64.89  ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 214.166 253.654 240.098 1.00 61.81  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 214.033 253.407 241.600 1.00 65.30  ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 213.368 254.158 242.316 1.00 69.36  ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 213.162 254.710 239.630 1.00 64.71  ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 213.139 254.917 238.124 1.00 68.31  ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 214.523 255.234 237.585 1.00 68.83  ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 215.054 256.479 238.127 1.00 67.24  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 216.264 256.952 237.865 1.00 65.81  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 217.104 256.303 237.076 1.00 63.94  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 216.642 258.105 238.410 1.00 65.84  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 214.665 252.341 242.079 1.00 66.75  ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 214.622 251.956 243.483 1.00 65.13  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 215.978 252.240 244.115 1.00 64.47  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 217.017 251.895 243.543 1.00 60.81  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 214.249 250.477 243.620 1.00 63.17  ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 213.941 250.004 245.034 1.00 69.45  ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 215.183 249.644 245.822 1.00 76.56  ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 216.187 249.235 245.201 1.00 74.35  ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 215.147 249.749 247.066 1.00 70.78  ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 215.965 252.864 245.291 1.00 47.18  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 217.193 253.280 245.956 1.00 43.98  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 217.706 252.181 246.876 1.00 46.94  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 216.974 251.692 247.742 1.00 48.22  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 216.969 254.568 246.751 1.00 42.57  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 218.179 255.012 247.519 1.00 44.40  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 218.382 254.905 248.864 1.00 43.06  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 219.363 255.614 246.982 1.00 46.31  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 219.613 255.413 249.199 1.00 40.18  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 220.237 255.853 248.061 1.00 40.56  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 219.768 255.977 245.694 1.00 44.91  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 221.489 256.439 247.892 1.00 42.44  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 221.011 256.557 245.529 1.00 45.26  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 221.856 256.783 246.621 1.00 44.05  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 218.969 251.807 246.690 1.00 46.60  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 219.653 250.847 247.546 1.00 42.69  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 220.727 251.591 248.326 1.00 44.35  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 221.575 252.262 247.731 1.00 50.31  ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 220.267 249.714 246.723 1.00 49.46  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 219.234 249.028 246.005 1.00 58.22  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 220.994 248.729 247.625 1.00 46.26  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 220.683 251.479 249.650 1.00 43.00  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 221.599 252.229 250.496 1.00 37.90  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 223.026 251.713 250.357 1.00 41.81  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 223.267 250.515 250.183 1.00 50.14  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 221.160 252.153 251.958 1.00 36.24  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 220.215 253.273 252.340 1.00 47.50  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 219.902 254.111 251.469 1.00 53.60  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 219.786 253.317 253.512 1.00 49.90  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 223.979 252.640 250.431 1.00 33.10  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 225.386 252.305 250.438 1.00 27.30  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 225.898 252.059 251.844 1.00 39.23  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 225.140 251.971 252.812 1.00 40.88  ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 227.223 251.945 251.949 1.00 39.43  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 227.837 251.682 253.247 1.00 30.86  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 227.653 252.862 254.194 1.00 40.63  ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 227.218 252.691 255.339 1.00 47.38  ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 229.319 251.353 253.068 1.00 25.03  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 230.074 250.959 254.338 1.00 32.14  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 229.334 249.860 255.080 1.00 43.59  ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 231.487 250.518 253.998 1.00 41.96  ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 227.980 254.072 253.733 1.00 36.65  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 227.822 255.249 254.581 1.00 31.95  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 226.351 255.568 254.822 1.00 37.99  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 225.963 255.931 255.938 1.00 48.52  ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 228.532 256.450 253.956 1.00 36.21  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 228.339 257.731 254.718 1.00 44.84  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 229.035 257.966 255.892 1.00 40.42  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 227.459 258.698 254.263 1.00 38.88  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 228.859 259.142 256.595 1.00 32.47  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 227.277 259.875 254.962 1.00 34.78  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 227.979 260.098 256.129 1.00 38.03  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 225.520 255.446 253.784 1.00 26.24  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 224.107 255.784 253.923 1.00 29.82  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 223.405 254.850 254.902 1.00 37.77  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 222.586 255.293 255.714 1.00 44.45  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 223.420 255.743 252.558 1.00 39.10  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 224.262 256.363 251.579 1.00 41.31  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 222.091 256.480 252.610 1.00 32.47  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 223.710 253.551 254.837 1.00 33.01  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 223.090 252.599 255.753 1.00 32.34  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 223.509 252.862 257.194 1.00 33.96  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 222.686 252.777 258.113 1.00 37.17  ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 223.443 251.170 255.342 1.00 42.93  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 223.216 250.156 256.419 1.00 46.32  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 221.963 249.682 256.743 1.00 45.18  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 224.082 249.523 257.245 1.00 38.66  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 222.067 248.802 257.723 1.00 42.68  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 223.343 248.687 258.046 1.00 39.63  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 224.788 253.175 257.412 1.00 36.81  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 225.269 253.450 258.764 1.00 27.26  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 224.617 254.714 259.313 1.00 35.83  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 224.156 254.749 260.460 1.00 41.37  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 226.805 253.554 258.775 1.00 29.39  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 227.290 254.181 260.072 1.00 31.28  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 227.430 252.182 258.576 1.00 35.81  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 224.569 255.771 258.498 1.00 34.88  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 223.963 257.021 258.944 1.00 26.42  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 222.467 256.860 259.182 1.00 33.86  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 221.924 257.395 260.156 1.00 42.52  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 224.230 258.127 257.923 1.00 33.03  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 223.690 259.515 258.276 1.00 41.07  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 224.425 260.086 259.478 1.00 33.42  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 223.796 260.453 257.085 1.00 30.88  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 221.781 256.128 258.300 1.00 29.06  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 220.342 255.937 258.454 1.00 29.34  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 220.020 255.115 259.696 1.00 39.73  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 219.009 255.362 260.364 1.00 45.73  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 219.764 255.273 257.206 1.00 29.41  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 218.248 255.285 257.142 1.00 37.59  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 217.739 254.343 256.064 1.00 40.62  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 218.263 254.687 254.747 1.00 38.69  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 217.844 255.712 254.018 1.00 36.19  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 216.883 256.515 254.442 1.00 37.73  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 218.401 255.934 252.831 1.00 26.96  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 220.860 254.128 260.014 1.00 47.46  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 220.636 253.323 261.210 1.00 29.79  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 220.734 254.172 262.472 1.00 32.00  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 219.934 254.012 263.401 1.00 44.56  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 221.636 252.167 261.257 1.00 26.42  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 221.616 251.375 262.553 1.00 37.41  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 222.611 250.228 262.512 1.00 37.42  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 222.208 249.185 261.485 1.00 43.82  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 220.903 248.552 261.820 1.00 42.02  ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 221.712 255.079 262.523 1.00 34.95  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 221.847 255.969 263.674 1.00 30.22  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 220.654 256.912 263.761 1.00 30.60  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 220.118 257.162 264.848 1.00 42.00  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 223.176 256.742 263.597 1.00 31.72  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 224.357 255.770 263.569 1.00 31.29  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 223.303 257.697 264.770 1.00 33.98  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 225.656 256.403 263.123 1.00 30.11  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 220.223 257.455 262.620 1.00 33.82  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 219.103 258.392 262.608 1.00 35.05  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 217.826 257.712 263.086 1.00 38.29  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 217.057 258.285 263.867 1.00 42.06  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 218.934 258.997 261.202 1.00 41.11  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 220.059 259.989 260.908 1.00 33.13  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 217.579 259.674 261.065 1.00 37.97  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 220.208 260.319 259.441 1.00 34.61  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 217.580 256.482 262.627 1.00 43.58  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 216.367 255.771 263.020 1.00 35.21  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 216.338 255.513 264.522 1.00 46.72  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 215.279 255.611 265.154 1.00 47.93  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 216.256 254.458 262.246 1.00 41.84  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 215.679 254.650 260.857 1.00 58.59  ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 215.251 255.780 260.540 1.00 50.53  ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 215.652 253.671 260.082 1.00 61.67  ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 217.492 255.183 265.107 1.00 48.83  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 217.621 254.956 266.548 1.00 39.75  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 216.671 253.864 267.034 1.00 50.96  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 216.025 253.995 268.075 1.00 56.37  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 217.405 256.250 267.335 1.00 39.66  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 217.478 256.017 268.730 1.00 46.74  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 216.580 252.775 266.266 1.00 50.12  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 215.779 251.634 266.688 1.00 50.32  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 216.349 250.995 267.947 1.00 55.79  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 215.588 250.572 268.825 1.00 57.61  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 215.674 250.603 265.548 1.00 52.13  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 214.846 249.404 265.982 1.00 48.47  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 215.077 251.247 264.307 1.00 54.85  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 217.675 250.927 268.066 1.00 57.29  ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 218.334 250.337 269.224 1.00 54.39  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 219.089 251.392 270.025 1.00 50.26  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 220.135 251.105 270.612 1.00 54.14  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 219.271 249.207 268.798 1.00 45.59  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 218.554 248.050 268.123 1.00 52.54  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 219.504 247.204 267.292 1.00 57.76  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 218.808 246.129 266.595 1.00 60.88  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 218.008 246.300 265.551 1.00 56.82  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 217.788 247.499 265.036 1.00 52.72  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 217.416 245.241 265.006 1.00 52.11  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 218.568 252.614 270.057 1.00 42.05  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 219.158 253.678 270.851 1.00 42.53  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 220.523 254.149 270.396 1.00 51.09  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 221.391 254.418 271.237 1.00 53.00  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 220.738 254.257 269.085 1.00 46.76  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 221.997 254.779 268.570 1.00 35.20  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 222.131 256.287 268.742 1.00 39.31  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 223.244 256.809 268.619 1.00 49.56  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 222.159 254.418 267.091 1.00 38.05  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 222.387 252.939 266.829 1.00 40.00  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 221.121 252.215 266.420 1.00 50.40  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 220.109 252.893 266.149 1.00 55.71  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 221.139 250.968 266.365 1.00 51.63  ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 221.036 256.996 269.018 1.00 38.06  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 221.094 258.438 269.217 1.00 38.56  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 221.557 258.828 270.613 1.00 44.78  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 221.891 259.998 270.831 1.00 52.57  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 219.725 259.064 268.939 1.00 38.45  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 219.368 259.275 267.467 1.00 39.66  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 218.092 260.091 267.335 1.00 38.19  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 220.514 259.942 266.727 1.00 37.95  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 221.586 257.889 271.556 1.00 47.25  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 222.069 258.147 272.905 1.00 47.01  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 223.542 257.808 273.074 1.00 48.87  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 224.074 257.945 274.179 1.00 49.53  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 221.238 257.360 273.923 1.00 44.63  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 219.744 257.356 273.641 1.00 50.31  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 219.185 258.750 273.436 1.00 55.38  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 218.581 259.043 272.404 1.00 54.56  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 219.382 259.618 274.421 1.00 51.30  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 224.209 257.372 272.011 1.00 42.56  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 225.611 256.990 272.048 1.00 38.06  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 226.435 257.935 271.184 1.00 46.52  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 225.926 258.571 270.257 1.00 52.88  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 225.795 255.547 271.567 1.00 37.07  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 225.154 254.506 272.467 1.00 48.66  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 225.481 253.098 271.999 1.00 48.05  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 224.680 252.733 270.761 1.00 48.48  ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 224.897 251.318 270.352 1.00 50.72  ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 227.723 258.022 271.502 1.00 37.74  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 228.653 258.852 270.740 1.00 29.67  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 229.063 258.077 269.494 1.00 38.23  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 229.821 257.108 269.570 1.00 45.67  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 229.858 259.229 271.593 1.00 29.91  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 231.029 259.797 270.810 1.00 34.39  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 232.093 260.354 271.741 1.00 41.62  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 231.664 261.586 272.393 1.00 40.74  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 231.431 261.703 273.693 1.00 36.78  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 231.568 260.675 274.515 1.00 42.75  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 231.050 262.880 274.180 1.00 32.40  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 228.553 258.499 268.341 1.00 29.78  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 228.795 257.818 267.075 1.00 28.23  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 229.886 258.555 266.310 1.00 35.31  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 229.761 259.756 266.045 1.00 48.96  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 227.513 257.743 266.246 1.00 34.63  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 226.289 257.299 267.029 1.00 27.84  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 226.224 255.796 267.209 1.00 33.26  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 225.798 255.302 268.253 1.00 46.20  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 226.646 255.060 266.190 1.00 32.45  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 230.949 257.837 265.956 1.00 27.33  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 232.077 258.395 265.216 1.00 25.90  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 232.257 257.588 263.937 1.00 31.68  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 232.621 256.409 263.987 1.00 47.06  ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 233.351 258.374 266.059 1.00 28.48  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 233.446 259.499 267.043 1.00 26.15  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 232.479 260.414 267.338 1.00 28.87  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 234.572 259.827 267.864 1.00 35.07  ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 232.933 261.293 268.291 1.00 30.29  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 234.216 260.954 268.631 1.00 33.61  ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 235.848 259.278 268.025 1.00 35.95  ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 235.088 261.541 269.544 1.00 32.13  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 236.712 259.863 268.932 1.00 35.38  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 236.328 260.982 269.679 1.00 32.33  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 232.006 258.222 262.794 1.00 23.00  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 232.168 257.581 261.493 1.00 27.61  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 233.544 257.979 260.969 1.00 32.22  ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 233.756 259.112 260.535 1.00 47.39  ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 231.052 257.972 260.524 1.00 32.28  ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 229.685 257.727 261.166 1.00 30.87  ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 231.180 257.191 259.226 1.00 30.57  ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 228.518 258.094 260.279 1.00 37.16  ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 234.483 257.038 261.007 1.00 33.91  ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 235.871 257.288 260.634 1.00 33.86  ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 236.100 256.782 259.218 1.00 33.73  ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 235.784 255.628 258.902 1.00 33.40  ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 236.841 256.617 261.621 1.00 22.37  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 238.266 257.071 261.353 1.00 28.42  ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 236.437 256.927 263.053 1.00 27.57  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 236.648 257.643 258.366 1.00 40.98  ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 236.996 257.300 256.990 1.00 22.61  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 238.506 257.099 256.931 1.00 32.98  ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 239.264 258.061 256.774 1.00 43.96  ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 236.539 258.387 256.022 1.00 31.36  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 235.075 258.335 255.700 1.00 31.07  ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 234.569 257.344 254.877 1.00 36.28  ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 234.205 259.279 256.217 1.00 22.86  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 233.223 257.295 254.578 1.00 41.26  ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 232.858 259.235 255.921 1.00 26.44  ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 232.367 258.241 255.100 1.00 36.42  ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 238.940 255.848 257.057 1.00 44.30  ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 240.360 255.501 257.066 1.00 36.05  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 240.735 255.087 255.646 1.00 34.14  ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 240.591 253.928 255.256 1.00 46.06  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 240.641 254.398 258.081 1.00 40.69  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 242.126 254.135 258.273 1.00 50.64  ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 242.940 254.608 257.453 1.00 49.65  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 242.482 253.455 259.258 1.00 50.12  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 241.220 256.048 254.871 1.00 29.59  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 241.623 255.775 253.507 1.00 40.26  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 241.939 257.061 252.777 1.00 43.07  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 241.919 258.155 253.350 1.00 43.98  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 242.233 256.905 251.490 1.00 42.77  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 242.560 258.048 250.650 1.00 37.66  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 241.319 258.892 250.379 1.00 42.34  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 240.190 258.395 250.371 1.00 47.67  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 243.172 257.581 249.331 1.00 43.19  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 244.554 256.985 249.509 1.00 51.35  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 245.035 256.927 250.661 1.00 59.43  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 245.160 256.573 248.498 1.00 42.80  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 241.540 260.184 250.159 1.00 40.12  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 240.470 261.143 249.907 1.00 41.38  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 240.685 261.756 248.530 1.00 47.00  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 241.750 262.322 248.254 1.00 47.67  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 240.417 262.231 250.991 1.00 32.59  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 239.574 263.405 250.524 1.00 41.12  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 239.854 261.661 252.279 1.00 39.94  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 239.678 261.641 247.670 1.00 44.98  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 239.670 262.297 246.374 1.00 36.33  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 238.309 262.935 246.130 1.00 43.23  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 237.318 262.539 246.750 1.00 52.37  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 240.038 261.315 245.243 1.00 37.91  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 239.009 260.207 245.025 1.00 51.30  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 237.920 260.223 245.623 1.00 54.91  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 239.308 259.290 244.233 1.00 58.58  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 238.235 263.943 245.254 1.00 37.91  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 236.958 264.664 245.092 1.00 39.70  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 235.818 263.805 244.569 1.00 44.22  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 234.654 264.208 244.675 1.00 48.25  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 237.316 265.792 244.111 1.00 45.13  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 238.579 265.351 243.450 1.00 37.44  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 239.320 264.574 244.485 1.00 36.24  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 236.112 262.637 243.995 1.00 41.59  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 235.045 261.813 243.433 1.00 41.98  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 234.090 261.315 244.513 1.00 47.17  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 232.872 261.279 244.301 1.00 52.53  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 235.637 260.642 242.652 1.00 46.32  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 236.402 261.065 241.410 1.00 50.43  ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 235.507 261.680 240.352 1.00 56.78  ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 234.328 261.278 240.259 1.00 59.54  ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 235.982 262.569 239.614 1.00 56.14  ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 234.615 260.927 245.676 1.00 40.00  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 233.766 260.409 246.742 1.00 33.85  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 233.581 261.379 247.901 1.00 33.78  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 232.542 261.325 248.567 1.00 33.66  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 234.327 259.082 247.282 1.00 28.37  ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 235.463 259.224 248.263 1.00 28.50  ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 236.793 259.135 247.990 1.00 25.55  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 235.361 259.441 249.678 1.00 40.86  ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 237.529 259.307 249.135 1.00 23.58  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 236.673 259.495 250.187 1.00 34.36  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 234.290 259.606 250.560 1.00 35.01  ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 236.941 259.709 251.535 1.00 31.20  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 234.559 259.816 251.898 1.00 28.49  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 235.873 259.862 252.373 1.00 30.44  ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 234.546 262.262 248.157 1.00 39.17  ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 234.486 263.099 249.351 1.00 31.56  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 233.589 264.322 249.180 1.00 39.90  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 233.107 264.867 250.184 1.00 45.80  ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 235.901 263.533 249.779 1.00 28.56  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 236.424 264.643 248.882 1.00 38.33  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 235.920 263.953 251.243 1.00 33.02  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 233.336 264.761 247.947 1.00 39.54  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 232.461 265.907 247.735 1.00 32.39  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 230.984 265.553 247.837 1.00 40.71  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 230.147 266.461 247.841 1.00 45.42  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 232.748 266.555 246.379 1.00 37.25  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 234.212 266.883 246.156 1.00 42.35  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 234.551 268.316 246.510 1.00 52.14  ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 233.629 269.158 246.530 1.00 56.22  ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 235.739 268.600 246.767 1.00 47.12  ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 230.643 264.265 247.914 1.00 40.58  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 229.276 263.883 248.243 1.00 34.25  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 228.941 264.190 249.695 1.00 43.56  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 227.759 264.246 250.050 1.00 53.85  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 229.057 262.398 247.958 1.00 32.32  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 229.024 262.090 246.476 1.00 40.41  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 229.982 262.361 245.753 1.00 48.27  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 227.918 261.519 246.015 1.00 41.67  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 229.954 264.389 250.535 1.00 28.61  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 229.778 264.776 251.926 1.00 30.89  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 229.876 266.282 252.124 1.00 26.61  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 229.972 266.740 253.266 1.00 40.15  ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 230.812 264.071 252.805 1.00 34.38  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 230.786 262.543 252.805 1.00 32.41  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 231.799 261.992 253.794 1.00 26.09  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 229.391 262.040 253.127 1.00 39.31  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 229.868 267.057 251.037 1.00 25.05  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 230.012 268.505 251.154 1.00 28.93  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 228.876 269.107 251.970 1.00 24.80  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 229.104 269.956 252.838 1.00 45.53  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 230.076 269.140 249.765 1.00 29.78  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 231.485 269.189 249.211 1.00 40.60  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 232.434 268.746 249.857 1.00 39.14  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 231.630 269.733 248.009 1.00 36.99  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 227.641 268.676 251.707 1.00 27.72  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 226.508 269.186 252.473 1.00 28.52  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 226.517 268.645 253.897 1.00 30.54  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 226.063 269.320 254.829 1.00 34.91  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 225.197 268.836 251.769 1.00 40.74  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 225.162 267.466 251.409 1.00 47.58  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 227.024 267.425 254.086 1.00 37.62  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 227.113 266.853 255.426 1.00 20.98  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 228.110 267.631 256.275 1.00 28.26  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 227.852 267.924 257.449 1.00 42.35  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 227.483 265.361 255.346 1.00 24.82  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 227.367 264.712 256.716 1.00 35.92  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 226.604 264.650 254.334 1.00 36.00  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 229.260 267.976 255.700 1.00 38.26  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 230.308 268.693 256.414 1.00 25.10  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 230.086 270.199 256.437 1.00 36.39  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 230.893 270.919 257.034 1.00 50.48  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 231.669 268.381 255.787 1.00 35.67  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 232.064 266.903 255.755 1.00 37.23  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 233.371 266.712 255.006 1.00 33.61  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 232.165 266.342 257.164 1.00 35.58  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 229.024 270.687 255.807 1.00 40.75  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 228.714 272.103 255.735 1.00 31.97  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 227.826 272.485 256.919 1.00 39.40  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 227.615 271.699 257.847 1.00 37.76  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 228.049 272.408 254.390 1.00 38.06  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 228.101 273.876 254.024 1.00 58.94  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 228.296 274.719 254.925 1.00 58.55  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 227.939 274.183 252.825 1.00 56.55  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 227.299 273.712 256.895 1.00 52.32  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 226.337 274.121 257.912 1.00 49.06  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 225.002 273.413 257.734 1.00 46.19  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 224.192 273.374 258.667 1.00 49.85  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 226.142 275.637 257.873 1.00 50.95  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 227.216 276.383 258.638 1.00 60.22  ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 228.135 275.725 259.172 1.00 58.18  ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 227.141 277.627 258.707 1.00 53.49  ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 224.751 272.858 256.545 1.00 42.62  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 223.506 272.134 256.310 1.00 34.76  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 223.421 270.884 257.176 1.00 42.32  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 222.354 270.570 257.717 1.00 49.68  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 223.382 271.769 254.830 1.00 29.28  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 223.375 272.987 253.928 1.00 49.87  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 222.438 273.784 253.951 1.00 55.71  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 224.423 273.136 253.127 1.00 46.21  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 224.535 270.165 257.323 1.00 37.84  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 224.579 268.906 258.068 1.00 33.52  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 223.524 267.936 257.543 1.00 34.81  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 222.682 267.424 258.283 1.00 45.45  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 224.411 269.151 259.568 1.00 30.38  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 225.595 269.845 260.217 1.00 37.35  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 225.382 270.021 261.710 1.00 40.21  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 224.214 270.950 261.993 1.00 42.35  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 224.468 272.329 261.493 1.00 39.35  ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 223.580 267.685 256.237 1.00 28.22  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 222.519 266.983 255.530 1.00 24.25  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 223.123 266.119 254.436 1.00 28.15  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 223.974 266.587 253.674 1.00 44.72  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 221.527 267.985 254.929 1.00 31.00  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 220.129 267.523 254.531 1.00 34.21  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 219.344 267.065 255.741 1.00 41.46  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 219.412 268.659 253.838 1.00 30.99  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 222.686 264.864 254.359 1.00 26.35  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 223.113 263.953 253.302 1.00 25.51  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 222.011 263.880 252.252 1.00 31.30  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 220.976 263.241 252.472 1.00 40.91  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 223.427 262.570 253.866 1.00 28.62  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 223.862 261.522 252.839 1.00 34.34  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 225.275 261.795 252.347 1.00 34.18  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 223.753 260.120 253.415 1.00 33.82  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 222.232 264.528 251.113 1.00 29.09  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 221.242 264.575 250.046 1.00 37.40  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 221.537 263.490 249.019 1.00 39.36  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 222.671 263.364 248.546 1.00 44.52  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 221.232 265.948 249.376 1.00 35.99  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 222.418 266.106 248.591 1.00 45.85  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 221.182 267.044 250.427 1.00 34.16  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 220.517 262.715 248.680 1.00 37.97  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 220.619 261.602 247.754 1.00 35.17  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 219.908 261.922 246.445 1.00 38.90  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 219.001 262.760 246.407 1.00 45.30  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 220.016 260.337 248.379 1.00 36.01  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 220.607 259.905 249.722 1.00 31.09  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 219.895 258.669 250.246 1.00 37.19  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 222.100 259.653 249.594 1.00 31.97  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 220.302 261.277 245.341 1.00 41.45  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 219.672 261.581 244.045 1.00 39.61  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 218.183 261.277 243.988 1.00 38.75  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 217.496 261.833 243.121 1.00 51.41  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 220.455 260.706 243.054 1.00 39.33  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 221.118 259.664 243.891 1.00 40.68  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 221.414 260.324 245.198 1.00 35.89  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 217.661 260.423 244.866 1.00 42.17  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 216.232 260.137 244.878 1.00 39.70  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 215.425 261.180 245.641 1.00 47.22  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 214.260 260.923 245.961 1.00 53.11  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 215.974 258.748 245.469 1.00 42.96  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 216.265 258.681 246.953 1.00 48.15  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 217.369 258.991 247.394 1.00 48.85  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 215.272 258.270 247.733 1.00 53.80  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 216.008 262.341 245.937 1.00 37.28  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 215.306 263.408 246.615 1.00 39.48  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 215.272 263.310 248.123 1.00 48.82  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 214.707 264.201 248.770 1.00 54.06  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 215.858 262.269 248.706 1.00 47.39  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 215.826 262.070 250.147 1.00 42.24  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 217.031 262.732 250.803 1.00 43.61  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 218.153 262.651 250.296 1.00 47.33  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 215.795 260.577 250.478 1.00 40.41  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 216.309 260.228 251.863 1.00 49.58  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 216.227 258.745 252.157 1.00 53.61  ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 216.205 258.379 253.349 1.00 51.73  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 216.184 257.948 251.197 1.00 53.47  ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 216.789 263.390 251.936 1.00 45.00  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 217.830 264.082 252.686 1.00 39.74  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 217.876 263.516 254.097 1.00 43.07  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 216.828 263.291 254.712 1.00 50.56  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 217.578 265.594 252.707 1.00 37.62  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 216.239 266.001 253.301 1.00 44.32  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 215.873 267.426 252.921 1.00 47.92  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 215.772 267.582 251.475 1.00 44.91  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 216.558 268.361 250.745 1.00 44.58  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 217.503 269.102 251.297 1.00 42.09  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 216.388 268.400 249.428 1.00 50.13  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 219.084 263.270 254.600 1.00 30.94  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 219.286 262.701 255.929 1.00 31.30  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 220.022 263.720 256.793 1.00 30.32  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 221.183 264.046 256.527 1.00 36.37  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 220.064 261.389 255.852 1.00 30.20  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 219.449 260.223 255.074 1.00 29.72  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 219.825 260.279 253.601 1.00 39.90  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 219.872 258.897 255.686 1.00 30.85  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 219.348 264.216 257.826 1.00 37.13  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 219.962 265.183 258.725 1.00 35.28  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 220.981 264.504 259.630 1.00 30.62  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 220.717 263.447 260.209 1.00 41.73  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 218.894 265.880 259.567 1.00 40.37  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 217.918 266.493 258.743 1.00 48.92  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 222.150 265.121 259.753 1.00 28.25  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 223.203 264.576 260.599 1.00 25.73  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 222.842 264.779 262.065 1.00 37.14  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 222.609 265.920 262.481 1.00 38.58  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 224.537 265.242 260.288 1.00 31.82  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 225.765 264.678 261.005 1.00 27.92  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 226.265 263.425 260.307 1.00 32.80  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 226.864 265.724 261.087 1.00 31.36  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 222.772 263.720 262.870 1.00 31.48  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 222.441 263.899 264.278 1.00 23.07  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 223.540 264.656 264.995 1.00 34.24  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 224.721 264.590 264.606 1.00 42.18  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 222.316 262.459 264.797 1.00 29.48  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 222.087 261.627 263.578 1.00 35.45  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 222.868 262.300 262.498 1.00 34.97  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 223.196 265.399 266.051 1.00 41.11  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 224.220 266.169 266.778 1.00 37.34  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 225.278 265.311 267.454 1.00 35.60  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 226.355 265.831 267.771 1.00 42.91  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 223.402 266.955 267.811 1.00 29.70  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 222.137 266.174 267.967 1.00 37.61  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 221.851 265.602 266.612 1.00 37.89  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 225.013 264.027 267.686 1.00 27.84  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 225.960 263.140 268.346 1.00 39.91  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 226.857 262.391 267.369 1.00 40.26  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 227.656 261.556 267.802 1.00 41.24  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 225.215 262.136 269.231 1.00 38.58  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 224.430 261.120 268.425 1.00 34.17  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 223.584 261.480 267.608 1.00 42.67  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 224.708 259.843 268.652 1.00 37.20  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 226.748 262.667 266.073 1.00 37.41  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 227.510 261.962 265.048 1.00 28.89  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 228.620 262.873 264.546 1.00 40.46  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 228.375 264.036 264.204 1.00 45.53  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 226.602 261.513 263.890 1.00 21.04  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 227.427 260.875 262.784 1.00 32.26  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 225.546 260.548 264.394 1.00 31.73  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 229.841 262.345 264.504 1.00 39.60  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 231.000 263.060 263.991 1.00 34.45  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 231.547 262.317 262.781 1.00 32.11  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 231.725 261.095 262.828 1.00 41.32  ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 232.087 263.193 265.061 1.00 33.47  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 231.655 263.942 266.308 1.00 29.70  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 231.484 265.424 266.031 1.00 29.53  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 231.289 266.189 267.256 1.00 32.50  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 230.117 266.367 267.850 1.00 31.04  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 229.005 265.850 267.353 1.00 36.70  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 230.058 267.081 268.969 1.00 32.16  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 231.810 263.051 261.706 1.00 33.83  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 232.414 262.497 260.501 1.00 31.96  ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 233.909 262.776 260.578 1.00 30.11  ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 234.339 263.933 260.510 1.00 40.03  ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 231.797 263.093 259.229 1.00 37.06  ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 230.274 262.953 259.260 1.00 32.30  ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 232.373 262.419 257.994 1.00 35.29  ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 229.792 261.521 259.241 1.00 35.52  ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 234.704 261.721 260.716 1.00 25.37  ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 236.139 261.839 260.923 1.00 24.61  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 236.886 261.204 259.759 1.00 28.70  ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 236.476 260.163 259.238 1.00 34.81  ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 236.557 261.179 262.240 1.00 31.16  ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 236.019 261.881 263.476 1.00 30.27  ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 236.453 261.043 265.010 1.00 53.83  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 238.210 261.370 265.088 1.00 48.59  ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 237.980 261.842 259.352 1.00 25.10  ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 238.834 261.350 258.280 1.00 22.01  ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 240.229 261.102 258.832 1.00 24.72  ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 240.807 261.978 259.484 1.00 39.94  ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 238.900 262.345 257.115 1.00 23.61  ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 237.569 262.631 256.477 1.00 23.82  ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 236.701 263.556 257.032 1.00 27.91  ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 237.191 261.983 255.315 1.00 31.89  ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 235.482 263.824 256.446 1.00 24.15  ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 235.971 262.249 254.725 1.00 26.28  ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 235.116 263.170 255.291 1.00 29.34  ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 240.765 259.914 258.575 1.00 34.89  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 242.130 259.559 258.958 1.00 39.36  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 242.916 259.335 257.671 1.00 40.22  ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 242.792 258.287 257.032 1.00 51.57  ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 242.147 258.326 259.856 1.00 32.14  ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 243.483 258.075 260.532 1.00 26.44  ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 243.571 256.697 261.152 1.00 40.44  ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 242.641 256.318 261.894 1.00 49.75  ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 244.571 255.992 260.902 1.00 45.48  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 243.726 260.325 257.295 1.00 31.03  ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 244.423 260.324 256.018 1.00 33.36  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 245.902 260.596 256.250 1.00 39.17  ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 246.312 261.099 257.298 1.00 43.44  ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 243.840 261.365 255.039 1.00 35.76  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 242.394 261.044 254.726 1.00 42.83  ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 243.964 262.763 255.620 1.00 34.39  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 246.706 260.248 255.246 1.00 42.86  ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 248.134 260.528 255.274 1.00 37.97  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 248.519 261.766 254.477 1.00 44.02  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 249.600 262.319 254.707 1.00 48.59  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 248.925 259.323 254.748 1.00 35.26  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 248.519 258.868 253.358 1.00 47.26  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 249.432 257.786 252.814 1.00 58.40  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 250.527 257.565 253.330 1.00 53.16  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 248.983 257.104 251.767 1.00 50.09  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 247.668 262.212 253.556 1.00 43.56  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 247.944 263.401 252.763 1.00 44.21  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 246.642 263.929 252.180 1.00 47.15  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 245.614 263.246 252.187 1.00 50.48  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 248.982 263.118 251.664 1.00 50.32  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 248.546 262.027 250.689 1.00 56.66  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 247.337 261.742 250.564 1.00 58.80  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 249.437 261.439 250.041 1.00 53.32  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 246.699 265.161 251.685 1.00 41.23  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 245.573 265.818 251.033 1.00 41.58  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 245.981 266.363 249.671 1.00 52.01  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 245.540 267.436 249.252 1.00 53.36  ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 245.013 266.936 251.907 1.00 46.69  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 244.077 266.531 253.044 1.00 34.97  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 243.524 267.774 253.714 1.00 39.91  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 242.959 265.641 252.530 1.00 34.59  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 246.835 265.622 248.964 1.00 51.22  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 247.384 266.120 247.707 1.00 50.88  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 246.315 266.205 246.624 1.00 52.31  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 246.395 267.057 245.731 1.00 56.65  ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 248.545 265.229 247.261 1.00 47.61  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 249.228 265.676 245.978 1.00 56.57  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 250.449 264.823 245.677 1.00 60.50  ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 250.057 263.436 245.201 1.00 61.26  ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 251.241 262.632 244.792 1.00 55.60  ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 245.301 265.343 246.687 1.00 48.54  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 244.262 265.304 245.667 1.00 49.32  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 242.948 265.935 246.108 1.00 53.81  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 242.085 266.181 245.259 1.00 55.25  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 244.009 263.857 245.229 1.00 44.27  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 245.203 263.214 244.564 1.00 53.03  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 245.562 263.551 243.266 1.00 50.86  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 245.977 262.279 245.236 1.00 51.39  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 246.653 262.970 242.653 1.00 51.47  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 247.071 261.692 244.631 1.00 48.18  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 247.405 262.041 243.340 1.00 51.76  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 248.494 261.460 242.733 1.00 52.64  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 242.770 266.202 247.399 1.00 49.21  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 241.533 266.809 247.868 1.00 40.41  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 241.468 268.277 247.464 1.00 41.54  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 242.470 268.996 247.504 1.00 48.97  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 241.416 266.677 249.385 1.00 36.94  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 240.277 268.719 247.072 1.00 35.58  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 240.072 270.105 246.684 1.00 33.21  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 239.837 270.976 247.916 1.00 37.60  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 239.643 270.489 249.033 1.00 39.23  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 238.894 270.226 245.717 1.00 30.43  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 237.706 269.727 246.343 1.00 43.35  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 239.164 269.433 244.449 1.00 38.20  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 239.856 272.293 247.698 1.00 42.82  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 239.641 273.235 248.790 1.00 35.24  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 238.210 273.201 249.310 1.00 40.38  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 237.951 273.701 250.410 1.00 47.06  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 240.002 274.652 248.337 1.00 35.00  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 240.180 275.712 249.426 1.00 41.03  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 241.570 275.625 250.036 1.00 42.31  ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 239.921 277.103 248.872 1.00 41.30  ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 237.277 272.622 248.549 1.00 44.98  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 235.893 272.546 249.002 1.00 34.97  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 235.755 271.695 250.257 1.00 33.17  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 234.907 271.981 251.109 1.00 39.50  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 235.004 271.995 247.887 1.00 37.25  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 236.573 270.652 250.390 1.00 24.58  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 236.501 269.772 251.549 1.00 34.73  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 237.521 270.120 252.622 1.00 32.47  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 237.279 269.849 253.804 1.00 44.63  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 236.692 268.316 251.119 1.00 38.24  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 238.006 268.145 250.573 1.00 42.59  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 235.661 267.941 250.070 1.00 41.96  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 238.659 270.705 252.241 1.00 38.66  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 239.647 271.125 253.230 1.00 37.98  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 239.067 272.207 254.132 1.00 43.26  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 239.254 272.185 255.355 1.00 48.20  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 240.936 271.598 252.532 1.00 40.16  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 241.935 272.117 253.552 1.00 39.02  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 241.542 270.466 251.718 1.00 29.22  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 238.351 273.167 253.545 1.00 37.00  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 237.735 274.241 254.312 1.00 27.97  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 236.560 273.772 255.159 1.00 35.94  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 236.139 274.505 256.060 1.00 36.70  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 237.271 275.352 253.368 1.00 26.71  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 236.346 274.858 252.415 1.00 34.73  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 236.027 272.579 254.901 1.00 38.21  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 234.827 272.101 255.573 1.00 34.92  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 235.111 271.321 256.849 1.00 43.16  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 234.163 270.946 257.547 1.00 38.06  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 234.013 271.216 254.624 1.00 32.72  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 233.027 271.969 253.754 1.00 31.45  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 232.243 271.007 252.879 1.00 30.66  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 230.999 271.593 252.396 1.00 42.75  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 230.921 272.486 251.420 1.00 44.05  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 231.999 272.910 250.782 1.00 38.62  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 229.730 272.964 251.072 1.00 39.74  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 236.376 271.067 257.174 1.00 44.05  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 236.730 270.201 258.289 1.00 32.70  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 237.710 270.903 259.215 1.00 33.86  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 238.386 271.855 258.815 1.00 46.08  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 237.344 268.886 257.795 1.00 35.86  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 236.213 267.835 256.861 1.00 49.55  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 237.764 270.438 260.460 1.00 35.41  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 238.814 270.875 261.366 1.00 33.25  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 239.987 269.914 261.310 1.00 32.18  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 239.849 268.723 261.614 1.00 41.77  ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 241.149 270.425 260.918 1.00 30.06  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 242.327 269.606 260.670 1.00 34.56  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 243.180 269.511 261.926 1.00 32.91  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 243.414 270.518 262.603 1.00 45.92  ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 243.160 270.175 259.519 1.00 35.42  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 242.593 269.904 258.136 1.00 36.67  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 241.138 270.897 257.765 1.00 83.40  ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 241.876 272.505 257.489 1.00 42.88  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 243.634 268.299 262.233 1.00 28.92  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 244.637 268.054 263.262 1.00 35.58  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 245.803 267.348 262.586 1.00 33.97  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 245.615 266.308 261.943 1.00 42.87  ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 244.083 267.216 264.425 1.00 30.22  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 245.125 267.083 265.523 1.00 30.87  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 242.807 267.837 264.968 1.00 34.45  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 247.001 267.908 262.728 1.00 28.77  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 248.179 267.425 262.020 1.00 25.98  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 249.008 266.550 262.951 1.00 36.45  ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 249.385 266.982 264.045 1.00 50.55  ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 249.011 268.593 261.492 1.00 35.05  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 250.382 268.200 261.040 1.00 41.91  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 251.557 268.426 261.694 1.00 37.39  ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 250.723 267.508 259.832 1.00 36.72  ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 252.608 267.920 260.969 1.00 39.49  ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 252.122 267.350 259.822 1.00 37.94  ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 249.981 267.008 258.759 1.00 30.74  ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 252.794 266.714 258.781 1.00 36.11  ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 250.650 266.376 257.727 1.00 32.22  ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 252.041 266.234 257.746 1.00 31.73  ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 249.290 265.325 262.514 1.00 16.83  ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 250.087 264.364 263.274 1.00 21.85  ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 251.416 264.166 262.552 1.00 34.15  ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 251.518 263.343 261.638 1.00 50.15  ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 249.350 263.037 263.427 1.00 29.45  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 248.222 263.072 264.417 1.00 25.69  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 247.013 263.663 264.092 1.00 31.54  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 248.369 262.504 265.671 1.00 26.64  ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 245.974 263.690 265.001 1.00 28.59  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 247.333 262.529 266.583 1.00 33.55  ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 246.135 263.123 266.248 1.00 32.53  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 252.433 264.917 262.962 1.00 42.43  ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 253.761 264.713 262.408 1.00 38.93  ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 254.350 263.401 262.921 1.00 45.93  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 253.954 262.877 263.964 1.00 54.25  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 254.679 265.882 262.765 1.00 46.60  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 254.919 265.936 264.160 1.00 53.55  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 255.305 262.862 262.161 1.00 55.42  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 255.950 261.617 262.564 1.00 52.07  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 256.762 261.761 263.843 1.00 56.34  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 257.029 260.750 264.501 1.00 58.67  ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 256.843 261.094 261.438 1.00 57.59  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 256.084 260.348 260.354 1.00 62.45  ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 256.876 259.195 259.774 1.00 66.23  ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 257.214 258.262 260.533 1.00 63.23  ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 257.159 259.218 258.557 1.00 57.73  ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 257.159 262.980 264.209 1.00 57.02  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 257.847 263.209 265.472 1.00 52.85  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 256.906 263.184 266.668 1.00 54.01  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 257.382 263.133 267.807 1.00 54.18  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 258.591 264.546 265.430 1.00 55.15  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 259.767 264.528 264.474 1.00 64.25  ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 260.354 263.444 264.272 1.00 68.89  ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 260.106 265.597 263.925 1.00 65.33  ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 255.592 263.228 266.438 1.00 51.12  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 254.635 263.113 267.536 1.00 47.80  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 254.764 261.754 268.210 1.00 50.45  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 254.789 261.653 269.443 1.00 50.84  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 253.205 263.363 267.022 1.00 40.46  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 252.181 262.896 268.035 1.00 46.73  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 253.007 264.836 266.701 1.00 46.08  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 254.855 260.691 267.416 1.00 45.32  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 255.084 259.340 267.922 1.00 39.35  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 256.566 259.029 267.742 1.00 44.10  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 257.014 258.698 266.642 1.00 51.08  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 254.202 258.331 267.195 1.00 43.25  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 254.521 256.848 267.400 1.00 44.17  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 254.072 256.382 268.772 1.00 42.17  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 253.881 256.006 266.310 1.00 48.57  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 257.329 259.147 268.825 1.00 43.83  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 258.752 258.862 268.765 1.00 38.88  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 258.996 257.356 268.770 1.00 37.01  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 258.118 256.555 269.104 1.00 47.72  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 259.488 259.524 269.930 1.00 44.68  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 258.847 259.256 271.163 1.00 46.67  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 260.215 256.976 268.381 1.00 48.40  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 260.557 255.561 268.273 1.00 47.24  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 260.523 254.862 269.627 1.00 47.57  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 260.070 253.715 269.717 1.00 55.09  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 261.934 255.404 267.629 1.00 48.40  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 261.970 256.134 266.397 1.00 57.33  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 262.222 253.941 267.343 1.00 46.80  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 260.991 255.529 270.685 1.00 43.16  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 261.004 254.906 272.005 1.00 42.76  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 259.596 254.615 272.507 1.00 42.24  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 259.402 253.691 273.305 1.00 53.24  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 261.754 255.796 272.997 1.00 48.54  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 261.301 257.240 272.941 1.00 57.61  ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 261.609 257.923 271.942 1.00 53.67  ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 260.637 257.693 273.895 1.00 59.72  ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 258.605 255.392 272.064 1.00 35.01  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 257.220 255.086 272.405 1.00 37.97  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 256.786 253.762 271.790 1.00 46.50  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 256.066 252.980 272.421 1.00 53.02  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 256.303 256.218 271.946 1.00 40.64  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 256.614 257.558 272.585 1.00 45.15  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 255.570 258.889 271.967 1.00 54.69  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 253.966 258.099 271.987 1.00 37.32  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 257.211 253.498 270.553 1.00 45.20  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 256.906 252.222 269.915 1.00 34.34  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 257.649 251.088 270.609 1.00 37.52  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 257.123 249.977 270.749 1.00 50.68  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 257.239 252.288 268.414 1.00 36.80  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 256.771 253.621 267.828 1.00 36.46  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 256.600 251.124 267.675 1.00 45.47  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 257.167 253.829 266.387 1.00 40.06  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 258.884 251.345 271.046 1.00 42.12  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 259.634 250.337 271.789 1.00 39.94  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 258.947 250.000 273.105 1.00 41.29  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 258.897 248.832 273.508 1.00 54.75  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 261.061 250.822 272.041 1.00 44.28  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 261.920 250.849 270.811 1.00 42.85  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 261.557 250.139 269.679 1.00 40.17  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 263.093 251.585 270.787 1.00 42.94  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 262.347 250.163 268.548 1.00 44.97  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 263.887 251.612 269.659 1.00 48.50  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 263.513 250.901 268.538 1.00 48.23  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 258.420 251.014 273.796 1.00 40.29  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 257.710 250.772 275.046 1.00 38.56  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 256.461 249.931 274.817 1.00 44.53  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 256.149 249.039 275.615 1.00 49.84  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 257.347 252.101 275.709 1.00 39.80  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 258.560 252.843 276.228 1.00 47.46  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 259.678 252.329 276.196 1.00 53.61  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 258.347 254.062 276.709 1.00 45.54  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 255.728 250.207 273.736 1.00 40.95  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 254.521 249.442 273.439 1.00 35.77  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 254.850 247.979 273.167 1.00 44.97  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 254.151 247.075 273.639 1.00 50.71  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 253.790 250.061 272.247 1.00 35.68  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 252.490 249.352 271.927 1.00 41.61  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 252.310 248.826 270.830 1.00 46.30  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 251.574 249.334 272.888 1.00 42.97  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 255.914 247.726 272.401 1.00 41.07  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 256.296 246.351 272.098 1.00 34.49  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 256.726 245.605 273.355 1.00 45.63  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 256.351 244.444 273.556 1.00 48.63  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 257.414 246.337 271.055 1.00 39.02  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 258.224 245.070 271.047 1.00 42.49  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 257.644 243.862 270.693 1.00 40.97  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 259.564 245.087 271.393 1.00 34.37  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 258.387 242.697 270.685 1.00 36.30  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 260.311 243.925 271.387 1.00 37.94  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 259.721 242.729 271.032 1.00 35.65  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 257.516 246.255 274.213 1.00 42.94  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 257.987 245.597 275.428 1.00 36.01  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 256.849 245.368 276.415 1.00 49.13  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 256.798 244.326 277.078 1.00 60.38  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 259.102 246.422 276.070 1.00 40.36  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 260.453 246.385 275.353 1.00 42.66  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 261.391 247.443 275.911 1.00 47.25  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 261.079 245.003 275.449 1.00 41.62  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 255.932 246.332 276.533 1.00 45.48  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 254.810 246.177 277.453 1.00 35.68  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 253.902 245.029 277.033 1.00 40.23  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 253.448 244.246 277.876 1.00 50.80  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 254.019 247.482 277.542 1.00 40.21  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 253.619 244.915 275.733 1.00 42.42  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 252.791 243.815 275.249 1.00 43.85  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 253.494 242.476 275.426 1.00 46.20  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 252.850 241.466 275.733 1.00 49.43  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 252.426 244.039 273.782 1.00 44.96  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 251.523 245.234 273.537 1.00 43.84  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 251.288 245.446 272.052 1.00 40.90  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 250.602 244.315 271.440 1.00 47.47  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 249.286 244.155 271.427 1.00 49.59  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 248.476 245.043 271.981 1.00 48.20  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 248.768 243.079 270.842 1.00 43.46  ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 254.814 242.445 275.224 1.00 45.42  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 255.560 241.201 275.376 1.00 46.84  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 255.526 240.705 276.817 1.00 48.44  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 255.384 239.502 277.065 1.00 57.02  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 257.002 241.397 274.910 1.00 44.86  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 257.834 240.129 274.716 1.00 50.27  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 257.275 239.289 273.579 1.00 44.19  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 259.288 240.481 274.461 1.00 45.96  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 255.655 241.618 277.782 1.00 48.82  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 255.670 241.224 279.185 1.00 49.61  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 254.287 240.854 279.706 1.00 51.05  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 254.183 240.293 280.801 1.00 56.25  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 256.252 242.348 280.042 1.00 41.17  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 257.742 242.569 279.855 1.00 47.75  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 258.214 243.799 280.612 1.00 53.06  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 259.665 243.838 280.741 1.00 55.48  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 260.428 244.833 280.309 1.00 58.22  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 259.908 245.895 279.716 1.00 50.50  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 261.745 244.761 280.477 1.00 56.47  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 253.229 241.152 278.955 1.00 50.91  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 251.863 240.944 279.417 1.00 49.17  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 251.105 239.900 278.610 1.00 51.10  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 250.570 238.947 279.184 1.00 59.81  ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 251.097 242.273 279.390 1.00 48.65  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 251.689 243.221 280.260 1.00 51.42  ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 251.043 240.053 277.293 1.00 54.38  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 250.239 239.183 276.439 1.00 59.38  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 251.066 237.944 276.108 1.00 57.42  ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 252.122 238.075 275.469 1.00 56.26  ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 249.799 239.903 275.160 1.00 56.97  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 249.168 241.255 275.498 1.00 56.83  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 248.826 239.040 274.372 1.00 54.30  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 248.797 242.073 274.283 1.00 55.49  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 250.640 236.750 276.515 1.00 65.11  ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 251.353 235.537 276.105 1.00 60.70  ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 251.219 235.297 274.610 1.00 62.73  ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 250.205 235.627 273.990 1.00 65.46  ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 250.667 234.425 276.911 1.00 62.53  ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 249.877 235.130 277.977 1.00 61.90  ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 249.501 236.452 277.395 1.00 63.64  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 252.267 234.711 274.030 1.00 65.35  ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 252.271 234.465 272.592 1.00 66.67  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 251.394 233.276 272.218 1.00 68.75  ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 250.759 233.283 271.157 1.00 67.27  ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 253.703 234.249 272.102 1.00 64.99  ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 254.550 235.516 271.974 1.00 60.65  ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 255.964 235.172 271.543 1.00 64.57  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 253.910 236.492 271.000 1.00 57.27  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 251.352 232.245 273.066 1.00 83.38  ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 250.540 231.072 272.760 1.00 83.62  ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 249.053 231.411 272.748 1.00 83.94  ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 248.308 230.919 271.892 1.00 83.10  ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 250.837 229.950 273.757 1.00 82.39  ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 250.409 230.292 275.171 1.00 87.10  ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 250.400 231.492 275.518 1.00 88.58  ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 250.082 229.361 275.937 1.00 87.88  ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 248.607 232.248 273.679 1.00 84.29  ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 247.206 232.652 273.744 1.00 85.94  ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 247.037 233.914 274.583 1.00 84.44  ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 247.692 234.085 275.611 0.00 85.67  ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 246.345 231.524 274.316 1.00 88.84  ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 244.847 231.740 274.154 1.00 87.74  ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 244.384 231.583 272.718 1.00 90.89  ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 244.521 232.548 271.936 1.00 93.18  ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 243.882 230.494 272.370 1.00 86.25  ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 252.118 231.537 283.554 1.00 74.07  ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 252.290 230.787 282.315 1.00 79.30  ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 253.764 230.670 281.948 1.00 79.39  ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 254.490 231.664 281.960 1.00 81.77  ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 251.514 231.450 281.176 1.00 76.92  ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 251.566 230.663 279.998 1.00 75.53  ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 254.210 229.449 281.632 1.00 80.14  ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 255.615 229.275 281.227 1.00 79.06  ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 255.982 230.063 279.982 1.00 79.12  ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 257.115 230.548 279.872 1.00 82.48  ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 255.728 227.760 281.004 1.00 79.95  ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 254.331 227.308 280.735 1.00 78.75  ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 253.448 228.192 281.563 1.00 78.51  ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 255.051 230.201 279.035 1.00 74.76  ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 255.315 231.014 277.851 1.00 71.16  ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 255.487 232.482 278.217 1.00 69.22  ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 256.366 233.166 277.680 1.00 71.86  ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 254.187 230.843 276.834 1.00 70.73  ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 254.480 231.458 275.477 1.00 73.44  ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 256.183 231.202 274.945 1.00 89.15  ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 256.022 231.458 273.181 1.00 73.26  ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 254.650 232.987 279.127 1.00 62.54  ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 254.767 234.378 279.550 1.00 63.50  ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 256.084 234.626 280.274 1.00 65.05  ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 256.710 235.677 280.097 1.00 72.51  ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 253.586 234.756 280.443 1.00 65.08  ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 253.328 236.253 280.626 1.00 63.05  ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 253.454 236.988 279.300 1.00 63.02  ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 251.963 236.493 281.252 1.00 62.04  ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 256.518 233.667 281.095 1.00 59.33  ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 257.766 233.826 281.834 1.00 62.22  ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 258.946 233.942 280.877 1.00 65.98  ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 259.874 234.726 281.109 1.00 67.87  ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 257.953 232.645 282.788 1.00 63.63  ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 259.177 232.706 283.695 1.00 68.02  ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 259.456 234.101 284.224 1.00 68.71  ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 260.347 234.797 283.742 1.00 66.35  ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 258.684 234.518 285.220 1.00 67.38  ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 258.921 233.172 279.786 1.00 68.78  ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 259.961 233.277 278.766 1.00 67.13  ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 259.948 234.664 278.136 1.00 71.03  ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 261.002 235.279 277.929 1.00 68.35  ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 259.778 232.171 277.709 1.00 64.38  ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 260.175 230.810 278.285 1.00 66.86  ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 260.583 232.482 276.457 1.00 64.44  ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 259.418 229.647 277.679 1.00 67.60  ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 258.756 235.179 277.826 1.00 66.70  ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 258.649 236.508 277.233 1.00 55.62  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 259.173 237.581 278.180 1.00 59.55  ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 259.865 238.512 277.752 1.00 67.34  ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 257.197 236.791 276.851 1.00 51.53  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 256.714 236.018 275.638 1.00 57.84  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 255.211 236.089 275.467 1.00 57.37  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 254.543 235.068 275.309 1.00 65.75  ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 254.669 237.301 275.500 1.00 54.12  ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 258.848 237.471 279.470 1.00 60.11  ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 259.318 238.457 280.439 1.00 55.84  ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 260.836 238.421 280.582 1.00 58.99  ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 261.478 239.472 280.684 1.00 62.96  ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 258.640 238.234 281.790 1.00 55.26  ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 257.131 238.408 281.750 1.00 57.46  ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 256.604 239.003 283.045 1.00 63.84  ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 255.166 239.237 282.988 1.00 65.73  ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 254.275 238.622 283.754 1.00 63.05  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 254.639 237.726 284.656 1.00 62.24  ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 252.985 238.914 283.610 1.00 58.49  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 261.426 237.223 280.604 1.00 57.19  ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 262.883 237.126 280.642 1.00 56.44  ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 263.505 237.679 279.367 1.00 64.76  ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 264.528 238.373 279.416 1.00 68.41  ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 263.313 235.676 280.860 1.00 66.02  ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 262.974 235.169 282.245 1.00 72.89  ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 262.935 235.990 283.186 1.00 72.70  ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 262.752 233.949 282.395 1.00 71.56  ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 262.905 237.376 278.213 1.00 62.03  ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 263.426 237.888 276.949 1.00 54.49  ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 263.321 239.406 276.881 1.00 56.09  ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 264.234 240.077 276.387 1.00 59.79  ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 262.686 237.244 275.777 1.00 56.36  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 262.210 239.965 277.368 1.00 53.43  ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 262.045 241.415 277.357 1.00 49.16  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 263.065 242.094 278.262 1.00 53.01  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 263.539 243.195 277.956 1.00 60.02  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 260.624 241.786 277.773 1.00 50.07  ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 263.407 241.459 279.386 1.00 59.43  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 264.427 242.015 280.269 1.00 60.53  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 265.786 242.056 279.582 1.00 58.08  ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 266.544 243.021 279.743 1.00 57.01  ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 264.504 241.201 281.561 1.00 58.32  ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 263.188 241.039 282.106 1.00 58.25  ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 265.384 241.904 282.583 1.00 56.93  ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 266.113 241.016 278.813 1.00 52.42  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 267.389 240.985 278.105 1.00 57.10  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 267.416 242.037 277.001 1.00 63.30  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 268.438 242.698 276.780 1.00 62.82  ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 267.656 239.573 277.553 1.00 55.53  ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 267.718 238.558 278.695 1.00 57.08  ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 268.948 239.545 276.754 1.00 56.05  ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 267.502 237.129 278.253 1.00 57.16  ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 266.298 242.214 276.296 1.00 56.00  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 266.227 243.174 275.202 1.00 53.78  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 265.989 244.603 275.671 1.00 55.51  ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 265.994 245.515 274.837 1.00 62.08  ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 265.121 242.777 274.222 1.00 48.79  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 265.389 241.485 273.476 1.00 54.66  ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 264.098 241.083 272.286 1.00 69.74  ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 262.785 240.548 273.378 1.00 50.07  ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 265.772 244.818 276.968 1.00 54.89  ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 265.500 246.167 277.461 1.00 53.85  ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 266.639 247.147 277.200 1.00 57.04  ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 266.359 248.263 276.728 1.00 56.03  ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 265.145 246.107 278.951 1.00 55.14  ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 264.828 247.460 279.564 1.00 58.39  ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 263.603 248.104 278.948 1.00 60.73  ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 262.490 247.593 279.070 1.00 56.38  ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 263.802 249.234 278.278 1.00 59.30  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 267.911 246.831 277.482 1.00 56.85  ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 268.972 247.817 277.207 1.00 52.00  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 269.070 248.225 275.747 1.00 50.03  ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 269.381 249.387 275.459 1.00 52.07  ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 270.246 247.100 277.675 1.00 50.63  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 269.775 246.112 278.672 1.00 55.57  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 268.454 245.637 278.156 1.00 55.21  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 268.817 247.305 274.815 1.00 56.91  ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 268.932 247.634 273.399 1.00 55.67  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 267.749 248.451 272.896 1.00 57.52  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 267.908 249.253 271.969 1.00 56.33  ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 269.075 246.354 272.575 1.00 52.70  ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 270.211 245.464 273.027 1.00 57.09  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 271.532 245.817 272.786 1.00 52.11  ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 269.964 244.275 273.699 1.00 51.54  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 272.574 245.010 273.197 1.00 52.08  ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 270.999 243.460 274.115 1.00 51.24  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 272.302 243.833 273.861 1.00 57.61  ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 273.337 243.025 274.273 1.00 61.67  ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 266.568 248.268 273.483 1.00 57.88  ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 265.368 248.979 273.043 1.00 51.58  ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 265.190 250.279 273.830 1.00 55.15  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 264.170 250.529 274.471 1.00 59.85  ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 264.145 248.078 273.170 1.00 49.06  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 263.966 247.139 272.014 1.00 45.39  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 263.734 247.628 270.740 1.00 49.12  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 264.035 245.770 272.198 1.00 51.78  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 263.571 246.770 269.673 1.00 53.27  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 263.872 244.906 271.134 1.00 55.72  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 263.640 245.407 269.870 1.00 54.34  ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 266.222 251.117 273.765 1.00 60.88  ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 266.210 252.432 274.384 1.00 60.27  ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 266.602 253.477 273.350 1.00 65.22  ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 267.078 253.152 272.259 1.00 72.85  ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 267.162 252.512 275.589 1.00 59.28  ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 268.511 252.303 275.151 1.00 57.99  ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 266.800 251.468 276.634 1.00 57.29  ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 266.389 254.741 273.705 1.00 71.52  ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 266.800 255.836 272.838 1.00 71.05  ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 268.312 255.819 272.656 1.00 70.74  ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 269.055 255.433 273.560 1.00 68.57  ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 266.349 257.176 273.421 1.00 70.88  ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 264.936 257.252 273.485 1.00 69.81  ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 268.755 256.207 271.457 1.00 74.52  ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 270.158 256.224 271.030 1.00 75.92  ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 270.866 254.887 271.258 1.00 77.19  ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 272.100 254.831 271.296 1.00 77.60  ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 270.932 257.404 271.661 1.00 76.93  ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 271.318 257.200 273.137 1.00 81.20  ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 271.567 256.091 273.609 1.00 79.88  ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 271.364 258.306 273.870 1.00 78.10  ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 270.107 253.801 271.378 1.00 68.21  ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 270.669 252.483 271.579 1.00 62.10  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 271.021 251.806 270.270 1.00 65.51  ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 271.121 252.436 269.215 1.00 70.08  ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 271.216 250.488 270.351 1.00 61.16  ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 271.616 249.721 269.175 1.00 57.93  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 270.528 249.732 268.108 1.00 53.78  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 270.805 249.954 266.924 1.00 56.55  ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 271.958 248.286 269.578 1.00 55.37  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 272.012 247.261 268.443 1.00 59.97  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 273.206 247.520 267.537 1.00 54.41  ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 272.051 245.845 268.997 1.00 60.81  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 269.278 249.492 268.510 1.00 55.25  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 268.190 249.418 267.540 1.00 53.96  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 267.941 250.780 266.904 1.00 56.95  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 267.717 250.881 265.692 1.00 58.57  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 266.918 248.861 268.204 1.00 52.22  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 265.832 248.638 267.164 1.00 46.03  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 267.227 247.571 268.945 1.00 54.30  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 267.967 251.845 267.708 1.00 59.45  ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 267.739 253.184 267.173 1.00 54.64  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 268.844 253.585 266.204 1.00 55.35  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 268.576 254.142 265.133 1.00 57.02  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 267.632 254.195 268.315 1.00 58.30  ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 266.785 253.669 269.344 1.00 60.91  ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 267.053 255.507 267.811 1.00 59.43  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 270.100 253.310 266.565 1.00 59.65  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 271.213 253.644 265.681 1.00 55.95  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 271.170 252.817 264.402 1.00 59.61  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 271.442 253.332 263.312 1.00 63.90  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 272.542 253.444 266.408 1.00 58.04  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 272.864 254.532 267.419 1.00 63.47  ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 274.282 254.396 267.945 1.00 63.40  ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 274.351 253.402 269.091 1.00 66.27  ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 275.700 253.374 269.721 1.00 62.82  ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 270.837 251.529 264.518 1.00 63.97  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 270.706 250.691 263.330 1.00 54.77  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 269.557 251.163 262.449 1.00 55.79  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 269.659 251.139 261.217 1.00 61.47  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 270.509 249.231 263.736 1.00 49.02  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 268.451 251.587 263.065 1.00 56.65  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 267.325 252.107 262.296 1.00 49.95  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 267.710 253.368 261.532 1.00 59.22  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 267.342 253.530 260.363 1.00 64.54  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 266.141 252.380 263.225 1.00 53.72  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 264.836 252.855 262.584 1.00 55.17  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 264.043 251.684 262.031 1.00 54.10  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 264.005 253.640 263.586 1.00 59.34  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 268.450 254.274 262.177 1.00 67.61  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 268.850 255.511 261.513 1.00 66.57  ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 269.784 255.237 260.341 1.00 69.17  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 269.665 255.867 259.283 1.00 71.07  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 269.513 256.456 262.516 1.00 65.51  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 268.579 256.968 263.600 1.00 72.07  ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 267.492 257.874 263.054 1.00 80.56  ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 267.749 258.580 262.057 1.00 76.32  ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 266.380 257.878 263.623 1.00 80.95  ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 270.724 254.306 260.511 1.00 63.50  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 271.661 253.994 259.436 1.00 61.98  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 270.956 253.329 258.260 1.00 65.51  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 271.315 253.565 257.100 1.00 70.91  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 272.784 253.102 259.961 1.00 62.65  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 273.923 252.938 259.004 1.00 65.98  ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 274.855 253.928 258.780 1.00 64.60  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 274.281 251.898 258.213 1.00 66.55  ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 275.737 253.506 257.892 1.00 63.59  ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 275.412 252.278 257.532 1.00 66.70  ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 269.956 252.488 258.538 1.00 59.22  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 269.262 251.779 257.468 1.00 53.26  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 268.504 252.731 256.552 1.00 59.28  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 268.314 252.427 255.369 1.00 71.50  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 268.310 250.741 258.057 1.00 57.26  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 268.058 253.876 257.074 1.00 61.30  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 267.365 254.847 256.236 1.00 59.53  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 268.283 255.459 255.187 1.00 65.16  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 267.812 255.818 254.102 1.00 65.18  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 266.751 255.948 257.101 1.00 58.16  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 265.354 255.646 257.562 1.00 68.28  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 265.134 254.926 258.724 1.00 64.78  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 264.260 256.080 256.833 1.00 68.17  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 263.851 254.645 259.150 1.00 61.02  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 262.973 255.802 257.254 1.00 62.08  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 262.769 255.084 258.414 1.00 61.94  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 269.578 255.589 255.483 1.00 68.96  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 270.520 256.100 254.495 1.00 66.12  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 270.690 255.143 253.322 1.00 68.76  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 270.777 255.589 252.173 1.00 66.66  ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 271.873 256.377 255.152 1.00 66.69  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 271.862 257.553 256.114 1.00 70.06  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 272.947 257.458 257.168 1.00 74.60  ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 273.996 256.854 256.942 1.00 75.24  ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 272.701 258.057 258.327 1.00 68.99  ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 270.745 253.840 253.587 1.00 66.88  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 270.792 252.857 252.518 1.00 62.65  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 269.470 252.842 251.755 1.00 65.45  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 268.390 253.010 252.327 1.00 66.87  ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 271.081 251.465 253.080 1.00 59.78  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 272.179 251.348 254.138 1.00 63.39  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 272.231 249.936 254.699 1.00 57.57  ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 273.527 251.750 253.565 1.00 65.55  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 269.562 252.639 250.445 1.00 60.01  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 268.373 252.534 249.614 1.00 60.51  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 267.948 251.076 249.501 1.00 61.50  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 268.776 250.161 249.522 1.00 50.20  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 268.599 253.128 248.219 1.00 58.52  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 269.470 252.302 247.288 1.00 60.80  ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 270.921 252.727 247.310 1.00 65.16  ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 271.312 253.473 248.232 1.00 61.72  ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 271.669 252.325 246.394 1.00 63.80  ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 266.639 250.869 249.395 1.00 56.67  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 266.056 249.538 249.379 1.00 41.21  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 265.209 249.374 248.127 1.00 42.03  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 264.968 250.330 247.385 1.00 46.90  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 265.211 249.288 250.635 1.00 43.67  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 265.891 249.692 251.905 1.00 51.37  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 266.501 248.785 252.745 1.00 52.32  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 266.064 250.908 252.475 1.00 44.57  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 267.018 249.425 253.778 1.00 46.90  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 266.768 250.714 253.639 1.00 46.09  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 264.759 248.139 247.896 1.00 39.99  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 263.938 247.863 246.724 1.00 45.78  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 262.587 248.561 246.819 1.00 48.71  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 261.941 248.801 245.793 1.00 49.52  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 263.775 246.344 246.532 1.00 42.28  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 263.311 246.037 245.109 1.00 42.76  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 262.801 245.769 247.551 1.00 40.45  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 264.337 246.392 244.058 1.00 40.37  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 262.148 248.902 248.028 1.00 49.02  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 260.934 249.673 248.244 1.00 46.30  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 261.214 250.751 249.281 1.00 55.01  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 262.172 250.664 250.053 1.00 57.74  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 259.768 248.784 248.698 1.00 35.98  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 259.294 247.804 247.639 1.00 47.71  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 258.102 246.609 248.265 1.00 65.67  ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 257.025 246.443 246.846 1.00 42.74  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 260.370 251.782 249.278 1.00 54.78  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 260.546 252.896 250.200 1.00 50.20  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 260.497 252.409 251.643 1.00 53.67  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 259.600 251.654 252.028 1.00 61.24  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 259.470 253.954 249.961 1.00 51.11  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 259.824 254.898 248.829 1.00 62.34  ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 260.990 254.881 248.381 1.00 64.65  ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 258.937 255.659 248.388 1.00 59.89  ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 261.469 252.845 252.439 1.00 50.15  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 261.583 252.390 253.815 1.00 49.96  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 260.700 253.221 254.736 1.00 57.15  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 260.643 254.449 254.627 1.00 57.74  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 263.034 252.467 254.287 1.00 50.32  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 263.399 251.533 255.442 1.00 51.16  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 263.312 250.084 254.994 1.00 53.00  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 264.777 251.852 255.997 1.00 52.81  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 260.011 252.539 255.646 1.00 54.84  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 259.227 253.185 256.686 1.00 45.45  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 259.641 252.621 258.036 1.00 48.03  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 260.104 251.481 258.135 1.00 58.84  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 257.718 252.991 256.473 1.00 53.49  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 257.430 251.600 256.298 1.00 56.31  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 257.250 253.759 255.246 1.00 54.64  ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 259.481 253.439 259.078 1.00 41.86  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 259.947 253.046 260.404 1.00 39.73  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 259.186 251.834 260.929 1.00 41.09  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 259.784 250.924 261.515 1.00 46.89  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 259.819 254.223 261.371 1.00 40.01  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 260.045 253.863 262.830 1.00 42.69  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 259.790 255.056 263.735 1.00 44.84  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 258.455 255.609 263.543 1.00 52.71  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 257.989 256.679 264.173 1.00 49.69  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 258.728 257.342 265.048 1.00 48.04  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 256.752 257.094 263.919 1.00 41.04  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 257.868 251.797 260.722 1.00 44.23  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 257.070 250.717 261.293 1.00 39.32  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 257.229 249.411 260.523 1.00 39.94  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 257.042 248.335 261.101 1.00 54.15  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 255.599 251.120 261.358 1.00 43.44  ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 255.260 252.128 262.455 1.00 37.94  ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 253.767 252.361 262.515 1.00 44.13  ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 255.780 251.643 263.798 1.00 34.56  ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 257.554 249.475 259.230 1.00 40.06  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 257.795 248.245 258.481 1.00 35.94  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 258.995 247.495 259.043 1.00 41.59  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 258.962 246.269 259.197 1.00 47.21  ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 258.001 248.552 256.997 1.00 36.64  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 258.208 247.304 256.150 1.00 40.02  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 258.011 247.574 254.667 1.00 45.91  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 258.979 248.525 254.136 1.00 50.39  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 260.062 248.183 253.452 1.00 44.50  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 260.361 246.916 253.220 1.00 48.52  ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 260.865 249.136 252.989 1.00 45.26  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 260.070 248.221 259.356 1.00 38.52  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 261.229 247.592 259.978 1.00 37.55  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 260.919 247.158 261.404 1.00 47.04  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 261.273 246.047 261.814 1.00 51.00  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 262.417 248.551 259.957 1.00 36.09  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 263.014 248.945 258.304 1.00 69.78  ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 260.262 248.025 262.178 1.00 43.21  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 259.923 247.680 263.554 1.00 34.35  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 258.913 246.541 263.606 1.00 25.48  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 259.043 245.624 264.424 1.00 45.19  ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 259.389 248.909 264.287 1.00 39.66  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 260.413 250.004 264.596 1.00 35.57  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 259.869 250.975 265.633 1.00 39.98  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 261.730 249.399 265.059 1.00 29.41  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 257.900 246.581 262.738 1.00 19.04  ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 256.918 245.509 262.716 1.00 28.26  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 257.526 244.169 262.351 1.00 44.09  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 257.184 243.141 262.941 1.00 40.08  ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 258.430 244.160 261.369 1.00 49.16  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 259.152 242.936 261.039 1.00 34.94  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 260.054 242.503 262.188 1.00 32.42  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 260.152 241.309 262.494 1.00 43.79  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 259.969 243.138 259.764 1.00 31.76  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 260.818 242.030 259.524 1.00 40.29  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 260.727 243.461 262.830 1.00 35.29  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 261.626 243.129 263.930 1.00 27.85  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 260.865 242.546 265.114 1.00 33.38  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 261.308 241.566 265.723 1.00 47.13  ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 262.411 244.370 264.355 1.00 27.95  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 263.310 244.234 265.584 1.00 34.64  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 264.493 243.331 265.284 1.00 39.05  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 263.782 245.599 266.053 1.00 39.93  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 259.716 243.135 265.455 1.00 33.89  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 258.942 242.645 266.592 1.00 27.11  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 258.411 241.240 266.339 1.00 32.53  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 258.398 240.403 267.249 1.00 48.00  ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 257.794 243.606 266.904 1.00 27.43  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 258.241 244.997 267.260 1.00 32.80  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 259.512 245.228 267.760 1.00 34.93  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 257.388 246.075 267.092 1.00 36.74  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 259.923 246.507 268.085 1.00 34.30  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 257.793 247.355 267.416 1.00 32.67  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 259.062 247.571 267.913 1.00 33.77  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 257.961 240.964 265.112 1.00 34.93  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 257.462 239.630 264.791 1.00 37.10  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 258.571 238.590 264.876 1.00 40.18  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 258.345 237.467 265.343 1.00 48.59  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 256.829 239.628 263.400 1.00 42.33  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 257.822 239.602 262.390 1.00 48.28  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 259.776 238.941 264.420 1.00 40.95  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 260.898 238.011 264.495 1.00 34.27  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 261.267 237.704 265.941 1.00 41.78  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 261.594 236.560 266.274 1.00 52.81  ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 262.101 238.577 263.742 1.00 25.60  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 261.995 238.465 262.231 1.00 38.99  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 263.601 238.495 261.414 1.00 42.92  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 264.080 236.776 261.557 1.00 40.58  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 261.225 238.715 266.812 1.00 38.62  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 261.537 238.493 268.220 1.00 36.64  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 260.491 237.608 268.885 1.00 42.55  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 260.809 236.850 269.809 1.00 49.91  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 261.657 239.831 268.946 1.00 37.74  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 262.802 240.721 268.462 1.00 39.53  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 262.728 242.092 269.107 1.00 35.77  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 264.143 240.061 268.739 1.00 37.34  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 259.236 237.698 268.439 1.00 44.07  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 258.210 236.790 268.940 1.00 38.94  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 258.529 235.348 268.568 1.00 44.09  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 258.270 234.425 269.348 1.00 54.83  ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 256.838 237.194 268.400 1.00 46.15  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 256.342 238.503 268.930 1.00 45.93  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 255.191 239.104 268.468 1.00 39.15  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 256.840 239.326 269.882 1.00 44.18  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 255.001 240.241 269.113 1.00 45.42  ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 255.988 240.400 269.976 1.00 50.38  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 259.087 235.135 267.373 1.00 49.02  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 259.501 233.794 266.977 1.00 48.31  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 260.630 233.284 267.864 1.00 52.83  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 260.704 232.085 268.159 1.00 65.11  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 259.928 233.790 265.510 1.00 50.04  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 260.161 232.406 264.926 1.00 49.52  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 258.970 231.487 265.106 1.00 57.91  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 257.829 231.872 264.850 1.00 58.85  ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 259.229 230.261 265.546 1.00 56.16  ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 261.524 234.179 268.292 1.00 41.89  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 262.600 233.780 269.192 1.00 45.29  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 262.049 233.268 270.516 1.00 51.63  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 262.550 232.280 271.065 1.00 61.77  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 263.554 234.950 269.425 1.00 46.14  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 261.021 233.933 271.048 1.00 56.77  ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 260.381 233.451 272.267 1.00 52.55  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 259.731 232.091 272.044 1.00 51.30  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 259.804 231.210 272.908 1.00 60.34  ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 259.352 234.468 272.757 1.00 54.01  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 260.055 236.054 273.264 1.00 64.97  ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 259.086 231.904 270.889 1.00 51.23  ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 258.501 230.605 270.572 1.00 53.86  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 259.580 229.545 270.396 1.00 52.89  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 259.369 228.372 270.726 1.00 60.73  ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 257.638 230.709 269.315 1.00 50.43  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 256.406 231.583 269.477 1.00 53.88  ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 255.652 231.717 268.166 1.00 57.50  ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 254.689 232.811 268.195 1.00 56.90  ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 253.456 232.712 268.672 1.00 60.61  ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 252.998 231.577 269.173 1.00 55.30  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 252.663 233.779 268.645 1.00 58.30  ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 260.742 229.937 269.866 1.00 49.75  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 261.851 228.998 269.740 1.00 50.23  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 262.328 228.524 271.106 1.00 55.25  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 262.661 227.346 271.283 1.00 64.32  ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 263.000 229.644 268.966 1.00 52.63  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 262.730 229.722 267.478 1.00 56.96  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 261.798 229.098 266.970 1.00 60.98  ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 263.546 230.492 266.768 1.00 51.96  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 262.377 229.432 272.083 1.00 62.52  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 262.766 229.054 273.439 1.00 58.98  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 261.742 228.099 274.040 1.00 52.78  ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 262.099 227.111 274.693 1.00 58.35  ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 262.952 230.310 274.309 1.00 58.30  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 263.183 229.926 275.762 1.00 53.81  ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 264.104 231.150 273.782 1.00 57.92  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 260.453 228.379 273.829 1.00 59.94  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 259.409 227.498 274.343 1.00 56.70  ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 259.496 226.113 273.716 1.00 63.87  ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 259.289 225.101 274.396 1.00 68.83  ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 258.033 228.115 274.096 1.00 53.82  ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 259.793 226.047 272.415 1.00 70.73  ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 259.966 224.755 271.760 1.00 64.97  ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 261.152 223.996 272.341 1.00 64.64  ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 261.082 222.778 272.541 1.00 70.13  ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 260.140 224.949 270.254 1.00 67.66  ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 260.240 223.651 269.470 1.00 69.98  ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 260.353 223.881 267.976 1.00 73.78  ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 260.396 225.020 267.513 1.00 75.68  ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 260.404 222.795 267.213 1.00 69.22  ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 262.254 224.700 272.612 1.00 65.32  ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 263.417 224.053 273.212 1.00 68.85  ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 263.094 223.519 274.601 1.00 70.30  ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 263.533 222.423 274.970 1.00 73.83  ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 264.589 225.034 273.268 1.00 69.44  ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 265.839 224.474 273.911 1.00 70.13  ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 266.779 223.781 273.159 1.00 72.07  ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 266.080 224.637 275.269 1.00 70.81  ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 267.922 223.269 273.740 1.00 72.50  ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 267.221 224.128 275.859 1.00 71.44  ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 268.138 223.445 275.090 1.00 71.08  ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 269.275 222.936 275.674 1.00 72.39  ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 262.336 224.284 275.390 1.00 73.33  ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 261.941 223.818 276.715 1.00 70.44  ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 261.068 222.573 276.623 1.00 73.81  ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 261.218 221.640 277.420 1.00 80.16  ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 261.213 224.931 277.468 1.00 71.97  ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 262.166 225.907 278.129 1.00 73.30  ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 263.383 225.806 277.973 1.00 73.48  ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 261.616 226.858 278.874 1.00 72.75  ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 260.142 222.546 275.662 1.00 73.76  ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 259.325 221.355 275.458 1.00 73.05  ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 260.174 220.176 274.999 1.00 74.19  ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 259.954 219.037 275.428 1.00 74.50  ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 258.215 221.645 274.448 1.00 72.47  ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 261.151 220.430 274.125 1.00 77.42  ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 262.016 219.361 273.640 1.00 76.57  ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 262.993 218.877 274.704 1.00 78.98  ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 263.528 217.771 274.577 1.00 80.10  ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 262.785 219.829 272.403 1.00 73.80  ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 261.916 219.882 271.163 1.00 78.90  ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 261.035 219.044 270.972 1.00 79.25  ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 262.160 220.871 270.312 1.00 80.29  ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 263.237 219.674 275.742 1.00 82.10  ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 264.115 219.299 276.850 1.00 81.31  ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 263.374 219.533 278.160 1.00 85.00  ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 263.669 220.483 278.896 1.00 86.96  ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 265.423 220.091 276.813 1.00 83.60  ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 266.238 219.864 275.577 1.00 86.68  ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 265.789 220.192 274.316 1.00 84.10  ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 267.477 219.344 275.411 1.00 85.42  ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 266.714 219.882 273.426 1.00 81.17  ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 267.749 219.366 274.064 1.00 84.55  ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 262.390 218.686 278.477 1.00 90.67  ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 261.612 218.898 279.710 1.00 92.24  ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 262.450 218.850 280.975 1.00 93.62  ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 262.159 219.584 281.927 1.00 90.72  ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 260.581 217.759 279.674 1.00 90.66  ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 260.548 217.304 278.246 1.00 89.08  ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 261.942 217.491 277.743 1.00 88.92  ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 263.483 218.007 281.016 1.00 104.58 ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 264.300 217.891 282.218 1.00 106.42 ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 265.255 219.066 282.384 1.00 104.59 ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 265.518 219.488 283.516 1.00 102.08 ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 265.086 216.579 282.193 1.00 106.58 ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 265.751 216.274 283.521 1.00 107.53 ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 265.028 216.111 284.526 1.00 105.56 ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 266.997 216.198 283.560 1.00 105.69 ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 265.779 219.606 281.285 1.00 101.85 ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 266.773 220.678 281.324 1.00 102.74 ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 266.298 221.845 280.470 1.00 102.72 ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 266.602 221.918 279.272 1.00 101.32 ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 268.138 220.178 280.854 1.00 101.93 ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 268.834 219.293 281.848 1.00 102.63 ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 269.128 219.756 283.119 1.00 101.64 ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 269.193 217.999 281.510 1.00 101.59 ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 269.769 218.944 284.036 1.00 100.98 ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 269.834 217.183 282.423 1.00 100.83 ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 270.122 217.656 283.687 1.00 100.98 ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 265.554 222.777 281.051 1.00 94.49  ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 265.130 223.971 280.317 1.00 94.28  ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 266.265 224.989 280.258 1.00 93.78  ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 267.313 224.827 280.881 1.00 93.75  ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 263.940 224.493 281.131 1.00 90.85  ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 263.970 223.753 282.449 1.00 89.19  ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 265.135 222.812 282.461 1.00 90.90  ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 266.038 226.048 279.484 1.00 79.38  ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 267.049 227.084 279.321 1.00 76.48  ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 267.311 227.802 280.639 1.00 77.85  ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 266.402 228.013 281.446 1.00 80.55  ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 266.611 228.095 278.262 1.00 78.18  ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 266.940 227.696 276.838 1.00 80.19  ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 267.233 229.132 275.789 1.00 78.22  ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 267.231 228.370 274.170 1.00 77.19  ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 268.568 228.177 280.851 1.00 82.33  ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 268.969 228.968 282.001 1.00 83.96  ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 269.029 230.443 281.612 1.00 81.85  ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 268.770 230.824 280.469 1.00 82.97  ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 270.314 228.482 282.545 1.00 85.06  ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 270.293 227.060 283.080 1.00 84.98  ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 269.370 226.902 284.271 1.00 84.68  ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 269.319 227.762 285.150 1.00 83.42  ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 268.633 225.798 284.307 1.00 81.15  ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 269.373 231.285 282.586 1.00 80.74  ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 269.483 232.716 282.325 1.00 81.37  ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 270.679 233.002 281.424 1.00 78.28  ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 270.601 233.821 280.501 1.00 79.89  ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 269.570 233.497 283.648 1.00 85.74  ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 268.275 233.337 284.447 1.00 84.12  ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 269.854 234.968 283.387 1.00 81.93  ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 267.034 233.744 283.683 1.00 80.83  ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 271.802 232.325 281.677 1.00 78.17  ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 273.020 232.594 280.919 1.00 79.18  ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 272.861 232.206 279.453 1.00 80.66  ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 273.327 232.926 278.562 1.00 81.97  ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 274.198 231.854 281.556 1.00 80.14  ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 275.575 232.314 281.096 1.00 82.11  ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 276.032 231.638 279.820 1.00 85.10  ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 275.610 230.491 279.566 1.00 84.64  ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 276.825 232.253 279.077 1.00 82.14  ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 272.208 231.073 279.183 1.00 74.02  ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 271.986 230.663 277.799 1.00 73.09  ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 270.960 231.557 277.114 1.00 72.11  ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 271.091 231.866 275.924 1.00 73.04  ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 271.540 229.202 277.746 1.00 73.80  ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 271.296 228.682 276.337 1.00 73.87  ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 271.271 227.169 276.267 1.00 76.91  ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 270.280 226.572 275.844 1.00 71.67  ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 272.364 226.539 276.678 1.00 78.90  ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 269.929 231.978 277.850 1.00 73.61  ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 268.892 232.820 277.261 1.00 68.51  ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 269.456 234.162 276.815 1.00 67.21  ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 269.057 234.695 275.773 1.00 70.39  ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 267.750 233.019 278.256 1.00 66.93  ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 266.435 233.533 277.668 1.00 64.57  ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 265.993 232.656 276.512 1.00 64.72  ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 265.361 233.587 278.738 1.00 66.58  ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 270.378 234.729 277.596 1.00 63.41  ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 270.985 236.002 277.220 1.00 67.01  ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 271.759 235.877 275.914 1.00 71.00  ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 271.693 236.761 275.053 1.00 74.78  ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 271.896 236.500 278.342 1.00 68.94  ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 271.159 236.910 279.606 1.00 73.40  ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 272.096 237.398 280.693 1.00 77.06  ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 273.156 237.965 280.355 1.00 77.11  ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 271.772 237.217 281.885 1.00 76.00  ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 272.504 234.781 275.750 1.00 65.34  ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 273.281 234.589 274.529 1.00 65.21  ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 272.373 234.446 273.314 1.00 61.20  ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 272.607 235.071 272.272 1.00 61.13  ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 274.183 233.363 274.669 1.00 64.61  ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 275.505 233.635 275.360 1.00 66.36  ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 276.034 232.380 276.024 1.00 63.80  ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 275.919 231.215 275.155 1.00 66.29  ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 275.567 230.005 275.568 1.00 68.39  ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 275.289 229.762 276.838 1.00 66.13  ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 275.492 229.015 274.683 1.00 68.29  ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 271.330 233.621 273.427 1.00 56.15  ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 270.443 233.395 272.291 1.00 52.24  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 269.661 234.653 271.935 1.00 58.80  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 269.518 234.989 270.754 1.00 69.57  ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 269.488 232.241 272.590 1.00 46.36  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 268.488 231.983 271.486 1.00 49.29  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 268.909 231.619 270.215 1.00 53.78  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 267.124 232.107 271.714 1.00 57.64  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 268.001 231.384 269.202 1.00 54.31  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 266.208 231.873 270.707 1.00 58.71  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 266.653 231.512 269.453 1.00 59.30  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 265.747 231.279 268.444 1.00 60.46  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 269.148 235.361 272.942 1.00 56.86  ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 268.303 236.522 272.677 1.00 49.92  ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 269.125 237.671 272.103 1.00 55.81  ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 268.706 238.331 271.144 1.00 57.68  ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 267.557 236.936 273.959 1.00 53.44  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 266.421 235.954 274.253 1.00 56.00  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 267.013 238.344 273.831 1.00 54.52  ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 265.453 235.778 273.104 1.00 53.28  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 270.303 237.930 272.676 1.00 57.21  ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 271.143 239.018 272.183 1.00 53.24  ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 271.603 238.758 270.754 1.00 58.97  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 271.609 239.668 269.917 1.00 65.91  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 272.345 239.215 273.107 1.00 53.42  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 272.013 239.893 274.426 1.00 60.77  ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 273.196 239.931 275.372 1.00 65.33  ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 274.324 240.208 274.964 1.00 62.41  ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 272.945 239.649 276.645 1.00 64.77  ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 271.999 237.518 270.456 1.00 56.93  ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 272.450 237.195 269.107 1.00 54.94  ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 271.292 237.209 268.117 1.00 48.60  ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 271.441 237.681 266.984 1.00 50.74  ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 273.150 235.837 269.098 1.00 55.50  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 274.546 235.859 269.691 1.00 52.21  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 274.988 234.468 270.110 1.00 58.54  ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 276.379 234.439 270.545 1.00 62.47  ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 276.810 234.887 271.716 1.00 58.51  ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 275.983 235.417 272.601 1.00 55.71  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 278.105 234.800 272.007 1.00 58.50  ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 270.131 236.688 268.523 1.00 40.56  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 268.968 236.714 267.643 1.00 39.88  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 268.502 238.137 267.370 1.00 42.69  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 268.010 238.425 266.274 1.00 53.89  ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 267.828 235.890 268.242 1.00 36.69  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 266.760 235.506 267.243 1.00 44.57  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 265.708 236.366 266.957 1.00 40.86  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 266.806 234.286 266.582 1.00 46.30  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 264.731 236.021 266.045 1.00 39.16  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 265.833 233.932 265.668 1.00 43.99  ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 264.798 234.804 265.403 1.00 46.57  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 263.826 234.456 264.493 1.00 49.03  ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 268.641 239.033 268.350 1.00 46.23  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 268.272 240.427 268.131 1.00 44.47  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 269.113 241.050 267.025 1.00 45.35  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 268.584 241.750 266.155 1.00 49.71  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 268.418 241.220 269.429 1.00 44.21  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 268.013 242.693 269.367 1.00 48.74  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 266.548 242.838 268.993 1.00 50.65  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 268.295 243.370 270.692 1.00 53.49  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 270.424 240.801 267.038 1.00 47.24  ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 271.284 241.277 265.957 1.00 41.87  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 270.886 240.620 264.641 1.00 42.52  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 270.824 241.272 263.592 1.00 46.96  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 272.763 241.019 266.296 1.00 40.14  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 273.647 241.301 265.091 1.00 43.14  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 273.188 241.866 267.485 1.00 46.43  ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 270.610 239.315 264.682 1.00 46.14  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 270.160 238.608 263.487 1.00 33.02  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 268.828 239.158 262.989 1.00 35.10  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 268.637 239.344 261.782 1.00 49.72  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 270.057 237.111 263.783 1.00 33.55  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 269.329 236.300 262.733 1.00 32.08  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 270.003 235.790 261.633 1.00 38.99  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 267.973 236.025 262.855 1.00 37.46  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 269.345 235.043 260.675 1.00 48.74  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 267.307 235.280 261.902 1.00 37.07  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 267.997 234.791 260.815 1.00 45.81  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 267.338 234.047 259.864 1.00 42.17  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 267.895 239.426 263.905 1.00 38.05  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 266.600 239.968 263.504 1.00 32.78  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 266.727 241.407 263.021 1.00 39.18  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 266.012 241.823 262.102 1.00 50.44  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 265.608 239.873 264.661 1.00 38.65  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 267.623 242.185 263.634 1.00 41.18  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 267.832 243.566 263.206 1.00 35.51  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 268.363 243.609 261.778 1.00 40.85  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 267.917 244.420 260.957 1.00 48.59  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 268.775 244.290 264.186 1.00 39.70  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 268.006 244.760 265.423 1.00 39.24  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 269.470 245.460 263.513 1.00 44.09  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 268.889 245.361 266.491 1.00 41.43  ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 269.320 242.735 261.460 1.00 45.93  ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 269.903 242.724 260.122 1.00 40.09  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 268.867 242.366 259.063 1.00 31.94  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 268.825 242.983 257.992 1.00 36.23  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 271.075 241.745 260.073 1.00 36.06  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 272.464 242.339 260.303 1.00 43.95  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 273.507 241.238 260.370 1.00 44.10  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 272.802 243.337 259.209 1.00 46.35  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 268.025 241.372 259.341 1.00 29.45  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 267.060 240.901 258.356 1.00 36.65  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 265.799 241.753 258.294 1.00 39.57  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 265.038 241.629 257.329 1.00 35.84  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 266.683 239.448 258.648 1.00 30.34  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 267.628 238.460 258.041 1.00 34.36  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 268.476 237.625 258.705 1.00 32.72  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 267.831 238.211 256.645 1.00 39.05  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 269.191 236.866 257.811 1.00 44.84  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 268.814 237.208 256.539 1.00 39.87  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 267.276 238.737 255.475 1.00 35.19  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 269.253 236.720 255.311 1.00 37.76  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 267.713 238.251 254.258 1.00 37.36  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 268.691 237.253 254.185 1.00 42.89  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 265.559 242.607 259.287 1.00 43.12  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 264.394 243.482 259.283 1.00 38.17  ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 264.673 244.844 258.670 1.00 39.66  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 263.756 245.462 258.119 1.00 42.56  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 263.867 243.675 260.709 1.00 31.29  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 263.480 242.437 261.278 1.00 32.12  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 265.912 245.325 258.751 1.00 41.22  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 266.269 246.617 258.183 1.00 39.16  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 266.886 246.509 256.797 1.00 45.57  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 266.716 247.427 255.988 1.00 52.10  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 267.244 247.350 259.110 1.00 41.30  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 266.696 247.807 260.463 1.00 45.71  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 267.815 247.915 261.478 1.00 50.54  ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 265.976 249.131 260.327 1.00 46.21  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 267.591 245.413 256.501 1.00 45.11  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 268.231 245.230 255.204 1.00 34.62  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 267.656 244.038 254.447 1.00 41.82  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 268.282 243.554 253.499 1.00 49.26  ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 269.745 245.069 255.365 1.00 40.63  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 270.051 244.064 256.315 1.00 51.87  ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 266.480 243.552 254.847 1.00 42.45  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 265.882 242.424 254.155 1.00 38.61  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 265.482 242.740 252.729 1.00 45.12  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 265.576 241.881 251.849 1.00 51.22  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 265.033 243.971 252.478 1.00 40.39  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 264.600 244.402 251.155 1.00 34.87  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 265.672 245.206 250.426 1.00 37.86  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 265.350 246.127 249.670 1.00 51.57  ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 263.308 245.212 251.261 1.00 40.08  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 263.448 246.415 252.172 1.00 49.84  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 264.238 246.343 253.136 1.00 45.89  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 262.766 247.432 251.925 1.00 51.86  ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 266.942 244.872 250.638 1.00 35.71  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 268.054 245.567 250.009 1.00 43.64  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 268.978 244.554 249.347 1.00 44.25  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 268.845 243.341 249.531 1.00 45.76  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 268.829 246.418 251.025 1.00 47.91  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 269.411 245.608 252.030 1.00 56.75  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 269.925 245.068 248.566 1.00 60.17  ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 270.861 244.217 247.851 1.00 54.78  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 271.851 243.573 248.820 1.00 56.40  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 271.919 243.909 250.006 1.00 65.59  ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 271.607 245.017 246.785 1.00 56.83  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 270.757 245.397 245.586 1.00 62.56  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 271.586 246.106 244.530 1.00 65.21  ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 272.099 247.384 245.009 1.00 65.96  ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 271.453 248.537 244.906 1.00 67.81  ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 270.259 248.612 244.341 1.00 67.85  ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 272.019 249.643 245.381 1.00 57.66  ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 272.633 242.630 248.290 1.00 57.42  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 273.587 241.901 249.121 1.00 60.78  ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 274.680 242.820 249.652 1.00 61.33  ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 275.138 242.657 250.790 1.00 62.02  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 274.198 240.746 248.328 1.00 62.85  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 275.187 239.857 249.084 1.00 68.58  ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 274.510 239.189 250.271 1.00 63.25  ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 275.799 238.820 248.155 1.00 65.08  ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 275.118 243.787 248.842 1.00 66.51  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 276.201 244.668 249.269 1.00 67.00  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 275.782 245.530 250.455 1.00 69.43  ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 276.596 245.816 251.340 1.00 72.09  ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 276.666 245.541 248.102 1.00 65.95  ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 275.622 246.510 247.570 1.00 69.70  ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 276.171 247.332 246.416 1.00 73.40  ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 275.154 248.350 245.930 1.00 72.46  ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 275.684 249.175 244.810 1.00 67.86  ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 274.516 245.953 250.494 1.00 64.95  ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 274.060 246.791 251.596 1.00 60.51  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 273.493 245.975 252.748 1.00 57.21  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 273.185 246.537 253.805 1.00 63.03  ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 273.038 247.809 251.091 1.00 57.16  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 273.662 248.830 250.159 1.00 61.54  ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 272.532 250.066 249.508 1.00 80.34  ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 273.651 250.953 248.428 1.00 64.72  ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 273.341 244.661 252.571 1.00 54.53  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 273.155 243.793 253.728 1.00 49.52  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 274.453 243.665 254.513 1.00 56.03  ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 274.439 243.560 255.745 1.00 59.94  ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 272.648 242.419 253.292 1.00 51.08  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 271.223 242.418 252.768 1.00 48.53  ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 270.807 241.036 252.296 1.00 51.49  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 269.433 241.017 251.812 1.00 44.76  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 268.877 239.995 251.175 1.00 47.93  ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 269.553 238.886 250.924 1.00 48.94  ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 267.610 240.089 250.780 1.00 46.12  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 275.588 243.669 253.810 1.00 60.40  ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 276.881 243.673 254.485 1.00 62.34  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 277.211 245.056 255.033 1.00 64.12  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 277.874 245.179 256.069 1.00 67.24  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 277.974 243.197 253.530 1.00 62.59  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 276.765 246.111 254.344 1.00 59.85  ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 277.015 247.467 254.824 1.00 61.40  ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 276.341 247.707 256.169 1.00 67.04  ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 276.935 248.312 257.070 1.00 70.77  ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 276.536 248.490 253.795 1.00 59.45  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 277.510 248.729 252.654 1.00 64.97  ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 277.106 249.900 251.780 1.00 70.52  ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 276.437 250.822 252.293 1.00 67.87  ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 277.456 249.900 250.582 1.00 69.72  ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 275.097 247.249 256.321 1.00 57.03  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 274.440 247.330 257.620 1.00 55.33  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 275.148 246.455 258.645 1.00 55.81  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 275.297 246.844 259.809 1.00 64.13  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 272.970 246.931 257.496 1.00 55.69  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 272.121 247.148 258.751 1.00 57.96  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 271.973 248.631 259.052 1.00 58.85  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 270.762 246.489 258.602 1.00 52.85  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 275.591 245.266 258.230 1.00 57.61  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 276.328 244.403 259.139 1.00 57.67  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 277.640 245.015 259.589 1.00 60.89  ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 278.036 244.875 260.749 1.00 65.67  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 278.338 245.695 258.676 1.00 65.45  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 279.569 246.383 259.050 1.00 68.85  ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 279.293 247.505 260.042 1.00 73.04  ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 280.046 247.691 261.005 1.00 73.42  ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 280.268 246.927 257.804 1.00 66.30  ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 280.945 245.865 256.954 1.00 70.54  ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 281.131 246.304 255.515 1.00 77.62  ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 280.877 247.490 255.217 1.00 75.60  ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 281.532 245.463 254.682 1.00 73.51  ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 278.221 248.270 259.820 1.00 66.46  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 277.869 249.336 260.753 1.00 61.54  ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 277.493 248.774 262.117 1.00 64.18  ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 277.860 249.341 263.152 1.00 73.44  ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 276.725 250.179 260.192 1.00 64.51  ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 276.325 251.321 261.099 1.00 69.07  ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 277.082 252.483 261.158 1.00 69.81  ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 275.197 251.232 261.904 1.00 67.10  ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 276.724 253.527 261.988 1.00 69.30  ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 274.832 252.271 262.739 1.00 63.82  ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 275.599 253.416 262.776 1.00 67.12  ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 275.239 254.454 263.604 1.00 71.41  ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 276.749 247.666 262.138 1.00 56.95  ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 276.383 247.043 263.407 1.00 55.48  ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 277.629 246.588 264.152 1.00 61.57  ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 277.773 246.833 265.356 1.00 68.95  ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 275.406 245.877 263.169 1.00 57.83  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 274.037 246.406 262.739 1.00 60.41  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 275.279 245.019 264.418 1.00 60.78  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 273.004 245.323 262.534 1.00 61.35  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 278.561 245.944 263.443 1.00 67.71  ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 279.796 245.481 264.070 1.00 69.34  ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 280.560 246.633 264.710 1.00 71.77  ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 281.234 246.452 265.732 1.00 70.25  ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 280.669 244.772 263.035 1.00 67.71  ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 281.666 243.786 263.618 1.00 69.11  ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 282.502 243.141 262.522 1.00 67.72  ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 281.917 241.895 262.041 1.00 71.42  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 281.972 240.740 262.689 1.00 73.47  ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 282.590 240.629 263.854 1.00 69.04  ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 281.396 239.667 262.154 1.00 69.92  ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 280.469 247.827 264.123 1.00 71.02  ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 281.185 248.977 264.662 1.00 71.21  ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 280.545 249.486 265.949 1.00 73.95  ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 281.241 250.001 266.832 1.00 74.16  ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 281.239 250.092 263.618 1.00 69.92  ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 282.521 250.128 262.805 1.00 73.00  ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 282.621 251.412 261.997 1.00 72.78  ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 281.449 251.620 261.155 1.00 74.65  ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 281.399 251.347 259.858 1.00 78.20  ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 282.443 250.848 259.216 1.00 74.77  ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 280.274 251.581 259.189 1.00 76.89  ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 279.224 249.353 266.077 1.00 67.93  ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 278.499 250.027 267.148 1.00 63.80  ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 277.995 249.094 268.249 1.00 65.75  ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 277.764 249.560 269.375 1.00 70.72  ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 277.320 250.841 266.573 1.00 65.79  ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 276.217 249.910 266.067 1.00 67.43  ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 277.801 251.759 265.460 1.00 65.62  ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 274.850 250.553 266.017 1.00 66.67  ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 277.816 247.807 267.969 1.00 70.64  ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 277.234 246.919 268.964 1.00 72.86  ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 278.312 246.347 269.879 1.00 74.18  ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 279.504 246.352 269.562 1.00 74.25  ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 276.462 245.773 268.306 1.00 72.62  ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 275.743 245.049 269.311 1.00 72.09  ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 277.419 244.808 267.626 1.00 70.63  ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 277.870 245.854 271.035 1.00 77.73  ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 278.733 245.149 271.972 1.00 80.49  ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 278.390 243.671 272.079 1.00 79.27  ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 279.068 242.942 272.811 1.00 77.60  ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 278.657 245.797 273.360 1.00 81.67  ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 277.478 245.344 274.036 1.00 79.92  ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 278.620 247.313 273.241 1.00 79.24  ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 277.360 243.216 271.378 1.00 76.14  ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 277.001 241.793 271.375 1.00 76.52  ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 278.107 241.002 270.687 1.00 76.13  ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 278.681 241.488 269.695 1.00 73.46  ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 275.656 241.590 270.671 1.00 69.46  ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 275.137 240.177 270.885 1.00 69.88  ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 274.642 242.611 271.165 1.00 68.57  ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 278.459 239.812 271.173 1.00 74.89  ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 279.442 238.990 270.458 1.00 69.29  ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 278.977 238.682 269.042 1.00 75.92  ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 277.794 238.438 268.794 1.00 78.19  ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 279.534 237.723 271.313 1.00 69.25  ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 279.148 238.167 272.679 1.00 72.84  ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 278.121 239.248 272.492 1.00 74.69  ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 279.923 238.694 268.116 1.00 73.64  ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 279.668 238.556 266.693 1.00 70.44  ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 280.620 237.529 266.104 1.00 71.85  ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 281.662 237.227 266.696 1.00 71.50  ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 279.838 239.905 265.977 1.00 66.55  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 278.713 240.918 266.200 1.00 66.71  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 278.861 242.100 265.260 1.00 66.53  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 277.353 240.261 266.026 1.00 66.75  ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 280.281 236.954 264.948 1.00 76.93  ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 281.193 235.997 264.310 1.00 72.50  ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 282.546 236.629 264.017 1.00 73.96  ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 282.642 237.805 263.659 1.00 73.98  ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 280.459 235.613 263.021 1.00 71.07  ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 279.023 235.850 263.325 1.00 72.19  ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 278.988 237.034 264.246 1.00 73.03  ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 283.599 235.829 264.174 1.00 84.31  ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 284.971 236.295 264.042 1.00 85.71  ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 285.553 236.039 262.658 1.00 87.39  ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 286.771 236.143 262.481 1.00 87.37  ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 285.855 235.638 265.105 1.00 87.30  ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 285.813 234.214 264.950 1.00 87.95  ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 285.370 236.005 266.499 1.00 82.72  ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 284.719 235.700 261.681 1.00 92.97  ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 285.210 235.470 260.331 1.00 90.82  ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 285.759 236.770 259.751 1.00 92.28  ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 285.072 237.800 259.790 1.00 91.81  ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 284.097 234.921 259.442 1.00 89.48  ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 286.984 236.770 259.219 1.00 97.38  ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 287.565 238.027 258.715 1.00 97.89  ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 286.794 238.647 257.563 1.00 97.62  ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 286.758 239.879 257.451 1.00 95.77  ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 288.979 237.609 258.286 1.00 95.84  ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 288.885 236.139 258.038 1.00 94.46  ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 287.886 235.622 259.027 1.00 94.65  ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 286.175 237.840 256.701 1.00 90.50  ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 285.516 238.359 255.508 1.00 91.75  ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 284.057 237.954 255.359 1.00 90.96  ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 283.334 238.621 254.610 1.00 88.93  ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 286.273 237.919 254.245 1.00 92.53  ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 287.494 238.774 253.970 1.00 94.35  ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 288.624 238.285 253.981 1.00 92.87  ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 287.272 240.059 253.721 1.00 91.15  ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 283.599 236.903 256.031 1.00 79.54  ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 282.221 236.439 255.881 1.00 77.17  ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 281.287 237.419 256.582 1.00 79.35  ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 281.456 237.687 257.780 1.00 80.11  ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 282.043 235.014 256.428 1.00 73.78  ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 283.033 234.046 255.771 1.00 77.53  ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 280.617 234.537 256.208 1.00 74.24  ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 283.206 234.243 254.276 1.00 79.36  ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 280.300 237.975 255.883 1.00 66.20  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 279.383 238.923 256.522 1.00 64.29  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 278.499 238.245 257.558 1.00 66.62  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 278.262 237.035 257.525 1.00 69.65  ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 278.552 239.461 255.353 1.00 61.66  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 278.645 238.406 254.304 1.00 58.98  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 280.006 237.793 254.452 1.00 62.92  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 278.013 239.059 258.498 1.00 60.30  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 277.133 238.564 259.550 1.00 59.17  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 275.825 238.033 258.979 1.00 56.78  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 275.205 237.145 259.574 1.00 59.31  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 276.873 239.676 260.587 1.00 58.56  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 278.186 240.348 260.985 1.00 56.37  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 276.188 239.112 261.822 1.00 58.71  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 278.000 241.657 261.714 1.00 60.00  ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 275.392 238.551 257.827 1.00 50.87  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 274.159 238.088 257.199 1.00 49.50  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 274.233 236.636 256.756 1.00 53.06  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 273.193 236.030 256.471 1.00 57.92  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 273.799 238.991 256.000 1.00 51.27  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 272.284 239.030 255.791 1.00 52.24  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 274.508 238.523 254.737 1.00 54.24  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 271.543 239.813 256.850 1.00 52.99  ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 275.431 236.058 256.695 1.00 51.60  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 275.612 234.661 256.332 1.00 49.48  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 275.575 233.729 257.536 1.00 56.12  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 275.775 232.521 257.372 1.00 59.88  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 276.936 234.478 255.584 1.00 50.08  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 276.876 234.987 254.158 1.00 61.95  ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 275.815 235.509 253.756 1.00 66.70  ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 277.890 234.867 253.439 1.00 59.17  ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 275.329 234.256 258.731 1.00 58.00  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 275.298 233.472 259.954 1.00 47.31  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 273.896 233.471 260.550 1.00 50.45  ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 273.139 234.435 260.405 1.00 56.82  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 276.287 234.019 260.988 1.00 48.07  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 277.730 233.664 260.721 1.00 50.04  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 278.516 234.447 259.888 1.00 51.15  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 278.309 232.548 261.309 1.00 56.11  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 279.836 234.127 259.645 1.00 52.93  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 279.628 232.220 261.072 1.00 56.72  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 280.387 233.012 260.239 1.00 56.87  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 281.703 232.689 260.000 1.00 64.89  ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 273.560 232.375 261.220 1.00 45.17  ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 272.323 232.253 261.974 1.00 41.72  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 272.651 232.011 263.441 1.00 54.02  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 273.801 231.770 263.816 1.00 57.80  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 271.445 231.120 261.430 1.00 42.41  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 272.060 229.741 261.564 1.00 49.19  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 271.022 228.637 261.560 1.00 53.83  ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 269.815 228.955 261.577 1.00 50.80  ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 271.414 227.452 261.542 1.00 52.38  ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 271.621 232.076 264.276 1.00 55.60  ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 271.760 231.890 265.715 1.00 54.44  ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 271.187 230.524 266.062 1.00 53.76  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 269.984 230.283 265.902 1.00 53.57  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 271.060 233.002 266.506 1.00 53.28  ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 271.383 232.876 267.985 1.00 47.28  ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 271.473 234.366 265.978 1.00 51.47  ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 272.047 229.628 266.536 1.00 54.71  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 271.592 228.323 266.984 1.00 56.20  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 270.814 228.455 268.289 1.00 58.80  ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 270.936 229.440 269.022 1.00 61.63  ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 272.777 227.375 267.169 1.00 59.56  ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 273.856 228.028 267.814 1.00 63.90  ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 269.996 227.439 268.574 1.00 59.77  ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 269.203 227.448 269.797 1.00 57.19  ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 270.092 227.384 271.034 1.00 58.80  ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 269.657 227.760 272.128 1.00 64.44  ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 268.184 226.293 269.777 1.00 63.66  ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 267.142 226.470 270.883 1.00 61.62  ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 268.889 224.951 269.914 1.00 66.24  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 266.253 227.679 270.692 1.00 60.17  ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 271.338 226.940 270.885 1.00 61.85  ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 272.282 226.891 271.994 1.00 63.22  ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 272.906 228.247 272.300 1.00 66.29  ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 273.671 228.353 273.264 1.00 71.11  ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 273.386 225.872 271.700 1.00 62.42  ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 274.218 226.312 270.641 1.00 66.06  ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 272.603 229.275 271.512 1.00 59.16  ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 273.145 230.595 271.766 1.00 58.07  ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 274.502 230.858 271.156 1.00 58.71  ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 275.277 231.646 271.707 1.00 62.92  ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 274.817 230.219 270.032 1.00 61.60  ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 276.092 230.406 269.355 1.00 62.91  ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 275.852 230.676 267.877 1.00 58.59  ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 274.932 230.113 267.276 1.00 63.59  ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 276.999 229.179 269.519 1.00 66.17  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 277.293 228.807 270.963 1.00 67.04  ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 278.377 229.669 271.578 1.00 70.16  ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 279.071 230.383 270.824 1.00 66.09  ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 278.537 229.631 272.816 1.00 66.96  ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 276.681 231.541 267.299 1.00 51.87  ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 276.596 231.822 265.872 1.00 53.80  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 277.035 230.603 265.071 1.00 60.79  ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 278.084 230.011 265.345 1.00 64.46  ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 277.464 233.026 265.511 1.00 53.42  ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 276.930 234.341 265.989 1.00 56.06  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 277.350 235.048 267.077 1.00 57.93  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 275.884 235.114 265.388 1.00 58.64  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 276.629 236.211 267.193 1.00 56.27  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 275.721 236.275 266.169 1.00 56.61  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 275.068 234.935 264.267 1.00 56.14  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 274.776 237.252 265.865 1.00 52.89  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 274.130 235.907 263.967 1.00 51.61  ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 273.993 237.050 264.763 1.00 51.53  ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 276.233 230.230 264.077 1.00 57.11  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 276.565 229.122 263.200 1.00 55.73  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 276.388 229.548 261.749 1.00 60.76  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 275.400 230.211 261.411 1.00 60.96  ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 275.691 227.895 263.497 1.00 53.72  ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 274.398 228.039 262.939 1.00 63.35  ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 277.327 229.190 260.874 1.00 56.37  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 277.224 229.612 259.472 1.00 51.49  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 276.040 228.961 258.774 1.00 49.14  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 275.641 227.840 259.098 1.00 49.24  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 278.554 229.152 258.865 1.00 45.95  ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 278.999 228.032 259.743 1.00 53.33  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 278.531 228.381 261.125 1.00 49.56  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 275.477 229.685 257.804 1.00 50.64  ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 274.379 229.137 257.016 1.00 46.44  ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 274.864 228.071 256.043 1.00 50.48  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 274.067 227.244 255.586 1.00 55.91  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 273.663 230.256 256.261 1.00 45.41  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 272.520 230.862 257.016 1.00 42.14  ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 272.405 232.156 257.429 1.00 46.36  ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 271.321 230.199 257.435 1.00 37.30  ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 271.212 232.341 258.084 1.00 47.19  ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 270.528 231.154 258.101 1.00 40.86  ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 270.842 228.891 257.315 1.00 47.77  ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 269.284 230.843 258.646 1.00 40.61  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 269.607 228.585 257.856 1.00 47.67  ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 268.843 229.555 258.513 1.00 42.95  ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 276.157 228.075 255.712 1.00 58.98  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 276.698 227.069 254.806 1.00 52.84  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 276.657 225.671 255.407 1.00 55.59  ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 276.664 224.687 254.660 1.00 63.53  ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 278.132 227.429 254.416 1.00 51.02  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 278.561 226.880 253.065 1.00 54.91  ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 277.778 227.487 251.917 1.00 59.73  ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 277.168 226.773 251.122 1.00 61.28  ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 277.793 228.811 251.826 1.00 57.23  ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 276.618 225.561 256.737 1.00 45.20  ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 276.510 224.254 257.373 1.00 46.00  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 275.181 223.577 257.070 1.00 50.93  ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 275.088 222.348 257.165 1.00 56.90  ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 276.696 224.387 258.885 1.00 50.35  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 274.156 224.346 256.710 1.00 52.59  ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 272.851 223.806 256.357 1.00 49.26  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 272.655 223.689 254.851 1.00 59.70  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 271.533 223.437 254.400 1.00 66.53  ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 271.742 224.668 256.964 1.00 48.46  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 271.551 224.468 258.457 1.00 57.14  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 270.281 225.141 258.948 1.00 56.36  ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 269.955 224.728 260.374 1.00 57.30  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 268.706 225.371 260.867 1.00 60.37  ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 273.712 223.866 254.070 1.00 58.38  ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 273.658 223.758 252.620 1.00 54.76  ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 274.513 222.569 252.201 1.00 55.65  ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 275.733 222.680 252.073 1.00 59.00  ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 274.138 225.053 251.939 1.00 50.26  ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 274.150 224.890 250.427 1.00 49.88  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 273.258 226.221 252.345 1.00 49.03  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 273.907 221.405 251.991 1.00 63.89  ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 274.663 220.235 251.546 1.00 67.44  ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 274.679 220.103 250.029 1.00 72.27  ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 273.855 220.674 249.312 1.00 72.49  ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 273.893 219.072 252.185 1.00 66.65  ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 272.473 219.555 252.208 1.00 63.92  ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 272.506 221.069 252.301 1.00 62.74  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 275.651 219.326 249.549 1.00 78.82  ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 275.754 219.003 248.126 1.00 78.19  ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 274.889 217.774 247.862 1.00 78.03  ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 275.348 216.630 247.861 1.00 78.02  ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 277.207 218.778 247.726 1.00 79.95  ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 277.414 218.547 246.238 1.00 80.95  ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 278.872 218.345 245.877 1.00 81.08  ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 279.743 218.334 246.748 1.00 83.98  ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 279.147 218.182 244.588 1.00 75.58  ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 273.600 218.028 247.639 1.00 72.53  ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 272.619 216.962 247.476 1.00 72.60  ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 272.807 216.285 246.126 1.00 76.81  ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 273.496 216.808 245.244 1.00 76.66  ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 271.182 217.498 247.618 1.00 74.27  ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 270.889 218.530 246.527 1.00 70.45  ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 270.973 218.102 248.997 1.00 74.28  ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 269.415 218.703 246.236 1.00 67.47  ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 272.195 215.116 245.961 1.00 74.41  ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 272.207 214.374 244.703 1.00 73.41  ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 270.755 214.165 244.284 1.00 72.39  ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 270.075 213.273 244.800 1.00 75.63  ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 272.946 213.047 244.850 1.00 73.24  ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 274.459 213.168 244.780 1.00 73.59  ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 274.939 213.705 243.446 1.00 79.46  ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 274.659 213.065 242.411 1.00 80.03  ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 275.597 214.766 243.434 1.00 76.66  ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 270.284 214.994 243.352 1.00 65.50  ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 268.908 214.900 242.885 1.00 65.40  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 268.714 213.596 242.125 1.00 66.59  ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 269.620 213.120 241.427 1.00 70.13  ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 268.560 216.119 242.012 1.00 61.57  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 267.122 216.048 241.524 1.00 63.21  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 268.794 217.406 242.785 1.00 63.93  ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 267.537 212.995 242.276 1.00 71.19  ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 267.206 211.799 241.517 1.00 70.43  ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 267.123 212.121 240.029 1.00 72.07  ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 266.776 213.236 239.629 1.00 80.86  ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 265.885 211.203 242.003 1.00 70.23  ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 265.943 210.620 243.407 1.00 73.81  ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 265.714 211.661 244.485 1.00 80.03  ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 265.426 212.826 244.138 1.00 80.80  ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 265.824 211.315 245.680 1.00 76.32  ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 267.455 211.124 239.205 1.00 66.66  ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 267.489 211.334 237.760 1.00 65.29  ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 266.109 211.684 237.215 1.00 65.42  ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 265.980 212.549 236.340 1.00 73.04  ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 268.041 210.092 237.061 1.00 68.72  ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 269.301 209.734 237.643 1.00 70.76  ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 268.235 210.358 235.577 1.00 66.60  ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 265.065 211.022 237.713 1.00 70.12  ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 263.713 211.302 237.244 1.00 71.33  ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 263.151 212.605 237.799 1.00 72.61  ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 262.108 213.061 237.319 1.00 73.08  ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 262.787 210.137 237.601 1.00 68.86  ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 262.435 210.066 239.054 1.00 73.93  ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 263.229 209.427 239.981 1.00 78.23  ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 261.368 210.543 239.737 1.00 75.00  ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 262.671 209.520 241.175 1.00 74.85  ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 261.540 210.192 241.054 1.00 73.78  ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 263.810 213.213 238.787 1.00 67.22  ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 263.371 214.471 239.380 1.00 65.13  ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 264.265 215.642 238.984 1.00 65.85  ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 264.430 216.587 239.762 1.00 65.83  ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 263.310 214.346 240.902 1.00 64.11  ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 262.215 213.426 241.407 1.00 67.50  ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 262.259 213.291 242.920 1.00 71.10  ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 261.826 214.575 243.603 1.00 70.47  ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 260.382 214.861 243.384 1.00 69.29  ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 264.841 215.601 237.787 1.00 56.04  ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 265.769 216.637 237.349 1.00 56.34  ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 264.980 217.893 237.004 1.00 61.87  ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 264.114 217.872 236.123 1.00 58.90  ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 266.607 216.160 236.155 1.00 50.42  ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 267.220 217.340 235.429 1.00 50.86  ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 267.693 215.209 236.623 1.00 50.57  ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 265.280 218.989 237.706 1.00 65.66  ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 264.645 220.290 237.485 1.00 59.85  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 263.123 220.195 237.555 1.00 60.03  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 262.406 220.828 236.777 1.00 62.09  ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 265.094 220.907 236.159 1.00 50.53  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 262.627 219.407 238.505 1.00 68.56  ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 261.194 219.261 238.689 1.00 68.81  ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 260.601 220.554 239.251 1.00 75.12  ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 261.316 221.363 239.849 1.00 77.02  ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 260.897 218.095 239.629 1.00 70.73  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 259.296 220.777 239.067 1.00 75.10  ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 258.693 222.027 239.564 1.00 72.99  ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 258.796 222.207 241.069 1.00 72.51  ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 258.706 223.346 241.545 1.00 74.42  ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 257.229 221.916 239.115 1.00 69.93  ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 257.245 220.950 237.984 1.00 71.77  ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 258.334 219.972 238.294 1.00 72.05  ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 258.981 221.132 241.834 1.00 68.03  ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 259.087 221.227 243.283 1.00 65.38  ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 260.478 220.919 243.822 1.00 65.04  ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 260.691 221.030 245.034 1.00 65.56  ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 258.058 220.303 243.954 1.00 66.16  ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 258.285 218.832 243.635 1.00 73.64  ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 259.210 218.509 242.860 1.00 75.47  ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 257.531 217.991 244.169 1.00 72.04  ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 261.426 220.540 242.970 1.00 58.14  ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 262.777 220.231 243.426 1.00 59.65  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 263.549 221.530 243.608 1.00 62.54  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 263.620 222.360 242.694 1.00 60.20  ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 263.488 219.294 242.437 1.00 58.51  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 264.991 219.326 242.663 1.00 59.11  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 262.963 217.880 242.585 1.00 59.78  ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 264.128 221.710 244.792 1.00 56.59  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 264.887 222.908 245.130 1.00 43.58  ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 266.301 222.486 245.497 1.00 45.27  ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 266.493 221.683 246.418 1.00 49.01  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 264.243 223.689 246.287 1.00 43.79  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 265.097 224.892 246.654 1.00 44.03  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 262.830 224.113 245.921 1.00 48.03  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 267.286 223.024 244.784 1.00 40.58  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 268.687 222.798 245.124 1.00 37.60  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 269.067 223.800 246.208 1.00 44.54  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 269.026 225.016 245.967 1.00 47.04  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 269.597 222.928 243.893 1.00 29.79  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 271.057 222.813 244.299 1.00 33.66  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 269.241 221.871 242.860 1.00 35.61  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 269.434 223.346 247.404 1.00 45.62  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 269.699 224.288 248.498 1.00 40.01  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 270.966 225.093 248.251 1.00 39.43  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 272.026 224.543 247.946 1.00 49.54  ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 269.836 223.375 249.722 1.00 40.25  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 270.251 222.059 249.162 1.00 39.39  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 269.569 221.944 247.832 1.00 39.37  ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 270.842 226.411 248.381 1.00 34.54  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 271.963 227.335 248.299 1.00 40.27  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 271.950 228.227 249.534 1.00 48.02  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 271.096 228.089 250.416 1.00 52.71  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 271.908 228.178 247.018 1.00 43.91  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 270.671 228.899 246.968 1.00 44.82  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 272.026 227.292 245.790 1.00 45.94  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 272.912 229.148 249.598 1.00 48.31  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 272.979 230.068 250.729 1.00 43.21  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 271.751 230.968 250.777 1.00 43.66  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 271.206 231.239 251.852 1.00 51.40  ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 274.259 230.901 250.651 1.00 51.63  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 274.580 231.756 251.877 1.00 49.22  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 275.275 230.925 252.943 1.00 47.09  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 275.432 232.953 251.487 1.00 48.18  ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 271.303 231.448 249.615 1.00 42.08  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 270.137 232.325 249.574 1.00 40.42  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 268.868 231.582 249.974 1.00 39.42  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 268.012 232.128 250.681 1.00 49.62  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 269.989 232.932 248.178 1.00 52.84  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 270.850 234.164 247.985 1.00 62.04  ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 271.801 234.355 248.771 1.00 58.11  ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 270.574 234.941 247.047 1.00 58.46  ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 268.725 230.334 249.523 1.00 39.17  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 267.493 229.592 249.779 1.00 40.96  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 267.311 229.298 251.263 1.00 43.95  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 266.208 229.451 251.800 1.00 47.84  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 267.480 228.294 248.971 1.00 45.78  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 268.653 227.528 249.272 1.00 54.06  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 267.440 228.595 247.481 1.00 43.92  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 268.378 228.877 251.947 1.00 44.33  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 268.241 228.518 253.356 1.00 38.45  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 267.953 229.748 254.208 1.00 40.56  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 267.180 229.675 255.171 1.00 51.54  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 269.492 227.765 253.850 1.00 42.18  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 269.584 226.400 253.185 1.00 43.43  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 270.751 228.574 253.592 1.00 46.79  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 268.562 230.889 253.881 1.00 33.10  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 268.313 232.113 254.635 1.00 33.61  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 266.896 232.625 254.411 1.00 43.57  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 266.219 233.037 255.360 1.00 57.11  ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 269.333 233.183 254.249 1.00 36.68  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 270.768 232.814 254.565 1.00 45.91  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 271.716 233.949 254.227 1.00 44.75  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 271.399 234.555 252.940 1.00 40.75  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 272.237 235.306 252.239 1.00 49.67  ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 273.460 235.565 252.671 1.00 43.96  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 271.838 235.810 251.074 1.00 53.98  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 266.433 232.612 253.159 1.00 41.09  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 265.106 233.135 252.855 1.00 34.11  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 264.001 232.231 253.386 1.00 38.65  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 262.978 232.729 253.867 1.00 49.93  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 264.957 233.335 251.348 1.00 41.74  ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 265.831 234.417 250.793 1.00 42.92  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 266.064 234.567 249.443 1.00 41.06  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 266.529 235.401 251.407 1.00 45.53  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 266.867 235.597 249.249 1.00 46.12  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 267.165 236.121 250.425 1.00 48.58  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 264.180 230.910 253.303 1.00 38.64  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 263.172 229.995 253.831 1.00 35.26  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 263.009 230.164 255.336 1.00 43.25  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 261.883 230.161 255.847 1.00 52.47  ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 263.537 228.550 253.493 1.00 37.02  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 263.355 228.183 252.030 1.00 48.56  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 263.889 226.801 251.711 1.00 54.50  ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 264.454 226.157 252.619 1.00 55.75  ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 263.751 226.362 250.550 1.00 48.68  ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 264.120 230.306 256.061 1.00 38.04  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 264.039 230.553 257.496 1.00 39.99  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 263.380 231.894 257.786 1.00 37.99  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 262.584 232.014 258.725 1.00 49.90  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 265.432 230.491 258.120 1.00 34.98  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 263.708 232.919 256.995 1.00 33.50  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 263.078 234.223 257.173 1.00 36.13  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 261.584 234.161 256.883 1.00 44.57  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 260.777 234.741 257.619 1.00 45.50  ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 263.756 235.258 256.276 1.00 34.29  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 263.358 236.716 256.505 1.00 36.31  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 263.861 237.202 257.853 1.00 39.77  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 263.884 237.594 255.383 1.00 38.81  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 261.195 233.465 255.812 1.00 43.33  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 259.777 233.332 255.493 1.00 35.76  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 259.051 232.498 256.540 1.00 42.40  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 257.895 232.782 256.872 1.00 52.74  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 259.601 232.721 254.103 1.00 37.33  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 260.012 233.605 252.925 1.00 34.40  ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 259.831 232.864 251.612 1.00 41.32  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 259.219 234.901 252.930 1.00 40.70  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 259.709 231.461 257.065 1.00 41.05  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 259.093 230.644 258.105 1.00 37.61  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 258.796 231.470 259.350 1.00 38.10  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 257.745 231.302 259.980 1.00 43.65  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 259.997 229.461 258.450 1.00 33.39  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 259.435 228.556 259.524 1.00 43.07  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 258.503 227.575 259.214 1.00 45.87  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 259.835 228.685 260.847 1.00 49.38  ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 257.986 226.748 260.193 1.00 46.94  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 259.324 227.863 261.832 1.00 44.40  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 258.400 226.896 261.500 1.00 45.84  ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 257.889 226.074 262.477 1.00 51.39  ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 259.715 232.363 259.724 1.00 38.62  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 259.496 233.209 260.892 1.00 41.62  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 258.282 234.110 260.705 1.00 40.15  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 257.449 234.241 261.610 1.00 45.69  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 260.746 234.045 261.170 1.00 41.72  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 261.793 233.197 261.660 1.00 42.69  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 260.453 235.127 262.195 1.00 42.77  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 258.156 234.731 259.531 1.00 43.16  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 257.035 235.629 259.281 1.00 36.07  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 255.731 234.873 259.056 1.00 38.76  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 254.669 235.342 259.480 1.00 44.17  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 257.337 236.520 258.077 1.00 34.80  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 258.431 237.514 258.315 1.00 35.62  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 258.878 237.970 259.520 1.00 37.19  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 259.222 238.172 257.319 1.00 40.17  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 259.897 238.874 259.336 1.00 36.82  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 260.127 239.014 257.993 1.00 42.68  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 259.252 238.131 255.921 1.00 43.30  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 261.051 239.809 257.318 1.00 41.90  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 260.170 238.920 255.254 1.00 44.95  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 261.057 239.748 255.952 1.00 45.93  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 255.785 233.717 258.391 1.00 41.23  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 254.570 232.954 258.122 1.00 36.45  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 254.012 232.314 259.387 1.00 41.24  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 252.790 232.233 259.554 1.00 42.04  ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 254.841 231.885 257.063 1.00 37.46  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 254.849 232.350 255.605 1.00 33.20  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 255.696 231.422 254.750 1.00 38.27  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 253.433 232.436 255.063 1.00 35.50  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 254.886 231.850 260.285 1.00 47.41  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 254.419 231.215 261.513 1.00 39.72  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 253.664 232.194 262.401 1.00 46.85  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 252.797 231.783 263.181 1.00 55.35  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 255.596 230.607 262.274 1.00 44.80  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 253.974 233.483 262.300 1.00 35.20  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 253.263 234.517 263.038 1.00 41.83  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 252.014 234.999 262.313 1.00 52.87  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 251.337 235.902 262.815 1.00 54.23  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 254.190 235.706 263.309 1.00 52.24  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 255.504 235.335 263.978 1.00 62.23  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 255.324 234.888 265.415 1.00 66.07  ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 254.397 235.391 266.086 1.00 62.29  ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 256.111 234.035 265.875 1.00 57.55  ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 251.706 234.426 261.147 1.00 43.24  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 250.557 234.824 260.331 1.00 31.27  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 250.637 236.293 259.928 1.00 39.93  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 249.614 236.953 259.731 1.00 45.88  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 249.235 234.527 261.045 1.00 31.46  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 249.132 233.126 261.561 1.00 34.47  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 248.847 232.836 262.877 1.00 45.33  ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 249.282 231.934 260.937 1.00 38.06  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 248.823 231.525 263.042 1.00 46.06  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 249.083 230.955 261.880 1.00 41.41  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 251.855 236.806 259.804 1.00 44.56  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 252.141 238.181 259.413 1.00 38.42  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 252.160 238.296 257.894 1.00 41.09  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 252.849 237.512 257.231 1.00 50.77  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 253.480 238.632 259.980 1.00 39.03  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 253.897 240.033 259.570 1.00 45.99  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 253.487 241.056 260.615 1.00 41.54  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 254.260 242.352 260.451 1.00 44.11  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 253.749 243.420 261.352 1.00 42.26  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 251.414 239.235 257.311 1.00 35.86  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 251.480 239.426 255.857 1.00 38.24  ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 252.890 239.798 255.424 1.00 37.34  ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 253.613 240.498 256.135 1.00 39.71  ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 250.489 240.568 255.603 1.00 27.01  ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 250.363 241.265 256.918 1.00 34.40  ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 250.511 240.200 257.958 1.00 36.31  ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 253.281 239.317 254.247 1.00 24.71  ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 254.653 239.480 253.789 1.00 23.66  ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 254.677 239.555 252.270 1.00 36.91  ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 253.755 239.100 251.589 1.00 46.85  ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 255.541 238.344 254.319 1.00 32.30  ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 255.225 236.895 253.925 1.00 34.90  ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 255.798 236.513 252.574 1.00 35.20  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 255.706 235.931 254.994 1.00 36.27  ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 255.753 240.140 251.746 1.00 33.12  ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 255.927 240.353 250.315 1.00 37.06  ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 257.345 239.967 249.918 1.00 37.18  ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 258.314 240.356 250.580 1.00 36.35  ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 255.631 241.817 249.920 1.00 30.56  ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 256.200 242.130 248.550 1.00 30.35  ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 254.138 242.067 249.928 1.00 30.07  ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 257.466 239.199 248.836 1.00 38.31  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 258.751 238.889 248.223 1.00 33.24  ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 258.906 239.761 246.984 1.00 33.34  ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 258.044 239.745 246.099 1.00 42.74  ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 258.862 237.410 247.849 1.00 30.53  ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 259.107 236.392 248.967 1.00 32.25  ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 257.836 236.128 249.744 1.00 34.37  ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 259.681 235.095 248.424 1.00 37.54  ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 259.996 240.518 246.926 1.00 32.24  ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 260.265 241.422 245.819 1.00 26.25  ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 261.536 240.996 245.098 1.00 30.91  ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 262.495 240.539 245.727 1.00 48.07  ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 260.400 242.866 246.309 1.00 32.87  ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 260.285 244.108 245.002 1.00 41.87  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 261.534 241.139 243.777 1.00 21.63  ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 262.684 240.803 242.975 1.00 28.73  ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 262.350 240.725 241.501 1.00 41.62  ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 261.189 240.839 241.096 1.00 46.24  ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 263.371 240.529 240.666 1.00 40.74  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 263.123 240.403 239.232 1.00 37.09  ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 262.337 239.140 238.935 1.00 35.65  ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 262.385 238.167 239.707 1.00 43.03  ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 264.539 240.340 238.630 1.00 40.84  ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 265.456 240.819 239.714 1.00 36.37  ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 264.802 240.428 240.993 1.00 33.62  ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 261.579 239.115 237.839 1.00 33.70  ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 260.809 237.909 237.506 1.00 37.97  ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 261.718 236.704 237.316 1.00 35.88  ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 262.810 236.806 236.755 1.00 39.69  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 260.094 238.289 236.204 1.00 37.44  ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 260.852 239.460 235.665 1.00 33.32  ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 261.380 240.191 236.855 1.00 38.49  ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 261.253 235.552 237.795 1.00 26.33  ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 262.030 234.333 237.727 1.00 25.42  ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 263.137 234.217 238.748 1.00 32.28  ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 263.959 233.300 238.642 1.00 35.32  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 263.188 235.114 239.735 1.00 33.56  ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 264.258 235.070 240.727 1.00 33.68  ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 264.121 233.854 241.636 1.00 38.30  ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 265.124 233.253 242.039 1.00 43.27  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 264.265 236.359 241.549 1.00 30.96  ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 262.976 236.641 242.064 1.00 42.64  ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 262.890 233.476 241.970 1.00 32.22  ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 262.676 232.358 242.866 1.00 26.31  ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 261.741 232.666 244.017 1.00 31.34  ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 261.710 231.931 245.008 1.00 38.36  ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 260.981 233.758 243.902 1.00 37.81  ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 260.076 234.151 244.978 1.00 28.76  ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 258.999 233.096 245.209 1.00 33.06  ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 258.755 232.680 246.348 1.00 45.93  ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 259.444 235.506 244.662 1.00 28.30  ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 260.450 236.607 244.378 1.00 27.43  ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 259.759 237.876 243.913 1.00 39.06  ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 259.136 237.694 242.541 1.00 31.40  ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 260.163 237.417 241.500 1.00 31.49  ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 258.338 232.655 244.137 1.00 32.17  ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 257.348 231.589 244.264 1.00 20.49  ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 258.011 230.285 244.691 1.00 28.46  ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 257.461 229.525 245.496 1.00 49.95  ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 256.597 231.409 242.944 1.00 35.53  ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 255.913 232.624 242.613 1.00 48.82  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 255.582 230.281 243.051 1.00 36.68  ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 259.202 230.013 244.155 1.00 35.05  ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 259.937 228.808 244.525 1.00 30.89  ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 260.294 228.813 246.007 1.00 31.23  ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 260.174 227.789 246.689 1.00 40.47  ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 261.190 228.691 243.650 1.00 33.72  ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 262.043 227.448 243.866 1.00 34.54  ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 263.169 227.581 245.269 1.00 70.11  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 264.372 228.737 244.623 1.00 42.73  ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 260.740 229.961 246.523 1.00 36.45  ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 261.146 230.031 247.923 1.00 35.78  ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 259.944 229.956 248.857 1.00 36.19  ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 260.008 229.310 249.910 1.00 37.65  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 261.940 231.312 248.177 1.00 30.83  ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 262.998 231.419 247.216 1.00 30.30  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 262.536 231.299 249.573 1.00 39.82  ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 258.841 230.614 248.493 1.00 31.12  ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 257.670 230.637 249.365 1.00 35.13  ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 257.063 229.248 249.518 1.00 33.90  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 256.755 228.811 250.632 1.00 45.22  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 256.629 231.614 248.823 1.00 29.85  ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 255.255 231.487 249.483 1.00 36.30  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 255.245 232.173 250.841 1.00 34.22  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 254.164 232.037 248.583 1.00 40.52  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 256.879 228.539 248.402 1.00 34.08  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 256.276 227.212 248.466 1.00 34.78  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 257.187 226.226 249.186 1.00 35.78  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 256.707 225.319 249.875 1.00 48.65  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 255.941 226.714 247.060 1.00 36.59  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 254.670 227.290 246.498 1.00 42.95  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 254.512 228.659 246.359 1.00 40.89  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 253.632 226.459 246.111 1.00 48.98  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 253.344 229.187 245.844 1.00 43.46  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 252.462 226.983 245.595 1.00 48.02  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 252.318 228.348 245.461 1.00 45.65  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 258.503 226.385 249.034 1.00 36.74  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 259.437 225.550 249.780 1.00 34.39  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 259.328 225.806 251.278 1.00 41.01  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 259.375 224.867 252.081 1.00 50.94  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 260.864 225.798 249.293 1.00 34.81  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 261.793 225.002 250.008 1.00 45.13  ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 259.184 227.073 251.673 1.00 39.79  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 259.020 227.393 253.087 1.00 31.85  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 257.655 226.951 253.599 1.00 31.70  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 257.515 226.587 254.772 1.00 47.47  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 259.222 228.890 253.314 1.00 34.38  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 256.636 226.981 252.737 1.00 33.51  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 255.305 226.553 253.154 1.00 31.89  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 255.238 225.046 253.363 1.00 39.81  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 254.391 224.566 254.125 1.00 48.82  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 254.264 226.992 252.125 1.00 30.24  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 253.733 228.418 252.274 1.00 34.03  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 252.908 228.811 251.060 1.00 34.49  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 252.916 228.555 253.548 1.00 35.81  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 256.111 224.286 252.696 1.00 42.77  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 256.158 222.845 252.910 1.00 43.11  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 256.580 222.489 254.328 1.00 47.82  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 256.255 221.397 254.805 1.00 50.94  ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 257.103 222.194 251.899 1.00 43.12  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 256.540 222.125 250.489 1.00 45.92  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 257.285 221.108 249.641 1.00 49.18  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 258.352 221.725 248.863 1.00 49.41  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 258.188 222.262 247.661 1.00 52.07  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 257.007 222.276 247.066 1.00 47.03  ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 259.235 222.799 247.042 1.00 50.76  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 257.294 223.384 255.012 1.00 44.60  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 257.639 223.179 256.411 1.00 43.31  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 256.494 223.522 257.354 1.00 48.96  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 256.617 223.292 258.561 1.00 49.29  ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 258.872 224.008 256.778 1.00 46.97  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 255.395 224.063 256.835 1.00 50.94  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 254.206 224.371 257.630 1.00 48.55  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 253.062 223.496 257.141 1.00 54.03  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 252.393 223.840 256.149 1.00 53.07  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 253.843 225.850 257.519 1.00 43.95  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 254.767 226.827 258.250 1.00 47.42  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 254.698 228.206 257.617 1.00 41.81  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 254.414 226.895 259.727 1.00 50.08  ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 252.795 222.362 257.794 1.00 59.48  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 251.778 221.437 257.271 1.00 59.46  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 250.350 221.920 257.449 1.00 60.73  ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 249.454 221.402 256.771 1.00 54.35  ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 252.032 220.153 258.070 1.00 58.13  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 252.618 220.632 259.355 1.00 54.29  ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 253.427 221.859 259.026 1.00 54.64  ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 250.103 222.890 258.329 1.00 62.46  ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 248.753 223.343 258.630 1.00 58.84  ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 248.350 224.578 257.833 1.00 58.96  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 247.397 225.266 258.216 1.00 64.70  ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 248.612 223.618 260.129 1.00 59.43  ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 248.730 222.359 260.966 1.00 70.50  ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 248.270 221.293 260.505 1.00 66.99  ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 249.280 222.436 262.084 1.00 66.63  ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 249.050 224.875 256.740 1.00 51.43  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 248.751 226.036 255.911 1.00 45.93  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 248.571 225.586 254.470 1.00 53.61  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 249.470 224.962 253.897 1.00 56.49  ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 249.862 227.085 256.007 1.00 48.46  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 249.765 227.980 257.228 1.00 49.41  ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 251.133 229.147 257.344 1.00 61.93  ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 251.191 229.415 259.113 1.00 51.13  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 247.418 225.903 253.890 1.00 47.29  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 247.155 225.673 252.476 1.00 47.58  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 247.287 226.994 251.732 1.00 45.78  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 246.876 228.042 252.240 1.00 54.37  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 245.766 225.064 252.257 1.00 48.34  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 244.606 225.967 252.638 1.00 55.89  ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 243.261 225.292 252.460 1.00 63.19  ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 243.238 224.110 252.059 1.00 60.87  ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 242.227 225.943 252.718 1.00 55.59  ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 247.874 226.945 250.540 1.00 37.47  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 248.149 228.136 249.746 1.00 35.90  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 247.208 228.165 248.550 1.00 40.62  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 246.930 227.130 247.931 1.00 41.23  ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 249.628 228.198 249.310 1.00 32.22  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 249.939 227.160 248.240 1.00 43.37  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 249.980 229.595 248.823 1.00 40.10  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 246.680 229.351 248.256 1.00 36.83  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 245.823 229.578 247.100 1.00 35.08  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 246.435 230.703 246.280 1.00 37.46  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 246.678 231.796 246.803 1.00 45.75  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 244.379 229.924 247.514 1.00 32.80  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 243.649 230.621 246.379 1.00 35.75  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 243.639 228.667 247.933 1.00 37.81  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 246.684 230.436 244.999 1.00 33.36  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 247.369 231.387 244.146 1.00 33.81  ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 246.406 232.319 243.441 1.00 36.35  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 245.418 231.877 242.849 1.00 40.63  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 246.698 233.615 243.510 1.00 40.37  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 245.950 234.639 242.795 1.00 37.69  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 246.918 235.441 241.941 1.00 38.77  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 247.958 235.890 242.433 1.00 46.05  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 245.202 235.569 243.757 1.00 38.64  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 243.931 235.046 244.429 1.00 42.85  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 244.258 234.150 245.612 1.00 46.13  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 243.040 236.200 244.856 1.00 45.80  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 246.578 235.618 240.669 1.00 47.53  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 247.405 236.368 239.730 1.00 43.50  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 246.763 237.731 239.517 1.00 48.88  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 245.667 237.828 238.955 1.00 47.08  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 247.557 235.616 238.410 1.00 35.44  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 247.813 234.139 238.611 1.00 45.88  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 246.898 233.322 238.523 1.00 52.48  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 249.063 233.788 238.891 1.00 44.96  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 247.445 238.777 239.966 1.00 46.39  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 246.954 240.136 239.817 1.00 38.63  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 247.339 240.688 238.451 1.00 40.69  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 248.346 240.290 237.858 1.00 45.15  ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 247.509 241.039 240.920 1.00 33.86  ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 246.782 240.922 242.231 1.00 33.10  ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 245.899 239.882 242.464 1.00 44.05  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 246.986 241.857 243.232 1.00 33.14  ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 245.233 239.776 243.670 1.00 46.25  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 246.323 241.757 244.439 1.00 37.80  ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 245.445 240.715 244.659 1.00 42.85  ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 246.516 241.604 237.949 1.00 41.36  ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 246.769 242.267 236.680 1.00 34.21  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 246.388 243.733 236.821 1.00 42.19  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 246.025 244.200 237.904 1.00 54.20  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 246.001 241.594 235.538 1.00 43.82  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 244.603 241.675 235.747 1.00 50.67  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 246.469 244.466 235.709 1.00 44.26  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 246.131 245.884 235.724 1.00 39.28  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 244.665 246.128 236.056 1.00 41.02  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 244.344 247.150 236.671 1.00 51.78  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 246.471 246.518 234.376 1.00 44.67  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 245.502 246.185 233.397 1.00 52.50  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 243.773 245.215 235.674 1.00 41.87  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 242.344 245.360 235.913 1.00 46.29  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 241.881 244.608 237.156 1.00 50.31  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 240.682 244.353 237.308 1.00 53.38  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 241.555 244.894 234.689 1.00 47.58  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 242.805 244.248 238.042 1.00 51.81  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 242.445 243.505 239.242 1.00 40.38  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 241.670 244.393 240.207 1.00 45.60  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 242.076 245.524 240.495 1.00 54.43  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 243.697 242.951 239.920 1.00 40.27  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 244.367 242.053 239.027 1.00 51.50  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 243.331 242.205 241.193 1.00 41.25  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 240.552 243.875 240.706 1.00 45.91  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 239.696 244.563 241.661 1.00 39.84  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 239.499 243.660 242.874 1.00 43.08  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 239.817 242.466 242.805 1.00 52.82  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 238.352 244.923 241.020 1.00 47.14  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 237.841 243.791 240.306 1.00 54.29  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 238.515 246.093 240.062 1.00 42.98  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 239.001 244.180 244.002 1.00 36.29  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 238.712 243.302 245.149 1.00 32.92  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 237.756 242.161 244.831 1.00 38.94  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 237.623 241.249 245.656 1.00 41.81  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 238.105 244.260 246.180 1.00 32.65  ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 238.699 245.578 245.850 1.00 36.93  ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 238.867 245.604 244.356 1.00 42.00  ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 237.089 242.185 243.674 1.00 47.52  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 236.238 241.067 243.281 1.00 37.19  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 237.036 239.778 243.138 1.00 38.80  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 236.515 238.694 243.419 1.00 49.03  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 235.517 241.392 241.972 1.00 40.48  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 234.181 240.689 241.808 1.00 51.12  ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 233.269 240.883 243.002 1.00 58.28  ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 232.974 242.048 243.343 1.00 55.47  ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 232.848 239.871 243.600 1.00 51.79  ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 238.295 239.872 242.702 1.00 35.92  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 239.133 238.682 242.589 1.00 31.89  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 239.347 238.036 243.952 1.00 40.27  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 239.297 236.808 244.086 1.00 51.72  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 240.472 239.044 241.945 1.00 42.58  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 241.306 237.878 241.411 1.00 42.06  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 240.779 237.413 240.063 1.00 37.80  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 242.772 238.269 241.311 1.00 41.54  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 239.596 238.852 244.978 1.00 43.12  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 239.715 238.323 246.333 1.00 36.23  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 238.382 237.778 246.830 1.00 33.38  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 238.339 236.746 247.509 1.00 45.73  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 240.236 239.408 247.275 1.00 41.18  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 241.652 239.924 247.012 1.00 44.15  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 241.917 241.183 247.818 1.00 47.25  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 242.679 238.856 247.342 1.00 41.67  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 237.283 238.465 246.507 1.00 27.94  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 235.969 238.029 246.971 1.00 29.06  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 235.578 236.687 246.361 1.00 36.25  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 235.001 235.833 247.045 1.00 42.15  ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 234.920 239.093 246.649 1.00 37.91  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 235.035 240.404 247.431 1.00 33.95  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 233.994 241.406 246.959 1.00 41.43  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 234.910 240.156 248.925 1.00 30.03  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 235.872 236.487 245.074 1.00 42.54  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 235.561 235.211 244.437 1.00 34.97  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 236.365 234.073 245.054 1.00 41.04  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 235.851 232.961 245.219 1.00 52.47  ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 235.813 235.294 242.932 1.00 42.00  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 234.910 236.276 242.205 1.00 43.51  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 233.458 235.830 242.251 1.00 46.41  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 232.552 236.829 241.551 1.00 48.13  ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 232.804 236.876 240.085 1.00 50.79  ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 237.631 234.330 245.392 1.00 34.11  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 238.430 233.323 246.082 1.00 36.24  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 237.838 233.000 247.449 1.00 39.75  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 237.815 231.835 247.866 1.00 41.29  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 239.876 233.804 246.216 1.00 42.14  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 240.484 233.858 244.920 1.00 42.19  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 240.680 232.864 247.103 1.00 45.52  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 237.347 234.019 248.157 1.00 36.78  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 236.703 233.787 249.446 1.00 30.83  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 235.450 232.935 249.294 1.00 40.48  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 235.170 232.075 250.137 1.00 46.82  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 236.364 235.121 250.112 1.00 39.08  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 237.565 235.887 250.586 1.00 40.35  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 238.747 235.232 250.886 1.00 37.63  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 237.511 237.263 250.731 1.00 37.64  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 239.852 235.935 251.323 1.00 39.69  ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 238.613 237.971 251.167 1.00 36.46  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 239.785 237.306 251.463 1.00 35.10  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 234.675 233.167 248.232 1.00 44.63  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 233.461 232.385 248.021 1.00 42.19  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 233.781 230.911 247.801 1.00 43.96  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 233.098 230.033 248.340 1.00 52.68  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 232.677 232.944 246.834 1.00 41.58  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 232.053 234.293 247.130 1.00 57.22  ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 231.751 234.563 248.311 1.00 54.42  ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 231.863 235.082 246.181 1.00 59.36  ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 234.814 230.621 247.008 1.00 33.53  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 235.130 229.233 246.686 1.00 36.89  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 235.792 228.516 247.857 1.00 39.62  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 235.464 227.360 248.148 1.00 43.96  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 236.025 229.175 245.448 1.00 36.29  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 236.294 227.785 244.963 1.00 42.42  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 237.225 226.957 245.553 1.00 47.50  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 235.752 227.075 243.946 1.00 44.55  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 237.245 225.798 244.919 1.00 44.96  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 236.360 225.844 243.940 1.00 49.81  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 236.724 229.180 248.542 1.00 38.67  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 237.560 228.513 249.531 1.00 38.53  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 237.148 228.778 250.972 1.00 39.61  ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 237.568 228.032 251.863 1.00 38.34  ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 239.025 228.929 249.348 1.00 38.70  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 239.646 228.407 248.073 1.00 35.30  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 240.277 227.172 248.040 1.00 30.98  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 239.597 229.150 246.901 1.00 40.58  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 240.844 226.691 246.876 1.00 31.87  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 240.161 228.677 245.732 1.00 42.84  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 240.783 227.447 245.726 1.00 41.86  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 241.347 226.972 244.564 1.00 50.74  ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 236.346 229.806 251.227 1.00 38.59  ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 235.922 230.152 252.574 1.00 34.04  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 234.402 230.203 252.646 1.00 45.05  ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 233.702 230.131 251.633 1.00 41.29  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 236.520 231.495 253.013 1.00 38.57  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 238.320 231.569 252.951 1.00 49.96  ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 233.893 230.322 253.870 1.00 48.51  ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 232.460 230.389 254.109 1.00 45.80  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 232.165 231.459 255.150 1.00 48.91  ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 232.965 231.707 256.056 1.00 56.79  ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 231.903 229.034 254.567 1.00 42.96  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 232.420 228.570 255.919 1.00 49.26  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 231.898 227.200 256.304 1.00 62.05  ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 231.149 226.602 255.504 1.00 55.47  ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 232.237 226.720 257.406 1.00 61.57  ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 231.006 232.096 255.005 1.00 39.84  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 230.525 233.070 255.976 1.00 36.82  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 229.602 232.375 256.967 1.00 47.14  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 228.718 231.611 256.567 1.00 54.27  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 229.781 234.216 255.288 1.00 43.04  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 230.588 234.981 254.261 1.00 45.33  ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 230.750 234.494 252.971 1.00 47.44  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 231.175 236.198 254.579 1.00 43.84  ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 231.480 235.193 252.030 1.00 46.80  ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 231.907 236.904 253.645 1.00 40.38  ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 232.057 236.397 252.372 1.00 46.33  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 232.785 237.097 251.438 1.00 47.68  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 229.807 232.637 258.255 1.00 45.07  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 228.975 232.054 259.297 1.00 40.74  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 228.540 233.130 260.281 1.00 40.99  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 229.302 234.050 260.592 1.00 44.51  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 229.707 230.915 260.028 1.00 43.34  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 230.848 231.349 260.935 1.00 47.31  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 231.417 230.157 261.690 1.00 43.80  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 232.261 230.558 262.809 1.00 45.07  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 233.583 230.647 262.757 1.00 48.22  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 234.251 230.370 261.649 1.00 47.69  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 234.251 231.022 263.844 1.00 40.26  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 227.301 233.012 260.754 1.00 54.99  ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 226.746 233.919 261.749 1.00 47.63  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 227.229 233.526 263.138 1.00 51.98  ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 227.089 232.370 263.549 1.00 59.02  ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 225.217 233.899 261.701 1.00 54.08  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 224.607 234.363 260.388 1.00 55.56  ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 224.866 235.841 260.144 1.00 61.67  ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 224.206 236.658 261.157 1.00 60.07  ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 224.491 237.929 261.406 1.00 62.02  ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 225.406 238.582 260.711 1.00 60.36  ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 223.835 238.563 262.374 1.00 58.24  ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 227.793 234.488 263.852 1.00 47.15  ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 228.243 234.328 265.224 1.00 47.62  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 227.643 235.445 266.061 1.00 51.13  ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 227.252 236.488 265.526 1.00 56.12  ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 229.776 234.364 265.323 1.00 46.06  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 230.257 235.641 264.886 1.00 57.59  ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 230.396 233.271 264.466 1.00 44.88  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 227.536 235.252 267.379 1.00 57.83  ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 227.029 236.338 268.233 1.00 61.22  ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 227.862 237.606 268.159 1.00 59.80  ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 227.330 238.693 268.417 1.00 57.98  ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 227.066 235.724 269.639 1.00 58.97  ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 226.945 234.259 269.401 1.00 58.14  ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 227.696 233.993 268.128 1.00 56.30  ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 229.146 237.505 267.822 1.00 58.94  ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 229.994 238.677 267.658 1.00 58.80  ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 229.898 239.298 266.269 1.00 57.13  ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 230.376 240.421 266.079 1.00 62.40  ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 231.454 238.315 267.954 1.00 61.26  ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 231.646 237.781 269.359 1.00 63.31  ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 231.670 236.570 269.578 1.00 61.44  ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 231.784 238.685 270.323 1.00 59.62  ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 229.296 238.609 265.307 1.00 47.66  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 229.140 239.127 263.967 1.00 45.34  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 229.413 238.048 262.942 1.00 45.92  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 229.281 236.858 263.220 1.00 59.56  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 229.799 238.480 261.744 1.00 47.39  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 230.096 237.572 260.642 1.00 39.89  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 231.575 237.215 260.684 1.00 39.83  ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 232.432 238.093 260.841 1.00 44.31  ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 229.725 238.202 259.290 1.00 40.74  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 229.968 237.213 258.161 1.00 40.25  ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 228.283 238.660 259.293 1.00 40.04  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 231.875 235.927 260.550 1.00 35.60  ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 233.244 235.429 260.526 1.00 35.35  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 233.457 234.674 259.222 1.00 37.57  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 232.704 233.745 258.906 1.00 52.78  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 233.542 234.527 261.737 1.00 35.85  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 234.879 233.833 261.561 1.00 36.16  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 233.529 235.343 263.018 1.00 39.66  ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 234.478 235.072 258.469 1.00 26.64  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 234.849 234.405 257.228 1.00 30.43  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 236.075 233.541 257.491 1.00 35.93  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 237.155 234.062 257.787 1.00 45.30  ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 235.128 235.420 256.120 1.00 38.09  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 235.505 234.843 254.754 1.00 33.31  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 234.296 234.195 254.101 1.00 30.09  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 236.085 235.920 253.855 1.00 33.34  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 235.906 232.228 257.381 1.00 33.42  ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 236.954 231.269 257.680 1.00 30.22  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 237.018 230.235 256.568 1.00 41.36  ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 236.022 230.008 255.871 1.00 45.56  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 236.708 230.570 259.027 1.00 39.23  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 238.175 229.602 256.371 1.00 45.30  ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 238.276 228.557 255.347 1.00 43.27  ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 237.343 227.393 255.642 1.00 45.03  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 237.007 227.111 256.794 1.00 42.19  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 239.745 228.125 255.422 1.00 34.46  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 240.452 229.295 256.002 1.00 35.51  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 239.486 229.926 256.959 1.00 39.21  ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 236.912 226.723 254.570 1.00 49.37  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 236.015 225.580 254.716 1.00 51.08  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 236.688 224.471 255.515 1.00 51.55  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 236.071 223.856 256.393 1.00 48.63  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 235.555 225.084 253.332 1.00 48.49  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 234.705 223.831 253.470 1.00 51.07  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 234.786 226.177 252.607 1.00 46.62  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 237.959 224.201 255.230 1.00 58.63  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 238.693 223.191 255.981 1.00 58.59  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 239.006 223.704 257.381 1.00 56.71  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 239.555 224.798 257.546 1.00 56.03  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 239.983 222.818 255.253 1.00 54.81  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 239.767 222.107 253.928 1.00 59.79  ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 241.071 221.772 253.232 1.00 64.07  ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 242.149 222.127 253.706 1.00 61.36  ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 240.978 221.085 252.100 1.00 62.21  ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 238.658 222.910 258.389 1.00 53.08  ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 238.884 223.297 259.774 1.00 56.48  ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 240.323 223.011 260.183 1.00 58.36  ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 240.904 221.992 259.798 1.00 62.24  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 237.922 222.558 260.706 1.00 59.19  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 236.503 223.108 260.898 1.00 60.80  ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 236.543 224.481 261.556 1.00 59.36  ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 235.713 223.151 259.596 1.00 59.01  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 240.897 223.922 260.966 1.00 54.65  ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 242.241 223.755 261.475 1.00 60.11  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 243.351 224.126 260.517 1.00 60.82  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 244.526 223.982 260.876 1.00 58.10  ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 243.025 224.596 259.317 1.00 59.77  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 244.017 224.977 258.323 1.00 53.85  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 243.960 226.480 258.084 1.00 53.49  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 242.877 227.071 258.039 1.00 56.17  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 243.791 224.231 257.005 1.00 52.77  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 244.102 222.745 257.070 1.00 60.10  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 245.522 222.459 256.611 1.00 62.24  ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 245.886 220.999 256.822 1.00 59.52  ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 245.811 220.608 258.257 1.00 59.63  ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 245.132 227.090 257.933 1.00 40.64  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 245.248 228.515 257.658 1.00 36.31  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 245.378 228.731 256.157 1.00 41.16  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 246.290 228.189 255.524 1.00 52.83  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 246.452 229.114 258.387 1.00 40.54  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 246.141 229.581 259.774 1.00 39.07  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 245.981 228.804 260.884 1.00 39.80  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 245.957 230.935 260.203 1.00 44.20  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 245.704 229.589 261.976 1.00 39.58  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 245.685 230.902 261.585 1.00 47.86  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 245.995 232.172 259.553 1.00 36.76  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 245.451 232.057 262.328 1.00 45.28  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 245.762 233.317 260.292 1.00 37.31  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 245.494 233.252 261.664 1.00 37.76  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 244.468 229.519 255.593 1.00 35.21  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 244.478 229.810 254.167 1.00 33.74  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 245.478 230.919 253.876 1.00 34.08  ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 245.454 231.971 254.523 1.00 48.88  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 243.085 230.216 253.684 1.00 35.51  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 242.925 230.348 252.169 1.00 39.39  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 242.959 228.983 251.508 1.00 44.66  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 241.642 231.077 251.822 1.00 35.79  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 246.353 230.681 252.905 1.00 25.11  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 247.365 231.645 252.494 1.00 28.74  ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 246.996 232.131 251.101 1.00 31.82  ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 247.026 231.358 250.135 1.00 39.70  ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 248.775 231.039 252.516 1.00 25.59  ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 249.819 232.121 252.303 1.00 30.93  ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 249.017 230.309 253.828 1.00 26.91  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 246.647 233.410 250.991 1.00 31.51  ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 246.333 234.014 249.701 1.00 25.66  ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 247.618 234.563 249.097 1.00 29.95  ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 248.135 235.590 249.547 1.00 36.60  ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 245.288 235.115 249.858 1.00 33.96  ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 243.822 234.688 249.951 1.00 36.00  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 243.482 234.206 251.350 1.00 30.39  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 242.911 235.831 249.535 1.00 43.50  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 248.135 233.883 248.078 1.00 35.45  ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 249.384 234.268 247.429 1.00 31.84  ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 249.050 235.111 246.204 1.00 42.69  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 248.630 234.586 245.170 1.00 51.30  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 250.205 233.039 247.056 1.00 29.59  ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 251.482 233.360 246.336 1.00 43.24  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 252.293 234.395 246.769 1.00 36.43  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 251.872 232.627 245.229 1.00 47.71  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 253.469 234.694 246.111 1.00 34.57  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 253.048 232.922 244.566 1.00 44.52  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 253.847 233.956 245.008 1.00 38.19  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 249.238 236.423 246.324 1.00 43.05  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 249.058 237.338 245.206 1.00 29.67  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 250.410 237.606 244.558 1.00 39.48  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 251.342 238.071 245.220 1.00 52.82  ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 248.414 238.642 245.676 1.00 43.14  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 247.098 238.421 246.896 1.00 55.58  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 250.509 237.314 243.261 1.00 45.11  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 251.793 237.282 242.573 1.00 46.44  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 252.189 238.606 241.932 1.00 53.04  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 253.370 238.793 241.624 1.00 62.61  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 251.777 236.194 241.492 1.00 48.10  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 253.168 235.724 241.114 1.00 59.54  ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 254.132 236.078 241.823 1.00 58.57  ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 253.296 234.999 240.105 1.00 60.87  ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 251.244 239.514 241.707 1.00 44.06  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 251.506 240.745 240.963 1.00 38.89  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 250.856 241.942 241.654 1.00 47.82  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 250.146 242.735 241.035 1.00 59.65  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 251.025 240.613 239.522 1.00 44.98  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 251.606 239.429 238.759 1.00 51.72  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 253.038 239.663 238.308 1.00 55.32  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 253.553 240.785 238.498 1.00 56.14  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 253.650 238.721 237.762 1.00 52.99  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 251.107 242.083 242.958 1.00 35.18  ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 250.378 243.048 243.781 1.00 41.25  ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 250.524 244.477 243.267 1.00 45.57  ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 249.632 245.309 243.479 1.00 55.54  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 250.839 242.939 245.247 1.00 40.63  ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 252.363 243.017 245.328 1.00 44.03  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 250.338 241.652 245.871 1.00 39.31  ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 252.892 243.118 246.732 1.00 44.91  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 251.628 244.795 242.596 1.00 45.73  ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 251.889 246.172 242.190 1.00 38.79  ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 251.431 246.489 240.769 1.00 39.84  ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 251.592 247.632 240.329 1.00 48.57  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 253.381 246.492 242.334 1.00 37.48  ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 254.269 245.404 241.772 1.00 49.05  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 253.794 244.337 241.386 1.00 60.06  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 255.570 245.665 241.730 1.00 47.66  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 250.867 245.524 240.043 1.00 38.27  ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 250.320 245.794 238.715 1.00 45.35  ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 248.954 246.483 238.690 1.00 48.27  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 248.712 247.270 237.766 1.00 59.71  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 250.228 244.514 237.880 1.00 43.58  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 251.536 243.860 237.445 1.00 42.32  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 251.261 242.550 236.740 1.00 50.27  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 252.286 244.798 236.528 1.00 42.77  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 248.028 246.205 239.619 1.00 33.10  ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 246.698 246.827 239.531 1.00 37.26  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 246.767 248.333 239.324 1.00 43.75  ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 247.535 249.039 239.981 1.00 52.19  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 246.058 246.472 240.874 1.00 38.88  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 246.643 245.163 241.205 1.00 42.02  ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 248.047 245.161 240.663 1.00 38.39  ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 245.958 248.813 238.380 1.00 46.34  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 246.025 250.204 237.956 1.00 45.46  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 245.756 251.149 239.116 1.00 49.05  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 244.825 250.955 239.901 1.00 52.31  ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 245.022 250.466 236.832 1.00 48.66  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 245.399 249.774 235.540 1.00 57.64  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 246.610 249.574 235.307 1.00 56.97  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 244.488 249.431 234.759 1.00 58.47  ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 246.586 252.180 239.215 1.00 46.40  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 246.389 253.258 240.169 1.00 45.61  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 245.665 254.394 239.462 1.00 46.72  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 246.126 254.876 238.422 1.00 57.75  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 247.727 253.739 240.734 1.00 43.44  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 247.581 254.660 241.921 1.00 51.13  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 248.984 254.652 243.054 1.00 71.14  ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 250.354 254.633 241.906 1.00 51.72  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 244.532 254.813 240.020 1.00 42.06  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 243.705 255.814 239.365 1.00 47.24  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 244.408 257.170 239.379 1.00 54.97  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 245.529 257.322 239.873 1.00 56.24  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 242.335 255.893 240.036 1.00 49.65  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 242.412 256.375 241.470 1.00 52.61  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 243.439 256.122 242.131 1.00 58.04  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 241.440 257.004 241.938 1.00 49.70  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 243.729 258.178 238.829 1.00 49.85  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 244.314 259.509 238.726 1.00 47.65  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 244.529 260.165 240.084 1.00 50.32  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 245.210 261.194 240.152 1.00 52.78  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 243.432 260.401 237.852 1.00 49.74  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 242.091 260.742 238.472 1.00 53.59  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 241.319 261.737 237.620 1.00 54.03  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 240.693 261.061 236.413 1.00 56.41  ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 239.612 260.116 236.807 1.00 57.42  ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 243.970 259.601 241.156 1.00 46.51  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 244.136 260.130 242.503 1.00 44.66  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 245.062 259.270 243.358 1.00 46.00  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 244.998 259.332 244.589 1.00 52.10  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 242.775 260.282 243.179 1.00 42.95  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 241.798 261.112 242.382 1.00 44.31  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 241.968 262.483 242.251 1.00 51.79  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 240.705 260.526 241.761 1.00 40.69  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 241.077 263.247 241.525 1.00 49.47  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 239.809 261.281 241.033 1.00 48.08  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 239.999 262.641 240.918 1.00 50.95  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 239.107 263.396 240.193 1.00 52.33  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 245.914 258.466 242.730 1.00 35.67  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 246.938 257.732 243.455 1.00 38.67  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 246.440 256.693 244.438 1.00 41.27  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 246.933 256.636 245.572 1.00 50.33  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 245.475 255.867 244.037 1.00 37.91  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 244.954 254.823 244.907 1.00 40.11  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 244.696 253.554 244.106 1.00 48.50  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 244.119 253.605 243.017 1.00 49.35  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 243.660 255.272 245.599 1.00 41.50  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 243.948 256.357 246.487 1.00 55.10  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 243.049 254.128 246.395 1.00 36.75  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 245.124 252.420 244.654 1.00 52.10  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 244.798 251.105 244.115 1.00 40.83  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 243.721 250.487 244.996 1.00 43.81  ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 243.936 250.291 246.197 1.00 45.39  ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 246.034 250.208 244.056 1.00 31.52  ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 247.075 250.649 243.041 1.00 38.83  ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 248.419 249.984 243.259 1.00 38.20  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 249.032 250.128 244.316 1.00 45.28  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 248.885 249.250 242.256 1.00 42.72  ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 242.564 250.187 244.399 1.00 46.06  ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 241.424 249.724 245.185 1.00 38.76  ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 241.708 248.382 245.848 1.00 39.65  ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 241.351 248.170 247.013 1.00 48.29  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 240.178 249.634 244.303 1.00 31.34  ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 238.928 249.196 245.049 1.00 38.72  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 237.741 249.033 244.115 1.00 40.41  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 237.394 250.281 243.446 1.00 47.94  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 236.458 250.393 242.513 1.00 51.86  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 235.752 249.349 242.113 1.00 47.42  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 236.225 251.584 241.968 1.00 46.79  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 242.345 247.459 245.123 1.00 39.39  ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 242.640 246.153 245.703 1.00 33.75  ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 243.679 246.274 246.813 1.00 34.77  ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 243.619 245.543 247.809 1.00 42.64  ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 243.073 245.160 244.606 1.00 30.28  ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 244.432 245.526 244.036 1.00 36.66  ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 243.080 243.739 245.149 1.00 34.89  ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 244.641 247.189 246.671 1.00 32.30  ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 245.610 247.417 247.738 1.00 29.62  ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 244.925 248.024 248.955 1.00 31.03  ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 245.213 247.651 250.099 1.00 33.62  ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 246.765 248.300 247.231 1.00 41.60  ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 247.562 247.564 246.152 1.00 35.55  ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 247.677 248.705 248.379 1.00 38.98  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 248.039 246.193 246.575 1.00 22.47  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 244.007 248.967 248.730 1.00 39.43  ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 243.235 249.528 249.833 1.00 30.22  ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 242.353 248.468 250.478 1.00 33.42  ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 242.133 248.490 251.695 1.00 36.91  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 242.390 250.702 249.341 1.00 32.87  ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 243.209 251.774 248.908 1.00 41.17  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 241.828 247.539 249.676 1.00 37.76  ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 241.039 246.444 250.230 1.00 26.08  ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 241.881 245.581 251.160 1.00 31.78  ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 241.463 245.269 252.279 1.00 41.46  ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 240.445 245.600 249.103 1.00 28.73  ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 239.377 244.646 249.558 1.00 40.44  ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 238.141 245.113 249.971 1.00 43.83  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 239.610 243.281 249.569 1.00 36.42  ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 237.158 244.236 250.388 1.00 37.39  ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 238.631 242.400 249.984 1.00 34.97  ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 237.404 242.878 250.395 1.00 35.94  ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 243.082 245.204 250.720 1.00 36.12  ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 243.942 244.356 251.540 1.00 31.84  ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 244.401 245.102 252.787 1.00 36.20  ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 244.457 244.529 253.881 1.00 47.32  ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 245.135 243.845 250.711 1.00 30.38  ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 244.641 243.030 249.515 1.00 25.50  ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 246.067 243.007 251.571 1.00 27.67  ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 245.733 242.651 248.541 1.00 28.10  ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 244.730 246.389 252.647 1.00 33.45  ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 245.223 247.159 253.786 1.00 25.83  ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 244.178 247.253 254.893 1.00 26.93  ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 244.496 247.065 256.073 1.00 38.51  ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 245.648 248.552 253.327 1.00 31.38  ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 246.234 249.413 254.427 1.00 35.00  ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 245.349 250.613 254.690 1.00 40.83  ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 245.702 251.298 255.927 1.00 41.85  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 245.005 252.298 256.448 1.00 38.84  ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 243.902 252.745 255.871 1.00 42.48  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 245.423 252.859 257.579 1.00 37.38  ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 242.926 247.547 254.533 1.00 37.63  ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 241.841 247.493 255.509 1.00 39.45  ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 241.656 246.079 256.038 1.00 30.80  ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 241.436 245.872 257.237 1.00 45.13  ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 240.545 247.993 254.873 1.00 34.14  ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 239.288 247.553 255.601 1.00 31.71  ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 238.032 247.837 254.809 1.00 40.53  ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 237.911 247.439 253.651 1.00 37.38  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 237.085 248.528 255.431 1.00 44.70  ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 241.757 245.094 255.150 1.00 39.29  ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 241.536 243.697 255.490 1.00 39.38  ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 242.761 243.054 256.133 1.00 33.17  ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 242.704 241.884 256.525 1.00 46.49  ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 241.067 242.988 254.214 1.00 32.70  ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 240.638 241.554 254.304 1.00 34.77  ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 240.573 240.919 252.619 1.00 61.15  ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 242.306 240.901 252.196 1.00 44.29  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 243.854 243.798 256.277 1.00 36.92  ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 244.982 243.350 257.090 1.00 37.62  ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 245.043 244.104 258.412 1.00 40.43  ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 245.203 243.503 259.478 1.00 42.66  ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 246.299 243.495 256.299 1.00 29.32  ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 247.484 243.492 257.243 1.00 31.23  ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 246.427 242.379 255.275 1.00 37.22  ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 244.911 245.433 258.364 1.00 36.28  ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 244.989 246.233 259.583 1.00 32.88  ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 243.785 245.999 260.487 1.00 40.60  ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 243.937 245.821 261.701 1.00 52.41  ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 245.104 247.716 259.230 1.00 33.00  ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 245.303 248.620 260.435 1.00 41.34  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 245.399 250.084 260.057 1.00 52.49  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 245.262 250.400 258.857 1.00 52.56  ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 245.610 250.918 260.962 1.00 49.09  ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 242.581 246.000 259.918 1.00 29.53  ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 241.355 245.867 260.694 1.00 31.43  ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 240.878 244.427 260.813 1.00 38.26  ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 239.879 244.174 261.492 1.00 36.63  ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 240.248 246.730 260.080 1.00 27.65  ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 240.544 248.197 260.106 1.00 36.96  ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 240.706 248.944 258.959 1.00 41.97  ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 240.710 249.055 261.140 1.00 39.24  ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 240.958 250.199 259.285 1.00 39.86  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 240.966 250.293 260.602 1.00 45.32  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 241.563 243.482 260.174 1.00 38.17  ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 241.203 242.083 260.299 1.00 30.04  ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 239.882 241.707 259.668 1.00 32.40  ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 239.263 240.725 260.087 1.00 42.58  ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 239.430 242.461 258.675 1.00 30.27  ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 238.179 242.138 258.015 1.00 20.48  ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 237.818 243.200 257.003 1.00 30.19  ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 238.559 244.163 256.782 1.00 43.78  ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 236.653 243.011 256.388 1.00 32.80  ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 236.153 243.923 255.368 1.00 30.42  ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 234.648 244.081 255.559 1.00 27.12  ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 234.073 243.613 256.546 1.00 42.69  ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 236.513 243.418 253.963 1.00 35.52  ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 235.931 242.072 253.630 1.00 33.33  ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 236.607 240.910 253.959 1.00 31.16  ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 234.711 241.970 252.983 1.00 24.79  ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 236.076 239.672 253.653 1.00 29.40  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 234.175 240.735 252.675 1.00 28.18  ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 234.859 239.585 253.011 1.00 34.90  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 234.008 244.747 254.602 1.00 31.24  ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 232.571 244.990 254.621 1.00 28.97  ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 231.932 244.221 253.474 1.00 38.95  ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 232.417 244.281 252.339 1.00 52.08  ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 232.263 246.484 254.493 1.00 28.72  ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 232.117 247.211 255.809 1.00 32.56  ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 230.990 247.037 256.599 1.00 28.83  ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 233.101 248.083 256.254 1.00 38.29  ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 230.851 247.704 257.801 1.00 35.18  ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 232.970 248.755 257.454 1.00 35.37  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 231.844 248.562 258.223 1.00 39.37  ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 231.709 249.228 259.418 1.00 38.33  ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 230.851 243.502 253.767 1.00 38.35  ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 230.089 242.834 252.720 1.00 38.86  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 229.049 243.803 252.173 1.00 39.66  ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 228.121 244.198 252.887 1.00 43.32  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 229.425 241.564 253.249 1.00 34.80  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 228.786 240.725 252.150 1.00 40.47  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 228.279 239.378 252.648 1.00 44.48  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 227.168 239.498 253.584 1.00 48.50  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 227.161 238.987 254.807 1.00 41.75  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 228.198 238.319 255.283 1.00 45.13  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 226.083 239.144 255.570 1.00 38.71  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 229.202 244.183 250.905 1.00 39.43  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 228.339 245.184 250.292 1.00 41.75  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 226.936 244.668 250.002 1.00 45.95  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 226.068 245.465 249.633 1.00 50.42  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 228.970 245.700 248.997 1.00 46.76  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 229.227 244.599 248.117 1.00 48.82  ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 230.279 246.416 249.296 1.00 42.44  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 226.697 243.363 250.145 1.00 46.19  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 225.356 242.831 249.932 1.00 43.67  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 224.375 243.371 250.966 1.00 45.36  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 223.232 243.703 250.631 1.00 48.43  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 225.387 241.303 249.965 1.00 42.75  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 225.258 240.818 251.289 1.00 48.00  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 224.801 243.467 252.228 1.00 40.46  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 223.940 243.951 253.299 1.00 40.63  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 224.634 244.954 254.214 1.00 49.84  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 224.124 245.230 255.306 1.00 46.57  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 223.403 242.777 254.126 1.00 44.47  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 224.509 241.918 254.701 1.00 52.08  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 225.551 241.766 254.031 1.00 47.27  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 224.335 241.392 255.820 1.00 53.09  ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 225.778 245.505 253.798 1.00 50.00  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 226.486 246.547 254.546 1.00 35.24  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 226.826 246.091 255.965 1.00 44.23  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 226.599 246.804 256.944 1.00 48.05  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 225.679 247.848 254.570 1.00 40.63  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 225.723 248.640 253.276 1.00 40.81  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 224.814 248.067 252.208 1.00 47.87  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 225.263 247.721 251.116 1.00 53.22  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 223.528 247.964 252.519 1.00 43.85  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 227.381 244.888 256.071 1.00 40.24  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 227.779 244.324 257.350 1.00 40.81  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 229.286 244.107 257.386 1.00 38.95  ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 229.939 243.934 256.353 1.00 49.06  ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 227.053 243.002 257.625 1.00 40.32  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 227.343 242.563 258.957 1.00 50.59  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 227.501 241.935 256.644 1.00 39.59  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 229.835 244.130 258.597 1.00 32.18  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 231.262 243.927 258.807 1.00 29.08  ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 231.544 242.434 258.926 1.00 37.80  ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 230.895 241.734 259.711 1.00 39.54  ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 231.737 244.666 260.057 1.00 30.95  ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 233.171 244.400 260.399 1.00 32.53  ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 233.641 243.541 261.348 1.00 39.47  ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 234.323 244.995 259.791 1.00 27.94  ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 235.014 243.565 261.370 1.00 35.86  ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 235.457 244.450 260.423 1.00 36.59  ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 234.505 245.937 258.774 1.00 27.60  ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 236.754 244.815 260.073 1.00 38.69  ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 235.793 246.298 258.427 1.00 31.93  ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 236.901 245.738 259.075 1.00 34.69  ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 232.510 241.952 258.150 1.00 32.71  ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 232.901 240.547 258.143 1.00 29.82  ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 234.328 240.459 258.662 1.00 33.22  ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 235.231 241.110 258.122 1.00 38.91  ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 232.785 239.935 256.739 1.00 29.65  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 233.291 238.503 256.741 1.00 33.64  ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 231.349 240.005 256.244 1.00 38.17  ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 234.535 239.656 259.701 1.00 31.45  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 235.840 239.508 260.331 1.00 28.50  ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 236.495 238.217 259.860 1.00 33.00  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 235.886 237.144 259.929 1.00 47.96  ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 235.714 239.511 261.856 1.00 29.80  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 236.919 238.927 262.575 1.00 39.43  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 236.835 239.156 264.075 1.00 41.22  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 237.617 238.100 264.838 1.00 41.39  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 237.044 236.739 264.647 1.00 41.92  ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 237.732 238.324 259.384 1.00 32.47  ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 238.447 237.156 258.891 1.00 28.13  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 238.907 236.271 260.043 1.00 36.62  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 239.135 236.743 261.160 1.00 44.80  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 239.653 237.582 258.058 1.00 28.12  ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 239.384 238.436 256.821 1.00 27.72  ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 240.600 238.417 255.926 1.00 32.96  ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 238.160 237.943 256.072 1.00 35.93  ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 239.042 234.978 259.760 1.00 38.47  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 239.585 234.018 260.712 1.00 39.02  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 240.386 232.976 259.950 1.00 42.51  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 239.903 232.429 258.954 1.00 49.33  ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 238.474 233.342 261.525 1.00 39.68  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 238.981 232.307 262.518 1.00 55.15  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 237.979 231.198 262.774 1.00 59.01  ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 238.411 230.056 263.038 1.00 51.39  ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 236.762 231.466 262.713 1.00 57.51  ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 241.607 232.710 260.419 1.00 36.14  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 242.487 231.702 259.823 1.00 34.74  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 242.758 231.989 258.348 1.00 37.80  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 242.831 231.076 257.522 1.00 46.90  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 241.916 230.293 260.002 1.00 42.27  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 242.002 229.756 261.419 1.00 38.51  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 241.456 228.342 261.497 1.00 40.05  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 240.039 228.287 261.158 1.00 45.96  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 239.540 227.626 260.123 1.00 44.43  ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 240.319 226.950 259.295 1.00 45.77  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 238.227 227.644 259.913 1.00 38.62  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 242.910 233.266 258.009 1.00 40.60  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 243.189 233.695 256.644 1.00 38.04  ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 244.473 234.515 256.654 1.00 40.79  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 244.598 235.473 257.425 1.00 41.76  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 242.020 234.502 256.051 1.00 38.88  ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 240.821 233.588 255.793 1.00 34.05  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 242.437 235.169 254.759 1.00 35.64  ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 239.569 234.327 255.380 1.00 29.76  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 245.419 234.139 255.794 1.00 46.23  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 246.736 234.757 255.738 1.00 28.03  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 247.004 235.240 254.319 1.00 24.99  ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 246.399 234.755 253.360 1.00 39.87  ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 247.828 233.771 256.184 1.00 38.14  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 249.176 234.401 256.489 1.00 43.02  ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 250.190 233.390 256.984 1.00 43.39  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 251.334 233.734 257.281 1.00 57.58  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 249.773 232.133 257.079 1.00 32.39  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 247.911 236.207 254.191 1.00 32.58  ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 248.181 236.845 252.910 1.00 33.17  ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 249.678 236.895 252.655 1.00 40.26  ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 250.456 237.248 253.547 1.00 45.14  ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 247.588 238.254 252.872 1.00 21.98  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 246.150 238.300 253.277 1.00 46.63  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 245.155 237.941 252.386 1.00 42.77  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 245.793 238.681 254.559 1.00 47.88  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 243.833 237.966 252.766 1.00 41.69  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 244.472 238.714 254.942 1.00 44.60  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 243.492 238.357 254.046 1.00 47.55  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 250.072 236.540 251.436 1.00 37.54  ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 251.458 236.614 250.990 1.00 26.07  ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 251.477 237.261 249.613 1.00 33.28  ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 250.680 236.908 248.739 1.00 42.30  ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 252.122 235.223 250.954 1.00 35.13  ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 253.396 235.265 250.131 1.00 28.16  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 252.415 234.745 252.364 1.00 38.27  ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 252.386 238.211 249.421 1.00 39.24  ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 252.484 238.942 248.174 1.00 32.61  ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 253.807 238.697 247.475 1.00 34.97  ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 254.821 238.405 248.109 1.00 48.36  ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 253.779 238.802 246.150 1.00 21.66  ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 254.976 238.785 245.324 1.00 26.97  ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 254.877 239.911 244.308 1.00 35.46  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 253.779 240.296 243.898 1.00 44.62  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 255.158 237.441 244.611 1.00 27.93  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 256.028 240.446 243.909 1.00 33.47  ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 256.021 241.575 242.990 1.00 32.57  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 257.408 241.787 242.408 1.00 35.03  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 258.419 241.430 243.019 1.00 37.76  ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 255.555 242.858 243.687 1.00 38.24  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 256.479 243.266 245.182 1.00 47.57  ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 257.435 242.374 241.218 1.00 37.32  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 258.648 242.922 240.644 1.00 32.93  ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 258.961 244.261 241.306 1.00 38.56  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 258.095 244.857 241.951 1.00 40.71  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 258.482 243.092 239.136 1.00 35.92  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 258.267 241.772 238.420 1.00 34.46  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 257.779 241.739 237.291 1.00 45.03  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 258.635 240.677 239.073 1.00 39.07  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 260.194 244.748 241.183 1.00 41.53  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 260.536 246.053 241.763 1.00 35.10  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 259.641 247.147 241.211 1.00 39.52  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 259.252 247.109 240.034 1.00 43.93  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 261.995 246.257 241.332 1.00 37.85  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 262.526 244.881 241.176 1.00 35.89  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 261.384 244.056 240.654 1.00 37.49  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 259.280 248.133 242.036 1.00 44.26  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 258.374 249.193 241.561 1.00 42.14  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 258.947 250.021 240.426 1.00 41.00  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 258.179 250.675 239.710 1.00 47.83  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 258.142 250.046 242.816 1.00 42.49  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 259.319 249.768 243.690 1.00 41.04  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 259.694 248.339 243.434 1.00 36.86  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 260.268 250.018 240.239 1.00 41.97  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 260.872 250.740 239.127 1.00 39.46  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 260.707 250.019 237.797 1.00 47.06  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 260.951 250.627 236.749 1.00 52.66  ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 262.358 250.978 239.402 1.00 48.63  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 263.037 249.719 239.487 1.00 52.70  ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 262.542 251.735 240.707 1.00 42.66  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 260.304 248.750 237.810 1.00 46.68  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 260.080 248.024 236.573 1.00 46.71  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 258.862 248.589 235.842 1.00 48.44  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 257.931 249.095 236.474 1.00 42.26  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 259.875 246.538 236.856 1.00 42.40  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 261.177 245.812 237.123 1.00 55.41  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 262.225 246.484 237.221 1.00 51.12  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 261.154 244.568 237.236 1.00 56.19  ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 258.852 248.530 234.510 1.00 49.58  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 257.715 249.081 233.760 1.00 43.18  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 256.413 248.384 234.124 1.00 36.13  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 256.361 247.162 234.282 1.00 44.90  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 258.099 248.832 232.296 1.00 44.58  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 259.160 247.779 232.340 1.00 45.45  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 259.897 248.000 233.620 1.00 44.23  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 255.354 249.179 234.253 1.00 36.92  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 254.051 248.669 234.618 1.00 36.41  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 253.841 248.439 236.098 1.00 42.21  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 252.738 248.042 236.494 1.00 50.14  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 254.852 248.678 236.929 1.00 43.35  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 254.763 248.446 238.364 1.00 37.80  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 254.591 249.775 239.086 1.00 42.87  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 255.333 250.729 238.828 1.00 51.48  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 256.007 247.722 238.880 1.00 39.22  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 256.442 246.546 238.025 1.00 36.99  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 255.413 245.434 238.059 1.00 42.15  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 255.889 244.221 237.405 1.00 54.04  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 255.822 243.996 236.100 1.00 41.88  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 255.325 244.895 235.267 1.00 44.51  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 256.270 242.840 235.617 1.00 41.92  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 253.614 249.831 239.988 1.00 41.58  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 253.328 251.029 240.755 1.00 40.84  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 253.767 250.849 242.203 1.00 44.38  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 253.516 249.794 242.796 1.00 50.12  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 251.832 251.364 240.716 1.00 37.22  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 251.410 252.188 239.510 1.00 45.38  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 251.289 251.330 238.262 1.00 43.51  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 250.113 250.374 238.359 1.00 43.02  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 249.982 249.538 237.135 1.00 41.57  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 254.429 251.845 242.790 1.00 46.11  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 254.871 251.712 244.184 1.00 40.67  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 253.690 251.531 245.126 1.00 48.51  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 252.638 252.153 244.963 1.00 52.36  ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 255.610 253.028 244.450 1.00 33.14  ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 255.053 253.985 243.448 1.00 37.83  ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 254.758 253.166 242.228 1.00 44.31  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 253.876 250.668 246.119 1.00 45.95  ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 252.822 250.383 247.080 1.00 37.43  ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 252.688 251.520 248.084 1.00 40.02  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 253.641 252.256 248.355 1.00 51.09  ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 253.099 249.069 247.810 1.00 38.77  ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 252.948 247.797 246.976 1.00 34.38  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 253.461 246.591 247.743 1.00 36.41  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 251.501 247.597 246.557 1.00 39.23  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 251.485 251.659 248.633 1.00 36.68  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 251.220 252.708 249.607 1.00 31.98  ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 252.030 252.480 250.876 1.00 39.95  ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 252.260 251.341 251.291 1.00 53.86  ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 249.729 252.759 249.937 1.00 39.46  ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 249.474 253.658 251.002 1.00 51.32  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 252.470 253.581 251.492 1.00 39.69  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 253.204 253.479 252.748 1.00 35.44  ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 252.330 252.918 253.859 1.00 36.71  ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 252.827 252.213 254.745 1.00 41.30  ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 253.757 254.847 253.146 1.00 44.61  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 254.984 255.246 252.388 1.00 49.11  ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 255.675 256.410 252.650 1.00 53.75  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 255.644 254.637 251.375 1.00 46.65  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 256.707 256.500 251.831 1.00 48.38  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 256.711 255.437 251.047 1.00 54.20  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 251.031 253.226 253.836 1.00 42.53  ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 250.116 252.658 254.820 1.00 35.03  ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 250.013 251.146 254.665 1.00 37.99  ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 249.983 250.413 255.660 1.00 50.92  ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 248.742 253.314 254.690 1.00 32.01  ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 248.612 254.613 255.468 1.00 41.48  ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 247.353 255.373 255.089 1.00 40.81  ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 246.829 256.144 256.210 1.00 42.59  ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 245.544 256.229 256.526 1.00 37.77  ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 244.615 255.622 255.808 1.00 42.98  ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 245.183 256.946 257.586 1.00 41.74  ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 249.952 250.661 253.423 1.00 38.65  ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 249.943 249.221 253.188 1.00 30.06  ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 251.264 248.584 253.599 1.00 30.93  ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 251.278 247.516 254.221 1.00 46.94  ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 249.642 248.931 251.718 1.00 33.58  ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 249.786 247.483 251.342 1.00 38.90  ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 248.806 246.565 251.678 1.00 36.77  ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 250.902 247.040 250.651 1.00 37.29  ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 248.936 245.234 251.334 1.00 34.65  ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 251.038 245.710 250.304 1.00 38.07  ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 250.053 244.806 250.646 1.00 40.81  ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 252.385 249.225 253.262 1.00 35.65  ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 253.699 248.677 253.571 1.00 33.86  ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 254.014 248.691 255.061 1.00 40.51  ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 254.977 248.038 255.476 1.00 44.70  ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 254.779 249.448 252.811 1.00 37.73  ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 254.880 249.173 251.310 1.00 38.12  ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 255.996 249.997 250.689 1.00 37.66  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 255.097 247.691 251.051 1.00 42.40  ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 253.236 249.416 255.868 1.00 40.61  ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 253.499 249.467 257.302 1.00 28.41  ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 253.350 248.093 257.944 1.00 39.62  ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 254.175 247.695 258.776 1.00 54.36  ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 252.561 250.475 257.966 1.00 25.52  ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 252.537 250.397 259.481 1.00 37.68  ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 251.336 251.127 260.054 1.00 38.67  ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 251.090 250.755 261.442 1.00 29.97  ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 249.898 250.769 262.022 1.00 36.24  ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 248.813 251.141 261.363 1.00 40.55  ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 249.792 250.400 263.295 1.00 48.26  ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 252.311 247.351 257.568 1.00 29.82  ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 252.028 246.055 258.167 1.00 32.23  ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 252.708 244.895 257.452 1.00 37.71  ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 252.644 243.765 257.946 1.00 42.97  ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 250.517 245.802 258.189 1.00 32.54  ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 249.702 247.023 258.481 1.00 38.21  ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 249.008 247.704 257.504 1.00 37.90  ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 249.465 247.682 259.639 1.00 36.80  ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 248.382 248.732 258.047 1.00 35.06  ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 248.642 248.741 259.342 1.00 32.04  ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 253.347 245.136 256.316 1.00 41.04  ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 253.834 244.078 255.442 1.00 32.27  ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 255.343 244.225 255.287 1.00 36.67  ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 255.821 245.091 254.554 1.00 45.43  ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 253.132 244.113 254.073 1.00 26.87  ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 253.495 242.888 253.274 1.00 39.25  ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 251.625 244.206 254.250 1.00 40.23  ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 256.130 243.393 255.970 1.00 32.99  ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 257.570 243.350 255.693 1.00 37.12  ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 257.844 242.842 254.286 1.00 38.41  ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 257.082 242.050 253.726 1.00 47.47  ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 258.110 242.382 256.753 1.00 30.61  ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 256.919 241.608 257.218 1.00 32.88  ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 255.763 242.549 257.118 1.00 41.22  ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 258.951 243.308 253.714 1.00 37.33  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 259.332 242.991 252.343 1.00 33.34  ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 260.736 242.403 252.351 1.00 37.01  ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 261.638 242.947 252.998 1.00 46.01  ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 259.265 244.232 251.434 1.00 26.43  ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 259.763 243.901 250.037 1.00 30.01  ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 257.846 244.777 251.385 1.00 34.85  ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 260.916 241.295 251.637 1.00 27.53  ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 262.214 240.652 251.470 1.00 30.67  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 262.575 240.688 249.991 1.00 41.79  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 261.729 240.411 249.132 1.00 44.06  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 262.212 239.209 252.013 1.00 31.47  ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 261.096 238.390 251.382 1.00 31.55  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 263.562 238.547 251.781 1.00 32.40  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 263.819 241.056 249.694 1.00 46.00  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 264.285 241.176 248.319 1.00 29.72  ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 264.970 239.882 247.898 1.00 41.82  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 265.984 239.489 248.486 1.00 47.04  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 265.238 242.362 248.174 1.00 33.23  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 265.726 242.586 246.761 1.00 34.80  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 264.830 242.770 245.717 1.00 38.96  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 267.083 242.617 246.471 1.00 40.36  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 265.271 242.976 244.425 1.00 40.56  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 267.534 242.822 245.182 1.00 43.76  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 266.624 243.001 244.163 1.00 49.52  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 267.067 243.206 242.877 1.00 48.48  ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 264.417 239.224 246.884 1.00 44.02  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 264.973 237.995 246.331 1.00 35.68  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 265.613 238.347 244.995 1.00 40.84  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 264.914 238.616 244.011 1.00 41.89  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 263.904 236.906 246.166 1.00 30.13  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 264.543 235.600 245.723 1.00 33.86  ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 263.136 236.717 247.465 1.00 33.70  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 266.941 238.342 244.957 1.00 40.01  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 267.680 238.698 243.757 1.00 42.10  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 267.999 237.452 242.933 1.00 42.56  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 267.816 236.315 243.374 1.00 49.18  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 268.963 239.443 244.123 1.00 48.77  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 269.453 240.346 243.008 1.00 50.76  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 268.711 240.527 242.019 1.00 48.57  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 270.579 240.874 243.120 1.00 49.17  ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 268.478 237.682 241.714 1.00 42.12  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 268.856 236.579 240.846 1.00 35.51  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 270.038 235.823 241.447 1.00 42.76  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 270.944 236.441 242.020 1.00 42.82  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 269.225 237.090 239.452 1.00 36.91  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 268.046 237.317 238.536 1.00 36.51  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 266.936 236.486 238.582 1.00 31.59  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 268.049 238.356 237.616 1.00 42.25  ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 265.858 236.689 237.743 1.00 35.53  ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 266.977 238.566 236.773 1.00 38.73  ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 265.884 237.729 236.840 1.00 37.83  ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 264.813 237.935 236.003 1.00 38.61  ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 270.058 234.495 241.351 1.00 43.64  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 271.233 233.743 241.806 1.00 38.70  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 272.472 234.138 241.016 1.00 45.75  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 272.408 234.405 239.815 1.00 45.35  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 270.842 232.283 241.553 1.00 35.18  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 269.347 232.290 241.499 1.00 35.33  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 268.973 233.609 240.897 1.00 39.26  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 273.609 234.172 241.706 1.00 45.56  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 274.855 234.563 241.093 1.00 41.39  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 275.434 233.467 240.223 1.00 47.67  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 274.929 232.340 240.187 1.00 52.75  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 276.505 233.785 239.490 1.00 50.63  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 277.142 232.755 238.651 1.00 43.85  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 277.627 231.555 239.443 1.00 45.56  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 277.570 230.423 238.946 1.00 47.27  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 278.303 233.513 237.991 1.00 42.55  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 277.902 234.952 238.050 1.00 47.03  ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 277.141 235.102 239.331 1.00 51.17  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 278.112 231.771 240.668 1.00 43.47  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 278.499 230.648 241.515 1.00 44.46  ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 277.282 229.838 241.943 1.00 43.24  ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 277.318 228.603 241.937 1.00 53.89  ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 279.268 231.151 242.735 1.00 46.65  ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 276.196 230.518 242.321 1.00 42.88  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 274.974 229.813 242.695 1.00 36.61  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 274.353 229.107 241.496 1.00 42.42  ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 273.858 227.982 241.621 1.00 51.97  ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 273.977 230.786 243.322 1.00 44.28  ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 274.516 231.389 244.485 1.00 55.12  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 274.372 229.752 240.326 1.00 40.53  ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 273.815 229.132 239.128 1.00 33.47  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 274.562 227.854 238.772 1.00 32.44  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 273.949 226.859 238.366 1.00 40.18  ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 273.854 230.117 237.960 1.00 34.44  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 272.775 231.200 237.943 1.00 37.48  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 273.021 232.173 236.804 1.00 39.19  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 271.392 230.580 237.833 1.00 41.34  ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 275.889 227.865 238.908 1.00 34.89  ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 276.672 226.658 238.664 1.00 37.10  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 276.303 225.560 239.654 1.00 46.39  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 276.195 224.385 239.286 1.00 59.81  ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 278.166 226.980 238.743 1.00 41.07  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 278.521 227.874 237.681 1.00 52.39  ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 278.997 225.711 238.625 1.00 35.72  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 276.100 225.927 240.921 1.00 42.73  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 275.762 224.935 241.938 1.00 39.80  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 274.373 224.351 241.702 1.00 36.82  ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 274.167 223.139 241.830 1.00 40.11  ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 275.857 225.561 243.329 1.00 41.64  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 275.374 224.656 244.451 1.00 50.43  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 275.234 225.386 245.771 1.00 55.00  ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 275.566 226.567 245.879 1.00 50.84  ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 274.740 224.686 246.785 1.00 44.33  ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 273.403 225.203 241.362 1.00 36.38  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 272.030 224.734 241.181 1.00 34.04  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 271.928 223.821 239.967 1.00 37.86  ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 271.362 222.724 240.037 1.00 48.58  ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 271.063 225.926 241.065 1.00 25.19  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 271.051 226.740 242.358 1.00 32.89  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 269.665 225.445 240.718 1.00 30.19  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 270.580 228.164 242.175 1.00 32.75  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 272.479 224.256 238.834 1.00 33.27  ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 272.303 223.514 237.593 1.00 31.43  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 273.444 222.548 237.312 1.00 37.96  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 273.306 221.689 236.434 1.00 51.22  ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 272.120 224.491 236.431 1.00 41.20  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 270.881 225.340 236.592 1.00 40.91  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 269.624 224.823 236.310 1.00 31.67  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 270.962 226.646 237.055 1.00 41.31  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 268.486 225.586 236.466 1.00 28.97  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 269.828 227.418 237.215 1.00 40.54  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 268.593 226.882 236.920 1.00 37.62  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 267.459 227.646 237.076 1.00 49.21  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 274.562 222.664 238.029 1.00 35.04  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 275.547 221.597 238.004 1.00 31.45  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 275.030 220.338 238.670 1.00 38.55  ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 275.314 219.224 238.222 1.00 38.23  ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 274.266 220.499 239.754 1.00 46.25  ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 273.613 219.356 240.383 1.00 48.91  ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 272.578 218.736 239.453 1.00 51.20  ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 272.472 217.508 239.358 1.00 55.16  ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 272.964 219.785 241.699 1.00 43.08  ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 273.971 220.263 242.599 1.00 54.27  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 272.234 218.618 242.343 1.00 44.58  ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 271.802 219.573 238.759 1.00 47.19  ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 270.806 219.056 237.826 1.00 38.22  ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 271.470 218.341 236.657 1.00 47.91  ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 271.009 217.277 236.226 1.00 56.20  ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 269.919 220.193 237.321 1.00 42.77  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 268.842 220.595 238.286 1.00 43.48  ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 268.225 219.652 239.089 1.00 44.90  ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 268.441 221.916 238.382 1.00 44.92  ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 267.236 220.023 239.979 1.00 46.22  ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 267.450 222.292 239.266 1.00 43.13  ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 266.847 221.344 240.066 1.00 44.00  ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 272.552 218.915 236.126 1.00 43.94  ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 273.255 218.289 235.011 1.00 40.22  ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 273.910 216.981 235.434 1.00 42.90  ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 273.951 216.022 234.655 1.00 54.50  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 274.295 219.252 234.440 1.00 38.79  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 273.672 220.355 233.609 1.00 44.14  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 272.477 220.327 233.316 1.00 43.76  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 274.480 221.335 233.227 1.00 44.57  ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 274.437 216.925 236.659 1.00 47.60  ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 275.030 215.686 237.152 1.00 42.11  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 273.989 214.578 237.241 1.00 48.20  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 274.264 213.426 236.887 1.00 53.40  ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 275.677 215.920 238.517 1.00 44.45  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 277.157 216.252 238.458 1.00 53.64  ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 277.761 216.297 239.852 1.00 51.16  ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 277.677 217.628 240.441 1.00 53.67  ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 276.931 217.934 241.494 1.00 54.06  ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 276.188 217.025 242.103 1.00 53.57  ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 276.931 219.185 241.947 1.00 50.34  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 272.786 214.908 237.715 1.00 51.25  ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 271.730 213.907 237.818 1.00 44.74  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 271.172 213.543 236.449 1.00 53.67  ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 270.887 212.370 236.181 1.00 61.69  ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 270.617 214.417 238.731 1.00 48.91  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 271.005 214.535 235.571 1.00 54.21  ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 270.433 214.273 234.254 1.00 50.26  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 271.369 213.430 233.398 1.00 53.13  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 270.920 212.535 232.673 1.00 61.80  ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 270.103 215.593 233.557 1.00 46.96  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 270.129 215.530 232.040 1.00 48.64  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 269.888 217.145 231.279 1.00 60.27  ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 271.575 217.736 231.206 1.00 52.43  ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 272.672 213.687 233.479 1.00 55.97  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 273.642 212.982 232.651 1.00 49.27  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 273.913 211.562 233.128 1.00 53.24  ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 274.654 210.835 232.458 1.00 66.75  ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 274.950 213.774 232.591 1.00 48.24  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 274.924 214.966 231.631 1.00 51.56  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 276.322 215.487 231.370 1.00 56.15  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 274.246 214.588 230.324 1.00 54.59  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 273.343 211.149 234.262 1.00 60.47  ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 273.477 209.767 234.705 1.00 62.42  ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 272.724 208.787 233.815 1.00 65.58  ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 272.949 207.578 233.932 1.00 65.87  ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 272.999 209.623 236.151 1.00 62.29  ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 273.981 210.150 237.186 1.00 62.01  ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 273.689 209.580 238.566 1.00 63.12  ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 272.454 210.107 239.134 1.00 68.10  ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 272.397 211.102 240.009 1.00 67.82  ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 273.493 211.703 240.444 1.00 59.91  ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 271.212 211.502 240.460 1.00 65.04  ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 271.835 209.272 232.943 1.00 68.07  ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 271.174 208.383 231.992 1.00 69.01  ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 272.182 207.747 231.045 1.00 69.24  ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 272.095 206.551 230.743 1.00 71.56  ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 270.110 209.147 231.203 1.00 65.19  ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 268.866 209.621 231.955 1.00 62.99  ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 268.404 210.967 231.423 1.00 63.38  ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 267.752 208.592 231.848 1.00 69.74  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 273.140 208.528 230.567 1.00 62.90  ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 274.190 208.055 229.678 1.00 66.63  ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 275.517 208.148 230.420 1.00 64.41  ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 276.081 209.232 230.571 1.00 67.42  ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 274.227 208.863 228.368 1.00 69.79  ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 272.830 208.928 227.748 1.00 69.73  ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 275.214 208.248 227.392 1.00 69.24  ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 272.769 209.719 226.462 1.00 67.68  ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 276.043 207.023 230.908 1.00 71.22  ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 277.288 207.067 231.695 1.00 74.47  ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 278.480 207.641 230.947 1.00 75.64  ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 279.375 208.217 231.579 1.00 76.48  ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 277.514 205.594 232.060 1.00 71.65  ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 276.151 204.986 232.024 1.00 73.51  ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 275.444 205.678 230.896 1.00 72.37  ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 278.527 207.497 229.621 1.00 66.80  ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 279.662 208.012 228.862 1.00 67.21  ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 279.728 209.534 228.924 1.00 69.88  ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 280.817 210.118 228.887 1.00 71.71  ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 279.585 207.536 227.412 1.00 69.17  ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 278.428 208.042 226.769 1.00 68.97  ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 278.575 210.192 229.018 1.00 69.95  ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 278.513 211.648 229.025 1.00 67.83  ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 278.665 212.252 230.415 1.00 69.58  ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 278.639 213.481 230.538 1.00 71.40  ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 277.194 212.120 228.407 1.00 68.05  ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 276.943 211.744 226.947 1.00 65.16  ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 275.623 212.325 226.466 1.00 66.09  ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 278.090 212.214 226.067 1.00 62.97  ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 278.826 211.431 231.458 1.00 70.64  ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 278.902 211.963 232.816 1.00 70.37  ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 280.108 212.873 233.006 1.00 70.53  ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 280.073 213.782 233.844 1.00 73.21  ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 278.943 210.819 233.829 1.00 66.75  ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 277.655 210.021 233.925 1.00 71.37  ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 277.759 208.956 235.003 1.00 75.60  ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 278.695 207.900 234.636 1.00 78.29  ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 279.847 207.674 235.251 1.00 78.36  ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 280.244 208.417 236.272 1.00 73.98  ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 280.623 206.679 234.830 1.00 74.64  ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 281.181 212.647 232.246 1.00 67.52  ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 282.374 213.478 232.345 1.00 67.61  ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 282.126 214.913 231.895 1.00 69.12  ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 282.809 215.825 232.372 1.00 67.81  ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 283.502 212.848 231.517 1.00 70.26  ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 283.773 211.530 232.010 1.00 72.16  ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 284.781 213.671 231.604 1.00 63.79  ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 281.141 215.140 231.028 1.00 62.86  ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 280.888 216.452 230.451 1.00 59.98  ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 279.897 217.276 231.263 1.00 59.91  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 279.453 218.326 230.791 1.00 57.92  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 280.386 216.302 229.014 1.00 62.18  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 281.328 215.527 228.122 1.00 64.19  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 282.568 216.045 227.773 1.00 60.04  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 280.981 214.274 227.635 1.00 64.87  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 283.433 215.339 226.960 1.00 61.17  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 281.839 213.561 226.822 1.00 67.32  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 283.064 214.098 226.488 1.00 67.39  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 283.922 213.390 225.678 1.00 65.61  ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 279.537 216.825 232.467 1.00 59.43  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 278.575 217.565 233.278 1.00 54.77  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 279.112 218.935 233.676 1.00 55.20  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 278.383 219.932 233.622 1.00 59.17  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 278.200 216.755 234.518 1.00 53.92  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 280.382 219.004 234.092 1.00 58.09  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 280.949 220.292 234.490 1.00 57.06  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 281.036 221.275 233.327 1.00 59.08  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 280.601 222.429 233.492 1.00 61.07  ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 282.308 220.085 235.168 1.00 57.32  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 282.340 218.995 236.236 1.00 62.49  ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 282.471 217.598 235.659 1.00 67.98  ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 283.156 217.444 234.627 1.00 66.93  ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 281.886 216.656 236.234 1.00 62.24  ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 281.577 220.920 232.153 1.00 53.09  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 281.577 221.902 231.054 1.00 49.59  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 280.189 222.216 230.527 1.00 48.98  ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 279.970 223.315 230.003 1.00 55.62  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 282.460 221.238 229.988 1.00 48.27  ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 282.393 219.793 230.285 1.00 53.67  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 282.295 219.688 231.775 1.00 54.90  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 279.244 221.280 230.640 1.00 37.44  ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 277.882 221.549 230.186 1.00 37.09  ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 277.245 222.664 231.003 1.00 46.07  ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 276.604 223.565 230.452 1.00 47.54  ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 277.040 220.275 230.259 1.00 43.01  ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 275.600 220.383 229.755 1.00 40.91  ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 275.576 220.588 228.251 1.00 44.62  ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 274.806 219.147 230.141 1.00 41.45  ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 277.415 222.619 232.326 1.00 45.04  ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 276.880 223.676 233.177 1.00 38.61  ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 277.561 225.010 232.896 1.00 44.42  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 276.901 226.055 232.864 1.00 49.36  ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 277.035 223.294 234.649 1.00 43.80  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 276.418 222.021 234.878 1.00 54.85  ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 276.380 224.334 235.543 1.00 46.71  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 278.879 224.993 232.684 1.00 44.06  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 279.605 226.228 232.409 1.00 38.17  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 279.119 226.876 231.118 1.00 43.30  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 278.957 228.100 231.046 1.00 51.74  ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 281.107 225.948 232.343 1.00 37.67  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 278.888 226.067 230.082 1.00 37.03  ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 278.361 226.602 228.831 1.00 30.22  ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 276.956 227.160 229.018 1.00 47.89  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 276.617 228.210 228.460 1.00 54.58  ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 278.372 225.520 227.751 1.00 34.65  ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 276.121 226.464 229.793 1.00 38.49  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 274.768 226.947 230.049 1.00 26.03  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 274.783 228.257 230.826 1.00 36.86  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 274.019 229.179 230.517 1.00 46.86  ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 273.971 225.883 230.803 1.00 29.64  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 273.701 224.627 229.996 1.00 48.13  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 272.838 223.366 230.946 1.00 45.39  ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 271.226 224.121 231.096 1.00 36.06  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 275.641 228.355 231.843 1.00 42.92  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 275.719 229.577 232.639 1.00 34.36  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 276.235 230.735 231.792 1.00 40.77  ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 275.711 231.853 231.855 1.00 51.36  ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 276.597 229.353 233.884 1.00 36.01  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 276.873 230.673 234.586 1.00 42.28  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 275.929 228.378 234.837 1.00 36.19  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 277.270 230.484 230.986 1.00 42.41  ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 277.894 231.560 230.222 1.00 40.31  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 276.936 232.136 229.186 1.00 41.34  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 276.778 233.358 229.086 1.00 53.56  ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 279.171 231.057 229.549 1.00 42.96  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 279.865 232.107 228.697 1.00 47.16  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 281.235 231.667 228.225 1.00 54.10  ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 282.097 231.383 229.082 1.00 56.12  ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 281.450 231.605 226.997 1.00 51.66  ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 276.288 231.271 228.402 1.00 33.95  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 275.382 231.760 227.368 1.00 39.07  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 274.181 232.473 227.976 1.00 39.63  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 273.717 233.488 227.442 1.00 50.38  ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 274.923 230.612 226.472 1.00 41.23  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 274.066 231.056 225.322 1.00 43.59  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 274.563 231.929 224.370 1.00 41.50  ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 272.760 230.613 225.201 1.00 45.43  ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 273.778 232.346 223.314 1.00 43.67  ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 271.970 231.027 224.146 1.00 41.36  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 272.479 231.895 223.203 1.00 37.18  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 273.657 231.951 229.087 1.00 36.93  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 272.554 232.621 229.767 1.00 40.93  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 272.976 233.994 230.275 1.00 46.75  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 272.211 234.961 230.182 1.00 50.09  ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 272.045 231.755 230.919 1.00 35.22  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 271.227 232.511 231.940 1.00 44.12  ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 269.967 233.001 231.624 1.00 44.00  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 271.717 232.737 233.219 1.00 39.36  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 269.218 233.694 232.555 1.00 41.01  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 270.975 233.428 234.155 1.00 37.87  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 269.727 233.904 233.818 1.00 41.98  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 268.988 234.594 234.751 1.00 51.49  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 274.189 234.097 230.821 1.00 38.57  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 274.689 235.386 231.289 1.00 33.48  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 274.874 236.359 230.130 1.00 42.08  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 274.514 237.537 230.232 1.00 51.63  ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 276.003 235.193 232.046 1.00 40.88  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 275.808 234.260 233.116 1.00 37.92  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 276.489 236.515 232.619 1.00 46.47  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 275.438 235.881 229.018 1.00 50.03  ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 275.665 236.750 227.866 1.00 41.04  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 274.349 237.226 227.265 1.00 43.33  ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 274.206 238.399 226.901 1.00 53.93  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 276.505 236.020 226.818 1.00 42.23  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 277.927 235.721 227.262 1.00 50.35  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 278.857 234.788 226.034 1.00 68.36  ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 279.074 236.031 224.765 1.00 51.86  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 273.374 236.322 227.142 1.00 41.27  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 272.075 236.703 226.597 1.00 36.69  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 271.358 237.686 227.514 1.00 40.04  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 270.712 238.629 227.042 1.00 46.53  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 271.217 235.460 226.366 1.00 44.17  ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 271.962 234.442 225.721 1.00 56.13  ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 271.457 237.479 228.829 1.00 46.54  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 270.821 238.382 229.781 1.00 41.77  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 271.399 239.789 229.717 1.00 50.75  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 270.680 240.756 229.990 1.00 53.16  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 270.958 237.825 231.199 1.00 41.57  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 269.953 238.383 232.191 1.00 42.21  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 270.137 237.813 233.583 1.00 52.75  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 269.176 237.393 234.226 1.00 50.83  ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 271.378 237.795 234.055 1.00 51.90  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 272.677 239.926 229.364 1.00 53.58  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 273.299 241.237 229.237 1.00 50.28  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 273.054 241.875 227.879 1.00 49.75  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 272.820 243.087 227.805 1.00 53.52  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 274.808 241.129 229.478 1.00 50.91  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 275.189 240.717 230.889 1.00 58.05  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 276.688 240.739 231.114 1.00 67.30  ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 277.439 240.739 230.116 1.00 61.82  ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 277.115 240.754 232.287 1.00 66.16  ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 273.104 241.087 226.803 1.00 54.74  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 272.923 241.631 225.462 1.00 51.41  ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 271.498 242.123 225.237 1.00 54.40  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 271.294 243.184 224.635 1.00 58.74  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 273.296 240.576 224.419 1.00 44.45  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 272.957 240.958 222.989 1.00 52.70  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 273.975 241.933 222.421 1.00 51.06  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 273.928 241.991 220.965 1.00 57.73  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 272.980 242.600 220.266 1.00 62.93  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 271.977 243.227 220.859 1.00 57.16  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 273.039 242.580 218.937 1.00 56.35  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 270.505 241.376 225.714 1.00 47.33  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 269.099 241.710 225.517 1.00 41.26  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 268.486 242.079 226.859 1.00 47.64  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 268.549 241.294 227.811 1.00 57.97  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 268.343 240.542 224.881 1.00 41.16  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 269.048 239.935 223.703 1.00 46.16  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 269.175 240.638 222.517 1.00 45.49  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 269.584 238.661 223.781 1.00 48.21  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 269.823 240.082 221.432 1.00 42.28  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 270.233 238.100 222.699 1.00 46.31  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 270.353 238.812 221.523 1.00 43.27  ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 267.891 243.268 226.931 1.00 50.89  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 267.248 243.768 228.138 1.00 56.10  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 265.883 244.341 227.774 1.00 51.07  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 265.503 244.404 226.602 1.00 53.03  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 268.113 244.827 228.835 1.00 57.64  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 268.469 245.850 227.898 1.00 58.89  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 269.378 244.200 229.404 1.00 50.75  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 265.140 244.768 228.798 1.00 55.56  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 263.818 245.343 228.581 1.00 57.35  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 263.868 246.701 227.893 1.00 60.88  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 262.826 247.177 227.431 1.00 62.79  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 263.072 245.468 229.910 1.00 57.67  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 262.527 244.154 230.440 1.00 59.11  ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 261.359 244.349 231.386 1.00 64.32  ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 261.495 244.192 232.599 1.00 64.76  ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 260.202 244.694 230.834 1.00 57.24  ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 265.040 247.334 227.821 1.00 64.25  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 265.154 248.599 227.104 1.00 60.95  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 264.892 248.412 225.615 1.00 63.18  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 264.283 249.276 224.972 1.00 67.58  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 266.534 249.212 227.336 1.00 61.22  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 266.728 249.686 228.763 1.00 69.18  ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 265.726 250.063 229.407 1.00 70.84  ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 267.881 249.682 229.241 1.00 71.83  ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 265.344 247.293 225.049 1.00 59.69  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 265.111 247.019 223.635 1.00 56.38  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 263.674 246.570 223.392 1.00 60.42  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 262.925 247.218 222.653 1.00 60.01  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 266.098 245.961 223.133 1.00 57.82  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 267.398 246.221 223.677 1.00 60.50  ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 266.175 245.983 221.615 1.00 60.11  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 263.274 245.462 224.007 1.00 59.42  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 261.925 244.936 223.881 1.00 55.89  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 261.375 244.577 225.252 1.00 50.41  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 262.118 244.113 226.122 1.00 53.29  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 261.894 243.697 222.973 1.00 51.11  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 262.378 243.953 221.556 1.00 54.31  ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 261.348 244.676 220.711 1.00 57.29  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 260.168 244.725 221.057 1.00 52.56  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 261.791 245.243 219.595 1.00 57.36  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 260.074 244.784 225.471 1.00 53.92  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 259.498 244.495 226.796 1.00 56.26  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 259.607 243.039 227.210 1.00 59.81  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 259.702 242.753 228.410 1.00 62.00  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 258.032 244.926 226.640 1.00 55.60  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 257.780 244.898 225.168 1.00 54.54  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 259.068 245.309 224.533 1.00 57.71  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 259.597 242.109 226.259 1.00 51.58  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 259.603 240.685 226.565 1.00 48.01  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 261.005 240.101 226.668 1.00 49.12  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 261.141 238.885 226.837 1.00 53.70  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 258.804 239.916 225.508 1.00 45.16  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 259.348 240.055 224.121 1.00 41.35  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 259.162 241.187 223.358 1.00 47.98  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 260.074 239.203 223.359 1.00 42.95  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 259.749 241.027 222.186 1.00 51.01  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 260.310 239.832 222.160 1.00 46.95  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 262.046 240.927 226.572 1.00 41.53  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 263.427 240.453 226.659 1.00 36.35  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 263.829 240.240 228.121 1.00 47.01  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 264.770 240.840 228.641 1.00 55.49  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 264.366 241.430 225.964 1.00 42.96  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 264.387 241.310 224.457 1.00 46.27  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 263.519 240.453 223.794 1.00 40.52  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 265.277 242.056 223.697 1.00 51.70  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 263.537 240.344 222.418 1.00 42.82  ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 265.302 241.953 222.321 1.00 43.76  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 264.430 241.095 221.687 1.00 40.87  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 264.452 240.989 220.316 1.00 52.67  ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 263.087 239.359 228.785 1.00 47.81  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 263.318 239.018 230.184 1.00 44.04  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 263.903 237.615 230.235 1.00 48.30  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 263.243 236.644 229.844 1.00 50.26  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 262.026 239.107 231.011 1.00 43.18  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 261.593 240.565 231.171 1.00 47.33  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 262.219 238.456 232.371 1.00 47.11  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 260.094 240.757 231.179 1.00 46.74  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 265.139 237.509 230.713 1.00 39.88  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 265.820 236.231 230.867 1.00 31.77  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 266.071 235.981 232.346 1.00 47.30  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 266.599 236.850 233.047 1.00 50.23  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 267.131 236.205 230.078 1.00 35.74  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 266.930 236.315 228.584 1.00 39.79  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 266.297 235.302 227.875 1.00 42.97  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 267.362 237.433 227.885 1.00 40.55  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 266.106 235.398 226.511 1.00 39.14  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 267.175 237.537 226.519 1.00 43.21  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 266.546 236.517 225.838 1.00 46.76  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 266.358 236.615 224.479 1.00 49.57  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 265.688 234.797 232.811 1.00 39.93  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 265.718 234.458 234.226 1.00 25.99  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 266.192 233.018 234.394 1.00 35.29  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 266.356 232.307 233.394 1.00 46.73  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 264.328 234.655 234.836 1.00 36.62  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 263.347 233.930 234.115 1.00 37.02  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 266.438 232.550 235.622 1.00 41.21  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 266.746 231.122 235.811 1.00 34.91  ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 265.636 230.189 235.350 1.00 37.57  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 265.878 228.979 235.253 1.00 52.77  ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 266.977 231.010 237.323 1.00 34.57  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 267.448 232.361 237.718 1.00 34.20  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 266.685 233.324 236.853 1.00 36.58  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 264.435 230.704 235.076 1.00 29.89  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 263.389 229.872 234.489 1.00 25.10  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 263.803 229.358 233.117 1.00 36.75  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 263.522 228.205 232.769 1.00 45.00  ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 262.083 230.659 234.394 1.00 29.65  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 261.471 231.017 235.735 1.00 44.16  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 260.004 231.371 235.582 1.00 36.08  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 259.825 232.565 234.766 1.00 42.82  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 259.220 233.670 235.177 1.00 49.18  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 258.710 233.767 236.394 1.00 40.25  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 259.125 234.704 234.347 1.00 43.49  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 264.463 230.202 232.319 1.00 39.75  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 265.006 229.742 231.046 1.00 28.43  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 266.070 228.675 231.263 1.00 33.93  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 266.170 227.717 230.487 1.00 50.15  ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 265.582 230.921 230.260 1.00 26.08  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 264.880 232.248 230.509 1.00 40.60  ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 263.492 232.308 229.902 1.00 47.49  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 263.162 231.439 229.068 1.00 51.37  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 262.728 233.228 230.261 1.00 41.64  ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 266.881 228.830 232.312 1.00 32.54  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 267.865 227.807 232.648 1.00 27.01  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 267.189 226.503 233.051 1.00 33.27  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 267.651 225.416 232.684 1.00 40.73  ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 268.777 228.307 233.767 1.00 33.86  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 269.992 229.075 233.282 1.00 33.42  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 271.242 227.991 232.573 1.00 59.04  ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 272.443 227.962 233.898 1.00 33.44  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 266.098 226.589 233.816 1.00 35.38  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 265.377 225.387 234.224 1.00 29.24  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 264.778 224.671 233.019 1.00 38.50  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 264.849 223.442 232.913 1.00 52.06  ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 264.288 225.745 235.235 1.00 34.79  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 264.864 226.488 236.316 1.00 46.84  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 263.637 224.486 235.785 1.00 36.45  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 264.180 225.429 232.096 1.00 43.42  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 263.652 224.828 230.875 1.00 33.24  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 264.774 224.259 230.017 1.00 36.75  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 264.575 223.283 229.286 1.00 46.86  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 262.847 225.858 230.086 1.00 33.22  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 261.502 226.202 230.695 1.00 43.32  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 260.800 227.276 229.883 1.00 50.32  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 259.913 226.703 228.877 1.00 55.15  ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 258.628 226.440 229.071 1.00 55.97  ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 258.039 226.692 230.228 1.00 50.34  ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 257.918 225.911 228.079 1.00 52.70  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 265.959 224.867 230.089 1.00 35.01  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 267.110 224.354 229.356 1.00 27.90  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 267.502 222.969 229.856 1.00 38.11  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 267.834 222.080 229.065 1.00 49.18  ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 268.276 225.334 229.483 1.00 34.23  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 269.282 225.245 228.382 1.00 36.68  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 269.409 224.245 227.466 1.00 34.87  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 270.304 226.200 228.079 1.00 35.52  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 270.449 224.516 226.611 1.00 37.54  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 271.015 225.711 226.967 1.00 36.56  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 270.688 227.421 228.642 1.00 36.65  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 272.087 226.400 226.406 1.00 33.80  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 271.753 228.102 228.084 1.00 38.53  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 272.439 227.591 226.977 1.00 33.16  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 267.470 222.769 231.175 1.00 36.32  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 267.803 221.464 231.737 1.00 27.63  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 266.725 220.442 231.393 1.00 42.03  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 267.027 219.287 231.069 1.00 55.89  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 268.018 221.576 233.258 1.00 40.12  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 268.438 220.239 233.828 1.00 41.59  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 269.061 222.630 233.567 1.00 46.00  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 265.453 220.844 231.468 1.00 39.95  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 264.365 219.934 231.121 1.00 41.43  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 264.418 219.549 229.648 1.00 49.19  ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 264.179 218.390 229.288 1.00 56.87  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 263.016 220.569 231.459 1.00 43.64  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 262.813 220.878 232.930 1.00 51.39  ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 262.751 219.608 233.756 1.00 59.43  ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 261.601 218.783 233.411 1.00 61.03  ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 261.476 217.504 233.735 1.00 57.80  ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 262.406 216.875 234.436 1.00 50.51  ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 260.392 216.838 233.349 1.00 55.16  ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 264.721 220.514 228.777 1.00 43.66  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 264.755 220.229 227.351 1.00 35.70  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 265.796 219.187 226.988 1.00 39.18  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 265.546 218.298 226.172 1.00 51.28  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 266.985 219.291 227.584 1.00 36.45  ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 268.016 218.284 227.351 1.00 30.11  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 267.633 216.966 228.011 1.00 38.74  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 267.802 215.889 227.427 1.00 49.91  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 269.385 218.789 227.844 1.00 33.30  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 269.700 220.157 227.238 1.00 35.50  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 270.477 217.791 227.498 1.00 38.93  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 271.020 220.737 227.694 1.00 40.45  ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 267.109 217.029 229.238 1.00 48.04  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 266.736 215.810 229.951 1.00 46.84  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 265.627 215.058 229.227 1.00 49.31  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 265.671 213.826 229.119 1.00 59.67  ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 266.309 216.144 231.379 1.00 45.84  ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 265.694 214.988 232.112 1.00 50.94  ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 266.462 213.898 232.485 1.00 49.32  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 264.344 214.986 232.420 1.00 47.95  ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 265.897 212.832 233.157 1.00 51.50  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 263.774 213.922 233.090 1.00 48.09  ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 264.551 212.845 233.459 1.00 51.52  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 264.617 215.778 228.733 1.00 41.73  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 263.532 215.123 228.010 1.00 48.24  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 264.025 214.492 226.717 1.00 50.35  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 263.507 213.450 226.299 1.00 58.65  ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 262.411 216.123 227.727 1.00 49.91  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 261.586 216.484 228.951 1.00 58.38  ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 260.519 217.517 228.651 1.00 60.67  ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 260.520 218.064 227.529 1.00 51.95  ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 259.681 217.786 229.537 1.00 61.46  ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 265.019 215.101 226.072 1.00 46.19  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 265.587 214.507 224.869 1.00 41.46  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 266.474 213.312 225.194 1.00 46.65  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 266.424 212.294 224.498 1.00 53.86  ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 266.379 215.554 224.088 1.00 41.95  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 267.288 213.411 226.247 1.00 51.32  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 268.233 212.342 226.557 1.00 50.25  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 267.540 211.100 227.099 1.00 56.00  ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 268.106 210.002 227.028 1.00 64.33  ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 269.267 212.824 227.571 1.00 50.10  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 270.254 213.885 227.109 1.00 51.65  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 271.209 214.211 228.232 1.00 53.27  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 271.004 213.378 225.905 1.00 55.25  ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 266.343 211.254 227.664 1.00 54.20  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 265.684 210.169 228.381 1.00 58.77  ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 265.390 208.971 227.482 1.00 68.12  ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 265.642 207.831 227.890 1.00 68.77  ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 264.403 210.679 229.044 1.00 61.86  ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 263.678 209.664 229.913 1.00 66.17  ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 262.444 210.296 230.511 1.00 67.16  ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 261.457 210.613 229.487 1.00 77.27  ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 260.363 211.329 229.704 1.00 74.88  ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 260.081 211.820 230.901 1.00 65.42  ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 259.537 211.567 228.692 1.00 75.77  ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 264.843 209.154 226.270 1.00 70.10  ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 264.579 207.970 225.439 1.00 63.08  ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 265.838 207.306 224.930 1.00 62.80  ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 265.817 206.096 224.679 1.00 66.41  ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 263.720 208.508 224.263 1.00 65.76  ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 264.038 209.941 224.188 1.00 71.14  ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 264.056 210.238 225.713 1.00 71.20  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 266.937 208.047 224.798 1.00 68.10  ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 268.122 207.513 224.141 1.00 68.93  ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 268.951 206.679 225.111 1.00 71.14  ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 269.215 207.098 226.243 1.00 71.50  ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 268.958 208.642 223.542 1.00 64.29  ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 268.499 209.277 222.222 1.00 73.89  ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 267.251 210.147 222.373 1.00 69.14  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 269.640 210.069 221.604 1.00 76.69  ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 269.334 205.482 224.659 1.00 79.16  ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 270.179 204.595 225.450 1.00 81.99  ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 271.631 205.065 225.439 1.00 81.24  ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 272.322 204.990 226.462 1.00 79.71  ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 270.066 203.162 224.912 1.00 82.51  ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 268.634 202.617 224.855 1.00 85.20  ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 268.015 202.479 226.231 1.00 86.46  ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 268.184 201.407 226.859 1.00 84.58  ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 267.355 203.434 226.685 1.00 82.30  ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 272.110 205.560 224.299 1.00 75.85  ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 273.476 206.043 224.169 1.00 75.52  ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 273.499 207.228 223.216 1.00 76.62  ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 272.615 207.383 222.369 1.00 77.57  ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 274.425 204.948 223.658 1.00 75.06  ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 275.746 205.483 223.520 1.00 75.00  ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 273.957 204.424 222.306 1.00 73.21  ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 274.531 208.064 223.362 1.00 64.79  ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 274.672 209.255 222.540 1.00 61.70  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 276.085 209.786 222.692 1.00 59.70  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 276.580 209.863 223.824 1.00 63.84  ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 273.657 210.329 222.945 1.00 59.27  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 273.715 211.654 222.182 1.00 61.53  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 273.076 211.512 220.812 1.00 66.45  ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 273.037 212.751 222.979 1.00 62.64  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 276.757 210.151 221.607 1.00 58.72  ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 278.097 210.728 221.722 1.00 61.00  ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 278.052 212.165 222.225 1.00 62.59  ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 276.990 212.752 222.440 1.00 64.58  ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 278.631 210.665 220.286 1.00 60.81  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 277.408 210.723 219.439 1.00 58.88  ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 276.347 209.977 220.204 1.00 58.08  ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 279.249 212.727 222.413 1.00 59.87  ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 279.359 214.098 222.904 1.00 57.26  ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 278.805 215.088 221.886 1.00 56.26  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 278.201 216.101 222.260 1.00 57.91  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 280.822 214.416 223.279 1.00 57.26  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 281.747 214.221 222.085 1.00 57.31  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 280.941 215.830 223.832 1.00 56.21  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 278.990 214.814 220.592 1.00 59.08  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 278.466 215.707 219.563 1.00 56.99  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 276.944 215.764 219.603 1.00 53.70  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 276.349 216.829 219.401 1.00 55.01  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 278.952 215.263 218.185 1.00 59.37  ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 280.404 215.605 217.902 1.00 61.80  ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 281.356 214.513 218.347 1.00 64.78  ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 280.879 213.424 218.729 1.00 59.91  ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 282.583 214.744 218.316 1.00 67.66  ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 276.296 214.625 219.852 1.00 50.17  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 274.847 214.621 219.961 1.00 52.68  ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 274.347 215.429 221.142 1.00 54.86  ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 273.325 216.114 221.048 1.00 62.12  ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 275.055 215.357 222.273 1.00 38.65  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 274.667 216.140 223.442 1.00 41.33  ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 274.783 217.634 223.170 1.00 43.96  ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 273.921 218.418 223.583 1.00 51.35  ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 275.523 215.744 224.645 1.00 46.54  ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 275.409 216.629 225.889 1.00 42.71  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 274.098 216.374 226.615 1.00 43.57  ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 276.593 216.409 226.817 1.00 43.97  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 275.847 218.047 222.478 1.00 37.59  ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 276.028 219.462 222.167 1.00 36.68  ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 274.953 219.940 221.199 1.00 44.36  ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 274.482 221.080 221.288 1.00 52.72  ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 277.445 219.706 221.618 1.00 41.28  ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 278.483 219.266 222.645 1.00 46.84  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 277.651 221.171 221.299 1.00 42.27  ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 278.389 220.026 223.943 1.00 57.74  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 274.547 219.081 220.260 1.00 42.62  ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 273.469 219.445 219.346 1.00 38.09  ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 272.162 219.664 220.097 1.00 45.25  ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 271.409 220.595 219.788 1.00 49.63  ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 273.301 218.370 218.274 1.00 42.70  ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 272.432 218.803 217.107 1.00 42.98  ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 272.590 217.875 215.917 1.00 45.53  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 271.890 218.380 214.742 1.00 53.50  ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 272.347 219.345 213.956 1.00 52.01  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 273.509 219.933 214.188 1.00 50.44  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 271.619 219.729 212.911 1.00 52.40  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 271.871 218.811 221.082 1.00 43.05  ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 270.704 219.028 221.933 1.00 36.56  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 270.874 220.305 222.744 1.00 47.33  ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 269.923 221.075 222.928 1.00 54.54  ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 270.467 217.806 222.840 1.00 32.79  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 270.285 216.544 221.997 1.00 43.96  ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 269.255 218.027 223.728 1.00 43.45  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 270.136 215.281 222.813 1.00 44.80  ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 272.088 220.549 223.243 1.00 41.00  ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 272.359 221.772 223.991 1.00 25.05  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 272.133 223.008 223.129 1.00 37.04  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 271.554 223.999 223.590 1.00 45.30  ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 273.791 221.740 224.528 1.00 33.02  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 274.223 222.999 225.216 1.00 42.35  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 274.104 223.290 226.542 1.00 35.72  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 274.857 224.134 224.612 1.00 41.91  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 274.619 224.536 226.802 1.00 32.82  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 275.086 225.076 225.633 1.00 39.13  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 275.248 224.446 223.307 1.00 38.51  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 275.689 226.307 225.391 1.00 44.78  ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 275.846 225.669 223.068 1.00 40.82  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 276.061 226.585 224.105 1.00 41.71  ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 272.584 222.970 221.873 1.00 41.52  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 272.399 224.112 220.984 1.00 34.16  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 270.939 224.277 220.582 1.00 38.42  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 270.449 225.406 220.462 1.00 54.14  ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 273.280 223.961 219.745 1.00 33.07  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 270.233 223.166 220.356 1.00 29.16  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 268.838 223.249 219.934 1.00 31.74  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 267.972 223.899 221.005 1.00 38.12  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 267.108 224.729 220.697 1.00 37.88  ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 268.309 221.858 219.590 1.00 31.76  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 266.874 221.848 219.163 1.00 31.08  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 265.868 221.325 219.946 1.00 37.38  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 266.276 222.299 218.035 1.00 32.11  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 264.713 221.453 219.319 1.00 39.07  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 264.933 222.042 218.158 1.00 33.70  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 268.185 223.532 222.271 1.00 38.90  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 267.414 224.137 223.353 1.00 32.74  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 267.745 225.616 223.507 1.00 43.08  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 266.860 226.426 223.805 1.00 55.34  ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 267.666 223.388 224.660 1.00 37.90  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 267.317 221.912 224.602 1.00 45.51  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 265.842 221.673 224.353 1.00 52.65  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 265.016 222.452 224.875 1.00 53.26  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 265.508 220.709 223.633 1.00 52.20  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 269.013 225.985 223.315 1.00 34.12  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 269.393 227.392 223.389 1.00 24.37  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 268.706 228.206 222.301 1.00 37.66  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 268.283 229.343 222.538 1.00 53.34  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 270.911 227.532 223.285 1.00 21.36  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 268.594 227.642 221.096 1.00 33.73  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 267.921 228.343 220.008 1.00 30.74  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 266.441 228.547 220.308 1.00 36.83  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 265.885 229.615 220.031 1.00 45.72  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 268.100 227.572 218.700 1.00 36.48  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 269.497 227.607 218.083 1.00 39.96  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 269.616 226.588 216.963 1.00 39.79  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 269.810 229.002 217.577 1.00 37.91  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 265.785 227.531 220.873 1.00 39.00  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 264.350 227.629 221.115 1.00 35.01  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 264.033 228.526 222.305 1.00 31.10  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 262.924 229.065 222.392 1.00 47.38  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 263.758 226.236 221.328 1.00 35.13  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 263.914 225.299 220.137 1.00 34.59  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 262.931 225.625 219.020 1.00 32.07  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 263.408 226.692 218.148 1.00 33.13  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 264.379 226.558 217.254 1.00 41.18  ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 265.001 225.404 217.076 1.00 34.61  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 264.734 227.608 216.520 1.00 50.46  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 264.981 228.698 223.225 1.00 27.86  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 264.729 229.465 224.440 1.00 37.05  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 265.144 230.926 224.317 1.00 37.39  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 264.466 231.807 224.856 1.00 43.37  ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 265.458 228.826 225.624 1.00 34.78  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 264.885 227.514 226.156 1.00 32.40  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 265.859 226.882 227.127 1.00 36.69  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 263.538 227.744 226.821 1.00 38.33  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 266.246 231.206 223.620 1.00 35.53  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 266.807 232.548 223.575 1.00 34.61  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 266.645 233.243 222.231 1.00 42.75  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 266.828 234.463 222.162 1.00 55.56  ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 268.297 232.508 223.944 1.00 34.05  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 268.563 232.020 225.339 1.00 45.38  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 268.510 232.891 226.414 1.00 41.88  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 268.863 230.689 225.577 1.00 39.10  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 268.753 232.445 227.699 1.00 42.21  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 269.107 230.237 226.859 1.00 35.22  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 269.051 231.116 227.921 1.00 40.74  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 266.307 232.512 221.167 1.00 34.04  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 266.194 233.099 219.840 1.00 27.21  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 264.767 233.171 219.317 1.00 40.32  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 264.507 233.943 218.389 1.00 50.87  ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 267.049 232.310 218.836 1.00 32.25  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 267.458 233.096 217.603 1.00 42.62  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 268.078 232.217 216.537 1.00 43.92  ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 269.229 232.413 216.147 1.00 38.78  ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 267.317 231.241 216.059 1.00 45.64  ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 263.840 232.396 219.885 1.00 41.26  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 262.468 232.398 219.389 1.00 35.95  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 261.771 233.728 219.646 1.00 39.66  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 260.940 234.156 218.837 1.00 43.94  ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 261.680 231.255 220.024 1.00 40.23  ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 262.036 229.905 219.435 1.00 49.51  ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 262.935 229.851 218.570 1.00 43.82  ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 261.417 228.898 219.837 1.00 50.55  ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 262.088 234.391 220.757 1.00 42.30  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 261.448 235.648 221.117 1.00 39.13  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 262.117 236.866 220.495 1.00 45.73  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 261.585 237.974 220.620 1.00 48.58  ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 261.427 235.808 222.640 1.00 41.36  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 262.789 236.097 223.247 1.00 39.36  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 262.702 236.241 224.755 1.00 46.13  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 262.385 234.976 225.405 1.00 44.92  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 262.132 234.842 226.700 1.00 49.67  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 262.149 235.880 227.518 1.00 49.33  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 261.855 233.635 227.185 1.00 50.45  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 263.258 236.692 219.836 1.00 42.57  ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 263.979 237.823 219.270 1.00 37.84  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 263.231 238.404 218.076 1.00 41.06  ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 262.607 237.684 217.292 1.00 48.80  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 265.388 237.399 218.859 1.00 42.34  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 266.288 236.988 220.025 1.00 30.15  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 267.679 236.630 219.537 1.00 39.26  ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 266.349 238.093 221.067 1.00 32.57  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 263.300 239.728 217.944 1.00 41.13  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 262.560 240.444 216.911 1.00 45.09  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 263.447 240.680 215.695 1.00 51.14  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 263.150 240.202 214.594 1.00 57.12  ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 262.010 241.776 217.451 1.00 41.57  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 261.193 242.484 216.383 1.00 46.43  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 261.178 241.539 218.701 1.00 40.22  ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 264.537 241.417 215.885 1.00 54.40  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 265.402 241.788 214.778 1.00 53.36  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 266.258 240.605 214.332 1.00 59.14  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 266.520 239.668 215.091 1.00 65.02  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 266.294 242.967 215.166 1.00 57.56  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 265.565 244.081 215.899 1.00 61.76  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 264.769 244.972 214.965 1.00 66.41  ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 264.923 244.835 213.733 1.00 63.49  ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 263.988 245.810 215.463 1.00 68.23  ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 266.698 240.664 213.072 1.00 62.95  ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 267.510 239.585 212.521 1.00 59.34  ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 268.934 239.614 213.059 1.00 60.99  ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 269.563 238.558 213.195 1.00 63.77  ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 267.521 239.660 210.995 1.00 64.99  ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 268.103 238.415 210.355 1.00 70.07  ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 267.332 237.473 210.076 1.00 67.35  ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 269.331 238.378 210.133 1.00 69.39  ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 269.465 240.802 213.360 1.00 60.00  ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 270.814 240.878 213.912 1.00 59.14  ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 270.876 240.294 215.318 1.00 63.89  ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 271.915 239.759 215.719 1.00 71.07  ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 271.315 242.324 213.903 1.00 61.36  ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 270.627 243.250 214.893 1.00 68.66  ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 269.465 244.004 214.278 1.00 70.54  ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 269.024 243.623 213.174 1.00 69.04  ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 268.993 244.979 214.899 1.00 64.05  ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 269.783 240.392 216.079 1.00 60.58  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 269.731 239.738 217.382 1.00 54.28  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 269.779 238.223 217.236 1.00 55.37  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 270.464 237.538 218.006 1.00 58.66  ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 268.472 240.167 218.134 1.00 55.59  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 268.375 241.662 218.381 1.00 56.15  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 266.968 242.103 218.731 1.00 62.25  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 266.062 241.244 218.743 1.00 61.94  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 266.768 243.307 218.995 1.00 65.46  ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 269.057 237.682 216.253 1.00 50.50  ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 269.082 236.242 216.021 1.00 49.07  ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 270.430 235.796 215.468 1.00 53.14  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 270.902 234.696 215.780 1.00 56.58  ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 267.949 235.844 215.076 1.00 45.82  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 266.586 236.370 215.496 1.00 43.61  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 265.461 235.620 214.805 1.00 53.52  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 265.062 236.264 213.560 1.00 56.57  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 263.894 236.862 213.367 1.00 61.67  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 262.979 236.916 214.321 1.00 55.43  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 263.638 237.420 212.188 1.00 59.96  ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 271.060 236.631 214.640 1.00 56.66  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 272.394 236.311 214.142 1.00 57.36  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 273.410 236.283 215.276 1.00 55.96  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 274.314 235.439 215.289 1.00 57.39  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 272.810 237.318 213.069 1.00 61.18  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 274.134 236.995 212.397 1.00 65.52  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 274.457 237.992 211.297 1.00 63.13  ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 274.661 239.338 211.819 1.00 66.82  ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 273.863 240.367 211.569 1.00 69.71  ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 272.792 240.242 210.802 1.00 64.83  ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 274.147 241.552 212.102 1.00 64.66  ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 273.281 237.204 216.235 1.00 52.23  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 274.176 237.210 217.388 1.00 50.81  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 274.021 235.937 218.211 1.00 54.51  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 275.012 235.371 218.686 1.00 60.27  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 273.908 238.446 218.248 1.00 50.86  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 274.775 238.546 219.468 1.00 56.57  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 275.963 239.208 219.576 1.00 57.36  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 274.515 237.978 220.758 1.00 58.18  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 276.462 239.082 220.849 1.00 53.03  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 275.591 238.332 221.595 1.00 50.77  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 273.478 237.201 221.285 1.00 55.67  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 275.662 237.936 222.928 1.00 47.62  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 273.550 236.810 222.609 1.00 50.83  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 274.633 237.177 223.415 1.00 54.67  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 272.781 235.478 218.397 1.00 42.79  ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 272.550 234.237 219.130 1.00 40.40  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 273.142 233.042 218.393 1.00 47.77  ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 273.732 232.150 219.014 1.00 56.69  ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 271.052 234.038 219.364 1.00 47.63  ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 270.539 235.132 220.133 1.00 49.08  ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 270.792 232.740 220.111 1.00 49.00  ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 272.994 233.007 217.066 1.00 50.24  ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 273.547 231.904 216.286 1.00 48.07  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 275.066 231.852 216.396 1.00 55.49  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 275.648 230.772 216.549 1.00 53.96  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 273.126 232.035 214.822 1.00 56.01  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 271.753 231.453 214.555 1.00 60.62  ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 271.397 230.447 215.202 1.00 62.19  ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 271.029 232.002 213.698 1.00 56.63  ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 275.724 233.010 216.317 1.00 57.86  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 277.182 233.039 216.381 1.00 52.54  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 277.687 232.679 217.773 1.00 58.60  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 278.613 231.872 217.913 1.00 61.65  ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 277.698 234.418 215.971 1.00 56.84  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 277.558 234.725 214.490 1.00 66.04  ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 277.714 236.202 214.187 1.00 71.07  ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 277.827 236.998 215.144 1.00 64.30  ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 277.724 236.569 212.993 1.00 63.74  ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 277.088 233.262 218.813 1.00 57.30  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 277.615 233.089 220.162 1.00 50.68  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 277.350 231.691 220.705 1.00 52.12  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 278.078 231.227 221.589 1.00 61.14  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 277.026 234.149 221.090 1.00 52.23  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 277.651 235.511 220.877 1.00 60.29  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 278.598 235.888 221.566 1.00 63.66  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 277.134 236.252 219.904 1.00 57.95  ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 276.321 231.009 220.200 1.00 44.61  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 276.105 229.614 220.575 1.00 48.33  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 277.285 228.764 220.120 1.00 52.61  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 277.771 227.895 220.854 1.00 52.24  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 274.775 229.100 219.995 1.00 47.01  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 273.612 229.490 220.908 1.00 49.96  ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 274.811 227.591 219.803 1.00 50.06  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 272.255 229.316 220.272 1.00 48.85  ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 277.767 229.012 218.900 1.00 58.49  ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 278.922 228.280 218.392 1.00 54.36  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 280.167 228.571 219.223 1.00 60.41  ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 280.941 227.661 219.541 1.00 66.49  ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 279.161 228.639 216.925 1.00 59.02  ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 278.140 228.013 215.997 1.00 63.74  ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 277.071 227.593 216.486 1.00 61.76  ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 278.406 227.941 214.780 1.00 66.87  ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 280.376 229.840 219.582 1.00 51.56  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 281.576 230.214 220.325 1.00 45.87  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 281.557 229.640 221.737 1.00 52.54  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 282.575 229.142 222.230 1.00 59.83  ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 281.716 231.736 220.368 1.00 53.15  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 280.663 232.294 221.162 1.00 57.37  ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 281.651 232.318 218.965 1.00 52.54  ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 280.405 229.711 222.408 1.00 51.00  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 280.304 229.184 223.768 1.00 49.71  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 280.506 227.675 223.771 1.00 51.86  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 281.223 227.130 224.620 1.00 55.50  ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 278.956 229.581 224.397 1.00 45.72  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 278.708 228.792 225.672 1.00 53.67  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 278.925 231.074 224.683 1.00 45.57  ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 279.881 226.975 222.822 1.00 55.13  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 280.052 225.528 222.735 1.00 51.07  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 281.489 225.159 222.391 1.00 54.17  ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 282.040 224.198 222.941 1.00 62.02  ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 279.086 224.946 221.704 1.00 51.26  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 282.112 225.909 221.479 1.00 54.71  ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 283.482 225.602 221.079 1.00 55.95  ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 284.473 225.868 222.204 1.00 57.16  ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 285.488 225.170 222.312 1.00 66.92  ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 283.856 226.411 219.837 1.00 61.07  ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 285.240 226.171 219.231 1.00 66.93  ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 285.370 224.735 218.748 1.00 57.52  ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 285.505 227.149 218.097 1.00 63.25  ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 284.201 226.862 223.050 1.00 49.50  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 285.118 227.197 224.135 1.00 51.51  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 285.057 226.161 225.253 1.00 53.71  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 286.083 225.598 225.650 1.00 55.24  ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 284.801 228.593 224.677 1.00 51.30  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 285.395 228.875 226.047 1.00 53.15  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 284.838 230.159 226.638 1.00 54.54  ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 285.378 230.399 228.038 1.00 57.18  ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 284.849 231.658 228.631 1.00 57.17  ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 283.857 225.900 225.775 1.00 54.05  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 283.724 224.954 226.879 1.00 51.87  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 283.871 223.514 226.403 1.00 49.78  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 284.244 222.633 227.186 1.00 54.70  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 282.389 225.164 227.588 1.00 46.05  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 282.228 226.533 228.169 1.00 48.20  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 282.922 226.952 229.284 1.00 48.49  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 281.469 227.585 227.781 1.00 53.97  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 282.588 228.199 229.564 1.00 55.26  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 281.708 228.606 228.667 1.00 58.70  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 283.587 223.253 225.131 1.00 57.22  ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 283.803 221.920 224.586 1.00 57.20  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 284.761 221.989 223.404 1.00 57.54  ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 284.325 222.103 222.251 1.00 59.56  ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 282.489 221.263 224.157 1.00 47.89  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 281.494 221.105 225.270 1.00 51.23  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 280.739 222.181 225.707 1.00 57.70  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 281.292 219.869 225.859 1.00 49.30  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 279.819 222.029 226.724 1.00 62.47  ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 280.376 219.712 226.877 1.00 54.63  ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 279.637 220.793 227.307 1.00 61.67  ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 286.068 221.926 223.649 1.00 68.21  ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 287.028 221.863 222.540 1.00 68.99  ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 287.033 220.492 221.885 1.00 73.40  ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 286.164 219.666 222.179 1.00 77.08  ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 288.374 222.177 223.212 1.00 68.18  ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 288.040 222.626 224.619 1.00 66.10  ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 286.741 221.976 224.955 1.00 68.43  ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 287.964 220.286 220.948 1.00 76.02  ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 288.263 219.026 220.261 1.00 75.39  ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 287.027 218.169 219.997 1.00 76.50  ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 287.021 216.966 220.280 1.00 77.12  ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 289.354 218.225 221.005 1.00 77.60  ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 288.951 217.757 222.405 1.00 81.04  ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 287.814 217.893 222.837 1.00 80.22  ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 289.916 217.191 223.121 1.00 77.46  ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 285.979 218.782 219.442 1.00 79.39  ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 284.785 218.070 219.006 1.00 79.97  ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 284.580 218.340 217.522 1.00 81.41  ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 285.186 219.243 216.941 1.00 80.50  ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 283.521 218.476 219.797 1.00 75.14  ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 283.316 219.992 219.735 1.00 76.03  ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 283.604 217.985 221.234 1.00 75.75  ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 281.929 220.437 220.142 1.00 75.89  ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 283.711 217.541 216.909 1.00 86.86  ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 283.373 217.710 215.496 1.00 87.21  ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 282.317 218.803 215.400 1.00 87.05  ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 281.128 218.575 215.628 1.00 89.32  ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 282.887 216.400 214.891 1.00 87.96  ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 283.088 216.343 213.389 1.00 90.84  ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 284.246 216.184 212.949 1.00 89.28  ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 282.091 216.459 212.646 1.00 92.08  ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 282.766 220.015 215.063 1.00 82.40  ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 281.866 221.163 215.035 1.00 83.17  ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 280.774 220.995 213.986 1.00 85.03  ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 279.607 221.311 214.238 1.00 86.82  ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 282.663 222.446 214.786 1.00 84.40  ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 281.897 223.530 214.044 1.00 86.29  ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 282.687 224.827 213.990 1.00 85.26  ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 282.486 225.637 215.186 1.00 88.25  ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 282.677 226.947 215.244 1.00 88.36  ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 283.076 227.635 214.186 1.00 85.73  ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 282.463 227.585 216.392 1.00 82.58  ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 281.132 220.489 212.803 1.00 89.83  ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 280.146 220.334 211.737 1.00 89.96  ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 279.051 219.350 212.131 1.00 89.28  ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 277.873 219.565 211.822 1.00 91.26  ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 280.831 219.888 210.445 1.00 88.86  ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 281.759 220.930 209.837 1.00 92.32  ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 283.136 220.937 210.473 1.00 96.05  ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 283.394 220.086 211.350 1.00 95.37  ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 283.961 221.795 210.096 1.00 94.79  ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 279.419 218.262 212.810 1.00 81.51  ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 278.421 217.289 213.241 1.00 83.49  ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 277.516 217.866 214.324 1.00 82.43  ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 276.326 217.535 214.387 1.00 79.73  ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 279.110 216.017 213.736 1.00 84.79  ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 278.161 214.892 214.109 1.00 84.80  ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 278.924 213.640 214.509 1.00 83.72  ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 277.978 212.514 214.891 1.00 84.13  ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 278.714 211.282 215.288 1.00 83.06  ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 278.058 218.730 215.181 1.00 75.55  ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 277.291 219.306 216.279 1.00 69.99  ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 276.661 220.646 215.918 1.00 70.47  ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 275.561 220.957 216.389 1.00 74.92  ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 278.182 219.469 217.513 1.00 66.66  ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 277.332 221.448 215.093 1.00 73.96  ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 276.835 222.774 214.745 1.00 74.18  ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 276.399 222.847 213.287 1.00 75.44  ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 276.670 223.842 212.607 1.00 77.62  ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 277.899 223.838 215.025 1.00 77.23  ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 278.218 224.025 216.495 1.00 74.09  ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 276.788 224.602 217.425 1.00 79.98  ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 276.652 223.310 218.651 1.00 73.70  ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 275.740 221.800 212.796 1.00 77.00  ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 275.186 221.841 211.450 1.00 75.93  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 274.168 222.970 211.347 1.00 79.64  ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 273.460 223.275 212.310 1.00 81.27  ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 274.538 220.503 211.096 1.00 80.42  ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 275.468 219.440 211.208 1.00 83.51  ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 274.110 223.601 210.171 1.00 85.24  ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 273.356 224.836 209.981 1.00 82.84  ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 271.898 224.689 210.416 1.00 81.73  ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 271.454 225.448 211.287 1.00 81.56  ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 273.456 225.301 208.524 1.00 86.91  ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 272.695 226.578 208.215 1.00 87.35  ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 272.656 226.829 206.717 1.00 83.63  ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 271.980 225.748 206.008 1.00 88.30  ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 272.556 224.969 205.103 1.00 86.91  ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 273.827 225.118 204.770 1.00 84.64  ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 271.838 224.012 204.520 1.00 84.25  ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 271.106 223.743 209.861 1.00 71.55  ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 269.757 223.548 210.404 1.00 68.83  ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 269.750 222.621 211.611 1.00 66.94  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 269.967 221.413 211.474 1.00 65.45  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 268.991 222.953 209.218 1.00 63.40  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 270.029 222.193 208.449 1.00 71.27  ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 271.394 222.753 208.805 1.00 70.46  ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 269.502 223.169 212.799 1.00 46.51  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 269.410 222.361 214.014 1.00 45.12  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 267.930 222.089 214.262 1.00 50.80  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 267.225 222.911 214.850 1.00 50.14  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 270.070 223.045 215.213 1.00 47.22  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 271.504 223.455 214.871 1.00 49.69  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 270.063 222.120 216.418 1.00 45.59  ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 272.289 223.978 216.054 1.00 44.14  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 267.453 220.931 213.814 1.00 44.34  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 266.047 220.567 213.905 1.00 36.72  ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 265.908 219.237 214.629 1.00 47.29  ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 266.604 218.271 214.300 1.00 51.03  ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 265.411 220.480 212.515 1.00 43.16  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 265.364 221.781 211.712 1.00 46.74  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 264.569 221.591 210.431 1.00 44.84  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 264.777 222.904 212.550 1.00 42.79  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 265.012 219.194 215.610 1.00 45.22  ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 264.688 217.981 216.345 1.00 27.45  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 263.189 217.736 216.267 1.00 34.95  ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 262.391 218.667 216.420 1.00 44.75  ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 265.126 218.081 217.809 1.00 33.95  ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 266.568 217.700 218.054 1.00 30.69  ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 267.606 218.421 217.481 1.00 31.02  ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 266.890 216.620 218.863 1.00 36.29  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 268.923 218.075 217.704 1.00 36.98  ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 268.203 216.267 219.093 1.00 37.33  ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 269.216 216.997 218.511 1.00 39.03  ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 270.526 216.645 218.738 1.00 48.11  ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 262.808 216.484 216.029 1.00 45.15  ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 261.401 216.139 215.893 1.00 38.34  ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 261.199 214.672 216.239 1.00 49.15  ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 262.101 213.847 216.069 1.00 55.47  ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 260.889 216.420 214.476 1.00 44.36  ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 259.525 216.059 214.348 1.00 49.03  ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 259.999 214.359 216.727 1.00 55.28  ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 259.592 212.991 217.018 1.00 50.14  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 258.542 212.487 216.035 1.00 46.46  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 257.819 211.533 216.337 1.00 53.32  ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 259.073 212.883 218.452 1.00 45.94  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 257.872 213.771 218.707 1.00 52.12  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 257.554 214.652 217.908 1.00 52.19  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 257.192 213.539 219.824 1.00 49.56  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 258.435 213.123 214.870 1.00 47.91  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 257.449 212.737 213.869 1.00 43.60  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 257.919 211.590 212.986 1.00 49.18  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 257.098 210.764 212.570 1.00 51.27  ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 257.095 213.944 212.998 1.00 42.16  ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 256.165 214.909 213.666 1.00 41.61  ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 255.299 214.641 214.685 1.00 40.52  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 256.014 216.301 213.367 1.00 45.44  ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 254.614 215.778 215.036 1.00 41.22  ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 255.035 216.812 214.242 1.00 44.82  ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 256.609 217.165 212.443 1.00 44.84  ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 254.639 218.147 214.221 1.00 45.07  ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 256.215 218.489 212.423 1.00 45.62  ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 255.239 218.968 213.306 1.00 48.96  ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 259.214 211.519 212.690 1.00 46.00  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 259.765 210.471 211.841 1.00 46.72  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 260.310 209.288 212.629 1.00 51.34  ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 260.850 208.356 212.023 1.00 52.39  ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 260.870 211.044 210.949 1.00 50.56  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 260.433 212.072 209.906 1.00 45.36  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 261.525 212.277 208.873 1.00 48.69  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 259.143 211.633 209.239 1.00 51.29  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 260.185 209.299 213.953 1.00 55.01  ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 260.689 208.211 214.779 1.00 55.34  ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 259.927 208.211 216.096 1.00 56.79  ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 259.124 209.105 216.373 1.00 58.68  ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 262.195 208.341 215.018 1.00 55.95  ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 262.498 209.567 215.660 1.00 63.34  ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 260.189 207.186 216.907 1.00 63.10  ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 259.534 207.083 218.205 1.00 61.77  ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 260.074 208.097 219.205 1.00 65.35  ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 259.304 208.640 220.006 1.00 64.74  ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 259.690 205.666 218.760 1.00 61.43  ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 258.965 205.428 220.074 1.00 68.59  ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 259.118 203.990 220.538 1.00 69.67  ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 258.317 203.732 221.803 1.00 66.29  ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 258.865 204.478 222.969 1.00 66.68  ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 261.375 208.369 219.174 1.00 60.31  ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 262.015 209.238 220.147 1.00 61.00  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 262.205 210.639 219.571 1.00 59.03  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 261.826 210.938 218.437 1.00 58.36  ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 263.352 208.641 220.591 1.00 61.36  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 263.232 207.189 221.008 1.00 66.90  ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 262.351 206.876 221.836 1.00 66.35  ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 264.023 206.361 220.510 1.00 67.49  ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 262.806 211.512 220.379 1.00 53.41  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 263.098 212.890 219.985 1.00 50.51  ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 264.532 212.931 219.472 1.00 52.37  ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 265.487 213.068 220.236 1.00 55.93  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 262.885 213.837 221.160 1.00 51.26  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 262.715 215.290 220.779 1.00 48.94  ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 261.642 215.705 220.002 1.00 44.45  ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 263.620 216.250 221.211 1.00 47.95  ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 261.481 217.033 219.658 1.00 46.99  ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 263.467 217.580 220.874 1.00 45.77  ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 262.397 217.966 220.097 1.00 42.70  ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 262.242 219.290 219.758 1.00 46.65  ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 264.682 212.809 218.156 1.00 41.04  ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 266.000 212.727 217.528 1.00 38.10  ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 266.080 213.789 216.440 1.00 42.49  ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 265.048 214.274 215.949 1.00 47.52  ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 266.270 211.317 216.951 1.00 44.09  ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 265.336 211.029 215.776 1.00 43.60  ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 266.127 210.256 218.032 1.00 43.91  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 265.704 209.786 214.998 1.00 42.97  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 267.294 214.190 216.054 1.00 42.34  ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 267.430 215.186 214.985 1.00 43.35  ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 266.825 214.695 213.679 1.00 42.66  ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 266.876 213.508 213.349 1.00 51.78  ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 268.947 215.377 214.863 1.00 42.31  ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 269.546 214.178 215.524 1.00 42.91  ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 268.602 213.824 216.623 1.00 38.54  ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 266.248 215.631 212.931 1.00 43.20  ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 265.559 215.330 211.684 1.00 45.79  ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 266.181 216.156 210.566 1.00 49.58  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 266.715 217.247 210.793 1.00 51.88  ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 264.040 215.601 211.799 1.00 41.66  ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 263.759 217.095 211.876 1.00 40.56  ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 263.283 214.961 210.645 1.00 49.87  ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 266.126 215.616 209.353 1.00 54.26  ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 266.614 216.311 208.172 1.00 56.85  ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 265.523 217.209 207.602 1.00 54.91  ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 264.332 216.899 207.684 1.00 53.96  ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 267.080 215.315 207.109 1.00 56.24  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 268.161 215.884 206.213 1.00 63.84  ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 269.159 216.415 206.745 1.00 61.24  ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 268.014 215.801 204.976 1.00 66.47  ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 265.947 218.336 207.026 1.00 51.78  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 264.988 219.300 206.495 1.00 49.87  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 264.187 218.716 205.338 1.00 60.39  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 262.967 218.908 205.262 1.00 63.79  ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 265.712 220.572 206.056 1.00 48.03  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 264.795 221.767 205.862 1.00 53.12  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 265.508 223.088 206.065 1.00 59.42  ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 266.479 223.394 205.373 1.00 62.27  ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 265.030 223.879 207.018 1.00 55.97  ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 264.852 218.004 204.424 1.00 64.16  ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 264.147 217.430 203.282 1.00 57.30  ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 263.199 216.318 203.715 1.00 60.32  ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 262.075 216.224 203.209 1.00 59.67  ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 265.151 216.913 202.252 1.00 55.92  ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 265.997 218.004 201.620 1.00 64.00  ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 265.172 219.201 201.187 1.00 65.97  ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 264.250 219.023 200.363 1.00 67.64  ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 265.445 220.320 201.670 1.00 59.23  ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 263.636 215.463 204.642 1.00 58.86  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 262.758 214.412 205.146 1.00 51.54  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 261.574 215.001 205.901 1.00 55.51  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 260.443 214.517 205.774 1.00 58.36  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 263.543 213.453 206.040 1.00 52.87  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 264.203 212.308 205.290 1.00 59.62  ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 265.015 211.408 206.199 1.00 66.55  ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 264.860 211.512 207.434 1.00 64.64  ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 265.807 210.595 205.679 1.00 65.41  ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 261.817 216.042 206.701 1.00 51.33  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 260.725 216.707 207.405 1.00 45.78  ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 259.763 217.372 206.428 1.00 49.72  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 258.543 217.327 206.620 1.00 56.78  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 261.284 217.732 208.391 1.00 49.26  ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 260.266 218.577 209.156 1.00 47.63  ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 259.667 217.785 210.307 1.00 46.57  ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 260.907 219.860 209.659 1.00 49.31  ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 260.296 217.997 205.374 1.00 43.72  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 259.439 218.655 204.393 1.00 45.01  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 258.531 217.655 203.691 1.00 54.31  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 257.349 217.936 203.457 1.00 58.94  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 260.293 219.409 203.374 1.00 50.89  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 259.513 220.395 202.520 1.00 51.99  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 260.322 220.840 201.312 1.00 47.82  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 261.681 221.224 201.673 1.00 54.28  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 262.010 222.374 202.245 1.00 58.85  ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 261.098 223.289 202.533 1.00 51.68  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 263.286 222.614 202.533 1.00 53.75  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 259.066 216.483 203.341 1.00 53.29  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 258.245 215.456 202.707 1.00 45.88  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 257.160 214.954 203.651 1.00 55.68  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 256.016 214.738 203.235 1.00 57.73  ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 259.125 214.299 202.235 1.00 51.27  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 260.131 214.724 201.184 1.00 59.98  ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 260.003 215.848 200.657 1.00 59.29  ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 261.051 213.933 200.887 1.00 57.41  ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 257.503 214.753 204.926 1.00 49.92  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 256.511 214.291 205.892 1.00 43.34  ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 255.422 215.334 206.109 1.00 44.61  ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 254.232 215.000 206.144 1.00 48.52  ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 257.188 213.943 207.217 1.00 45.38  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 256.223 213.511 208.298 1.00 50.07  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 255.728 212.215 208.337 1.00 45.00  ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 255.804 214.401 209.280 1.00 50.98  ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 254.845 211.816 209.322 1.00 46.37  ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 254.920 214.011 210.266 1.00 46.99  ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 254.445 212.718 210.284 1.00 49.70  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 253.566 212.327 211.267 1.00 53.00  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 255.809 216.602 206.260 1.00 35.80  ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 254.825 217.659 206.469 1.00 38.86  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 253.938 217.810 205.240 1.00 44.22  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 252.723 218.011 205.357 1.00 52.77  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 255.528 218.980 206.833 1.00 41.45  ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 254.538 220.133 206.831 1.00 41.76  ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 256.201 218.861 208.191 1.00 41.16  ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 254.524 217.706 204.045 1.00 46.20  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 253.730 217.782 202.823 1.00 41.37  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 252.713 216.650 202.758 1.00 42.63  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 251.555 216.868 202.383 1.00 45.81  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 254.645 217.752 201.600 1.00 43.25  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 254.155 218.597 200.436 1.00 47.56  ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 255.250 218.799 199.403 1.00 51.03  ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 256.499 219.396 200.030 1.00 50.77  ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 257.555 219.655 199.015 1.00 51.00  ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 253.127 215.434 203.121 1.00 40.16  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 252.193 214.314 203.150 1.00 35.95  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 251.105 214.531 204.194 1.00 44.98  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 249.929 214.238 203.947 1.00 47.44  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 252.943 213.009 203.417 1.00 41.61  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 251.478 215.041 205.370 1.00 50.39  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 250.483 215.323 206.400 1.00 41.86  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 249.590 216.490 206.001 1.00 42.86  ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 248.388 216.487 206.290 1.00 49.68  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 251.172 215.606 207.735 1.00 43.08  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 251.911 214.417 208.329 1.00 45.41  ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 251.167 213.108 208.110 1.00 44.95  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 249.967 213.009 208.932 1.00 46.21  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 248.925 212.241 208.646 1.00 52.89  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 248.899 211.487 207.560 1.00 50.48  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 247.884 212.226 209.474 1.00 53.03  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 250.160 217.502 205.340 1.00 42.50  ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 249.353 218.637 204.904 1.00 36.43  ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 248.339 218.229 203.847 1.00 43.72  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 247.247 218.805 203.787 1.00 49.51  ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 250.244 219.758 204.372 1.00 33.61  ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 250.629 220.848 205.373 1.00 40.93  ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 251.641 221.791 204.763 1.00 41.54  ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 249.402 221.613 205.834 1.00 41.31  ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 248.677 217.252 203.001 1.00 52.83  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 247.701 216.764 202.034 1.00 47.46  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 246.493 216.159 202.735 1.00 45.65  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 245.351 216.487 202.403 1.00 44.58  ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 248.338 215.739 201.095 1.00 44.70  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 249.363 216.318 200.136 1.00 56.10  ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 249.821 215.271 199.132 1.00 53.02  ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 250.733 214.238 199.773 1.00 53.33  ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 251.266 213.270 198.775 1.00 49.73  ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 246.728 215.300 203.730 1.00 47.96  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 245.630 214.679 204.466 1.00 43.20  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 244.858 215.726 205.260 1.00 52.89  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 243.640 215.615 205.444 1.00 59.07  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 246.170 213.560 205.375 1.00 40.76  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 245.030 212.853 206.092 1.00 44.66  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 246.989 212.572 204.562 1.00 51.00  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 245.556 216.751 205.750 1.00 49.90  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 244.905 217.806 206.520 1.00 40.98  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 243.868 218.548 205.684 1.00 40.92  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 242.909 219.109 206.227 1.00 47.18  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 245.963 218.773 207.053 1.00 43.02  ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 245.403 219.934 207.821 1.00 37.44  ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 244.804 219.745 209.054 1.00 43.92  ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 245.482 221.218 207.310 1.00 39.16  ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 244.296 220.816 209.764 1.00 41.20  ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 244.973 222.291 208.013 1.00 40.02  ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 244.378 222.090 209.241 1.00 35.94  ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 244.047 218.574 204.360 1.00 46.29  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 243.149 219.354 203.512 1.00 46.16  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 241.765 218.722 203.402 1.00 51.78  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 240.752 219.418 203.539 1.00 57.89  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 243.769 219.561 202.130 1.00 43.15  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 245.056 220.358 202.157 1.00 42.73  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 245.313 221.262 203.181 1.00 45.27  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 246.005 220.222 201.153 1.00 51.18  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 246.485 221.998 203.212 1.00 41.47  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 247.181 220.957 201.175 1.00 46.11  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 247.415 221.842 202.206 1.00 40.90  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 248.581 222.574 202.233 1.00 50.27  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 241.687 217.411 203.153 1.00 54.71  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 240.367 216.800 203.010 1.00 63.12  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 239.663 216.674 204.354 1.00 64.42  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 238.427 216.660 204.414 1.00 66.31  ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 240.455 215.427 202.335 1.00 63.59  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 240.893 215.438 200.873 1.00 71.13  ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 242.392 215.500 200.700 1.00 71.57  ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 243.103 215.467 201.720 1.00 68.95  ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 242.858 215.575 199.543 1.00 66.03  ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 240.424 216.592 205.443 1.00 62.94  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 239.838 216.284 206.741 1.00 64.53  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 239.336 217.525 207.470 1.00 66.00  ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 238.166 217.584 207.860 1.00 66.02  ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 240.854 215.544 207.614 1.00 60.78  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 241.169 214.143 207.128 1.00 63.39  ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 241.894 213.314 208.168 1.00 68.51  ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 242.109 213.817 209.291 1.00 68.55  ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 242.245 212.156 207.861 1.00 67.84  ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 240.199 218.522 207.665 1.00 56.71  ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 239.890 219.647 208.538 1.00 56.85  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 239.745 220.963 207.784 1.00 57.57  ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 238.703 221.617 207.885 1.00 61.22  ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 240.968 219.769 209.623 1.00 54.19  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 240.894 218.688 210.690 1.00 55.15  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 239.824 218.964 211.728 1.00 61.96  ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 239.396 220.131 211.848 1.00 67.62  ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 239.403 218.012 212.419 1.00 61.71  ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 240.762 221.377 207.032 1.00 50.32  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 240.760 222.690 206.388 1.00 48.27  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 241.326 222.546 204.984 1.00 51.82  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 242.497 222.188 204.820 1.00 53.25  ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 241.568 223.701 207.202 1.00 53.10  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 241.156 225.166 207.062 1.00 49.43  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 239.689 225.334 207.416 1.00 51.23  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 242.026 226.050 207.938 1.00 47.07  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 240.505 222.837 203.977 1.00 53.80  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 240.914 222.718 202.577 1.00 53.32  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 241.500 224.039 202.073 1.00 58.36  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 241.080 224.604 201.064 1.00 69.35  ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 239.737 222.269 201.720 1.00 58.00  ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 240.173 221.554 200.455 1.00 66.55  ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 240.955 222.139 199.676 1.00 63.47  ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 239.734 220.405 200.239 1.00 70.95  ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 242.493 224.529 202.808 1.00 55.41  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 243.221 225.735 202.425 1.00 56.71  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 244.647 225.332 202.068 1.00 59.05  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 245.415 224.932 202.955 1.00 59.19  ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 243.196 226.787 203.545 1.00 55.31  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 244.210 227.887 203.268 1.00 54.51  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 241.798 227.369 203.692 1.00 50.90  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 245.034 225.387 200.795 1.00 54.81  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 246.400 224.998 200.422 1.00 52.79  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 247.439 225.916 201.052 1.00 53.60  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 247.210 227.114 201.234 1.00 58.26  ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 246.398 225.115 198.893 1.00 51.10  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 244.955 225.039 198.504 1.00 50.29  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 244.209 225.703 199.618 1.00 48.36  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 248.591 225.338 201.383 1.00 49.47  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 249.704 226.068 201.973 1.00 46.17  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 250.962 225.847 201.149 1.00 43.56  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 251.151 224.779 200.560 1.00 45.54  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 249.961 225.636 203.423 1.00 34.16  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 249.293 226.441 204.538 1.00 41.22  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 247.808 226.154 204.596 1.00 48.79  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 249.951 226.141 205.875 1.00 45.27  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 251.817 226.863 201.112 1.00 41.50  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 253.125 226.761 200.478 1.00 42.24  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 254.164 226.523 201.564 1.00 41.92  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 254.274 227.306 202.515 1.00 46.18  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 253.448 228.027 199.669 1.00 42.74  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 254.837 227.927 199.061 1.00 43.92  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 252.401 228.245 198.587 1.00 36.91  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 254.925 225.441 201.426 1.00 46.52  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 255.878 225.021 202.447 1.00 46.07  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 257.236 225.653 202.167 1.00 53.32  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 257.851 225.389 201.129 1.00 58.41  ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 255.988 223.499 202.484 1.00 41.62  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 254.930 222.754 203.295 1.00 42.53  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 255.184 221.257 203.255 1.00 43.88  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 254.930 223.256 204.724 1.00 50.19  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 257.703 226.485 203.092 1.00 40.61  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 259.065 226.991 203.076 1.00 43.86  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 259.731 226.688 204.412 1.00 47.50  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 259.111 226.152 205.335 1.00 48.56  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 259.115 228.495 202.756 1.00 36.86  ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 258.175 229.339 203.572 1.00 36.52  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 256.841 229.459 203.218 1.00 39.35  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 258.634 230.042 204.673 1.00 44.34  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 255.980 230.246 203.958 1.00 37.28  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 257.777 230.831 205.416 1.00 38.73  ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 256.450 230.934 205.057 1.00 35.53  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 261.017 227.033 204.501 1.00 49.85  ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 261.834 226.593 205.629 1.00 48.32  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 261.322 227.149 206.953 1.00 50.77  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 261.342 226.453 207.974 1.00 55.09  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 263.291 226.993 205.405 1.00 46.12  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 263.922 226.258 204.240 1.00 50.89  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 263.302 225.384 203.634 1.00 48.05  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 265.162 226.608 203.919 1.00 50.49  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 260.865 228.404 206.960 1.00 46.92  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 260.395 229.003 208.205 1.00 44.86  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 259.133 228.323 208.720 1.00 48.87  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 258.940 228.218 209.937 1.00 56.40  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 260.156 230.500 208.012 1.00 47.61  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 261.422 231.291 207.726 1.00 51.92  ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 261.160 232.773 207.560 1.00 59.83  ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 259.980 233.180 207.604 1.00 57.68  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 262.136 233.533 207.387 1.00 57.97  ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 258.262 227.861 207.819 1.00 37.88  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 257.070 227.132 208.248 1.00 38.49  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 257.462 225.823 208.922 1.00 39.83  ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 256.900 225.449 209.960 1.00 52.06  ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 256.124 226.897 207.056 1.00 40.18  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 255.180 225.742 207.343 1.00 36.19  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 255.330 228.153 206.765 1.00 42.47  ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 258.435 225.111 208.350 1.00 38.75  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 258.888 223.856 208.943 1.00 39.04  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 259.448 224.085 210.341 1.00 41.41  ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 259.234 223.275 211.250 1.00 44.84  ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 259.936 223.200 208.043 1.00 34.33  ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 259.515 222.906 206.603 1.00 30.53  ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 260.603 222.130 205.881 1.00 37.57  ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 258.199 222.145 206.571 1.00 35.26  ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 260.184 225.182 210.528 1.00 41.12  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 260.660 225.530 211.861 1.00 36.40  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 259.501 225.875 212.787 1.00 39.60  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 259.486 225.468 213.955 1.00 49.84  ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 261.643 226.698 211.778 1.00 44.63  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 262.873 226.367 210.959 1.00 59.70  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 263.197 225.168 210.830 1.00 59.86  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 263.516 227.305 210.444 1.00 55.67  ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 258.517 226.625 212.282 1.00 33.16  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 257.423 227.088 213.130 1.00 22.34  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 256.530 225.939 213.581 1.00 28.18  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 256.109 225.898 214.743 1.00 46.34  ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 256.606 228.150 212.395 1.00 29.46  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 257.312 229.462 212.254 1.00 43.10  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 256.994 230.377 211.273 1.00 51.45  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 258.320 230.013 212.970 1.00 39.05  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 257.777 231.435 211.392 1.00 46.64  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 258.590 231.239 212.414 1.00 40.25  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 256.222 225.000 212.682 1.00 30.09  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 255.383 223.871 213.074 1.00 32.73  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 256.094 223.004 214.104 1.00 29.86  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 255.445 222.355 214.933 1.00 38.86  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 254.950 223.054 211.841 1.00 29.28  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 254.172 223.927 210.872 1.00 31.47  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 256.152 222.429 211.152 1.00 25.42  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 257.428 222.971 214.073 1.00 28.89  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 258.173 222.253 215.101 1.00 28.96  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 258.101 222.981 216.438 1.00 33.83  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 257.994 222.346 217.494 1.00 37.96  ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 259.625 222.070 214.663 1.00 33.00  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 259.880 220.970 213.632 1.00 26.94  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 261.370 220.785 213.397 1.00 29.01  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 259.237 219.666 214.072 1.00 26.29  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 258.166 224.315 216.413 1.00 43.42  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 258.060 225.087 217.647 1.00 31.81  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 256.667 224.972 218.254 1.00 34.14  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 256.519 224.906 219.479 1.00 46.26  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 258.408 226.552 217.384 1.00 29.74  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 259.824 226.777 216.887 1.00 31.43  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 260.027 228.218 216.455 1.00 25.06  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 261.197 228.374 215.600 1.00 41.90  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 261.621 229.533 215.117 1.00 47.83  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 260.992 230.666 215.385 1.00 47.24  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 262.703 229.557 214.343 1.00 47.91  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 255.632 224.966 217.414 1.00 26.37  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 254.273 224.800 217.919 1.00 28.18  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 254.079 223.391 218.468 1.00 32.49  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 253.400 223.192 219.482 1.00 31.64  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 253.254 225.132 216.814 1.00 33.60  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 253.409 226.588 216.372 1.00 21.10  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 251.836 224.882 217.294 1.00 32.52  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 252.601 226.943 215.145 1.00 28.10  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 254.679 222.394 217.812 1.00 43.09  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 254.529 221.011 218.255 1.00 32.39  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 255.179 220.784 219.615 1.00 32.55  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 254.632 220.063 220.458 1.00 40.94  ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 255.121 220.063 217.213 1.00 33.03  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 255.061 218.611 217.643 1.00 53.23  ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 253.941 218.090 217.828 1.00 60.95  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 256.134 217.989 217.793 1.00 53.28  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 256.351 221.382 219.844 1.00 34.84  ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 257.056 221.165 221.104 1.00 32.41  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 256.274 221.731 222.285 1.00 30.60  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 256.290 221.158 223.380 1.00 34.50  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 258.464 221.766 221.029 1.00 32.98  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 258.534 223.277 221.191 1.00 42.88  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 259.958 223.831 221.169 1.00 43.37  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 260.791 223.332 222.258 1.00 45.74  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 261.568 222.260 222.186 1.00 47.50  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 261.671 221.554 221.072 1.00 45.62  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 262.267 221.893 223.256 1.00 45.81  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 255.586 222.858 222.085 1.00 40.54  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 254.785 223.437 223.159 1.00 39.85  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 253.548 222.587 223.424 1.00 38.15  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 253.150 222.387 224.578 1.00 47.67  ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 254.415 224.893 222.825 1.00 39.53  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 255.676 225.709 222.532 1.00 40.70  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 253.632 225.520 223.966 1.00 34.89  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 256.763 225.557 223.575 1.00 39.66  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 252.922 222.072 222.363 1.00 35.85  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 251.712 221.270 222.513 1.00 28.43  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 251.966 219.951 223.231 1.00 35.26  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 251.008 219.307 223.670 1.00 41.71  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 251.090 220.998 221.143 1.00 24.83  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 250.262 222.135 220.616 1.00 28.06  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 249.889 223.180 221.443 1.00 37.94  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 249.852 222.155 219.293 1.00 29.63  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 249.125 224.225 220.961 1.00 37.05  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 249.088 223.197 218.806 1.00 31.90  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 248.725 224.233 219.640 1.00 39.61  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 253.225 219.535 223.358 1.00 42.48  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 253.580 218.290 224.023 1.00 37.60  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 253.978 218.495 225.481 1.00 40.39  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 254.495 217.565 226.110 1.00 46.23  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 254.711 217.593 223.264 1.00 37.66  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 254.268 216.914 221.980 1.00 39.14  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 255.418 216.166 221.328 1.00 40.16  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 256.418 217.073 220.780 1.00 45.55  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 257.657 217.189 221.238 1.00 44.05  ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 258.085 216.468 222.261 1.00 43.77  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 258.486 218.050 220.656 1.00 40.89  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 253.750 219.686 226.030 1.00 40.51  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 254.137 220.002 227.393 1.00 39.46  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 252.909 220.318 228.238 1.00 42.28  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 251.941 220.902 227.739 1.00 44.32  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 255.096 221.199 227.429 1.00 30.83  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 256.444 220.939 226.780 1.00 47.80  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 257.314 222.179 226.733 1.00 55.32  ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 256.902 223.256 227.164 1.00 52.56  ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 258.523 222.034 226.205 1.00 50.28  ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 252.915 219.941 229.516 1.00 45.93  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 251.790 220.295 230.389 1.00 36.88  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 251.698 221.800 230.581 1.00 41.23  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 252.709 222.483 230.766 1.00 38.12  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 252.121 219.579 231.704 1.00 37.56  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 253.604 219.412 231.676 1.00 46.36  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 253.959 219.190 230.234 1.00 49.18  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 250.465 222.309 230.543 1.00 47.84  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 250.198 223.745 230.636 1.00 36.73  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 251.006 224.519 229.597 1.00 39.16  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 251.568 225.580 229.875 1.00 41.83  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 250.473 224.268 232.047 1.00 32.09  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 249.580 225.427 232.459 1.00 39.78  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 249.639 225.707 233.946 1.00 44.76  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 250.423 225.100 234.674 1.00 47.50  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 248.806 226.633 234.407 1.00 39.27  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 251.065 223.976 228.384 1.00 34.45  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 251.818 224.597 227.315 1.00 24.22  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 251.006 225.609 226.536 1.00 29.89  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 250.219 225.245 225.659 1.00 27.82  ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 251.191 226.886 226.851 1.00 40.42  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 250.481 227.968 226.189 1.00 30.14  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 251.411 228.690 225.223 1.00 30.93  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 252.607 228.847 225.482 1.00 37.92  ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 249.914 228.952 227.212 1.00 30.35  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 249.062 228.308 228.261 1.00 32.72  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 247.931 227.582 227.958 1.00 30.44  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 249.177 228.280 229.609 1.00 36.92  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 247.385 227.134 229.074 1.00 30.81  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 248.122 227.544 230.091 1.00 34.51  ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 250.848 229.127 224.101 1.00 31.51  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 251.610 229.734 223.021 1.00 26.43  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 251.214 231.192 222.842 1.00 26.98  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 250.038 231.548 222.969 1.00 46.87  ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 251.394 228.977 221.709 1.00 36.98  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 252.432 227.910 221.363 1.00 36.65  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 251.987 227.113 220.154 1.00 44.04  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 253.786 228.550 221.117 1.00 31.50  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 252.204 232.030 222.546 1.00 25.06  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 251.989 233.439 222.220 1.00 29.88  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 252.682 233.704 220.888 1.00 36.20  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 253.897 233.921 220.845 1.00 45.57  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 252.518 234.354 223.319 1.00 31.16  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 252.395 235.858 223.064 1.00 34.33  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 250.959 236.235 222.735 1.00 32.64  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 252.901 236.651 224.258 1.00 29.33  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 251.912 233.682 219.804 1.00 34.60  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 252.449 233.888 218.465 1.00 31.40  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 252.305 235.357 218.089 1.00 32.30  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 251.193 235.894 218.081 1.00 41.13  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 251.732 232.997 217.451 1.00 34.45  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 251.690 231.501 217.765 1.00 35.53  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 251.095 230.729 216.601 1.00 33.08  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 253.079 230.983 218.100 1.00 44.50  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 253.425 236.001 217.780 1.00 37.03  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 253.456 237.417 217.436 1.00 36.30  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 253.943 237.542 216.001 1.00 37.99  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 255.030 237.057 215.663 1.00 43.69  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 254.350 238.218 218.394 1.00 33.44  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 253.996 237.895 219.846 1.00 33.42  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 254.209 239.706 218.132 1.00 35.70  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 254.783 238.690 220.858 1.00 37.69  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 253.143 238.186 215.162 1.00 30.67  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 253.508 238.370 213.770 1.00 29.08  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 252.397 239.080 213.033 1.00 39.86  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 251.282 239.242 213.541 1.00 44.05  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 252.725 239.511 211.813 1.00 38.76  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 251.751 240.214 210.989 1.00 39.09  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 250.631 239.262 210.577 1.00 40.41  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 250.806 238.040 210.493 1.00 48.01  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 252.438 240.843 209.765 1.00 37.30  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 252.869 239.768 208.780 1.00 34.49  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 251.536 241.875 209.096 1.00 39.01  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 249.454 239.834 210.337 1.00 34.97  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 248.305 239.044 209.924 1.00 29.17  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 248.552 238.402 208.563 1.00 39.48  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 249.237 238.960 207.702 1.00 54.11  ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 247.049 239.913 209.872 1.00 38.66  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 246.774 240.485 211.138 1.00 47.72  ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 247.989 237.211 208.378 1.00 36.82  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 248.181 236.462 207.157 1.00 31.26  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 249.471 235.677 207.081 1.00 38.31  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 249.757 235.089 206.030 1.00 50.07  ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 250.261 235.647 208.154 1.00 28.70  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 251.519 234.914 208.160 1.00 33.45  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 251.339 233.420 208.390 1.00 41.94  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 252.323 232.677 208.318 1.00 48.97  ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 252.456 235.486 209.226 1.00 35.78  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 250.122 232.965 208.662 1.00 39.18  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 249.867 231.562 208.903 1.00 34.19  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 249.911 231.124 210.349 1.00 30.02  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 249.994 229.917 210.603 1.00 37.09  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 249.862 232.058 211.302 1.00 30.72  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 249.951 231.689 212.712 1.00 25.74  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 248.787 230.797 213.126 1.00 35.56  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 248.980 229.773 213.792 1.00 45.03  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 249.996 232.948 213.578 1.00 33.88  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 251.135 233.894 213.244 1.00 32.28  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 251.182 235.058 214.217 1.00 34.16  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 249.931 235.912 214.115 1.00 34.55  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 249.793 236.535 212.771 1.00 34.77  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 247.564 231.171 212.742 1.00 29.52  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 246.401 230.366 213.102 1.00 22.54  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 246.358 229.067 212.307 1.00 34.23  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 246.040 228.007 212.857 1.00 54.64  ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 245.118 231.168 212.887 1.00 29.61  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 245.172 232.375 213.657 1.00 43.93  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 243.903 230.358 213.313 1.00 22.64  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 246.674 229.130 211.011 1.00 34.69  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 246.619 227.933 210.177 1.00 26.18  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 247.640 226.895 210.626 1.00 28.93  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 247.342 225.696 210.660 1.00 44.96  ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 246.840 228.301 208.711 1.00 38.71  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 246.055 229.455 208.383 1.00 39.72  ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 246.429 227.149 207.811 1.00 31.69  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 248.853 227.335 210.968 1.00 22.21  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 249.858 226.403 211.469 1.00 29.36  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 249.449 225.829 212.820 1.00 29.55  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 249.667 224.643 213.089 1.00 38.63  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 251.219 227.092 211.568 1.00 31.20  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 251.943 227.379 210.250 1.00 32.60  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 253.417 227.656 210.500 1.00 31.43  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 251.767 226.230 209.269 1.00 33.10  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 248.859 226.659 213.684 1.00 27.06  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 248.413 226.175 214.987 1.00 25.48  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 247.334 225.111 214.839 1.00 32.30  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 247.353 224.095 215.544 1.00 48.05  ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 247.906 227.342 215.833 1.00 24.72  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 248.892 228.351 215.951 1.00 30.63  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 246.380 225.329 213.931 1.00 33.79  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 245.354 224.321 213.682 1.00 33.07  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 245.952 223.068 213.057 1.00 34.73  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 245.543 221.947 213.383 1.00 46.50  ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 244.258 224.898 212.787 1.00 22.88  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 243.472 226.031 213.423 1.00 30.72  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 242.522 226.673 212.429 1.00 44.29  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 241.364 225.831 212.160 1.00 49.55  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 240.270 226.242 211.533 1.00 49.56  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 240.149 227.484 211.096 1.00 38.44  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 239.272 225.384 211.341 1.00 47.92  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 246.915 223.237 212.148 1.00 24.22  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 247.546 222.085 211.512 1.00 25.22  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 248.322 221.249 212.522 1.00 30.59  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 248.244 220.015 212.508 1.00 45.24  ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 248.464 222.552 210.383 1.00 26.90  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 249.282 221.452 209.770 1.00 28.78  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 248.682 220.283 209.334 1.00 38.07  ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 250.652 221.588 209.628 1.00 32.09  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 249.432 219.271 208.770 1.00 35.97  ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 251.408 220.579 209.065 1.00 33.00  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 250.796 219.419 208.635 1.00 30.92  ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 249.077 221.902 213.406 1.00 30.90  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 249.863 221.169 214.394 1.00 28.13  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 248.954 220.525 215.433 1.00 34.64  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 249.186 219.388 215.861 1.00 49.46  ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 250.904 222.099 215.043 1.00 24.52  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 251.601 221.392 216.188 1.00 31.69  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 251.917 222.559 214.009 1.00 24.96  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 247.907 221.238 215.857 1.00 29.87  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 246.966 220.671 216.819 1.00 11.11  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 246.269 219.443 216.248 1.00 28.15  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 246.008 218.475 216.972 1.00 37.34  ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 245.943 221.724 217.240 1.00 19.67  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 245.953 219.467 214.951 1.00 37.28  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 245.364 218.296 214.309 1.00 31.54  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 246.325 217.114 214.332 1.00 40.76  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 245.910 215.971 214.555 1.00 45.44  ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 244.958 218.639 212.875 1.00 34.56  ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 244.615 217.450 212.023 1.00 38.98  ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 243.434 216.767 212.004 1.00 39.61  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 245.460 216.817 211.055 1.00 39.73  ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 243.493 215.744 211.088 1.00 35.91  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 244.727 215.753 210.493 1.00 33.27  ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 246.766 217.044 210.612 1.00 40.30  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 245.257 214.919 209.511 1.00 39.93  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 247.290 216.215 209.638 1.00 39.62  ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 246.537 215.166 209.098 1.00 43.38  ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 247.615 217.369 214.103 1.00 33.55  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 248.598 216.292 214.134 1.00 40.93  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 248.828 215.775 215.549 1.00 41.23  ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 249.080 214.580 215.736 1.00 45.78  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 249.917 216.763 213.524 1.00 37.59  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 250.062 216.449 212.046 1.00 44.39  ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 251.782 216.470 211.512 1.00 69.35  ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 252.143 218.219 211.613 1.00 45.07  ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 248.757 216.652 216.548 1.00 33.63  ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 248.955 216.272 217.941 1.00 26.01  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 247.698 215.709 218.589 1.00 35.70  ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 247.750 215.303 219.755 1.00 40.71  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 249.452 217.474 218.751 1.00 31.52  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 250.962 217.599 218.742 1.00 42.20  ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 251.653 216.971 219.544 1.00 46.01  ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 251.483 218.413 217.833 1.00 32.40  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 246.578 215.675 217.872 1.00 30.29  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 245.338 215.167 218.414 1.00 23.28  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 244.515 216.164 219.197 1.00 23.83  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 243.469 215.785 219.739 1.00 40.26  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 244.944 217.420 219.279 1.00 23.71  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 244.186 218.430 220.000 1.00 25.48  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 242.958 218.849 219.201 1.00 28.51  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 242.927 218.759 217.971 1.00 33.56  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 245.053 219.656 220.290 1.00 25.41  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 246.479 219.439 220.801 1.00 21.94  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 247.117 220.772 221.141 1.00 25.88  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 246.505 218.515 222.003 1.00 34.65  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 241.937 219.311 219.918 1.00 29.11  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 240.716 219.822 219.310 1.00 27.91  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 240.770 221.344 219.315 1.00 33.41  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 240.876 221.961 220.380 1.00 52.38  ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 239.480 219.321 220.056 1.00 31.46  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 239.488 217.909 220.166 1.00 34.84  ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 240.691 221.944 218.133 1.00 28.83  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 240.824 223.390 218.004 1.00 38.14  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 239.512 224.053 218.400 1.00 35.95  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 238.446 223.719 217.869 1.00 33.68  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 241.230 223.773 216.572 1.00 26.31  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 241.097 225.273 216.366 1.00 26.11  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 242.649 223.313 216.285 1.00 30.57  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 239.587 224.993 219.339 1.00 30.00  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 238.439 225.778 219.768 1.00 33.27  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 238.730 227.253 219.537 1.00 36.17  ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 239.772 227.759 219.967 1.00 45.72  ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 238.110 225.530 221.243 1.00 36.10  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 236.767 226.081 221.673 1.00 38.13  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 236.611 227.427 221.982 1.00 38.95  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 235.655 225.256 221.769 1.00 34.06  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 235.387 227.934 222.373 1.00 29.33  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 234.427 225.755 222.161 1.00 43.60  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 234.299 227.094 222.461 1.00 44.62  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 233.078 227.594 222.851 1.00 48.84  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 237.811 227.935 218.860 1.00 41.09  ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 237.886 229.373 218.655 1.00 43.11  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 236.546 229.994 219.014 1.00 47.71  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 235.491 229.463 218.653 1.00 47.95  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 238.253 229.723 217.208 1.00 38.73  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 239.455 228.970 216.664 1.00 40.61  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 239.799 229.375 215.246 1.00 46.27  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 239.584 228.617 214.301 1.00 50.49  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 240.338 230.579 215.090 1.00 43.12  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 236.588 231.115 219.724 1.00 51.49  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 235.367 231.815 220.105 1.00 56.66  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 234.826 232.561 218.893 1.00 58.52  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 235.564 233.275 218.202 1.00 61.77  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 235.624 232.764 221.287 1.00 54.33  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 236.807 233.691 221.001 1.00 55.04  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 235.865 231.970 222.563 1.00 53.62  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 237.123 234.641 222.134 1.00 57.46  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 233.534 232.381 218.618 1.00 62.21  ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 232.888 233.015 217.470 1.00 63.00  ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 232.369 234.383 217.901 1.00 63.53  ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 231.197 234.570 218.234 1.00 64.13  ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 231.777 232.129 216.923 1.00 65.10  ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 232.245 230.748 216.490 1.00 66.23  ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 233.400 230.840 215.505 1.00 63.08  ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 234.162 229.528 215.424 1.00 64.61  ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 233.249 228.363 215.263 1.00 66.20  ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 233.278 235.360 217.894 1.00 58.42  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 232.908 236.713 218.288 1.00 61.48  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 232.098 237.378 217.179 1.00 60.43  ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 232.194 237.031 215.996 1.00 59.50  ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 234.156 237.541 218.636 1.00 60.17  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 234.747 237.080 219.958 1.00 59.50  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 235.184 237.441 217.521 1.00 60.28  ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 231.286 238.351 217.575 1.00 62.48  ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 230.459 239.105 216.641 1.00 63.42  ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 230.128 240.451 217.278 1.00 67.58  ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 230.721 240.840 218.290 1.00 70.17  ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 229.207 238.309 216.254 1.00 64.12  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 228.418 237.810 217.423 1.00 60.18  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 227.586 238.622 218.163 1.00 61.16  ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 228.332 236.578 217.979 1.00 65.28  ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 227.023 237.913 219.124 1.00 66.72  ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 227.459 236.669 219.035 1.00 71.05  ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 229.180 241.171 216.673 1.00 73.43  ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 228.854 242.516 217.140 1.00 73.92  ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 228.268 242.496 218.547 1.00 73.10  ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 228.589 243.359 219.373 1.00 71.27  ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 227.889 243.189 216.164 1.00 71.73  ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 226.719 242.316 215.739 1.00 75.16  ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 225.841 243.024 214.721 1.00 78.94  ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 225.163 244.181 215.293 1.00 78.92  ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 225.454 245.441 215.000 1.00 75.84  ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 226.415 245.747 214.144 1.00 74.06  ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 224.764 246.419 215.580 1.00 74.16  ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 227.407 241.525 218.840 1.00 71.77  ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 226.721 241.451 220.122 1.00 74.20  ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 227.443 240.569 221.134 1.00 71.75  ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 226.898 240.315 222.214 1.00 71.79  ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 225.288 240.951 219.923 1.00 77.14  ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 224.430 241.829 219.016 1.00 74.23  ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 224.021 243.130 219.700 1.00 74.44  ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 224.859 244.310 219.224 1.00 74.38  ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 224.397 245.598 219.811 1.00 73.84  ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 228.643 240.093 220.811 1.00 65.88  ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 229.416 239.299 221.755 1.00 61.49  ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 229.792 240.147 222.964 1.00 64.44  ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 230.281 241.271 222.819 1.00 66.83  ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 230.672 238.752 221.078 1.00 63.57  ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 231.248 237.518 221.733 1.00 65.45  ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 230.711 236.262 221.486 1.00 62.56  ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 232.333 237.608 222.594 1.00 63.18  ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 231.237 235.131 222.078 1.00 61.29  ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 232.866 236.482 223.192 1.00 59.37  ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 232.313 235.247 222.931 1.00 58.97  ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 232.840 234.124 223.524 1.00 65.63  ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 229.564 239.606 224.161 1.00 66.94  ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 229.829 240.351 225.386 1.00 66.06  ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 230.636 239.520 226.376 1.00 68.70  ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 231.097 238.423 226.046 1.00 66.58  ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 228.518 240.810 226.030 1.00 66.97  ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 228.805 241.589 227.198 1.00 68.82  ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 227.667 239.613 226.422 1.00 61.42  ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 230.814 240.042 227.591 1.00 74.49  ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 231.568 239.312 228.597 1.00 71.46  ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 230.878 238.036 229.040 1.00 69.80  ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 231.537 237.032 229.327 1.00 73.03  ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 229.545 238.057 229.110 1.00 70.25  ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 228.806 236.860 229.499 1.00 71.44  ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 228.972 235.748 228.471 1.00 74.45  ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 229.071 234.570 228.834 1.00 78.00  ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 227.328 237.196 229.698 1.00 70.47  ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 227.072 238.360 230.645 1.00 75.53  ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 227.932 238.305 231.895 1.00 80.14  ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 228.557 239.333 232.233 1.00 77.93  ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 227.974 237.240 232.548 1.00 78.31  ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 228.997 236.100 227.183 1.00 63.98  ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 229.221 235.096 226.148 1.00 58.01  ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 230.611 234.483 226.269 1.00 57.82  ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 230.786 233.277 226.057 1.00 65.43  ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 229.024 235.710 224.763 1.00 65.51  ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 227.605 236.190 224.534 1.00 70.34  ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 226.665 235.403 224.769 1.00 72.48  ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 227.430 237.352 224.112 1.00 69.31  ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 231.613 235.300 226.600 1.00 50.85  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 232.959 234.773 226.801 1.00 52.49  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 233.005 233.823 227.991 1.00 62.47  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 233.701 232.801 227.953 1.00 66.82  ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 233.950 235.922 226.991 1.00 51.83  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 235.388 235.492 226.963 1.00 49.88  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 235.937 234.938 225.818 1.00 53.35  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 236.192 235.642 228.079 1.00 56.02  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 237.260 234.542 225.789 1.00 55.58  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 237.516 235.248 228.056 1.00 60.22  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 238.050 234.697 226.909 1.00 56.05  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 232.275 234.148 229.061 1.00 60.54  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 232.203 233.251 230.210 1.00 51.47  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 231.545 231.929 229.836 1.00 52.35  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 231.978 230.862 230.287 1.00 57.65  ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 231.448 233.925 231.355 1.00 56.96  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 232.221 235.080 231.962 1.00 65.22  ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 233.357 235.339 231.512 1.00 66.44  ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 231.693 235.730 232.888 1.00 61.73  ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 230.490 231.979 229.017 1.00 55.11  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 229.861 230.750 228.543 1.00 52.28  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 230.832 229.918 227.716 1.00 52.38  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 230.892 228.692 227.862 1.00 59.73  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 228.613 231.078 227.723 1.00 52.25  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 227.481 231.715 228.512 1.00 57.08  ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 226.880 230.771 229.535 1.00 72.98  ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 226.864 229.548 229.280 1.00 64.80  ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 226.420 231.251 230.592 1.00 76.04  ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 231.599 230.568 226.838 1.00 47.98  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 232.564 229.842 226.018 1.00 45.12  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 233.681 229.254 226.871 1.00 51.10  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 234.140 228.134 226.618 1.00 52.88  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 233.134 230.764 224.940 1.00 48.20  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 232.169 230.979 223.791 1.00 59.68  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 231.237 230.162 223.634 1.00 58.87  ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 232.341 231.965 223.044 1.00 52.37  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 234.135 229.997 227.883 1.00 51.74  ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 235.181 229.487 228.765 1.00 42.55  ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 234.707 228.260 229.534 1.00 45.74  ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 235.464 227.298 229.707 1.00 49.41  ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 235.636 230.583 229.729 1.00 41.41  ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 236.797 231.462 229.259 1.00 41.63  ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 237.204 232.437 230.351 1.00 44.52  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 237.979 230.606 228.836 1.00 44.82  ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 233.460 228.277 230.009 1.00 47.89  ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 232.927 227.124 230.728 1.00 41.99  ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 232.817 225.908 229.818 1.00 41.71  ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 233.051 224.774 230.253 1.00 51.94  ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 231.569 227.465 231.340 1.00 44.46  ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 231.658 228.342 232.575 1.00 41.56  ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 230.296 228.576 233.201 1.00 43.67  ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 230.121 229.964 233.612 1.00 50.92  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 229.151 230.757 233.179 1.00 49.05  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 228.233 230.325 232.330 1.00 36.62  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 229.098 232.013 233.611 1.00 53.64  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 232.452 226.122 228.552 1.00 40.06  ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 232.376 225.017 227.602 1.00 39.24  ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 233.748 224.388 227.382 1.00 38.06  ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 233.882 223.160 227.332 1.00 46.09  ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 231.788 225.506 226.278 1.00 38.42  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 230.464 226.007 226.498 1.00 44.13  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 231.730 224.372 225.266 1.00 41.58  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 234.782 225.221 227.250 1.00 38.94  ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 236.133 224.707 227.037 1.00 34.80  ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 236.623 223.958 228.270 1.00 38.75  ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 237.195 222.866 228.164 1.00 45.88  ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 237.087 225.855 226.660 1.00 31.43  ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 238.504 225.339 226.512 1.00 35.49  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 236.629 226.520 225.379 1.00 39.59  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 236.411 224.532 229.456 1.00 35.17  ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 236.901 223.902 230.679 1.00 33.00  ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 236.175 222.593 230.962 1.00 39.02  ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 236.788 221.629 231.433 1.00 44.30  ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 236.761 224.863 231.858 1.00 36.48  ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 237.661 226.100 231.820 1.00 31.75  ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 237.723 226.765 233.185 1.00 31.88  ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 239.053 225.736 231.334 1.00 39.81  ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 234.869 222.542 230.692 1.00 45.94  ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 234.124 221.304 230.892 1.00 33.42  ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 234.633 220.199 229.976 1.00 46.40  ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 234.794 219.050 230.405 1.00 52.50  ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 232.633 221.544 230.661 1.00 35.00  ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 231.821 221.684 231.935 1.00 43.90  ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 230.615 222.582 231.721 1.00 44.82  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 229.802 222.697 232.925 1.00 50.93  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 229.089 223.767 233.248 1.00 52.65  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 229.064 224.839 232.474 1.00 47.77  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 228.385 223.761 234.376 1.00 48.30  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 234.892 220.527 228.709 1.00 48.43  ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 235.375 219.522 227.768 1.00 35.28  ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 236.790 219.072 228.110 1.00 37.87  ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 237.103 217.879 228.030 1.00 50.25  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 235.317 220.071 226.344 1.00 36.94  ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 233.919 220.145 225.756 1.00 45.54  ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 233.916 220.940 224.461 1.00 47.54  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 234.908 220.446 223.514 1.00 42.29  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 235.214 221.042 222.370 1.00 44.36  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 234.621 222.164 221.996 1.00 44.22  ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 236.138 220.500 221.582 1.00 39.35  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 237.658 220.008 228.490 1.00 35.88  ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 239.054 219.687 228.756 1.00 40.08  ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 239.317 219.268 230.195 1.00 40.53  ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 240.385 218.712 230.475 1.00 48.29  ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 239.946 220.883 228.408 1.00 34.43  ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 239.706 221.971 229.282 1.00 45.86  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 238.382 219.514 231.108 1.00 36.90  ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 238.587 219.159 232.498 1.00 33.10  ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 237.783 217.958 232.948 1.00 44.84  ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 238.276 217.125 233.714 1.00 49.98  ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 236.541 217.857 232.478 1.00 49.81  ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 235.668 216.756 232.865 1.00 44.25  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 235.712 215.603 231.870 1.00 46.95  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 235.673 214.436 232.275 1.00 49.27  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 234.228 217.254 233.017 1.00 37.64  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 234.037 218.656 234.139 1.00 52.95  ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 235.793 215.904 230.577 1.00 42.61  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 235.765 214.885 229.537 1.00 39.18  ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 237.154 214.434 229.103 1.00 37.48  ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 237.257 213.578 228.217 1.00 41.86  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 234.988 215.400 228.322 1.00 32.37  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 233.524 215.688 228.607 1.00 39.06  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 232.813 216.223 227.376 1.00 49.15  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 231.339 216.461 227.654 1.00 47.55  ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 231.133 217.554 228.644 1.00 43.68  ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 238.213 214.981 229.703 1.00 38.37  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 239.593 214.605 229.384 1.00 33.95  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 239.888 214.765 227.894 1.00 39.95  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 240.540 213.920 227.277 1.00 45.53  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 239.899 213.180 229.849 1.00 38.24  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 241.379 212.949 230.084 1.00 42.10  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 242.071 213.801 230.641 1.00 50.93  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 241.872 211.792 229.660 1.00 35.66  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 239.404 215.857 227.311 1.00 38.40  ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 239.594 216.142 225.895 1.00 35.80  ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 240.680 217.198 225.737 1.00 45.10  ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 240.561 218.301 226.281 1.00 49.67  ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 238.290 216.614 225.255 1.00 29.53  ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 238.441 217.092 223.821 1.00 39.65  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 237.136 217.581 223.229 1.00 51.65  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 236.104 217.518 223.929 1.00 54.30  ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 237.141 218.031 222.065 1.00 52.94  ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 241.730 216.862 224.994 1.00 41.84  ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 242.793 217.821 224.720 1.00 34.38  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 242.286 218.876 223.746 1.00 39.17  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 241.842 218.548 222.641 1.00 49.14  ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 244.017 217.106 224.156 1.00 33.02  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 244.722 216.201 225.150 1.00 38.64  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 246.033 215.682 224.585 1.00 43.91  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 245.793 214.694 223.456 1.00 42.98  ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 247.065 214.100 222.959 1.00 38.71  ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 242.352 220.142 224.152 1.00 33.26  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 241.796 221.246 223.381 1.00 29.81  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 242.879 222.293 223.168 1.00 29.61  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 243.561 222.690 224.119 1.00 35.62  ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 240.574 221.872 224.081 1.00 28.26  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 239.414 220.877 224.118 1.00 31.64  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 240.152 223.157 223.383 1.00 34.84  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 238.118 221.477 224.597 1.00 38.61  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 243.037 222.733 221.922 1.00 32.57  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 243.930 223.835 221.575 1.00 28.69  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 243.075 225.090 221.436 1.00 29.21  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 242.459 225.322 220.394 1.00 43.05  ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 244.702 223.533 220.296 1.00 26.60  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 243.040 225.899 222.492 1.00 23.82  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 242.215 227.105 222.530 1.00 21.81  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 242.966 228.219 221.813 1.00 33.18  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 243.872 228.837 222.376 1.00 45.25  ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 241.885 227.482 223.969 1.00 26.57  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 240.851 228.565 224.095 1.00 31.43  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 239.922 228.778 223.090 1.00 33.79  ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 240.805 229.367 225.222 1.00 37.37  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 238.971 229.773 223.206 1.00 36.94  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 239.856 230.363 225.344 1.00 44.05  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 238.937 230.566 224.335 1.00 43.99  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 242.588 228.480 220.566 1.00 34.82  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 243.228 229.510 219.757 1.00 35.28  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 242.419 230.793 219.880 1.00 36.06  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 241.220 230.814 219.581 1.00 43.95  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 243.351 229.071 218.291 1.00 35.17  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 244.051 227.714 218.203 1.00 30.99  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 244.104 230.116 217.486 1.00 35.83  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 244.284 227.238 216.791 1.00 39.16  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 243.073 231.864 220.321 1.00 44.84  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 242.424 233.148 220.535 1.00 47.30  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 243.269 234.249 219.914 1.00 47.24  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 244.502 234.196 219.955 1.00 51.38  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 242.213 233.413 222.033 1.00 48.99  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 241.467 234.696 222.352 1.00 56.39  ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 241.179 234.887 224.121 1.00 75.69  ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 240.401 236.499 224.168 1.00 55.02  ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 242.602 235.243 219.336 1.00 58.70  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 243.257 236.362 218.680 1.00 52.47  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 243.039 237.639 219.481 1.00 54.32  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 242.092 237.755 220.263 1.00 62.90  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 242.733 236.539 217.249 1.00 49.39  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 243.586 237.484 216.426 1.00 63.20  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 244.775 237.173 216.204 1.00 64.57  ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 243.068 238.538 216.001 1.00 68.30  ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 243.943 238.603 219.281 1.00 54.83  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 243.824 239.882 219.974 1.00 60.14  ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 242.556 240.623 219.570 1.00 64.29  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 242.004 241.388 220.369 1.00 66.30  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 245.054 240.747 219.700 1.00 61.45  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 245.357 240.944 218.225 1.00 64.57  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 246.364 242.049 217.981 1.00 66.49  ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 246.778 242.706 218.959 1.00 66.58  ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 246.740 242.263 216.810 1.00 62.75  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 242.084 240.416 218.338 1.00 61.11  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 240.836 241.031 217.905 1.00 60.72  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 239.632 240.479 218.655 1.00 62.22  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 238.606 241.163 218.745 1.00 68.50  ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 240.647 240.834 216.400 1.00 64.58  ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 240.611 239.457 216.066 1.00 69.43  ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 239.732 239.261 219.193 1.00 58.00  ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 238.631 238.684 219.954 1.00 56.80  ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 238.472 239.330 221.324 1.00 61.24  ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 237.432 239.144 221.964 1.00 69.15  ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 238.836 237.177 220.111 1.00 59.25  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 238.754 236.437 218.790 1.00 60.48  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 238.448 237.026 217.754 1.00 64.50  ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 239.029 235.138 218.822 1.00 54.04  ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 239.472 240.077 221.788 1.00 64.03  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 239.417 240.738 223.090 1.00 68.19  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 238.556 241.988 222.930 1.00 70.55  ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 239.035 243.033 222.487 1.00 71.70  ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 240.812 241.078 223.619 1.00 67.05  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 240.724 241.600 225.044 1.00 65.73  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 241.721 239.861 223.543 1.00 65.00  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 237.279 241.884 223.290 1.00 74.27  ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 236.341 242.989 223.165 1.00 73.69  ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 236.193 243.798 224.447 1.00 75.86  ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 235.484 244.809 224.445 1.00 78.14  ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 234.969 242.465 222.727 1.00 73.50  ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 234.903 241.853 221.327 1.00 73.73  ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 233.532 241.249 221.069 1.00 73.95  ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 235.243 242.893 220.271 1.00 75.94  ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 236.840 243.385 225.533 1.00 74.91  ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 236.719 244.080 226.807 1.00 77.68  ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 237.884 243.652 227.689 1.00 77.64  ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 238.465 242.580 227.497 1.00 78.77  ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 235.367 243.782 227.475 1.00 76.73  ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 235.305 244.241 228.918 1.00 78.19  ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 234.907 245.400 229.158 1.00 76.51  ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 235.645 243.441 229.814 1.00 77.06  ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 238.224 244.511 228.655 1.00 77.27  ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 239.340 244.219 229.550 1.00 78.42  ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 239.077 242.986 230.406 1.00 78.26  ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 240.024 242.357 230.891 1.00 83.43  ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 239.630 245.427 230.440 1.00 77.99  ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 240.716 245.168 231.313 1.00 79.87  ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 237.807 242.627 230.608 1.00 67.51  ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 237.500 241.428 231.368 1.00 61.66  ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 237.870 240.153 230.638 1.00 62.09  ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 238.061 239.108 231.266 1.00 62.97  ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 237.967 240.216 229.308 1.00 60.06  ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 238.395 239.054 228.535 1.00 60.41  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 239.805 238.632 228.926 1.00 59.90  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 240.090 237.441 229.094 1.00 62.80  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 238.326 239.363 227.037 1.00 59.15  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 236.943 239.269 226.451 1.00 57.84  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 235.855 239.833 227.096 1.00 59.52  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 236.736 238.621 225.244 1.00 62.46  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 234.588 239.748 226.553 1.00 64.36  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 235.471 238.533 224.696 1.00 66.10  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 234.396 239.097 225.351 1.00 66.23  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 240.705 239.607 229.075 1.00 60.83  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 242.076 239.296 229.462 1.00 54.44  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 242.179 238.938 230.938 1.00 56.38  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 243.051 238.150 231.321 1.00 65.92  ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 242.992 240.475 229.135 1.00 60.18  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 243.234 240.739 227.648 1.00 67.71  ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 244.078 241.988 227.451 1.00 64.86  ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 243.891 239.536 226.987 1.00 61.76  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 241.313 239.508 231.779 1.00 54.54  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 241.352 239.199 233.206 1.00 49.23  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 241.019 237.734 233.459 1.00 55.74  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 241.677 237.066 234.265 1.00 59.50  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 240.389 240.112 233.967 1.00 53.15  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 240.388 239.896 235.474 1.00 62.74  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 241.712 240.253 236.121 1.00 66.88  ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 242.446 241.093 235.559 1.00 67.45  ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 242.022 239.692 237.194 1.00 63.40  ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 239.991 237.217 232.781 1.00 54.84  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 239.671 235.799 232.901 1.00 48.52  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 240.772 234.936 232.300 1.00 45.55  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 241.115 233.881 232.846 1.00 45.53  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 238.331 235.500 232.228 1.00 46.41  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 237.181 236.368 232.707 1.00 46.84  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 236.762 236.006 234.121 1.00 57.38  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 235.312 235.983 234.267 1.00 65.36  ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 234.673 235.519 235.332 1.00 58.87  ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 235.328 235.035 236.375 1.00 54.18  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 233.343 235.542 235.352 1.00 55.81  ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 241.336 235.369 231.170 1.00 47.02  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 242.396 234.599 230.529 1.00 39.36  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 243.663 234.593 231.375 1.00 40.12  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 244.376 233.585 231.427 1.00 46.66  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 242.680 235.161 229.136 1.00 43.95  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 241.806 234.576 228.032 1.00 50.28  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 241.813 232.774 227.930 1.00 57.77  ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 243.568 232.422 227.979 1.00 52.55  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 243.959 235.712 232.043 1.00 50.98  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 245.152 235.790 232.880 1.00 46.56  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 245.097 234.774 234.014 1.00 51.25  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 246.094 234.109 234.318 1.00 51.67  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 245.307 237.207 233.434 1.00 46.03  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 246.574 237.382 234.243 1.00 47.73  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 247.678 237.348 233.703 1.00 57.81  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 246.422 237.572 235.548 1.00 49.61  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 243.935 234.645 234.657 1.00 52.49  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 243.787 233.666 235.729 1.00 43.42  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 243.870 232.243 235.190 1.00 43.10  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 244.454 231.361 235.830 1.00 49.61  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 242.464 233.885 236.461 1.00 44.12  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 242.273 235.286 236.697 1.00 50.83  ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 242.466 233.153 237.792 1.00 49.59  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 243.286 232.000 234.014 1.00 41.33  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 243.277 230.655 233.449 1.00 39.16  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 244.658 230.227 232.970 1.00 39.11  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 244.994 229.039 233.037 1.00 39.80  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 242.270 230.580 232.301 1.00 39.61  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 242.047 229.208 231.664 1.00 36.07  ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 241.409 228.257 232.662 1.00 41.75  ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 241.192 229.332 230.414 1.00 37.95  ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 245.469 231.168 232.483 1.00 43.01  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 246.782 230.810 231.954 1.00 40.01  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 247.738 230.365 233.053 1.00 45.75  ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 248.586 229.497 232.817 1.00 47.63  ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 247.378 231.987 231.183 1.00 33.92  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 246.796 232.264 229.797 1.00 33.55  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 247.461 233.477 229.170 1.00 44.26  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 246.946 231.047 228.902 1.00 41.32  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 247.625 230.940 234.249 1.00 40.21  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 248.575 230.656 235.320 1.00 37.09  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 248.097 229.524 236.227 1.00 42.99  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 248.767 228.494 236.348 1.00 42.85  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 248.832 231.927 236.137 1.00 35.92  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 246.942 229.702 236.869 1.00 46.18  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 246.445 228.701 237.804 1.00 41.43  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 245.731 227.547 237.115 1.00 42.50  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 245.503 226.512 237.751 1.00 49.50  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 245.497 229.345 238.819 1.00 40.14  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 246.115 230.537 239.519 1.00 47.94  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 247.175 230.429 240.135 1.00 47.85  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 245.450 231.683 239.431 1.00 48.23  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 245.375 227.695 235.842 1.00 45.86  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 244.588 226.674 235.182 1.00 43.51  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 243.147 226.624 235.628 1.00 43.44  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 242.463 225.629 235.379 1.00 46.32  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 242.665 227.675 236.287 1.00 53.36  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 241.308 227.705 236.809 1.00 50.17  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 240.876 229.155 236.963 1.00 54.41  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 241.711 230.058 237.052 1.00 60.77  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 241.210 226.977 238.153 1.00 48.53  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 241.994 227.651 239.268 1.00 50.31  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 241.939 226.882 240.571 1.00 63.69  ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 241.306 225.807 240.602 1.00 69.73  ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 242.529 227.354 241.566 1.00 58.80  ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 239.569 229.363 236.991 1.00 45.20  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 238.968 230.675 237.216 1.00 46.73  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 238.108 230.586 238.470 1.00 57.28  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 237.230 229.719 238.542 1.00 56.75  ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 238.127 231.136 236.010 1.00 50.47  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 237.596 232.541 236.238 1.00 52.71  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 238.952 231.075 234.734 1.00 45.09  ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 238.326 231.443 239.472 1.00 59.63  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 237.598 231.276 240.742 1.00 57.36  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 236.096 231.473 240.624 1.00 61.82  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 235.328 230.682 241.185 1.00 60.81  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 238.244 232.333 241.649 1.00 56.86  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 238.776 233.362 240.705 1.00 55.93  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 239.246 232.593 239.506 1.00 55.87  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 235.651 232.508 239.912 1.00 51.41  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 234.239 232.812 239.800 1.00 49.84  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 233.560 232.379 238.521 1.00 57.80  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 232.435 232.826 238.258 1.00 61.70  ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 234.191 231.530 237.708 1.00 48.41  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 233.581 231.134 236.442 1.00 46.75  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 232.357 230.255 236.663 1.00 51.17  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 231.318 230.451 236.021 1.00 50.30  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 234.607 230.416 235.568 1.00 45.09  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 234.289 230.362 234.074 1.00 40.17  ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 234.224 231.765 233.493 1.00 51.38  ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 235.317 229.523 233.337 1.00 41.84  ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 232.456 229.283 237.567 1.00 49.91  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 231.375 228.342 237.844 1.00 42.67  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 230.731 228.725 239.171 1.00 55.38  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 231.345 228.570 240.232 1.00 56.98  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 231.891 226.905 237.879 1.00 44.20  ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 232.520 226.449 236.591 1.00 49.27  ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 233.834 226.767 236.293 1.00 49.35  ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 231.794 225.702 235.679 1.00 49.18  ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 234.413 226.349 235.110 1.00 43.74  ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 232.368 225.281 234.494 1.00 49.20  ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 233.679 225.605 234.210 1.00 40.35  ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 229.497 229.223 239.109 1.00 63.21  ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 228.749 229.603 240.297 1.00 58.35  ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 227.304 229.150 240.152 1.00 63.97  ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 226.785 229.023 239.040 1.00 66.81  ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 228.788 231.118 240.543 1.00 56.37  ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 230.178 231.696 240.739 1.00 58.83  ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 230.179 233.212 240.725 1.00 63.48  ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 229.082 233.807 240.746 1.00 59.00  ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 231.276 233.808 240.697 1.00 67.24  ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 226.660 228.916 241.291 1.00 55.05  ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 225.254 228.538 241.276 1.00 52.85  ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 225.050 227.177 240.642 1.00 55.26  ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 225.704 226.192 241.002 1.00 57.93  ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 224.121 227.115 239.683 1.00 58.32  ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 223.819 225.851 239.020 1.00 61.05  ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 224.988 225.360 238.177 1.00 60.24  ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 225.163 224.147 238.012 1.00 61.21  ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 222.567 225.997 238.157 1.00 57.40  ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 221.313 226.204 238.981 1.00 65.07  ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 221.261 225.700 240.122 1.00 63.48  ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 220.380 226.871 238.488 1.00 65.97  ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 225.788 226.278 237.629 1.00 54.56  ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 226.943 225.872 236.835 1.00 51.27  ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 227.950 225.103 237.681 1.00 53.30  ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 228.518 224.103 237.227 1.00 61.54  ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 227.599 227.098 236.199 1.00 51.93  ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 226.623 228.040 235.515 1.00 45.86  ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 226.242 227.576 234.123 1.00 56.57  ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 226.837 226.590 233.638 1.00 59.24  ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 225.346 228.196 233.513 1.00 61.72  ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 228.191 225.560 238.912 1.00 46.76  ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 229.102 224.846 239.801 1.00 48.02  ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 228.556 223.472 240.169 1.00 52.82  ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 229.305 222.489 240.198 1.00 50.77  ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 229.363 225.674 241.058 1.00 49.41  ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 230.468 225.124 241.931 1.00 48.82  ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 231.795 225.194 241.530 1.00 44.55  ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 230.183 224.535 243.155 1.00 49.67  ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 232.807 224.693 242.324 1.00 48.69  ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 231.189 224.031 243.956 1.00 55.92  ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 232.499 224.113 243.535 1.00 59.82  ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 233.505 223.613 244.330 1.00 58.86  ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 227.255 223.386 240.462 1.00 52.00  ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 226.658 222.101 240.813 1.00 44.35  ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 226.707 221.130 239.640 1.00 50.24  ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 226.990 219.940 239.821 1.00 57.63  ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 225.219 222.302 241.284 1.00 50.69  ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 226.426 221.619 238.430 1.00 51.12  ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 226.513 220.764 237.250 1.00 45.76  ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 227.950 220.333 236.989 1.00 49.76  ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 228.198 219.201 236.558 1.00 58.42  ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 225.941 221.489 236.032 1.00 53.44  ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 224.722 222.150 236.394 1.00 55.79  ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 225.660 220.502 234.910 1.00 54.62  ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 228.910 221.226 237.239 1.00 49.72  ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 230.314 220.886 237.029 1.00 50.09  ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 230.759 219.768 237.963 1.00 50.21  ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 231.485 218.857 237.550 1.00 51.14  ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 231.185 222.129 237.218 1.00 43.63  ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 232.700 221.930 237.142 1.00 47.80  ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 233.157 221.869 235.695 1.00 47.92  ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 233.423 223.042 237.886 1.00 40.77  ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 230.331 219.818 239.228 1.00 45.56  ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 230.692 218.766 240.173 1.00 44.56  ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 230.064 217.434 239.786 1.00 47.53  ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 230.661 216.372 239.999 1.00 58.30  ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 230.281 219.165 241.589 1.00 44.89  ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 231.080 220.323 242.161 1.00 46.05  ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 232.849 219.971 242.187 1.00 61.38  ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 233.457 221.163 241.000 1.00 51.77  ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 228.852 217.467 239.228 1.00 47.76  ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 228.231 216.240 238.740 1.00 48.12  ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 229.045 215.635 237.603 1.00 53.16  ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 229.266 214.420 237.558 1.00 52.41  ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 226.796 216.521 238.290 1.00 46.92  ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 226.022 216.969 239.409 1.00 54.90  ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 226.160 215.265 237.714 1.00 51.19  ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 229.507 216.476 236.675 1.00 53.75  ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 230.339 215.988 235.580 1.00 48.18  ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 231.710 215.550 236.079 1.00 51.53  ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 232.269 214.561 235.590 1.00 58.77  ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 230.477 217.066 234.506 1.00 45.83  ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 229.160 217.487 233.876 1.00 47.45  ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 229.317 218.663 232.933 1.00 55.23  ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 228.711 219.716 233.129 1.00 54.12  ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 230.135 218.489 231.902 1.00 59.06  ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 232.273 216.280 237.045 1.00 51.31  ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 233.582 215.919 237.580 1.00 48.21  ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 233.539 214.572 238.291 1.00 52.83  ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 234.490 213.786 238.200 1.00 60.93  ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 234.085 217.008 238.527 1.00 53.18  ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 234.627 218.524 237.706 1.00 66.83  ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 232.451 214.292 239.014 1.00 57.73  ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 232.321 213.000 239.679 1.00 55.84  ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 232.275 211.863 238.667 1.00 56.01  ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 232.886 210.809 238.877 1.00 59.33  ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 231.074 212.987 240.562 1.00 56.40  ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 230.958 211.760 241.450 1.00 60.01  ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 229.818 211.901 242.444 1.00 62.67  ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 229.746 210.701 243.373 1.00 63.22  ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 231.038 210.463 244.074 1.00 66.17  ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 231.547 212.055 237.564 1.00 59.83  ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 231.531 211.052 236.505 1.00 56.79  ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 232.905 210.906 235.864 1.00 58.44  ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 233.355 209.787 235.589 1.00 67.76  ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 230.485 211.415 235.451 1.00 59.86  ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 229.081 211.592 236.002 1.00 63.66  ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 228.123 212.167 234.978 1.00 68.71  ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 228.565 212.456 233.846 1.00 65.48  ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 226.928 212.329 235.304 1.00 66.89  ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 233.586 212.027 235.615 1.00 52.96  ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 234.908 211.960 235.014 1.00 53.67  ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 235.928 211.285 235.910 1.00 53.89  ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 236.774 210.522 235.436 1.00 58.45  ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 235.869 211.562 237.214 1.00 55.59  ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 236.770 210.900 238.151 1.00 55.80  ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 236.495 209.403 238.213 1.00 68.00  ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 237.427 208.596 238.307 1.00 72.45  ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 236.643 211.530 239.538 1.00 59.09  ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 235.218 209.014 238.171 1.00 71.34  ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 234.873 207.596 238.173 1.00 65.63  ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 235.397 206.897 236.925 1.00 68.52  ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 235.886 205.763 236.999 1.00 71.96  ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 233.359 207.424 238.290 1.00 69.15  ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 232.875 207.139 239.701 1.00 73.88  ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 231.364 207.145 239.810 1.00 75.08  ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 230.731 208.201 239.783 1.00 72.08  ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 230.775 205.961 239.934 1.00 73.12  ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 235.298 207.555 235.766 1.00 68.68  ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 235.824 206.972 234.536 1.00 67.22  ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 237.334 206.787 234.605 1.00 71.13  ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 237.886 205.924 233.914 1.00 75.10  ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 235.448 207.844 233.338 1.00 63.62  ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 233.958 207.879 233.040 1.00 69.09  ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 233.668 208.625 231.747 1.00 69.77  ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 233.840 210.125 231.927 1.00 71.62  ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 233.455 210.882 230.705 1.00 67.99  ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 238.015 207.583 235.426 1.00 71.41  ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 239.446 207.442 235.648 1.00 68.85  ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 239.763 206.500 236.805 1.00 72.76  ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 240.939 206.230 237.067 1.00 75.89  ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 240.071 208.821 235.901 1.00 70.02  ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 241.585 208.882 235.738 1.00 74.09  ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 242.076 210.267 235.368 1.00 77.39  ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 241.549 210.846 234.395 1.00 75.72  ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 242.991 210.777 236.049 1.00 75.20  ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 238.744 205.977 237.484 1.00 70.55  ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 238.957 205.103 238.620 1.00 71.40  ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 239.586 205.806 239.805 1.00 73.71  ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 240.509 205.277 240.431 1.00 75.46  ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 239.093 207.000 240.121 1.00 76.88  ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 239.600 207.799 241.227 1.00 77.38  ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 238.552 207.876 242.328 1.00 76.85  ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 237.359 208.040 242.054 1.00 72.84  ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 239.978 209.208 240.762 1.00 70.80  ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 241.283 209.318 239.971 1.00 72.35  ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 241.559 210.761 239.590 1.00 74.96  ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 242.443 208.740 240.766 1.00 73.92  ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 239.007 207.756 243.575 1.00 85.49  ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 238.117 207.789 244.737 1.00 86.14  ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 237.965 209.232 245.223 1.00 85.65  ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 238.529 209.655 246.234 1.00 82.32  ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 238.646 206.878 245.836 1.00 85.52  ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 238.425 205.397 245.578 1.00 83.21  ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 239.540 204.353 246.537 1.00 92.90  ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 239.586 205.242 248.092 1.00 83.35  ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 237.177 209.993 244.468 1.00 74.19  ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 236.923 211.399 244.756 1.00 71.66  ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 235.427 211.603 244.942 1.00 73.00  ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 234.639 211.287 244.044 1.00 66.95  ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 237.456 212.290 243.633 1.00 67.77  ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 238.913 212.045 243.239 1.00 68.96  ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 239.294 212.900 242.047 1.00 67.78  ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 239.839 212.316 244.414 1.00 67.86  ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 235.042 212.126 246.097 1.00 74.95  ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 233.639 212.382 246.403 1.00 70.93  ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 233.381 213.808 246.865 1.00 72.33  ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 232.342 214.378 246.524 1.00 70.77  ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 233.149 211.389 247.472 1.00 74.36  ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 231.772 211.736 248.004 1.00 78.76  ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 230.856 211.961 247.185 1.00 78.59  ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 231.604 211.782 249.240 1.00 75.49  ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 234.299 214.398 247.626 1.00 60.07  ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 234.101 215.750 248.127 1.00 57.73  ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 234.257 216.772 247.006 1.00 57.67  ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 234.937 216.533 246.005 1.00 62.70  ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 235.091 216.053 249.251 1.00 61.33  ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 234.939 217.381 249.721 1.00 60.28  ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 233.610 217.926 247.187 1.00 57.93  ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 233.665 218.975 246.174 1.00 51.64  ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 235.072 219.543 246.036 1.00 53.72  ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 235.507 219.871 244.926 1.00 60.97  ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 232.668 220.082 246.512 1.00 52.85  ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 231.264 219.780 246.090 1.00 57.10  ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 230.239 220.694 246.207 1.00 61.33  ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 230.716 218.666 245.551 1.00 56.76  ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 229.119 220.155 245.758 1.00 59.32  ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 229.381 218.925 245.354 1.00 55.68  ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 235.792 219.680 247.152 1.00 58.72  ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 237.154 220.204 247.092 1.00 51.53  ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 238.071 219.272 246.311 1.00 56.53  ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 238.890 219.729 245.505 1.00 62.24  ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 237.694 220.428 248.505 1.00 54.79  ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 236.863 221.378 249.354 1.00 61.93  ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 235.734 220.677 250.083 1.00 68.03  ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 236.018 219.752 250.872 1.00 66.01  ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 234.562 221.052 249.867 1.00 64.85  ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 237.955 217.962 246.542 1.00 60.53  ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 238.774 217.006 245.804 1.00 58.85  ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 238.419 217.000 244.323 1.00 53.55  ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 239.304 216.896 243.465 1.00 58.70  ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 238.614 215.607 246.400 1.00 61.92  ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 238.446 215.590 247.909 1.00 61.80  ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 238.041 214.226 248.433 1.00 67.39  ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 238.423 213.888 249.573 1.00 65.30  ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 237.342 213.491 247.704 1.00 64.81  ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 237.127 217.099 244.003 1.00 48.35  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 236.707 217.101 242.605 1.00 47.88  ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 237.227 218.331 241.872 1.00 51.39  ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 237.662 218.236 240.718 1.00 55.84  ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 235.183 217.026 242.515 1.00 44.64  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 234.551 215.680 242.873 1.00 44.17  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 233.037 215.797 242.933 1.00 46.77  ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 234.971 214.610 241.879 1.00 47.62  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 237.183 219.497 242.521 1.00 45.08  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 237.675 220.714 241.883 1.00 33.02  ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 239.183 220.659 241.674 1.00 37.86  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 239.691 221.143 240.656 1.00 50.81  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 237.291 221.937 242.714 1.00 35.00  ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 237.261 223.223 241.920 1.00 41.82  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 236.185 223.526 241.096 1.00 45.07  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 238.309 224.130 241.989 1.00 49.00  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 236.153 224.698 240.367 1.00 43.68  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 238.285 225.305 241.263 1.00 45.93  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 237.205 225.584 240.453 1.00 48.53  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 237.176 226.752 239.728 1.00 53.84  ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 239.916 220.083 242.630 1.00 39.11  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 241.357 219.930 242.463 1.00 32.20  ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 241.679 219.007 241.295 1.00 40.49  ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 242.609 219.269 240.524 1.00 47.96  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 241.984 219.405 243.754 1.00 43.17  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 242.356 220.492 244.748 1.00 42.71  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 242.971 219.902 246.005 1.00 46.39  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 243.697 220.964 246.815 1.00 50.12  ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 244.923 221.447 246.123 1.00 50.28  ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 240.924 217.915 241.155 1.00 41.89  ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 241.082 217.051 239.989 1.00 33.87  ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 240.695 217.782 238.711 1.00 33.66  ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 241.340 217.613 237.669 1.00 42.97  ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 240.245 215.785 240.157 1.00 33.83  ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 240.186 214.937 238.925 1.00 38.47  ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 241.111 214.025 238.513 1.00 38.00  ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 239.144 214.923 237.943 1.00 38.06  ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 240.711 213.443 237.335 1.00 32.47  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 239.506 213.978 236.964 1.00 41.04  ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 237.940 215.619 237.796 1.00 40.67  ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 238.708 213.710 235.854 1.00 44.22  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 237.150 215.352 236.693 1.00 40.11  ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 237.537 214.407 235.737 1.00 41.86  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 239.635 218.591 238.770 1.00 37.83  ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 239.218 219.360 237.603 1.00 33.21  ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 240.298 220.348 237.180 1.00 41.71  ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 240.582 220.495 235.985 1.00 52.14  ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 237.907 220.086 237.906 1.00 28.86  ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 237.496 221.069 236.849 1.00 32.59  ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 237.091 220.633 235.599 1.00 39.60  ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 237.507 222.429 237.108 1.00 35.62  ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 236.709 221.536 234.627 1.00 37.18  ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 237.127 223.336 236.140 1.00 36.14  ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 236.727 222.889 234.898 1.00 40.75  ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 240.914 221.034 238.146 1.00 34.54  ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 241.971 221.985 237.821 1.00 27.08  ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 243.194 221.280 237.247 1.00 33.46  ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 243.810 221.767 236.291 1.00 47.71  ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 242.351 222.793 239.062 1.00 36.20  ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 241.192 223.469 239.566 1.00 40.71  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 243.421 223.820 238.726 1.00 43.26  ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 243.563 220.130 237.818 1.00 28.52  ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 244.720 219.394 237.319 1.00 25.11  ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 244.485 218.892 235.900 1.00 32.83  ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 245.402 218.901 235.070 1.00 40.95  ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 245.045 218.228 238.253 1.00 35.26  ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 244.043 217.229 238.188 1.00 37.42  ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 243.264 218.441 235.605 1.00 39.98  ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 242.948 217.990 234.254 1.00 29.91  ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 243.006 219.140 233.258 1.00 26.53  ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 243.507 218.978 232.140 1.00 33.63  ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 241.572 217.327 234.230 1.00 23.03  ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 241.550 215.927 234.815 1.00 27.00  ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 241.959 214.873 233.807 1.00 36.44  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 243.054 214.316 233.883 1.00 38.01  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 241.077 214.592 232.855 1.00 38.69  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 242.496 220.312 233.645 1.00 24.08  ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 242.529 221.472 232.757 1.00 30.09  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 243.967 221.878 232.464 1.00 27.40  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 244.306 222.252 231.334 1.00 26.00  ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 241.722 222.634 233.368 1.00 27.00  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 241.996 223.929 232.622 1.00 32.08  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 240.238 222.315 233.348 1.00 25.54  ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 244.837 221.800 233.473 1.00 36.08  ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 246.232 222.194 233.295 1.00 27.42  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 246.913 221.307 232.259 1.00 36.21  ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 247.641 221.793 231.385 1.00 47.52  ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 246.968 222.156 234.647 1.00 28.75  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 246.630 223.398 235.474 1.00 37.04  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 248.471 222.045 234.443 1.00 36.79  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 247.281 223.416 236.838 1.00 36.53  ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 246.678 219.998 232.328 1.00 33.90  ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 247.361 219.047 231.462 1.00 31.22  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 246.653 218.808 230.133 1.00 29.26  ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 247.223 218.142 229.262 1.00 42.54  ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 247.535 217.708 232.187 1.00 35.64  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 246.252 216.907 232.323 1.00 32.48  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 246.533 215.491 232.794 1.00 37.05  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 246.569 214.547 231.683 1.00 50.35  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 245.512 213.895 231.220 1.00 48.03  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 244.312 214.059 231.751 1.00 40.24  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 245.662 213.058 230.197 1.00 43.29  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 245.438 219.327 229.948 1.00 32.56  ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 244.683 219.087 228.726 1.00 28.41  ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 244.426 220.329 227.888 1.00 28.28  ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 244.190 220.193 226.683 1.00 41.89  ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 243.328 218.433 229.047 1.00 32.96  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 243.446 216.946 229.313 1.00 31.36  ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 244.222 216.247 228.662 1.00 44.48  ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 242.673 216.454 230.273 1.00 26.51  ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 244.464 221.521 228.474 1.00 21.73  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 244.138 222.749 227.761 1.00 21.75  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 245.410 223.479 227.356 1.00 29.63  ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 246.263 223.771 228.202 1.00 30.28  ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 243.259 223.661 228.617 1.00 28.72  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 242.732 224.909 227.907 1.00 24.55  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 242.027 224.528 226.618 1.00 21.12  ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 241.803 225.693 228.818 1.00 28.13  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 245.532 223.770 226.063 1.00 33.02  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 246.620 224.573 225.522 1.00 26.25  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 246.015 225.806 224.868 1.00 19.78  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 245.113 225.687 224.033 1.00 30.63  ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 247.451 223.777 224.515 1.00 27.27  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 248.001 222.497 225.062 1.00 23.99  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 247.312 221.305 225.004 1.00 25.67  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 249.175 222.224 225.680 1.00 30.94  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 248.037 220.353 225.562 1.00 34.62  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 249.172 220.883 225.980 1.00 32.82  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 246.508 226.981 225.246 1.00 24.78  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 245.981 228.249 224.755 1.00 27.43  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 246.995 228.867 223.806 1.00 36.39  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 248.162 229.061 224.169 1.00 34.13  ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 245.659 229.206 225.915 1.00 23.74  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 245.375 230.601 225.385 1.00 26.83  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 244.479 228.685 226.720 1.00 30.63  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 246.553 229.178 222.592 1.00 35.53  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 247.387 229.814 221.579 1.00 24.63  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 246.872 231.233 221.393 1.00 29.43  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 245.707 231.440 221.030 1.00 46.56  ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 247.371 229.039 220.255 1.00 22.38  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 248.363 229.646 219.276 1.00 36.95  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 247.681 227.572 220.497 1.00 30.26  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 247.734 232.213 221.643 1.00 23.68  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 247.383 233.619 221.504 1.00 25.08  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 248.152 234.220 220.336 1.00 38.31  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 249.385 234.147 220.294 1.00 43.97  ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 247.686 234.385 222.793 1.00 33.95  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 246.825 235.598 222.993 1.00 47.24  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 245.540 235.476 223.495 1.00 42.99  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 247.299 236.861 222.681 1.00 46.89  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 244.745 236.590 223.680 1.00 44.20  ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 246.509 237.979 222.864 1.00 44.26  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 245.230 237.843 223.365 1.00 46.37  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 247.423 234.811 219.393 1.00 42.44  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 248.007 235.428 218.210 1.00 37.93  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 247.730 236.923 218.241 1.00 44.33  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 246.594 237.341 218.487 1.00 47.16  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 247.444 234.811 216.926 1.00 40.98  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 246.034 235.052 216.856 1.00 56.58  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 247.697 233.312 216.900 1.00 34.57  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 248.765 237.723 217.995 1.00 44.25  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 248.621 239.171 218.007 1.00 43.79  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 249.640 239.788 217.061 1.00 48.27  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 250.662 239.182 216.731 1.00 50.64  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 248.783 239.739 219.422 1.00 47.04  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 250.177 239.579 220.003 1.00 51.65  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 250.378 240.457 221.564 1.00 74.68  ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 249.975 242.129 221.067 1.00 54.12  ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 249.342 241.013 216.626 1.00 53.37  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 250.210 241.757 215.729 1.00 50.30  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 251.453 242.251 216.470 1.00 55.72  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 251.416 242.464 217.685 1.00 57.33  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 249.459 242.940 215.128 1.00 54.31  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 248.572 242.536 213.967 1.00 52.43  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 249.001 241.820 213.063 1.00 44.72  ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 247.326 242.993 213.988 1.00 55.61  ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 252.570 242.445 215.759 1.00 60.89  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 253.817 242.881 216.414 1.00 58.36  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 253.855 244.385 216.670 1.00 62.51  ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 254.774 245.095 216.252 1.00 65.72  ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 254.885 242.425 215.412 1.00 55.28  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 254.216 242.528 214.093 1.00 55.33  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 252.761 242.206 214.316 1.00 60.64  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 252.841 244.882 217.372 1.00 75.39  ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 252.811 246.286 217.745 1.00 78.37  ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 253.832 246.565 218.845 1.00 80.28  ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 254.227 245.678 219.605 1.00 76.81  ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 251.412 246.690 218.210 1.00 77.92  ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 251.387 248.039 218.641 1.00 75.79  ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 254.268 247.823 218.918 1.00 87.33  ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 255.251 248.231 219.917 1.00 89.48  ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 254.584 248.615 221.236 1.00 87.41  ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 254.878 248.028 222.282 1.00 83.69  ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 256.094 249.393 219.379 1.00 88.57  ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 256.874 248.985 218.269 1.00 85.97  ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 253.686 249.602 221.199 1.00 91.35  ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 253.009 250.030 222.418 1.00 89.98  ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 252.018 248.983 222.912 1.00 91.42  ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 251.848 248.819 224.126 1.00 93.30  ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 252.302 251.366 222.187 1.00 89.94  ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 251.381 251.385 220.979 1.00 92.00  ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 250.399 252.539 221.013 1.00 95.49  ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 250.427 253.316 221.991 1.00 95.99  ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 249.600 252.669 220.063 1.00 93.03  ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 251.354 248.275 221.996 1.00 77.78  ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 250.421 247.239 222.410 1.00 74.73  ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 251.109 246.077 223.099 1.00 74.10  ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 250.550 245.465 224.012 1.00 74.85  ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 252.328 245.751 222.664 1.00 73.55  ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 253.078 244.672 223.297 1.00 74.83  ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 253.401 245.006 224.748 1.00 77.41  ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 253.305 244.143 225.629 1.00 73.20  ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 254.360 244.399 222.510 1.00 75.74  ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 255.251 243.251 222.981 1.00 75.96  ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 254.505 241.934 222.876 1.00 68.63  ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 256.539 243.205 222.177 1.00 75.92  ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 253.790 246.256 225.016 1.00 74.77  ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 254.045 246.673 226.391 1.00 65.76  ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 252.754 246.738 227.197 1.00 69.01  ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 252.739 246.404 228.387 1.00 73.36  ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 254.754 248.027 226.408 1.00 65.13  ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 256.078 248.049 225.666 1.00 70.16  ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 256.636 249.459 225.578 1.00 72.71  ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 257.815 249.529 224.622 1.00 70.16  ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 258.148 250.934 224.262 1.00 72.71  ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 251.662 247.180 226.568 1.00 67.59  ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 250.385 247.264 227.271 1.00 67.38  ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 249.901 245.885 227.701 1.00 71.99  ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 249.356 245.723 228.799 1.00 72.32  ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 249.343 247.949 226.387 1.00 70.26  ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 247.943 247.855 226.958 1.00 74.94  ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 247.698 248.443 228.032 1.00 74.16  ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 247.087 247.193 226.334 1.00 72.83  ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 250.087 244.877 226.845 1.00 68.83  ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 249.687 243.520 227.200 1.00 62.72  ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 250.544 242.955 228.326 1.00 62.48  ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 250.107 242.043 229.036 1.00 64.34  ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 249.759 242.613 225.972 1.00 67.32  ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 248.619 242.811 224.987 1.00 68.28  ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 247.400 241.992 225.377 1.00 67.26  ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 246.342 242.079 224.378 1.00 69.75  ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 245.462 243.069 224.303 1.00 71.52  ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 245.483 244.079 225.157 1.00 67.66  ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 244.537 243.043 223.348 1.00 69.36  ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 251.761 243.477 228.502 1.00 61.07  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 252.642 242.982 229.553 1.00 60.78  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 252.111 243.287 230.947 1.00 64.49  ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 252.480 242.596 231.903 1.00 65.44  ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 254.043 243.571 229.388 1.00 61.97  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 251.261 244.300 231.086 1.00 64.14  ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 250.654 244.649 232.365 1.00 62.31  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 249.203 244.215 232.478 1.00 59.55  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 248.775 243.789 233.553 1.00 64.08  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 250.747 246.160 232.600 1.00 62.47  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 248.431 244.316 231.393 1.00 60.16  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 247.039 243.880 231.431 1.00 65.23  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 246.936 242.370 231.606 1.00 66.95  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 246.076 241.883 232.348 1.00 68.22  ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 246.314 244.322 230.160 1.00 68.00  ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 246.614 245.697 229.891 1.00 66.50  ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 244.811 244.165 230.326 1.00 63.67  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 247.797 241.613 230.926 1.00 61.99  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 247.825 240.155 231.025 1.00 58.18  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 249.263 239.716 231.267 1.00 54.08  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 249.964 239.305 230.332 1.00 56.79  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 247.250 239.502 229.770 1.00 58.82  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 247.210 238.092 229.902 1.00 64.15  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 249.742 239.802 232.511 1.00 49.09  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 251.129 239.394 232.791 1.00 49.29  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 251.410 237.931 232.496 1.00 51.71  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 252.560 237.581 232.202 1.00 54.88  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 251.291 239.711 234.285 1.00 46.73  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 249.898 239.737 234.824 1.00 53.39  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 249.052 240.285 233.718 1.00 51.83  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 250.399 237.061 232.568 1.00 54.52  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 250.627 235.642 232.316 1.00 48.38  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 250.986 235.374 230.861 1.00 52.24  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 251.542 234.316 230.544 1.00 60.29  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 249.395 234.830 232.715 1.00 50.70  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 250.674 236.312 229.962 1.00 48.33  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 251.038 236.141 228.559 1.00 41.51  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 252.549 236.135 228.367 1.00 47.30  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 253.050 235.537 227.409 1.00 57.47  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 250.405 237.246 227.713 1.00 49.76  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 248.973 237.025 227.224 1.00 48.24  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 248.543 238.159 226.307 1.00 46.38  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 248.848 235.687 226.517 1.00 49.63  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 253.287 236.794 229.259 1.00 51.93  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 254.736 236.902 229.152 1.00 53.52  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 255.461 236.103 230.227 1.00 53.72  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 256.696 236.105 230.260 1.00 61.95  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 255.156 238.371 229.209 1.00 52.13  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 254.612 239.197 228.079 1.00 53.14  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 253.322 239.700 228.130 1.00 50.26  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 255.385 239.462 226.964 1.00 53.94  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 252.816 240.453 227.091 1.00 55.66  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 254.885 240.217 225.923 1.00 58.06  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 253.598 240.713 225.988 1.00 58.86  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 254.726 235.422 231.103 1.00 49.80  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 255.325 234.567 232.120 1.00 51.47  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 254.919 233.107 232.011 1.00 55.23  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 255.661 232.247 232.499 1.00 54.21  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 254.968 235.071 233.527 1.00 49.62  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 255.530 236.450 233.813 1.00 61.92  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 256.745 236.636 233.876 1.00 65.30  ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 254.647 237.425 233.989 1.00 62.05  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 253.781 232.796 231.394 1.00 50.98  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 253.325 231.424 231.229 1.00 46.68  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 253.290 230.964 229.781 1.00 51.75  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 253.358 229.758 229.532 1.00 55.89  ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 251.921 231.244 231.833 1.00 46.56  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 251.893 230.961 233.332 1.00 52.34  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 252.315 232.174 234.148 1.00 53.51  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 252.148 231.959 235.580 1.00 53.05  ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 252.537 232.814 236.516 1.00 60.93  ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 253.124 233.959 236.205 1.00 57.62  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 252.331 232.514 237.795 1.00 54.77  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 253.186 231.883 228.826 1.00 45.26  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 253.078 231.546 227.413 1.00 38.06  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 254.447 231.635 226.755 1.00 38.58  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 255.173 232.615 226.953 1.00 44.61  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 252.096 232.480 226.705 1.00 37.35  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 250.418 232.457 227.367 1.00 63.44  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 254.794 230.614 225.975 1.00 40.92  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 256.041 230.636 225.219 1.00 30.14  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 255.881 231.597 224.048 1.00 35.08  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 254.970 231.451 223.225 1.00 47.91  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 256.419 229.229 224.742 1.00 30.23  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 257.486 229.302 223.661 1.00 40.10  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 256.901 228.388 225.913 1.00 32.45  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 256.768 232.585 223.969 1.00 40.92  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 256.677 233.631 222.959 1.00 38.39  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 257.473 233.215 221.728 1.00 44.70  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 258.682 232.976 221.815 1.00 48.00  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 257.188 234.959 223.517 1.00 40.51  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 256.843 236.248 222.766 1.00 40.08  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 256.769 237.410 223.740 1.00 46.25  ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 257.853 236.547 221.669 1.00 45.28  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 256.794 233.130 220.588 1.00 38.22  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 257.419 232.831 219.302 1.00 33.49  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 257.150 234.011 218.374 1.00 45.26  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 256.015 234.219 217.937 1.00 48.35  ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 256.886 231.527 218.716 1.00 32.37  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 257.538 230.304 219.327 1.00 50.49  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 258.755 230.139 219.263 1.00 55.75  ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 256.729 229.437 219.922 1.00 54.60  ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 258.193 234.781 218.076 1.00 45.51  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 258.070 235.945 217.200 1.00 35.75  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 258.093 235.470 215.754 1.00 41.80  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 259.148 235.354 215.129 1.00 44.36  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 259.180 236.951 217.475 1.00 33.57  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 258.837 238.339 217.034 1.00 40.64  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 258.934 238.844 215.770 1.00 38.33  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 258.331 239.400 217.851 1.00 38.58  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 258.525 240.154 215.751 1.00 35.97  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 258.149 240.520 217.016 1.00 37.32  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 258.017 239.514 219.209 1.00 38.77  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 257.669 241.737 217.494 1.00 41.93  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 257.538 240.722 219.680 1.00 40.32  ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 257.369 241.817 218.825 1.00 40.64  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 256.905 235.181 215.218 1.00 38.43  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 256.804 234.827 213.807 1.00 34.25  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 257.203 235.999 212.920 1.00 40.39  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 257.934 235.825 211.938 1.00 48.67  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 255.382 234.368 213.477 1.00 42.17  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 255.103 232.932 213.831 1.00 40.36  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 255.692 232.344 214.939 1.00 45.44  ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 254.248 232.171 213.052 1.00 43.64  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 255.432 231.026 215.262 1.00 47.34  ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 253.985 230.853 213.370 1.00 47.77  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 254.577 230.280 214.476 1.00 48.55  ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 256.738 237.201 213.257 1.00 34.80  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 257.062 238.374 212.470 1.00 31.03  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 256.446 238.313 211.083 1.00 42.06  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 255.433 237.648 210.845 1.00 47.73  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 257.073 239.022 210.154 1.00 46.54  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 256.683 239.006 208.754 1.00 42.21  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 257.555 238.022 207.984 1.00 44.65  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 258.632 237.625 208.436 1.00 48.77  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 256.796 240.405 208.143 1.00 47.74  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 255.893 240.592 206.939 1.00 58.45  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 255.596 239.592 206.253 1.00 61.05  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 255.480 241.741 206.678 1.00 56.43  ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 257.069 237.623 206.811 1.00 44.76  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 257.835 236.727 205.956 1.00 39.47  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 259.121 237.408 205.510 1.00 41.62  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 259.089 238.505 204.945 1.00 48.73  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 257.004 236.308 204.745 1.00 45.89  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 255.905 235.343 205.064 1.00 44.00  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 255.500 234.939 206.303 1.00 42.73  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 255.069 234.655 204.126 1.00 43.91  ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 254.464 234.045 206.194 1.00 39.38  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 254.180 233.853 204.868 1.00 41.46  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 254.985 234.641 202.730 1.00 41.88  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 253.220 233.046 204.262 1.00 42.95  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 254.031 233.839 202.131 1.00 40.66  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 253.162 233.053 202.896 1.00 38.45  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 260.251 236.755 205.764 1.00 40.44  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 261.541 237.315 205.398 1.00 48.35  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 261.720 237.273 203.881 1.00 48.68  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 260.889 236.742 203.140 1.00 52.38  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 262.666 236.561 206.103 1.00 50.58  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 262.562 235.166 205.881 1.00 50.27  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 262.829 237.851 203.416 1.00 46.26  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 263.131 237.824 201.989 1.00 42.11  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 263.301 236.392 201.497 1.00 47.02  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 262.852 236.046 200.397 1.00 53.31  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 264.387 238.648 201.704 1.00 47.81  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 264.141 240.021 202.034 1.00 57.52  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 264.765 238.556 200.237 1.00 52.74  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 263.940 235.543 202.304 1.00 53.04  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 264.050 234.130 201.957 1.00 49.12  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 262.678 233.471 201.893 1.00 49.56  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 262.412 232.658 201.000 1.00 52.46  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 264.946 233.412 202.966 1.00 53.39  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 265.164 231.939 202.669 1.00 59.93  ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 266.522 231.448 203.130 1.00 62.92  ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 266.647 231.068 204.313 1.00 59.57  ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 267.464 231.443 202.311 1.00 61.26  ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 261.795 233.804 202.838 1.00 46.40  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 260.447 233.248 202.821 1.00 39.01  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 259.679 233.698 201.585 1.00 44.47  ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 258.982 232.896 200.952 1.00 48.12  ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 259.698 233.645 204.092 1.00 43.76  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 259.790 234.980 201.227 1.00 45.43  ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 259.125 235.472 200.025 1.00 39.69  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 259.694 234.819 198.773 1.00 40.86  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 258.948 234.478 197.847 1.00 47.65  ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 259.249 236.993 199.940 1.00 32.46  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 258.605 237.802 201.067 1.00 36.81  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 258.798 239.290 200.830 1.00 41.02  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 257.129 237.463 201.196 1.00 37.02  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 261.017 234.646 198.721 1.00 41.42  ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 261.637 234.016 197.560 1.00 36.37  ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 261.203 232.562 197.419 1.00 46.63  ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 260.913 232.099 196.309 1.00 54.65  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 263.159 234.115 197.665 1.00 42.04  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 263.898 233.511 196.492 1.00 48.39  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 264.136 234.251 195.342 1.00 47.78  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 264.363 232.203 196.537 1.00 51.05  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 264.810 233.704 194.268 1.00 45.36  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 265.038 231.648 195.468 1.00 48.48  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 265.259 232.403 194.337 1.00 48.35  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 265.933 231.854 193.271 1.00 57.84  ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 261.158 231.825 198.531 1.00 45.21  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 260.793 230.413 198.468 1.00 43.87  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 259.340 230.230 198.047 1.00 48.67  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 259.022 229.309 197.285 1.00 52.09  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 261.053 229.744 199.817 1.00 45.20  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 262.525 229.517 200.117 1.00 48.58  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 262.745 228.695 201.369 1.00 54.99  ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 263.427 229.127 202.298 1.00 53.94  ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 262.167 227.500 201.401 1.00 52.20  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 258.443 231.087 198.539 1.00 43.03  ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 257.040 231.000 198.145 1.00 36.94  ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 256.885 231.297 196.659 1.00 44.35  ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 256.150 230.605 195.944 1.00 46.72  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 256.182 231.944 199.007 1.00 43.38  ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 254.770 232.035 198.456 1.00 48.50  ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 256.156 231.466 200.445 1.00 41.74  ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 257.575 232.329 196.170 1.00 48.53  ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 257.510 232.643 194.753 1.00 37.63  ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 258.134 231.568 193.885 1.00 44.28  ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 257.605 231.229 192.824 1.00 53.62  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 259.270 231.020 194.321 1.00 45.48  ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 259.931 229.967 193.554 1.00 46.84  ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 259.065 228.715 193.479 1.00 50.62  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 258.970 228.074 192.426 1.00 57.07  ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 261.291 229.644 194.174 1.00 48.35  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 262.305 229.082 193.194 1.00 48.76  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 262.765 230.137 192.204 1.00 58.24  ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 264.053 229.719 191.514 1.00 56.86  ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 263.974 228.327 190.993 1.00 58.16  ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 258.430 228.348 194.593 1.00 54.53  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 257.599 227.149 194.614 1.00 51.31  ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 256.344 227.330 193.770 1.00 54.15  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 255.961 226.436 193.006 1.00 59.56  ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 257.232 226.792 196.056 1.00 51.91  ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 256.602 225.415 196.226 1.00 58.36  ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 257.495 224.284 195.747 1.00 66.74  ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 258.734 224.450 195.752 1.00 63.69  ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 256.955 223.225 195.366 1.00 66.70  ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 255.685 228.484 193.897 1.00 47.95  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 254.416 228.683 193.206 1.00 48.58  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 254.624 228.851 191.705 1.00 53.91  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 253.888 228.264 190.902 1.00 57.67  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 253.683 229.888 193.802 1.00 47.74  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 252.244 230.007 193.371 1.00 53.20  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 251.909 230.338 192.068 1.00 62.55  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 251.225 229.819 194.289 1.00 47.17  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 250.589 230.448 191.683 1.00 60.91  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 249.904 229.927 193.908 1.00 51.77  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 249.587 230.244 192.603 1.00 57.05  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 255.622 229.636 191.304 1.00 56.00  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 255.875 229.877 189.889 1.00 54.85  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 256.640 228.744 189.218 1.00 55.60  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 257.099 228.918 188.084 1.00 59.51  ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 256.640 231.191 189.703 1.00 58.69  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 257.923 231.095 190.334 1.00 62.98  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 255.863 232.351 190.311 1.00 50.17  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 256.795 227.599 189.887 1.00 59.94  ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 257.465 226.463 189.262 1.00 56.27  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 256.658 225.924 188.088 1.00 56.83  ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 257.226 225.549 187.055 1.00 58.66  ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 257.712 225.366 190.298 1.00 53.32  ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 256.495 224.914 190.865 1.00 58.02  ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 255.330 225.874 188.227 1.00 60.33  ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 254.487 225.415 187.126 1.00 60.32  ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 254.560 226.371 185.942 1.00 65.03  ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 254.369 225.962 184.791 1.00 64.06  ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 253.041 225.255 187.598 1.00 62.93  ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 252.351 226.564 187.951 1.00 69.47  ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 250.929 226.332 188.431 1.00 70.83  ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 250.258 227.639 188.818 1.00 67.49  ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 250.049 228.516 187.634 1.00 67.04  ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 254.825 227.648 186.206 1.00 66.78  ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 254.965 228.626 185.138 1.00 57.92  ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 256.200 228.321 184.301 1.00 64.37  ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 257.181 227.751 184.786 1.00 69.08  ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 255.060 230.034 185.723 1.00 58.03  ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 253.789 230.509 186.404 1.00 59.64  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 253.989 232.136 187.149 1.00 68.36  ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 254.091 233.155 185.685 1.00 55.95  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 256.141 228.695 183.022 1.00 71.49  ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 257.255 228.438 182.118 1.00 73.43  ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 258.505 229.171 182.588 1.00 76.21  ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 259.470 228.537 183.026 1.00 77.22  ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 256.892 228.858 180.692 1.00 70.85  ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 257.901 228.381 179.667 1.00 77.83  ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 258.775 227.563 180.024 1.00 78.24  ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 257.821 228.824 178.503 1.00 77.74  ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 258.479 230.505 182.526 1.00 65.92  ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 259.559 231.359 183.034 1.00 65.45  ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 260.938 230.904 182.557 1.00 62.16  ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 261.948 231.142 183.223 1.00 66.79  ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 259.522 231.436 184.562 1.00 65.00  ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 258.252 232.013 185.192 1.00 63.37  ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 258.509 232.413 186.636 1.00 63.88  ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 257.739 233.200 184.390 1.00 61.78  ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 260.996 230.249 181.401 1.00 73.49  ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 262.241 229.718 180.859 1.00 76.46  ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 262.643 230.541 179.644 1.00 79.45  ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 261.854 230.699 178.707 1.00 82.16  ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 262.095 228.241 180.487 1.00 76.31  ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 262.070 227.296 181.680 1.00 77.92  ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 263.420 227.167 182.361 1.00 82.17  ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 264.439 227.556 181.752 1.00 81.59  ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 263.462 226.677 183.509 1.00 81.15  ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 263.870 231.060 179.665 1.00 80.58  ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 264.389 231.890 178.581 1.00 84.31  ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 265.876 231.605 178.437 1.00 84.91  ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 266.713 232.236 179.097 1.00 82.66  ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 264.128 233.374 178.844 1.00 80.34  ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 264.521 234.293 177.705 1.00 78.53  ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 264.146 235.733 178.012 1.00 79.86  ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 264.546 236.662 176.880 1.00 82.95  ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 264.190 238.076 177.177 1.00 81.30  ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 266.244 230.643 177.586 1.00 90.31  ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 267.664 230.277 177.456 1.00 89.48  ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 268.552 231.408 176.968 1.00 90.87  ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 269.748 231.414 177.285 1.00 88.09  ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 267.637 229.116 176.452 1.00 87.91  ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 266.356 229.290 175.701 1.00 86.70  ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 265.382 229.860 176.686 1.00 86.62  ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 268.015 232.362 176.213 1.00 88.15  ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 268.803 233.464 175.679 1.00 85.69  ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 268.831 234.677 176.599 1.00 87.24  ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 269.307 235.737 176.182 1.00 88.64  ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 268.277 233.872 174.298 1.00 86.51  ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 267.040 234.744 174.379 1.00 89.85  ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 265.991 234.311 174.856 1.00 90.55  ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 267.156 235.981 173.912 1.00 86.78  ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 268.328 234.553 177.825 1.00 77.29  ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 268.349 235.661 178.771 1.00 74.49  ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 269.783 236.055 179.108 1.00 75.99  ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 270.627 235.198 179.387 1.00 76.17  ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 267.589 235.269 180.039 1.00 71.37  ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 267.805 236.188 181.220 1.00 72.93  ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 267.197 237.434 181.278 1.00 73.97  ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 268.607 235.800 182.286 1.00 72.39  ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 267.389 238.273 182.360 1.00 72.69  ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 268.804 236.632 183.371 1.00 72.71  ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 268.194 237.866 183.403 1.00 70.83  ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 268.388 238.697 184.482 1.00 69.86  ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 270.057 237.358 179.083 1.00 73.60  ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 271.376 237.899 179.395 1.00 74.24  ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 271.330 238.469 180.805 1.00 74.71  ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 270.477 239.309 181.115 1.00 75.55  ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 271.817 238.979 178.391 1.00 79.30  ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 271.957 238.412 176.976 1.00 77.89  ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 273.126 239.616 178.836 1.00 75.07  ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 270.696 238.495 176.148 1.00 73.62  ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 272.246 238.017 181.655 1.00 84.32  ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 272.361 238.541 183.013 1.00 85.71  ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 272.990 239.927 182.948 1.00 88.02  ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 274.095 240.080 182.406 1.00 89.20  ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 273.182 237.600 183.909 1.00 84.58  ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 273.350 238.204 185.294 1.00 83.44  ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 272.518 236.236 183.993 1.00 84.29  ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 272.333 240.957 183.474 1.00 89.01  ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 272.928 242.297 183.455 1.00 90.14  ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 274.160 242.373 184.342 1.00 90.08  ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 274.318 241.607 185.295 1.00 91.54  ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 271.803 243.194 183.987 1.00 86.66  ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 270.931 242.276 184.775 1.00 84.17  ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 270.989 240.953 184.076 1.00 84.14  ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 275.047 243.312 184.003 1.00 103.73 ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 276.283 243.472 184.764 1.00 105.50 ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 275.996 243.834 186.216 1.00 105.97 ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 276.602 243.271 187.135 1.00 104.19 ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 277.168 244.532 184.111 1.00 106.69 ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 277.724 244.084 182.774 1.00 108.11 ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 277.916 242.864 182.587 1.00 106.82 ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 277.969 244.952 181.910 1.00 107.12 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 275.076 244.768 186.442 1.00 108.20 ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 274.641 245.141 187.785 1.00 108.49 ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 273.264 244.523 188.012 1.00 108.59 ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 272.230 245.157 187.800 1.00 107.40 ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 274.619 246.663 187.960 1.00 108.19 ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 274.175 247.108 189.336 1.00 110.99 ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 274.968 246.873 190.451 1.00 108.60 ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 272.963 247.761 189.519 1.00 111.18 ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 274.567 247.276 191.711 1.00 108.17 ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 272.554 248.168 190.776 1.00 109.74 ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 273.359 247.923 191.867 1.00 109.49 ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 272.956 248.326 193.120 1.00 108.40 ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 273.261 243.269 188.445 1.00 102.51 ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 272.014 242.574 188.733 1.00 102.69 ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 271.411 243.111 190.024 1.00 103.99 ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 272.064 243.048 191.072 1.00 103.26 ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 272.256 241.074 188.852 1.00 100.97 ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 270.991 240.242 189.001 1.00 101.12 ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 269.924 240.274 187.550 1.00 106.82 ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 268.343 239.867 188.287 1.00 99.57  ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 270.188 243.642 190.000 1.00 92.48  ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 269.557 244.075 191.252 1.00 90.31  ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 269.164 242.876 192.094 1.00 93.38  ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 268.186 242.187 191.786 1.00 94.78  ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 268.327 244.864 190.781 1.00 88.34  ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 268.537 245.098 189.312 1.00 89.24  ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 269.350 243.943 188.831 1.00 88.44  ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 269.913 242.618 193.158 1.00 85.37  ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 269.731 241.425 193.974 1.00 85.30  ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 268.958 241.822 195.225 1.00 85.64  ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 269.338 242.754 195.946 1.00 84.49  ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 271.071 240.744 194.303 1.00 85.00  ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 271.963 241.627 195.173 1.00 84.64  ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 270.831 239.399 194.965 1.00 81.97  ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 267.832 241.147 195.450 1.00 69.60  ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 267.047 241.373 196.657 1.00 66.95  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 267.239 240.225 197.637 1.00 68.82  ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 267.402 240.440 198.843 1.00 70.24  ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 265.566 241.572 196.291 1.00 63.74  ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 264.734 241.752 197.542 1.00 66.38  ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 265.409 242.766 195.363 1.00 64.02  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 267.225 238.993 197.135 1.00 65.99  ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 267.477 237.807 197.943 1.00 66.26  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 268.986 237.601 198.020 1.00 65.60  ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 269.627 237.284 197.014 1.00 68.43  ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 266.769 236.597 197.339 1.00 63.31  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 267.003 235.296 198.068 1.00 61.28  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 266.831 235.207 199.442 1.00 59.95  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 267.375 234.151 197.378 1.00 64.28  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 267.038 234.016 200.110 1.00 63.60  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 267.582 232.956 198.037 1.00 62.93  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 267.410 232.894 199.402 1.00 67.08  ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 267.618 231.706 200.063 1.00 67.81  ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 269.551 237.785 199.217 1.00 71.03  ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 271.004 237.793 199.364 1.00 71.86  ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 271.621 236.456 198.967 1.00 74.10  ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 272.790 236.399 198.568 1.00 77.07  ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 271.382 238.154 200.800 1.00 73.72  ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 271.062 239.596 201.140 1.00 77.74  ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 271.083 240.443 200.222 1.00 74.95  ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 270.789 239.883 202.324 1.00 78.91  ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 270.856 235.373 199.068 1.00 72.68  ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 271.342 234.048 198.712 1.00 70.15  ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 271.011 233.664 197.274 1.00 71.81  ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 271.134 232.488 196.917 1.00 72.82  ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 270.777 233.002 199.675 1.00 71.34  ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 271.176 233.219 201.125 1.00 71.75  ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 272.670 233.028 201.320 1.00 73.29  ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 273.053 233.128 202.787 1.00 74.48  ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 272.910 234.517 203.304 1.00 76.22  ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 270.589 234.619 196.452 1.00 76.55  ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 270.318 234.334 195.051 1.00 78.10  ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 271.612 233.933 194.348 1.00 78.75  ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 272.667 234.522 194.622 1.00 75.75  ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 269.702 235.556 194.368 1.00 73.83  ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 269.251 235.420 192.912 1.00 71.42  ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 267.941 234.657 192.822 1.00 68.56  ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 269.122 236.788 192.261 1.00 72.68  ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 271.583 232.936 193.464 1.00 79.14  ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 272.806 232.535 192.761 1.00 80.08  ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 273.400 233.687 191.962 1.00 82.81  ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 272.680 234.505 191.385 1.00 81.72  ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 272.329 231.402 191.848 1.00 76.70  ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 271.149 230.833 192.557 1.00 76.67  ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 270.470 232.004 193.212 1.00 75.72  ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 274.732 233.749 191.943 1.00 93.52  ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 275.417 234.835 191.245 1.00 93.52  ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 275.120 234.865 189.750 1.00 96.78  ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 274.929 235.969 189.211 1.00 97.76  ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 276.923 234.757 191.523 1.00 93.63  ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 277.275 234.568 192.990 1.00 96.88  ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 276.613 235.595 193.886 1.00 97.98  ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 276.816 236.799 193.725 1.00 95.96  ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 275.817 235.125 194.839 1.00 95.35  ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 275.143 233.752 189.014 1.00 93.36  ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 274.612 233.755 187.643 1.00 89.15  ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 273.152 233.334 187.610 1.00 91.19  ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 272.848 232.170 187.306 1.00 88.38  ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 275.505 232.737 186.923 1.00 88.62  ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 275.893 231.763 187.994 1.00 90.31  ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 275.764 232.452 189.339 1.00 89.87  ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 272.217 234.232 187.911 1.00 84.41  ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 270.815 233.821 188.002 1.00 81.41  ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 270.228 233.495 186.638 1.00 78.44  ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 270.663 234.004 185.603 1.00 79.09  ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 270.134 235.050 188.613 1.00 78.46  ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 270.917 236.189 188.064 1.00 80.91  ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 272.338 235.700 187.851 1.00 81.97  ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 269.223 232.625 186.652 1.00 66.21  ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 268.496 232.283 185.442 1.00 68.03  ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 267.309 233.229 185.272 1.00 68.52  ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 267.087 234.139 186.073 1.00 72.39  ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 268.046 230.824 185.481 1.00 65.06  ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 267.042 230.624 186.460 1.00 64.83  ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 266.537 233.018 184.203 1.00 58.62  ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 265.365 233.856 183.972 1.00 59.73  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 264.325 233.669 185.069 1.00 62.65  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 263.720 234.644 185.529 1.00 67.51  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 264.760 233.552 182.602 1.00 62.10  ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 263.651 234.479 182.215 1.00 59.17  ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 263.835 235.837 182.065 1.00 57.76  ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 262.344 234.245 181.950 1.00 57.47  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 262.689 236.399 181.723 1.00 57.27  ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 261.768 235.455 181.647 1.00 58.47  ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 264.102 232.424 185.499 1.00 56.10  ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 263.121 232.170 186.549 1.00 55.02  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 263.539 232.810 187.867 1.00 59.32  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 262.712 233.409 188.563 1.00 66.50  ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 262.915 230.666 186.724 1.00 53.62  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 261.714 230.306 187.582 1.00 59.43  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 261.631 228.809 187.818 1.00 55.08  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 261.371 228.077 186.585 1.00 57.25  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 260.165 227.877 186.073 1.00 58.34  ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 259.077 228.341 186.666 1.00 58.24  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 260.046 227.193 184.939 1.00 57.79  ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 264.821 232.696 188.225 1.00 56.43  ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 265.292 233.288 189.474 1.00 53.31  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 265.221 234.808 189.424 1.00 55.82  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 264.941 235.458 190.439 1.00 56.76  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 266.717 232.823 189.770 1.00 56.54  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 266.919 231.325 189.629 1.00 59.93  ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 268.018 230.796 190.528 1.00 65.60  ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 267.820 230.774 191.760 1.00 64.13  ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 269.080 230.402 190.001 1.00 70.05  ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 265.481 235.395 188.254 1.00 51.89  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 265.352 236.841 188.107 1.00 44.72  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 263.904 237.285 188.272 1.00 50.77  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 263.633 238.343 188.851 1.00 51.84  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 265.900 237.282 186.751 1.00 48.39  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 262.960 236.493 187.758 1.00 49.74  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 261.546 236.830 187.896 1.00 39.01  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 261.127 236.791 189.361 1.00 44.97  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 260.442 237.698 189.850 1.00 52.13  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 260.685 235.888 187.035 1.00 43.17  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 260.890 236.185 185.548 1.00 44.75  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 259.216 236.010 187.410 1.00 48.42  ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 260.222 237.459 185.081 1.00 48.64  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 261.534 235.746 190.085 1.00 46.90  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 261.173 235.635 191.495 1.00 43.27  ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 261.835 236.742 192.305 1.00 44.65  ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 261.251 237.263 193.263 1.00 49.24  ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 261.536 234.239 192.033 1.00 40.51  ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 261.086 234.091 193.476 1.00 45.36  ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 260.902 233.162 191.171 1.00 38.61  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 263.061 237.121 191.936 1.00 49.12  ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 263.716 238.245 192.597 1.00 42.83  ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 262.928 239.532 192.396 1.00 45.70  ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 262.802 240.344 193.321 1.00 49.26  ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 265.144 238.401 192.074 1.00 45.38  ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 266.019 239.214 193.005 1.00 53.55  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 266.269 238.819 194.144 1.00 57.80  ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 266.489 240.359 192.525 1.00 56.80  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 262.393 239.739 191.191 1.00 49.21  ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 261.545 240.901 190.947 1.00 44.01  ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 260.245 240.807 191.737 1.00 45.29  ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 259.711 241.826 192.190 1.00 53.03  ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 261.258 241.038 189.453 1.00 44.49  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 262.459 241.177 188.714 1.00 42.70  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 259.716 239.593 191.903 1.00 40.21  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 258.505 239.412 192.697 1.00 35.56  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 258.738 239.808 194.150 1.00 45.82  ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 257.891 240.460 194.773 1.00 50.66  ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 258.027 237.962 192.602 1.00 36.72  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 257.448 237.470 190.962 1.00 50.37  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 259.884 239.415 194.710 1.00 48.26  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 260.222 239.815 196.074 1.00 36.29  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 260.433 241.321 196.148 1.00 42.32  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 260.031 241.974 197.119 1.00 47.27  ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 261.461 239.042 196.565 1.00 34.21  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 261.833 239.469 197.975 1.00 45.17  ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 261.207 237.546 196.509 1.00 38.93  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 261.067 241.896 195.123 1.00 41.40  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 261.294 243.338 195.099 1.00 38.73  ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 259.980 244.107 195.069 1.00 41.92  ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 259.841 245.136 195.740 1.00 51.29  ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 262.160 243.710 193.896 1.00 42.58  ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 262.382 245.188 193.741 1.00 49.44  ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 263.353 245.838 194.483 1.00 50.55  ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 261.623 245.926 192.847 1.00 46.88  ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 263.560 247.196 194.342 1.00 45.91  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 261.825 247.284 192.702 1.00 44.99  ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 262.795 247.920 193.449 1.00 46.83  ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 259.007 243.624 194.294 1.00 37.34  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 257.724 244.315 194.184 1.00 33.63  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 257.034 244.371 195.541 1.00 34.95  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 256.473 245.401 195.933 1.00 42.25  ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 256.838 243.631 193.126 1.00 31.15  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 255.382 244.015 193.318 1.00 29.00  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 257.308 243.996 191.727 1.00 32.91  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 257.071 243.261 196.282 1.00 32.79  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 256.431 243.221 197.592 1.00 30.25  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 257.083 244.205 198.558 1.00 38.89  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 256.392 244.873 199.336 1.00 46.13  ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 256.482 241.800 198.151 1.00 25.99  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 255.664 241.606 199.390 1.00 34.98  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 254.290 241.508 199.365 1.00 42.13  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 256.026 241.486 200.689 1.00 30.37  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 253.840 241.338 200.595 1.00 36.69  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 254.873 241.321 201.417 1.00 29.22  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 258.414 244.310 198.522 1.00 46.10  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 259.121 245.197 199.440 1.00 39.70  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 258.888 246.671 199.130 1.00 43.46  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 258.867 247.492 200.053 1.00 52.73  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 260.620 244.899 199.422 1.00 37.79  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 261.027 243.718 200.285 1.00 47.70  ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 262.387 243.174 199.908 1.00 53.42  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 263.173 243.853 199.249 1.00 52.41  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 262.671 241.945 200.321 1.00 44.40  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 258.735 247.031 197.852 1.00 34.47  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 258.502 248.431 197.507 1.00 36.78  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 257.205 248.952 198.109 1.00 41.31  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 257.043 250.166 198.276 1.00 47.34  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 258.484 248.615 195.989 1.00 39.72  ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 257.485 247.765 195.411 1.00 43.05  ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 259.841 248.288 195.396 1.00 42.91  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 256.270 248.058 198.434 1.00 41.04  ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 255.054 248.481 199.117 1.00 38.38  ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 255.350 248.891 200.554 1.00 43.21  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 254.657 249.744 201.121 1.00 51.01  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 254.014 247.362 199.080 1.00 44.51  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 253.053 247.372 197.890 1.00 38.43  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 252.249 248.655 197.883 1.00 32.89  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 253.786 247.188 196.570 1.00 39.13  ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 256.372 248.285 201.161 1.00 45.69  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 256.737 248.641 202.528 1.00 41.44  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 257.342 250.038 202.587 1.00 45.35  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 256.999 250.835 203.468 1.00 48.01  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 257.708 247.605 203.091 1.00 41.85  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 257.061 246.300 203.436 1.00 46.99  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 256.145 246.169 204.458 1.00 48.91  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 257.190 245.070 202.887 1.00 41.76  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 255.742 244.913 204.526 1.00 46.57  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 256.361 244.225 203.583 1.00 42.32  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 258.247 250.352 201.656 1.00 50.19  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 258.802 251.700 201.589 1.00 50.27  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 257.747 252.711 201.159 1.00 52.82  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 257.764 253.865 201.603 1.00 62.27  ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 260.001 251.736 200.639 1.00 49.26  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 261.264 251.067 201.174 1.00 53.06  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 261.144 249.560 201.280 1.00 59.58  ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 260.925 248.873 200.282 1.00 61.81  ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 261.284 249.038 202.492 1.00 54.81  ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 256.825 252.299 200.284 1.00 45.80  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 255.740 253.188 199.882 1.00 43.55  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 254.849 253.540 201.066 1.00 48.61  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 254.435 254.696 201.217 1.00 58.61  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 254.919 252.547 198.764 1.00 44.08  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 254.538 252.557 201.913 1.00 49.04  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 253.777 252.836 203.126 1.00 51.95  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 254.575 253.719 204.077 1.00 59.94  ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 254.019 254.608 204.733 1.00 63.35  ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 253.379 251.527 203.809 1.00 53.57  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 252.050 250.992 203.314 1.00 56.42  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 251.400 251.601 202.465 1.00 58.07  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 251.637 249.848 203.847 1.00 56.64  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 255.885 253.481 204.169 1.00 65.40  ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 256.732 254.302 205.027 1.00 61.50  ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 256.765 255.750 204.552 1.00 61.85  ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 256.734 256.679 205.368 1.00 70.73  ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 258.145 253.721 205.082 1.00 58.99  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 256.838 255.961 203.236 1.00 62.30  ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 256.847 257.319 202.701 1.00 67.80  ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 255.527 258.028 202.982 1.00 71.71  ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 255.505 259.220 203.311 1.00 76.26  ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 257.140 257.289 201.201 1.00 71.09  ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 258.588 256.967 200.865 1.00 70.11  ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 258.814 256.901 199.364 1.00 72.02  ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 258.427 258.138 198.696 1.00 74.94  ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 258.127 258.231 197.407 1.00 76.61  ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 258.155 257.174 196.613 1.00 75.02  ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 257.791 259.415 196.904 1.00 71.95  ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 254.409 257.308 202.849 1.00 67.76  ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 253.110 257.891 203.171 1.00 69.03  ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 253.008 258.231 204.653 1.00 69.74  ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 252.425 259.257 205.023 1.00 76.53  ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 251.989 256.935 202.765 1.00 72.68  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 251.707 256.773 201.272 1.00 70.43  ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 250.640 255.717 201.048 1.00 69.96  ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 251.268 258.101 200.685 1.00 69.27  ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 253.559 257.375 205.516 1.00 69.34  ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 253.504 257.624 206.953 1.00 73.67  ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 254.257 258.897 207.321 1.00 79.55  ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 253.810 259.673 208.173 1.00 81.10  ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 254.065 256.424 207.714 1.00 72.28  ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 255.411 259.124 206.688 1.00 86.45  ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 256.202 260.312 206.993 1.00 84.44  ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 255.473 261.592 206.606 1.00 85.89  ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 255.663 262.632 207.247 1.00 87.45  ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 257.555 260.238 206.286 1.00 82.67  ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 258.478 259.160 206.828 1.00 84.48  ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 259.772 259.093 206.036 1.00 86.70  ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 260.641 260.311 206.300 1.00 85.95  ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 261.159 260.330 207.697 1.00 83.82  ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 254.640 261.542 205.569 1.00 82.33  ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 253.866 262.696 205.135 1.00 83.01  ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 252.503 262.776 205.809 1.00 85.70  ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 251.629 263.505 205.328 1.00 85.76  ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 253.695 262.675 203.613 1.00 80.13  ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 254.993 262.867 202.844 1.00 82.39  ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 254.769 262.815 201.341 1.00 86.23  ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 254.371 261.490 200.882 1.00 87.19  ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 253.987 261.212 199.644 1.00 85.89  ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 253.928 262.149 198.712 1.00 86.05  ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 253.657 259.962 199.332 1.00 85.82  ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 252.303 262.048 206.905 1.00 85.81  ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 251.020 262.054 207.586 1.00 86.61  ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 249.890 261.473 206.769 1.00 87.52  ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 248.748 261.930 206.885 1.00 85.06  ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 250.177 260.471 205.945 1.00 85.50  ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 249.176 259.859 205.087 1.00 82.86  ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 248.707 258.528 205.647 1.00 82.25  ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 249.462 257.821 206.316 1.00 80.11  ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 247.448 258.200 205.369 1.00 73.94  ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 246.887 256.940 205.831 1.00 72.22  ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 247.481 255.773 205.052 1.00 73.51  ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 247.653 255.840 203.832 1.00 72.44  ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 245.364 256.961 205.693 1.00 67.83  ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 244.643 257.326 206.981 1.00 67.58  ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 243.166 257.603 206.750 1.00 73.64  ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 242.944 258.585 205.696 1.00 75.98  ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 242.876 259.893 205.900 1.00 76.97  ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 243.025 260.413 207.107 1.00 74.51  ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 242.653 260.701 204.867 1.00 72.87  ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 247.799 254.698 205.770 1.00 61.78  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 248.437 253.527 205.191 1.00 61.41  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 247.674 252.274 205.593 1.00 61.22  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 247.038 252.218 206.649 1.00 63.67  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 249.902 253.396 205.636 1.00 64.70  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 249.961 253.291 207.064 1.00 64.35  ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 250.709 254.603 205.193 1.00 64.73  ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 247.749 251.263 204.733 1.00 54.87  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 247.184 249.950 205.001 1.00 55.44  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 248.312 248.937 205.121 1.00 55.51  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 249.300 249.003 204.383 1.00 61.07  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 246.204 249.527 203.903 1.00 55.45  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 244.962 250.398 203.817 1.00 59.37  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 243.953 250.300 205.308 1.00 71.35  ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 242.746 251.581 204.988 1.00 55.07  ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 248.162 248.007 206.060 1.00 38.65  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 249.214 247.041 206.336 1.00 42.88  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 249.446 246.126 205.140 1.00 45.03  ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 248.500 245.639 204.515 1.00 44.66  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 248.860 246.211 207.569 1.00 47.11  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 250.717 245.894 204.827 1.00 45.54  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 251.118 244.972 203.772 1.00 38.98  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 251.411 243.626 204.418 1.00 45.37  ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 252.294 243.519 205.278 1.00 45.51  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 252.337 245.495 202.997 1.00 34.70  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 252.011 246.833 202.332 1.00 42.35  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 252.782 244.480 201.957 1.00 39.16  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 250.860 246.763 201.354 1.00 38.68  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 250.676 242.604 204.006 1.00 44.85  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 250.706 241.285 204.612 1.00 38.64  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 251.172 240.247 203.600 1.00 43.84  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 251.147 240.494 202.388 1.00 45.65  ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 249.315 240.908 205.142 1.00 31.63  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 248.386 240.846 204.054 1.00 44.78  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 248.838 241.938 206.153 1.00 35.44  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 251.625 239.077 204.061 1.00 42.47  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 251.987 238.011 203.114 1.00 31.66  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 250.840 237.579 202.221 1.00 39.88  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 251.090 237.036 201.138 1.00 49.15  ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 252.442 236.869 204.031 1.00 31.59  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 252.916 237.552 205.262 1.00 34.14  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 252.009 238.734 205.442 1.00 38.51  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 249.589 237.794 202.639 1.00 37.16  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 248.460 237.503 201.764 1.00 30.27  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 248.473 238.388 200.525 1.00 38.92  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 247.972 237.986 199.470 1.00 46.23  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 247.147 237.667 202.529 1.00 31.33  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 246.958 236.653 203.645 1.00 40.88  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 245.512 236.584 204.102 1.00 45.66  ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 244.626 236.100 203.050 1.00 35.17  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 243.325 235.894 203.203 1.00 40.35  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 242.723 236.115 204.360 1.00 37.60  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 242.611 235.454 202.171 1.00 40.33  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 249.032 239.597 200.635 1.00 36.66  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 249.243 240.423 199.450 1.00 20.53  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 250.214 239.753 198.488 1.00 29.19  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 249.997 239.754 197.270 1.00 34.98  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 249.763 241.803 199.852 1.00 31.38  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 248.739 242.673 200.510 1.00 36.44  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 248.187 242.376 201.737 1.00 40.05  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 248.172 243.837 200.114 1.00 36.18  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 247.321 243.318 202.068 1.00 39.69  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 247.293 244.216 201.099 1.00 47.12  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 251.298 239.181 199.018 1.00 36.97  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 252.254 238.468 198.177 1.00 23.10  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 251.613 237.251 197.524 1.00 30.50  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 251.866 236.962 196.349 1.00 41.96  ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 253.470 238.054 199.005 1.00 30.34  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 254.605 237.482 198.188 1.00 31.88  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 255.375 238.295 197.366 1.00 29.00  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 254.908 236.129 198.240 1.00 34.71  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 256.413 237.775 196.619 1.00 29.16  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 255.944 235.600 197.497 1.00 32.61  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 256.694 236.427 196.688 1.00 30.21  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 257.726 235.904 195.946 1.00 35.18  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 250.785 236.520 198.275 1.00 34.72  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 250.103 235.360 197.711 1.00 25.85  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 249.146 235.769 196.599 1.00 32.22  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 249.051 235.090 195.571 1.00 38.85  ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 249.359 234.604 198.810 1.00 27.22  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 250.231 234.029 199.926 1.00 29.91  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 249.373 233.621 201.112 1.00 42.67  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 251.046 232.851 199.417 1.00 25.95  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 248.426 236.877 196.787 1.00 37.17  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 247.548 237.372 195.731 1.00 34.36  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 248.348 237.799 194.508 1.00 43.40  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 247.902 237.615 193.369 1.00 47.25  ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 246.705 238.535 196.251 1.00 35.28  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 245.423 238.075 196.911 1.00 56.01  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 245.304 236.866 197.204 1.00 61.18  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 244.532 238.921 197.135 1.00 58.13  ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 249.529 238.381 194.725 1.00 42.27  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 250.355 238.835 193.610 1.00 19.54  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 250.798 237.663 192.741 1.00 30.38  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 250.763 237.742 191.508 1.00 43.01  ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 251.561 239.609 194.145 1.00 24.19  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 252.640 239.846 193.126 1.00 27.96  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 252.340 240.388 191.887 1.00 37.25  ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 253.958 239.533 193.411 1.00 30.36  ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 253.332 240.607 190.952 1.00 33.18  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 254.952 239.751 192.480 1.00 34.29  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 254.639 240.288 191.249 1.00 31.44  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 251.212 236.559 193.367 1.00 31.91  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 251.676 235.412 192.592 1.00 28.52  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 250.494 234.620 192.044 1.00 38.49  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 250.602 233.966 190.999 1.00 45.06  ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 252.615 234.530 193.435 1.00 32.10  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 251.943 234.119 194.744 1.00 43.25  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 253.920 235.260 193.710 1.00 29.29  ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 252.852 233.365 195.681 1.00 36.65  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 249.353 234.652 192.739 1.00 32.18  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 248.139 234.070 192.174 1.00 28.56  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 247.724 234.804 190.906 1.00 42.93  ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 247.384 234.176 189.897 1.00 49.96  ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 247.004 234.101 193.197 1.00 40.04  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 247.220 233.138 194.347 1.00 54.93  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 247.655 232.007 194.151 1.00 52.29  ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 246.914 233.587 195.558 1.00 53.02  ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 247.749 236.138 190.939 1.00 39.05  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 247.411 236.917 189.752 1.00 28.96  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 248.451 236.729 188.657 1.00 33.25  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 248.110 236.660 187.471 1.00 51.33  ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 247.278 238.395 190.117 1.00 32.69  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 246.019 238.725 190.855 1.00 32.67  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 246.005 239.515 191.985 1.00 36.30  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 244.732 238.376 190.623 1.00 38.71  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 244.763 239.636 192.418 1.00 38.62  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 243.971 238.955 191.609 1.00 41.25  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 249.728 236.644 189.036 1.00 36.02  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 250.794 236.510 188.049 1.00 32.61  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 250.695 235.179 187.314 1.00 36.99  ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 250.972 235.098 186.112 1.00 53.06  ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 252.153 236.668 188.734 1.00 29.19  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 253.344 236.579 187.808 1.00 35.01  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 253.339 237.216 186.575 1.00 42.13  ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 254.488 235.887 188.183 1.00 43.12  ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 254.430 237.144 185.730 1.00 42.86  ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 255.585 235.815 187.347 1.00 44.15  ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 255.550 236.444 186.122 1.00 43.99  ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 256.638 236.374 185.284 1.00 53.88  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 250.298 234.122 188.023 1.00 34.44  ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 250.128 232.823 187.380 1.00 34.43  ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 248.890 232.808 186.490 1.00 37.30  ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 248.926 232.294 185.366 1.00 44.42  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 250.047 231.724 188.438 1.00 41.30  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 247.779 233.363 186.982 1.00 40.74  ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 246.547 233.378 186.199 1.00 32.18  ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 246.695 234.241 184.952 1.00 41.48  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 246.260 233.855 183.861 1.00 50.95  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 245.383 233.871 187.060 1.00 32.40  ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 245.136 232.989 188.267 1.00 42.73  ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 245.818 231.984 188.466 1.00 39.22  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 244.157 233.362 189.081 1.00 44.41  ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 247.301 235.422 185.096 1.00 40.32  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 247.489 236.299 183.944 1.00 35.65  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 248.433 235.678 182.924 1.00 41.38  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 248.207 235.787 181.713 1.00 54.76  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 248.010 237.662 184.396 1.00 34.07  ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 246.992 238.575 185.081 1.00 38.28  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 247.688 239.753 185.739 1.00 44.30  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 245.954 239.050 184.080 1.00 43.95  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 249.498 235.025 183.393 1.00 39.36  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 250.450 234.404 182.479 1.00 37.49  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 249.786 233.311 181.653 1.00 47.39  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 249.963 233.245 180.432 1.00 52.17  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 251.632 233.840 183.264 1.00 40.59  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 252.798 233.441 182.409 1.00 44.28  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 253.665 234.395 181.906 1.00 49.74  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 253.031 232.109 182.111 1.00 42.93  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 254.741 234.029 181.121 1.00 47.61  ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 254.103 231.737 181.326 1.00 47.44  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 254.960 232.699 180.830 1.00 50.60  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 249.006 232.446 182.305 1.00 54.06  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 248.320 231.383 181.578 1.00 53.95  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 247.287 231.953 180.615 1.00 57.27  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 247.132 231.458 179.493 1.00 62.65  ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 247.663 230.414 182.560 1.00 54.86  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 246.709 229.456 181.917 1.00 63.95  ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 247.128 228.400 181.137 1.00 66.74  ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 245.357 229.397 181.936 1.00 61.45  ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 246.074 227.730 180.704 1.00 64.20  ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 244.987 228.315 181.175 1.00 62.82  ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 246.567 232.994 181.039 1.00 52.33  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 245.543 233.589 180.187 1.00 50.58  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 246.161 234.269 178.969 1.00 53.06  ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 245.655 234.139 177.849 1.00 62.47  ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 244.707 234.580 180.997 1.00 53.23  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 243.571 235.222 180.221 1.00 60.50  ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 243.063 236.489 180.881 1.00 64.74  ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 242.816 236.464 182.105 1.00 63.49  ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 242.910 237.509 180.177 1.00 61.69  ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 247.258 235.002 179.171 1.00 47.55  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 247.872 235.728 178.061 1.00 49.23  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 248.491 234.778 177.043 1.00 56.94  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 248.366 234.995 175.832 1.00 65.96  ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 248.918 236.710 178.587 1.00 48.88  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 248.328 237.896 179.332 1.00 51.38  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 247.236 238.567 178.516 1.00 55.15  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 246.531 239.649 179.316 1.00 54.13  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 245.572 240.419 178.479 1.00 54.65  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 249.170 233.727 177.509 1.00 58.62  ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 249.733 232.747 176.585 1.00 57.83  ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 248.632 232.011 175.830 1.00 62.61  ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 248.751 231.760 174.626 1.00 69.10  ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 250.626 231.759 177.337 1.00 60.58  ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 251.772 232.404 178.098 1.00 64.66  ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 253.015 232.536 177.235 1.00 68.30  ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 253.759 231.283 177.165 1.00 67.42  ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 255.076 231.200 177.037 1.00 70.61  ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 255.832 232.283 176.961 1.00 66.28  ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 255.648 230.001 176.986 1.00 65.57  ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 247.550 231.656 176.525 1.00 60.10  ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 246.457 230.936 175.878 1.00 58.27  ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 245.791 231.792 174.806 1.00 62.32  ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 245.486 231.307 173.710 1.00 71.89  ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 245.434 230.488 176.922 1.00 62.18  ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 246.024 229.621 177.875 1.00 66.18  ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 245.553 233.071 175.107 1.00 66.65  ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 244.905 233.948 174.137 1.00 66.14  ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 245.801 234.206 172.933 1.00 68.10  ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 245.338 234.175 171.787 1.00 76.05  ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 244.514 235.270 174.798 1.00 66.45  ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 243.366 235.168 175.788 1.00 70.50  ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 242.860 236.529 176.226 1.00 76.51  ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 242.531 237.353 175.347 1.00 76.23  ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 242.794 236.778 177.447 1.00 72.54  ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 247.089 234.464 173.172 1.00 68.55  ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 247.975 234.844 172.077 1.00 69.54  ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 248.363 233.636 171.231 1.00 70.47  ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 248.567 233.763 170.018 1.00 78.01  ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 249.209 235.559 172.630 1.00 67.88  ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 250.336 235.908 171.660 1.00 72.42  ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 249.958 237.123 170.832 1.00 76.45  ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 251.608 236.186 172.430 1.00 71.94  ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 248.475 232.457 171.850 1.00 71.18  ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 248.656 231.236 171.068 1.00 72.99  ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 247.423 230.941 170.223 1.00 74.17  ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 247.539 230.526 169.064 1.00 76.53  ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 248.967 230.053 171.985 1.00 72.13  ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 250.409 229.984 172.464 1.00 75.23  ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 250.605 228.964 173.570 1.00 81.48  ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 249.613 228.317 173.967 1.00 80.93  ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 251.751 228.806 174.041 1.00 81.09  ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 246.232 231.140 170.793 1.00 76.76  ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 245.002 230.949 170.033 1.00 72.55  ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 244.899 231.955 168.893 1.00 74.62  ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 244.463 231.611 167.788 1.00 82.10  ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 243.792 231.062 170.960 1.00 72.76  ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 242.459 230.802 170.282 1.00 79.67  ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 241.281 231.032 171.209 1.00 82.05  ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 241.505 231.439 172.368 1.00 81.12  ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 240.131 230.806 170.778 1.00 82.13  ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 245.287 233.207 169.147 1.00 75.70  ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 245.266 234.219 168.097 1.00 70.40  ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 246.226 233.866 166.968 1.00 74.87  ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 245.893 234.024 165.788 1.00 83.32  ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 245.609 235.588 168.684 1.00 75.86  ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 245.527 236.731 167.686 1.00 81.41  ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 245.817 238.077 168.319 1.00 83.47  ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 246.119 238.164 169.509 1.00 79.67  ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 245.727 239.136 167.524 1.00 80.74  ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 247.425 233.389 167.312 1.00 79.42  ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 248.394 233.011 166.288 1.00 78.60  ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 247.884 231.850 165.444 1.00 82.85  ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 248.053 231.842 164.219 1.00 86.08  ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 249.732 232.657 166.938 1.00 79.08  ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 250.744 232.034 165.989 1.00 82.62  ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 251.508 233.068 165.185 1.00 84.86  ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 251.186 234.256 165.212 1.00 84.67  ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 252.529 232.620 164.463 1.00 82.01  ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 247.257 230.858 166.081 1.00 83.89  ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 246.712 229.729 165.334 1.00 81.06  ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 245.601 230.175 164.392 1.00 84.57  ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 245.514 229.701 163.254 1.00 91.38  ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 246.203 228.658 166.299 1.00 79.28  ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 245.662 227.414 165.615 1.00 82.99  ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 245.097 226.165 166.786 1.00 96.54  ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 243.602 226.933 167.405 1.00 85.23  ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 244.739 231.085 164.852 1.00 76.85  ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 243.669 231.591 163.998 1.00 75.67  ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 244.226 232.341 162.795 1.00 78.66  ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 243.734 232.181 161.671 1.00 83.83  ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 242.738 232.493 164.807 1.00 79.19  ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 241.713 231.747 165.602 1.00 78.38  ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 242.035 230.991 166.708 1.00 82.25  ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 240.371 231.647 165.457 1.00 79.34  ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 240.936 230.453 167.206 1.00 79.07  ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 239.912 230.836 166.466 1.00 80.06  ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 245.251 233.169 163.010 1.00 77.92  ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 245.823 233.940 161.911 1.00 78.43  ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 246.519 233.037 160.900 1.00 81.52  ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 246.429 233.267 159.689 1.00 86.80  ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 246.794 234.987 162.456 1.00 80.18  ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 246.161 236.121 163.264 1.00 81.71  ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 247.197 237.176 163.607 1.00 81.49  ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 244.995 236.736 162.507 1.00 82.51  ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 247.224 232.009 161.379 1.00 84.00  ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 247.914 231.101 160.468 1.00 84.09  ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 246.927 230.339 159.593 1.00 84.59  ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 247.171 230.143 158.396 1.00 87.49  ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 248.794 230.132 161.258 1.00 84.05  ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 249.971 230.821 161.919 1.00 85.58  ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 250.006 232.047 162.028 1.00 85.55  ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 250.943 230.035 162.365 1.00 85.25  ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 245.809 229.895 160.172 1.00 82.77  ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 244.787 229.209 159.386 1.00 83.30  ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 244.185 230.157 158.356 1.00 86.81  ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 243.977 229.785 157.194 1.00 91.67  ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 243.710 228.614 160.311 1.00 81.44  ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 242.537 228.091 159.497 1.00 82.22  ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 244.301 227.507 161.168 1.00 83.78  ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 243.898 231.395 158.762 1.00 85.36  ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 243.361 232.365 157.821 1.00 82.94  ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 244.337 232.704 156.711 1.00 84.28  ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 243.951 232.816 155.545 1.00 86.82  ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 245.614 232.880 157.058 1.00 84.98  ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 246.628 233.136 156.039 1.00 83.81  ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 246.801 231.934 155.119 1.00 84.84  ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 246.993 232.093 153.908 1.00 85.69  ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 247.957 233.504 156.700 1.00 83.60  ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 248.043 234.902 157.314 1.00 84.47  ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 249.439 235.166 157.854 1.00 85.88  ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 247.650 235.960 156.295 1.00 84.03  ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 246.745 230.723 155.679 1.00 88.57  ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 246.848 229.522 154.856 1.00 89.10  ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 245.670 229.408 153.897 1.00 89.92  ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 245.842 229.027 152.733 1.00 91.90  ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 246.936 228.281 155.744 1.00 89.03  ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 247.709 227.126 155.125 1.00 90.20  ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 247.507 225.824 155.894 1.00 90.73  ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 247.223 226.030 157.310 1.00 90.90  ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 248.125 226.385 158.216 1.00 90.36  ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 249.393 226.576 157.892 1.00 89.11  ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 247.744 226.550 159.480 1.00 87.92  ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 244.463 229.732 154.369 1.00 87.65  ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 243.283 229.647 153.514 1.00 88.76  ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 243.384 230.608 152.336 1.00 91.84  ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 243.011 230.261 151.209 1.00 95.99  ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 242.022 229.930 154.330 1.00 89.19  ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 241.553 228.759 155.178 1.00 89.77  ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 241.070 227.606 154.313 1.00 91.39  ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 241.448 226.265 154.921 1.00 92.33  ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 240.687 225.986 156.170 1.00 89.11  ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 243.876 231.825 152.579 1.00 89.34  ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 244.035 232.792 151.496 1.00 87.43  ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 245.072 232.305 150.492 1.00 90.41  ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 244.865 232.384 149.275 1.00 97.09  ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 244.399 234.176 152.064 1.00 89.78  ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 243.247 234.724 152.908 1.00 90.68  ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 244.740 235.142 150.940 1.00 91.02  ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 243.517 236.093 153.493 1.00 91.23  ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 246.203 231.789 150.984 1.00 95.28  ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 247.253 231.316 150.087 1.00 98.30  ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 246.771 230.148 149.235 1.00 100.28 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 247.085 230.070 148.041 1.00 101.97 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 248.492 230.921 150.890 1.00 99.47  ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 249.715 230.633 150.034 1.00 98.72  ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 251.002 230.821 150.823 1.00 100.09 ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 251.062 232.199 151.461 1.00 98.48  ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 251.210 233.276 150.444 1.00 97.73  ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 246.013 229.225 149.832 1.00 96.88  ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 245.430 228.135 149.056 1.00 98.34  ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 244.447 228.666 148.020 1.00 98.47  ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 244.383 228.157 146.895 1.00 99.14  ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 244.744 227.134 149.985 1.00 98.04  ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 245.693 226.400 150.917 1.00 98.91  ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 244.964 225.521 151.915 1.00 100.46 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 243.716 225.495 151.885 1.00 100.93 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 245.640 224.858 152.730 1.00 99.16  ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 243.667 229.686 148.386 1.00 98.46  ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 242.743 230.295 147.435 1.00 99.71  ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 243.493 230.956 146.284 1.00 100.93 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 243.074 230.863 145.124 1.00 104.09 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 241.845 231.303 148.154 1.00 97.91  ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 240.896 230.601 148.965 1.00 98.83  ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 241.096 232.167 147.156 1.00 97.12  ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 244.611 231.625 146.585 1.00 102.72 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 245.436 232.215 145.533 1.00 103.23 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 245.921 231.135 144.574 1.00 104.83 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 245.967 231.338 143.355 1.00 104.04 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 246.612 232.996 146.150 1.00 104.07 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 247.586 233.443 145.069 1.00 102.98 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 246.105 234.192 146.937 1.00 102.18 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 246.293 229.971 145.109 1.00 109.15 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 246.658 228.850 144.250 1.00 109.77 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 245.450 228.335 143.477 1.00 109.97 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 245.575 227.926 142.316 1.00 112.31 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 247.280 227.731 145.084 1.00 110.06 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 248.740 227.986 145.404 1.00 111.87 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 249.321 228.929 144.826 1.00 112.83 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 249.307 227.244 146.234 1.00 111.29 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 244.272 228.341 144.106 1.00 107.80 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 243.081 227.807 143.452 1.00 107.44 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 242.671 228.655 142.254 1.00 108.88 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 242.293 228.118 141.207 1.00 111.87 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 241.928 227.707 144.450 1.00 108.08 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 240.674 227.075 143.869 1.00 107.32 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 239.563 226.932 144.888 1.00 110.17 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 239.705 227.341 146.040 1.00 112.84 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 238.449 226.344 144.469 1.00 109.74 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 242.728 229.982 142.387 1.00 110.79 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 242.334 230.835 141.269 1.00 111.08 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 243.340 230.729 140.130 1.00 111.44 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 242.976 230.880 138.957 1.00 113.17 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 242.144 232.292 141.732 1.00 107.87 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 241.070 232.368 142.804 1.00 107.15 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 243.449 232.882 142.238 1.00 109.81 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 244.613 230.477 140.445 1.00 110.85 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 245.614 230.301 139.397 1.00 111.76 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 245.330 229.051 138.572 1.00 111.26 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 245.403 229.076 137.338 1.00 111.14 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 247.012 230.239 140.012 1.00 111.90 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 248.142 230.293 138.995 1.00 111.11 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 248.627 228.916 138.584 1.00 113.34 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 248.139 227.917 139.153 1.00 113.78 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 249.493 228.832 137.688 1.00 110.79 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 245.003 227.941 139.240 1.00 109.96 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 244.701 226.713 138.513 1.00 110.57 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 243.321 226.767 137.872 1.00 111.10 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 243.102 226.158 136.819 1.00 113.89 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 244.818 225.501 139.442 1.00 110.86 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 243.798 225.460 140.567 1.00 111.61 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 243.996 224.278 141.495 1.00 113.27 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 244.946 223.498 141.274 1.00 114.02 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 243.199 224.127 142.445 1.00 112.96 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 242.380 227.488 138.485 1.00 109.94 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 241.048 227.608 137.903 1.00 110.70 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 241.054 228.533 136.692 1.00 111.15 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 240.264 228.334 135.762 1.00 113.32 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 240.058 228.092 138.967 1.00 110.60 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 238.550 228.008 138.708 1.00 109.18 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 237.812 227.858 140.028 1.00 109.55 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 238.038 229.227 137.970 1.00 109.27 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 241.930 229.542 136.686 1.00 110.64 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 242.148 230.323 135.473 1.00 111.15 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 242.750 229.459 134.372 1.00 112.36 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 242.390 229.594 133.197 1.00 112.98 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 243.052 231.520 135.769 1.00 110.67 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 243.246 232.457 134.587 1.00 111.76 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 244.125 233.645 134.949 1.00 112.06 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 243.512 234.498 135.960 1.00 114.90 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 243.974 234.647 137.194 1.00 114.02 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 245.055 234.008 137.610 1.00 112.71 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 243.335 235.458 138.032 1.00 111.79 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 243.679 228.571 134.736 1.00 110.81 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 244.226 227.627 133.767 1.00 110.10 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 243.141 226.697 133.239 1.00 111.61 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 243.118 226.370 132.046 1.00 111.90 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 245.364 226.829 134.405 1.00 110.93 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 245.641 225.486 133.749 1.00 111.68 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 246.044 224.444 134.781 1.00 111.77 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 244.996 224.214 135.770 1.00 113.31 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 243.909 223.486 135.557 1.00 113.05 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 243.690 222.892 134.396 1.00 111.39 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 243.018 223.349 136.536 1.00 112.62 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 242.229 226.264 134.114 1.00 112.81 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 241.104 225.447 133.672 1.00 112.60 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 240.218 226.212 132.697 1.00 112.40 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 239.642 225.623 131.775 1.00 111.94 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 240.296 224.974 134.881 1.00 113.70 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 239.046 224.210 134.487 1.00 114.22 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 237.987 224.849 134.312 1.00 114.50 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 239.122 222.971 134.354 1.00 112.20 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 240.091 227.528 132.891 1.00 111.76 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 239.313 228.343 131.964 1.00 112.47 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 239.929 228.334 130.570 1.00 114.17 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 239.211 228.255 129.566 1.00 114.43 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 239.202 229.773 132.493 1.00 112.33 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 238.429 230.772 131.629 1.00 113.29 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 236.931 230.578 131.793 1.00 113.11 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 238.828 232.199 131.970 1.00 111.55 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 241.259 228.422 130.488 1.00 114.67 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 241.926 228.401 129.189 1.00 113.81 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 241.733 227.061 128.488 1.00 113.56 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 241.512 227.015 127.272 1.00 112.94 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 243.413 228.712 129.359 1.00 112.90 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 244.212 228.664 128.067 1.00 112.05 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 245.695 228.474 128.341 1.00 112.73 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 245.939 227.530 129.425 1.00 115.42 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 245.911 226.211 129.291 1.00 116.44 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 245.654 225.639 128.125 1.00 114.03 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 246.149 225.446 130.352 1.00 115.24 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 241.820 225.960 129.238 1.00 113.30 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 241.602 224.640 128.653 1.00 112.77 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 240.171 224.510 128.147 1.00 113.61 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 239.927 223.984 127.054 1.00 114.61 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 241.946 223.539 129.674 1.00 112.62 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 243.454 223.499 129.925 1.00 112.64 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 241.450 222.183 129.194 1.00 111.01 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 243.860 222.577 131.052 1.00 113.02 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 239.203 224.991 128.931 1.00 113.06 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 237.807 224.921 128.513 1.00 111.68 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 237.561 225.761 127.266 1.00 111.99 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 236.770 225.376 126.398 1.00 112.38 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 236.897 225.368 129.657 1.00 112.25 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 235.513 224.743 129.630 1.00 112.61 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 234.684 225.202 130.817 1.00 112.92 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 235.073 224.447 132.078 1.00 112.26 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 233.989 224.462 133.097 1.00 111.27 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 238.223 226.917 127.164 1.00 115.36 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 238.127 227.718 125.947 1.00 115.68 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 238.699 226.968 124.751 1.00 116.62 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 238.138 227.017 123.651 1.00 114.87 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 238.843 229.054 126.140 1.00 113.97 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 240.250 228.885 126.134 1.00 116.05 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 239.823 226.274 124.947 1.00 117.85 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 240.380 225.448 123.881 1.00 117.12 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 239.433 224.312 123.515 1.00 116.56 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 239.291 223.966 122.337 1.00 116.48 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 241.744 224.901 124.301 1.00 116.31 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 242.666 224.565 123.139 1.00 115.85 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 242.498 223.138 122.655 1.00 117.59 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 241.843 222.323 123.305 1.00 117.12 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 243.089 222.829 121.508 1.00 115.96 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 238.784 223.713 124.517 1.00 117.03 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 237.807 222.663 124.246 1.00 116.65 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 236.627 223.200 123.446 1.00 115.79 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 236.126 222.529 122.537 1.00 115.59 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 237.328 222.042 125.559 1.00 117.41 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 236.328 220.912 125.386 1.00 117.29 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 235.715 220.469 126.701 1.00 119.31 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 235.996 221.111 127.735 1.00 118.37 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 234.953 219.480 126.700 1.00 118.56 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 236.164 224.409 123.777 1.00 116.96 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 235.058 225.008 123.036 1.00 117.04 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 235.435 225.258 121.582 1.00 118.13 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 234.624 225.032 120.676 1.00 118.89 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 234.621 226.309 123.706 1.00 117.52 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 233.571 226.162 124.806 1.00 118.75 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 233.226 227.516 125.400 1.00 117.89 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 232.331 225.479 124.255 1.00 115.93 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 236.660 225.732 121.339 1.00 121.61 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 237.104 225.962 119.969 1.00 122.33 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 237.157 224.659 119.181 1.00 122.22 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 236.771 224.619 118.007 1.00 120.14 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 238.471 226.647 119.969 1.00 120.59 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 238.458 228.057 120.538 1.00 121.59 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 239.777 228.438 121.180 1.00 122.67 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 240.711 227.610 121.160 1.00 122.48 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 239.880 229.567 121.706 1.00 121.98 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 237.638 223.584 119.809 1.00 121.66 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 237.690 222.288 119.138 1.00 120.16 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 236.282 221.784 118.845 1.00 119.80 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 235.985 221.320 117.738 1.00 119.86 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 238.489 221.279 119.984 1.00 119.68 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 238.140 219.851 119.591 1.00 117.74 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 239.982 221.530 119.837 1.00 118.41 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 235.390 221.872 119.837 1.00 120.24 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 234.022 221.400 119.647 1.00 119.81 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 233.290 222.226 118.596 1.00 118.85 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 232.552 221.677 117.769 1.00 118.43 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 233.266 221.432 120.975 1.00 119.46 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 233.678 220.342 121.954 1.00 120.28 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 233.774 218.988 121.270 1.00 118.18 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 234.586 218.007 122.100 1.00 118.10 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 234.869 216.749 121.356 1.00 118.25 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 233.473 223.549 118.618 1.00 120.56 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 232.826 224.399 117.624 1.00 122.55 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 233.356 224.113 116.224 1.00 123.21 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 232.582 224.051 115.260 1.00 121.95 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 233.025 225.872 117.983 1.00 121.97 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 231.912 226.755 117.454 1.00 122.58 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 231.493 226.625 116.304 1.00 123.40 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 231.427 227.661 118.294 1.00 120.71 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 234.674 223.942 116.090 1.00 123.89 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 235.251 223.635 114.785 1.00 122.94 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 234.786 222.275 114.281 1.00 123.72 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 234.485 222.115 113.092 1.00 122.72 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 236.777 223.687 114.860 1.00 122.07 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 234.727 221.280 115.170 1.00 124.67 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 234.259 219.956 114.770 1.00 123.05 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 232.795 219.991 114.352 1.00 123.85 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 232.406 219.343 113.373 1.00 122.56 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 234.471 218.958 115.907 1.00 120.45 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 231.966 220.735 115.088 1.00 126.11 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 230.554 220.839 114.735 1.00 125.60 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 230.369 221.536 113.392 1.00 125.61 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 229.531 221.124 112.581 1.00 124.51 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 229.791 221.578 115.834 1.00 123.73 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 231.138 222.599 113.144 1.00 127.35 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 231.034 223.306 111.871 1.00 127.57 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 231.472 222.422 110.709 1.00 127.38 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 230.827 222.407 109.654 1.00 126.20 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 231.865 224.588 111.912 1.00 127.24 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 231.299 225.618 112.869 1.00 127.28 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 230.218 225.435 113.429 1.00 127.52 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 232.030 226.710 113.062 1.00 125.43 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 232.569 221.680 110.883 1.00 133.68 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 233.045 220.803 109.818 1.00 133.96 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 232.044 219.692 109.529 1.00 132.99 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 231.803 219.351 108.364 1.00 131.94 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 234.406 220.215 110.191 1.00 132.84 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 235.503 221.260 110.221 1.00 132.51 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 235.212 222.440 109.931 1.00 132.38 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 236.658 220.903 110.535 1.00 131.74 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 231.455 219.110 110.577 1.00 133.96 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 230.466 218.055 110.380 1.00 134.06 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 229.220 218.585 109.681 1.00 134.72 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 228.664 217.916 108.801 1.00 134.31 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 230.100 217.425 111.724 1.00 132.93 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 231.145 216.464 112.267 1.00 133.72 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 230.800 216.018 113.679 1.00 134.91 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 231.987 215.354 114.356 1.00 134.11 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 231.723 215.083 115.796 1.00 132.35 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 228.765 219.781 110.060 1.00 134.04 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 227.569 220.348 109.444 1.00 133.70 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 227.817 220.722 107.988 1.00 134.67 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 226.922 220.585 107.145 1.00 134.26 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 227.096 221.564 110.239 1.00 133.37 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 225.927 221.332 111.198 1.00 134.67 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 225.535 222.626 111.896 1.00 132.52 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 224.738 220.735 110.460 1.00 133.70 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 229.023 221.196 107.672 1.00 133.80 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 229.346 221.590 106.305 1.00 133.19 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 229.484 220.403 105.361 1.00 132.65 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 229.548 220.610 104.144 1.00 130.94 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 230.634 222.416 106.287 1.00 131.99 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 230.460 223.847 106.771 1.00 131.30 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 231.786 224.448 107.207 1.00 132.80 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 231.577 225.671 108.084 1.00 131.84 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 232.839 226.105 108.743 1.00 130.56 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 229.534 219.181 105.881 1.00 134.86 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 229.641 217.994 105.039 1.00 134.27 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 228.352 217.760 104.257 1.00 133.95 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 227.280 218.221 104.648 0.00 133.72 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 229.973 216.763 105.884 1.00 133.05 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 231.396 216.738 106.418 1.00 133.85 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 231.608 215.569 107.366 1.00 134.43 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 233.005 215.591 107.966 1.00 134.75 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 233.149 214.607 109.075 1.00 134.00 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 220.918 215.562 112.809 1.00 137.31 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 220.325 215.116 114.064 1.00 138.19 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 221.377 215.034 115.165 1.00 138.39 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 221.229 215.646 116.224 1.00 138.66 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 219.643 213.760 113.883 1.00 138.35 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 218.610 213.732 112.769 1.00 139.01 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 217.927 212.385 112.642 1.00 139.15 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 218.270 211.468 113.417 1.00 138.95 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 217.046 212.244 111.767 1.00 138.09 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 222.441 214.269 114.908 1.00 137.82 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 223.522 214.156 115.882 1.00 138.83 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 224.265 215.475 116.050 1.00 138.37 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 224.733 215.785 117.151 1.00 136.07 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 224.491 213.049 115.467 1.00 137.67 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 225.545 212.722 116.513 1.00 137.72 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 226.340 211.478 116.172 1.00 137.91 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 226.246 211.009 115.018 1.00 137.30 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 227.061 210.970 117.056 1.00 137.21 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 224.385 216.259 114.975 1.00 133.01 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 225.064 217.547 115.069 1.00 132.06 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 224.326 218.503 115.996 1.00 132.39 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 224.954 219.351 116.639 1.00 130.92 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 225.217 218.163 113.677 1.00 131.56 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 225.721 217.195 112.629 1.00 134.14 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 226.763 216.319 112.906 1.00 134.04 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 225.154 217.158 111.362 1.00 133.69 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 227.224 215.432 111.952 1.00 134.14 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 225.610 216.276 110.401 1.00 133.83 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 226.645 215.416 110.701 1.00 135.09 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 227.102 214.535 109.747 1.00 133.19 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 222.998 218.386 116.075 1.00 131.57 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 222.239 219.198 117.019 1.00 130.60 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 222.618 218.864 118.456 1.00 131.30 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 222.669 219.751 119.316 1.00 129.70 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 220.740 219.001 116.797 1.00 128.17 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 222.874 217.585 118.739 1.00 130.50 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 223.337 217.197 120.068 1.00 130.24 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 224.746 217.721 120.312 1.00 129.42 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 225.086 218.138 121.427 1.00 128.66 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 223.262 215.668 120.235 1.00 128.79 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 223.574 215.272 121.671 1.00 127.21 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 221.891 215.156 119.820 1.00 127.07 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 225.590 217.705 119.276 1.00 126.26 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 226.963 218.177 119.430 1.00 126.56 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 227.009 219.666 119.750 1.00 126.10 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 227.758 220.094 120.636 1.00 125.70 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 227.766 217.876 118.165 1.00 126.52 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 229.287 217.982 118.292 1.00 126.25 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 229.825 216.913 119.231 1.00 123.80 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 229.950 217.882 116.927 1.00 124.48 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 226.219 220.475 119.039 1.00 122.51 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 226.184 221.903 119.336 1.00 123.18 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 225.514 222.155 120.681 1.00 123.77 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 225.838 223.130 121.370 1.00 123.25 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 225.500 222.685 118.197 1.00 123.80 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 224.003 222.371 118.133 1.00 123.90 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 226.171 222.384 116.865 1.00 123.01 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 223.214 223.335 117.275 1.00 121.57 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 224.569 221.296 121.075 1.00 122.82 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 223.975 221.412 122.403 1.00 123.65 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 225.013 221.161 123.489 1.00 123.27 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 225.031 221.851 124.515 1.00 122.50 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 222.804 220.439 122.543 1.00 122.22 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 223.263 219.122 122.790 1.00 121.84 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 225.883 220.168 123.283 1.00 120.78 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 226.970 219.929 124.226 1.00 120.87 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 227.923 221.116 124.276 1.00 121.09 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 228.382 221.509 125.355 1.00 120.29 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 227.719 218.651 123.848 1.00 120.99 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 228.806 218.247 124.832 1.00 121.37 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 230.179 218.742 124.420 1.00 122.46 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 230.368 219.046 123.223 1.00 120.81 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 231.069 218.827 125.292 1.00 122.39 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 228.233 221.700 123.115 1.00 120.50 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 229.089 222.882 123.085 1.00 120.89 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 228.438 224.051 123.812 1.00 120.79 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 229.113 224.802 124.526 1.00 119.30 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 229.414 223.259 121.640 1.00 118.85 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 227.126 224.225 123.636 1.00 120.15 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 226.416 225.280 124.352 1.00 119.85 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 226.456 225.048 125.858 1.00 120.34 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 226.588 226.001 126.635 1.00 118.75 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 224.972 225.370 123.858 1.00 118.79 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 224.199 226.557 124.410 1.00 119.06 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 222.822 226.693 123.792 1.00 119.98 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 222.688 226.928 122.591 1.00 119.55 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 221.788 226.546 124.613 1.00 118.90 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 226.335 223.789 126.287 1.00 118.57 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 226.435 223.478 127.710 1.00 118.17 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 227.818 223.819 128.251 1.00 117.94 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 227.945 224.348 129.362 1.00 117.49 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 226.110 222.005 127.951 1.00 115.39 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 228.867 223.518 127.483 1.00 114.97 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 230.216 223.897 127.890 1.00 114.68 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 230.368 225.413 127.889 1.00 116.08 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 231.075 225.974 128.736 1.00 116.36 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 231.261 223.218 126.985 1.00 115.15 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 231.100 221.697 127.028 1.00 115.25 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 232.671 223.601 127.407 1.00 115.46 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 230.997 221.127 128.429 1.00 114.02 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 229.712 226.101 126.949 1.00 116.92 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 229.750 227.560 126.937 1.00 115.73 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 229.162 228.136 128.219 1.00 116.00 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 229.713 229.081 128.795 1.00 115.33 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 228.997 228.097 125.719 1.00 114.86 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 229.786 228.055 124.422 1.00 115.99 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 229.230 229.035 123.403 1.00 116.33 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 229.532 230.472 123.797 1.00 114.80 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 230.995 230.722 123.905 1.00 114.17 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 228.037 227.581 128.677 1.00 113.54 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 227.457 228.021 129.942 1.00 113.28 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 228.377 227.696 131.111 1.00 113.47 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 228.527 228.502 132.037 1.00 111.49 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 226.084 227.380 130.142 1.00 111.22 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 228.996 226.512 131.091 1.00 112.65 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 229.922 226.141 132.156 1.00 112.44 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 231.129 227.071 132.186 1.00 111.48 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 231.589 227.469 133.262 1.00 111.35 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 230.366 224.689 131.983 1.00 111.77 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 230.866 224.076 133.275 1.00 112.25 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 230.643 224.679 134.346 1.00 111.89 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 231.484 222.992 133.220 1.00 111.22 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 231.659 227.424 131.012 1.00 109.50 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 232.761 228.378 130.957 1.00 109.85 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 232.318 229.753 131.440 1.00 112.57 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 233.086 230.466 132.096 1.00 111.85 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 233.320 228.449 129.533 1.00 110.01 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 234.601 229.252 129.280 1.00 111.87 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 235.365 228.649 128.120 1.00 110.89 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 234.302 230.717 128.991 1.00 110.66 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 231.083 230.145 131.116 1.00 112.08 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 230.565 231.426 131.588 1.00 111.06 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 230.480 231.458 133.109 1.00 110.85 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 230.801 232.474 133.735 1.00 110.97 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 229.197 231.702 130.966 1.00 109.33 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 230.040 230.355 133.720 1.00 108.03 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 230.021 230.278 135.177 1.00 109.66 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 231.433 230.300 135.748 1.00 109.50 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 231.676 230.903 136.800 1.00 108.90 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 229.276 229.022 135.627 1.00 108.71 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 232.375 229.640 135.071 1.00 107.96 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 233.752 229.595 135.559 1.00 106.48 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 234.386 230.980 135.506 1.00 106.15 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 235.019 231.425 136.472 1.00 107.27 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 234.568 228.563 134.758 1.00 107.36 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 236.058 228.815 134.920 1.00 105.74 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 234.214 227.153 135.201 1.00 107.16 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 234.225 231.687 134.383 1.00 104.81 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 234.809 233.020 134.273 1.00 106.22 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 234.115 234.014 135.196 1.00 105.61 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 234.751 234.961 135.674 1.00 104.18 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 234.764 233.507 132.823 1.00 106.66 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 233.371 233.741 132.269 1.00 107.64 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 233.393 234.241 130.839 1.00 109.29 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 233.924 235.347 130.603 1.00 108.30 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 232.880 233.530 129.950 1.00 107.29 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 232.819 233.822 135.455 1.00 104.37 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 232.149 234.624 136.473 1.00 105.28 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 232.720 234.332 137.853 1.00 104.75 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 232.850 235.236 138.687 1.00 103.63 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 230.643 234.363 136.445 1.00 101.99 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 233.064 233.068 138.112 1.00 102.92 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 233.707 232.716 139.373 1.00 102.36 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 235.112 233.302 139.452 1.00 101.72 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 235.600 233.620 140.543 1.00 100.85 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 233.739 231.196 139.531 1.00 101.15 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 234.288 230.705 140.859 1.00 100.40 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 234.200 229.190 140.953 1.00 100.88 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 234.752 228.681 142.272 1.00 103.41 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 234.671 227.198 142.372 1.00 102.06 ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 235.780 233.448 138.305 1.00 100.14 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 237.104 234.066 138.285 1.00 99.14  ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 237.013 235.526 138.708 1.00 100.88 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 237.765 235.991 139.573 1.00 103.20 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 237.742 233.928 136.891 1.00 101.29 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 238.888 234.916 136.728 1.00 99.73  ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 238.227 232.511 136.664 1.00 100.69 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 236.087 236.271 138.101 1.00 96.19  ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 235.969 237.697 138.392 1.00 95.94  ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 235.504 237.931 139.824 1.00 97.02  ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 236.022 238.811 140.521 1.00 98.07  ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 235.008 238.353 137.400 1.00 96.73  ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 235.571 238.410 135.994 1.00 99.63  ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 236.787 238.409 135.800 1.00 100.16 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 234.688 238.463 135.003 1.00 97.28  ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 234.520 237.152 140.278 1.00 92.63  ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 233.979 237.350 141.619 1.00 93.22  ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 235.014 237.018 142.686 1.00 94.02  ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 235.149 237.739 143.682 1.00 96.86  ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 232.720 236.505 141.811 1.00 90.96  ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 232.050 236.731 143.152 1.00 91.60  ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 230.761 235.948 143.284 1.00 90.22  ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 230.153 236.155 144.592 1.00 92.56  ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 229.011 235.609 144.985 1.00 94.88  ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 228.327 234.795 144.199 1.00 93.91  ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 228.542 235.892 146.196 1.00 93.67  ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 235.749 235.919 142.501 1.00 91.95  ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 236.780 235.559 143.467 1.00 91.14  ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 237.908 236.580 143.475 1.00 91.04  ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 238.366 237.001 144.543 1.00 94.97  ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 237.322 234.162 143.166 1.00 90.59  ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 238.445 233.870 143.978 1.00 93.23  ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 238.355 237.009 142.291 1.00 89.24  ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 239.446 237.977 142.214 1.00 91.37  ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 239.085 239.268 142.939 1.00 92.96  ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 239.947 239.906 143.555 1.00 93.37  ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 239.796 238.258 140.751 1.00 90.80  ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 240.129 237.027 140.096 1.00 88.21  ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 240.982 239.206 140.654 1.00 88.83  ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 237.812 239.664 142.885 1.00 90.20  ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 237.360 240.801 143.677 1.00 90.92  ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 237.461 240.506 145.168 1.00 91.33  ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 237.814 241.388 145.961 1.00 91.86  ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 235.926 241.170 143.297 1.00 89.91  ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 237.146 239.272 145.570 1.00 88.71  ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 237.205 238.912 146.984 1.00 87.84  ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 238.636 238.964 147.508 1.00 88.51  ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 238.887 239.473 148.606 1.00 94.17  ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 236.599 237.524 147.196 1.00 86.83  ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 236.636 236.995 148.630 1.00 87.79  ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 235.805 237.884 149.537 1.00 87.37  ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 236.143 235.559 148.685 1.00 88.63  ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 239.591 238.440 146.735 1.00 89.43  ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 240.994 238.532 147.134 1.00 89.81  ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 241.454 239.982 147.200 1.00 92.13  ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 242.233 240.353 148.086 1.00 94.17  ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 241.881 237.729 146.180 1.00 88.27  ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 241.946 236.203 146.314 1.00 90.53  ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 240.676 235.515 145.863 1.00 92.37  ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 243.135 235.673 145.530 1.00 92.39  ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 240.992 240.814 146.265 1.00 91.56  ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 241.319 242.236 146.313 1.00 91.16  ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 240.761 242.878 147.577 1.00 91.62  ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 241.422 243.708 148.212 1.00 92.27  ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 240.784 242.938 145.064 1.00 91.91  ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 241.184 244.400 144.954 1.00 92.52  ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 240.565 245.050 143.727 1.00 92.64  ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 241.249 244.584 142.453 1.00 93.21  ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 240.733 245.298 141.253 1.00 92.81  ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 239.535 242.508 147.954 1.00 90.55  ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 238.954 243.013 149.194 1.00 91.83  ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 239.717 242.501 150.410 1.00 93.85  ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 239.913 243.237 151.384 1.00 93.22  ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 237.480 242.621 149.278 1.00 88.36  ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 236.859 243.213 150.405 1.00 90.85  ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 240.158 241.245 150.371 1.00 89.97  ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 240.865 240.627 151.485 1.00 87.22  ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 242.358 240.929 151.486 1.00 88.99  ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 243.079 240.401 152.339 1.00 91.14  ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 240.654 239.109 151.470 1.00 87.97  ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 239.231 238.597 151.702 1.00 89.27  ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 239.225 237.084 151.844 1.00 87.67  ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 238.616 239.255 152.926 1.00 89.10  ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 242.839 241.750 150.550 1.00 94.14  ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 244.260 242.081 150.510 1.00 96.14  ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 244.688 242.818 151.773 1.00 98.52  ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 245.762 242.553 152.326 1.00 97.03  ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 244.568 242.916 149.266 1.00 96.59  ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 243.873 244.151 149.297 1.00 97.25  ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 243.860 243.755 152.241 1.00 100.22 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 244.185 244.495 153.457 1.00 97.92  ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 244.222 243.573 154.670 1.00 99.01  ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 245.093 243.707 155.537 1.00 100.77 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 243.178 245.626 153.667 1.00 97.56  ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 243.275 242.636 154.753 1.00 96.44  ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 243.255 241.695 155.869 1.00 95.15  ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 244.495 240.810 155.870 1.00 95.26  ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 245.068 240.531 156.929 1.00 99.04  ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 241.988 240.842 155.813 1.00 94.60  ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 240.734 241.623 155.464 1.00 97.00  ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 240.229 242.460 156.621 1.00 99.49  ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 240.462 242.070 157.785 1.00 99.23  ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 239.598 243.508 156.369 1.00 98.98  ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 244.919 240.353 154.689 1.00 95.10  ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 246.114 239.520 154.604 1.00 95.96  ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 247.356 240.286 155.041 1.00 95.56  ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 248.226 239.735 155.725 1.00 99.61  ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 246.280 238.988 153.181 1.00 97.99  ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 247.437 238.017 153.010 1.00 98.45  ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 247.531 237.519 151.577 1.00 97.19  ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 247.899 238.584 150.651 1.00 98.84  ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 247.884 238.465 149.331 1.00 99.74  ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 247.526 237.336 148.742 1.00 98.02  ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 248.237 239.506 148.582 1.00 98.20  ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 247.460 241.558 154.647 1.00 95.75  ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 248.603 242.368 155.058 1.00 98.16  ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 248.633 242.561 156.569 1.00 97.57  ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 249.690 242.436 157.197 1.00 97.99  ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 248.571 243.721 154.348 1.00 98.51  ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 248.767 243.645 152.843 1.00 100.46 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 250.155 243.175 152.457 1.00 100.12 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 251.112 243.467 153.204 1.00 99.35  ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 250.290 242.515 151.405 1.00 98.42  ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 247.480 242.865 157.170 1.00 97.00  ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 247.437 243.108 158.609 1.00 94.71  ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 247.747 241.842 159.398 1.00 95.67  ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 248.483 241.885 160.391 1.00 100.57 ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 246.070 243.665 159.007 1.00 94.27  ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 245.947 244.002 160.483 1.00 96.79  ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 244.491 244.084 160.911 1.00 97.69  ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 243.666 244.753 159.913 1.00 96.46  ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 242.570 244.233 159.378 1.00 95.35  ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 242.138 243.030 159.719 1.00 95.58  ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 241.890 244.937 158.478 1.00 95.65  ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 247.193 240.704 158.974 1.00 89.90  ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 247.416 239.459 159.702 1.00 87.65  ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 248.865 239.000 159.587 1.00 90.49  ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 249.407 238.401 160.522 1.00 96.61  ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 246.464 238.377 159.196 1.00 88.82  ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 245.021 238.709 159.414 1.00 89.19  ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 244.510 239.566 160.345 1.00 89.41  ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 243.901 238.195 158.684 1.00 91.40  ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 243.142 239.615 160.242 1.00 91.85  ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 242.743 238.783 159.230 1.00 93.20  ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 243.766 237.295 157.624 1.00 90.10  ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 241.466 238.499 158.751 1.00 91.25  ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 242.497 237.015 157.150 1.00 90.32  ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 241.365 237.615 157.713 1.00 89.53  ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 249.504 239.264 158.444 1.00 96.18  ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 250.914 238.922 158.295 1.00 99.50  ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 251.781 239.732 159.251 1.00 100.14 ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 252.729 239.202 159.842 1.00 100.28 ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 251.358 239.139 156.849 1.00 98.68  ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 252.793 238.720 156.573 1.00 100.74 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 253.184 238.899 155.119 1.00 102.07 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 252.341 239.375 154.330 1.00 101.75 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 254.333 238.563 154.766 1.00 100.76 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 251.474 241.022 159.412 1.00 96.31  ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 252.226 241.852 160.348 1.00 95.95  ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 252.055 241.363 161.781 1.00 97.30  ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 253.022 241.320 162.550 1.00 100.84 ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 251.791 243.312 160.225 1.00 96.79  ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 252.003 243.910 158.846 1.00 99.30  ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 253.476 243.949 158.479 1.00 97.96  ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 253.695 244.686 157.169 1.00 97.39  ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 253.110 243.948 156.015 1.00 96.26  ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 250.828 240.994 162.158 1.00 93.70  ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 250.591 240.485 163.505 1.00 92.95  ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 251.326 239.170 163.733 1.00 89.68  ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 251.831 238.915 164.833 1.00 95.05  ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 249.091 240.311 163.746 1.00 90.45  ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 248.388 241.448 163.231 1.00 87.96  ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 248.803 240.177 165.234 1.00 93.32  ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 251.392 238.320 162.705 1.00 88.34  ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 252.148 237.077 162.820 1.00 94.37  ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 253.634 237.353 163.012 1.00 96.24  ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 254.316 236.636 163.753 1.00 95.30  ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 251.917 236.207 161.585 1.00 93.59  ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 252.733 235.049 161.617 1.00 94.12  ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 254.156 238.384 162.343 1.00 100.59 ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 255.558 238.750 162.519 1.00 101.29 ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 255.829 239.235 163.938 1.00 101.10 ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 256.894 238.958 164.502 1.00 102.86 ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 255.953 239.819 161.500 1.00 99.99  ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 256.006 239.321 160.065 1.00 101.39 ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 256.572 240.353 159.110 1.00 103.69 ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 257.482 241.105 159.516 1.00 102.86 ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 256.106 240.413 157.953 1.00 101.17 ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 254.880 239.958 164.530 1.00 96.29  ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 255.032 240.477 165.883 1.00 95.49  ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 254.667 239.458 166.954 1.00 94.97  ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 254.728 239.788 168.144 1.00 97.85  ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 254.179 241.736 166.066 1.00 95.03  ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 252.796 241.412 165.871 1.00 94.21  ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 254.589 242.808 165.068 1.00 95.26  ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 254.280 238.241 166.565 1.00 88.58  ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 253.923 237.219 167.544 1.00 87.63  ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 255.112 236.859 168.426 1.00 88.84  ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 254.975 236.716 169.646 1.00 89.10  ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 253.383 235.980 166.824 1.00 88.37  ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 253.442 234.722 167.645 1.00 90.32  ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 252.454 234.438 168.571 1.00 90.05  ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 254.476 233.813 167.475 1.00 89.54  ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 252.501 233.279 169.323 1.00 88.89  ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 254.529 232.654 168.225 1.00 87.69  ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 253.539 232.386 169.150 1.00 87.02  ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 256.292 236.706 167.821 1.00 93.48  ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 257.481 236.359 168.595 1.00 92.68  ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 257.852 237.470 169.569 1.00 93.86  ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 258.274 237.197 170.699 1.00 92.53  ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 258.648 236.051 167.658 1.00 93.02  ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 259.619 235.021 168.208 1.00 94.11  ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 259.274 233.624 167.722 1.00 93.72  ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 260.438 232.668 167.917 1.00 92.27  ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 260.005 231.246 167.841 1.00 90.89  ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 257.711 238.728 169.145 1.00 94.64  ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 257.961 239.846 170.049 1.00 91.99  ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 256.976 239.832 171.211 1.00 89.28  ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 257.348 240.113 172.357 1.00 90.58  ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 257.877 241.165 169.278 1.00 91.70  ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 258.332 242.362 170.098 1.00 94.32  ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 258.694 242.236 171.267 1.00 95.50  ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 258.312 243.537 169.480 1.00 92.67  ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 255.713 239.499 170.936 1.00 82.98  ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 254.712 239.454 171.995 1.00 81.72  ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 254.973 238.314 172.972 1.00 82.37  ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 254.678 238.447 174.164 1.00 82.83  ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 253.314 239.332 171.388 1.00 85.54  ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 252.716 240.662 170.957 1.00 85.86  ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 251.207 240.613 170.836 1.00 87.67  ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 250.663 240.536 169.735 1.00 85.71  ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 250.521 240.661 171.972 1.00 85.48  ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 255.521 237.193 172.493 1.00 84.03  ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 255.845 236.082 173.385 1.00 80.84  ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 256.886 236.482 174.422 1.00 82.25  ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 256.776 236.116 175.598 1.00 87.17  ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 256.345 234.883 172.578 1.00 82.80  ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 255.317 234.245 171.663 1.00 89.60  ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 253.904 233.600 172.574 1.00 93.45  ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 254.659 232.224 173.435 1.00 84.62  ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 257.908 237.233 174.004 1.00 72.71  ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 259.034 237.514 174.888 1.00 74.32  ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 258.646 238.427 176.045 1.00 72.57  ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 259.284 238.383 177.103 1.00 75.12  ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 260.180 238.133 174.090 1.00 75.35  ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 261.240 238.530 174.943 1.00 78.20  ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 257.616 239.253 175.873 1.00 64.22  ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 257.253 240.257 176.864 1.00 63.93  ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 256.086 239.835 177.750 1.00 62.55  ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 255.587 240.656 178.524 1.00 61.66  ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 256.925 241.582 176.174 1.00 64.34  ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 255.871 241.382 175.224 1.00 65.54  ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 258.151 242.125 175.455 1.00 62.00  ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 255.638 238.581 177.656 1.00 59.01  ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 254.534 238.129 178.499 1.00 54.69  ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 254.945 238.113 179.966 1.00 58.11  ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 254.186 238.546 180.841 1.00 60.09  ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 254.033 236.747 178.040 1.00 57.32  ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 253.561 236.801 176.589 1.00 59.91  ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 252.904 236.265 178.936 1.00 51.40  ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 252.408 237.754 176.361 1.00 62.43  ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 256.148 237.612 180.261 1.00 56.51  ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 256.579 237.479 181.649 1.00 46.62  ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 256.685 238.839 182.331 1.00 49.41  ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 256.228 239.014 183.467 1.00 53.90  ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 257.914 236.738 181.713 1.00 44.77  ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 257.291 239.815 181.653 1.00 45.21  ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 257.412 241.139 182.239 1.00 42.28  ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 256.083 241.861 182.358 1.00 41.32  ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 255.809 242.512 183.369 1.00 51.91  ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 255.241 241.760 181.326 1.00 46.78  ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 253.961 242.463 181.342 1.00 45.87  ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 253.023 241.889 182.396 1.00 50.13  ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 252.318 242.636 183.083 1.00 53.68  ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 253.313 242.404 179.960 1.00 49.50  ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 253.918 243.400 178.990 1.00 64.04  ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 254.556 244.369 179.452 1.00 66.01  ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 253.755 243.212 177.767 1.00 60.98  ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 252.994 240.561 182.532 1.00 41.82  ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 252.110 239.941 183.514 1.00 40.62  ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 252.564 240.243 184.936 1.00 45.34  ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 251.735 240.363 185.845 1.00 51.23  ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 252.039 238.433 183.278 1.00 42.74  ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 251.138 237.961 181.784 1.00 72.17  ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 253.876 240.361 185.150 1.00 37.12  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 254.385 240.694 186.477 1.00 27.01  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 253.927 242.083 186.903 1.00 39.25  ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 253.519 242.292 188.051 1.00 43.18  ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 255.912 240.595 186.487 1.00 31.65  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 256.632 240.531 187.837 1.00 32.42  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 257.899 239.703 187.712 1.00 38.63  ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 256.960 241.922 188.359 1.00 31.17  ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 253.990 243.049 185.985 1.00 36.44  ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 253.543 244.401 186.302 1.00 28.06  ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 252.031 244.455 186.481 1.00 34.07  ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 251.528 245.137 187.382 1.00 46.82  ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 253.987 245.369 185.207 1.00 36.95  ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 255.496 245.512 185.009 1.00 34.17  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 255.798 246.543 183.937 1.00 39.45  ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 256.168 245.882 186.317 1.00 34.81  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 251.290 243.749 185.624 1.00 29.24  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 249.834 243.757 185.719 1.00 25.03  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 249.358 243.102 187.009 1.00 30.54  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 248.438 243.603 187.665 1.00 49.99  ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 249.229 243.056 184.505 1.00 44.12  ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 249.733 243.603 183.299 1.00 49.67  ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 249.970 241.977 187.387 1.00 24.51  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 249.579 241.298 188.618 1.00 22.72  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 249.884 242.150 189.841 1.00 34.27  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 249.102 242.180 190.799 1.00 34.55  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 250.287 239.950 188.720 1.00 29.60  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 251.026 242.841 189.833 1.00 37.60  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 251.388 243.689 190.963 1.00 20.66  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 250.411 244.847 191.120 1.00 33.86  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 250.096 245.255 192.244 1.00 50.34  ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 252.814 244.206 190.789 1.00 26.35  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 249.930 245.397 190.003 1.00 27.50  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 248.991 246.512 190.070 1.00 23.77  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 247.680 246.099 190.727 1.00 26.55  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 247.134 246.835 191.557 1.00 40.72  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 248.738 247.066 188.669 1.00 25.95  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 248.257 248.486 188.659 1.00 35.71  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 249.159 249.536 188.662 1.00 38.70  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 246.903 248.772 188.650 1.00 39.15  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 248.718 250.844 188.655 1.00 44.72  ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 246.456 250.077 188.644 1.00 32.09  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 247.365 251.115 188.645 1.00 40.92  ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 247.157 244.926 190.367 1.00 16.67  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 245.889 244.473 190.930 1.00 21.05  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 246.038 244.162 192.414 1.00 35.84  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 245.179 244.521 193.228 1.00 39.24  ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 245.363 243.255 190.150 1.00 24.37  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 245.353 243.543 188.648 1.00 26.01  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 243.970 242.876 190.628 1.00 34.50  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 245.317 242.297 187.792 1.00 24.67  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 247.126 243.490 192.791 1.00 29.88  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 247.276 243.008 194.159 1.00 19.50  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 247.661 244.108 195.140 1.00 33.12  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 247.352 243.998 196.331 1.00 43.49  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 248.315 241.887 194.206 1.00 22.70  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 248.327 245.165 194.678 1.00 29.44  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 248.924 246.140 195.583 1.00 19.20  ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 248.344 247.538 195.440 1.00 39.76  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 247.980 248.157 196.447 1.00 38.14  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 250.443 246.188 195.364 1.00 30.32  ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 251.170 244.933 195.790 1.00 37.42  ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 251.163 244.517 197.114 1.00 27.86  ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 251.868 244.166 194.867 1.00 35.45  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 251.829 243.374 197.507 1.00 22.22  ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 252.535 243.021 195.251 1.00 30.64  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 252.512 242.629 196.571 1.00 23.01  ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 253.177 241.489 196.957 1.00 40.49  ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 248.244 248.059 194.218 1.00 35.21  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 247.938 249.467 193.991 1.00 30.94  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 246.455 249.800 194.131 1.00 30.30  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 246.041 250.884 193.703 1.00 46.17  ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 248.437 249.895 192.609 1.00 31.42  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 245.649 248.908 194.707 1.00 33.81  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 244.225 249.177 194.814 1.00 33.42  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 243.893 250.329 195.744 1.00 27.67  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 243.069 251.186 195.414 1.00 34.09  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 244.526 250.368 196.918 1.00 43.63  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 244.192 251.382 197.913 1.00 40.09  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 244.761 252.753 197.571 1.00 42.20  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 244.171 253.773 197.944 1.00 45.25  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 244.687 250.946 199.294 1.00 36.07  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 244.450 251.971 200.382 1.00 45.90  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 243.168 252.250 200.837 1.00 49.26  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 245.512 252.660 200.953 1.00 42.59  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 242.951 253.188 201.829 1.00 48.23  ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 245.305 253.598 201.945 1.00 41.17  ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 244.024 253.858 202.380 1.00 52.68  ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 243.817 254.792 203.369 1.00 58.74  ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 245.889 252.802 196.871 1.00 41.10  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 246.589 254.057 196.653 1.00 37.06  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 245.902 254.903 195.585 1.00 40.63  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 245.115 254.417 194.770 1.00 46.80  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 248.042 253.791 196.263 1.00 34.43  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 248.768 252.904 197.228 1.00 37.31  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 249.346 253.432 198.369 1.00 45.00  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 248.854 251.541 197.008 1.00 32.98  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 250.010 252.622 199.265 1.00 36.28  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 249.514 250.725 197.903 1.00 41.39  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 250.094 251.266 199.033 1.00 41.69  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 246.220 256.195 195.605 1.00 38.15  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 245.662 257.153 194.665 1.00 30.79  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 246.479 257.165 193.374 1.00 35.80  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 247.443 256.414 193.208 1.00 50.92  ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 245.594 258.533 195.310 1.00 42.67  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 246.922 258.969 195.890 1.00 48.91  ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 247.853 258.137 195.942 1.00 52.12  ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 247.029 260.138 196.313 1.00 43.08  ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 246.090 258.045 192.446 1.00 34.60  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 246.628 257.981 191.089 1.00 36.81  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 248.132 258.224 191.060 1.00 43.01  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 248.868 257.512 190.366 1.00 50.86  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 245.909 258.989 190.192 1.00 43.47  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 246.607 259.233 188.864 1.00 37.72  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 246.021 260.402 188.101 1.00 47.25  ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 245.343 261.254 188.674 1.00 48.35  ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 246.278 260.447 186.799 1.00 48.47  ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 248.611 259.227 191.800 1.00 39.92  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 250.039 259.534 191.780 1.00 44.45  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 250.867 258.395 192.362 1.00 46.15  ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 251.928 258.055 191.825 1.00 53.10  ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 250.319 260.847 192.517 1.00 49.14  ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 249.289 261.957 192.291 1.00 51.29  ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 248.044 261.816 193.145 1.00 57.27  ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 248.121 261.761 194.371 1.00 50.43  ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 246.886 261.761 192.497 1.00 51.07  ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 250.402 257.787 193.456 1.00 36.50  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 251.153 256.685 194.050 1.00 36.92  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 251.069 255.425 193.197 1.00 42.40  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 252.023 254.639 193.149 1.00 54.23  ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 250.662 256.415 195.472 1.00 39.73  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 251.470 255.356 196.205 1.00 48.47  ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 253.194 255.819 196.469 1.00 63.53  ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 253.035 257.070 197.735 1.00 47.19  ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 249.940 255.211 192.518 1.00 38.40  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 249.834 254.075 191.607 1.00 32.92  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 250.854 254.185 190.482 1.00 37.78  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 251.486 253.193 190.100 1.00 44.26  ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 248.416 253.981 191.042 1.00 27.76  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 247.381 253.462 192.024 1.00 23.99  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 246.033 253.285 191.348 1.00 25.26  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 244.977 252.978 192.305 1.00 27.82  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 243.779 252.516 191.975 1.00 34.04  ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 243.446 252.296 190.713 1.00 37.57  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 242.892 252.269 192.934 1.00 36.30  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 251.024 255.390 189.934 1.00 41.32  ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 252.026 255.595 188.893 1.00 39.95  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 253.437 255.430 189.444 1.00 41.14  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 254.308 254.863 188.775 1.00 39.84  ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 251.852 256.978 188.266 1.00 42.17  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 252.685 257.200 187.016 1.00 44.16  ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 252.505 256.094 185.995 1.00 48.65  ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 253.461 255.414 185.624 1.00 46.54  ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 251.274 255.909 185.535 1.00 48.64  ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 253.682 255.922 190.661 1.00 40.90  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 255.012 255.814 191.254 1.00 36.73  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 255.404 254.356 191.463 1.00 43.42  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 256.547 253.964 191.199 1.00 51.24  ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 255.062 256.578 192.577 1.00 36.47  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 254.946 258.077 192.390 1.00 55.11  ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 254.873 258.570 191.264 1.00 55.46  ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 254.929 258.812 193.496 1.00 45.67  ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 254.467 253.539 191.947 1.00 42.07  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 254.750 252.120 192.135 1.00 24.37  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 255.033 251.432 190.806 1.00 29.31  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 255.960 250.621 190.703 1.00 43.16  ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 253.583 251.441 192.851 1.00 32.97  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 253.429 251.734 194.344 1.00 28.43  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 252.112 251.179 194.863 1.00 32.79  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 254.599 251.159 195.125 1.00 29.66  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 254.244 251.744 189.774 1.00 29.26  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 254.430 251.101 188.478 1.00 29.57  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 255.777 251.462 187.866 1.00 37.53  ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 256.456 250.602 187.292 1.00 52.20  ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 253.292 251.483 187.533 1.00 36.70  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 253.060 250.489 186.432 1.00 40.52  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 252.282 249.365 186.649 1.00 44.84  ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 253.620 250.678 185.180 1.00 37.75  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 252.066 248.448 185.638 1.00 38.95  ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 253.408 249.765 184.166 1.00 39.68  ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 252.630 248.649 184.395 1.00 36.12  ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 256.178 252.732 187.968 1.00 44.06  ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 257.479 253.137 187.444 1.00 37.12  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 258.615 252.458 188.198 1.00 44.71  ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 259.592 252.012 187.587 1.00 48.68  ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 257.628 254.657 187.508 1.00 42.41  ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 257.407 255.106 188.850 1.00 43.97  ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 256.633 255.332 186.576 1.00 41.26  ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 258.502 252.365 189.526 1.00 41.96  ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 259.537 251.701 190.312 1.00 31.28  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 259.657 250.231 189.930 1.00 37.17  ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 260.768 249.703 189.801 1.00 50.12  ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 259.239 251.845 191.804 1.00 33.76  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 259.099 253.232 192.134 1.00 37.27  ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 260.364 251.245 192.634 1.00 36.16  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 258.522 249.553 189.748 1.00 32.29  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 258.552 248.170 189.285 1.00 25.58  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 259.121 248.075 187.875 1.00 34.65  ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 259.894 247.160 187.568 1.00 44.21  ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 257.148 247.570 189.333 1.00 31.38  ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 256.507 247.614 190.685 1.00 25.28  ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 257.137 247.626 191.893 1.00 26.44  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 255.102 247.657 190.964 1.00 32.27  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 256.213 247.670 192.909 1.00 35.22  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 254.956 247.690 192.364 1.00 31.91  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 253.954 247.670 190.166 1.00 31.79  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 253.710 247.735 192.984 1.00 30.82  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 252.718 247.716 190.783 1.00 27.16  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 252.605 247.747 192.177 1.00 31.29  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 258.743 249.011 187.000 1.00 44.18  ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 259.217 248.979 185.620 1.00 39.60  ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 260.723 249.193 185.541 1.00 47.01  ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 261.409 248.537 184.748 1.00 49.66  ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 258.482 250.030 184.789 1.00 40.22  ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 257.082 249.818 184.822 1.00 47.28  ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 261.256 250.114 186.349 1.00 50.08  ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 262.694 250.368 186.331 1.00 45.07  ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 263.480 249.139 186.770 1.00 52.96  ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 264.534 248.832 186.202 1.00 58.15  ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 263.035 251.567 187.216 1.00 46.43  ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 262.538 252.875 186.683 1.00 62.15  ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 262.733 253.267 185.376 1.00 64.18  ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 261.871 253.889 187.284 1.00 59.01  ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 262.197 254.460 185.192 1.00 56.76  ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 261.667 254.860 186.334 1.00 58.30  ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 262.985 248.425 187.785 1.00 45.54  ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 263.681 247.232 188.258 1.00 43.52  ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 263.747 246.163 187.175 1.00 51.58  ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 264.772 245.489 187.021 1.00 61.47  ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 262.994 246.685 189.508 1.00 44.36  ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 263.732 245.554 190.155 1.00 53.23  ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 263.488 244.233 189.848 1.00 54.16  ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 264.706 245.548 191.095 1.00 53.19  ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 264.281 243.462 190.569 1.00 50.24  ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 265.030 244.235 191.335 1.00 53.04  ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 262.660 245.987 186.421 1.00 43.84  ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 262.668 245.017 185.331 1.00 41.09  ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 263.658 245.420 184.245 1.00 48.67  ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 264.306 244.560 183.637 1.00 58.52  ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 261.262 244.866 184.750 1.00 52.96  ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 260.217 244.207 185.653 1.00 45.84  ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 258.946 243.915 184.874 1.00 43.26  ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 260.766 242.938 186.282 1.00 49.49  ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 263.779 246.723 183.980 1.00 53.97  ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 264.765 247.193 183.012 1.00 53.46  ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 266.183 246.883 183.474 1.00 59.85  ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 267.023 246.448 182.678 1.00 58.49  ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 264.598 248.694 182.776 1.00 55.82  ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 263.299 249.079 182.092 1.00 56.73  ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 263.168 250.576 181.896 1.00 61.34  ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 264.023 251.347 182.331 1.00 60.61  ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 262.093 250.995 181.239 1.00 59.09  ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 266.469 247.104 184.760 1.00 56.28  ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 267.798 246.823 185.288 1.00 55.71  ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 268.097 245.331 185.346 1.00 61.14  ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 269.271 244.948 185.351 1.00 70.60  ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 267.953 247.436 186.680 1.00 54.93  ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 267.694 248.931 186.740 1.00 60.26  ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 267.562 249.441 188.161 1.00 63.85  ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 267.329 248.669 189.091 1.00 63.00  ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 267.708 250.749 188.337 1.00 60.65  ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 267.070 244.486 185.393 1.00 58.33  ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 267.241 243.042 185.441 1.00 59.31  ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 267.174 242.394 184.064 1.00 60.46  ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 267.213 241.163 183.972 1.00 64.48  ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 266.188 242.416 186.360 1.00 56.57  ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 267.077 243.195 183.001 1.00 55.30  ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 266.988 242.694 181.627 1.00 60.21  ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 265.806 241.742 181.453 1.00 65.26  ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 265.926 240.677 180.844 1.00 64.70  ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 268.295 242.024 181.194 1.00 63.64  ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 269.400 243.025 180.927 1.00 69.71  ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 269.232 244.225 181.142 1.00 69.29  ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 270.540 242.535 180.454 1.00 70.59  ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 264.654 242.131 181.991 1.00 56.28  ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 263.412 241.381 181.841 1.00 55.80  ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 262.529 242.146 180.866 1.00 58.01  ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 262.181 243.308 181.112 1.00 54.48  ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 262.706 241.171 183.189 1.00 53.93  ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 263.524 240.228 184.073 1.00 54.79  ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 261.304 240.624 182.976 1.00 53.83  ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 262.937 240.017 185.450 1.00 56.45  ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 262.168 241.496 179.763 1.00 63.16  ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 261.444 242.172 178.695 1.00 62.20  ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 259.999 242.435 179.099 1.00 63.88  ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 259.319 241.554 179.634 1.00 64.85  ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 261.490 241.336 177.417 1.00 62.12  ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 262.883 241.181 176.829 1.00 62.49  ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 263.639 242.493 176.771 1.00 69.58  ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 264.680 242.652 177.409 1.00 69.64  ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 263.119 243.442 176.002 1.00 66.66  ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 259.531 243.654 178.839 1.00 57.00  ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 258.142 244.019 179.074 1.00 53.35  ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 257.786 245.176 178.153 1.00 58.99  ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 258.635 246.019 177.853 1.00 59.68  ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 257.895 244.403 180.538 1.00 50.63  ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 258.588 245.666 180.964 1.00 52.70  ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 259.936 245.662 181.279 1.00 56.30  ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 257.890 246.859 181.050 1.00 56.31  ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 260.574 246.822 181.671 1.00 56.95  ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 258.523 248.022 181.441 1.00 55.06  ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 259.866 248.003 181.752 1.00 54.69  ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 256.534 245.208 177.708 1.00 72.49  ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 256.073 246.267 176.823 1.00 71.09  ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 255.765 247.530 177.617 1.00 75.43  ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 255.210 247.472 178.718 1.00 81.05  ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 254.832 245.818 176.051 1.00 69.71  ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 255.141 245.130 174.733 1.00 74.22  ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 253.965 245.215 173.775 1.00 75.38  ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 252.687 245.166 174.474 1.00 77.79  ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 251.919 244.088 174.555 1.00 76.08  ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 252.271 242.945 173.992 1.00 77.47  ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 250.768 244.160 175.218 1.00 72.58  ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 256.133 248.679 177.049 1.00 83.30  ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 255.898 249.972 177.679 1.00 88.09  ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 254.973 250.863 176.860 1.00 89.91  ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 254.783 252.032 177.214 1.00 90.18  ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 257.225 250.695 177.929 1.00 88.48  ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 256.967 252.014 178.426 1.00 85.78  ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 258.029 250.792 176.641 1.00 85.54  ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 254.393 250.347 175.777 1.00 92.95  ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 253.512 251.125 174.916 1.00 93.75  ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 252.038 250.958 175.260 1.00 94.55  ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 251.267 251.915 175.138 1.00 93.75  ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 253.737 250.745 173.449 1.00 92.56  ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 253.619 249.252 173.208 1.00 95.29  ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 253.514 248.494 174.195 1.00 97.30  ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 253.629 248.836 172.030 1.00 92.95  ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 251.628 249.768 175.685 1.00 87.22  ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 250.228 249.509 175.997 1.00 85.56  ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 249.925 249.965 177.418 1.00 85.48  ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 250.762 249.871 178.324 1.00 79.60  ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 249.892 248.017 175.790 1.00 84.63  ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 248.377 247.800 175.787 1.00 82.52  ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 250.568 247.150 176.845 1.00 82.34  ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 247.957 246.425 175.318 1.00 81.13  ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 248.720 250.493 177.610 1.00 69.86  ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 248.273 250.906 178.931 1.00 66.53  ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 247.800 249.700 179.733 1.00 63.38  ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 247.342 248.698 179.178 1.00 68.04  ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 247.150 251.937 178.822 1.00 62.78  ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 247.921 249.806 181.059 1.00 47.62  ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 247.503 248.707 181.923 1.00 51.99  ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 245.997 248.486 181.864 1.00 52.44  ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 245.531 247.354 182.035 1.00 58.06  ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 247.951 248.968 183.362 1.00 52.25  ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 247.586 250.343 183.891 1.00 51.52  ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 248.646 250.859 184.849 1.00 42.41  ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 248.330 252.192 185.347 1.00 49.59  ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 249.175 252.958 186.024 1.00 48.98  ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 250.403 252.553 186.302 1.00 48.09  ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 248.777 254.159 186.432 1.00 50.78  ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 245.223 249.548 181.629 1.00 52.76  ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 243.780 249.387 181.476 1.00 55.63  ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 243.438 248.567 180.240 1.00 57.27  ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 242.500 247.762 180.269 1.00 61.46  ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 243.097 250.753 181.406 1.00 55.47  ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 243.613 251.491 180.291 1.00 57.67  ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 243.344 251.539 182.683 1.00 56.31  ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 244.179 248.757 179.149 1.00 56.64  ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 243.935 248.014 177.920 1.00 57.06  ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 244.536 246.616 177.947 1.00 61.42  ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 244.040 245.724 177.248 1.00 65.53  ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 244.490 248.785 176.720 1.00 59.07  ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 244.141 250.264 176.722 1.00 60.41  ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 244.239 250.889 175.345 1.00 67.97  ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 244.471 250.145 174.369 1.00 67.06  ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 244.085 252.123 175.239 1.00 66.72  ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 245.597 246.404 178.727 1.00 56.71  ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 246.196 245.079 178.825 1.00 49.27  ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 245.380 244.142 179.705 1.00 50.14  ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 245.335 242.935 179.441 1.00 47.00  ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 247.625 245.186 179.362 1.00 46.68  ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 248.440 243.924 179.191 1.00 51.39  ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 248.813 243.481 177.929 1.00 56.51  ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 248.834 243.175 180.291 1.00 50.68  ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 249.558 242.328 177.768 1.00 54.58  ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 249.579 242.020 180.140 1.00 50.98  ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 249.938 241.602 178.877 1.00 55.92  ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 250.679 240.453 178.721 1.00 56.82  ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 244.736 244.668 180.743 1.00 43.33  ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 244.005 243.856 181.705 1.00 42.74  ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 242.528 243.699 181.365 1.00 48.67  ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 241.814 243.001 182.093 1.00 51.00  ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 244.144 244.455 183.108 1.00 47.98  ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 245.471 244.198 183.819 1.00 44.62  ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 245.538 244.969 185.127 1.00 45.72  ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 245.654 242.712 184.062 1.00 40.18  ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 242.053 244.321 180.290 1.00 46.87  ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 240.651 244.215 179.915 1.00 49.55  ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 240.521 244.459 178.420 1.00 55.34  ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 241.382 245.085 177.797 1.00 55.77  ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 239.782 245.202 180.701 1.00 49.75  ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 240.145 246.541 180.414 1.00 49.79  ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 239.429 243.957 177.854 1.00 60.18  ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 239.133 244.136 176.441 1.00 54.98  ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 238.103 245.245 176.254 1.00 56.13  ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 237.481 245.724 177.205 1.00 57.43  ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 238.639 242.825 175.820 1.00 52.74  ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 237.578 242.143 176.658 1.00 54.58  ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 236.479 242.665 176.833 1.00 58.15  ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 237.904 240.967 177.182 1.00 52.46  ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 237.932 245.654 174.995 1.00 56.72  ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 237.038 246.767 174.691 1.00 52.78  ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 235.586 246.420 174.991 1.00 51.90  ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 234.822 247.275 175.453 1.00 52.76  ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 237.203 247.185 173.232 1.00 53.06  ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 235.183 245.174 174.727 1.00 55.32  ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 233.799 244.777 174.969 1.00 50.32  ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 233.446 244.860 176.449 1.00 54.25  ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 232.354 245.316 176.809 1.00 57.68  ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 233.559 243.363 174.439 1.00 54.53  ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 233.917 243.223 172.973 1.00 63.39  ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 233.254 243.870 172.134 1.00 64.24  ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 234.860 242.467 172.659 1.00 59.71  ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 234.355 244.420 177.322 1.00 60.18  ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 234.099 244.502 178.757 1.00 53.06  ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 234.019 245.950 179.220 1.00 47.56  ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 233.195 246.291 180.077 1.00 55.02  ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 235.184 243.752 179.529 1.00 54.00  ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 234.673 243.024 180.759 1.00 56.59  ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 235.685 242.047 181.321 1.00 65.73  ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 236.814 241.984 180.790 1.00 58.87  ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 235.347 241.335 182.289 1.00 63.03  ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 234.872 246.817 178.668 1.00 44.37  ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 234.871 248.217 179.077 1.00 43.20  ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 233.575 248.913 178.679 1.00 46.97  ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 233.062 249.755 179.425 1.00 52.44  ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 236.082 248.938 178.484 1.00 43.00  ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 237.326 248.851 179.358 1.00 50.13  ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 238.568 249.374 178.653 1.00 44.99  ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 238.675 248.911 177.275 1.00 47.82  ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 239.800 248.920 176.573 1.00 46.46  ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 240.933 249.366 177.089 1.00 55.40  ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 239.788 248.471 175.321 1.00 46.93  ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 233.026 248.574 177.510 1.00 52.16  ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 231.758 249.165 177.089 1.00 50.34  ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 230.636 248.794 178.050 1.00 48.98  ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 229.779 249.625 178.374 1.00 52.18  ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 231.412 248.723 175.667 1.00 54.42  ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 232.320 249.197 174.533 1.00 61.53  ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 231.902 248.548 173.224 1.00 56.87  ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 232.293 250.712 174.417 1.00 55.22  ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 230.619 247.541 178.509 1.00 48.14  ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 229.608 247.121 179.473 1.00 47.53  ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 229.781 247.844 180.803 1.00 53.06  ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 228.802 248.095 181.514 1.00 57.78  ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 229.671 245.606 179.672 1.00 50.52  ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 228.522 245.038 180.488 1.00 55.62  ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 228.737 243.567 180.802 1.00 56.68  ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 229.814 243.365 181.763 1.00 55.95  ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 230.912 242.661 181.522 1.00 60.87  ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 231.114 242.076 180.353 1.00 55.63  ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 231.828 242.540 182.478 1.00 58.70  ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 231.023 248.183 181.157 1.00 48.88  ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 231.274 248.870 182.420 1.00 43.75  ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 230.673 250.271 182.416 1.00 46.54  ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 229.991 250.668 183.367 1.00 56.90  ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 232.777 248.922 182.697 1.00 48.56  ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 233.355 247.598 183.096 1.00 43.89  ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 232.669 246.506 183.541 1.00 41.91  ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 234.739 247.227 183.089 1.00 45.14  ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 233.539 245.478 183.811 1.00 41.80  ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 234.816 245.895 183.542 1.00 49.63  ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 235.920 247.890 182.745 1.00 39.89  ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 236.026 245.214 183.658 1.00 43.35  ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 237.120 247.213 182.860 1.00 39.54  ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 237.163 245.889 183.313 1.00 41.24  ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 230.909 251.037 181.346 1.00 52.41  ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 230.313 252.367 181.252 1.00 56.63  ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 228.795 252.286 181.151 1.00 54.93  ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 228.086 253.176 181.634 1.00 54.40  ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 230.894 253.134 180.062 1.00 51.55  ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 232.087 254.018 180.409 1.00 57.04  ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 233.380 253.246 180.569 1.00 61.71  ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 233.703 252.378 179.760 1.00 61.18  ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 234.130 253.560 181.619 1.00 58.08  ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 228.278 251.228 180.521 1.00 51.15  ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 226.835 251.011 180.517 1.00 49.60  ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 226.308 250.767 181.924 1.00 56.07  ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 225.132 251.031 182.203 1.00 61.44  ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 226.480 249.839 179.603 1.00 43.92  ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 227.157 250.267 182.820 1.00 50.54  ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 226.807 250.059 184.218 1.00 45.05  ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 227.114 251.272 185.089 1.00 47.43  ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 227.353 251.105 186.290 1.00 53.41  ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 227.535 248.829 184.765 1.00 45.56  ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 227.189 247.666 184.033 1.00 49.53  ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 227.133 252.471 184.502 1.00 48.95  ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 227.341 253.727 185.218 1.00 52.37  ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 228.731 253.819 185.836 1.00 53.28  ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 228.902 254.423 186.900 1.00 60.47  ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 226.271 253.916 186.298 1.00 55.74  ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 226.484 255.116 187.020 1.00 61.38  ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 229.731 253.226 185.184 1.00 45.90  ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 231.104 253.417 185.642 1.00 52.55  ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 231.667 254.708 185.061 1.00 59.28  ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 231.551 254.934 183.850 1.00 59.60  ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 231.989 252.247 185.236 1.00 50.95  ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 233.465 252.374 185.621 1.00 47.01  ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 233.664 252.089 187.102 1.00 48.66  ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 234.334 251.459 184.774 1.00 47.65  ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 232.259 255.576 185.881 1.00 60.14  ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 232.845 256.812 185.349 1.00 57.08  ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 233.946 256.518 184.339 1.00 54.04  ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 234.697 255.549 184.469 1.00 60.91  ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 233.400 257.507 186.597 1.00 57.27  ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 232.594 256.952 187.725 1.00 54.14  ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 232.317 255.525 187.351 1.00 56.97  ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 234.033 257.371 183.319 1.00 57.88  ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 235.022 257.218 182.253 1.00 60.72  ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 236.338 257.818 182.728 1.00 60.50  ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 236.642 258.986 182.480 1.00 62.81  ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 234.534 257.873 180.967 1.00 58.21  ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 237.131 257.005 183.423 1.00 55.57  ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 238.423 257.440 183.931 1.00 54.47  ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 239.372 256.253 183.955 1.00 57.20  ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 238.944 255.098 184.033 1.00 60.23  ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 238.302 258.052 185.331 1.00 54.34  ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 239.467 258.959 185.672 1.00 64.01  ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 239.988 259.630 184.756 1.00 64.24  ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 239.862 259.001 186.856 1.00 62.86  ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 240.672 256.550 183.882 1.00 51.31  ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 241.674 255.491 183.931 1.00 46.71  ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 241.719 254.833 185.304 1.00 50.28  ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 241.840 253.607 185.407 1.00 55.36  ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 243.046 256.048 183.555 1.00 54.50  ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 243.241 256.153 182.056 1.00 60.85  ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 242.315 255.775 181.307 1.00 58.73  ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 244.319 256.613 181.625 1.00 58.90  ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 241.630 255.631 186.371 1.00 41.90  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 241.617 255.065 187.716 1.00 34.42  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 240.355 254.245 187.953 1.00 44.99  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 240.407 253.176 188.573 1.00 55.14  ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 241.747 256.179 188.756 1.00 42.48  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 241.925 255.771 190.222 1.00 41.00  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 242.905 256.702 190.913 1.00 44.50  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 240.593 255.771 190.957 1.00 41.44  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 239.209 254.734 187.474 1.00 54.22  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 237.970 253.973 187.600 1.00 45.00  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 238.034 252.682 186.794 1.00 41.23  ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 237.546 251.637 187.242 1.00 58.15  ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 236.782 254.826 187.158 1.00 48.33  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 236.196 255.988 188.411 1.00 69.78  ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 238.624 252.736 185.597 1.00 35.45  ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 238.793 251.525 184.800 1.00 35.20  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 239.705 250.528 185.504 1.00 39.62  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 239.433 249.322 185.507 1.00 52.22  ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 239.347 251.878 183.419 1.00 50.52  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 238.457 252.791 182.765 1.00 48.55  ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 239.493 250.627 182.566 1.00 43.43  ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 240.792 251.014 186.108 1.00 44.77  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 241.663 250.136 186.885 1.00 35.75  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 240.920 249.545 188.075 1.00 36.08  ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 241.089 248.364 188.399 1.00 44.51  ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 242.899 250.902 187.354 1.00 35.33  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 243.923 251.161 186.265 1.00 48.49  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 244.852 252.310 186.602 1.00 52.31  ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 244.694 252.904 187.689 1.00 50.81  ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 245.740 252.620 185.780 1.00 53.92  ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 240.099 250.357 188.744 1.00 38.84  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 239.309 249.858 189.863 1.00 38.73  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 238.289 248.825 189.402 1.00 40.94  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 238.031 247.840 190.104 1.00 46.44  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 238.619 251.023 190.572 1.00 32.12  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 239.589 251.885 191.352 1.00 33.43  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 240.798 251.659 191.327 1.00 38.01  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 239.062 252.881 192.053 1.00 39.88  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 237.692 249.036 188.227 1.00 37.56  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 236.749 248.059 187.691 1.00 27.15  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 237.448 246.751 187.344 1.00 35.90  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 236.867 245.670 187.493 1.00 42.84  ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 236.039 248.632 186.465 1.00 37.07  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 238.692 246.831 186.868 1.00 36.93  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 239.467 245.624 186.593 1.00 32.24  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 239.713 244.847 187.879 1.00 34.56  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 239.588 243.617 187.915 1.00 44.20  ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 240.788 245.988 185.889 1.00 35.11  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 240.522 246.453 184.457 1.00 36.02  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 241.747 244.808 185.900 1.00 35.63  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 241.696 247.158 183.818 1.00 34.46  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 240.064 245.554 188.957 1.00 40.26  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 240.321 244.893 190.232 1.00 35.00  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 239.066 244.237 190.789 1.00 34.38  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 239.153 243.204 191.462 1.00 39.23  ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 240.888 245.899 191.231 1.00 33.01  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 242.294 246.361 190.901 1.00 38.76  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 242.862 247.669 191.996 1.00 50.08  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 244.048 248.501 190.944 1.00 30.02  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 237.894 244.818 190.524 1.00 40.55  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 236.637 244.220 190.955 1.00 36.60  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 236.288 242.961 190.173 1.00 42.02  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 235.331 242.272 190.539 1.00 45.96  ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 235.502 245.237 190.832 1.00 33.30  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 235.515 246.396 191.830 1.00 33.77  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 234.565 247.497 191.388 1.00 36.79  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 235.158 245.906 193.223 1.00 43.79  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 237.025 242.656 189.107 1.00 41.88  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 236.799 241.465 188.297 1.00 38.77  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 237.832 240.373 188.543 1.00 42.37  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 237.466 239.202 188.681 1.00 46.70  ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 236.794 241.836 186.810 1.00 37.03  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 237.174 240.698 185.877 1.00 39.89  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 237.625 241.217 184.522 1.00 42.63  ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 238.684 242.298 184.666 1.00 51.58  ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 239.255 242.696 183.349 1.00 47.42  ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 239.115 240.729 188.611 1.00 34.68  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 240.197 239.764 188.756 1.00 37.96  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 240.670 239.623 190.198 1.00 42.49  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 241.798 239.177 190.431 1.00 55.78  ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 241.372 240.152 187.858 1.00 32.18  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 241.061 240.120 186.374 1.00 34.44  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 242.171 240.774 185.569 1.00 36.55  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 241.913 240.720 184.136 1.00 41.72  ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 242.148 239.663 183.371 1.00 45.35  ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 242.646 238.545 183.873 1.00 46.76  ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 241.877 239.729 182.071 1.00 39.92  ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 239.838 239.995 191.165 1.00 38.31  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 240.244 239.934 192.561 1.00 36.78  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 240.398 238.489 193.022 1.00 40.66  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 239.684 237.587 192.577 1.00 41.18  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 239.227 240.657 193.446 1.00 35.35  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 237.862 240.027 193.446 1.00 40.92  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 236.909 240.415 192.521 1.00 40.63  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 237.526 239.059 194.379 1.00 41.85  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 235.654 239.841 192.518 1.00 38.67  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 236.274 238.483 194.380 1.00 41.59  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 235.337 238.875 193.449 1.00 42.15  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 241.353 238.276 193.926 1.00 40.20  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 241.519 237.002 194.613 1.00 39.99  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 240.877 237.019 195.993 1.00 45.78  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 240.132 236.100 196.346 1.00 46.45  ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 243.008 236.655 194.728 1.00 39.77  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 243.571 236.082 193.445 1.00 51.63  ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 242.899 235.331 192.738 1.00 54.72  ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 244.807 236.444 193.131 1.00 53.80  ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 241.154 238.052 196.779 1.00 38.54  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 240.450 238.295 198.026 1.00 32.54  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 239.252 239.197 197.766 1.00 39.48  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 239.251 240.003 196.831 1.00 46.17  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 241.380 238.930 199.059 1.00 35.13  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 242.472 237.998 199.554 1.00 39.20  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 243.564 238.757 200.284 1.00 38.42  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 244.118 239.834 199.471 1.00 33.99  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 244.884 240.808 199.941 1.00 40.90  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 245.211 240.874 201.221 1.00 31.49  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 245.335 241.740 199.106 1.00 42.11  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 238.228 239.052 198.598 1.00 38.14  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 236.983 239.773 198.376 1.00 35.49  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 237.219 241.277 198.494 1.00 37.89  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 237.834 241.729 199.469 1.00 50.10  ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 235.921 239.313 199.371 1.00 40.33  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 235.440 237.904 199.112 1.00 40.60  ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 234.894 237.552 197.885 1.00 43.18  ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 235.542 236.923 200.089 1.00 37.97  ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 234.456 236.265 197.640 1.00 39.41  ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 235.106 235.633 199.853 1.00 41.20  ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 234.565 235.310 198.627 1.00 47.49  ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 234.130 234.027 198.386 1.00 53.26  ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 236.757 242.075 197.534 1.00 30.53  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 237.131 243.493 197.507 1.00 31.91  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 236.480 244.293 198.622 1.00 35.91  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 235.396 243.966 199.111 1.00 43.63  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 236.640 243.968 196.131 1.00 35.37  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 236.184 242.731 195.398 1.00 36.41  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 235.843 241.723 196.438 1.00 38.80  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 237.167 245.362 199.021 1.00 34.56  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 236.631 246.371 199.929 1.00 32.41  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 236.618 247.694 199.176 1.00 41.65  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 237.678 248.254 198.877 1.00 46.99  ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 237.456 246.463 201.212 1.00 33.23  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 236.823 247.204 202.394 1.00 35.51  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 237.284 246.604 203.710 1.00 37.57  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 237.144 248.691 202.354 1.00 35.80  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 235.424 248.190 198.872 1.00 46.37  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 235.256 249.366 198.027 1.00 33.63  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 235.212 250.612 198.900 1.00 41.87  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 234.481 250.661 199.895 1.00 48.16  ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 233.984 249.248 197.172 1.00 33.25  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 234.058 248.011 196.277 1.00 40.55  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 233.783 250.501 196.337 1.00 36.71  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 232.747 247.660 195.615 1.00 41.74  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 235.999 251.619 198.531 1.00 43.40  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 236.006 252.912 199.206 1.00 42.03  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 235.561 253.947 198.180 1.00 48.58  ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 236.353 254.373 197.331 1.00 54.78  ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 237.380 253.260 199.789 1.00 42.24  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 237.963 252.059 200.535 1.00 47.35  ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 237.275 254.463 200.713 1.00 42.61  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 239.389 252.260 200.994 1.00 42.67  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 234.296 254.354 198.251 1.00 53.54  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 233.742 255.360 197.346 1.00 54.89  ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 232.815 256.281 198.127 1.00 57.94  ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 231.643 255.942 198.360 1.00 63.28  ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 233.002 254.717 196.175 1.00 51.15  ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 232.944 255.621 194.959 1.00 64.35  ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 233.649 256.653 194.950 1.00 65.77  ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 232.191 255.307 194.014 1.00 66.25  ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 233.303 257.446 198.558 1.00 56.50  ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 232.409 258.409 199.220 1.00 55.66  ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 231.274 258.884 198.331 1.00 55.70  ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 230.183 259.176 198.837 1.00 55.77  ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 233.352 259.560 199.600 1.00 56.49  ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 234.531 259.411 198.694 1.00 55.78  ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 234.686 257.942 198.461 1.00 50.63  ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 231.496 258.971 197.017 1.00 60.85  ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 230.441 259.419 196.115 1.00 60.36  ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 229.364 258.357 195.932 1.00 61.74  ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 228.217 258.690 195.614 1.00 60.96  ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 231.036 259.807 194.762 1.00 57.12  ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 231.413 258.658 194.024 1.00 62.66  ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 229.709 257.086 196.124 1.00 58.63  ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 228.759 256.006 195.967 1.00 57.45  ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 228.546 255.530 194.548 1.00 59.08  ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 227.679 254.675 194.325 1.00 57.79  ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 229.303 256.052 193.579 1.00 64.65  ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 229.136 255.618 192.197 1.00 62.01  ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 229.587 254.177 191.999 1.00 64.18  ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 229.010 253.456 191.177 1.00 68.43  ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 229.901 256.549 191.256 1.00 62.23  ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 229.052 257.663 190.666 1.00 66.94  ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 229.728 258.357 189.501 1.00 74.11  ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 230.729 259.052 189.674 1.00 69.37  ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 229.183 258.171 188.304 1.00 68.37  ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 230.615 253.742 192.732 1.00 54.76  ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 231.060 252.357 192.631 1.00 48.23  ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 230.002 251.397 193.159 1.00 49.81  ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 229.849 250.286 192.639 1.00 59.46  ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 232.375 252.170 193.384 1.00 50.65  ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 229.273 251.805 194.200 1.00 54.92  ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 228.201 250.968 194.729 1.00 51.08  ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 227.108 250.755 193.689 1.00 56.07  ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 226.610 249.635 193.521 1.00 64.43  ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 227.624 251.599 195.997 1.00 58.37  ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 228.656 251.719 196.984 1.00 61.19  ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 226.495 250.750 196.554 1.00 57.97  ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 226.725 251.817 192.976 1.00 56.86  ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 225.726 251.678 191.922 1.00 55.68  ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 226.257 250.842 190.765 1.00 57.70  ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 225.513 250.061 190.160 1.00 62.76  ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 225.286 253.057 191.431 1.00 57.33  ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 224.082 253.620 192.168 1.00 65.88  ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 222.893 252.680 192.143 1.00 70.60  ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 222.458 252.298 191.036 1.00 66.79  ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 222.392 252.322 193.230 1.00 65.52  ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 227.542 250.998 190.438 1.00 50.55  ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 228.140 250.203 189.370 1.00 46.08  ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 228.136 248.720 189.719 1.00 44.99  ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 227.874 247.872 188.858 1.00 51.66  ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 229.563 250.689 189.092 1.00 47.50  ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 230.429 249.674 188.399 1.00 46.46  ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 230.261 249.405 187.051 1.00 48.10  ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 231.417 248.996 189.094 1.00 50.17  ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 231.057 248.474 186.412 1.00 52.18  ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 232.216 248.064 188.459 1.00 48.65  ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 232.036 247.804 187.117 1.00 46.68  ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 228.431 248.387 190.978 1.00 49.89  ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 228.445 246.989 191.399 1.00 48.25  ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 227.048 246.388 191.307 1.00 49.26  ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 226.871 245.259 190.832 1.00 57.66  ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 229.029 246.869 192.820 1.00 44.61  ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 230.556 246.933 192.772 1.00 42.61  ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 228.574 245.583 193.487 1.00 47.33  ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 231.190 245.782 192.024 1.00 45.14  ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 226.034 247.131 191.758 1.00 48.12  ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 224.664 246.632 191.688 1.00 44.87  ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 224.212 246.449 190.244 1.00 51.38  ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 223.543 245.463 189.916 1.00 55.93  ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 223.720 247.578 192.431 1.00 48.25  ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 224.038 247.737 193.908 1.00 53.19  ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 223.327 246.424 194.919 1.00 68.32  ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 221.605 246.524 194.440 1.00 54.47  ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 224.562 247.394 189.368 1.00 50.53  ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 224.187 247.272 187.963 1.00 43.79  ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 224.924 246.120 187.290 1.00 43.58  ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 224.352 245.418 186.448 1.00 48.25  ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 224.462 248.584 187.230 1.00 50.57  ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 223.411 249.640 187.510 1.00 56.36  ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 222.227 249.332 187.648 1.00 57.30  ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 223.840 250.893 187.595 1.00 56.87  ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 226.194 245.913 187.644 1.00 48.37  ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 226.974 244.849 187.021 1.00 46.60  ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 226.470 243.468 187.418 1.00 49.42  ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 226.504 242.540 186.602 1.00 53.60  ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 228.452 245.000 187.384 1.00 43.73  ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 229.391 244.176 186.520 1.00 49.07  ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 229.640 244.804 185.162 1.00 56.52  ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 229.223 245.962 184.954 1.00 56.74  ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 230.252 244.137 184.302 1.00 57.42  ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 226.004 243.309 188.657 1.00 53.30  ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 225.517 242.028 189.154 1.00 52.79  ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 224.000 242.006 189.307 1.00 54.35  ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 223.470 241.206 190.085 1.00 53.09  ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 226.190 241.687 190.485 1.00 49.23  ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 227.651 241.317 190.357 1.00 48.61  ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 228.627 242.296 190.225 1.00 48.19  ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 228.055 239.989 190.369 1.00 54.72  ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 229.962 241.963 190.107 1.00 50.12  ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 229.388 239.646 190.252 1.00 52.33  ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 230.338 240.637 190.121 1.00 52.75  ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 231.667 240.301 190.005 1.00 52.04  ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 223.292 242.876 188.582 1.00 59.79  ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 221.836 242.916 188.682 1.00 56.70  ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 221.207 241.626 188.169 1.00 61.47  ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 220.247 241.117 188.761 1.00 62.28  ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 221.295 244.122 187.913 1.00 59.86  ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 219.780 244.159 187.788 1.00 57.87  ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 219.321 245.345 186.953 1.00 58.09  ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 219.816 246.665 187.527 1.00 58.89  ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 219.693 246.722 189.011 1.00 62.34  ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 221.733 241.083 187.069 1.00 66.61  ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 221.173 239.858 186.507 1.00 66.83  ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 221.383 238.672 187.440 1.00 68.12  ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 220.571 237.740 187.465 1.00 68.73  ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 221.788 239.579 185.136 1.00 66.39  ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 223.302 239.673 185.145 1.00 70.45  ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 223.874 239.991 186.209 1.00 70.87  ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 223.919 239.428 184.088 1.00 67.99  ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 222.466 238.687 188.214 1.00 61.82  ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 222.766 237.613 189.153 1.00 59.41  ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 222.045 237.774 190.486 1.00 62.50  ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 222.346 237.031 191.427 1.00 66.42  ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 224.277 237.523 189.382 1.00 59.10  ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 225.072 237.231 188.119 1.00 60.34  ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 226.509 236.849 188.434 1.00 63.18  ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 226.611 236.020 189.628 1.00 70.60  ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 227.752 235.704 190.226 1.00 70.06  ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 228.915 236.131 189.764 1.00 66.19  ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 227.725 234.940 191.314 1.00 63.37  ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 221.112 238.724 190.582 1.00 61.55  ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 220.311 238.954 191.785 1.00 65.32  ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 221.196 239.313 192.981 1.00 65.24  ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 221.223 238.624 194.003 1.00 64.35  ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 219.424 237.743 192.094 1.00 66.76  ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 218.481 237.361 190.967 1.00 66.42  ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 217.333 238.350 190.851 1.00 68.06  ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 216.263 237.843 189.899 1.00 67.30  ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 216.418 238.420 188.535 1.00 64.03  ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 221.927 240.418 192.831 1.00 57.48  ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 222.739 240.923 193.929 1.00 51.43  ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 221.841 241.629 194.940 1.00 55.30  ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 220.804 242.210 194.592 1.00 56.32  ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 223.845 241.858 193.402 1.00 47.47  ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 224.852 242.183 194.507 1.00 50.02  ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 223.247 243.133 192.823 1.00 54.79  ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 226.004 243.041 194.048 1.00 54.42  ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 222.232 241.565 196.210 1.00 55.80  ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 221.457 242.133 197.304 1.00 53.08  ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 222.320 243.115 198.082 1.00 50.59  ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 223.496 242.841 198.345 1.00 54.41  ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 220.938 241.036 198.239 1.00 59.91  ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 220.388 239.964 197.463 1.00 59.30  ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 219.864 241.587 199.166 1.00 55.12  ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 221.738 244.256 198.442 1.00 56.50  ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 222.411 245.236 199.281 1.00 55.17  ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 222.040 245.003 200.739 1.00 59.40  ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 220.858 244.881 201.074 1.00 64.29  ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 222.040 246.663 198.874 1.00 55.53  ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 222.770 247.726 199.682 1.00 56.00  ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 222.444 249.135 199.217 1.00 57.24  ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 222.966 249.425 197.888 1.00 63.40  ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 222.675 250.518 197.195 1.00 66.63  ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 221.875 251.452 197.682 1.00 64.93  ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 223.202 250.678 195.985 1.00 59.27  ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 223.053 244.943 201.600 1.00 49.66  ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 222.849 244.808 203.033 1.00 51.22  ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 223.917 245.617 203.753 1.00 53.61  ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 224.842 246.154 203.137 1.00 59.64  ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 222.882 243.339 203.477 1.00 50.60  ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 222.523 243.247 204.861 1.00 54.46  ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 224.267 242.752 203.277 1.00 55.82  ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 223.778 245.712 205.072 1.00 56.66  ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 224.707 246.473 205.890 1.00 53.20  ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 225.064 245.670 207.131 1.00 56.67  ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 224.292 244.821 207.583 1.00 65.30  ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 224.120 247.833 206.294 1.00 54.59  ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 224.944 248.483 207.245 1.00 61.42  ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 226.252 245.945 207.676 1.00 49.74  ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 226.665 245.288 208.911 1.00 49.96  ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 225.766 245.676 210.076 1.00 55.26  ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 225.584 244.887 211.010 1.00 56.78  ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 228.121 245.631 209.231 1.00 54.21  ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 229.122 244.838 208.440 1.00 56.54  ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 229.194 243.462 208.569 1.00 56.25  ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 230.001 245.471 207.577 1.00 55.61  ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 230.118 242.731 207.847 1.00 52.51  ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 230.928 244.745 206.853 1.00 52.61  ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 230.985 243.374 206.988 1.00 50.03  ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 225.197 246.884 210.041 1.00 67.40  ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 224.323 247.335 211.117 1.00 70.57  ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 222.957 246.664 211.067 1.00 71.42  ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 222.290 246.551 212.102 1.00 71.93  ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 224.148 248.855 211.061 1.00 66.12  ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 225.215 249.757 211.693 1.00 68.74  ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 225.290 249.537 213.199 1.00 70.95  ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 226.579 249.580 211.044 1.00 64.02  ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 222.524 246.226 209.885 1.00 69.18  ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 221.200 245.637 209.735 1.00 68.59  ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 221.083 244.350 210.541 1.00 73.23  ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 221.996 243.520 210.556 1.00 77.13  ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 220.911 245.360 208.259 1.00 69.21  ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 220.744 246.631 207.450 1.00 78.31  ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 220.933 247.727 208.017 1.00 79.57  ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 220.423 246.533 206.247 1.00 74.46  ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 219.942 244.190 211.216 1.00 73.70  ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 219.691 242.977 211.984 1.00 78.11  ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 219.475 241.763 211.091 1.00 78.63  ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 219.600 240.629 211.566 1.00 77.19  ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 218.480 243.175 212.896 1.00 79.15  ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 218.750 244.159 214.017 1.00 80.25  ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 219.918 244.269 214.444 1.00 75.73  ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 217.795 244.824 214.470 1.00 80.95  ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 219.157 241.972 209.816 1.00 68.00  ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 218.965 240.890 208.862 1.00 65.48  ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 220.233 240.558 208.088 1.00 65.25  ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 220.168 239.809 207.108 1.00 69.17  ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 217.837 241.239 207.888 1.00 64.78  ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 221.380 241.107 208.499 1.00 56.52  ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 222.632 240.824 207.806 1.00 52.32  ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 222.990 239.345 207.888 1.00 57.05  ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 223.439 238.753 206.900 1.00 64.91  ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 223.757 241.679 208.387 1.00 50.88  ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 225.133 241.198 208.024 1.00 52.56  ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 225.559 241.201 206.706 1.00 58.73  ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 226.000 240.739 209.001 1.00 52.01  ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 226.824 240.758 206.371 1.00 58.10  ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 227.266 240.294 208.672 1.00 51.64  ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 227.678 240.304 207.355 1.00 54.75  ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 222.806 238.735 209.061 1.00 57.37  ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 223.130 237.320 209.217 1.00 55.53  ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 222.259 236.451 208.319 1.00 56.08  ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 222.751 235.504 207.694 1.00 59.49  ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 222.979 236.906 210.680 1.00 60.58  ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 223.951 237.595 211.622 1.00 61.05  ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 225.321 236.939 211.581 1.00 59.04  ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 225.242 235.494 211.760 1.00 62.48  ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 225.645 234.851 212.847 1.00 65.41  ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 226.161 235.496 213.881 1.00 61.68  ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 225.527 233.527 212.899 1.00 62.55  ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 220.961 236.752 208.247 1.00 56.07  ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 220.075 235.996 207.367 1.00 53.30  ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 220.440 236.203 205.902 1.00 54.38  ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 220.450 235.246 205.119 1.00 57.70  ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 218.621 236.393 207.618 1.00 61.24  ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 217.608 235.504 206.916 1.00 64.04  ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 216.269 236.207 206.758 1.00 62.98  ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 216.423 237.526 206.019 1.00 63.39  ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 216.706 237.321 204.572 1.00 62.54  ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 220.735 237.446 205.513 1.00 51.57  ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 221.111 237.720 204.129 1.00 45.35  ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 222.431 237.049 203.772 1.00 51.34  ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 222.590 236.526 202.662 1.00 52.25  ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 221.196 239.228 203.898 1.00 47.58  ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 219.832 239.881 203.813 1.00 58.60  ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 219.061 239.616 202.892 1.00 60.60  ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 219.527 240.741 204.777 1.00 57.60  ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 223.392 237.061 204.698 1.00 52.74  ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 224.672 236.407 204.447 1.00 43.94  ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 224.502 234.900 204.296 1.00 52.43  ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 225.142 234.279 203.440 1.00 61.64  ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 225.652 236.730 205.573 1.00 43.21  ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 227.041 236.096 205.498 1.00 52.32  ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 227.720 236.433 204.180 1.00 53.46  ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 227.889 236.554 206.671 1.00 52.33  ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 223.644 234.295 205.122 1.00 53.55  ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 223.412 232.857 205.030 1.00 47.24  ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 222.804 232.478 203.685 1.00 51.94  ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 223.201 231.478 203.076 1.00 52.49  ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 222.507 232.398 206.172 1.00 49.89  ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 223.204 232.289 207.516 1.00 58.33  ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 222.253 231.918 208.637 1.00 62.17  ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 221.472 230.960 208.462 1.00 61.96  ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 222.288 232.585 209.693 1.00 59.76  ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 221.833 233.262 203.210 1.00 50.72  ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 221.204 232.968 201.927 1.00 47.05  ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 222.196 233.108 200.778 1.00 50.92  ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 222.193 232.297 199.845 1.00 56.32  ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 220.001 233.885 201.711 1.00 49.67  ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 219.161 233.897 202.852 1.00 56.22  ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 223.046 234.136 200.825 1.00 49.73  ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 224.027 234.334 199.763 1.00 44.09  ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 225.027 233.187 199.712 1.00 48.27  ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 225.380 232.709 198.627 1.00 53.97  ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 224.746 235.668 199.955 1.00 43.01  ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 225.503 232.736 200.874 1.00 44.92  ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 226.426 231.606 200.907 1.00 42.22  ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 225.753 230.326 200.429 1.00 49.07  ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 226.357 229.536 199.694 1.00 55.23  ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 226.982 231.421 202.319 1.00 44.38  ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 227.907 232.512 202.860 1.00 42.89  ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 227.795 232.601 204.372 1.00 42.45  ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 229.344 232.251 202.447 1.00 51.14  ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 224.502 230.103 200.838 1.00 54.83  ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 223.823 228.855 200.506 1.00 49.22  ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 223.405 228.815 199.040 1.00 50.82  ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 223.576 227.790 198.370 1.00 54.69  ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 222.609 228.668 201.415 1.00 47.09  ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 221.833 227.387 201.170 1.00 50.59  ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 220.821 227.146 202.276 1.00 52.74  ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 221.460 227.007 203.579 1.00 53.47  ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 221.255 227.822 204.605 1.00 58.80  ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 220.431 228.853 204.514 1.00 56.53  ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 221.893 227.597 205.750 1.00 58.43  ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 222.857 229.913 198.526 1.00 46.29  ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 222.349 229.960 197.162 1.00 49.05  ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 223.359 230.502 196.160 1.00 55.60  ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 223.056 230.548 194.963 1.00 58.29  ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 221.069 230.800 197.107 1.00 49.72  ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 219.944 230.243 197.930 1.00 55.54  ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 219.656 228.889 197.904 1.00 54.47  ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 219.176 231.070 198.731 1.00 59.10  ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 218.623 228.371 198.660 1.00 55.02  ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 218.141 230.558 199.490 1.00 53.93  ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 217.864 229.206 199.454 1.00 57.38  ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 224.543 230.904 196.609 1.00 50.67  ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 225.549 231.431 195.703 1.00 48.21  ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 225.165 232.728 195.025 1.00 49.99  ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 225.437 232.903 193.831 1.00 56.86  ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 224.537 233.643 195.757 1.00 50.44  ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 224.165 234.919 195.165 1.00 52.84  ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 225.174 235.997 195.538 1.00 55.77  ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 225.723 235.976 196.645 1.00 54.61  ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 222.774 235.350 195.633 1.00 51.55  ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 221.685 234.407 195.167 1.00 58.50  ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 221.854 233.677 194.190 1.00 58.30  ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 220.556 234.415 195.867 1.00 51.51  ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 225.447 236.936 194.633 1.00 54.85  ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 226.321 238.060 194.986 1.00 47.43  ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 225.727 238.880 196.120 1.00 51.34  ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 224.513 239.079 196.199 1.00 54.36  ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 226.408 238.870 193.686 1.00 38.73  ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 225.257 238.410 192.855 1.00 47.50  ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 225.016 236.985 193.227 1.00 52.00  ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 226.598 239.354 197.005 1.00 44.22  ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 226.189 240.132 198.164 1.00 38.38  ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 227.035 241.391 198.256 1.00 41.91  ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 228.240 241.362 197.990 1.00 48.80  ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 226.317 239.316 199.456 1.00 47.15  ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 225.683 239.916 200.713 1.00 41.29  ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 224.167 239.858 200.630 1.00 44.26  ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 226.182 239.200 201.957 1.00 42.12  ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 226.397 242.497 198.628 1.00 38.50  ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 227.075 243.773 198.820 1.00 39.50  ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 226.780 244.257 200.229 1.00 48.55  ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 225.615 244.468 200.583 1.00 60.33  ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 226.619 244.801 197.782 1.00 41.08  ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 227.040 246.254 198.004 1.00 45.88  ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 228.551 246.397 197.929 1.00 45.63  ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 226.365 247.152 196.984 1.00 51.26  ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 227.827 244.434 201.029 1.00 42.21  ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 227.696 244.805 202.433 1.00 38.22  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 228.297 246.192 202.613 1.00 46.48  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 229.464 246.421 202.272 1.00 52.44  ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 228.378 243.785 203.356 1.00 42.69  ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 228.144 244.153 204.810 1.00 46.26  ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 227.876 242.381 203.064 1.00 45.31  ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 227.502 247.113 203.150 1.00 47.52  ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 227.950 248.473 203.393 1.00 44.21  ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 228.345 248.643 204.859 1.00 51.69  ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 228.194 247.736 205.681 1.00 58.91  ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 226.862 249.469 202.998 1.00 48.08  ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 226.256 249.215 201.631 1.00 56.97  ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 225.192 250.230 201.270 1.00 61.60  ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 225.295 250.923 200.259 1.00 61.11  ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 224.159 250.325 202.101 1.00 55.78  ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 228.860 249.831 205.187 1.00 54.05  ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 229.276 250.174 206.548 1.00 52.08  ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 230.311 249.180 207.075 1.00 55.16  ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 230.180 248.630 208.170 1.00 62.98  ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 228.070 250.262 207.486 1.00 56.77  ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 226.924 251.055 206.890 1.00 66.94  ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 227.191 252.013 206.134 1.00 72.11  ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 225.755 250.720 207.175 1.00 63.16  ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 231.357 248.953 206.276 1.00 54.69  ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 232.406 248.012 206.655 1.00 50.43  ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 233.247 248.512 207.820 1.00 56.88  ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 233.992 247.727 208.417 1.00 61.19  ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 233.295 247.694 205.433 1.00 49.43  ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 234.231 248.847 205.138 1.00 55.87  ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 234.063 246.392 205.639 1.00 52.93  ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 233.142 249.798 208.170 1.00 56.82  ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 233.794 250.290 209.379 1.00 60.65  ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 233.213 249.655 210.635 1.00 58.22  ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 233.853 249.693 211.692 1.00 57.61  ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 233.685 251.813 209.457 1.00 57.43  ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 232.261 252.340 209.515 1.00 59.06  ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 231.707 252.664 208.141 1.00 64.52  ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 232.308 252.226 207.138 1.00 62.94  ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 230.673 253.360 208.064 1.00 66.52  ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 232.017 249.078 210.541 1.00 50.92  ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 231.406 248.287 211.606 1.00 52.62  ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 231.498 246.798 211.303 1.00 52.19  ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 230.544 246.047 211.526 1.00 50.47  ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 229.956 248.707 211.817 1.00 51.59  ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 229.868 250.074 212.177 1.00 56.30  ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 232.642 246.368 210.771 1.00 53.66  ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 232.808 245.009 210.268 1.00 48.89  ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 232.456 243.972 211.328 1.00 52.59  ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 232.894 244.063 212.478 1.00 50.53  ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 234.248 244.813 209.793 1.00 44.74  ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 234.634 243.378 209.516 1.00 47.27  ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 234.221 242.738 208.356 1.00 48.77  ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 235.426 242.669 210.409 1.00 45.44  ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 234.577 241.428 208.098 1.00 50.01  ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 235.787 241.360 210.160 1.00 47.60  ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 235.360 240.745 209.003 1.00 50.02  ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 235.718 239.441 208.751 1.00 54.79  ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 231.658 242.985 210.927 1.00 58.48  ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 231.239 241.915 211.820 1.00 54.82  ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 232.235 240.766 211.733 1.00 57.20  ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 232.450 240.234 210.635 1.00 57.04  ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 229.847 241.428 211.452 1.00 50.75  ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 229.106 240.824 212.628 1.00 56.88  ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 229.703 240.709 213.718 1.00 59.78  ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 227.921 240.465 212.462 1.00 59.86  ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 232.862 240.357 212.840 1.00 51.15  ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 233.846 239.263 212.770 1.00 48.07  ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 233.264 237.924 212.341 1.00 50.77  ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 234.029 236.961 212.198 1.00 52.00  ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 234.396 239.192 214.202 1.00 49.86  ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 234.122 240.542 214.781 1.00 51.30  ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 232.827 240.984 214.171 1.00 52.51  ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 231.948 237.825 212.135 1.00 50.89  ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 231.352 236.582 211.662 1.00 53.24  ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 231.794 236.260 210.241 1.00 53.96  ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 231.713 235.104 209.811 1.00 60.22  ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 229.812 236.660 211.767 1.00 54.30  ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 229.246 237.593 210.706 1.00 51.09  ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 229.189 235.273 211.670 1.00 55.20  ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 232.278 237.257 209.501 1.00 49.79  ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 232.722 237.069 208.126 1.00 45.88  ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 234.151 236.553 208.023 1.00 48.20  ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 234.620 236.312 206.905 1.00 54.40  ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 232.601 238.386 207.354 1.00 42.08  ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 231.347 238.594 206.506 1.00 41.99  ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 231.370 239.967 205.861 1.00 46.42  ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 231.230 237.511 205.450 1.00 48.36  ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 234.849 236.384 209.147 1.00 40.19  ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 236.251 235.970 209.097 1.00 38.93  ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 236.457 234.635 208.390 1.00 49.55  ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 237.343 234.558 207.521 1.00 53.45  ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 236.830 235.948 210.516 1.00 44.47  ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 237.147 237.334 211.038 1.00 47.24  ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 236.956 238.330 210.343 1.00 51.56  ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 237.634 237.404 212.271 1.00 45.20  ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 235.717 233.561 208.697 1.00 49.25  ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 235.889 232.329 207.909 1.00 42.58  ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 235.529 232.494 206.443 1.00 49.52  ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 236.141 231.843 205.587 1.00 52.01  ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 234.958 231.329 208.611 1.00 45.01  ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 233.966 232.173 209.324 1.00 44.68  ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 234.731 233.372 209.777 1.00 42.99  ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 234.548 233.342 206.129 1.00 49.32  ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 234.143 233.533 204.739 1.00 40.99  ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 235.239 234.247 203.956 1.00 40.31  ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 235.590 233.844 202.841 1.00 49.74  ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 232.810 234.299 204.672 1.00 45.83  ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 232.451 234.617 203.229 1.00 42.99  ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 231.704 233.498 205.340 1.00 47.44  ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 235.794 235.318 204.528 1.00 40.72  ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 236.851 236.058 203.845 1.00 41.71  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 238.120 235.227 203.705 1.00 41.95  ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 238.819 235.335 202.691 1.00 45.11  ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 237.148 237.359 204.590 1.00 36.47  ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 235.988 238.344 204.750 1.00 32.69  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 236.495 239.700 205.208 1.00 37.86  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 235.205 238.473 203.453 1.00 34.34  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 238.433 234.401 204.702 1.00 43.76  ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 239.612 233.548 204.648 1.00 44.58  ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 239.410 232.306 203.791 1.00 47.34  ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 240.379 231.575 203.559 1.00 49.18  ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 240.022 233.130 206.062 1.00 46.01  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 240.804 234.206 206.784 1.00 52.10  ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 241.173 235.221 206.194 1.00 58.13  ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 241.061 233.991 208.068 1.00 47.15  ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 238.185 232.055 203.323 1.00 47.99  ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 237.869 230.889 202.496 1.00 48.73  ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 238.245 229.587 203.201 1.00 53.21  ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 238.770 228.655 202.589 1.00 56.55  ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 238.544 230.982 201.126 1.00 44.98  ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 237.824 231.888 200.143 1.00 48.54  ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 238.332 231.678 198.725 1.00 51.03  ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 237.926 232.753 197.828 1.00 49.18  ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 238.431 233.980 197.844 1.00 56.50  ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 239.381 234.326 198.697 1.00 52.39  ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 237.974 234.881 196.979 1.00 55.33  ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 237.973 229.523 204.503 1.00 50.69  ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 238.244 228.331 205.304 1.00 51.21  ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 237.063 227.380 205.158 1.00 56.63  ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 236.090 227.437 205.911 1.00 59.38  ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 238.485 228.704 206.761 1.00 49.02  ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 239.656 229.645 206.974 1.00 52.51  ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 239.670 230.251 208.362 1.00 61.37  ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 238.746 229.959 209.149 1.00 57.30  ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 240.606 231.019 208.667 1.00 65.62  ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 237.153 226.488 204.176 1.00 60.40  ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 236.081 225.551 203.870 1.00 58.89  ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 236.564 224.133 204.135 1.00 62.66  ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 237.758 223.828 204.034 1.00 70.70  ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 235.591 225.698 202.414 1.00 57.03  ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 234.986 227.073 202.197 1.00 59.14  ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 236.734 225.454 201.441 1.00 58.92  ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 235.620 223.264 204.484 1.00 67.85  ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 235.882 221.849 204.710 1.00 66.67  ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 235.129 221.043 203.661 1.00 68.73  ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 233.906 221.171 203.536 1.00 74.58  ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 235.459 221.431 206.118 1.00 69.80  ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 236.131 220.164 206.620 1.00 72.68  ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 235.844 219.926 208.095 1.00 73.35  ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 234.622 219.159 208.304 1.00 76.98  ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 233.423 219.693 208.494 1.00 75.81  ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 233.246 221.004 208.519 1.00 73.64  ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 232.376 218.891 208.667 1.00 70.96  ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 235.857 220.219 202.912 1.00 70.82  ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 235.273 219.383 201.863 1.00 70.17  ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 235.196 217.957 202.399 1.00 71.16  ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 236.110 217.152 202.215 1.00 70.34  ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 236.095 219.467 200.583 1.00 66.34  ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 236.192 220.869 200.003 1.00 69.08  ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 236.183 220.845 198.483 1.00 71.29  ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 235.813 222.136 197.916 1.00 76.24  ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 236.621 223.185 197.845 1.00 74.60  ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 237.866 223.131 198.290 1.00 71.70  ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 236.170 224.317 197.312 1.00 71.09  ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 234.087 217.643 203.066 1.00 78.43  ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 233.890 216.343 203.693 1.00 83.95  ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 232.585 215.735 203.201 1.00 83.11  ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 231.531 216.374 203.277 1.00 82.98  ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 233.871 216.461 205.221 1.00 83.11  ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 235.057 217.131 205.665 1.00 79.76  ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 233.804 215.082 205.861 1.00 81.45  ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 232.661 214.503 202.707 1.00 81.88  ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 231.472 213.793 202.259 1.00 81.69  ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 230.760 214.446 201.096 1.00 82.79  ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 229.523 214.455 201.054 1.00 80.55  ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 231.512 214.997 200.146 1.00 77.25  ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 230.907 215.635 198.995 1.00 75.67  ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 230.264 216.973 199.268 1.00 79.17  ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 229.543 217.484 198.406 1.00 76.43  ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 230.496 217.557 200.441 1.00 70.06  ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 229.906 218.831 200.825 1.00 63.33  ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 231.009 219.846 201.079 1.00 67.27  ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 231.982 219.548 201.781 1.00 70.04  ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 229.039 218.681 202.078 1.00 63.78  ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 227.899 217.690 201.945 1.00 65.96  ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 227.208 217.484 203.283 1.00 66.15  ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 226.574 218.705 203.764 1.00 64.63  ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 226.251 218.933 205.030 1.00 68.71  ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 226.494 218.040 205.976 1.00 67.93  ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 225.672 220.085 205.355 1.00 67.14  ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 230.856 221.037 200.512 1.00 63.34  ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 231.737 222.164 200.793 1.00 55.28  ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 231.094 222.957 201.922 1.00 56.79  ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 230.100 223.661 201.714 1.00 63.77  ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 231.963 223.034 199.550 1.00 60.72  ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 232.982 224.123 199.846 1.00 63.91  ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 232.416 222.177 198.380 1.00 59.87  ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 231.657 222.845 203.121 1.00 57.64  ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 231.060 223.398 204.328 1.00 59.20  ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 231.832 224.628 204.781 1.00 55.56  ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 233.064 224.596 204.871 1.00 60.16  ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 231.034 222.355 205.448 1.00 60.83  ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 230.045 221.201 205.278 1.00 58.11  ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 230.097 220.272 206.478 1.00 64.29  ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 228.640 221.738 205.077 1.00 60.26  ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 231.105 225.705 205.062 1.00 58.61  ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 231.662 226.914 205.656 1.00 62.05  ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 231.070 227.064 207.051 1.00 62.54  ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 229.860 226.889 207.243 1.00 66.84  ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 231.396 228.155 204.782 1.00 62.14  ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 232.149 229.371 205.326 1.00 61.04  ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 229.903 228.440 204.645 1.00 59.28  ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 233.620 229.381 204.981 1.00 59.22  ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 231.926 227.344 208.031 1.00 65.19  ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 231.499 227.443 209.426 1.00 69.26  ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 231.229 228.908 209.741 1.00 71.87  ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 232.114 229.651 210.166 1.00 77.54  ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 232.549 226.851 210.358 1.00 75.78  ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 232.819 225.497 209.976 1.00 77.54  ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 232.054 226.872 211.798 1.00 69.16  ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 229.985 229.329 209.527 1.00 72.28  ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 229.552 230.686 209.829 1.00 71.29  ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 228.916 230.699 211.213 1.00 73.87  ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 227.858 230.094 211.419 1.00 72.15  ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 228.568 231.195 208.777 1.00 71.13  ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 228.129 232.650 208.938 1.00 74.85  ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 229.160 233.578 208.320 1.00 75.36  ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 226.760 232.876 208.319 1.00 69.55  ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 229.551 231.393 212.148 1.00 82.07  ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 229.070 231.383 213.519 1.00 79.28  ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 229.189 229.991 214.107 1.00 81.28  ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 230.267 229.383 214.112 1.00 82.55  ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 228.073 229.467 214.613 1.00 88.91  ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 228.020 228.125 215.179 1.00 89.66  ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 227.269 227.148 214.279 1.00 88.28  ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 226.801 226.109 214.753 1.00 87.94  ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 227.385 228.161 216.569 1.00 90.85  ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 226.010 228.800 216.565 1.00 93.03  ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 225.901 229.977 216.160 1.00 89.47  ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 225.038 228.126 216.966 1.00 93.39  ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 227.146 227.461 212.991 1.00 82.11  ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 226.396 226.643 212.050 1.00 80.40  ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 227.232 226.393 210.804 1.00 80.76  ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 227.975 227.271 210.357 1.00 81.04  ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 225.071 227.320 211.669 1.00 80.51  ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 224.179 226.494 210.758 1.00 84.63  ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 223.351 227.353 209.823 1.00 86.09  ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 223.356 228.580 209.922 1.00 83.97  ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 222.633 226.711 208.909 1.00 81.80  ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 227.106 225.189 210.248 1.00 76.63  ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 227.779 224.831 209.007 1.00 77.20  ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 226.816 225.003 207.840 1.00 75.96  ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 225.681 224.517 207.887 1.00 77.78  ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 228.296 223.393 209.064 1.00 77.94  ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 229.438 223.224 210.045 1.00 81.76  ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 230.189 224.199 210.260 1.00 82.19  ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 229.588 222.115 210.600 1.00 84.44  ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 227.270 225.694 206.798 1.00 65.39  ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 226.438 226.044 205.654 1.00 68.75  ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 227.084 225.505 204.386 1.00 64.34  ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 228.293 225.660 204.180 1.00 71.79  ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 226.232 227.570 205.551 1.00 66.99  ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 225.694 228.126 206.869 1.00 67.39  ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 225.291 227.908 204.405 1.00 63.86  ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 225.622 229.632 206.906 1.00 69.14  ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 226.277 224.864 203.544 1.00 61.90  ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 226.738 224.412 202.235 1.00 63.16  ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 227.063 225.627 201.375 1.00 61.89  ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 226.168 226.395 201.011 1.00 65.28  ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 225.673 223.543 201.572 1.00 67.20  ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 225.564 222.169 202.205 1.00 70.88  ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 226.612 221.587 202.550 1.00 72.94  ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 224.428 221.672 202.357 1.00 67.56  ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 228.340 225.804 201.048 1.00 59.63  ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 228.789 226.965 200.292 1.00 59.30  ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 228.723 226.680 198.797 1.00 60.38  ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 229.342 225.729 198.310 1.00 59.05  ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 230.213 227.352 200.691 1.00 55.05  ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 230.879 228.414 199.813 1.00 58.72  ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 230.125 229.730 199.893 1.00 56.68  ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 232.333 228.604 200.208 1.00 61.68  ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 227.970 227.507 198.076 1.00 55.92  ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 227.892 227.391 196.627 1.00 55.19  ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 229.116 228.039 195.982 1.00 57.02  ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 229.609 229.059 196.472 1.00 63.71  ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 226.617 228.049 196.106 1.00 53.35  ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 226.643 228.178 194.696 1.00 61.14  ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 229.629 227.468 194.888 1.00 59.17  ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 230.829 228.040 194.256 1.00 59.51  ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 230.611 229.413 193.640 1.00 61.96  ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 231.597 230.111 193.374 1.00 64.00  ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 231.191 227.002 193.185 1.00 59.28  ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 229.906 226.304 192.890 1.00 60.32  ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 229.157 226.259 194.190 1.00 61.74  ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 229.367 229.823 193.406 1.00 55.05  ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 229.078 231.093 192.754 1.00 54.76  ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 228.959 232.255 193.731 1.00 54.26  ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 228.656 233.374 193.303 1.00 54.41  ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 227.790 230.983 191.932 1.00 52.21  ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 226.749 230.391 192.689 1.00 58.89  ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 229.183 232.022 195.021 1.00 44.08  ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 229.067 233.089 196.006 1.00 43.95  ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 230.172 234.122 195.826 1.00 50.12  ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 231.329 233.782 195.561 1.00 52.97  ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 229.116 232.515 197.421 1.00 38.23  ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 229.253 233.560 198.493 1.00 40.28  ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 228.184 234.375 198.825 1.00 52.11  ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 230.452 233.729 199.165 1.00 41.85  ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 228.309 235.337 199.809 1.00 45.35  ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 230.582 234.690 200.148 1.00 40.16  ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 229.508 235.494 200.471 1.00 43.22  ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 229.806 235.391 195.973 1.00 49.36  ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 230.759 236.495 195.948 1.00 42.12  ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 230.205 237.616 196.817 1.00 42.13  ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 228.995 237.860 196.840 1.00 49.51  ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 231.044 236.966 194.503 1.00 40.42  ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 229.794 237.542 193.859 1.00 43.20  ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 232.168 237.983 194.488 1.00 43.31  ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 231.090 238.279 197.556 1.00 36.06  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 230.704 239.336 198.481 1.00 30.56  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 231.581 240.557 198.237 1.00 47.06  ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 232.793 240.434 198.029 1.00 40.47  ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 230.797 238.869 199.952 1.00 32.57  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 230.379 239.990 200.905 1.00 40.16  ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 232.193 238.359 200.279 1.00 38.97  ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 230.210 239.539 202.336 1.00 39.75  ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 230.959 241.734 198.239 1.00 40.82  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 231.658 243.005 198.094 1.00 26.83  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 231.410 243.844 199.339 1.00 36.69  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 230.257 244.048 199.733 1.00 46.71  ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 231.194 243.757 196.844 1.00 33.38  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 231.393 242.995 195.566 1.00 37.97  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 232.577 243.108 194.856 1.00 41.00  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 230.396 242.174 195.069 1.00 34.19  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 232.763 242.412 193.678 1.00 42.80  ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 230.577 241.475 193.893 1.00 38.27  ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 231.762 241.595 193.196 1.00 42.15  ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 232.485 244.327 199.952 1.00 43.32  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 232.401 245.230 201.090 1.00 40.43  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 232.622 246.659 200.615 1.00 35.88  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 233.505 246.921 199.794 1.00 47.39  ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 233.428 244.862 202.162 1.00 41.55  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 233.536 243.381 202.531 1.00 33.07  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 234.545 243.180 203.650 1.00 34.87  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 232.179 242.822 202.928 1.00 36.98  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 231.810 247.582 201.125 1.00 36.89  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 231.851 248.968 200.686 1.00 40.30  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 231.816 249.905 201.883 1.00 48.33  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 231.283 249.570 202.944 1.00 51.78  ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 230.685 249.291 199.742 1.00 46.30  ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 229.439 249.071 200.379 1.00 54.83  ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 232.397 251.089 201.697 1.00 52.36  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 232.356 252.142 202.699 1.00 50.22  ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 232.339 253.489 201.993 1.00 51.28  ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 232.857 253.630 200.881 1.00 46.74  ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 233.544 252.064 203.668 1.00 51.10  ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 233.404 253.066 204.683 1.00 54.09  ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 234.859 252.272 202.931 1.00 50.13  ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 231.726 254.474 202.643 1.00 59.25  ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 231.660 255.830 202.121 1.00 53.10  ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 232.625 256.780 202.816 1.00 55.35  ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 232.602 257.981 202.534 1.00 61.87  ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 230.231 256.371 202.235 1.00 54.88  ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 229.266 255.789 201.216 1.00 55.92  ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 227.890 256.427 201.324 1.00 59.11  ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 227.250 256.143 202.603 1.00 62.84  ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 227.143 257.013 203.598 1.00 61.31  ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 227.626 258.241 203.497 1.00 57.56  ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 226.538 256.642 204.722 1.00 60.70  ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 233.467 256.275 203.714 1.00 57.06  ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 234.406 257.111 204.452 1.00 58.09  ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 235.824 256.844 203.972 1.00 61.14  ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 236.381 255.776 204.268 1.00 65.10  ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 234.294 256.844 205.954 1.00 58.43  ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 234.901 257.954 206.789 1.00 67.70  ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 235.233 259.015 206.220 1.00 72.59  ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 235.048 257.764 208.014 1.00 62.52  ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 236.447 257.762 203.228 1.00 61.13  ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 237.849 257.556 202.835 1.00 59.79  ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 238.829 257.677 203.989 1.00 62.19  ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 239.986 257.264 203.841 1.00 62.88  ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 238.086 258.652 201.788 1.00 63.19  ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 237.100 259.717 202.136 1.00 62.25  ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 235.888 259.006 202.670 1.00 62.97  ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 238.410 258.228 205.127 1.00 69.38  ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 239.293 258.483 206.257 1.00 68.55  ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 239.263 257.372 207.299 1.00 69.07  ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 239.877 257.519 208.361 1.00 72.03  ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 238.930 259.815 206.915 1.00 73.85  ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 237.521 259.851 207.177 1.00 73.52  ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 239.297 260.975 206.003 1.00 69.78  ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 238.562 256.271 207.029 1.00 72.86  ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 238.400 255.228 208.033 1.00 70.84  ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 239.679 254.410 208.155 1.00 68.09  ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 240.361 254.124 207.160 1.00 66.48  ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 237.191 254.337 207.692 1.00 67.40  ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 237.400 253.617 206.370 1.00 67.71  ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 236.925 253.342 208.811 1.00 65.74  ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 240.020 254.045 209.387 1.00 70.94  ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 241.103 253.120 209.677 1.00 68.48  ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 240.576 251.691 209.680 1.00 70.23  ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 239.403 251.444 209.972 1.00 73.14  ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 241.746 253.428 211.032 1.00 70.42  ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 242.507 254.738 211.094 1.00 73.12  ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 243.774 254.711 210.263 1.00 74.55  ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 244.370 253.623 210.117 1.00 73.71  ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 244.181 255.780 209.763 1.00 72.35  ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 241.454 250.750 209.343 1.00 62.67  ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 241.107 249.340 209.387 1.00 59.07  ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 242.181 248.566 210.137 1.00 61.15  ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 243.376 248.846 209.980 1.00 64.26  ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 240.944 248.764 207.973 1.00 58.32  ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 239.691 249.209 207.278 1.00 58.30  ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 238.447 248.848 207.767 1.00 57.12  ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 239.755 249.984 206.133 1.00 55.85  ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 237.293 249.255 207.129 1.00 57.06  ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 238.605 250.393 205.491 1.00 53.87  ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 237.373 250.029 205.990 1.00 57.78  ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 241.790 247.590 210.960 1.00 53.94  ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 242.790 246.784 211.654 1.00 52.68  ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 243.574 245.938 210.668 1.00 54.26  ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 243.075 245.606 209.579 1.00 54.94  ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 241.946 245.912 212.601 1.00 57.63  ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 240.589 245.886 211.988 1.00 58.12  ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 240.414 247.219 211.330 1.00 53.16  ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 244.817 245.577 210.998 1.00 56.49  ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 245.646 244.835 210.032 1.00 53.81  ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 245.047 243.510 209.591 1.00 54.93  ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 245.279 243.092 208.450 1.00 63.62  ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 246.966 244.630 210.791 1.00 57.57  ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 246.985 245.707 211.824 1.00 58.52  ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 245.556 245.901 212.230 1.00 60.73  ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 244.293 242.829 210.458 1.00 52.60  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 243.703 241.551 210.070 1.00 55.32  ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 242.679 241.730 208.955 1.00 54.18  ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 242.623 240.923 208.019 1.00 58.57  ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 243.071 240.868 211.283 1.00 57.72  ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 242.045 241.739 211.978 1.00 64.94  ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 241.940 242.930 211.624 1.00 63.65  ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 241.344 241.233 212.878 1.00 68.56  ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 241.856 242.779 209.040 1.00 51.29  ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 240.881 243.039 207.985 1.00 49.86  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 241.570 243.421 206.681 1.00 46.54  ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 241.129 243.021 205.598 1.00 49.63  ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 239.909 244.134 208.422 1.00 47.93  ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 238.748 244.434 207.470 1.00 49.46  ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 238.092 243.149 206.988 1.00 45.86  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 237.726 245.339 208.137 1.00 51.16  ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 242.651 244.201 206.766 1.00 47.06  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 243.385 244.585 205.564 1.00 46.97  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 243.964 243.372 204.848 1.00 48.39  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 244.089 243.378 203.618 1.00 54.18  ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 244.498 245.570 205.921 1.00 49.54  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 243.940 247.047 206.797 1.00 61.77  ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 244.328 242.329 205.597 1.00 41.93  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 244.865 241.124 204.975 1.00 41.97  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 243.771 240.282 204.334 1.00 44.73  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 244.030 239.579 203.350 1.00 49.70  ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 245.628 240.296 206.008 1.00 44.00  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 244.758 239.815 207.018 1.00 37.41  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 242.552 240.333 204.871 1.00 33.75  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 241.470 239.483 204.392 1.00 22.20  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 240.776 240.029 203.152 1.00 32.46  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 240.055 239.277 202.488 1.00 44.62  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 240.434 239.283 205.501 1.00 30.92  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 240.917 238.417 206.647 1.00 37.69  ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 239.762 237.964 207.520 1.00 36.70  ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 240.202 237.041 208.559 1.00 45.78  ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 240.687 237.415 209.734 1.00 44.50  ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 240.801 238.692 210.061 1.00 39.07  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 241.067 236.484 210.605 1.00 42.98  ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 240.970 241.305 202.823 1.00 37.58  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 240.295 241.931 201.696 1.00 35.85  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 241.323 242.652 200.837 1.00 37.61  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 242.427 242.974 201.280 1.00 45.18  ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 239.195 242.920 202.144 1.00 30.08  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 238.185 242.232 203.047 1.00 34.04  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 239.815 244.120 202.839 1.00 34.60  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 240.942 242.900 199.587 1.00 25.65  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 241.714 243.743 198.683 1.00 39.23  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 240.996 245.085 198.581 1.00 35.64  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 239.768 245.137 198.457 1.00 36.81  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 241.904 243.074 197.319 1.00 44.84  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 242.932 243.755 196.586 1.00 54.75  ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 240.619 243.055 196.500 1.00 29.00  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 241.754 246.170 198.697 1.00 38.63  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 241.155 247.496 198.709 1.00 29.40  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 240.985 248.014 197.289 1.00 39.99  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 241.879 247.870 196.451 1.00 50.00  ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 242.012 248.457 199.529 1.00 34.24  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 241.950 248.210 201.007 1.00 36.52  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 240.804 248.510 201.724 1.00 41.81  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 243.033 247.672 201.680 1.00 41.29  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 240.742 248.282 203.084 1.00 45.25  ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 242.977 247.441 203.040 1.00 43.59  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 241.830 247.747 203.743 1.00 47.96  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 239.826 248.607 197.016 1.00 36.70  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 239.534 249.230 195.725 1.00 37.09  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 239.089 250.656 196.039 1.00 40.78  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 237.908 250.916 196.284 1.00 46.73  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 238.466 248.474 194.929 1.00 34.74  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 238.420 248.977 193.501 1.00 38.23  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 238.734 246.977 194.956 1.00 32.69  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 240.037 251.589 196.032 1.00 33.75  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 239.774 252.968 196.421 1.00 37.57  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 239.348 253.770 195.197 1.00 40.63  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 240.108 253.887 194.230 1.00 43.44  ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 241.011 253.587 197.070 1.00 38.72  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 240.680 254.794 197.924 1.00 41.64  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 239.557 255.298 197.901 1.00 47.01  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 241.660 255.266 198.685 1.00 37.10  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 238.137 254.319 195.243 1.00 35.55  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 237.605 255.120 194.142 1.00 41.52  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 237.839 256.603 194.425 1.00 48.14  ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 236.920 257.376 194.699 1.00 37.30  ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 236.125 254.815 193.933 1.00 40.84  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 235.865 253.553 193.163 1.00 42.79  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 235.967 252.317 193.778 1.00 43.03  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 235.509 253.603 191.826 1.00 36.20  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 235.724 251.154 193.073 1.00 35.99  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 235.265 252.443 191.115 1.00 42.52  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 235.372 251.217 191.740 1.00 44.12  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 239.108 256.991 194.352 1.00 55.96  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 239.479 258.380 194.565 1.00 42.77  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 239.105 259.227 193.351 1.00 46.36  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 238.833 258.716 192.261 1.00 49.82  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 240.976 258.507 194.847 1.00 40.44  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 241.712 257.714 193.907 1.00 51.61  ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 241.295 258.037 196.258 1.00 42.46  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 239.093 260.540 193.556 1.00 46.15  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 238.768 261.500 192.508 1.00 50.36  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 240.070 262.091 191.987 1.00 49.64  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 240.858 262.654 192.757 1.00 49.37  ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 237.828 262.600 193.024 1.00 48.84  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 237.529 263.602 191.921 1.00 45.21  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 236.543 261.991 193.561 1.00 49.26  ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 240.297 261.964 190.685 1.00 50.71  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 241.499 262.474 190.046 1.00 47.46  ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 241.223 263.822 189.391 1.00 45.39  ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 240.078 264.182 189.109 1.00 52.53  ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 242.026 261.483 189.004 1.00 49.94  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 241.062 261.329 187.956 1.00 52.66  ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 242.289 260.130 189.644 1.00 46.43  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 242.303 264.572 189.158 1.00 49.46  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 242.171 265.894 188.553 1.00 47.38  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 241.604 265.804 187.142 1.00 50.31  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 240.758 266.617 186.752 1.00 56.97  ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 243.526 266.601 188.543 1.00 52.15  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 244.040 266.967 189.925 1.00 51.40  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 245.415 267.610 189.857 1.00 52.58  ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 245.651 268.514 190.977 1.00 59.84  ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 245.153 269.739 191.071 1.00 57.98  ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 244.387 270.250 190.120 1.00 55.25  ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 245.430 270.472 192.146 1.00 50.78  ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 242.062 264.823 186.360 1.00 49.24  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 241.563 264.667 184.998 1.00 49.60  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 240.084 264.299 184.984 1.00 49.27  ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 239.323 264.801 184.149 1.00 52.66  ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 242.385 263.613 184.257 1.00 55.48  ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 242.250 262.341 184.866 1.00 59.07  ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 239.662 263.416 185.893 1.00 46.50  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 238.261 263.006 185.932 1.00 50.03  ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 237.350 264.175 186.284 1.00 55.40  ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 236.284 264.343 185.681 1.00 55.19  ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 238.075 261.865 186.931 1.00 53.72  ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 236.716 261.473 187.009 1.00 61.90  ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 237.750 264.991 187.261 1.00 49.72  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 236.925 266.128 187.654 1.00 43.53  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 236.875 267.181 186.554 1.00 47.81  ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 235.837 267.820 186.347 1.00 60.91  ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 237.446 266.733 188.956 1.00 43.92  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 236.593 267.860 189.539 1.00 46.80  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 235.210 267.349 189.907 1.00 46.13  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 237.276 268.474 190.742 1.00 47.56  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 237.987 267.380 185.843 1.00 49.54  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 237.995 268.330 184.735 1.00 46.93  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 237.013 267.914 183.648 1.00 45.40  ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 236.306 268.756 183.083 1.00 54.32  ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 239.406 268.459 184.161 1.00 45.03  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 240.312 269.399 184.936 1.00 49.99  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 241.780 269.166 184.641 1.00 55.03  ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 242.132 268.551 183.634 1.00 50.48  ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 242.646 269.659 185.519 1.00 55.39  ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 236.960 266.616 183.338 1.00 51.20  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 236.005 266.130 182.347 1.00 53.18  ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 234.570 266.310 182.827 1.00 52.31  ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 233.687 266.673 182.041 1.00 56.28  ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 236.285 264.662 182.027 1.00 55.74  ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 237.636 264.473 181.645 1.00 60.97  ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 234.317 266.052 184.112 1.00 50.41  ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 232.972 266.224 184.654 1.00 45.78  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 232.536 267.682 184.587 1.00 56.65  ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 231.402 267.988 184.200 1.00 65.47  ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 232.918 265.717 186.095 1.00 51.13  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 233.064 264.213 186.240 1.00 60.27  ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 233.126 263.776 187.690 1.00 63.18  ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 234.027 263.039 188.091 1.00 59.38  ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 232.166 264.231 188.487 1.00 53.75  ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 233.429 268.600 184.964 1.00 51.40  ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 233.081 270.017 184.955 1.00 44.26  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 232.967 270.552 183.533 1.00 49.29  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 232.126 271.413 183.255 1.00 59.96  ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 234.111 270.812 185.754 1.00 48.37  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 234.210 270.340 187.495 1.00 62.75  ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 233.811 270.060 182.622 1.00 47.55  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 233.716 270.480 181.227 1.00 51.07  ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 232.397 270.036 180.608 1.00 52.34  ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 231.772 270.787 179.851 1.00 58.18  ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 234.898 269.930 180.430 1.00 50.10  ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 234.888 270.185 178.922 1.00 45.94  ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 235.108 271.659 178.624 1.00 48.14  ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 235.939 269.334 178.229 1.00 52.13  ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 231.961 268.811 180.913 1.00 50.18  ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 230.672 268.342 180.416 1.00 53.47  ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 229.522 269.114 181.050 1.00 57.77  ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 228.531 269.426 180.380 1.00 62.22  ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 230.522 266.844 180.681 1.00 57.02  ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 231.496 266.010 179.874 1.00 60.96  ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 232.164 266.514 178.971 1.00 60.26  ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 231.583 264.725 180.197 1.00 59.27  ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 229.632 269.423 182.345 1.00 60.56  ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 228.550 270.117 183.037 1.00 56.00  ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 228.348 271.524 182.487 1.00 57.23  ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 227.209 271.957 182.277 1.00 58.86  ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 228.833 270.162 184.538 1.00 57.25  ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 227.634 270.557 185.385 1.00 64.37  ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 226.339 269.949 184.883 1.00 69.68  ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 226.145 268.728 185.063 1.00 65.24  ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 225.513 270.692 184.311 1.00 74.32  ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 229.439 272.257 182.253 1.00 54.11  ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 229.309 273.597 181.690 1.00 51.95  ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 228.868 273.528 180.233 1.00 59.53  ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 228.141 274.408 179.757 1.00 65.46  ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 230.620 274.390 181.857 1.00 50.09  ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 231.736 273.800 181.008 1.00 55.33  ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 230.400 275.856 181.513 1.00 54.48  ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 229.291 272.493 179.504 1.00 60.31  ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 228.854 272.340 178.121 1.00 53.14  ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 227.351 272.109 178.045 1.00 54.01  ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 226.672 272.669 177.179 1.00 61.98  ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 229.611 271.191 177.455 1.00 59.33  ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 229.393 271.011 175.952 1.00 64.87  ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 229.891 272.229 175.190 1.00 61.78  ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 230.083 269.748 175.460 1.00 65.56  ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 226.813 271.285 178.948 1.00 59.21  ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 225.371 271.068 178.985 1.00 59.42  ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 224.629 272.344 179.364 1.00 65.23  ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 223.578 272.653 178.789 1.00 69.10  ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 225.040 269.939 179.961 1.00 59.96  ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 223.586 269.889 180.398 1.00 60.70  ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 223.363 268.816 181.450 1.00 65.69  ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 223.683 267.434 180.906 1.00 66.39  ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 222.624 266.943 179.982 1.00 65.43  ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 225.162 273.101 180.325 1.00 64.82  ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 224.483 274.310 180.780 1.00 58.02  ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 224.565 275.425 179.745 1.00 62.81  ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 223.572 276.117 179.492 1.00 70.84  ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 225.075 274.772 182.111 1.00 55.12  ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 225.735 275.614 179.134 1.00 66.22  ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 225.944 276.737 178.227 1.00 66.32  ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 225.557 276.416 176.789 1.00 71.64  ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 224.928 277.244 176.121 1.00 74.28  ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 227.407 277.187 178.279 1.00 66.99  ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 227.788 277.900 179.564 1.00 69.86  ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 227.105 279.244 179.708 1.00 74.17  ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 227.423 280.161 178.921 1.00 74.23  ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 226.248 279.384 180.605 1.00 72.93  ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 225.916 275.233 176.296 1.00 70.75  ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 225.664 274.835 174.912 1.00 67.93  ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 224.940 273.495 174.905 1.00 71.91  ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 225.538 272.451 174.617 1.00 74.75  ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 226.969 274.756 174.118 1.00 68.43  ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 227.928 275.908 174.375 1.00 66.98  ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 227.421 277.198 173.754 1.00 73.18  ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 227.278 277.088 172.308 1.00 75.40  ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 228.279 277.202 171.446 1.00 77.33  ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 229.516 277.439 171.850 1.00 71.15  ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 228.033 277.075 170.145 1.00 73.35  ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 223.643 273.489 175.229 1.00 72.83  ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 222.912 272.211 175.272 1.00 74.32  ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 222.893 271.481 173.940 1.00 74.86  ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 222.897 270.244 173.918 1.00 75.21  ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 221.503 272.629 175.716 1.00 74.42  ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 221.398 274.074 175.356 1.00 70.77  ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 222.773 274.639 175.526 1.00 69.22  ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 222.869 272.215 172.825 1.00 77.00  ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 222.886 271.571 171.515 1.00 76.08  ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 224.208 270.853 171.268 1.00 80.25  ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 224.230 269.754 170.703 1.00 83.57  ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 222.620 272.603 170.420 1.00 79.59  ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 223.561 273.789 170.496 1.00 82.74  ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 223.345 274.667 171.357 1.00 79.73  ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 224.515 273.844 169.693 1.00 82.95  ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 225.322 271.463 171.676 1.00 72.54  ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 226.624 270.830 171.490 1.00 69.07  ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 226.766 269.618 172.402 1.00 74.74  ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 227.327 268.589 172.005 1.00 83.77  ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 227.752 271.851 171.721 1.00 70.40  ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 229.105 271.224 171.425 1.00 72.50  ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 227.534 273.084 170.859 1.00 73.58  ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 226.269 269.718 173.637 1.00 71.15  ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 226.399 268.612 174.582 1.00 71.24  ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 225.621 267.388 174.114 1.00 77.27  ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 226.125 266.260 174.178 1.00 80.62  ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 225.931 269.048 175.970 1.00 74.82  ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 226.342 268.071 177.054 1.00 78.88  ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 227.558 267.922 177.292 1.00 77.27  ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 225.448 267.451 177.667 1.00 79.22  ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 224.386 267.586 173.646 1.00 80.93  ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 223.606 266.454 173.155 1.00 77.76  ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 224.195 265.904 171.862 1.00 76.30  ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 224.154 264.692 171.622 1.00 80.91  ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 222.140 266.857 172.967 1.00 77.50  ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 221.888 267.947 171.936 1.00 80.31  ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 221.648 267.397 170.543 1.00 83.22  ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 221.327 266.196 170.424 1.00 81.62  ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 221.778 268.166 169.568 1.00 83.64  ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 224.745 266.779 171.017 1.00 73.57  ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 225.442 266.313 169.824 1.00 76.75  ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 226.692 265.526 170.195 1.00 77.49  ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 226.994 264.498 169.578 1.00 82.23  ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 225.793 267.499 168.925 1.00 76.87  ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 226.405 267.113 167.590 1.00 81.67  ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 226.490 268.310 166.656 1.00 82.14  ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 227.553 269.296 167.113 1.00 82.35  ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 227.748 270.399 166.132 1.00 79.97  ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 227.434 265.996 171.202 1.00 77.03  ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 228.606 265.260 171.663 1.00 74.47  ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 228.214 263.917 172.264 1.00 76.77  ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 228.846 262.893 171.977 1.00 83.46  ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 229.383 266.094 172.682 1.00 76.59  ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 230.606 265.393 173.253 1.00 78.63  ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 231.180 266.151 174.440 1.00 78.02  ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 230.267 266.160 175.577 1.00 81.58  ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 230.090 265.139 176.405 1.00 81.14  ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 230.757 264.006 176.259 1.00 76.74  ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 229.223 265.258 177.406 1.00 79.14  ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 227.169 263.898 173.095 1.00 81.32  ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 226.754 262.655 173.738 1.00 82.44  ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 226.299 261.626 172.711 1.00 82.93  ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 226.594 260.433 172.843 1.00 83.12  ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 225.643 262.932 174.750 1.00 84.87  ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 224.465 263.380 174.104 1.00 88.04  ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 225.570 262.068 171.683 1.00 82.20  ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 225.163 261.156 170.620 1.00 82.43  ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 226.370 260.636 169.849 1.00 81.05  ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 226.414 259.460 169.469 1.00 85.89  ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 224.182 261.852 169.678 1.00 85.14  ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 222.863 262.180 170.349 1.00 89.30  ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 222.529 261.524 171.358 1.00 87.68  ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 222.160 263.094 169.869 1.00 88.68  ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 227.358 261.500 169.605 1.00 77.66  ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 228.538 261.085 168.853 1.00 77.17  ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 229.332 260.019 169.600 1.00 81.71  ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 229.840 259.074 168.984 1.00 87.90  ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 229.417 262.295 168.546 1.00 80.50  ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 228.981 263.180 167.378 1.00 83.99  ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 230.016 264.259 167.117 1.00 81.69  ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 228.743 262.346 166.128 1.00 82.99  ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 229.460 260.155 170.923 1.00 80.49  ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 230.139 259.124 171.704 1.00 80.84  ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 229.411 257.790 171.607 1.00 82.96  ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 230.047 256.735 171.495 1.00 85.18  ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 230.268 259.557 173.166 1.00 81.04  ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 231.519 260.334 173.590 1.00 80.78  ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 231.566 261.723 172.980 1.00 78.33  ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 231.601 260.412 175.108 1.00 82.78  ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 228.077 257.814 171.657 1.00 79.06  ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 227.311 256.580 171.518 1.00 77.28  ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 227.491 255.971 170.132 1.00 78.32  ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 227.641 254.752 169.997 1.00 82.82  ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 225.833 256.845 171.801 1.00 79.58  ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 224.957 255.606 171.721 1.00 81.34  ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 223.528 255.910 172.140 1.00 81.80  ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 222.801 256.718 171.079 1.00 84.66  ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 221.367 256.922 171.424 1.00 83.47  ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 227.473 256.806 169.089 1.00 77.01  ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 227.641 256.297 167.731 1.00 78.10  ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 229.026 255.694 167.529 1.00 78.02  ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 229.162 254.628 166.918 1.00 83.53  ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 227.387 257.411 166.715 1.00 77.46  ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 225.992 257.457 166.087 1.00 79.88  ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 224.930 257.787 167.124 1.00 81.65  ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 225.956 258.458 164.942 1.00 78.14  ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 230.067 256.362 168.032 1.00 73.92  ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 231.417 255.821 167.902 1.00 77.12  ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 231.567 254.519 168.679 1.00 77.50  ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 232.236 253.588 168.218 1.00 81.73  ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 232.448 256.849 168.366 1.00 77.69  ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 232.533 258.082 167.481 1.00 79.36  ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 233.551 259.088 167.978 1.00 81.84  ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 234.160 258.904 169.032 1.00 81.40  ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 233.746 260.157 167.216 1.00 82.40  ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 230.957 254.438 169.862 1.00 73.39  ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 231.009 253.199 170.622 1.00 70.75  ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 230.341 252.047 169.897 1.00 73.34  ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 230.835 250.917 169.909 1.00 74.87  ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 229.202 252.320 169.257 1.00 78.02  ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 228.524 251.286 168.482 1.00 77.41  ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 229.328 250.903 167.245 1.00 77.38  ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 229.413 249.721 166.892 1.00 79.80  ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 227.126 251.759 168.086 1.00 75.69  ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 226.165 251.908 169.253 1.00 76.87  ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 224.861 252.567 168.853 1.00 80.85  ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 224.730 252.961 167.675 1.00 77.74  ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 223.967 252.692 169.716 1.00 82.60  ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 229.917 251.892 166.568 1.00 71.25  ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 230.674 251.611 165.351 1.00 70.38  ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 231.911 250.771 165.643 1.00 71.26  ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 232.220 249.835 164.897 1.00 82.04  ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 231.063 252.918 164.660 1.00 74.17  ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 229.895 253.677 164.093 1.00 77.45  ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 228.657 253.070 163.949 1.00 74.96  ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 230.035 254.999 163.706 1.00 75.65  ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 227.583 253.767 163.430 1.00 73.60  ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 228.964 255.700 163.186 1.00 76.72  ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 227.737 255.083 163.048 1.00 76.29  ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 232.635 251.092 166.719 1.00 67.33  ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 233.805 250.298 167.081 1.00 65.68  ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 233.408 248.884 167.485 1.00 63.53  ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 234.127 247.923 167.187 1.00 63.73  ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 234.583 250.984 168.204 1.00 68.85  ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 235.141 252.349 167.833 1.00 69.20  ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 236.270 252.269 166.822 1.00 74.53  ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 236.833 251.201 166.582 1.00 75.99  ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 236.605 253.405 166.221 1.00 70.00  ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 232.272 248.738 168.171 1.00 64.08  ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 231.784 247.407 168.517 1.00 62.95  ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 231.461 246.600 167.266 1.00 68.35  ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 231.753 245.401 167.199 1.00 72.24  ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 230.555 247.518 169.419 1.00 63.48  ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 229.799 246.220 169.707 1.00 67.52  ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 230.526 245.398 170.759 1.00 68.75  ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 228.372 246.512 170.140 1.00 63.53  ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 230.855 247.243 166.265 1.00 69.51  ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 230.557 246.555 165.013 1.00 64.75  ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 231.833 246.132 164.296 1.00 63.27  ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 231.892 245.046 163.709 1.00 67.92  ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 229.707 247.452 164.113 1.00 66.30  ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 229.153 246.753 162.883 1.00 69.91  ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 228.026 245.800 163.246 1.00 66.26  ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 227.929 244.691 162.304 1.00 67.82  ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 227.925 243.412 162.652 1.00 66.53  ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 228.006 243.039 163.919 1.00 64.07  ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 227.836 242.482 161.705 1.00 65.44  ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 232.865 246.981 164.329 1.00 62.62  ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 234.123 246.644 163.669 1.00 61.95  ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 234.762 245.409 164.292 1.00 66.61  ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 235.294 244.550 163.578 1.00 70.35  ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 235.083 247.831 163.731 1.00 66.81  ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 234.755 249.020 162.827 1.00 66.98  ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 235.648 250.206 163.151 1.00 68.31  ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 234.890 248.628 161.364 1.00 66.57  ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 234.731 245.307 165.622 1.00 65.81  ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 235.273 244.125 166.285 1.00 63.31  ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 234.491 242.874 165.908 1.00 68.61  ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 235.081 241.817 165.655 1.00 72.73  ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 235.269 244.325 167.800 1.00 64.81  ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 236.090 245.512 168.268 1.00 64.02  ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 236.038 245.654 169.777 1.00 64.88  ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 235.759 247.027 170.180 1.00 68.36  ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 234.689 247.404 170.866 1.00 64.87  ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 233.771 246.531 171.248 1.00 61.84  ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 234.538 248.687 171.180 1.00 64.68  ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 233.159 242.971 165.872 1.00 71.90  ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 232.344 241.823 165.488 1.00 70.27  ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 232.612 241.413 164.045 1.00 69.31  ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 232.731 240.220 163.744 1.00 76.52  ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 230.862 242.139 165.688 1.00 69.39  ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 230.477 242.445 167.125 1.00 72.45  ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 229.012 242.809 167.269 1.00 72.41  ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 228.509 243.694 166.578 1.00 72.51  ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 228.319 242.125 168.172 1.00 70.19  ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 232.705 242.388 163.138 1.00 65.14  ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 232.968 242.074 161.738 1.00 67.26  ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 234.348 241.455 161.557 1.00 72.70  ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 234.505 240.485 160.806 1.00 78.59  ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 232.827 243.333 160.883 1.00 68.95  ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 231.403 243.863 160.706 1.00 69.53  ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 231.422 245.293 160.193 1.00 70.90  ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 230.612 242.966 159.770 1.00 72.08  ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 235.362 242.006 162.229 1.00 77.24  ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 236.703 241.437 162.137 1.00 76.29  ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 236.753 240.040 162.742 1.00 76.66  ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 237.380 239.134 162.180 1.00 78.75  ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 237.713 242.357 162.822 1.00 79.66  ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 239.151 241.868 162.742 1.00 79.95  ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 239.684 241.842 161.322 1.00 84.48  ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 239.184 242.618 160.479 1.00 81.88  ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 240.604 241.044 161.047 1.00 85.73  ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 236.104 239.848 163.893 1.00 75.67  ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 236.060 238.523 164.503 1.00 73.91  ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 235.301 237.538 163.624 1.00 75.02  ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 235.741 236.398 163.433 1.00 79.37  ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 235.428 238.607 165.893 1.00 75.68  ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 234.759 237.323 166.357 1.00 79.24  ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 233.693 237.604 167.403 1.00 79.14  ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 232.983 236.328 167.827 1.00 79.15  ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 232.462 235.569 166.657 1.00 76.24  ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 234.162 237.962 163.071 1.00 76.09  ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 233.390 237.083 162.200 1.00 74.08  ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 234.171 236.728 160.941 1.00 73.25  ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 234.116 235.587 160.469 1.00 76.69  ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 232.057 237.737 161.838 1.00 72.72  ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 231.284 237.996 162.997 1.00 76.27  ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 234.898 237.696 160.380 1.00 75.83  ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 235.707 237.428 159.195 1.00 75.94  ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 236.798 236.408 159.496 1.00 78.64  ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 237.052 235.498 158.698 1.00 82.96  ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 236.314 238.731 158.674 1.00 79.85  ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 237.180 238.637 157.417 1.00 78.10  ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 236.348 238.197 156.226 1.00 80.97  ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 237.854 239.967 157.138 1.00 79.10  ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 237.460 236.549 160.646 1.00 79.14  ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 238.508 235.603 161.015 1.00 74.84  ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 237.927 234.236 161.353 1.00 76.16  ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 238.472 233.204 160.947 1.00 78.12  ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 239.317 236.151 162.191 1.00 79.40  ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 240.500 235.303 162.659 1.00 82.73  ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 241.536 235.175 161.554 1.00 79.93  ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 241.120 235.897 163.913 1.00 81.39  ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 236.819 234.208 162.100 1.00 81.79  ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 236.206 232.936 162.468 1.00 79.89  ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 235.668 232.202 161.246 1.00 83.04  ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 235.743 230.970 161.175 1.00 88.78  ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 235.090 233.160 163.489 1.00 77.76  ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 235.571 233.595 164.865 1.00 84.85  ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 236.820 232.860 165.310 1.00 89.15  ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 237.875 233.466 165.500 1.00 85.46  ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 236.706 231.549 165.486 1.00 86.03  ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 235.114 232.939 160.280 1.00 88.15  ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 234.558 232.302 159.091 1.00 85.87  ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 235.632 231.569 158.299 1.00 85.39  ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 235.412 230.444 157.837 1.00 89.73  ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 233.859 233.339 158.213 1.00 84.82  ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 236.804 232.187 158.134 1.00 83.37  ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 237.876 231.547 157.379 1.00 83.10  ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 238.361 230.278 158.070 1.00 84.62  ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 238.668 229.280 157.409 1.00 88.29  ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 239.034 232.524 157.181 1.00 84.95  ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 238.782 233.675 156.207 1.00 82.85  ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 239.921 234.677 156.255 1.00 84.24  ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 238.597 233.141 154.799 1.00 83.63  ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 238.442 230.301 159.402 1.00 86.92  ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 238.960 229.151 160.135 1.00 87.31  ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 238.012 227.960 160.057 1.00 87.46  ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 238.459 226.810 159.986 1.00 89.45  ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 239.219 229.537 161.591 1.00 85.39  ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 240.179 230.702 161.721 1.00 87.34  ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 241.297 230.661 161.210 1.00 88.14  ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 239.742 231.755 162.402 1.00 89.00  ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 236.701 228.212 160.070 1.00 94.37  ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 235.737 227.119 160.137 1.00 95.43  ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 235.486 226.464 158.784 1.00 96.04  ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 234.879 225.389 158.738 1.00 96.82  ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 234.419 227.619 160.737 1.00 92.54  ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 233.725 228.720 159.944 1.00 95.13  ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 232.835 228.185 158.838 1.00 98.01  ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 232.452 226.998 158.901 1.00 97.74  ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 232.519 228.953 157.904 1.00 97.52  ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 235.929 227.078 157.686 1.00 96.32  ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 235.717 226.489 156.369 1.00 96.68  ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 236.603 225.263 156.207 1.00 101.13 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 237.816 225.314 156.449 1.00 102.61 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 235.987 227.518 155.261 1.00 97.91  ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 235.870 226.862 153.895 1.00 100.73 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 235.005 228.665 155.359 1.00 99.16  ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 235.998 224.153 155.795 1.00 107.93 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 236.721 222.925 155.498 1.00 107.75 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 236.861 222.788 153.988 1.00 105.23 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 235.861 222.803 153.263 1.00 104.35 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 235.998 221.710 156.080 1.00 106.19 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 235.651 221.840 157.555 1.00 105.67 ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 236.885 222.127 158.397 1.00 106.78 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 237.837 220.942 158.405 1.00 106.88 ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 238.992 221.163 159.319 1.00 105.05 ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 238.099 222.654 153.521 1.00 110.90 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 238.365 222.605 152.098 1.00 112.74 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 238.917 223.912 151.569 1.00 113.72 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 240.062 224.270 151.860 1.00 113.55 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 238.112 224.636 150.794 1.00 114.00 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 238.519 225.919 150.239 1.00 114.57 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 237.331 226.870 150.238 1.00 114.95 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 236.171 226.452 150.287 1.00 113.95 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 239.080 225.776 148.818 1.00 113.59 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 240.459 225.141 148.748 1.00 113.45 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 240.705 224.508 147.390 1.00 113.77 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 239.677 223.533 147.047 1.00 114.02 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 239.690 222.785 145.953 1.00 113.93 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 240.669 222.872 145.068 1.00 112.49 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 238.695 221.928 145.741 1.00 114.13 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 237.641 228.167 150.186 1.00 111.16 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 236.599 229.188 150.168 1.00 110.43 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 235.770 229.093 148.893 1.00 112.20 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 234.536 229.163 148.931 1.00 113.54 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 237.224 230.585 150.335 1.00 110.05 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 237.953 230.687 151.677 1.00 110.48 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 236.164 231.669 150.206 1.00 111.03 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 239.247 231.465 151.610 1.00 110.26 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 236.431 228.926 147.745 1.00 113.52 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 235.730 228.923 146.466 1.00 114.48 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 234.863 227.685 146.269 1.00 114.42 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 234.017 227.678 145.369 1.00 113.39 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 236.733 229.039 145.317 1.00 112.72 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 237.030 230.448 144.797 1.00 111.71 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 237.771 231.266 145.841 1.00 111.50 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 237.823 230.383 143.502 1.00 112.65 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 235.056 226.641 147.079 1.00 116.90 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 234.258 225.429 146.921 1.00 117.19 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 232.784 225.691 147.207 1.00 116.37 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 231.906 225.160 146.517 1.00 115.41 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 234.792 224.323 147.831 1.00 119.09 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 236.051 223.678 147.287 1.00 119.07 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 236.103 223.407 146.068 1.00 116.60 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 236.987 223.435 148.077 1.00 118.42 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 232.493 226.504 148.218 1.00 115.32 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 231.126 226.820 148.608 1.00 115.94 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 230.840 228.287 148.317 1.00 115.29 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 231.640 229.162 148.665 1.00 114.85 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 230.897 226.518 150.090 1.00 113.81 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 229.558 227.021 150.587 1.00 114.84 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 228.522 226.626 150.013 1.00 114.49 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 229.543 227.811 151.552 1.00 116.44 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 229.698 228.549 147.677 1.00 111.96 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 229.346 229.920 147.320 1.00 112.89 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 228.977 230.751 148.542 1.00 112.80 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 229.237 231.959 148.565 1.00 113.44 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 228.195 229.923 146.315 1.00 114.38 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 228.624 229.470 144.934 1.00 116.27 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 229.807 229.667 144.583 1.00 115.61 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 227.779 228.918 144.199 1.00 114.80 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 228.374 230.130 149.559 1.00 108.46 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 227.901 230.887 150.715 1.00 108.21 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 229.056 231.538 151.468 1.00 106.62 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 228.902 232.628 152.031 1.00 105.63 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 227.097 229.983 151.649 1.00 106.94 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 227.989 229.147 152.396 1.00 108.83 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 226.142 229.110 150.850 1.00 106.31 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 230.218 230.882 151.497 1.00 103.60 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 231.387 231.475 152.143 1.00 103.80 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 231.801 232.749 151.416 1.00 104.17 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 232.130 233.764 152.042 1.00 105.83 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 232.542 230.460 152.209 1.00 105.01 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 232.109 229.203 152.965 1.00 103.99 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 233.758 231.082 152.876 1.00 103.07 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 231.417 229.486 154.283 1.00 102.24 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 231.787 232.715 150.081 1.00 97.94  ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 232.125 233.903 149.302 1.00 98.43  ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 231.113 235.014 149.557 1.00 100.55 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 231.473 236.194 149.642 1.00 99.43  ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 232.224 233.550 147.806 1.00 98.41  ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 233.356 232.548 147.572 1.00 99.13  ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 232.451 234.801 146.972 1.00 98.57  ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 233.365 231.948 146.182 1.00 99.49  ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 229.831 234.656 149.686 1.00 98.31  ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 228.821 235.656 150.020 1.00 96.75  ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 229.081 236.257 151.395 1.00 101.68 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 228.996 237.478 151.575 1.00 103.56 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 227.422 235.040 149.983 1.00 96.34  ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 227.317 234.032 150.995 1.00 99.18  ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 227.141 234.414 148.631 1.00 98.88  ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 229.396 235.411 152.379 1.00 96.80  ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 229.619 235.899 153.736 1.00 90.13  ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 230.846 236.799 153.808 1.00 90.04  ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 230.809 237.858 154.445 1.00 96.40  ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 229.763 234.719 154.698 1.00 90.08  ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 228.565 233.932 154.672 1.00 90.76  ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 230.007 235.211 156.115 1.00 91.01  ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 231.939 236.398 153.155 1.00 86.31  ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 233.158 237.200 153.196 1.00 88.72  ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 232.945 238.564 152.551 1.00 91.79  ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 233.417 239.584 153.067 1.00 96.45  ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 234.301 236.456 152.506 1.00 90.47  ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 234.807 235.164 153.151 1.00 88.74  ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 236.183 234.807 152.613 1.00 89.40  ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 234.830 235.275 154.667 1.00 87.95  ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 232.239 238.601 151.419 1.00 89.85  ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 231.975 239.873 150.755 1.00 91.57  ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 231.054 240.755 151.590 1.00 91.25  ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 231.257 241.972 151.674 1.00 94.37  ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 231.375 239.626 149.371 1.00 92.63  ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 232.383 239.145 148.339 1.00 93.15  ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 231.737 238.791 147.014 1.00 95.19  ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 230.866 237.897 146.996 1.00 95.65  ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 232.101 239.408 145.991 1.00 92.48  ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 230.032 240.159 152.211 1.00 84.74  ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 229.111 240.937 153.034 1.00 87.76  ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 229.812 241.520 154.255 1.00 87.23  ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 229.560 242.670 154.635 1.00 87.28  ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 227.925 240.071 153.459 1.00 88.41  ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 227.016 239.719 152.299 1.00 90.26  ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 227.289 240.073 151.152 1.00 89.04  ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 225.926 239.020 152.592 1.00 88.25  ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 230.688 240.739 154.891 1.00 85.64  ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 231.418 241.242 156.050 1.00 83.30  ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 232.360 242.374 155.660 1.00 84.08  ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 232.508 243.353 156.402 1.00 89.40  ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 232.191 240.106 156.720 1.00 80.82  ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 231.352 239.007 157.375 1.00 83.53  ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 232.231 238.071 158.184 1.00 84.47  ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 230.258 239.604 158.246 1.00 85.42  ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 233.013 242.257 154.501 1.00 81.40  ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 233.947 243.294 154.074 1.00 83.16  ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 233.219 244.573 153.680 1.00 86.75  ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 233.689 245.678 153.977 1.00 89.43  ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 234.806 242.785 152.917 1.00 84.31  ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 235.856 241.763 153.325 1.00 84.46  ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 236.946 242.389 154.184 1.00 84.60  ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 237.501 243.656 153.551 1.00 85.53  ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 238.818 244.041 154.128 1.00 85.91  ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 232.074 244.449 153.004 1.00 87.55  ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 231.340 245.642 152.592 1.00 86.66  ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 230.715 246.346 153.790 1.00 89.03  ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 230.597 247.577 153.804 1.00 92.98  ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 230.276 245.283 151.551 1.00 87.67  ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 229.041 244.589 152.101 1.00 88.90  ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 228.014 244.337 151.009 1.00 87.12  ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 228.460 243.327 150.057 1.00 92.68  ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 228.801 243.581 148.801 1.00 91.69  ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 228.758 244.808 148.308 1.00 89.03  ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 229.193 242.579 148.020 1.00 88.86  ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 230.306 245.584 154.808 1.00 80.11  ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 229.778 246.201 156.020 1.00 79.57  ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 230.882 246.901 156.801 1.00 79.77  ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 230.652 247.950 157.413 1.00 83.51  ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 229.083 245.153 156.887 1.00 80.87  ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 228.224 245.742 157.994 1.00 83.38  ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 227.450 244.687 158.758 1.00 87.10  ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 227.605 243.489 158.443 1.00 87.89  ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 226.686 245.057 159.674 1.00 84.50  ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 232.089 246.329 156.797 1.00 79.95  ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 233.218 246.980 157.452 1.00 79.64  ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 233.553 248.305 156.779 1.00 82.72  ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 233.845 249.297 157.457 1.00 89.27  ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 234.433 246.053 157.451 1.00 79.39  ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 233.521 248.338 155.445 1.00 80.78  ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 233.794 249.579 154.727 1.00 82.44  ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 232.734 250.633 155.021 1.00 82.71  ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 233.054 251.815 155.191 1.00 85.17  ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 233.884 249.309 153.226 1.00 82.20  ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 231.463 250.225 155.074 1.00 83.49  ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 230.397 251.170 155.390 1.00 83.70  ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 230.539 251.708 156.808 1.00 86.51  ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 230.341 252.904 157.050 1.00 89.78  ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 229.032 250.508 155.201 1.00 85.15  ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 227.887 251.493 155.031 1.00 88.55  ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 226.558 250.927 155.490 1.00 90.81  ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 225.507 251.454 155.068 1.00 88.98  ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 226.563 249.955 156.275 1.00 88.08  ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 230.877 250.837 157.761 1.00 81.29  ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 231.076 251.284 159.136 1.00 79.05  ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 232.325 252.152 159.238 1.00 79.14  ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 232.339 253.161 159.954 1.00 85.47  ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 231.138 250.073 160.085 1.00 79.63  ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 231.670 250.484 161.448 1.00 80.57  ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 229.763 249.436 160.219 1.00 78.61  ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 233.388 251.784 158.517 1.00 76.16  ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 234.607 252.588 158.526 1.00 77.10  ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 234.348 253.988 157.984 1.00 81.04  ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 234.860 254.974 158.527 1.00 87.13  ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 235.704 251.895 157.718 1.00 79.64  ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 235.965 250.601 158.276 1.00 81.86  ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 236.986 252.715 157.738 1.00 79.11  ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 233.556 254.096 156.915 1.00 84.54  ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 233.173 255.412 156.414 1.00 85.42  ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 232.354 256.170 157.450 1.00 87.20  ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 232.516 257.386 157.613 1.00 90.98  ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 232.389 255.274 155.110 1.00 86.29  ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 232.005 256.604 154.484 1.00 87.93  ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 231.236 256.408 153.191 1.00 87.29  ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 229.970 255.721 153.416 1.00 91.74  ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 228.855 256.319 153.812 1.00 90.93  ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 228.813 257.622 154.042 1.00 88.48  ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 227.754 255.593 153.984 1.00 87.71  ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 231.465 255.468 158.157 1.00 82.79  ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 230.700 256.104 159.224 1.00 81.86  ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 231.610 256.561 160.357 1.00 83.06  ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 231.367 257.601 160.977 1.00 86.33  ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 229.628 255.149 159.748 1.00 82.77  ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 228.472 254.923 158.789 1.00 83.88  ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 227.511 253.877 159.329 1.00 83.95  ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 226.366 253.623 158.364 1.00 86.87  ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 225.537 252.464 158.792 1.00 84.83  ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 232.663 255.793 160.647 1.00 87.64  ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 233.627 256.214 161.659 1.00 85.77  ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 234.309 257.508 161.233 1.00 86.69  ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 234.494 258.426 162.042 1.00 91.42  ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 234.650 255.093 161.926 1.00 85.86  ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 235.808 255.615 162.763 1.00 86.49  ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 233.979 253.921 162.621 1.00 85.96  ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 234.681 257.606 159.956 1.00 87.56  ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 235.351 258.805 159.462 1.00 89.83  ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 234.450 260.030 159.575 1.00 91.12  ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 234.909 261.120 159.937 1.00 94.72  ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 235.797 258.595 158.015 1.00 91.40  ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 236.811 257.477 157.831 1.00 91.49  ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 238.165 257.812 158.424 1.00 95.75  ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 238.510 259.010 158.484 1.00 93.59  ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 238.885 256.875 158.831 1.00 95.94  ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 233.162 259.874 159.259 1.00 88.85  ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 232.268 261.028 159.258 1.00 88.41  ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 231.923 261.474 160.675 1.00 89.84  ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 231.661 262.659 160.908 1.00 92.78  ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 231.002 260.724 158.453 1.00 88.81  ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 230.037 259.741 159.094 1.00 90.81  ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 229.095 259.117 158.081 1.00 93.21  ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 229.342 259.274 156.867 1.00 92.06  ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 228.108 258.472 158.497 1.00 92.06  ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 231.906 260.548 161.637 1.00 88.47  ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 231.656 260.947 163.020 1.00 86.59  ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 232.863 261.659 163.620 1.00 86.63  ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 232.711 262.530 164.484 1.00 94.10  ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 231.269 259.737 163.871 1.00 88.11  ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 232.341 258.785 163.878 1.00 91.33  ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 229.996 259.091 163.347 1.00 88.46  ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 234.071 261.293 163.183 1.00 85.42  ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 235.272 261.947 163.696 1.00 86.42  ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 235.313 263.423 163.320 1.00 86.77  ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 235.670 264.268 164.148 1.00 90.58  ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 236.523 261.230 163.186 1.00 88.67  ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 236.683 259.843 163.778 1.00 92.76  ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 235.700 259.317 164.339 1.00 91.07  ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 237.792 259.277 163.676 1.00 92.39  ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 234.957 263.757 162.077 1.00 88.66  ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 235.005 265.155 161.658 1.00 88.52  ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 233.933 265.968 162.376 1.00 88.65  ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 234.150 267.136 162.720 1.00 92.57  ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 234.897 265.274 160.125 1.00 89.92  ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 233.565 264.725 159.614 1.00 90.60  ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 236.063 264.564 159.452 1.00 88.54  ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 233.303 265.024 158.154 1.00 89.95  ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 232.763 265.372 162.616 1.00 86.85  ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 231.759 266.035 163.444 1.00 87.05  ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 232.238 266.118 164.888 1.00 85.69  ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 231.940 267.083 165.601 1.00 87.27  ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 230.402 265.316 163.329 1.00 88.09  ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 229.319 266.113 164.038 1.00 87.28  ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 230.029 265.126 161.871 1.00 85.59  ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 232.989 265.110 165.341 1.00 85.49  ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 233.601 265.179 166.664 1.00 84.73  ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 234.609 266.318 166.748 1.00 83.39  ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 234.728 266.975 167.789 1.00 87.83  ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 234.273 263.849 167.006 1.00 86.89  ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 234.843 263.782 168.417 1.00 88.34  ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 233.601 263.910 169.716 1.00 95.15  ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 232.818 262.308 169.580 1.00 88.34  ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 235.346 266.567 165.661 1.00 86.16  ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 236.365 267.613 165.680 1.00 86.45  ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 235.748 268.987 165.908 1.00 85.11  ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 236.298 269.806 166.653 1.00 86.42  ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 237.165 267.596 164.377 1.00 88.57  ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 238.009 266.348 164.169 1.00 90.76  ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 239.179 266.260 165.129 1.00 89.39  ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 239.684 267.277 165.604 1.00 86.98  ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 239.612 265.040 165.428 1.00 87.29  ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 234.606 269.261 165.272 1.00 87.39  ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 233.958 270.556 165.454 1.00 89.01  ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 233.398 270.695 166.865 1.00 88.69  ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 233.310 271.807 167.400 1.00 89.99  ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 232.855 270.741 164.412 1.00 90.26  ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 232.167 272.096 164.463 1.00 91.66  ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 231.118 272.258 163.382 1.00 93.58  ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 230.912 271.302 162.604 1.00 92.51  ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 230.500 273.341 163.308 1.00 93.23  ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 233.020 269.576 167.486 1.00 81.96  ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 232.554 269.613 168.870 1.00 78.14  ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 233.690 270.016 169.801 1.00 79.47  ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 233.490 270.777 170.756 1.00 84.97  ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 231.950 268.252 169.265 1.00 82.82  ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 231.686 268.197 170.762 1.00 80.72  ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 230.672 267.994 168.487 1.00 83.02  ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 234.901 269.519 169.534 1.00 79.78  ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 236.039 269.827 170.395 1.00 76.55  ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 236.347 271.319 170.401 1.00 77.95  ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 236.646 271.890 171.455 1.00 84.10  ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 237.267 269.030 169.951 1.00 75.02  ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 237.059 267.523 169.899 1.00 78.65  ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 236.998 266.884 171.274 1.00 83.12  ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 237.235 267.589 172.278 1.00 85.39  ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 236.711 265.671 171.352 1.00 84.05  ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 236.278 271.966 169.234 1.00 76.09  ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 236.580 273.393 169.154 1.00 80.41  ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 235.650 274.209 170.043 1.00 81.68  ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 236.058 275.224 170.619 1.00 80.53  ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 236.486 273.873 167.705 1.00 80.94  ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 235.118 273.856 167.280 1.00 80.96  ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 237.308 272.975 166.792 1.00 80.01  ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 234.391 273.784 170.160 1.00 73.15  ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 233.464 274.446 171.071 1.00 70.40  ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 233.915 274.268 172.516 1.00 73.65  ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 233.877 275.212 173.314 1.00 76.96  ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 232.035 273.917 170.851 1.00 71.15  ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 231.098 274.442 171.928 1.00 74.53  ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 231.534 274.301 169.468 1.00 71.27  ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 234.358 273.061 172.873 1.00 65.83  ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 234.721 272.773 174.256 1.00 63.96  ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 236.096 273.312 174.633 1.00 64.88  ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 236.439 273.311 175.820 1.00 68.32  ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 234.669 271.266 174.509 1.00 64.54  ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 235.569 270.575 173.660 1.00 68.98  ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 236.892 273.764 173.661 1.00 63.66  ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 238.200 274.325 173.987 1.00 66.89  ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 238.063 275.640 174.744 1.00 67.19  ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 238.885 275.952 175.615 1.00 67.07  ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 239.028 274.524 172.717 1.00 68.10  ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 239.397 273.238 172.001 1.00 69.46  ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 240.268 272.330 172.845 1.00 72.06  ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 239.825 271.278 173.306 1.00 72.09  ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 241.517 272.733 173.051 1.00 69.12  ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 237.037 276.429 174.419 1.00 68.07  ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 236.832 277.701 175.105 1.00 66.04  ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 236.517 277.489 176.580 1.00 68.22  ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 236.986 278.246 177.438 1.00 68.33  ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 235.714 278.487 174.421 1.00 66.84  ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 235.438 279.846 175.039 1.00 70.27  ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 234.144 280.458 174.544 1.00 72.64  ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 233.419 279.853 173.754 1.00 71.90  ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 233.846 281.667 175.006 1.00 71.77  ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 235.726 276.467 176.895 1.00 62.57  ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 235.344 276.163 178.267 1.00 58.24  ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 236.392 275.343 179.009 1.00 56.01  ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 236.213 275.072 180.201 1.00 60.26  ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 234.006 275.419 178.286 1.00 56.54  ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 232.855 276.218 177.720 1.00 57.55  ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 232.382 277.348 178.372 1.00 61.68  ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 232.245 275.846 176.530 1.00 57.48  ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 231.332 278.083 177.859 1.00 64.19  ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 231.194 276.574 176.008 1.00 64.90  ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 230.742 277.692 176.676 1.00 66.80  ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 229.695 278.421 176.161 1.00 68.64  ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 237.466 274.937 178.335 1.00 53.22  ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 238.498 274.141 178.995 1.00 55.82  ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 239.172 274.856 180.163 1.00 56.12  ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 239.365 274.211 181.208 1.00 56.32  ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 239.536 273.681 177.962 1.00 57.69  ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 240.464 272.546 178.396 1.00 56.52  ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 239.713 271.224 178.429 1.00 54.13  ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 241.672 272.458 177.478 1.00 53.77  ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 239.569 276.135 180.069 1.00 56.29  ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 240.188 276.783 181.242 1.00 55.81  ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 239.298 276.803 182.475 1.00 55.64  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 239.805 276.727 183.602 1.00 55.79  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 240.490 278.196 180.729 1.00 53.14  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 240.674 278.028 179.273 1.00 52.64  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 239.668 276.991 178.871 1.00 55.72  ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 237.981 276.914 182.294 1.00 48.93  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 237.073 276.900 183.437 1.00 41.00  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 237.124 275.559 184.160 1.00 48.79  ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 237.106 275.506 185.395 1.00 57.68  ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 235.648 277.213 182.979 1.00 48.97  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 234.567 277.121 184.057 1.00 52.98  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 234.790 278.172 185.133 1.00 49.84  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 233.185 277.265 183.445 1.00 51.74  ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 237.186 274.462 183.402 1.00 47.87  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 237.260 273.139 184.014 1.00 41.37  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 238.542 272.974 184.820 1.00 45.64  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 238.535 272.359 185.893 1.00 49.08  ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 237.157 272.057 182.940 1.00 45.06  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 238.294 272.068 182.095 1.00 52.07  ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 239.656 273.509 184.313 1.00 43.17  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 240.912 273.444 185.053 1.00 42.23  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 240.815 274.206 186.369 1.00 44.60  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 241.320 273.747 187.401 1.00 46.12  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 242.055 273.994 184.199 1.00 48.00  ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 242.111 273.279 182.958 1.00 52.91  ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 243.385 273.845 184.923 1.00 42.37  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 240.168 275.374 186.352 1.00 49.04  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 239.974 276.131 187.584 1.00 45.17  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 239.107 275.362 188.572 1.00 44.45  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 239.351 275.399 189.784 1.00 49.70  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 239.354 277.493 187.272 1.00 40.73  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 238.083 274.665 188.073 1.00 43.51  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 237.214 273.888 188.951 1.00 38.44  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 237.986 272.780 189.658 1.00 42.92  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 237.806 272.559 190.861 1.00 49.85  ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 236.053 273.302 188.151 1.00 35.96  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 234.901 274.525 187.497 1.00 55.25  ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 238.844 272.067 188.925 1.00 43.47  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 239.646 271.017 189.544 1.00 42.12  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 240.620 271.595 190.562 1.00 48.78  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 240.815 271.024 191.641 1.00 52.94  ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 240.396 270.227 188.472 1.00 43.08  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 241.476 270.978 187.947 1.00 48.58  ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 241.245 272.728 190.234 1.00 44.40  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 242.166 273.362 191.171 1.00 35.78  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 241.441 273.841 192.421 1.00 40.88  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 241.973 273.742 193.533 1.00 46.94  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 242.888 274.525 190.491 1.00 39.84  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 243.641 274.077 189.378 1.00 52.33  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 240.227 274.371 192.259 1.00 41.58  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 239.472 274.869 193.406 1.00 35.18  ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 239.103 273.723 194.340 1.00 38.70  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 239.309 273.802 195.557 1.00 49.71  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 238.224 275.639 192.937 1.00 36.16  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 238.608 277.039 192.456 1.00 42.31  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 237.197 275.731 194.056 1.00 37.38  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 237.431 277.866 191.991 1.00 35.45  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 238.560 272.636 193.784 1.00 37.79  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 238.101 271.531 194.621 1.00 35.02  ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 239.253 270.888 195.381 1.00 43.98  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 239.125 270.580 196.572 1.00 57.70  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 237.380 270.484 193.773 1.00 43.76  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 237.240 269.146 194.467 1.00 42.98  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 236.296 268.957 195.467 1.00 43.72  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 238.058 268.075 194.128 1.00 43.25  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 236.167 267.740 196.107 1.00 48.67  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 237.936 266.854 194.762 1.00 42.62  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 236.989 266.692 195.750 1.00 49.11  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 236.864 265.478 196.384 1.00 49.62  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 240.386 270.666 194.711 1.00 35.22  ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 241.526 270.059 195.388 1.00 35.25  ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 242.110 270.988 196.443 1.00 46.15  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 242.759 270.521 197.386 1.00 52.02  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 242.588 269.652 194.368 1.00 45.70  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 242.337 268.310 193.742 1.00 50.74  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 241.460 268.178 192.680 1.00 47.21  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 242.973 267.178 194.223 1.00 49.78  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 241.224 266.944 192.106 1.00 42.77  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 242.742 265.941 193.653 1.00 48.24  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 241.866 265.824 192.593 1.00 48.21  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 241.900 272.298 196.302 1.00 39.93  ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 242.222 273.212 197.391 1.00 37.02  ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 241.285 272.994 198.572 1.00 39.64  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 241.718 273.001 199.730 1.00 47.73  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 242.152 274.660 196.902 1.00 42.91  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 243.141 274.871 195.887 1.00 43.23  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 242.405 275.627 198.048 1.00 42.13  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 239.994 272.790 198.295 1.00 41.06  ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 239.043 272.466 199.354 1.00 36.44  ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 239.364 271.120 199.990 1.00 43.96  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 239.264 270.962 201.213 1.00 52.17  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 237.619 272.459 198.798 1.00 32.35  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 237.284 273.640 197.909 1.00 34.78  ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 235.523 274.018 197.889 1.00 60.80  ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 234.823 272.371 197.879 1.00 44.59  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 239.739 270.133 199.172 1.00 45.03  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 240.027 268.801 199.694 1.00 43.55  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 241.216 268.822 200.645 1.00 49.61  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 241.206 268.146 201.680 1.00 62.36  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 240.280 267.831 198.540 1.00 44.84  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 240.518 266.396 198.976 1.00 54.36  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 240.725 265.457 197.804 1.00 60.77  ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 240.705 265.933 196.649 1.00 59.53  ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 240.908 264.244 198.036 1.00 57.05  ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 242.250 269.594 200.313 1.00 43.30  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 243.432 269.680 201.159 1.00 51.24  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 243.308 270.737 202.249 1.00 51.30  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 244.273 270.955 202.988 1.00 46.76  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 244.671 269.952 200.302 1.00 53.25  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 244.798 271.328 200.002 1.00 58.59  ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 242.152 271.399 202.363 1.00 50.14  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 241.922 272.313 203.477 1.00 34.62  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 241.846 271.583 204.810 1.00 43.23  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 241.943 272.223 205.862 1.00 49.72  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 240.636 273.112 203.255 1.00 33.47  ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 240.747 274.443 202.511 1.00 40.44  ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 239.366 275.004 202.218 1.00 36.50  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 241.572 275.437 203.309 1.00 46.76  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 241.663 270.261 204.791 1.00 47.65  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 241.616 269.489 206.027 1.00 41.55  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 242.967 269.430 206.726 1.00 49.34  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 243.028 269.040 207.896 1.00 49.58  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 241.117 268.073 205.737 1.00 38.32  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 242.095 267.227 204.938 1.00 42.18  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 241.676 265.768 204.912 1.00 46.00  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 240.340 265.593 204.210 1.00 48.55  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 240.416 265.980 202.775 1.00 49.37  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 244.049 269.801 206.037 1.00 51.17  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 245.370 269.758 206.653 1.00 48.02  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 245.547 270.852 207.698 1.00 52.60  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 246.262 270.652 208.686 1.00 58.28  ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 246.454 269.871 205.582 1.00 47.16  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 246.347 268.836 204.476 1.00 50.33  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 246.376 267.416 205.004 1.00 55.84  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 245.472 266.624 204.739 1.00 58.54  ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 247.418 267.086 205.757 1.00 50.84  ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 244.911 272.009 207.504 1.00 44.84  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 245.076 273.114 208.441 1.00 49.70  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 244.080 273.067 209.595 1.00 49.75  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 244.289 273.750 210.608 1.00 52.44  ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 244.966 274.469 207.719 1.00 45.33  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 243.564 274.658 207.137 1.00 44.92  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 246.010 274.569 206.619 1.00 49.72  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 243.304 276.056 206.621 1.00 41.47  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 243.010 272.283 209.477 1.00 41.99  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 242.036 272.145 210.550 1.00 42.72  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 241.208 270.894 210.298 1.00 44.81  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 240.862 270.594 209.153 1.00 56.48  ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 241.129 273.376 210.648 1.00 45.84  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 240.495 273.557 211.991 1.00 48.17  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 239.493 272.735 212.458 1.00 48.65  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 240.719 274.468 212.967 1.00 43.44  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 239.127 273.131 213.665 1.00 45.71  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 239.857 274.180 213.997 1.00 47.18  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 240.896 270.170 211.376 1.00 41.46  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 240.135 268.932 211.244 1.00 41.96  ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 238.704 269.190 210.789 1.00 39.46  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 238.093 268.323 210.155 1.00 48.34  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 240.141 268.169 212.570 1.00 41.91  ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 239.593 268.957 213.729 1.00 45.39  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 238.235 268.962 214.003 1.00 42.05  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 240.437 269.691 214.544 1.00 46.58  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 237.730 269.687 215.064 1.00 46.36  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 239.938 270.416 215.609 1.00 44.94  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 238.583 270.414 215.869 1.00 43.71  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 238.156 270.364 211.102 1.00 34.71  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 236.760 270.654 210.801 1.00 34.98  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 236.512 270.922 209.324 1.00 36.72  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 235.358 270.869 208.886 1.00 43.49  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 236.288 271.855 211.625 1.00 36.70  ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 234.781 272.012 211.830 1.00 38.16  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 234.279 271.056 212.900 1.00 39.56  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 234.437 273.448 212.186 1.00 34.40  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 237.556 271.200 208.545 1.00 39.53  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 237.387 271.591 207.145 1.00 42.01  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 237.277 270.340 206.271 1.00 46.02  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 238.138 270.028 205.447 1.00 49.56  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 238.531 272.493 206.697 1.00 39.16  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 238.721 273.741 207.536 1.00 40.46  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 237.715 274.203 208.377 1.00 43.06  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 239.905 274.464 207.476 1.00 41.15  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 237.890 275.338 209.144 1.00 34.92  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 240.085 275.604 208.235 1.00 41.48  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 239.075 276.035 209.067 1.00 42.78  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 239.250 277.169 209.826 1.00 50.72  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 236.178 269.618 206.472 1.00 37.86  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 235.869 268.422 205.701 1.00 32.49  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 234.830 268.773 204.644 1.00 41.09  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 233.706 269.161 204.978 1.00 43.02  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 235.357 267.303 206.607 1.00 33.54  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 236.235 267.027 207.815 1.00 41.20  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 237.622 266.553 207.432 1.00 37.34  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 237.785 265.751 206.513 1.00 42.67  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 238.631 267.046 208.139 1.00 37.22  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 235.206 268.638 203.375 1.00 43.43  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 234.334 268.975 202.259 1.00 39.44  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 234.288 267.807 201.287 1.00 45.68  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 235.334 267.311 200.857 1.00 45.59  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 234.816 270.243 201.547 1.00 35.91  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 234.969 271.432 202.466 1.00 36.36  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 233.865 271.998 203.090 1.00 44.65  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 236.217 271.986 202.715 1.00 39.96  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 234.000 273.083 203.934 1.00 36.05  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 236.361 273.072 203.557 1.00 42.47  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 235.250 273.616 204.164 1.00 41.79  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 235.388 274.696 205.003 1.00 53.84  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 233.080 267.373 200.946 1.00 41.35  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 232.888 266.285 200.003 1.00 37.52  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 232.848 266.819 198.573 1.00 41.43  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 232.744 268.023 198.331 1.00 51.37  ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 231.606 265.518 200.324 1.00 42.22  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 230.469 266.357 200.215 1.00 44.49  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 232.943 265.895 197.613 1.00 43.15  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 232.861 266.280 196.209 1.00 37.04  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 231.492 266.855 195.868 1.00 37.14  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 231.386 267.736 195.008 1.00 45.38  ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 233.176 265.080 195.315 1.00 42.72  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 233.095 265.300 193.803 1.00 40.79  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 234.114 266.335 193.356 1.00 39.73  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 233.295 263.990 193.058 1.00 42.33  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 230.439 266.376 196.534 1.00 38.81  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 229.102 266.906 196.290 1.00 35.21  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 228.990 268.367 196.706 1.00 36.90  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 228.238 269.128 196.086 1.00 49.18  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 228.059 266.065 197.024 1.00 42.70  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 226.630 266.306 196.564 1.00 44.63  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 226.514 266.430 195.058 1.00 48.21  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 226.828 265.496 194.320 1.00 44.72  ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 226.062 267.588 194.593 1.00 42.25  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 229.722 268.775 197.745 1.00 39.48  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 229.686 270.169 198.178 1.00 32.44  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 230.192 271.096 197.079 1.00 41.63  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 229.616 272.161 196.834 1.00 49.38  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 230.510 270.343 199.454 1.00 37.57  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 230.443 271.726 200.036 1.00 43.58  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 229.227 272.372 200.183 1.00 47.67  ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 231.596 272.379 200.435 1.00 40.09  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 229.164 273.645 200.718 1.00 45.66  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 231.538 273.651 200.971 1.00 35.23  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 230.321 274.284 201.112 1.00 42.63  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 231.277 270.705 196.407 1.00 41.66  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 231.775 271.497 195.289 1.00 39.01  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 230.812 271.471 194.109 1.00 38.94  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 230.663 272.481 193.411 1.00 42.79  ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 233.153 270.996 194.858 1.00 35.93  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 233.694 271.689 193.643 1.00 43.36  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 234.172 272.986 193.725 1.00 45.54  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 233.720 271.048 192.416 1.00 41.27  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 234.668 273.628 192.609 1.00 43.19  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 234.215 271.685 191.296 1.00 42.75  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 234.689 272.978 191.393 1.00 45.36  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 230.160 270.332 193.866 1.00 37.44  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 229.233 270.235 192.743 1.00 36.76  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 228.017 271.131 192.947 1.00 38.87  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 227.487 271.693 191.982 1.00 52.70  ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 228.807 268.782 192.537 1.00 44.95  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 229.915 267.832 192.075 1.00 43.07  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 229.372 266.428 191.864 1.00 43.35  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 230.576 268.353 190.809 1.00 34.33  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 227.555 271.270 194.193 1.00 37.65  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 226.479 272.215 194.474 1.00 40.79  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 226.922 273.645 194.193 1.00 45.49  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 226.140 274.458 193.687 1.00 44.40  ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 226.011 272.074 195.923 1.00 41.31  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 225.665 270.645 196.288 1.00 56.57  ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 225.398 269.843 195.369 1.00 58.82  ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 225.661 270.324 197.494 1.00 51.51  ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 228.172 273.972 194.526 1.00 44.33  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 228.714 275.288 194.199 1.00 32.63  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 228.760 275.478 192.689 1.00 46.20  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 228.366 276.525 192.162 1.00 57.30  ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 230.106 275.466 194.831 1.00 38.03  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 230.005 275.490 196.356 1.00 43.37  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 230.771 276.732 194.316 1.00 37.86  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 231.346 275.451 197.055 1.00 35.61  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 229.241 274.461 191.969 1.00 48.58  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 229.320 274.550 190.515 1.00 38.82  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 227.934 274.637 189.888 1.00 38.73  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 227.715 275.418 188.955 1.00 52.64  ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 230.087 273.350 189.961 1.00 45.48  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 230.605 273.552 188.558 1.00 47.08  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 231.070 274.791 188.143 1.00 48.92  ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 230.634 272.502 187.651 1.00 42.08  ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 231.546 274.982 186.862 1.00 48.25  ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 231.109 272.683 186.368 1.00 46.30  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 231.564 273.924 185.980 1.00 48.98  ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 232.040 274.110 184.704 1.00 54.22  ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 226.988 273.835 190.382 1.00 40.11  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 225.626 273.882 189.859 1.00 44.17  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 224.980 275.237 190.122 1.00 48.83  ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 224.278 275.774 189.258 1.00 56.60  ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 224.792 272.757 190.474 1.00 48.58  ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 223.348 272.782 190.078 1.00 58.45  ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 222.842 271.997 189.064 1.00 59.47  ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 222.300 273.487 190.566 1.00 54.85  ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 221.546 272.222 188.941 1.00 56.80  ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 221.193 273.123 189.840 1.00 56.33  ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 225.200 275.800 191.312 1.00 47.99  ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 224.639 277.109 191.630 1.00 50.40  ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 225.220 278.193 190.730 1.00 50.24  ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 224.491 279.068 190.250 1.00 57.23  ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 224.888 277.440 193.101 1.00 51.59  ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 224.628 278.897 193.423 1.00 54.60  ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 225.551 279.653 193.725 1.00 53.66  ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 223.364 279.300 193.362 1.00 53.65  ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 226.532 278.155 190.496 1.00 52.91  ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 227.165 279.149 189.634 1.00 48.05  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 226.668 279.008 188.200 1.00 51.60  ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 226.370 280.003 187.527 1.00 54.08  ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 228.698 279.027 189.717 1.00 48.61  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 229.360 279.802 188.588 1.00 51.97  ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 229.196 279.516 191.067 1.00 51.45  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 226.567 277.770 187.711 1.00 56.83  ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 226.204 277.550 186.315 1.00 51.22  ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 224.755 277.936 186.040 1.00 51.27  ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 224.462 278.578 185.024 1.00 54.51  ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 226.447 276.090 185.934 1.00 43.87  ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 227.894 275.706 185.627 1.00 46.21  ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 227.977 274.264 185.160 1.00 55.53  ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 228.477 276.643 184.586 1.00 50.87  ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 223.847 277.533 186.931 1.00 59.49  ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 222.401 277.773 186.680 1.00 57.73  ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 221.885 278.915 187.559 1.00 59.39  ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 221.385 279.912 187.004 1.00 63.42  ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 221.621 276.481 186.930 1.00 55.41  ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 222.094 275.312 186.105 1.00 59.49  ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 221.975 275.319 184.726 1.00 59.59  ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 222.691 274.212 186.697 1.00 57.09  ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 222.412 274.253 183.958 1.00 58.03  ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 223.138 273.139 185.944 1.00 59.85  ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 222.998 273.159 184.568 1.00 61.47  ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 223.436 272.102 183.808 1.00 63.17  ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 222.003 278.775 188.881 1.00 66.40  ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 221.454 279.800 189.808 1.00 66.26  ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 222.415 280.992 189.872 1.00 66.09  ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 222.886 281.311 190.982 1.00 66.55  ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 221.246 279.177 191.189 1.00 61.97  ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 220.900 277.701 191.126 1.00 67.15  ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 220.988 276.964 192.451 1.00 72.42  ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 221.311 277.611 193.466 1.00 72.32  ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 220.738 275.742 192.463 1.00 70.74  ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 222.690 281.621 188.725 1.00 61.94  ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 223.610 282.790 188.683 1.00 62.88  ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 222.805 284.052 188.358 1.00 67.79  ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 222.351 284.186 187.204 1.00 68.95  ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 224.750 282.582 187.683 1.00 63.09  ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 225.753 283.716 187.679 1.00 64.54  ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 225.608 284.685 188.421 1.00 66.85  ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 226.776 283.604 186.848 1.00 64.21  ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 222.620 284.984 189.318 1.00 78.78  ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 221.909 286.237 189.056 1.00 77.77  ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 222.633 287.045 187.972 1.00 77.07  ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 221.967 287.635 187.142 1.00 78.70  ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 221.981 286.986 190.394 1.00 79.93  ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 222.217 285.899 191.419 1.00 78.20  ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 223.074 284.876 190.705 1.00 78.46  ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 223.969 287.044 188.004 1.00 74.33  ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 224.763 287.805 187.003 1.00 75.50  ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 224.397 287.310 185.601 1.00 77.11  ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 224.258 288.158 184.698 1.00 79.61  ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 226.264 287.702 187.284 1.00 73.33  ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 226.643 288.272 188.634 1.00 76.91  ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 226.444 289.457 188.891 1.00 81.07  ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 227.187 287.437 189.504 1.00 74.13  ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 224.240 285.995 185.430 1.00 77.10  ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 223.805 285.447 184.117 1.00 73.66  ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 222.278 285.522 184.034 1.00 78.72  ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 221.642 284.459 183.898 1.00 79.21  ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 224.293 284.001 183.987 1.00 74.01  ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 225.773 283.842 183.645 1.00 75.80  ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 226.032 282.494 182.994 1.00 70.20  ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 226.235 284.969 182.736 1.00 78.64  ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 221.720 286.734 184.115 1.00 91.52  ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 220.244 286.908 184.074 1.00 88.70  ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 219.791 287.044 182.617 1.00 91.78  ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 219.026 286.175 182.157 1.00 93.60  ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 219.827 288.135 184.889 1.00 89.08  ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 218.332 288.425 184.897 1.00 92.38  ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 217.504 287.247 185.363 1.00 93.21  ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 216.015 287.516 185.322 1.00 92.74  ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 215.232 286.334 185.755 1.00 91.20  ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 220.244 288.095 181.927 1.00 90.20  ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 219.852 288.305 180.549 1.00 89.42  ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 221.010 288.338 179.574 1.00 89.99  ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 220.842 288.741 178.419 1.00 93.16  ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 222.194 287.917 180.024 1.00 84.85  ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 223.362 287.922 179.153 1.00 85.12  ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 223.219 286.830 178.105 1.00 87.12  ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 222.889 285.680 178.420 1.00 87.38  ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 224.645 287.747 179.980 1.00 83.42  ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 225.872 288.014 179.121 1.00 81.99  ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 224.624 288.668 181.188 1.00 84.17  ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 223.465 287.189 176.844 1.00 86.59  ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 223.351 286.254 175.732 1.00 85.65  ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 224.685 285.860 175.121 1.00 85.16  ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 224.794 284.761 174.573 1.00 84.41  ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 222.462 286.843 174.628 1.00 86.23  ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 223.053 288.049 174.128 1.00 87.89  ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 221.075 287.151 175.170 1.00 84.74  ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 225.695 286.724 175.193 1.00 82.18  ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 226.995 286.405 174.622 1.00 81.61  ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 227.649 285.262 175.388 1.00 85.76  ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 227.667 285.249 176.622 1.00 88.67  ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 227.899 287.637 174.640 1.00 81.38  ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 229.160 287.450 173.819 1.00 84.78  ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 229.269 286.426 173.112 1.00 86.93  ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 230.045 288.330 173.878 1.00 83.22  ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 228.192 284.295 174.644 1.00 83.10  ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 228.810 283.135 175.277 1.00 79.48  ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 230.099 283.514 175.997 1.00 75.72  ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 230.372 283.014 177.095 1.00 80.62  ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 229.074 282.049 174.235 1.00 80.76  ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 227.829 281.445 173.665 1.00 84.39  ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 226.839 280.898 174.453 1.00 83.08  ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 227.412 281.302 172.385 1.00 82.39  ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 225.866 280.445 173.682 1.00 80.42  ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 226.190 280.677 172.423 1.00 81.22  ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 230.907 284.387 175.392 1.00 71.15  ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 232.148 284.812 176.033 1.00 77.22  ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 231.871 285.592 177.313 1.00 77.45  ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 232.553 285.396 178.326 1.00 77.89  ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 232.981 285.650 175.064 1.00 81.06  ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 233.177 284.922 173.846 1.00 79.33  ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 234.336 285.980 175.672 1.00 79.68  ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 230.876 286.482 177.286 1.00 75.52  ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 230.536 287.247 178.482 1.00 74.97  ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 229.999 286.343 179.584 1.00 75.75  ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 230.329 286.525 180.762 1.00 79.37  ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 229.521 288.336 178.137 1.00 76.66  ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 230.066 289.422 177.225 1.00 79.76  ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 229.029 290.475 176.888 1.00 81.74  ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 227.868 290.369 177.282 1.00 80.77  ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 229.445 291.501 176.153 1.00 78.97  ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 229.164 285.366 179.222 1.00 66.46  ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 228.624 284.448 180.220 1.00 62.51  ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 229.724 283.594 180.838 1.00 63.79  ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 229.704 283.319 182.043 1.00 71.76  ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 227.543 283.566 179.594 1.00 62.35  ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 226.241 284.297 179.312 1.00 63.34  ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 225.188 283.364 178.739 1.00 62.71  ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 224.810 282.321 179.684 1.00 63.50  ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 223.637 282.259 180.299 1.00 67.04  ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 222.700 283.171 180.095 1.00 64.91  ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 223.397 281.257 181.140 1.00 70.27  ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 230.690 283.158 180.025 1.00 63.41  ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 231.795 282.361 180.550 1.00 62.15  ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 232.639 283.164 181.533 1.00 62.70  ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 233.064 282.640 182.569 1.00 66.51  ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 232.659 281.839 179.402 1.00 62.85  ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 233.830 280.937 179.795 1.00 63.09  ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 233.368 279.823 180.721 1.00 61.84  ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 234.504 280.365 178.559 1.00 63.55  ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 232.898 284.436 181.221 1.00 59.40  ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 233.654 285.282 182.139 1.00 61.60  ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 232.893 285.497 183.441 1.00 62.72  ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 233.492 285.519 184.523 1.00 63.79  ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 233.974 286.622 181.477 1.00 62.34  ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 232.815 287.430 181.376 1.00 67.76  ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 231.572 285.667 183.354 1.00 63.49  ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 230.756 285.816 184.556 1.00 58.28  ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 230.798 284.541 185.389 1.00 60.04  ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 230.937 284.588 186.618 1.00 67.01  ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 229.314 286.197 184.176 1.00 56.77  ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 229.254 287.647 183.693 1.00 58.69  ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 228.379 285.989 185.352 1.00 60.39  ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 227.941 288.018 183.041 1.00 60.98  ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 230.679 283.383 184.735 1.00 58.16  ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 230.701 282.111 185.452 1.00 50.43  ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 232.046 281.908 186.138 1.00 47.87  ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 232.110 281.481 187.298 1.00 54.54  ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 230.372 280.953 184.491 1.00 49.48  ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 228.877 280.934 184.173 1.00 53.72  ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 230.803 279.621 185.083 1.00 58.62  ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 228.517 280.077 182.981 1.00 54.95  ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 233.140 282.214 185.437 1.00 45.94  ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 234.465 282.066 186.032 1.00 52.94  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 234.641 282.993 187.228 1.00 56.74  ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 235.208 282.595 188.253 1.00 62.00  ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 235.546 282.334 184.984 1.00 53.83  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 235.256 281.590 183.794 1.00 60.39  ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 236.912 281.921 185.510 1.00 48.42  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 234.167 284.235 187.115 1.00 55.57  ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 234.261 285.170 188.232 1.00 52.55  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 233.416 284.707 189.413 1.00 57.87  ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 233.866 284.742 190.564 1.00 59.51  ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 233.836 286.568 187.784 1.00 52.74  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 233.788 287.587 188.910 1.00 60.16  ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 233.286 288.935 188.422 1.00 59.04  ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 233.382 289.986 189.516 1.00 58.24  ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 232.889 291.314 189.058 1.00 55.01  ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 232.185 284.265 189.146 1.00 53.26  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 231.294 283.851 190.223 1.00 50.17  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 231.674 282.499 190.808 1.00 53.52  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 231.278 282.196 191.938 1.00 59.35  ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 229.848 283.813 189.726 1.00 51.69  ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 229.299 285.194 189.432 1.00 64.97  ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 229.746 286.164 190.081 1.00 64.01  ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 228.421 285.312 188.553 1.00 72.83  ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 232.422 281.678 190.068 1.00 52.93  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 232.863 280.396 190.607 1.00 44.98  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 233.791 280.597 191.799 1.00 44.28  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 233.673 279.907 192.817 1.00 47.29  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 233.554 279.578 189.516 1.00 47.58  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 234.266 278.303 189.971 1.00 47.04  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 233.259 277.210 190.295 1.00 49.28  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 235.251 277.835 188.914 1.00 47.54  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 234.723 281.545 191.688 1.00 48.72  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 235.623 281.832 192.800 1.00 48.61  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 234.882 282.497 193.953 1.00 50.05  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 235.160 282.216 195.124 1.00 52.81  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 236.778 282.714 192.324 1.00 42.56  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 237.803 281.981 191.508 1.00 46.96  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 238.867 281.341 192.120 1.00 46.90  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 237.701 281.932 190.128 1.00 45.11  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 239.811 280.667 191.371 1.00 45.26  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 238.642 281.259 189.374 1.00 46.03  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 239.698 280.626 189.996 1.00 48.76  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 233.939 283.389 193.640 1.00 47.64  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 233.220 284.110 194.685 1.00 43.21  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 232.330 283.173 195.493 1.00 46.83  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 232.348 283.194 196.729 1.00 55.58  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 232.394 285.238 194.066 1.00 49.29  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 231.697 286.130 195.080 1.00 47.82  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 232.672 286.872 195.972 1.00 47.46  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 233.361 287.790 195.528 1.00 55.97  ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 232.736 286.476 197.237 1.00 43.67  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 231.543 282.340 194.809 1.00 41.50  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 230.614 281.456 195.507 1.00 37.77  ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 231.371 280.390 196.289 1.00 36.18  ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 230.976 280.021 197.402 1.00 43.07  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 229.618 280.837 194.509 1.00 37.06  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 228.777 279.764 195.184 1.00 36.50  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 228.726 281.916 193.919 1.00 43.94  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 232.470 279.881 195.727 1.00 40.22  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 233.266 278.881 196.432 1.00 39.88  ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 233.821 279.444 197.734 1.00 42.70  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 233.814 278.768 198.769 1.00 47.90  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 234.397 278.380 195.535 1.00 36.98  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 234.314 280.684 197.699 1.00 38.99  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 234.800 281.316 198.920 1.00 32.08  ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 233.668 281.548 199.913 1.00 41.19  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 233.823 281.287 201.111 1.00 48.98  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 235.497 282.636 198.590 1.00 37.85  ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 236.000 283.372 199.799 1.00 46.70  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 237.167 282.976 200.431 1.00 50.14  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 235.305 284.458 200.306 1.00 44.04  ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 237.631 283.649 201.545 1.00 41.79  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 235.765 285.134 201.418 1.00 41.71  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 236.929 284.729 202.038 1.00 41.12  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 232.520 282.031 199.434 1.00 42.95  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 231.425 282.382 200.335 1.00 31.91  ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 230.915 281.160 201.089 1.00 41.35  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 230.656 281.225 202.296 1.00 57.33  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 230.290 283.040 199.550 1.00 30.06  ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 230.683 284.385 198.976 1.00 47.26  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 231.801 284.856 199.178 1.00 58.32  ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 229.762 285.011 198.253 1.00 45.55  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 230.763 280.033 200.392 1.00 39.43  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 230.229 278.838 201.037 1.00 33.67  ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 231.254 278.201 201.969 1.00 38.06  ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 230.910 277.771 203.075 1.00 52.46  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 229.764 277.838 199.980 1.00 33.97  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 228.633 278.355 199.106 1.00 32.45  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 227.727 277.230 198.640 1.00 34.64  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 226.655 277.720 197.782 1.00 41.09  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 225.687 276.963 197.285 1.00 49.13  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 225.624 275.666 197.539 1.00 51.30  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 224.759 277.521 196.513 1.00 45.28  ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 232.514 278.127 201.538 1.00 36.07  ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 233.540 277.477 202.349 1.00 33.76  ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 233.875 278.320 203.573 1.00 43.30  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 233.975 277.804 204.693 1.00 48.46  ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 234.791 277.191 201.500 1.00 36.45  ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 235.966 276.814 202.389 1.00 38.91  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 234.502 276.087 200.506 1.00 42.20  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 234.047 279.631 203.383 1.00 40.27  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 234.446 280.490 204.492 1.00 27.40  ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 233.351 280.640 205.538 1.00 34.94  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 233.643 281.050 206.666 1.00 52.81  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 234.864 281.867 203.977 1.00 31.23  ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 232.101 280.322 205.195 1.00 41.45  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 231.038 280.335 206.192 1.00 36.05  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 231.222 279.242 207.234 1.00 38.14  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 230.645 279.334 208.322 1.00 44.37  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 229.674 280.188 205.517 1.00 42.53  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 229.061 281.505 205.070 1.00 47.08  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 229.176 282.568 206.149 1.00 52.01  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 228.558 283.824 205.744 1.00 53.39  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 228.617 284.948 206.445 1.00 53.25  ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 229.262 285.010 207.598 1.00 50.20  ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 228.015 286.037 205.976 1.00 47.29  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 232.011 278.215 206.926 1.00 36.49  ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 232.304 277.160 207.874 1.00 36.80  ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 233.781 277.074 208.193 1.00 39.14  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 234.325 275.981 208.376 1.00 41.85  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 234.441 278.228 208.259 1.00 39.28  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 235.856 278.307 208.585 1.00 36.03  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 236.070 279.381 209.640 1.00 41.86  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 235.300 280.341 209.737 1.00 45.54  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 236.711 278.629 207.347 1.00 34.97  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 237.090 277.418 206.511 1.00 43.91  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 238.368 277.769 205.288 1.00 48.22  ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 237.930 279.433 204.796 1.00 48.42  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 237.121 279.207 210.436 1.00 46.84  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 237.515 280.243 211.377 1.00 38.99  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 238.013 281.471 210.622 1.00 42.66  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 238.590 281.367 209.537 1.00 53.27  ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 238.598 279.727 212.323 1.00 42.35  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 238.215 278.534 213.200 1.00 39.45  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 239.413 278.048 213.999 1.00 46.23  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 237.065 278.897 214.124 1.00 42.13  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 237.775 282.647 211.208 1.00 41.63  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 238.109 283.891 210.521 1.00 35.35  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 239.608 284.010 210.275 1.00 43.78  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 240.037 284.661 209.316 1.00 46.68  ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 237.601 285.090 211.319 1.00 40.54  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 237.630 286.376 210.554 1.00 48.17  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 238.698 287.246 210.600 1.00 47.98  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 236.725 286.934 209.715 1.00 46.53  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 238.448 288.287 209.826 1.00 45.51  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 237.258 288.123 209.277 1.00 47.29  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 240.422 283.391 211.133 1.00 47.84  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 241.866 283.419 210.924 1.00 48.34  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 242.267 282.637 209.679 1.00 50.62  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 243.315 282.913 209.084 1.00 59.21  ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 242.587 282.871 212.156 1.00 49.19  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 242.315 281.403 212.437 1.00 46.93  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 242.999 280.916 213.698 1.00 54.02  ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 243.729 281.663 214.350 1.00 58.17  ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 242.767 279.657 214.048 1.00 49.39  ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 241.454 281.660 209.272 1.00 45.89  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 241.752 280.872 208.084 1.00 39.46  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 241.089 281.419 206.828 1.00 46.03  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 241.292 280.860 205.745 1.00 51.98  ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 241.321 279.419 208.295 1.00 43.16  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 241.924 278.809 209.544 1.00 57.99  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 243.163 278.851 209.689 1.00 59.38  ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 241.158 278.288 210.382 1.00 58.94  ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 240.299 282.489 206.947 1.00 44.58  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 239.621 283.048 205.781 1.00 41.52  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 240.620 283.594 204.768 1.00 41.08  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 240.468 283.395 203.558 1.00 47.37  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 238.646 284.143 206.217 1.00 43.13  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 237.344 283.620 206.738 1.00 37.59  ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 236.249 284.430 206.949 1.00 39.52  ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 236.961 282.370 207.089 1.00 35.03  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 235.247 283.701 207.409 1.00 40.87  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 235.653 282.448 207.503 1.00 42.25  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 241.649 284.295 205.249 1.00 47.08  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 242.638 284.873 204.344 1.00 47.56  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 243.454 283.778 203.668 1.00 44.57  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 243.826 283.898 202.495 1.00 52.56  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 243.532 285.880 205.095 1.00 49.48  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 244.496 286.569 204.126 1.00 39.84  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 244.282 285.206 206.238 1.00 46.10  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 243.806 287.385 203.056 1.00 43.53  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 243.737 282.690 204.390 1.00 41.58  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 244.543 281.610 203.829 1.00 36.86  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 243.865 280.994 202.611 1.00 45.75  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 244.511 280.729 201.591 1.00 52.97  ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 244.805 280.544 204.894 1.00 45.44  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 245.431 281.148 206.033 1.00 57.33  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 245.710 279.452 204.346 1.00 43.36  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 242.555 280.761 202.701 1.00 40.94  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 241.814 280.236 201.559 1.00 37.84  ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 241.766 281.253 200.426 1.00 42.87  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 241.859 280.893 199.247 1.00 52.03  ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 240.403 279.836 201.992 1.00 38.77  ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 239.625 279.114 200.931 1.00 43.24  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 240.223 278.130 200.161 1.00 41.01  ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 238.293 279.416 200.705 1.00 39.24  ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 239.508 277.464 199.185 1.00 39.08  ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 237.573 278.754 199.730 1.00 43.88  ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 238.182 277.776 198.970 1.00 43.33  ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 241.616 282.536 200.768 1.00 36.45  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 241.553 283.578 199.748 1.00 30.89  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 242.874 283.714 199.002 1.00 38.29  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 242.888 283.935 197.785 1.00 44.09  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 241.157 284.910 200.384 1.00 42.13  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 243.996 283.598 199.717 1.00 50.39  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 245.304 283.691 199.074 1.00 44.56  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 245.494 282.584 198.044 1.00 49.49  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 245.990 282.825 196.938 1.00 59.16  ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 246.412 283.638 200.128 1.00 43.40  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 246.442 284.824 201.076 1.00 49.13  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 246.720 286.385 200.224 1.00 76.27  ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 248.423 286.175 199.712 1.00 49.29  ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 245.100 281.358 198.394 1.00 39.82  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 245.233 280.246 197.458 1.00 39.89  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 244.254 280.379 196.299 1.00 47.23  ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 244.566 279.994 195.167 1.00 56.35  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 245.032 278.923 198.191 1.00 39.54  ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 245.916 278.752 199.427 1.00 47.21  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 245.327 277.716 200.357 1.00 45.09  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 247.334 278.375 199.028 1.00 46.02  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 243.061 280.916 196.564 1.00 38.93  ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 242.118 281.189 195.484 1.00 35.95  ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 242.680 282.230 194.525 1.00 42.00  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 242.492 282.137 193.306 1.00 49.32  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 240.777 281.649 196.058 1.00 41.26  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 239.861 280.561 196.619 1.00 40.53  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 238.532 281.156 197.052 1.00 39.39  ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 239.648 279.457 195.596 1.00 37.77  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 243.369 283.240 195.063 1.00 48.34  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 244.011 284.237 194.213 1.00 47.30  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 245.112 283.611 193.366 1.00 48.43  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 245.289 283.976 192.198 1.00 59.29  ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 244.570 285.374 195.068 1.00 50.81  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 245.868 282.673 193.941 1.00 47.26  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 246.918 282.000 193.182 1.00 50.67  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 246.334 281.184 192.036 1.00 57.52  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 246.910 281.137 190.942 1.00 64.38  ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 247.749 281.112 194.106 1.00 51.71  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 248.573 281.877 195.129 1.00 55.27  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 249.807 281.093 195.541 1.00 57.83  ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 250.662 280.784 194.401 1.00 63.02  ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 251.780 280.075 194.473 1.00 61.44  ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 252.213 279.581 195.621 1.00 58.39  ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 252.481 279.856 193.364 1.00 57.25  ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 245.195 280.527 192.269 1.00 54.24  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 244.548 279.756 191.210 1.00 46.40  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 244.126 280.674 190.069 1.00 48.22  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 244.329 280.363 188.889 1.00 60.16  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 243.351 278.967 191.773 1.00 48.84  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 243.828 277.925 192.786 1.00 44.56  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 242.571 278.302 190.651 1.00 53.19  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 242.703 277.210 193.497 1.00 49.08  ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 243.530 281.821 190.405 1.00 53.09  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 243.164 282.789 189.377 1.00 55.52  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 244.394 283.368 188.690 1.00 55.95  ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 244.354 283.656 187.489 1.00 59.56  ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 242.318 283.908 189.982 1.00 52.63  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 241.515 284.697 188.960 1.00 56.45  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 240.728 285.817 189.619 1.00 58.61  ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 239.746 286.447 188.646 1.00 54.78  ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 238.709 285.477 188.199 1.00 56.52  ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 245.489 283.547 189.432 1.00 61.68  ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 246.724 284.043 188.838 1.00 62.70  ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 247.321 283.050 187.850 1.00 69.66  ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 247.855 283.461 186.813 1.00 72.24  ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 247.739 284.372 189.934 1.00 61.23  ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 249.065 284.979 189.474 1.00 66.06  ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 248.819 286.199 188.602 1.00 69.71  ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 249.930 285.339 190.670 1.00 64.54  ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 247.244 281.751 188.148 1.00 66.48  ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 247.745 280.742 187.222 1.00 63.63  ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 246.947 280.702 185.925 1.00 68.30  ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 247.518 280.401 184.872 1.00 71.56  ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 247.729 279.363 187.883 1.00 62.28  ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 248.689 279.222 189.053 1.00 68.03  ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 248.630 277.824 189.649 1.00 69.05  ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 249.653 277.652 190.760 1.00 68.65  ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 249.340 278.503 191.942 1.00 66.72  ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 245.652 280.996 185.977 1.00 71.77  ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 244.805 281.020 184.804 1.00 70.54  ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 244.628 282.378 184.162 1.00 75.27  ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 243.769 282.522 183.285 1.00 74.64  ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 245.406 283.379 184.565 1.00 85.43  ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 245.284 284.712 183.998 1.00 85.38  ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 246.193 284.862 182.783 1.00 85.37  ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 247.345 284.420 182.782 1.00 83.24  ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 245.629 285.774 185.044 1.00 83.33  ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 244.811 285.584 186.205 1.00 82.65  ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 245.384 287.171 184.492 1.00 81.51  ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 245.660 285.495 181.742 1.00 92.10  ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 246.380 285.715 180.493 1.00 95.40  ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 247.218 286.977 180.640 1.00 96.66  ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 246.696 288.043 180.985 1.00 92.67  ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 245.415 285.828 179.302 1.00 95.88  ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 246.169 286.238 178.046 1.00 92.17  ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 244.682 284.513 179.087 1.00 93.57  ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 248.517 286.857 180.379 1.00 97.90  ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 249.419 287.987 180.450 1.00 94.36  ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 250.175 288.138 181.749 1.00 93.61  ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 250.844 289.161 181.940 1.00 92.99  ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 250.095 287.158 182.649 1.00 88.69  ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 250.788 287.248 183.922 1.00 86.93  ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 251.919 286.229 183.993 1.00 88.91  ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 251.731 285.069 183.609 1.00 90.42  ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 249.828 287.013 185.094 1.00 88.44  ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 248.807 288.119 185.299 1.00 89.22  ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 249.448 289.466 185.559 1.00 90.41  ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 250.322 289.550 186.447 1.00 89.47  ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 249.074 290.442 184.876 1.00 88.53  ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 253.096 286.629 184.470 1.00 89.80  ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 254.185 285.664 184.663 1.00 87.79  ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 253.818 284.621 185.708 1.00 87.59  ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 252.849 284.755 186.458 1.00 89.72  ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 255.360 286.534 185.124 1.00 85.54  ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 255.023 287.913 184.654 1.00 86.07  ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 253.529 288.012 184.722 1.00 86.14  ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 254.617 283.553 185.746 1.00 86.31  ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 254.344 282.468 186.682 1.00 90.29  ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 254.527 282.906 188.131 1.00 90.96  ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 253.834 282.396 189.019 1.00 89.52  ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 255.234 281.261 186.368 1.00 91.18  ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 254.932 280.191 187.273 1.00 89.90  ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 256.711 281.623 186.480 1.00 89.43  ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 255.444 283.844 188.387 1.00 85.31  ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 255.734 284.338 189.736 1.00 82.29  ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 256.094 283.205 190.692 1.00 82.86  ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 255.914 283.323 191.906 1.00 83.18  ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 254.566 285.155 190.297 1.00 81.82  ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 254.275 286.422 189.526 1.00 82.88  ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 255.246 287.401 189.369 1.00 81.30  ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 253.026 286.641 188.961 1.00 80.91  ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 254.984 288.561 188.666 1.00 79.12  ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 252.754 287.798 188.256 1.00 79.16  ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 253.736 288.754 188.113 1.00 82.04  ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 253.468 289.907 187.411 1.00 84.73  ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 256.601 282.094 190.151 1.00 89.70  ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 256.943 280.951 190.990 1.00 90.55  ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 258.082 281.286 191.945 1.00 91.74  ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 258.046 280.902 193.119 1.00 92.00  ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 257.306 279.750 190.118 1.00 91.94  ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 256.930 278.429 190.761 1.00 94.18  ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 256.621 278.422 191.971 1.00 92.14  ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 256.944 277.399 190.055 1.00 93.08  ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 259.101 281.999 191.458 1.00 89.40  ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 260.229 282.359 192.311 1.00 89.11  ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 259.803 283.298 193.433 1.00 90.56  ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 260.238 283.141 194.579 1.00 92.67  ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 261.339 282.991 191.473 1.00 87.99  ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 258.960 284.285 193.121 1.00 84.65  ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 258.507 285.225 194.142 1.00 84.69  ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 257.673 284.522 195.206 1.00 84.49  ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 257.854 284.754 196.407 1.00 86.06  ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 257.714 286.361 193.494 1.00 85.02  ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 258.574 287.401 192.792 1.00 87.88  ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 259.053 286.945 191.427 1.00 90.55  ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 258.622 285.865 190.971 1.00 90.89  ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 259.864 287.667 190.809 1.00 85.85  ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 256.750 283.656 194.782 1.00 77.23  ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 255.950 282.908 195.746 1.00 74.79  ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 256.781 281.862 196.476 1.00 76.36  ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 256.459 281.503 197.614 1.00 79.07  ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 254.760 282.251 195.048 1.00 73.72  ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 253.604 283.181 194.820 1.00 78.11  ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 252.959 283.778 195.890 1.00 76.30  ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 253.162 283.458 193.538 1.00 77.64  ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 251.895 284.635 195.685 1.00 77.19  ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 252.098 284.313 193.327 1.00 75.20  ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 251.464 284.902 194.402 1.00 77.59  ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 257.840 281.355 195.840 1.00 85.26  ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 258.716 280.404 196.514 1.00 84.97  ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 259.423 281.054 197.696 1.00 85.91  ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 259.523 280.459 198.775 1.00 87.60  ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 259.734 279.835 195.528 1.00 85.35  ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 260.639 278.781 196.129 1.00 86.64  ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 259.863 277.573 196.605 1.00 89.43  ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 259.659 277.387 197.804 1.00 89.67  ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 259.423 276.744 195.666 1.00 88.43  ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 259.921 282.279 197.510 1.00 86.36  ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 260.559 282.990 198.611 1.00 86.27  ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 259.535 283.493 199.619 1.00 87.82  ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 259.871 283.705 200.789 1.00 88.36  ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 261.391 284.153 198.073 1.00 85.78  ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 262.261 284.800 199.104 1.00 87.57  ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 263.247 284.115 199.781 1.00 88.07  ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 262.290 286.068 199.579 1.00 87.92  ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 263.847 284.934 200.626 1.00 89.85  ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 263.285 286.124 200.523 1.00 87.30  ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 258.290 283.698 199.186 1.00 74.59  ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 257.254 284.154 200.107 1.00 71.04  ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 256.894 283.072 201.118 1.00 72.12  ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 256.587 283.375 202.276 1.00 72.69  ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 256.016 284.594 199.325 1.00 68.90  ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 254.889 285.071 200.194 1.00 73.38  ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 255.037 286.197 200.986 1.00 71.87  ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 253.680 284.397 200.217 1.00 73.35  ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 254.003 286.639 201.788 1.00 67.17  ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 252.642 284.835 201.016 1.00 72.00  ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 252.803 285.958 201.801 1.00 70.14  ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 256.929 281.805 200.702 1.00 74.04  ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 256.493 280.712 201.562 1.00 74.21  ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 257.642 280.055 202.318 1.00 75.27  ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 257.502 279.753 203.508 1.00 76.68  ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 255.744 279.664 200.735 1.00 73.76  ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 254.370 280.094 200.216 1.00 72.12  ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 253.605 278.905 199.661 1.00 74.12  ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 253.571 280.785 201.311 1.00 71.19  ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 258.777 279.824 201.661 1.00 89.77  ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 259.936 279.197 202.293 1.00 91.90  ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 261.175 280.064 202.118 1.00 92.30  ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 262.247 279.597 201.730 1.00 94.34  ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 260.185 277.790 201.753 1.00 91.75  ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 259.112 276.786 202.140 1.00 91.88  ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 259.428 275.376 201.654 1.00 88.76  ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 259.355 275.234 200.205 1.00 90.71  ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 260.398 274.992 199.424 1.00 92.67  ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 261.619 274.870 199.919 1.00 94.22  ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 260.212 274.865 198.113 1.00 91.45  ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 261.035 281.358 202.400 1.00 97.56  ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 262.169 282.259 202.391 1.00 96.92  ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 262.970 282.301 203.669 1.00 98.72  ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 264.084 282.834 203.674 1.00 98.88  ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 262.434 281.752 204.759 1.00 105.57 ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 263.135 281.744 206.036 1.00 104.61 ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 264.060 280.546 206.208 1.00 105.49 ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 264.809 280.499 207.190 1.00 104.17 ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 262.124 281.801 207.189 1.00 105.14 ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 261.212 280.582 207.244 1.00 107.62 ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 261.387 279.614 206.504 1.00 110.05 ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 260.227 280.629 208.133 1.00 104.70 ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 264.029 279.583 205.286 1.00 106.12 ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 264.905 278.422 205.368 1.00 105.70 ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 266.270 278.663 204.738 1.00 104.90 ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 267.110 277.757 204.757 1.00 103.58 ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 264.244 277.211 204.704 1.00 104.77 ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 264.039 277.359 203.206 1.00 105.48 ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 263.324 276.171 202.595 1.00 106.29 ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 262.967 275.239 203.346 1.00 104.29 ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 263.120 276.167 201.363 1.00 106.01 ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 266.507 279.850 204.180 1.00 106.45 ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 267.793 280.150 203.564 1.00 107.22 ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 268.867 280.209 204.641 1.00 109.22 ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 268.704 280.879 205.669 1.00 107.29 ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 267.717 281.466 202.776 1.00 107.32 ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 266.711 281.343 201.630 1.00 105.77 ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 269.089 281.853 202.244 1.00 106.20 ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 266.533 282.616 200.833 1.00 104.96 ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 269.971 279.506 204.409 1.00 116.23 ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 271.059 279.448 205.379 1.00 115.11 ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 271.873 280.731 205.292 1.00 113.60 ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 272.335 281.118 204.212 1.00 111.31 ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 271.940 278.213 205.134 1.00 113.85 ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 272.981 278.078 206.235 1.00 112.55 ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 271.082 276.960 205.044 1.00 112.43 ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 272.051 281.394 206.433 1.00 116.10 ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 272.807 282.634 206.513 1.00 115.73 ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 273.866 282.518 207.598 1.00 118.31 ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 273.600 281.995 208.685 1.00 116.60 ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 271.891 283.828 206.805 1.00 114.05 ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 271.158 284.438 205.610 1.00 116.62 ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 270.557 285.782 205.987 1.00 115.62 ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 272.091 284.577 204.417 1.00 115.20 ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 275.064 283.006 207.299 1.00 122.61 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 276.158 283.010 208.256 1.00 121.85 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 276.137 284.290 209.086 1.00 122.53 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 275.518 285.291 208.716 1.00 122.12 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 277.502 282.868 207.540 1.00 119.86 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 277.542 281.684 206.762 1.00 119.90 ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 276.823 284.240 210.231 1.00 120.65 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 276.881 285.404 211.109 1.00 120.04 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 277.578 286.576 210.429 1.00 120.47 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 277.111 287.718 210.511 1.00 118.85 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 277.586 285.042 212.415 1.00 117.65 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 278.699 286.314 209.752 1.00 119.22 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 279.407 287.370 209.051 1.00 119.21 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 278.809 287.748 207.714 1.00 120.76 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 279.117 288.825 207.194 1.00 119.73 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 277.963 286.887 207.145 1.00 122.27 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 277.358 287.189 205.852 1.00 122.13 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 276.327 288.306 205.956 1.00 121.73 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 276.164 289.085 205.010 1.00 119.54 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 276.718 285.931 205.264 1.00 120.00 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 277.697 284.948 204.976 1.00 118.58 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 275.627 288.401 207.084 1.00 122.97 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 274.591 289.411 207.255 1.00 122.66 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 275.205 290.690 207.808 1.00 122.69 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 275.717 290.680 208.936 1.00 121.44 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 273.504 288.915 208.193 1.00 122.28 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 272.868 287.764 207.624 1.00 123.83 ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 272.463 290.001 208.424 1.00 119.97 ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 275.180 291.794 207.070 1.00 124.30 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 275.713 293.054 207.593 1.00 123.10 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 274.728 293.716 208.549 1.00 122.24 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 273.572 293.311 208.682 1.00 122.38 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 275.917 293.900 206.333 1.00 121.80 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 274.885 293.393 205.385 1.00 121.55 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 274.708 291.924 205.680 1.00 122.32 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 275.214 294.754 209.222 1.00 118.97 ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 274.420 295.532 210.169 1.00 119.76 ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 274.049 296.850 209.496 1.00 120.64 ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 274.844 297.794 209.478 1.00 119.18 ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 275.187 295.762 211.468 1.00 119.24 ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 274.454 296.633 212.476 1.00 119.56 ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 275.383 297.096 213.585 1.00 120.19 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 276.575 297.750 213.059 1.00 121.91 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 277.517 298.307 213.809 1.00 121.04 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 277.438 298.309 215.130 1.00 119.71 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 278.564 298.877 213.219 1.00 120.46 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 272.843 296.908 208.942 1.00 114.48 ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 272.366 298.116 208.279 1.00 112.96 ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 271.760 299.042 209.324 1.00 112.45 ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 270.913 298.625 210.124 1.00 111.61 ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 271.348 297.777 207.177 1.00 112.71 ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 271.988 296.926 206.075 1.00 113.86 ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 270.773 299.049 206.577 1.00 111.87 ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 271.922 295.428 206.314 1.00 112.45 ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 272.200 300.298 209.327 1.00 115.72 ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 271.710 301.261 210.304 1.00 115.19 ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 270.216 301.499 210.121 1.00 116.04 ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 269.725 301.652 209.000 1.00 114.90 ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 272.476 302.578 210.176 1.00 114.11 ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 272.197 303.571 211.293 1.00 114.07 ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 272.960 304.869 211.120 1.00 115.53 ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 273.688 305.050 210.145 1.00 116.33 ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 272.797 305.782 212.071 1.00 114.33 ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 269.493 301.531 211.239 1.00 109.64 ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 268.061 301.732 211.225 1.00 108.44 ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 267.231 300.481 211.034 1.00 108.15 ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 265.998 300.581 210.976 1.00 106.90 ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 267.857 299.311 210.935 1.00 107.30 ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 267.151 298.052 210.749 1.00 104.86 ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 267.497 297.090 211.877 1.00 104.71 ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 268.657 296.990 212.290 1.00 105.72 ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 267.486 297.411 209.394 1.00 102.54 ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 266.812 297.977 208.138 1.00 104.06 ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 267.353 299.348 207.758 1.00 105.38 ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 266.958 297.005 206.976 1.00 105.10 ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 266.480 296.388 212.369 1.00 103.80 ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 266.649 295.438 213.456 1.00 104.23 ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 267.360 294.183 212.934 1.00 104.18 ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 267.433 293.936 211.726 1.00 106.17 ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 265.280 295.116 214.070 1.00 104.22 ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 264.679 296.332 214.531 1.00 103.55 ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 265.402 294.191 215.272 1.00 102.79 ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 267.910 293.394 213.864 1.00 102.72 ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 268.680 292.208 213.492 1.00 104.43 ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 267.835 291.259 212.649 1.00 106.31 ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 268.283 290.761 211.609 1.00 103.90 ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 269.224 291.507 214.750 1.00 104.83 ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 269.967 290.235 214.371 1.00 102.96 ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 270.127 292.446 215.534 1.00 103.47 ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 266.600 290.991 213.084 1.00 110.94 ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 265.726 290.130 212.293 1.00 108.12 ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 265.316 290.808 210.991 1.00 104.97 ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 265.151 290.140 209.963 1.00 105.67 ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 264.495 289.720 213.104 1.00 105.92 ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 263.667 290.872 213.646 1.00 107.71 ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 263.927 291.131 215.116 1.00 109.63 ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 264.909 290.579 215.654 1.00 109.68 ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 263.146 291.884 215.735 1.00 108.40 ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 265.141 292.132 211.015 1.00 97.27  ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 264.857 292.858 209.782 1.00 98.52  ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 266.033 292.783 208.817 1.00 100.38 ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 265.845 292.579 207.612 1.00 100.34 ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 264.512 294.314 210.095 1.00 97.84  ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 263.075 294.534 210.535 1.00 97.63  ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 262.685 295.999 210.538 1.00 99.97  ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 263.520 296.875 210.312 1.00 102.02 ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 261.412 296.272 210.794 1.00 99.54  ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 267.256 292.945 209.330 1.00 106.19 ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 268.436 292.870 208.475 1.00 105.69 ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 268.609 291.473 207.893 1.00 106.00 ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 269.003 291.320 206.731 1.00 104.88 ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 269.681 293.285 209.259 1.00 106.16 ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 268.327 290.440 208.691 1.00 102.49 ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 268.417 289.071 208.192 1.00 101.64 ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 267.418 288.831 207.067 1.00 102.69 ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 267.727 288.138 206.090 1.00 102.69 ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 268.189 288.082 209.335 1.00 102.01 ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 268.554 286.647 209.000 1.00 103.64 ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 268.959 285.849 210.223 1.00 104.40 ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 269.722 286.382 211.057 1.00 102.27 ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 268.514 284.689 210.353 1.00 104.00 ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 266.212 289.389 207.191 1.00 98.96  ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 265.215 289.247 206.135 1.00 96.69  ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 265.665 289.933 204.852 1.00 98.13  ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 265.423 289.426 203.750 1.00 100.33 ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 263.872 289.807 206.603 1.00 95.46  ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 266.314 291.094 204.973 1.00 100.39 ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 266.790 291.813 203.793 1.00 102.99 ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 267.827 290.986 203.045 1.00 103.21 ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 267.802 290.900 201.811 1.00 103.74 ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 267.348 293.190 204.195 1.00 101.70 ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 267.941 293.897 202.988 1.00 100.74 ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 266.258 294.037 204.820 1.00 100.49 ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 268.758 290.369 203.776 1.00 102.57 ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 269.764 289.524 203.139 1.00 101.48 ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 269.102 288.330 202.462 1.00 104.14 ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 269.458 287.958 201.337 1.00 105.21 ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 270.820 289.081 204.167 1.00 102.86 ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 271.850 288.173 203.514 1.00 102.97 ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 271.491 290.294 204.792 1.00 103.57 ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 268.130 287.710 203.137 1.00 101.51 ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 267.389 286.612 202.524 1.00 99.19  ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 266.605 287.088 201.308 1.00 100.24 ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 266.550 286.395 200.285 1.00 102.49 ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 266.452 285.973 203.549 1.00 100.27 ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 267.165 285.209 204.652 1.00 100.13 ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 266.174 284.625 205.644 1.00 101.14 ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 266.778 284.401 206.952 1.00 102.03 ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 267.090 283.208 207.439 1.00 103.66 ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 266.870 282.101 206.748 1.00 105.33 ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 267.636 283.123 208.648 1.00 100.42 ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 265.984 288.265 201.401 1.00 99.52  ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 265.258 288.814 200.262 1.00 100.00 ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 266.194 289.254 199.144 1.00 99.40  ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 265.762 289.342 197.989 1.00 99.75  ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 264.385 289.987 200.716 1.00 98.83  ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 263.398 290.578 199.707 1.00 99.38  ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 262.382 289.535 199.279 1.00 98.81  ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 262.699 291.792 200.293 1.00 97.43  ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 267.464 289.516 199.455 1.00 101.63 ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 268.421 289.946 198.443 1.00 103.10 ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 268.767 288.848 197.446 1.00 103.12 ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 269.355 289.151 196.403 1.00 101.45 ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 269.699 290.451 199.113 1.00 103.06 ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 269.441 291.605 199.893 1.00 106.84 ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 268.427 287.590 197.738 1.00 102.92 ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 268.746 286.507 196.814 1.00 103.95 ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 267.987 286.637 195.499 1.00 103.97 ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 268.509 286.249 194.449 1.00 103.25 ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 268.457 285.153 197.461 1.00 104.22 ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 269.089 284.975 199.143 1.00 107.53 ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 266.767 287.159 195.535 1.00 104.58 ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 265.996 287.335 194.310 1.00 104.33 ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 266.662 288.376 193.414 1.00 101.93 ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 267.105 289.418 193.911 1.00 101.58 ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 264.565 287.756 194.635 1.00 102.89 ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 263.723 286.775 195.452 1.00 102.03 ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 262.244 287.115 195.352 1.00 99.94  ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 263.975 285.351 194.993 1.00 100.56 ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 266.780 288.119 192.107 1.00 104.41 ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 267.351 289.123 191.204 1.00 105.79 ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 266.741 290.509 191.334 1.00 105.42 ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 267.467 291.510 191.291 1.00 104.55 ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 267.022 288.510 189.840 1.00 104.57 ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 267.125 286.968 190.101 1.00 104.28 ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 267.248 286.809 191.629 1.00 103.02 ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 265.418 290.593 191.492 1.00 102.51 ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 264.751 291.887 191.575 1.00 101.75 ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 265.133 292.661 192.828 1.00 101.78 ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 265.036 293.893 192.833 1.00 100.08 ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 263.234 291.703 191.523 1.00 100.83 ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 265.554 291.973 193.888 1.00 101.78 ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 265.963 292.616 195.129 1.00 102.94 ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 267.461 292.479 195.380 1.00 103.39 ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 267.899 292.527 196.534 1.00 101.58 ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 265.171 292.047 196.307 1.00 101.44 ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 263.696 292.316 196.230 1.00 102.98 ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 263.185 293.562 196.553 1.00 102.60 ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 262.819 291.320 195.834 1.00 101.03 ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 261.826 293.810 196.481 1.00 100.22 ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 261.461 291.562 195.761 1.00 99.73  ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 260.964 292.808 196.085 1.00 98.73  ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 268.254 292.305 194.319 1.00 109.05 ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 269.695 292.143 194.483 1.00 108.94 ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 270.330 293.389 195.089 1.00 108.73 ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 271.191 293.291 195.971 1.00 106.46 ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 270.337 291.808 193.136 1.00 109.69 ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 271.835 292.059 193.072 1.00 109.02 ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 272.369 291.892 191.657 1.00 108.25 ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 271.558 292.701 190.657 1.00 107.43 ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 271.606 294.160 190.951 1.00 107.89 ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 269.915 294.572 194.633 1.00 110.69 ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 270.422 295.838 195.147 1.00 111.01 ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 269.479 296.463 196.170 1.00 110.82 ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 269.362 297.692 196.239 1.00 109.97 ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 270.684 296.809 193.996 1.00 110.20 ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 269.533 296.871 193.009 1.00 112.30 ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 268.384 297.101 193.440 1.00 113.96 ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 269.779 296.688 191.798 1.00 112.69 ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 268.796 295.635 196.963 1.00 109.44 ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 267.854 296.154 197.949 1.00 109.27 ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 268.565 296.940 199.044 1.00 110.07 ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 268.061 297.973 199.499 1.00 111.05 ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 267.044 295.008 198.553 1.00 108.61 ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 265.971 295.401 199.570 1.00 109.43 ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 264.830 296.140 198.888 1.00 106.95 ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 265.458 294.174 200.302 1.00 108.92 ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 269.735 296.466 199.480 1.00 109.11 ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 270.454 297.132 200.564 1.00 109.73 ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 270.853 298.544 200.153 1.00 110.49 ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 270.712 299.497 200.931 1.00 109.11 ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 271.675 296.294 200.987 1.00 109.33 ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 271.242 295.148 201.903 1.00 109.12 ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 272.715 297.163 201.680 1.00 109.71 ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 272.371 294.223 202.301 1.00 109.03 ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 271.352 298.703 198.925 1.00 109.94 ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 271.735 300.029 198.448 1.00 110.03 ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 270.531 300.959 198.370 1.00 110.86 ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 270.625 302.140 198.724 1.00 110.31 ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 272.419 299.919 197.086 1.00 107.80 ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 269.390 300.446 197.902 1.00 107.63 ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 268.195 301.277 197.790 1.00 106.95 ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 267.681 301.703 199.161 1.00 107.56 ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 267.244 302.846 199.340 1.00 104.49 ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 267.108 300.531 197.017 1.00 105.48 ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 267.323 300.506 195.513 1.00 104.49 ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 266.111 299.939 194.792 1.00 105.01 ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 266.206 300.157 193.291 1.00 105.63 ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 267.296 299.347 192.680 1.00 105.64 ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 267.718 300.794 200.139 1.00 109.35 ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 267.241 301.124 201.480 1.00 110.35 ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 268.115 302.201 202.110 1.00 112.46 ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 267.612 303.164 202.702 1.00 111.83 ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 267.182 299.857 202.353 1.00 109.84 ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 266.967 300.223 203.814 1.00 108.03 ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 266.078 298.931 201.869 1.00 111.28 ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 269.437 302.058 201.991 1.00 113.68 ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 270.345 303.038 202.579 1.00 110.59 ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 270.232 304.396 201.898 1.00 110.99 ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 270.314 305.432 202.569 1.00 110.20 ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 271.784 302.527 202.508 1.00 110.01 ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 272.113 301.456 203.535 1.00 111.43 ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 273.411 300.735 203.231 1.00 112.15 ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 273.986 300.896 202.154 1.00 110.73 ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 273.880 299.935 204.181 1.00 110.76 ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 270.045 304.417 200.579 1.00 112.85 ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 269.970 305.668 199.836 1.00 112.48 ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 268.652 306.405 200.029 1.00 112.87 ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 268.539 307.557 199.597 1.00 111.81 ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 270.194 305.407 198.344 1.00 111.27 ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 267.660 305.781 200.660 1.00 115.80 ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 266.353 306.394 200.874 1.00 116.03 ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 266.320 307.000 202.273 1.00 114.88 ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 266.316 306.273 203.272 1.00 112.76 ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 265.236 305.368 200.692 1.00 115.01 ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 263.875 306.013 200.523 1.00 114.77 ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 263.811 307.257 200.437 1.00 114.38 ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 262.868 305.275 200.475 1.00 114.47 ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 266.295 308.332 202.341 1.00 114.86 ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 266.246 309.023 203.623 1.00 115.19 ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 264.872 308.958 204.275 1.00 114.52 ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 264.769 309.144 205.492 1.00 110.59 ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 266.664 310.486 203.450 1.00 113.39 ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 265.657 311.342 202.693 1.00 115.01 ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 265.817 311.251 201.186 1.00 115.40 ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 266.503 310.324 200.709 1.00 115.69 ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 265.252 312.110 200.477 1.00 114.61 ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 263.822 308.700 203.500 1.00 108.79 ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 262.466 308.607 204.023 1.00 107.62 ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 262.081 307.189 204.419 1.00 104.53 ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 260.924 306.957 204.786 1.00 102.04 ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 261.466 309.144 202.993 1.00 105.44 ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 261.725 310.578 202.552 1.00 105.32 ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 261.383 311.595 203.625 1.00 105.97 ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 262.094 311.730 204.622 1.00 103.87 ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 260.288 312.319 203.425 1.00 105.81 ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 263.015 306.238 204.348 1.00 100.33 ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 262.702 304.862 204.718 1.00 99.91  ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 262.365 304.739 206.198 1.00 98.89  ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 261.535 303.903 206.574 1.00 99.08  ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 263.868 303.942 204.362 1.00 97.28  ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 263.541 302.484 204.478 1.00 96.26  ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 262.772 301.856 203.513 1.00 97.49  ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 263.994 301.741 205.555 1.00 95.45  ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 262.465 300.515 203.617 1.00 98.58  ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 263.691 300.399 205.664 1.00 96.25  ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 262.925 299.786 204.694 1.00 97.44  ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 262.999 305.548 207.049 1.00 90.60  ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 262.667 305.520 208.464 1.00 89.47  ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 261.238 305.948 208.734 1.00 90.27  ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 260.584 305.425 209.640 1.00 89.27  ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 260.736 306.909 207.956 1.00 89.71  ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 259.348 307.337 208.096 1.00 90.22  ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 258.399 306.203 207.727 1.00 90.94  ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 257.391 305.971 208.406 1.00 87.41  ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 259.093 308.595 207.245 1.00 89.26  ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 259.775 309.811 207.874 1.00 90.29  ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 257.601 308.846 207.083 1.00 86.41  ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 259.242 310.168 209.245 1.00 88.33  ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 258.702 305.480 206.647 1.00 86.59  ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 257.851 304.368 206.238 1.00 83.67  ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 257.954 303.191 207.200 1.00 82.05  ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 256.984 302.444 207.366 1.00 83.61  ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 258.212 303.926 204.820 1.00 80.96  ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 257.458 302.717 204.358 1.00 83.52  ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 256.191 302.684 203.856 1.00 81.21  ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 257.925 301.362 204.357 1.00 84.07  ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 255.839 301.394 203.542 1.00 80.65  ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 256.886 300.563 203.840 1.00 80.87  ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 259.120 300.748 204.743 1.00 84.43  ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 257.006 299.183 203.698 1.00 80.25  ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 259.237 299.377 204.602 1.00 82.05  ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 258.186 298.610 204.084 1.00 79.40  ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 259.115 303.007 207.835 1.00 83.80  ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 259.309 301.853 208.708 1.00 84.53  ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 258.386 301.901 209.920 1.00 87.17  ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 257.816 300.876 210.312 1.00 90.02  ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 260.770 301.770 209.149 1.00 88.47  ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 261.319 300.361 209.386 1.00 87.31  ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 260.998 299.454 208.208 1.00 86.77  ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 262.817 300.404 209.641 1.00 85.59  ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 258.223 303.076 210.529 1.00 87.66  ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 257.392 303.228 211.716 1.00 86.71  ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 256.010 303.789 211.397 1.00 90.25  ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 255.286 304.194 212.313 1.00 89.59  ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 258.100 304.104 212.753 1.00 87.27  ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 258.535 305.447 212.193 1.00 90.90  ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 258.145 305.783 211.056 1.00 91.49  ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 259.270 306.171 212.896 1.00 90.74  ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 255.634 303.825 210.122 1.00 84.03  ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 254.320 304.320 209.740 1.00 82.15  ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 253.224 303.382 210.238 1.00 83.75  ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 253.436 302.179 210.416 1.00 82.17  ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 254.228 304.477 208.223 1.00 80.11  ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 254.390 303.231 207.572 1.00 81.86  ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 252.041 303.955 210.473 1.00 84.28  ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 250.930 303.172 211.008 1.00 81.49  ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 250.476 302.099 210.025 1.00 79.19  ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 250.192 300.964 210.424 1.00 77.70  ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 249.766 304.096 211.369 1.00 81.62  ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 249.360 304.865 210.250 1.00 81.33  ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 250.401 302.437 208.740 1.00 75.77  ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 249.958 301.512 207.697 1.00 75.42  ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 250.975 301.510 206.563 1.00 77.40  ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 250.742 302.092 205.497 1.00 77.48  ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 248.567 301.887 207.185 1.00 74.94  ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 248.597 303.119 206.486 1.00 75.79  ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 252.127 300.863 206.765 1.00 71.56  ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 253.146 300.833 205.704 1.00 72.04  ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 252.721 300.062 204.467 1.00 74.23  ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 253.301 300.282 203.396 1.00 78.21  ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 254.345 300.166 206.389 1.00 73.27  ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 253.734 299.315 207.446 1.00 69.12  ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 252.527 300.066 207.937 1.00 71.52  ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 251.733 299.171 204.574 1.00 73.18  ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 251.337 298.352 203.434 1.00 70.45  ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 250.669 299.164 202.332 1.00 73.45  ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 250.609 298.700 201.189 1.00 76.02  ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 250.403 297.230 203.892 1.00 65.57  ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 248.992 297.688 204.222 1.00 67.26  ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 248.810 298.004 205.692 1.00 74.48  ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 249.646 297.558 206.505 1.00 79.41  ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 247.831 298.699 206.036 1.00 73.02  ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 250.168 300.359 202.644 1.00 74.10  ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 249.504 301.187 201.647 1.00 74.74  ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 250.465 302.071 200.867 1.00 77.84  ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 250.113 302.531 199.775 1.00 76.99  ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 248.441 302.064 202.316 1.00 74.44  ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 247.103 301.372 202.518 1.00 76.40  ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 245.930 302.326 202.406 1.00 79.81  ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 245.422 302.577 201.313 1.00 80.33  ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 245.495 302.864 203.539 1.00 76.97  ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 251.663 302.319 201.393 1.00 85.33  ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 252.656 303.188 200.766 1.00 82.38  ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 254.008 302.489 200.698 1.00 81.99  ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 255.044 303.049 201.060 1.00 84.44  ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 252.792 304.516 201.509 1.00 84.42  ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 253.464 304.301 202.757 1.00 84.70  ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 251.427 305.141 201.771 1.00 81.81  ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 254.010 301.246 200.234 1.00 82.64  ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 255.267 300.494 200.125 1.00 83.60  ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 256.143 301.137 199.054 1.00 85.37  ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 255.691 301.308 197.908 1.00 82.60  ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 254.985 299.028 199.798 1.00 78.81  ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 256.289 298.261 199.635 1.00 79.24  ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 254.123 298.398 200.879 1.00 78.12  ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 257.382 301.507 199.368 1.00 89.22  ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 258.229 302.172 198.374 1.00 89.50  ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 258.668 301.223 197.269 1.00 94.46  ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 258.714 300.001 197.431 1.00 95.76  ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 259.427 302.657 199.197 1.00 88.31  ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 259.481 301.727 200.359 1.00 87.34  ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 258.056 301.364 200.669 1.00 87.40  ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 258.996 301.819 196.123 1.00 98.54  ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 259.471 301.084 194.951 1.00 95.31  ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 260.953 300.772 195.143 1.00 98.13  ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 261.845 301.512 194.721 1.00 100.75 ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 259.217 301.890 193.683 1.00 97.85  ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 259.637 301.203 192.404 1.00 101.40 ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 258.877 300.175 191.862 1.00 98.93  ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 260.787 301.594 191.732 1.00 101.66 ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 259.258 299.550 190.689 1.00 99.95  ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 261.174 300.977 190.561 1.00 101.02 ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 260.407 299.956 190.044 1.00 102.88 ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 260.795 299.342 188.876 1.00 101.63 ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 261.214 299.643 195.802 1.00 94.85  ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 262.568 299.238 196.158 1.00 95.77  ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 263.083 298.073 195.322 1.00 98.26  ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 264.102 297.472 195.679 1.00 100.82 ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 262.637 298.882 197.645 1.00 95.29  ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 262.216 299.975 198.630 1.00 95.12  ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 262.600 299.591 200.050 1.00 95.84  ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 262.832 301.313 198.249 1.00 94.98  ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 262.411 297.736 194.224 1.00 95.01  ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 262.844 296.658 193.348 1.00 95.05  ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 263.078 297.194 191.943 1.00 98.76  ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 262.466 298.182 191.527 1.00 99.85  ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 261.820 295.515 193.310 1.00 95.14  ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 260.467 295.925 192.821 1.00 95.49  ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 259.998 295.844 191.543 1.00 94.01  ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 259.399 296.471 193.606 1.00 97.41  ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 258.708 296.310 191.481 1.00 94.64  ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 258.317 296.700 192.734 1.00 96.78  ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 259.255 296.789 194.959 1.00 96.43  ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 257.107 297.234 193.172 1.00 95.39  ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 258.053 297.319 195.392 1.00 95.01  ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 256.995 297.536 194.501 1.00 97.23  ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 263.972 296.531 191.215 1.00 111.76 ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 264.348 296.927 189.865 1.00 110.64 ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 263.819 295.906 188.868 1.00 109.74 ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 264.030 294.700 189.036 1.00 108.72 ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 265.867 297.056 189.737 1.00 110.68 ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 266.518 295.875 190.173 1.00 110.34 ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 263.135 296.392 187.835 1.00 113.44 ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 262.569 295.538 186.801 1.00 115.77 ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 262.884 296.126 185.435 1.00 114.94 ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 262.928 297.348 185.271 1.00 114.05 ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 261.053 295.383 186.975 1.00 115.72 ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 260.321 296.698 187.174 1.00 115.55 ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 258.878 296.508 187.597 1.00 115.83 ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 258.640 295.812 188.607 1.00 115.41 ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 257.983 297.060 186.924 1.00 114.28 ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 263.104 295.246 184.455 1.00 119.69 ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 263.421 295.707 183.107 1.00 120.72 ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 262.191 296.252 182.393 1.00 120.92 ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 262.318 297.109 181.511 1.00 120.78 ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 264.045 294.571 182.296 1.00 121.41 ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 265.438 294.167 182.754 1.00 121.93 ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 265.414 293.174 183.900 1.00 122.66 ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 264.311 292.727 184.278 1.00 121.93 ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 266.498 292.841 184.423 1.00 121.03 ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 261.005 295.775 182.754 1.00 119.96 ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 259.757 296.199 182.145 1.00 120.29 ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 258.761 296.584 183.228 1.00 119.50 ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 258.826 296.064 184.347 1.00 117.55 ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 259.167 295.085 181.264 1.00 119.44 ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 257.972 295.548 180.622 1.00 118.24 ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 258.849 293.848 182.094 1.00 118.08 ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 257.849 297.512 182.936 1.00 116.39 ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 256.807 297.858 183.917 1.00 115.69 ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 255.966 296.642 184.276 1.00 116.90 ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 255.306 296.045 183.423 1.00 116.04 ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 255.984 298.928 183.192 1.00 113.82 ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 256.941 299.545 182.233 1.00 114.94 ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 257.856 298.438 181.789 1.00 115.84 ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 255.997 296.279 185.555 1.00 108.83 ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 255.288 295.095 186.015 1.00 105.87 ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 253.786 295.347 186.080 1.00 103.50 ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 253.325 296.483 186.217 1.00 102.66 ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 255.802 294.663 187.388 1.00 102.64 ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 253.023 294.262 185.977 1.00 90.02  ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 251.580 294.334 186.095 1.00 89.11  ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 251.186 294.659 187.535 1.00 89.49  ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 251.975 294.460 188.462 1.00 88.98  ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 250.951 293.013 185.656 1.00 89.15  ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 251.160 292.021 186.669 1.00 88.86  ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 251.573 292.536 184.352 1.00 88.77  ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 249.973 295.181 187.747 1.00 85.05  ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 249.545 295.485 189.124 1.00 83.11  ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 249.592 294.284 190.051 1.00 80.53  ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 249.877 294.448 191.244 1.00 80.78  ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 248.109 296.004 188.944 1.00 81.24  ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 247.725 295.667 187.531 1.00 81.55  ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 248.996 295.656 186.754 1.00 81.79  ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 249.316 293.081 189.544 1.00 75.40  ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 249.487 291.881 190.356 1.00 73.41  ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 250.957 291.682 190.704 1.00 71.64  ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 251.300 291.351 191.845 1.00 77.02  ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 248.903 290.651 189.637 1.00 71.93  ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 247.383 290.777 189.487 1.00 70.45  ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 249.255 289.377 190.387 1.00 72.84  ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 246.935 291.418 188.188 1.00 74.10  ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 251.847 291.884 189.730 1.00 71.81  ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 253.270 291.759 190.002 1.00 73.27  ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 253.763 292.776 191.013 1.00 75.32  ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 254.638 292.479 191.830 1.00 75.41  ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 253.217 293.993 190.964 1.00 81.10  ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 253.548 294.989 191.978 1.00 77.72  ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 253.086 294.539 193.357 1.00 78.82  ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 253.807 294.710 194.347 1.00 80.73  ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 252.923 296.337 191.619 1.00 75.35  ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 253.559 297.023 190.423 1.00 79.63  ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 252.946 298.379 190.141 1.00 81.63  ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 251.983 298.786 190.791 1.00 80.53  ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 253.503 299.090 189.167 1.00 78.31  ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 251.889 293.951 193.439 1.00 72.23  ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 251.361 293.512 194.727 1.00 61.49  ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 252.239 292.434 195.350 1.00 64.76  ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 252.469 292.436 196.565 1.00 72.62  ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 249.928 293.008 194.562 1.00 59.47  ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 252.734 291.500 194.534 1.00 68.70  ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 253.600 290.443 195.051 1.00 71.63  ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 254.898 291.032 195.588 1.00 70.55  ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 255.387 290.629 196.651 1.00 72.56  ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 253.864 289.388 193.962 1.00 71.87  ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 252.544 288.814 193.447 1.00 69.36  ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 254.750 288.278 194.501 1.00 70.98  ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 252.713 287.746 192.393 1.00 71.38  ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 255.482 291.987 194.860 1.00 75.66  ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 256.711 292.624 195.323 1.00 73.95  ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 256.477 293.408 196.608 1.00 75.88  ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 257.309 293.377 197.523 1.00 78.90  ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 257.274 293.529 194.229 1.00 77.12  ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 257.857 292.781 193.071 1.00 79.57  ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 257.297 292.803 191.812 1.00 79.89  ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 258.950 291.986 192.982 1.00 77.08  ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 258.021 292.055 190.997 1.00 78.09  ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 259.029 291.549 191.683 1.00 78.51  ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 255.352 294.122 196.695 1.00 72.00  ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 254.996 294.785 197.946 1.00 69.19  ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 254.727 293.767 199.046 1.00 68.87  ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 255.038 294.011 200.218 1.00 72.19  ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 253.779 295.687 197.739 1.00 66.48  ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 253.971 296.761 196.682 1.00 68.01  ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 253.069 297.957 196.936 1.00 71.02  ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 252.430 298.427 195.713 1.00 73.87  ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 252.996 299.248 194.839 1.00 75.68  ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 254.222 299.711 195.020 1.00 72.83  ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 252.314 299.614 193.757 1.00 72.47  ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 254.141 292.622 198.687 1.00 66.34  ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 253.913 291.563 199.664 1.00 66.55  ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 255.229 291.030 200.216 1.00 66.98  ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 255.349 290.773 201.420 1.00 66.42  ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 253.097 290.438 199.026 1.00 63.41  ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 252.574 289.321 199.928 1.00 67.60  ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 251.440 289.821 200.805 1.00 70.39  ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 252.120 288.142 199.083 1.00 66.58  ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 256.228 290.850 199.348 1.00 75.64  ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 257.538 290.403 199.810 1.00 74.12  ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 258.217 291.467 200.664 1.00 74.36  ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 258.845 291.149 201.681 1.00 75.32  ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 258.417 290.036 198.614 1.00 74.22  ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 258.098 288.712 197.919 1.00 73.28  ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 258.952 288.542 196.673 1.00 75.98  ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 258.298 287.546 198.872 1.00 69.08  ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 258.109 292.736 200.262 1.00 71.00  ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 258.737 293.811 201.024 1.00 74.05  ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 258.110 293.954 202.404 1.00 77.53  ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 258.815 294.181 203.394 1.00 76.91  ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 258.640 295.127 200.252 1.00 74.40  ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 259.716 295.364 199.190 1.00 75.59  ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 259.596 296.763 198.610 1.00 75.63  ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 261.101 295.139 199.774 1.00 78.13  ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 256.783 293.834 202.489 1.00 72.99  ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 256.108 293.927 203.781 1.00 65.91  ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 256.549 292.792 204.696 1.00 67.40  ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 256.809 293.001 205.887 1.00 73.20  ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 254.580 293.943 203.585 1.00 67.23  ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 254.126 295.318 203.094 1.00 67.77  ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 253.866 293.582 204.878 1.00 70.51  ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 254.419 296.435 204.069 1.00 68.07  ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 256.654 291.577 204.153 1.00 68.74  ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 257.076 290.437 204.962 1.00 67.85  ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 258.476 290.644 205.527 1.00 71.97  ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 258.742 290.305 206.686 1.00 74.74  ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 257.023 289.157 204.129 1.00 70.90  ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 257.286 287.889 204.922 1.00 70.75  ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 257.425 286.667 204.037 1.00 73.31  ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 257.513 286.780 202.815 1.00 74.76  ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 257.444 285.490 204.650 1.00 73.18  ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 259.385 291.196 204.721 1.00 77.31  ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 260.763 291.368 205.169 1.00 77.14  ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 260.881 292.461 206.225 1.00 75.63  ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 261.599 292.296 207.218 1.00 74.96  ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 261.666 291.677 203.976 1.00 77.96  ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 260.187 293.583 206.034 1.00 78.34  ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 260.357 294.755 206.886 1.00 78.84  ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 259.332 294.837 208.011 1.00 83.16  ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 259.701 295.069 209.166 1.00 88.29  ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 260.300 296.031 206.038 1.00 81.15  ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 261.487 296.210 205.136 1.00 84.20  ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 262.754 296.386 205.665 1.00 83.46  ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 261.336 296.203 203.759 1.00 83.63  ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 263.848 296.550 204.839 1.00 84.66  ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 262.428 296.368 202.928 1.00 81.76  ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 263.685 296.542 203.469 1.00 84.82  ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 258.049 294.653 207.704 1.00 74.96  ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 256.967 294.821 208.675 1.00 69.29  ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 256.108 293.564 208.685 1.00 69.47  ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 255.027 293.530 208.081 1.00 72.89  ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 256.130 296.060 208.355 1.00 66.98  ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 256.876 297.372 208.535 1.00 69.44  ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 257.104 297.679 210.005 1.00 71.62  ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 255.855 297.722 210.754 1.00 71.54  ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 255.082 298.794 210.860 1.00 71.18  ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 255.406 299.939 210.283 1.00 72.54  ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 253.957 298.716 211.565 1.00 69.61  ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 256.563 292.505 209.360 1.00 67.28  ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 255.770 291.265 209.393 1.00 64.86  ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 254.408 291.429 210.044 1.00 66.16  ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 253.495 290.646 209.752 1.00 70.90  ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 256.662 290.299 210.187 1.00 64.63  ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 257.585 291.177 210.967 1.00 67.49  ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 257.822 292.383 210.113 1.00 67.70  ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 254.241 292.422 210.922 1.00 70.23  ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 252.952 292.621 211.577 1.00 66.82  ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 251.879 293.061 210.590 1.00 68.15  ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 250.686 292.851 210.837 1.00 70.42  ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 253.088 293.645 212.704 1.00 66.05  ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 253.862 294.878 212.281 1.00 73.17  ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 255.069 294.752 211.988 1.00 72.33  ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 253.262 295.973 212.242 1.00 71.74  ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 252.276 293.667 209.475 1.00 65.65  ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 251.338 294.128 208.462 1.00 67.36  ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 251.211 293.164 207.290 1.00 67.76  ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 250.652 293.542 206.255 1.00 68.05  ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 251.753 295.510 207.949 1.00 63.91  ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 251.934 296.546 209.046 1.00 65.00  ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 250.661 296.728 209.855 1.00 66.62  ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 249.581 297.301 209.061 1.00 68.13  ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 248.322 297.393 209.467 1.00 68.18  ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 247.946 296.958 210.658 1.00 66.29  ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 247.417 297.936 208.657 1.00 67.08  ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 251.721 291.938 207.423 1.00 64.14  ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 251.634 290.967 206.337 1.00 60.57  ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 250.185 290.612 206.026 1.00 63.59  ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 249.802 290.474 204.859 1.00 72.59  ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 252.433 289.712 206.693 1.00 56.53  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 252.612 288.683 205.576 1.00 58.56  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 253.199 289.337 204.335 1.00 64.32  ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 253.487 287.532 206.044 1.00 59.33  ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 249.363 290.451 207.067 1.00 60.17  ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 247.954 290.129 206.862 1.00 56.52  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 247.234 291.254 206.128 1.00 58.07  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 246.397 291.006 205.253 1.00 60.35  ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 247.280 289.843 208.204 1.00 56.67  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 247.460 288.435 208.772 1.00 58.37  ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 246.516 288.212 209.941 1.00 58.81  ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 247.240 287.386 207.693 1.00 57.05  ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 247.541 292.502 206.485 1.00 56.65  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 246.937 293.639 205.798 1.00 59.92  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 247.359 293.680 204.334 1.00 63.26  ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 246.547 293.970 203.448 1.00 63.82  ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 247.312 294.940 206.507 1.00 61.17  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 248.635 293.395 204.063 1.00 63.81  ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 249.107 293.363 202.683 1.00 61.71  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 248.517 292.179 201.927 1.00 62.92  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 248.277 292.263 200.717 1.00 69.03  ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 250.635 293.316 202.654 1.00 60.31  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 251.237 293.486 201.270 1.00 63.49  ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 251.141 295.182 200.667 1.00 76.14  ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 250.208 294.951 199.156 1.00 62.39  ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 248.282 291.064 202.625 1.00 53.47  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 247.684 289.897 201.984 1.00 44.41  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 246.275 290.197 201.489 1.00 47.60  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 245.878 289.746 200.409 1.00 58.10  ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 247.672 288.715 202.953 1.00 44.12  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 245.501 290.952 202.273 1.00 52.76  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 244.164 291.341 201.836 1.00 52.98  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 244.228 292.240 200.608 1.00 52.66  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 243.365 292.162 199.726 1.00 58.00  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 243.419 292.037 202.975 1.00 55.29  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 242.917 291.100 204.029 1.00 56.05  ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 243.753 290.479 204.933 1.00 57.16  ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 241.665 290.678 204.324 1.00 57.09  ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 243.037 289.715 205.738 1.00 56.95  ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 241.767 289.818 205.391 1.00 60.83  ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 245.240 293.110 200.539 1.00 59.84  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 245.419 293.940 199.353 1.00 61.29  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 245.735 293.089 198.130 1.00 63.20  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 245.258 293.375 197.026 1.00 64.43  ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 246.524 294.968 199.591 1.00 63.58  ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 246.192 296.012 200.643 1.00 65.11  ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 247.552 297.161 200.922 1.00 76.27  ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 247.523 298.095 199.395 1.00 62.87  ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 246.540 292.037 198.307 1.00 59.28  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 246.849 291.141 197.197 1.00 53.63  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 245.594 290.455 196.674 1.00 55.15  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 245.428 290.289 195.460 1.00 60.37  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 247.884 290.104 197.630 1.00 51.15  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 248.174 289.066 196.584 1.00 56.12  ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 248.947 289.372 195.478 1.00 60.41  ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 247.664 287.785 196.705 1.00 60.18  ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 249.210 288.416 194.514 1.00 63.38  ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 247.924 286.825 195.746 1.00 58.53  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 248.698 287.141 194.649 1.00 59.91  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 244.704 290.039 197.577 1.00 54.34  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 243.443 289.434 197.160 1.00 51.50  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 242.616 290.432 196.360 1.00 57.68  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 242.004 290.083 195.342 1.00 62.63  ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 242.674 288.907 198.386 1.00 51.16  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 241.284 288.436 197.988 1.00 53.65  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 243.451 287.785 199.057 1.00 50.52  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 242.585 291.691 196.806 1.00 57.90  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 241.844 292.724 196.093 1.00 58.44  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 242.408 292.993 194.704 1.00 62.41  ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 241.644 293.338 193.795 1.00 64.50  ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 241.832 294.017 196.910 1.00 57.91  ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 241.287 293.801 198.200 1.00 61.04  ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 243.723 292.855 194.518 1.00 62.50  ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 244.301 293.039 193.190 1.00 59.48  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 243.848 291.952 192.224 1.00 61.13  ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 243.639 292.229 191.037 1.00 59.30  ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 245.829 293.066 193.266 1.00 59.51  ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 246.311 291.818 193.782 1.00 68.28  ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 246.306 294.205 194.154 1.00 57.06  ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 243.690 290.721 192.706 1.00 59.08  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 243.322 289.588 191.866 1.00 55.08  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 241.817 289.355 191.807 1.00 59.40  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 241.235 289.339 190.719 1.00 60.54  ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 244.022 288.317 192.363 1.00 50.98  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 245.529 288.394 192.239 1.00 58.03  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 246.173 289.239 192.861 1.00 55.11  ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 246.102 287.505 191.437 1.00 63.79  ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 241.171 289.174 192.958 1.00 52.68  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 239.772 288.774 193.009 1.00 49.59  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 238.812 289.936 193.234 1.00 55.77  ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 237.601 289.711 193.311 1.00 58.44  ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 239.571 287.719 194.101 1.00 52.88  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 240.384 286.435 193.929 1.00 49.48  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 240.809 285.876 195.277 1.00 49.01  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 239.595 285.402 193.142 1.00 53.12  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 239.311 291.161 193.336 1.00 59.55  ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 238.454 292.312 193.515 1.00 56.99  ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 238.401 292.778 194.962 1.00 59.52  ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 238.679 292.031 195.904 1.00 65.59  ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 238.024 294.048 195.134 1.00 58.99  ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 238.002 294.645 196.465 1.00 62.55  ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 236.916 294.042 197.347 1.00 65.85  ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 237.127 293.867 198.553 1.00 65.02  ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 237.814 296.159 196.362 1.00 60.49  ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 238.984 296.900 195.729 1.00 62.78  ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 238.949 296.873 194.213 1.00 70.86  ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 237.977 296.331 193.647 1.00 71.28  ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 239.895 297.396 193.587 1.00 70.77  ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 235.756 293.720 196.776 1.00 58.20  ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 234.630 293.196 197.536 1.00 57.12  ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 234.578 291.672 197.540 1.00 59.83  ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 233.494 291.099 197.701 1.00 58.35  ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 233.318 293.764 196.990 1.00 59.70  ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 233.112 293.371 195.645 1.00 61.16  ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 235.720 291.005 197.363 1.00 50.82  ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 235.730 289.546 197.336 1.00 48.18  ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 235.419 288.966 198.712 1.00 52.81  ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 234.590 288.058 198.841 1.00 59.22  ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 237.083 289.044 196.830 1.00 48.48  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 237.163 287.551 196.693 1.00 55.35  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 236.472 286.898 195.687 1.00 47.43  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 237.930 286.801 197.568 1.00 52.50  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 236.543 285.525 195.556 1.00 48.01  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 238.005 285.427 197.443 1.00 46.39  ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 237.311 284.789 196.434 1.00 49.48  ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 236.075 289.479 199.751 1.00 52.71  ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 235.904 288.991 201.113 1.00 47.52  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 234.958 289.856 201.938 1.00 56.60  ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 234.821 289.627 203.144 1.00 56.10  ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 237.262 288.898 201.810 1.00 43.85  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 238.309 288.125 201.029 1.00 48.15  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 239.913 288.108 201.850 1.00 56.21  ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 239.576 287.011 203.224 1.00 48.11  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 234.304 290.841 201.320 1.00 64.36  ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 233.484 291.778 202.082 1.00 61.90  ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 232.219 291.126 202.625 1.00 67.59  ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 231.622 291.639 203.579 1.00 70.60  ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 233.125 292.984 201.214 1.00 63.87  ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 234.265 293.786 200.960 1.00 62.58  ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 231.790 290.006 202.038 1.00 62.31  ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 230.543 289.376 202.465 1.00 60.95  ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 230.705 288.695 203.820 1.00 59.78  ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 229.722 288.497 204.545 1.00 61.65  ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 230.050 288.397 201.380 1.00 61.84  ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 228.626 287.919 201.683 1.00 62.49  ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 231.008 287.228 201.235 1.00 61.30  ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 227.956 287.220 200.520 1.00 61.51  ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 231.937 288.339 204.194 1.00 58.09  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 232.177 287.693 205.480 1.00 58.06  ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 232.071 288.646 206.664 1.00 63.08  ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 232.040 288.178 207.806 1.00 61.89  ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 233.551 287.019 205.486 1.00 56.38  ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 233.703 285.881 204.489 1.00 63.15  ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 232.636 284.482 204.893 1.00 64.09  ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 231.341 284.647 203.670 1.00 61.40  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 232.019 289.954 206.430 1.00 71.93  ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 231.877 290.920 207.511 1.00 69.97  ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 230.424 291.237 207.837 1.00 71.54  ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 230.166 291.999 208.775 1.00 74.79  ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 232.621 292.215 207.168 1.00 71.00  ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 234.130 292.066 207.106 1.00 74.41  ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 234.826 293.362 206.747 1.00 82.16  ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 234.126 294.345 206.423 1.00 80.63  ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 236.074 293.399 206.790 1.00 84.16  ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 229.475 290.679 207.091 1.00 66.58  ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 228.059 290.883 207.335 1.00 65.83  ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 227.487 289.734 208.159 1.00 72.70  ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 228.015 288.618 208.127 1.00 72.06  ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 227.285 290.998 206.016 1.00 62.88  ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 228.059 291.692 204.910 1.00 66.56  ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 228.077 293.199 205.068 1.00 70.04  ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 227.353 293.758 205.892 1.00 69.95  ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 228.912 293.866 204.280 1.00 67.15  ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 226.419 289.976 208.922 1.00 66.97  ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 225.804 288.886 209.686 1.00 62.71  ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 225.297 287.782 208.770 1.00 69.79  ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 224.839 288.031 207.653 1.00 72.77  ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 224.650 289.575 210.427 1.00 59.91  ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 224.412 290.848 209.678 1.00 60.91  ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 225.753 291.265 209.169 1.00 60.34  ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 225.398 286.548 209.258 1.00 64.11  ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 224.987 285.391 208.473 1.00 63.04  ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 223.494 285.444 208.176 1.00 67.39  ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 222.679 285.709 209.064 1.00 67.59  ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 225.335 284.104 209.220 1.00 61.26  ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 224.920 282.788 208.561 1.00 64.74  ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 225.699 282.566 207.277 1.00 65.27  ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 225.120 281.624 209.518 1.00 63.84  ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 223.139 285.191 206.916 1.00 73.90  ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 221.744 285.176 206.481 1.00 72.83  ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 221.284 283.722 206.423 1.00 74.65  ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 221.313 283.067 205.381 1.00 74.93  ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 221.589 285.880 205.137 1.00 70.65  ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 220.166 286.329 204.874 1.00 77.73  ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 219.314 286.166 205.773 1.00 77.07  ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 219.897 286.846 203.769 1.00 80.48  ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 220.853 283.214 207.580 1.00 69.78  ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 220.435 281.820 207.669 1.00 66.88  ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 219.155 281.558 206.887 1.00 71.51  ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 218.931 280.431 206.432 1.00 77.08  ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 220.252 281.419 209.132 1.00 67.37  ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 221.458 280.772 209.814 1.00 72.95  ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 221.124 280.394 211.248 1.00 72.64  ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 221.931 279.557 209.032 1.00 70.17  ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 218.304 282.574 206.727 1.00 78.55  ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 217.045 282.384 206.013 1.00 77.87  ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 217.286 282.008 204.555 1.00 77.06  ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 216.650 281.090 204.025 1.00 79.65  ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 216.193 283.651 206.104 1.00 76.93  ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 216.084 284.060 207.473 1.00 78.52  ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 214.803 283.400 205.540 1.00 75.59  ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 218.204 282.710 203.890 1.00 67.83  ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 218.448 282.456 202.474 1.00 70.07  ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 219.142 281.116 202.263 1.00 77.09  ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 218.784 280.353 201.358 1.00 77.81  ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 219.277 283.594 201.876 1.00 70.52  ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 219.806 283.302 200.507 1.00 75.73  ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 218.992 283.214 199.398 1.00 78.14  ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 221.066 283.077 200.066 1.00 75.24  ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 219.728 282.949 198.334 1.00 74.99  ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 220.990 282.860 198.712 1.00 75.45  ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 220.145 280.813 203.090 1.00 68.08  ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 220.933 279.600 202.888 1.00 63.63  ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 220.107 278.356 203.190 1.00 64.31  ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 220.109 277.392 202.415 1.00 68.54  ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 222.212 279.650 203.742 1.00 58.69  ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 222.998 280.929 203.446 1.00 62.95  ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 223.069 278.424 203.483 1.00 62.65  ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 224.282 281.050 204.232 1.00 62.91  ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 219.396 278.350 204.319 1.00 62.57  ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 218.625 277.172 204.707 1.00 63.24  ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 217.493 276.919 203.719 1.00 70.11  ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 217.250 275.777 203.309 1.00 70.51  ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 218.101 277.330 206.146 1.00 58.24  ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 217.008 276.313 206.436 1.00 61.37  ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 219.241 277.191 207.143 1.00 59.34  ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 216.786 277.976 203.317 1.00 70.17  ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 215.651 277.801 202.427 1.00 69.99  ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 216.040 277.325 201.040 1.00 71.14  ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 215.323 276.531 200.424 1.00 71.51  ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 217.174 277.800 200.526 1.00 72.70  ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 217.561 277.559 199.142 1.00 76.20  ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 218.789 276.672 198.997 1.00 73.70  ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 218.738 275.660 198.292 1.00 76.78  ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 217.812 278.897 198.430 1.00 77.46  ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 218.943 279.549 199.019 1.00 75.26  ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 216.594 279.800 198.549 1.00 71.22  ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 219.895 277.022 199.646 1.00 61.52  ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 221.172 276.360 199.412 1.00 65.22  ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 221.352 275.081 200.218 1.00 65.46  ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 222.389 274.424 200.079 1.00 70.16  ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 222.327 277.318 199.722 1.00 63.30  ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 222.183 278.694 199.098 1.00 66.54  ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 223.320 279.622 199.475 1.00 69.59  ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 224.230 279.182 200.209 1.00 67.42  ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 223.305 280.792 199.036 1.00 70.49  ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 220.386 274.708 201.052 1.00 56.26  ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 220.496 273.532 201.907 1.00 58.42  ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 219.414 272.540 201.507 1.00 62.36  ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 218.223 272.878 201.503 1.00 65.77  ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 220.380 273.895 203.396 1.00 53.55  ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 220.120 272.648 204.220 1.00 55.66  ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 221.644 274.596 203.867 1.00 53.89  ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 219.828 271.320 201.169 1.00 57.31  ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 218.895 270.245 200.882 1.00 56.85  ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 218.350 269.655 202.181 1.00 57.78  ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 219.022 269.689 203.215 1.00 59.28  ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 219.577 269.153 200.065 1.00 60.15  ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 220.219 269.651 198.781 1.00 60.05  ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 219.173 270.153 197.801 1.00 59.76  ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 219.818 270.648 196.517 1.00 60.55  ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 220.603 271.894 196.740 1.00 62.01  ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 217.127 269.118 202.158 1.00 58.99  ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 216.584 268.494 203.376 1.00 56.86  ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 217.414 267.327 203.879 1.00 61.29  ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 217.494 267.113 205.095 1.00 59.90  ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 215.180 268.047 202.945 1.00 52.90  ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 215.234 267.982 201.453 1.00 58.00  ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 216.169 269.073 201.041 1.00 59.75  ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 218.038 266.565 202.979 1.00 60.00  ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 218.862 265.435 203.386 1.00 55.62  ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 220.181 265.864 204.013 1.00 60.42  ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 220.816 265.056 204.699 1.00 61.73  ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 219.139 264.527 202.185 1.00 61.80  ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 219.329 263.078 202.582 1.00 67.15  ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 218.418 262.444 203.113 1.00 67.72  ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 220.519 262.545 202.329 1.00 64.20  ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 220.604 267.108 203.798 1.00 55.84  ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 221.876 267.587 204.321 1.00 47.92  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 221.673 268.195 205.702 1.00 49.95  ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 220.959 269.200 205.823 1.00 52.44  ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 222.486 268.619 203.387 1.00 45.01  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 222.784 268.010 202.124 1.00 52.07  ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 223.762 269.186 203.982 1.00 46.17  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 222.260 267.628 206.756 1.00 42.87  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 222.153 268.254 208.079 1.00 36.69  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 222.877 269.590 208.116 1.00 38.57  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 223.878 269.796 207.427 1.00 47.22  ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 222.811 267.231 209.013 1.00 38.14  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 223.700 266.424 208.130 1.00 43.88  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 223.023 266.370 206.794 1.00 45.41  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 222.358 270.501 208.931 1.00 38.84  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 222.885 271.858 209.020 1.00 30.16  ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 223.643 271.967 210.339 1.00 33.03  ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 223.040 271.952 211.415 1.00 42.83  ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 221.762 272.897 208.924 1.00 29.46  ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 222.324 274.295 208.938 1.00 28.10  ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 220.938 272.672 207.672 1.00 35.94  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 224.967 272.081 210.260 1.00 33.40  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 225.828 271.979 211.435 1.00 29.04  ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 226.061 273.364 212.029 1.00 35.40  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 226.626 274.244 211.372 1.00 47.55  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 227.151 271.312 211.071 1.00 33.48  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 227.047 269.984 210.317 1.00 39.86  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 228.411 269.334 210.183 1.00 41.26  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 226.072 269.042 211.003 1.00 38.46  ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 225.625 273.552 213.275 1.00 42.66  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 225.929 274.757 214.049 1.00 32.72  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 227.189 274.529 214.887 1.00 46.88  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 227.152 274.342 216.105 1.00 56.45  ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 224.737 275.146 214.915 1.00 45.05  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 223.442 275.335 214.148 1.00 41.19  ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 223.510 276.854 213.180 1.00 61.19  ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 223.494 276.210 211.521 1.00 50.01  ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 228.325 274.526 214.195 1.00 46.53  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 229.611 274.498 214.876 1.00 37.80  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 229.913 275.874 215.453 1.00 37.45  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 229.785 276.889 214.762 1.00 53.58  ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 230.717 274.071 213.913 1.00 39.07  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 230.347 272.579 212.968 1.00 57.17  ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 230.306 275.914 216.722 1.00 40.31  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 230.584 277.171 217.401 1.00 43.84  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 231.805 277.024 218.294 1.00 46.27  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 232.059 275.948 218.842 1.00 40.93  ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 229.379 277.629 218.230 1.00 40.28  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 229.006 276.641 219.173 1.00 44.44  ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 232.556 278.111 218.437 1.00 53.04  ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 233.715 278.146 219.324 1.00 48.39  ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 233.207 278.139 220.762 1.00 58.34  ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 232.033 278.461 220.997 1.00 65.56  ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 234.600 279.369 219.037 1.00 49.95  ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 234.984 279.409 217.567 1.00 52.39  ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 233.889 280.649 219.444 1.00 51.03  ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 234.028 277.761 221.743 1.00 64.84  ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 233.565 277.777 223.135 1.00 57.54  ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 233.091 279.163 223.551 1.00 53.99  ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 233.694 280.180 223.202 1.00 53.37  ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 234.804 277.343 223.922 1.00 59.93  ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 235.577 276.513 222.962 1.00 63.47  ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 235.359 277.140 221.614 1.00 60.53  ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 231.997 279.193 224.307 1.00 59.65  ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 231.384 280.435 224.721 1.00 58.80  ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 230.325 280.974 223.787 1.00 56.49  ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 229.680 281.976 224.121 1.00 56.98  ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 230.123 280.347 222.631 1.00 55.02  ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 229.098 280.753 221.683 1.00 58.51  ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 228.159 279.586 221.427 1.00 63.05  ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 228.602 278.446 221.258 1.00 67.52  ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 229.713 281.238 220.365 1.00 51.90  ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 230.285 282.634 220.447 1.00 60.82  ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 231.476 282.878 221.116 1.00 61.09  ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 229.623 283.710 219.872 1.00 59.75  ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 231.997 284.152 221.202 1.00 55.52  ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 230.139 284.989 219.949 1.00 62.01  ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 231.326 285.204 220.615 1.00 65.22  ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 231.844 286.476 220.697 1.00 71.10  ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 226.862 279.877 221.408 1.00 65.01  ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 225.838 278.864 221.192 1.00 60.98  ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 224.961 279.313 220.036 1.00 66.17  ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 224.340 280.377 220.104 1.00 63.59  ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 225.003 278.646 222.457 1.00 53.63  ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 223.847 277.698 222.236 1.00 62.10  ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 224.087 276.565 221.769 1.00 64.13  ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 222.697 278.084 222.529 1.00 63.60  ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 224.913 278.506 218.980 1.00 62.70  ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 224.185 278.859 217.770 1.00 60.37  ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 222.748 278.358 217.766 1.00 59.22  ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 222.033 278.591 216.786 1.00 64.82  ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 224.918 278.322 216.540 1.00 61.66  ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 222.308 277.673 218.824 1.00 56.60  ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 220.925 277.211 218.866 1.00 55.47  ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 219.957 278.383 218.939 1.00 55.40  ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 218.895 278.355 218.307 1.00 61.68  ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 220.712 276.266 220.049 1.00 55.78  ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 221.228 276.814 221.246 1.00 61.60  ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 220.315 279.428 219.691 1.00 62.43  ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 219.417 280.563 219.851 1.00 64.41  ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 219.054 281.220 218.533 1.00 65.86  ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 217.965 281.780 218.388 1.00 65.89  ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 219.962 281.167 217.557 1.00 63.43  ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 219.638 281.661 216.224 1.00 62.35  ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 218.575 280.792 215.563 1.00 66.72  ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 217.765 281.283 214.768 1.00 68.93  ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 220.896 281.711 215.357 1.00 61.47  ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 222.024 282.486 215.965 1.00 68.94  ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 223.306 282.451 215.459 1.00 70.23  ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 222.063 283.323 217.029 1.00 66.79  ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 224.087 283.228 216.189 1.00 65.44  ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 223.357 283.768 217.148 1.00 69.35  ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 218.566 279.495 215.878 1.00 63.58  ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 217.677 278.566 215.188 1.00 60.91  ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 216.223 278.797 215.591 1.00 67.57  ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 215.328 278.797 214.737 1.00 68.73  ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 218.120 277.115 215.445 1.00 58.29  ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 217.291 276.156 214.614 1.00 58.72  ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 219.600 276.952 215.135 1.00 53.47  ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 215.954 278.986 216.889 1.00 72.17  ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 214.585 279.295 217.297 1.00 70.11  ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 214.124 280.616 216.698 1.00 74.62  ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 212.979 280.736 216.247 1.00 79.61  ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 214.444 279.346 218.822 1.00 73.72  ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 214.591 278.022 219.556 1.00 75.26  ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 215.996 277.786 220.058 1.00 78.35  ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 216.831 278.697 219.914 1.00 74.49  ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 216.257 276.701 220.618 1.00 83.67  ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 215.001 281.622 216.694 1.00 72.88  ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 214.654 282.903 216.090 1.00 74.28  ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 214.398 282.754 214.596 1.00 77.57  ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 213.451 283.342 214.061 1.00 77.89  ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 215.765 283.921 216.347 1.00 74.02  ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 215.861 284.320 217.807 1.00 79.43  ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 214.824 284.290 218.502 1.00 81.42  ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 216.974 284.664 218.259 1.00 77.91  ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 215.233 281.972 213.906 1.00 72.08  ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 215.013 281.727 212.485 1.00 72.46  ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 213.701 280.990 212.249 1.00 75.25  ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 212.946 281.329 211.331 1.00 80.51  ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 216.187 280.938 211.903 1.00 75.01  ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 215.988 280.324 210.517 1.00 74.23  ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 215.842 281.411 209.465 1.00 72.85  ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 217.139 279.392 210.173 1.00 71.05  ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 213.411 279.978 213.071 1.00 77.63  ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 212.159 279.242 212.926 1.00 75.08  ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 210.957 280.126 213.233 1.00 75.80  ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 209.910 280.006 212.586 1.00 80.08  ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 212.166 278.010 213.831 1.00 73.26  ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 211.084 281.013 214.223 1.00 78.93  ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 209.983 281.907 214.565 1.00 78.65  ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 209.667 282.862 213.421 1.00 84.92  ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 208.496 283.147 213.146 1.00 85.82  ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 210.314 282.684 215.839 1.00 80.45  ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 210.701 283.377 212.750 1.00 89.71  ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 210.480 284.299 211.640 1.00 86.47  ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 209.735 283.623 210.495 1.00 86.52  ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 208.841 284.223 209.886 1.00 90.01  ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 211.814 284.864 211.152 1.00 86.38  ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 212.508 285.771 212.155 1.00 91.00  ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 213.835 286.295 211.644 1.00 92.26  ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 214.274 285.854 210.561 1.00 93.50  ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 214.440 287.149 212.325 1.00 90.05  ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 210.088 282.378 210.186 1.00 84.51  ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 209.461 281.640 209.097 1.00 85.19  ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 208.178 280.935 209.517 1.00 88.19  ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 207.550 280.280 208.679 1.00 88.84  ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 210.442 280.613 208.515 1.00 85.07  ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 211.877 281.109 208.336 1.00 84.63  ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 211.972 282.518 207.771 1.00 90.68  ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 211.207 282.903 206.885 1.00 89.25  ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 212.913 283.297 208.291 1.00 89.07  ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 207.781 281.054 210.787 1.00 88.54  ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 206.578 280.401 211.310 1.00 86.37  ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 206.628 278.890 211.096 1.00 87.84  ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 205.629 278.260 210.740 1.00 91.35  ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 205.309 280.997 210.695 1.00 86.42  ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 205.069 282.429 211.128 1.00 90.23  ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 204.929 283.326 210.296 1.00 90.75  ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 205.019 282.651 212.436 1.00 87.72  ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 207.801 278.304 211.312 1.00 76.00  ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 208.000 276.867 211.189 1.00 74.12  ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 208.158 276.270 212.582 1.00 76.74  ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 209.054 276.668 213.334 1.00 79.97  ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 209.226 276.553 210.331 1.00 73.76  ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 209.175 277.319 209.121 1.00 79.48  ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 209.269 275.072 209.986 1.00 71.45  ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 207.288 275.322 212.922 1.00 73.44  ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 207.374 274.659 214.216 1.00 68.07  ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 208.614 273.777 214.263 1.00 63.18  ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 208.883 273.014 213.329 1.00 63.49  ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 206.116 273.831 214.472 1.00 65.74  ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 206.099 273.118 215.814 1.00 66.16  ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 206.198 271.612 215.674 1.00 71.08  ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 205.594 271.020 214.779 1.00 67.42  ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 206.961 270.983 216.560 1.00 66.46  ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 209.373 273.882 215.350 1.00 50.22  ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 210.643 273.183 215.492 1.00 51.17  ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 210.663 272.445 216.823 1.00 53.77  ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 210.189 272.962 217.841 1.00 54.78  ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 211.839 274.155 215.380 1.00 49.64  ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 213.159 273.411 215.586 1.00 51.22  ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 211.699 275.305 216.368 1.00 53.76  ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 214.373 274.242 215.288 1.00 51.27  ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 211.201 271.229 216.808 1.00 47.40  ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 211.384 270.421 218.007 1.00 45.56  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 212.859 270.446 218.385 1.00 47.04  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 213.714 270.053 217.584 1.00 52.31  ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 210.910 268.985 217.781 1.00 50.99  ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 209.480 268.959 217.693 1.00 58.11  ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 211.358 268.089 218.925 1.00 47.61  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 213.152 270.906 219.597 1.00 44.52  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 214.518 271.028 220.088 1.00 38.49  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 214.780 269.955 221.134 1.00 44.86  ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 214.006 269.808 222.086 1.00 49.16  ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 214.763 272.418 220.680 1.00 41.26  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 214.429 273.433 219.751 1.00 53.56  ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 215.868 269.210 220.955 1.00 39.89  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 216.246 268.127 221.854 1.00 42.64  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 217.721 268.272 222.198 1.00 36.90  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 218.554 268.502 221.315 1.00 42.39  ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 215.965 266.744 221.229 1.00 38.54  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 214.464 266.554 221.006 1.00 38.80  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 216.514 265.632 222.108 1.00 37.74  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 214.133 265.734 219.786 1.00 46.21  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 218.041 268.137 223.482 1.00 39.48  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 219.416 268.199 223.960 1.00 34.80  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 219.972 266.783 224.049 1.00 35.08  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 219.402 265.929 224.736 1.00 40.95  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 219.490 268.898 225.316 1.00 29.09  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 221.079 266.542 223.357 1.00 34.16  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 221.677 265.214 223.286 1.00 43.36  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 222.513 264.966 224.534 1.00 39.83  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 223.174 265.876 225.050 1.00 39.01  ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 222.515 265.080 222.001 1.00 39.88  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 221.602 265.049 220.775 1.00 39.83  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 223.389 263.834 222.034 1.00 37.58  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 220.495 264.021 220.863 1.00 31.92  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 222.487 263.728 225.026 1.00 41.95  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 223.280 263.360 226.182 1.00 42.25  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 222.637 262.330 227.086 1.00 46.84  ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 223.326 261.681 227.878 1.00 52.21  ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 221.323 262.161 226.978 1.00 53.92  ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 220.592 261.187 227.773 1.00 50.41  ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 220.176 260.006 226.905 1.00 56.77  ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 220.040 260.119 225.684 1.00 61.57  ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 219.358 261.822 228.424 1.00 50.17  ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 218.599 262.553 227.478 1.00 52.66  ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 219.986 258.856 227.559 1.00 52.65  ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 219.573 257.655 226.839 1.00 56.00  ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 218.214 257.848 226.179 1.00 52.34  ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 218.014 257.455 225.024 1.00 56.58  ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 219.546 256.457 227.787 1.00 59.33  ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 217.265 258.449 226.899 1.00 57.08  ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 215.977 258.780 226.305 1.00 59.69  ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 216.070 259.968 225.358 1.00 63.37  ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 215.167 260.160 224.537 1.00 69.54  ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 214.945 259.056 227.401 1.00 59.86  ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 215.351 260.139 228.386 1.00 64.44  ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 216.180 259.595 229.536 1.00 67.74  ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 216.598 258.420 229.467 1.00 67.15  ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 216.416 260.340 230.507 1.00 61.66  ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 217.135 260.767 225.455 1.00 56.05  ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 217.318 261.855 224.508 1.00 51.36  ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 217.498 261.362 223.086 1.00 51.60  ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 217.047 262.004 222.134 1.00 56.66  ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 218.165 260.217 222.922 1.00 52.24  ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 218.287 259.615 221.599 1.00 43.93  ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 216.931 259.154 221.081 1.00 48.13  ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 216.650 259.255 219.881 1.00 60.59  ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 219.270 258.446 221.642 1.00 48.07  ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 220.622 258.809 222.187 1.00 51.61  ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 221.266 259.960 221.766 1.00 50.95  ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 221.248 257.999 223.118 1.00 52.12  ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 222.510 260.296 222.265 1.00 50.57  ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 222.491 258.329 223.620 1.00 52.10  ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 223.123 259.479 223.193 1.00 52.01  ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 216.082 258.633 221.970 1.00 48.71  ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 214.752 258.196 221.558 1.00 51.17  ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 213.914 259.368 221.064 1.00 51.72  ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 213.226 259.261 220.042 1.00 55.27  ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 214.051 257.485 222.714 1.00 53.97  ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 214.749 256.201 223.116 1.00 60.45  ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 215.487 255.610 222.329 1.00 61.93  ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 214.519 255.764 224.349 1.00 55.95  ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 213.957 260.497 221.776 1.00 47.51  ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 213.224 261.678 221.328 1.00 45.88  ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 213.781 262.201 220.011 1.00 47.91  ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 213.024 262.661 219.148 1.00 49.02  ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 213.267 262.768 222.398 1.00 48.15  ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 212.939 262.285 223.799 1.00 50.99  ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 212.944 263.408 224.816 1.00 60.09  ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 212.938 264.586 224.457 1.00 55.46  ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 212.954 263.050 226.094 1.00 57.38  ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 215.104 262.150 219.843 1.00 43.21  ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 215.707 262.583 218.587 1.00 38.26  ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 215.248 261.712 217.425 1.00 50.95  ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 214.919 262.224 216.350 1.00 55.81  ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 217.231 262.567 218.703 1.00 40.68  ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 215.219 260.392 217.623 1.00 52.91  ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 214.767 259.496 216.563 1.00 48.86  ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 213.294 259.716 216.240 1.00 51.81  ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 212.906 259.739 215.066 1.00 58.53  ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 215.019 258.043 216.962 1.00 55.27  ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 216.465 257.628 216.769 1.00 62.34  ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 217.110 258.137 215.829 1.00 59.28  ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 216.955 256.793 217.558 1.00 61.53  ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 212.458 259.876 217.269 1.00 47.78  ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 211.034 260.103 217.036 1.00 43.92  ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 210.791 261.430 216.329 1.00 52.73  ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 209.940 261.520 215.437 1.00 60.43  ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 210.269 260.053 218.359 1.00 50.64  ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 210.267 258.687 219.025 1.00 58.27  ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 209.478 258.709 220.325 1.00 54.74  ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 209.400 257.323 220.945 1.00 56.96  ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 210.733 256.844 221.402 1.00 51.17  ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 211.522 262.476 216.722 1.00 54.89  ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 211.348 263.779 216.087 1.00 51.96  ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 211.758 263.741 214.620 1.00 51.56  ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 211.065 264.299 213.761 1.00 53.96  ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 212.146 264.842 216.840 1.00 48.00  ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 212.881 263.090 214.314 1.00 42.60  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 213.344 263.011 212.932 1.00 44.89  ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 212.381 262.183 212.091 1.00 48.65  ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 212.054 262.546 210.955 1.00 55.22  ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 214.776 262.449 212.876 1.00 50.90  ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 215.752 263.412 213.553 1.00 48.56  ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 215.197 262.192 211.438 1.00 51.39  ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 217.131 262.835 213.764 1.00 43.12  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 211.905 261.061 212.638 1.00 51.71  ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 211.005 260.192 211.884 1.00 48.55  ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 209.706 260.907 211.532 1.00 48.75  ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 209.166 260.725 210.435 1.00 53.31  ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 210.716 258.919 212.680 1.00 46.90  ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 211.907 257.984 212.734 1.00 53.82  ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 212.940 258.238 212.115 1.00 57.59  ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 211.769 256.893 213.478 1.00 50.15  ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 209.182 261.715 212.454 1.00 50.28  ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 207.959 262.460 212.177 1.00 52.86  ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 208.218 263.652 211.261 1.00 55.80  ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 207.393 263.960 210.393 1.00 60.97  ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 207.323 262.925 213.489 1.00 50.07  ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 207.091 261.793 214.336 1.00 50.21  ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 205.999 263.628 213.225 1.00 51.44  ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 209.359 264.324 211.431 1.00 53.65  ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 209.604 265.565 210.702 1.00 48.53  ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 209.856 265.313 209.220 1.00 51.86  ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 209.478 266.131 208.374 1.00 52.62  ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 210.779 266.317 211.322 1.00 47.58  ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 210.501 264.192 208.883 1.00 50.23  ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 210.804 263.909 207.483 1.00 49.12  ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 209.536 263.713 206.665 1.00 57.13  ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 209.575 263.802 205.433 1.00 58.72  ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 211.730 262.681 207.360 1.00 45.82  ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 213.079 262.969 207.994 1.00 48.01  ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 211.085 261.459 207.989 1.00 50.94  ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 208.409 263.445 207.319 1.00 61.49  ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 207.114 263.348 206.659 1.00 59.44  ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 206.300 264.627 206.784 1.00 55.05  ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 205.742 265.106 205.793 1.00 58.24  ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 206.319 262.167 207.233 1.00 54.47  ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 206.917 260.806 206.922 1.00 56.29  ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 205.998 259.684 207.376 1.00 59.41  ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 206.013 259.536 208.889 1.00 58.63  ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 205.203 258.371 209.340 1.00 58.85  ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 206.220 265.197 207.989 1.00 54.27  ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 205.439 266.414 208.186 1.00 57.63  ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 206.131 267.627 207.577 1.00 60.08  ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 205.465 268.573 207.140 1.00 59.27  ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 205.181 266.636 209.676 1.00 60.54  ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 206.388 266.895 210.371 1.00 66.73  ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 207.460 267.623 207.539 1.00 65.34  ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 208.215 268.741 207.019 1.00 61.53  ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 208.660 269.763 208.040 1.00 64.85  ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 209.057 270.867 207.649 1.00 66.74  ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 208.605 269.439 209.328 1.00 67.80  ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 209.012 270.369 210.368 1.00 63.83  ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 210.532 270.374 210.522 1.00 64.60  ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 211.259 269.643 209.846 1.00 63.79  ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 208.343 270.011 211.694 1.00 63.03  ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 206.829 270.133 211.677 1.00 63.17  ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 206.401 271.587 211.574 1.00 69.99  ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 204.954 271.740 211.667 1.00 74.23  ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 204.132 271.738 210.627 1.00 73.60  ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 204.582 271.590 209.391 1.00 70.87  ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 202.827 271.888 210.831 1.00 69.16  ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 211.009 271.219 211.431 1.00 58.77  ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 212.430 271.349 211.717 1.00 53.56  ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 212.766 270.646 213.025 1.00 55.91  ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 212.002 270.713 213.992 1.00 58.95  ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 212.843 272.820 211.799 1.00 46.91  ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 212.856 273.525 210.479 1.00 51.60  ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 212.455 273.023 209.276 1.00 52.88  ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 213.299 274.864 210.227 1.00 54.30  ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 212.618 273.966 208.291 1.00 50.94  ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 213.135 275.105 208.849 1.00 56.68  ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 213.818 275.882 211.033 1.00 54.50  ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 213.470 276.322 208.260 1.00 55.89  ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 214.150 277.088 210.446 1.00 54.69  ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 213.975 277.298 209.073 1.00 55.18  ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 213.908 269.965 213.046 1.00 45.66  ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 214.409 269.293 214.240 1.00 44.91  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 215.823 269.788 214.497 1.00 45.73  ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 216.675 269.742 213.601 1.00 54.55  ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 214.381 267.764 214.092 1.00 38.64  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 215.122 267.107 215.245 1.00 41.92  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 212.950 267.268 214.034 1.00 50.32  ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 216.074 270.261 215.714 1.00 37.56  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 217.399 270.697 216.128 1.00 40.66  ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 217.871 269.846 217.297 1.00 38.79  ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 217.133 269.649 218.267 1.00 46.72  ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 217.404 272.174 216.524 1.00 45.19  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 218.703 272.611 217.182 1.00 36.50  ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 218.738 274.361 217.584 1.00 55.00  ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 217.389 274.447 218.752 1.00 47.24  ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 219.099 269.345 217.199 1.00 34.41  ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 219.723 268.555 218.251 1.00 32.08  ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 220.969 269.290 218.721 1.00 32.67  ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 221.873 269.557 217.923 1.00 45.55  ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 220.065 267.152 217.746 1.00 39.58  ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 218.934 266.482 216.963 1.00 36.29  ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 219.397 265.184 216.330 1.00 33.60  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 217.731 266.240 217.861 1.00 35.27  ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 221.014 269.617 220.008 1.00 32.01  ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 222.082 270.428 220.572 1.00 34.05  ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 223.106 269.556 221.286 1.00 31.41  ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 222.783 268.488 221.811 1.00 34.74  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 221.521 271.466 221.546 1.00 30.32  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 220.141 271.983 221.182 1.00 32.24  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 219.597 272.892 222.270 1.00 35.88  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 218.094 273.066 222.145 1.00 44.35  ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 217.539 273.891 223.252 1.00 44.21  ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 224.352 270.037 221.301 1.00 37.95  ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 225.466 269.353 221.960 1.00 24.59  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 225.619 267.923 221.446 1.00 36.53  ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 225.808 266.976 222.212 1.00 55.13  ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 225.302 269.379 223.482 1.00 40.45  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 224.973 270.761 224.009 1.00 43.37  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 225.719 271.715 223.789 1.00 45.17  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 223.851 270.876 224.708 1.00 39.72  ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 225.532 267.771 220.122 1.00 40.15  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 225.686 266.456 219.513 1.00 36.73  ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 227.116 265.946 219.626 1.00 35.05  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 227.353 264.743 219.473 1.00 47.01  ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 225.241 266.487 218.039 1.00 31.77  ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 223.761 266.818 217.941 1.00 33.60  ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 226.069 267.490 217.255 1.00 34.33  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 228.078 266.832 219.893 1.00 38.36  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 229.469 266.422 220.041 1.00 34.61  ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 229.696 265.527 221.251 1.00 44.55  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 230.730 264.854 221.315 1.00 55.79  ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 230.370 267.654 220.139 1.00 41.98  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 230.107 268.499 221.346 1.00 44.14  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 229.118 269.458 221.382 1.00 42.81  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 230.700 268.525 222.563 1.00 44.55  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 229.115 270.041 222.567 1.00 41.16  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 230.065 269.493 223.303 1.00 45.45  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 228.766 265.504 222.206 1.00 41.63  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 228.893 264.649 223.377 1.00 39.09  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 228.576 263.189 223.084 1.00 45.26  ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 228.856 262.331 223.928 1.00 45.88  ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 227.982 265.155 224.498 1.00 37.22  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 228.206 266.600 224.947 1.00 37.98  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 227.058 267.075 225.819 1.00 36.13  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 229.531 266.733 225.680 1.00 36.82  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 228.003 262.886 221.920 1.00 47.41  ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 227.677 261.516 221.523 1.00 42.23  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 228.218 261.272 220.121 1.00 48.39  ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 227.451 261.194 219.151 1.00 52.24  ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 226.170 261.266 221.587 1.00 43.59  ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 229.542 261.156 219.973 1.00 54.28  ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 230.094 260.894 218.634 1.00 49.91  ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 229.689 259.544 218.071 1.00 52.86  ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 229.526 259.412 216.852 1.00 54.92  ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 231.609 260.993 218.859 1.00 51.56  ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 231.795 260.635 220.292 1.00 53.71  ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 230.582 261.150 221.016 1.00 50.64  ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 229.525 258.533 218.927 1.00 52.97  ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 229.125 257.223 218.438 1.00 52.44  ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 227.730 257.223 217.843 1.00 53.63  ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 227.486 256.598 216.808 1.00 56.27  ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 226.797 257.923 218.490 1.00 47.50  ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 225.447 258.032 217.950 1.00 46.33  ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 225.409 258.933 216.722 1.00 54.06  ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 224.514 258.795 215.880 1.00 52.88  ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 224.497 258.544 219.034 1.00 46.81  ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 223.168 258.996 218.522 1.00 48.98  ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 222.070 258.222 218.290 1.00 50.87  ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 222.793 260.336 218.185 1.00 50.12  ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 221.035 258.996 217.825 1.00 52.10  ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 221.454 260.298 217.751 1.00 50.30  ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 223.462 261.563 218.205 1.00 53.34  ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 220.771 261.439 217.343 1.00 51.53  ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 222.783 262.694 217.799 1.00 55.74  ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 221.452 262.625 217.374 1.00 54.20  ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 226.369 259.853 216.601 1.00 57.60  ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 226.429 260.716 215.426 1.00 48.55  ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 226.713 259.912 214.163 1.00 57.29  ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 226.177 260.220 213.092 1.00 64.53  ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 227.489 261.798 215.623 1.00 51.93  ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 227.023 263.090 216.296 1.00 55.51  ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 228.159 264.097 216.364 1.00 50.27  ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 225.825 263.675 215.563 1.00 53.30  ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 227.562 258.886 214.266 1.00 67.09  ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 227.840 258.036 213.113 1.00 62.54  ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 226.584 257.307 212.651 1.00 64.27  ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 226.335 257.187 211.446 1.00 68.27  ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 228.947 257.038 213.452 1.00 58.93  ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 230.305 257.678 213.680 1.00 69.13  ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 231.585 256.475 214.086 1.00 90.26  ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 232.983 257.555 214.377 1.00 69.74  ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 225.784 256.808 213.596 1.00 59.61  ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 224.517 256.181 213.236 1.00 56.60  ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 223.558 257.195 212.625 1.00 61.33  ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 222.817 256.874 211.688 1.00 65.93  ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 223.888 255.520 214.462 1.00 61.38  ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 224.874 254.770 215.341 1.00 65.89  ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 224.361 254.577 216.755 1.00 68.88  ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 223.155 254.592 216.997 1.00 63.50  ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 225.278 254.393 217.697 1.00 65.15  ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 223.550 258.422 213.152 1.00 61.85  ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 222.679 259.460 212.610 1.00 54.58  ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 223.042 259.789 211.167 1.00 59.63  ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 222.157 259.985 210.326 1.00 61.89  ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 222.753 260.712 213.483 1.00 50.16  ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 222.035 261.956 212.960 1.00 56.55  ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 220.533 261.728 212.921 1.00 54.44  ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 222.374 263.168 213.811 1.00 58.25  ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 224.340 259.861 210.864 1.00 60.52  ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 224.765 260.131 209.494 1.00 56.06  ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 224.346 259.007 208.555 1.00 62.77  ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 223.918 259.260 207.423 1.00 67.13  ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 226.279 260.338 209.446 1.00 56.15  ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 226.787 260.928 208.140 1.00 62.45  ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 227.162 259.866 207.125 1.00 66.01  ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 227.931 258.948 207.479 1.00 68.61  ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 226.687 259.949 205.972 1.00 62.63  ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 224.471 257.756 209.005 1.00 62.40  ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 224.038 256.627 208.187 1.00 56.57  ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 222.534 256.663 207.951 1.00 59.35  ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 222.064 256.371 206.845 1.00 63.23  ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 224.445 255.313 208.852 1.00 57.41  ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 225.911 254.958 208.683 1.00 59.51  ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 226.332 253.893 209.679 1.00 64.14  ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 227.780 253.488 209.472 1.00 64.92  ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 228.685 254.669 209.437 1.00 63.81  ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 221.763 257.010 208.983 1.00 59.63  ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 220.316 257.115 208.829 1.00 57.25  ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 219.944 258.232 207.862 1.00 58.97  ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 219.020 258.083 207.053 1.00 61.27  ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 219.664 257.341 210.194 1.00 53.87  ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 218.247 257.887 210.135 1.00 58.96  ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 217.674 258.075 211.530 1.00 62.65  ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 216.188 258.386 211.479 1.00 62.78  ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 215.562 258.318 212.828 1.00 60.35  ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 220.657 259.358 207.927 1.00 63.96  ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 220.352 260.485 207.051 1.00 64.90  ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 220.670 260.178 205.594 1.00 61.16  ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 219.965 260.653 204.697 1.00 63.28  ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 221.122 261.724 207.505 1.00 61.37  ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 220.601 262.442 208.750 1.00 60.67  ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 221.586 263.511 209.190 1.00 60.89  ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 219.229 263.043 208.490 1.00 59.22  ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 221.726 259.400 205.337 1.00 61.62  ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 222.122 259.119 203.960 1.00 65.97  ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 221.033 258.359 203.211 1.00 67.18  ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 220.723 258.680 202.058 1.00 62.54  ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 223.432 258.333 203.941 1.00 65.73  ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 223.919 258.004 202.565 1.00 68.11  ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 224.456 258.951 201.720 1.00 66.15  ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 223.950 256.834 201.886 1.00 65.31  ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 224.797 258.378 200.579 1.00 65.02  ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 224.501 257.093 200.654 1.00 64.85  ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 220.441 257.351 203.850 1.00 75.96  ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 219.361 256.571 203.248 1.00 76.33  ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 218.036 257.137 203.751 1.00 75.61  ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 217.367 256.569 204.614 1.00 79.22  ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 219.514 255.091 203.582 1.00 76.61  ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 219.528 254.884 204.984 1.00 73.50  ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 217.658 258.283 203.190 1.00 69.74  ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 216.457 258.978 203.629 1.00 70.16  ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 215.957 259.870 202.504 1.00 73.00  ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 216.748 260.451 201.756 1.00 73.77  ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 216.727 259.804 204.892 1.00 74.26  ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 215.527 260.178 205.762 1.00 76.01  ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 214.809 258.930 206.248 1.00 72.49  ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 215.979 261.029 206.936 1.00 72.29  ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 214.634 259.970 202.396 1.00 80.03  ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 213.970 260.826 201.413 1.00 79.27  ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 212.977 261.703 202.163 1.00 79.13  ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 211.764 261.454 202.138 1.00 79.50  ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 213.281 259.999 200.327 1.00 79.67  ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 214.238 259.248 199.414 1.00 80.46  ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 215.173 260.174 198.661 1.00 83.95  ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 216.393 260.015 198.708 1.00 83.14  ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 214.604 261.147 197.959 1.00 79.70  ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 213.456 262.738 202.839 1.00 69.22  ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 212.595 263.538 203.713 1.00 66.20  ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 211.727 264.505 202.913 1.00 62.72  ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 211.814 264.602 201.691 1.00 68.40  ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 213.599 264.284 204.592 1.00 62.57  ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 214.799 264.438 203.727 1.00 64.95  ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 214.845 263.231 202.825 1.00 67.34  ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 210.876 265.223 203.640 1.00 54.85  ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 210.023 266.237 203.042 1.00 57.78  ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 210.864 267.409 202.542 1.00 62.56  ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 211.980 267.653 203.009 1.00 67.07  ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 208.982 266.717 204.054 1.00 59.64  ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 207.899 267.563 203.460 1.00 63.23  ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 207.974 268.938 203.404 1.00 64.83  ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 206.713 267.228 202.900 1.00 63.62  ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 206.882 269.413 202.833 1.00 63.53  ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 206.100 268.396 202.518 1.00 65.05  ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 210.312 268.137 201.568 1.00 61.60  ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 211.047 269.242 200.960 1.00 61.32  ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 211.355 270.344 201.966 1.00 61.25  ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 212.401 270.996 201.868 1.00 62.47  ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 210.260 269.809 199.779 1.00 59.71  ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 210.469 270.568 202.933 1.00 56.80  ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 210.652 271.616 203.927 1.00 58.09  ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 211.349 271.130 205.191 1.00 59.66  ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 211.546 271.925 206.115 1.00 60.89  ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 209.299 272.234 204.294 1.00 60.71  ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 208.503 273.141 202.948 1.00 73.30  ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 211.723 269.855 205.258 1.00 53.31  ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 212.389 269.334 206.443 1.00 43.64  ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 213.809 269.876 206.546 1.00 52.83  ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 214.542 269.939 205.556 1.00 59.75  ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 212.414 267.806 206.411 1.00 47.43  ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 213.373 267.194 207.393 1.00 46.31  ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 213.061 267.135 208.740 1.00 49.75  ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 214.585 266.675 206.970 1.00 47.80  ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 213.939 266.572 209.646 1.00 46.13  ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 215.467 266.111 207.871 1.00 50.89  ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 215.143 266.060 209.211 1.00 48.49  ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 214.193 270.269 207.759 1.00 53.88  ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 215.543 270.734 208.042 1.00 46.61  ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 215.995 270.160 209.375 1.00 45.83  ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 215.218 270.108 210.332 1.00 44.20  ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 215.620 272.266 208.082 1.00 46.99  ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 215.481 272.939 206.728 1.00 48.78  ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 216.555 272.469 205.761 1.00 51.13  ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 216.482 273.165 204.482 1.00 52.95  ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 215.579 272.920 203.543 1.00 53.65  ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 214.653 271.987 203.700 1.00 51.71  ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 215.606 273.626 202.417 1.00 51.61  ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 217.252 269.728 209.432 1.00 43.03  ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 217.847 269.198 210.652 1.00 37.62  ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 219.059 270.043 211.011 1.00 42.50  ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 219.985 270.181 210.204 1.00 47.82  ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 218.245 267.730 210.484 1.00 37.16  ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 218.981 267.110 211.673 1.00 37.63  ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 218.016 266.816 212.808 1.00 38.02  ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 219.716 265.850 211.254 1.00 40.41  ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 219.052 270.606 212.215 1.00 34.79  ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 220.146 271.428 212.713 1.00 23.85  ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 220.881 270.675 213.812 1.00 40.41  ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 220.254 270.159 214.742 1.00 49.48  ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 219.637 272.772 213.241 1.00 27.43  ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 218.892 273.588 212.220 1.00 35.47  ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 217.566 273.318 211.925 1.00 32.09  ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 219.517 274.639 211.570 1.00 37.01  ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 216.883 274.071 210.990 1.00 31.05  ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 218.838 275.395 210.635 1.00 35.93  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 217.520 275.111 210.345 1.00 40.71  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 222.205 270.612 213.700 1.00 37.71  ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 223.053 269.949 214.686 1.00 33.55  ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 223.968 270.996 215.306 1.00 33.56  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 224.733 271.658 214.597 1.00 46.90  ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 223.861 268.820 214.047 1.00 35.76  ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 223.055 267.709 213.372 1.00 28.01  ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 223.956 266.540 213.009 1.00 34.19  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 221.914 267.251 214.266 1.00 39.13  ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 223.892 271.143 216.626 1.00 35.07  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 224.693 272.124 217.344 1.00 39.18  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 225.838 271.425 218.066 1.00 32.30  ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 225.612 270.497 218.849 1.00 44.22  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 223.831 272.899 218.341 1.00 44.02  ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 222.913 273.738 217.630 1.00 36.77  ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 224.701 273.761 219.243 1.00 47.44  ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 227.063 271.872 217.800 1.00 33.67  ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 228.254 271.300 218.409 1.00 42.03  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 229.189 272.433 218.816 1.00 50.45  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 228.857 273.616 218.687 1.00 54.35  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 228.936 270.310 217.458 1.00 43.63  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 229.480 270.936 216.188 1.00 55.26  ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 230.173 269.707 215.067 1.00 76.78  ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 228.679 268.932 214.456 1.00 46.45  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 230.370 272.067 219.312 1.00 48.64  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 231.327 273.028 219.849 1.00 48.97  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 232.686 272.928 219.158 1.00 52.50  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 233.709 273.311 219.731 1.00 64.89  ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 231.473 272.849 221.360 1.00 51.19  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 232.208 271.584 221.781 1.00 57.22  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 232.571 271.584 223.253 1.00 61.50  ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 232.204 272.547 223.957 1.00 59.06  ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 233.223 270.619 223.705 1.00 56.86  ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 232.699 272.442 217.915 1.00 44.74  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 233.922 272.232 217.145 1.00 54.75  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 234.831 271.304 217.945 1.00 54.48  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 236.005 271.606 218.187 1.00 49.32  ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 234.616 273.564 216.796 1.00 43.41  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 233.617 274.531 216.165 1.00 48.54  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 235.736 273.350 215.786 1.00 47.73  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 234.169 275.925 215.956 1.00 46.47  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 234.278 270.184 218.393 1.00 56.71  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 235.063 269.196 219.117 1.00 53.19  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 235.836 268.321 218.131 1.00 53.97  ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 235.307 267.959 217.077 1.00 58.81  ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 234.157 268.329 219.988 1.00 55.67  ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 234.919 267.590 221.069 1.00 60.53  ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 235.034 266.366 221.037 1.00 59.76  ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 235.443 268.333 222.036 1.00 52.82  ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 237.088 267.969 218.442 1.00 52.00  ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 237.868 267.125 217.526 1.00 45.93  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 237.372 265.691 217.423 1.00 50.77  ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 237.873 264.945 216.574 1.00 54.48  ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 239.281 267.176 218.126 1.00 47.94  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 239.062 267.469 219.568 1.00 54.45  ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 237.877 268.389 219.613 1.00 56.03  ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 236.411 265.279 218.248 1.00 51.05  ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 235.877 263.924 218.212 1.00 54.78  ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 234.611 263.815 217.371 1.00 57.42  ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 234.001 262.742 217.324 1.00 57.65  ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 235.610 263.422 219.633 1.00 55.92  ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 236.844 263.396 220.520 1.00 57.39  ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 236.544 262.772 221.873 1.00 58.56  ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 235.445 263.525 222.603 1.00 61.87  ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 235.142 262.916 223.927 1.00 60.05  ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 234.199 264.893 216.717 1.00 49.51  ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 233.038 264.831 215.822 1.00 47.63  ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 233.390 263.975 214.610 1.00 50.08  ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 234.466 264.164 214.016 1.00 49.29  ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 232.615 266.240 215.401 1.00 45.70  ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 231.539 266.180 214.327 1.00 46.43  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 232.123 267.025 216.608 1.00 48.30  ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 232.544 263.022 214.221 1.00 52.17  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 232.878 262.150 213.088 1.00 48.06  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 233.102 262.937 211.805 1.00 51.93  ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 232.411 263.919 211.524 1.00 55.60  ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 231.654 261.234 212.982 1.00 46.37  ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 231.077 261.222 214.355 1.00 53.73  ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 231.305 262.602 214.896 1.00 56.25  ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 234.088 262.494 211.022 1.00 47.35  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 234.406 263.163 209.763 1.00 38.62  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 233.273 262.980 208.760 1.00 42.11  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 232.928 263.905 208.014 1.00 51.13  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 235.748 262.645 209.212 1.00 37.99  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 235.911 263.013 207.744 1.00 48.22  ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 236.903 263.195 210.034 1.00 35.35  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 232.671 261.788 208.732 1.00 46.19  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 231.602 261.519 207.775 1.00 47.33  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 230.402 262.430 208.003 1.00 47.45  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 229.690 262.780 207.054 1.00 54.86  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 231.198 260.043 207.842 1.00 54.62  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 230.614 259.644 209.191 1.00 61.76  ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 230.385 260.480 210.064 1.00 61.87  ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 230.370 258.350 209.361 1.00 59.56  ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 230.156 262.821 209.256 1.00 40.32  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 229.082 263.769 209.531 1.00 43.44  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 229.424 265.157 209.004 1.00 48.37  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 228.557 265.852 208.461 1.00 51.51  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 228.797 263.823 211.031 1.00 44.33  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 227.656 264.752 211.451 1.00 44.44  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 226.312 264.055 211.309 1.00 39.59  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 227.862 265.253 212.870 1.00 47.62  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 230.681 265.580 209.163 1.00 44.60  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 231.091 266.891 208.671 1.00 40.80  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 230.979 266.972 207.154 1.00 39.62  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 230.536 267.990 206.610 1.00 46.36  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 232.520 267.195 209.121 1.00 37.23  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 232.748 267.344 210.626 1.00 41.85  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 234.225 267.537 210.927 1.00 37.34  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 231.929 268.496 211.183 1.00 36.68  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 231.382 265.910 206.454 1.00 43.22  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 231.288 265.904 204.998 1.00 42.24  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 229.838 265.854 204.534 1.00 44.04  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 229.471 266.514 203.555 1.00 47.06  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 232.072 264.722 204.428 1.00 36.06  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 233.556 264.752 204.740 1.00 38.08  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 234.256 263.521 204.195 1.00 39.95  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 233.665 263.071 202.940 1.00 52.73  ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 234.245 263.188 201.754 1.00 56.11  ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 235.440 263.739 201.621 1.00 50.66  ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 233.610 262.742 200.674 1.00 46.63  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 229.001 265.071 205.219 1.00 39.76  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 227.609 264.928 204.803 1.00 39.76  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 226.840 266.234 204.958 1.00 44.54  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 226.037 266.594 204.090 1.00 45.72  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 226.935 263.813 205.601 1.00 40.68  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 227.070 266.956 206.054 1.00 42.93  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 226.339 268.169 206.340 1.00 36.46  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 227.095 269.429 205.945 1.00 33.70  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 228.267 269.404 205.585 1.00 49.70  ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 226.384 270.550 206.022 1.00 40.55  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 226.953 271.861 205.745 1.00 47.79  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 227.388 272.503 207.056 1.00 48.88  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 226.606 272.569 208.010 1.00 51.72  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 225.950 272.758 205.018 1.00 42.18  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 226.464 274.164 204.762 1.00 50.52  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 226.046 274.668 203.392 1.00 50.92  ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 226.409 276.067 203.196 1.00 53.48  ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 225.954 276.828 202.211 1.00 55.49  ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 225.118 276.355 201.302 1.00 45.45  ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 226.349 278.096 202.135 1.00 51.37  ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 228.630 272.975 207.096 1.00 38.51  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 229.252 273.466 208.319 1.00 28.32  ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 229.127 274.981 208.370 1.00 33.25  ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 229.472 275.676 207.406 1.00 46.14  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 230.725 273.034 208.401 1.00 39.41  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 230.832 271.509 208.363 1.00 45.51  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 231.377 273.591 209.656 1.00 36.94  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 232.223 271.002 208.069 1.00 41.20  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 228.623 275.491 209.492 1.00 36.30  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 228.596 276.921 209.774 1.00 33.04  ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 229.337 277.151 211.080 1.00 37.08  ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 228.971 276.576 212.110 1.00 50.04  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 227.161 277.446 209.868 1.00 34.36  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 226.403 277.374 208.576 1.00 39.86  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 226.597 278.326 207.591 1.00 42.15  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 225.498 276.353 208.346 1.00 39.03  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 225.901 278.261 206.400 1.00 45.98  ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 224.800 276.283 207.158 1.00 40.49  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 225.002 277.238 206.184 1.00 44.97  ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 230.370 277.985 211.040 1.00 36.65  ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 231.207 278.255 212.203 1.00 28.13  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 230.761 279.572 212.819 1.00 39.90  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 230.698 280.600 212.134 1.00 47.39  ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 232.697 278.293 211.829 1.00 31.92  ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 233.501 278.977 212.923 1.00 38.71  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 233.213 276.885 211.595 1.00 37.78  ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 230.449 279.541 214.111 1.00 46.05  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 230.032 280.720 214.858 1.00 44.41  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 231.133 281.087 215.841 1.00 42.09  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 231.548 280.256 216.656 1.00 50.45  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 228.708 280.469 215.576 1.00 46.50  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 227.540 280.332 214.646 1.00 45.85  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 227.252 279.116 214.050 1.00 43.33  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 226.733 281.420 214.361 1.00 53.06  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 226.183 278.989 213.189 1.00 46.83  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 225.660 281.297 213.502 1.00 51.52  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 225.384 280.080 212.916 1.00 45.31  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 231.597 282.325 215.761 1.00 45.93  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 232.752 282.780 216.520 1.00 45.22  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 232.581 284.267 216.774 1.00 52.69  ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 231.644 284.889 216.257 1.00 54.46  ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 234.055 282.493 215.761 1.00 45.99  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 233.980 282.757 214.270 1.00 51.02  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 235.331 282.642 213.595 1.00 58.58  ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 236.341 282.479 214.312 1.00 54.36  ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 235.383 282.714 212.350 1.00 63.15  ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 233.448 284.866 217.590 1.00 57.06  ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 233.397 286.319 217.774 1.00 50.22  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 233.524 287.041 216.446 1.00 59.47  ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 234.315 286.635 215.580 1.00 61.33  ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 234.604 286.603 218.679 1.00 55.32  ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 234.760 285.367 219.469 1.00 60.22  ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 234.341 284.228 218.578 1.00 58.86  ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 232.747 288.103 216.241 1.00 55.28  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 232.838 288.841 214.986 1.00 49.26  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 234.223 289.425 214.807 1.00 56.58  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 234.914 289.748 215.792 1.00 64.14  ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 231.775 289.939 215.142 1.00 48.88  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 231.383 289.928 216.584 1.00 58.68  ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 231.626 288.553 217.079 1.00 51.26  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 234.681 289.570 213.559 1.00 52.23  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 236.075 289.994 213.333 1.00 49.99  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 236.424 291.338 213.948 1.00 56.01  ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 237.562 291.526 214.397 1.00 62.14  ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 236.184 290.031 211.800 1.00 53.23  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 234.775 290.065 211.299 1.00 52.82  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 233.962 289.317 212.300 1.00 49.79  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 235.487 292.281 213.985 1.00 48.56  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 235.800 293.599 214.500 1.00 40.89  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 234.626 294.340 215.102 1.00 44.72  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 233.534 293.783 215.244 1.00 57.21  ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 234.849 295.606 215.466 1.00 45.50  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 233.790 296.414 216.065 1.00 45.99  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 232.657 296.634 215.070 1.00 48.10  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 231.475 296.535 215.421 1.00 54.72  ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 234.365 297.749 216.575 1.00 42.60  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 233.250 298.748 216.844 1.00 39.63  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 235.197 297.525 217.827 1.00 42.69  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 232.999 296.935 213.815 1.00 48.22  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 231.977 297.179 212.802 1.00 43.58  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 231.125 295.937 212.572 1.00 45.65  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 229.896 296.023 212.464 1.00 51.65  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 232.632 297.636 211.499 1.00 47.71  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 231.651 297.922 210.375 1.00 44.59  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 232.368 298.424 209.134 1.00 50.20  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 231.432 298.483 207.939 1.00 59.37  ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 232.141 298.907 206.701 1.00 55.88  ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 231.763 294.768 212.496 1.00 44.74  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 231.012 293.529 212.326 1.00 41.73  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 230.244 293.171 213.592 1.00 46.95  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 229.158 292.583 213.520 1.00 55.95  ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 231.954 292.394 211.929 1.00 46.49  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 230.795 293.509 214.760 1.00 42.15  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 230.107 293.233 216.017 1.00 39.62  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 228.806 294.019 216.115 1.00 41.80  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 227.773 293.487 216.538 1.00 50.03  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 231.022 293.563 217.197 1.00 37.71  ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 230.680 292.769 218.441 1.00 43.94  ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 229.528 292.733 218.872 1.00 51.41  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 231.685 292.131 219.029 1.00 38.24  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 228.837 295.294 215.725 1.00 40.14  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 227.646 296.127 215.831 1.00 39.76  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 226.610 295.764 214.776 1.00 52.46  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 225.405 295.868 215.032 1.00 53.95  ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 228.031 297.601 215.724 1.00 37.04  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 228.868 298.092 216.892 1.00 37.82  ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 229.385 299.806 216.715 1.00 56.27  ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 227.821 300.640 216.949 1.00 43.41  ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 227.054 295.347 213.588 1.00 52.76  ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 226.115 294.914 212.558 1.00 44.26  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 225.369 293.658 212.987 1.00 45.55  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 224.165 293.526 212.738 1.00 50.94  ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 226.852 294.678 211.240 1.00 42.08  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 227.280 295.931 210.473 1.00 44.93  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 228.080 295.554 209.238 1.00 45.58  ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 226.069 296.769 210.099 1.00 48.72  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 226.070 292.719 213.628 1.00 44.62  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 225.411 291.519 214.132 1.00 47.34  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 224.413 291.861 215.231 1.00 50.16  ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 223.327 291.273 215.300 1.00 58.69  ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 226.452 290.523 214.643 1.00 46.17  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 226.829 289.448 213.638 1.00 53.80  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 228.048 288.664 214.096 1.00 53.85  ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 227.731 287.745 215.183 1.00 66.19  ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 228.361 286.600 215.404 1.00 67.15  ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 229.354 286.197 214.628 1.00 62.82  ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 227.985 285.839 216.428 1.00 58.40  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 224.769 292.805 216.106 1.00 52.88  ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 223.862 293.204 217.178 1.00 46.72  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 222.603 293.859 216.623 1.00 49.35  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 221.487 293.529 217.040 1.00 54.37  ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 224.577 294.150 218.143 1.00 48.02  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 225.554 293.420 218.895 1.00 50.06  ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 223.585 294.795 219.100 1.00 47.87  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 222.760 294.783 215.672 1.00 50.64  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 221.602 295.486 215.129 1.00 47.57  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 220.714 294.562 214.306 1.00 53.90  ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 219.498 294.777 214.234 1.00 61.31  ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 222.059 296.676 214.286 1.00 45.45  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 222.281 297.930 215.082 1.00 52.51  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 221.218 298.582 215.684 1.00 53.08  ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 223.554 298.456 215.231 1.00 50.50  ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 221.420 299.735 216.418 1.00 50.22  ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 223.761 299.608 215.964 1.00 54.30  ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 222.693 300.248 216.558 1.00 54.99  ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 221.294 293.537 213.680 1.00 48.61  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 220.489 292.601 212.901 1.00 50.70  ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 219.694 291.667 213.804 1.00 49.61  ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 218.526 291.371 213.525 1.00 56.40  ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 221.384 291.801 211.955 1.00 54.59  ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 222.063 290.767 212.647 1.00 52.36  ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 220.311 291.188 214.888 1.00 50.34  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 219.626 290.259 215.783 1.00 51.49  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 218.442 290.920 216.478 1.00 51.78  ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 217.373 290.311 216.606 1.00 50.25  ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 220.610 289.703 216.812 1.00 51.54  ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 221.009 290.706 217.729 1.00 54.38  ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 218.610 292.154 216.933 1.00 54.85  ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 217.520 292.855 217.622 1.00 56.98  ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 216.438 293.218 216.610 1.00 58.45  ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 216.756 293.766 215.539 1.00 54.31  ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 218.052 294.101 218.333 1.00 53.85  ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 219.208 293.730 219.263 1.00 57.37  ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 216.942 294.785 219.116 1.00 49.68  ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 219.893 294.924 219.889 1.00 55.75  ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 215.167 292.930 216.888 1.00 63.73  ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 214.105 293.295 215.944 1.00 58.96  ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 214.010 294.803 215.763 1.00 61.00  ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 214.311 295.582 216.670 1.00 68.93  ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 212.837 292.730 216.597 1.00 58.05  ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 213.323 291.686 217.549 1.00 63.16  ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 214.650 292.172 218.040 1.00 64.85  ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 213.589 295.206 214.563 1.00 66.96  ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 213.469 296.628 214.249 1.00 69.61  ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 212.408 297.281 215.126 1.00 69.88  ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 212.555 298.433 215.553 1.00 69.59  ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 213.166 296.818 212.751 1.00 71.50  ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 213.009 298.294 212.416 1.00 70.62  ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 214.260 296.186 211.905 1.00 68.89  ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 211.323 296.556 215.410 1.00 70.52  ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 210.254 297.111 216.235 1.00 70.29  ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 210.736 297.397 217.652 1.00 72.11  ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 210.332 298.394 218.262 1.00 72.00  ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 209.061 296.156 216.259 1.00 73.62  ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 209.410 294.919 216.855 1.00 74.23  ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 211.597 296.532 218.194 1.00 71.09  ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 212.079 296.720 219.559 1.00 64.06  ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 212.863 298.019 219.700 1.00 67.18  ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 212.698 298.749 220.684 1.00 69.73  ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 212.940 295.530 219.979 1.00 60.64  ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 212.977 295.296 221.477 1.00 63.84  ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 213.496 293.909 221.805 1.00 64.01  ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 214.048 293.843 223.152 1.00 60.95  ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 214.880 292.901 223.576 1.00 63.98  ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 215.279 291.923 222.780 1.00 69.56  ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 215.321 292.942 224.829 1.00 62.97  ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 213.725 298.323 218.728 1.00 65.49  ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 214.511 299.550 218.792 1.00 63.99  ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 213.623 300.777 218.628 1.00 64.96  ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 213.881 301.823 219.235 1.00 69.89  ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 215.636 299.516 217.741 1.00 64.82  ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 216.357 298.167 217.782 1.00 66.71  ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 216.619 300.651 217.972 1.00 64.86  ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 217.605 298.108 216.929 1.00 69.97  ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 212.571 300.678 217.821 1.00 73.96  ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 211.681 301.801 217.530 1.00 78.47  ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 210.386 301.622 218.323 1.00 79.81  ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 209.424 301.019 217.846 1.00 78.71  ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 211.409 301.903 216.031 1.00 80.71  ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 212.897 301.958 215.006 1.00 90.56  ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 210.369 302.163 219.536 1.00 84.09  ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 209.194 302.188 220.399 1.00 82.08  ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 208.775 303.636 220.650 1.00 83.01  ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 209.286 304.571 220.027 1.00 85.59  ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 209.460 301.446 221.711 1.00 81.77  ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 209.777 299.970 221.559 1.00 82.98  ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 208.557 299.211 221.058 1.00 82.29  ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 208.822 297.717 220.973 1.00 85.73  ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 207.645 296.975 220.443 1.00 83.13  ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 207.823 303.809 221.567 1.00 87.90  ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 207.281 305.134 221.870 1.00 92.27  ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 208.343 306.157 222.258 1.00 91.52  ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 208.299 307.280 221.731 1.00 91.81  ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 206.209 305.004 222.962 1.00 94.48  ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 205.666 306.269 223.297 1.00 94.68  ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 209.302 305.866 223.143 1.00 83.38  ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 210.362 306.854 223.405 1.00 80.86  ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 211.342 306.896 222.242 1.00 80.71  ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 211.962 305.887 221.901 1.00 85.43  ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 211.027 306.334 224.688 1.00 77.52  ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 210.109 305.279 225.224 1.00 82.28  ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 209.437 304.699 224.031 1.00 79.90  ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 211.480 308.075 221.629 1.00 80.98  ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 212.406 308.231 220.513 1.00 83.61  ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 213.860 308.105 220.946 1.00 81.53  ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 214.735 307.926 220.092 1.00 77.79  ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 212.182 309.580 219.829 1.00 82.11  ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 210.836 309.665 219.137 1.00 82.34  ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 210.463 310.712 218.607 1.00 81.81  ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 210.099 308.561 219.137 1.00 80.18  ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 214.135 308.192 222.245 1.00 77.54  ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 215.488 308.063 222.769 1.00 74.78  ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 215.908 306.613 222.966 1.00 73.03  ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 217.051 306.365 223.361 1.00 78.44  ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 215.606 308.823 224.094 1.00 71.73  ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 215.636 310.341 223.952 1.00 74.34  ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 214.287 310.937 223.588 1.00 76.72  ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 213.284 310.193 223.569 1.00 78.58  ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 214.231 312.156 223.321 1.00 72.18  ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 215.012 305.659 222.707 1.00 64.42  ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 215.352 304.249 222.864 1.00 61.57  ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 216.396 303.816 221.843 1.00 62.47  ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 217.264 302.987 222.140 1.00 66.01  ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 214.090 303.394 222.741 1.00 60.38  ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 214.320 301.904 222.921 1.00 62.11  ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 213.002 301.152 222.964 1.00 61.73  ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 212.032 301.809 223.831 1.00 69.02  ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 211.462 301.241 224.885 1.00 66.24  ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 211.738 299.995 225.231 1.00 65.34  ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 210.592 301.940 225.608 1.00 62.83  ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 216.323 304.365 220.628 1.00 65.26  ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 217.242 303.960 219.567 1.00 61.33  ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 218.685 304.291 219.928 1.00 62.09  ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 219.594 303.486 219.697 1.00 68.92  ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 216.847 304.629 218.251 1.00 62.01  ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 218.915 305.478 220.493 1.00 57.52  ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 220.269 305.862 220.879 1.00 55.19  ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 220.773 305.009 222.037 1.00 59.97  ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 221.966 304.699 222.124 1.00 65.62  ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 220.312 307.346 221.240 1.00 54.78  ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 221.693 307.965 221.111 1.00 57.94  ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 221.656 309.461 221.358 1.00 60.81  ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 222.792 310.141 220.749 1.00 62.27  ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 222.691 311.077 219.815 1.00 63.56  ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 221.514 311.472 219.358 1.00 62.89  ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 223.798 311.629 219.328 1.00 60.70  ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 219.871 304.628 222.945 1.00 54.97  ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 220.252 303.761 224.055 1.00 48.69  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 220.724 302.403 223.551 1.00 45.05  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 221.700 301.841 224.060 1.00 50.68  ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 219.076 303.600 225.020 1.00 50.52  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 218.770 304.800 225.917 1.00 51.91  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 217.628 304.482 226.868 1.00 56.13  ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 220.010 305.219 226.687 1.00 53.50  ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 220.033 301.857 222.548 1.00 48.68  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 220.448 300.587 221.963 1.00 43.61  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 221.783 300.723 221.241 1.00 52.02  ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 222.612 299.806 221.262 1.00 56.21  ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 219.370 300.071 221.010 1.00 45.68  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 218.334 299.196 221.677 1.00 52.20  ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 217.333 299.748 222.464 1.00 49.49  ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 218.361 297.817 221.522 1.00 57.51  ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 216.386 298.950 223.075 1.00 47.16  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 217.419 297.013 222.130 1.00 52.77  ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 216.434 297.584 222.905 1.00 53.57  ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 215.494 296.783 223.510 1.00 59.36  ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 222.002 301.863 220.581 1.00 52.44  ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 223.266 302.090 219.889 1.00 44.04  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 224.431 302.117 220.871 1.00 50.06  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 225.487 301.527 220.620 1.00 53.43  ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 223.203 303.395 219.095 1.00 47.42  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 224.474 303.722 218.366 1.00 54.35  ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 224.732 303.177 217.120 1.00 53.27  ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 225.417 304.565 218.930 1.00 52.53  ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 225.899 303.475 216.448 1.00 55.99  ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 226.587 304.862 218.264 1.00 43.50  ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 226.829 304.316 217.022 1.00 49.98  ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 224.253 302.809 221.999 1.00 50.53  ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 225.290 302.841 223.025 1.00 42.84  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 225.536 301.447 223.585 1.00 47.85  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 226.681 301.057 223.843 1.00 57.74  ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 224.893 303.809 224.140 1.00 41.92  ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 225.056 305.299 223.838 1.00 47.31  ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 224.256 306.133 224.825 1.00 46.38  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 226.524 305.695 223.858 1.00 47.78  ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 224.461 300.684 223.787 1.00 43.97  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 224.593 299.304 224.239 1.00 39.63  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 225.332 298.460 223.208 1.00 38.25  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 226.169 297.620 223.558 1.00 44.11  ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 223.209 298.722 224.524 1.00 42.18  ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 223.152 297.415 225.312 1.00 51.24  ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 224.069 297.482 226.521 1.00 47.79  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 221.722 297.126 225.731 1.00 52.31  ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 225.022 298.664 221.926 1.00 40.82  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 225.711 297.935 220.867 1.00 38.87  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 227.189 298.302 220.817 1.00 41.22  ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 228.054 297.432 220.659 1.00 42.41  ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 225.041 298.211 219.520 1.00 38.88  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 227.496 299.595 220.942 1.00 44.31  ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 228.889 300.032 220.938 1.00 29.53  ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 229.633 299.503 222.157 1.00 35.37  ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 230.774 299.040 222.051 1.00 49.06  ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 228.959 301.559 220.880 1.00 28.67  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 230.345 302.107 221.049 1.00 36.95  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 230.922 302.534 222.208 1.00 41.79  ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 231.327 302.289 220.021 1.00 44.31  ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 232.202 302.969 221.968 1.00 35.88  ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 232.475 302.829 220.633 1.00 42.79  ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 231.347 302.048 218.644 1.00 38.39  ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 233.630 303.132 219.916 1.00 42.50  ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 232.495 302.349 217.934 1.00 37.17  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 233.620 302.885 218.571 1.00 41.71  ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 228.996 299.564 223.329 1.00 34.83  ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 229.630 299.078 224.551 1.00 25.45  ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 229.906 297.582 224.470 1.00 31.31  ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 230.973 297.111 224.878 1.00 46.37  ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 228.750 299.403 225.760 1.00 40.29  ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 229.183 298.724 227.028 1.00 41.07  ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 230.246 299.218 227.765 1.00 35.55  ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 228.520 297.599 227.490 1.00 29.98  ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 230.646 298.597 228.933 1.00 31.83  ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 228.915 296.975 228.657 1.00 34.54  ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 229.979 297.475 229.379 1.00 37.01  ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 228.946 296.818 223.947 1.00 30.27  ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 229.131 295.377 223.808 1.00 26.68  ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 230.254 295.059 222.829 1.00 40.48  ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 231.050 294.140 223.052 1.00 46.25  ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 227.822 294.726 223.360 1.00 34.59  ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 227.848 293.230 223.399 1.00 35.28  ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 227.927 292.517 224.576 1.00 43.10  ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 227.805 292.311 222.405 1.00 34.28  ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 227.931 291.224 224.305 1.00 45.86  ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 227.858 291.072 222.995 1.00 42.76  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 230.326 295.810 221.728 1.00 43.62  ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 231.364 295.576 220.729 1.00 28.89  ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 232.752 295.862 221.292 1.00 32.38  ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 233.711 295.136 221.011 1.00 38.83  ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 231.098 296.434 219.491 1.00 28.10  ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 232.876 296.929 222.086 1.00 35.17  ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 234.182 297.324 222.607 1.00 31.68  ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 234.726 296.260 223.553 1.00 39.94  ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 235.887 295.846 223.448 1.00 49.58  ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 234.091 298.697 223.299 1.00 33.41  ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 233.818 299.800 222.274 1.00 35.19  ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 235.366 298.992 224.073 1.00 45.74  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 234.750 299.784 221.087 1.00 44.13  ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 233.894 295.796 224.488 1.00 37.42  ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 234.365 294.840 225.488 1.00 37.14  ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 234.629 293.478 224.854 1.00 40.63  ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 235.546 292.756 225.265 1.00 44.36  ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 233.370 294.752 226.662 1.00 33.12  ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 232.083 294.036 226.248 1.00 34.68  ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 233.061 296.140 227.203 1.00 38.84  ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 231.131 293.802 227.390 1.00 40.71  ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 233.831 293.099 223.852 1.00 36.09  ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 234.052 291.823 223.180 1.00 33.64  ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 235.353 291.834 222.389 1.00 40.40  ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 236.078 290.833 222.356 1.00 47.72  ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 232.871 291.494 222.267 1.00 38.82  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 231.681 290.886 222.990 1.00 38.87  ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 230.785 290.088 222.065 1.00 45.57  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 230.245 290.618 221.095 1.00 46.45  ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 230.624 288.804 222.361 1.00 42.20  ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 235.665 292.958 221.739 1.00 44.54  ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 236.904 293.047 220.974 1.00 40.55  ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 238.125 293.090 221.883 1.00 43.65  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 239.199 292.618 221.496 1.00 54.42  ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 236.870 294.272 220.063 1.00 37.94  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 235.996 294.104 218.834 1.00 47.16  ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 236.310 292.835 218.068 1.00 62.92  ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 237.439 292.719 217.547 1.00 58.36  ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 235.428 291.954 217.986 1.00 60.54  ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 237.985 293.652 223.086 1.00 35.28  ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 239.076 293.649 224.053 1.00 34.53  ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 239.454 292.247 224.508 1.00 39.32  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 240.562 292.059 225.021 1.00 48.97  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 238.704 294.500 225.269 1.00 40.74  ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 238.679 295.995 225.000 1.00 36.19  ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 238.535 296.784 226.291 1.00 38.43  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 239.707 296.656 227.148 1.00 37.54  ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 240.575 297.630 227.379 1.00 37.89  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 240.437 298.825 226.828 1.00 39.23  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 241.609 297.401 228.184 1.00 41.70  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 238.566 291.265 224.338 1.00 40.49  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 238.877 289.889 224.701 1.00 33.79  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 239.937 289.270 223.800 1.00 46.21  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 240.581 288.296 224.205 1.00 53.97  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 237.607 289.037 224.661 1.00 37.95  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 236.637 289.214 225.830 1.00 42.27  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 235.332 288.485 225.558 1.00 35.15  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 237.264 288.727 227.125 1.00 47.42  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 240.130 289.806 222.593 1.00 52.70  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 241.168 289.296 221.705 1.00 53.36  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 242.566 289.546 222.253 1.00 52.95  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 243.505 288.843 221.868 1.00 61.40  ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 241.032 289.926 220.319 1.00 52.53  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 239.695 289.662 219.651 1.00 56.56  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 239.672 290.201 218.230 1.00 58.32  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 238.396 289.948 217.571 1.00 58.75  ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 238.013 288.767 217.106 1.00 59.12  ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 238.791 287.700 217.200 1.00 54.95  ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 236.821 288.653 216.529 1.00 60.36  ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 242.720 290.527 223.135 1.00 46.61  ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 243.985 290.826 223.800 1.00 53.46  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 243.815 290.400 225.256 1.00 54.46  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 243.417 291.193 226.110 1.00 55.33  ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 244.334 292.304 223.661 1.00 46.53  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 244.003 292.865 222.295 1.00 50.42  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 244.882 292.720 221.230 1.00 52.30  ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 242.804 293.530 222.068 1.00 49.17  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 244.580 293.226 219.980 1.00 54.73  ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 242.494 294.038 220.821 1.00 45.62  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 243.385 293.884 219.782 1.00 53.17  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 243.080 294.390 218.539 1.00 49.35  ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 244.117 289.130 225.525 1.00 57.56  ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 243.789 288.536 226.820 1.00 56.26  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 244.458 289.227 228.002 1.00 66.64  ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 243.763 289.503 228.994 1.00 71.35  ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 244.119 287.039 226.793 1.00 58.54  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 245.772 289.528 227.991 1.00 65.04  ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 246.375 290.133 229.188 1.00 58.46  ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 246.053 291.611 229.347 1.00 58.08  ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 245.920 292.100 230.472 1.00 65.94  ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 247.882 289.913 228.978 1.00 62.51  ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 248.001 288.966 227.820 1.00 64.05  ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 246.798 289.219 226.982 1.00 61.86  ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 245.927 292.335 228.235 1.00 43.62  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 245.737 293.780 228.297 1.00 51.27  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 244.264 294.175 228.274 1.00 52.09  ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 243.842 295.041 229.047 1.00 53.24  ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 246.483 294.465 227.146 1.00 55.56  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 248.001 294.636 227.271 1.00 49.78  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 248.743 293.313 227.127 1.00 53.02  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 248.507 295.650 226.256 1.00 47.36  ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 243.474 293.561 227.391 1.00 46.67  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 242.061 293.898 227.321 1.00 40.09  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 241.322 293.595 228.610 1.00 43.86  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 240.502 294.392 229.070 1.00 55.83  ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 241.601 292.442 229.207 1.00 37.55  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 241.015 292.057 230.486 1.00 46.33  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 242.086 291.300 231.263 1.00 51.27  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 243.274 291.342 230.927 1.00 55.28  ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 239.729 291.244 230.272 1.00 44.59  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 238.641 292.011 229.581 1.00 45.38  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 238.285 291.925 228.267 1.00 52.42  ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 237.776 292.992 230.167 1.00 43.77  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 237.249 292.786 227.999 1.00 42.86  ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 236.918 293.453 229.149 1.00 42.02  ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 237.642 293.523 231.453 1.00 51.05  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 235.941 294.418 229.377 1.00 44.84  ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 236.670 294.481 231.677 1.00 49.47  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 235.834 294.919 230.644 1.00 46.81  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 241.682 290.613 232.331 1.00 48.52  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 242.590 289.726 233.043 1.00 49.15  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 242.377 288.259 232.700 1.00 53.86  ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 243.264 287.441 232.966 1.00 62.13  ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 242.449 289.914 234.559 1.00 49.67  ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 242.974 291.164 234.968 1.00 52.76  ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 241.232 287.914 232.118 1.00 46.68  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 240.946 286.546 231.712 1.00 51.06  ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 239.889 286.586 230.618 1.00 54.63  ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 239.227 287.603 230.402 1.00 59.95  ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 240.489 285.691 232.898 1.00 53.93  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 239.275 286.238 233.626 1.00 51.49  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 238.915 285.371 234.821 1.00 57.98  ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 239.926 285.534 235.944 1.00 55.76  ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 239.899 286.907 236.519 1.00 52.48  ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 239.741 285.459 229.925 1.00 54.54  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 238.802 285.350 228.810 1.00 52.42  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 237.390 285.248 229.372 1.00 52.64  ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 236.858 284.158 229.590 1.00 58.55  ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 239.144 284.151 227.934 1.00 55.70  ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 240.521 284.224 227.295 1.00 57.95  ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 240.636 285.424 226.369 1.00 58.85  ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 239.731 285.276 225.157 1.00 57.55  ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 240.138 284.132 224.296 1.00 61.11  ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 236.775 286.403 229.610 1.00 43.06  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 235.404 286.435 230.096 1.00 45.56  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 234.434 286.008 229.001 1.00 50.59  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 234.722 286.110 227.806 1.00 52.10  ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 235.041 287.833 230.593 1.00 45.98  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 235.772 288.246 231.847 1.00 40.38  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 235.550 287.591 233.050 1.00 41.97  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 236.682 289.293 231.828 1.00 44.26  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 236.214 287.966 234.200 1.00 45.15  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 237.350 289.675 232.972 1.00 48.20  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 237.113 289.009 234.155 1.00 48.46  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 237.779 289.386 235.298 1.00 49.39  ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 233.274 285.518 229.425 1.00 53.55  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 232.260 285.013 228.502 1.00 51.92  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 231.221 286.079 228.161 1.00 53.18  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 230.019 285.873 228.321 1.00 54.31  ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 231.600 283.774 229.093 1.00 54.78  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 232.561 282.619 229.331 1.00 51.92  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 233.178 282.101 228.050 1.00 59.32  ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 232.512 282.175 226.999 1.00 63.78  ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 234.330 281.619 228.093 1.00 61.76  ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 231.680 287.232 227.682 1.00 47.37  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 230.779 288.313 227.286 1.00 46.29  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 230.119 287.941 225.964 1.00 49.91  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 230.699 288.125 224.892 1.00 54.28  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 231.538 289.630 227.171 1.00 41.97  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 232.067 290.142 228.480 1.00 45.93  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 231.245 290.222 229.591 1.00 49.97  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 233.384 290.555 228.597 1.00 43.66  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 231.728 290.696 230.796 1.00 48.01  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 233.871 291.032 229.798 1.00 44.01  ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 233.043 291.101 230.899 1.00 42.73  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 228.899 287.415 226.036 1.00 46.11  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 228.210 286.956 224.846 1.00 48.98  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 226.830 287.547 224.648 1.00 49.74  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 226.517 288.617 225.178 1.00 49.01  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 225.993 286.847 223.877 1.00 53.20  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 224.659 287.349 223.565 1.00 50.46  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 223.768 287.418 224.800 1.00 56.47  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 222.945 288.333 224.912 1.00 66.48  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 224.008 286.477 222.491 1.00 54.83  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 224.697 286.546 221.138 1.00 62.49  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 224.577 287.912 220.490 1.00 71.05  ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 223.551 288.590 220.711 1.00 70.96  ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 225.509 288.309 219.759 1.00 68.85  ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 223.902 286.457 225.719 1.00 46.82  ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 223.058 286.442 226.911 1.00 43.99  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 223.208 287.731 227.710 1.00 47.93  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 222.233 288.248 228.268 1.00 57.13  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 223.395 285.228 227.777 1.00 48.84  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 224.771 285.208 228.113 1.00 51.32  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 224.430 288.262 227.781 1.00 52.81  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 224.641 289.550 228.435 1.00 41.46  ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 223.941 290.670 227.676 1.00 37.61  ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 223.351 291.572 228.280 1.00 40.33  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 226.138 289.835 228.559 1.00 45.10  ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 226.825 288.922 229.553 1.00 50.47  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 226.165 288.493 230.523 1.00 50.76  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 228.026 288.635 229.367 1.00 51.55  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 224.003 290.631 226.343 1.00 44.98  ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 223.379 291.678 225.539 1.00 36.93  ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 221.862 291.659 225.685 1.00 46.73  ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 221.228 292.711 225.825 1.00 58.08  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 223.780 291.521 224.072 1.00 40.70  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 223.261 292.595 223.116 1.00 43.40  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 223.981 293.914 223.344 1.00 42.95  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 223.407 292.140 221.674 1.00 47.45  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 221.261 290.468 225.650 1.00 49.72  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 219.809 290.368 225.771 1.00 44.53  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 219.334 290.857 227.133 1.00 45.55  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 218.315 291.549 227.237 1.00 53.42  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 219.356 288.930 225.524 1.00 49.77  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 219.642 288.423 224.123 1.00 54.87  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 218.791 289.159 223.100 1.00 59.11  ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 217.365 288.972 223.340 1.00 61.77  ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 216.653 287.953 222.880 1.00 64.60  ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 217.204 287.001 222.144 1.00 56.39  ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 215.356 287.886 223.166 1.00 61.92  ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 220.059 290.497 228.195 1.00 38.39  ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 219.706 290.978 229.526 1.00 32.68  ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 219.831 292.493 229.614 1.00 39.44  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 218.990 293.160 230.228 1.00 44.55  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 220.585 290.304 230.578 1.00 39.84  ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 220.494 288.893 230.492 1.00 46.81  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 220.881 293.054 229.009 1.00 43.67  ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 221.057 294.502 229.020 1.00 35.56  ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 219.962 295.201 228.225 1.00 39.18  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 219.482 296.269 228.623 1.00 48.28  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 222.437 294.864 228.474 1.00 32.38  ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 219.560 294.621 227.091 1.00 43.50  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 218.476 295.204 226.306 1.00 37.43  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 217.161 295.178 227.074 1.00 40.68  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 216.386 296.141 227.025 1.00 48.63  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 218.335 294.471 224.972 1.00 44.08  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 219.739 294.669 223.850 1.00 49.26  ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 216.885 294.080 227.782 1.00 43.66  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 215.687 294.012 228.612 1.00 38.96  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 215.741 295.043 229.733 1.00 47.05  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 214.729 295.670 230.067 1.00 52.03  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 215.518 292.603 229.182 1.00 42.54  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 215.360 291.553 228.102 1.00 55.08  ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 215.355 291.920 226.909 1.00 56.33  ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 215.243 290.358 228.446 1.00 55.59  ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 216.919 295.222 230.335 1.00 46.91  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 217.076 296.218 231.390 1.00 43.60  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 216.815 297.622 230.858 1.00 43.75  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 216.146 298.433 231.510 1.00 58.85  ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 218.477 296.119 231.996 1.00 43.34  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 218.577 294.922 232.777 1.00 47.73  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 218.771 297.322 232.879 1.00 42.35  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 217.334 297.926 229.667 1.00 44.26  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 217.095 299.233 229.059 1.00 43.36  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 215.610 299.420 228.776 1.00 45.64  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 215.033 300.477 229.057 1.00 53.98  ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 217.941 299.392 227.782 1.00 43.07  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 217.389 300.507 226.907 1.00 43.50  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 219.394 299.659 228.139 1.00 43.01  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 214.967 298.389 228.222 1.00 48.38  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 213.544 298.478 227.907 1.00 45.61  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 212.708 298.660 229.168 1.00 50.45  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 211.774 299.469 229.196 1.00 59.60  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 213.099 297.229 227.146 1.00 48.35  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 213.389 297.316 225.662 1.00 57.86  ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 214.076 298.271 225.244 1.00 64.67  ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 212.931 296.427 224.914 1.00 56.87  ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 213.029 297.910 230.223 1.00 53.64  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 212.221 297.948 231.438 1.00 49.98  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 212.302 299.310 232.118 1.00 51.75  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 211.277 299.892 232.494 1.00 58.47  ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 212.666 296.842 232.397 1.00 49.73  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 212.314 295.565 231.851 1.00 52.72  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 212.000 297.008 233.753 1.00 51.28  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 213.516 299.839 232.280 1.00 45.29  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 213.681 301.081 233.028 1.00 50.01  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 213.270 302.300 232.214 1.00 53.23  ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 212.788 303.286 232.783 1.00 62.35  ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 215.125 301.212 233.509 1.00 46.81  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 215.425 300.310 234.661 1.00 51.39  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 216.056 299.102 234.613 1.00 50.59  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 215.088 300.533 236.035 1.00 50.81  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 216.139 298.563 235.873 1.00 53.30  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 215.553 299.422 236.764 1.00 49.06  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 214.442 301.567 236.719 1.00 48.22  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 215.393 299.315 238.143 1.00 52.63  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 214.284 301.459 238.088 1.00 51.23  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 214.758 300.342 238.786 1.00 54.05  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 213.454 302.262 230.892 1.00 53.45  ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 213.025 303.386 230.065 1.00 55.64  ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 211.506 303.495 230.032 1.00 57.63  ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 210.958 304.604 230.017 1.00 61.43  ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 213.589 303.247 228.652 1.00 56.18  ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 213.380 304.442 227.722 1.00 58.45  ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 214.097 305.669 228.262 1.00 60.37  ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 213.859 304.114 226.320 1.00 60.20  ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 210.810 302.356 230.015 1.00 65.35  ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 209.351 302.379 230.063 1.00 63.25  ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 208.852 302.933 231.391 1.00 65.11  ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 207.829 303.626 231.438 1.00 64.45  ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 208.794 300.976 229.823 1.00 62.02  ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 209.042 300.484 228.412 1.00 68.24  ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 209.584 301.260 227.598 1.00 69.19  ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 208.698 299.320 228.117 1.00 67.09  ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 209.556 302.628 232.483 1.00 68.35  ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 209.153 303.128 233.794 1.00 66.72  ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 209.219 304.649 233.845 1.00 66.60  ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 208.335 305.303 234.410 1.00 66.07  ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 210.033 302.513 234.882 1.00 63.34  ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 209.782 301.029 235.065 1.00 71.53  ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 208.645 300.581 234.810 1.00 73.37  ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 210.723 300.311 235.464 1.00 70.28  ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 210.268 305.232 233.262 1.00 66.97  ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 210.397 306.686 233.261 1.00 68.97  ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 209.553 307.311 232.157 1.00 71.44  ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 208.767 308.232 232.408 1.00 70.33  ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 211.865 307.085 233.108 1.00 68.95  ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 212.671 306.296 233.991 1.00 66.79  ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 212.049 308.556 233.440 1.00 68.42  ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 209.703 306.823 230.925 1.00 74.49  ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 208.936 307.331 229.788 1.00 74.46  ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 207.661 306.504 229.657 1.00 78.33  ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 207.559 305.569 228.860 1.00 78.10  ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 209.771 307.295 228.515 1.00 75.87  ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 206.666 306.866 230.468 1.00 79.84  ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 205.382 306.165 230.493 1.00 79.32  ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 204.526 306.671 229.336 1.00 81.45  ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 203.605 307.476 229.498 1.00 80.78  ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 204.690 306.362 231.835 1.00 79.38  ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 205.440 305.767 233.013 1.00 82.16  ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 204.664 305.940 234.306 1.00 82.80  ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 204.641 307.395 234.743 1.00 81.49  ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 205.999 307.884 235.112 1.00 77.31  ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 204.845 306.182 228.139 1.00 90.98  ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 204.129 306.561 226.941 1.00 91.72  ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 204.562 307.866 226.315 1.00 92.82  ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 203.996 308.256 225.286 1.00 93.56  ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 205.540 308.557 226.895 1.00 88.11  ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 206.005 309.818 226.333 1.00 86.01  ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 206.731 309.572 225.018 1.00 88.25  ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 207.594 308.692 224.929 1.00 86.23  ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 206.923 310.527 227.327 1.00 85.81  ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 206.293 310.776 228.688 1.00 85.85  ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 207.348 310.853 229.780 1.00 88.65  ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 208.384 311.833 229.476 1.00 93.07  ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 209.422 312.093 230.258 1.00 91.80  ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 209.598 311.461 231.407 1.00 87.39  ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 210.307 313.011 229.878 1.00 90.14  ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 206.375 310.349 223.993 1.00 89.49  ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 207.039 310.217 222.701 1.00 86.25  ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 208.509 310.606 222.786 1.00 84.33  ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 209.353 309.984 222.132 1.00 86.25  ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 206.322 311.067 221.652 1.00 86.28  ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 206.849 310.890 220.238 1.00 87.83  ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 206.582 309.503 219.687 1.00 89.93  ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 207.432 308.913 219.019 1.00 90.94  ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 205.397 308.973 219.966 1.00 87.68  ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 208.833 311.623 223.581 1.00 81.89  ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 210.205 312.061 223.785 1.00 83.24  ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 210.486 312.168 225.275 1.00 81.36  ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 209.656 312.669 226.039 1.00 83.95  ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 210.470 313.411 223.107 1.00 84.13  ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 210.607 313.291 221.603 1.00 86.03  ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 209.691 313.633 220.855 1.00 85.46  ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 211.757 312.805 221.151 1.00 86.42  ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 211.660 311.694 225.683 1.00 75.81  ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 212.109 311.764 227.068 1.00 77.97  ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 213.396 312.577 227.099 1.00 78.81  ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 214.287 312.373 226.264 1.00 82.29  ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 212.312 310.366 227.680 1.00 78.24  ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 212.840 310.475 229.112 1.00 74.75  ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 213.229 309.512 226.813 1.00 79.74  ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 212.896 309.152 229.842 1.00 76.59  ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 213.479 313.514 228.034 1.00 73.85  ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 214.664 314.349 228.142 1.00 71.63  ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 215.875 313.487 228.493 1.00 76.85  ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 215.750 312.532 229.271 1.00 80.65  ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 214.457 315.433 229.203 1.00 75.31  ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 215.652 316.157 229.433 1.00 75.40  ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 217.052 313.778 227.932 1.00 76.38  ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 218.240 312.975 228.267 1.00 74.40  ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 218.578 312.987 229.746 1.00 73.14  ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 219.089 311.986 230.264 1.00 75.68  ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 219.349 313.625 227.427 1.00 74.98  ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 218.631 314.321 226.317 1.00 74.08  ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 217.338 314.795 226.907 1.00 76.52  ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 218.311 314.092 230.445 1.00 73.66  ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 218.564 314.147 231.879 1.00 77.58  ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 217.598 313.276 232.672 1.00 78.46  ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 217.937 312.850 233.781 1.00 78.87  ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 218.482 315.593 232.372 1.00 76.49  ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 219.622 316.448 231.858 1.00 82.41  ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 220.718 315.899 231.616 1.00 85.75  ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 219.423 317.670 231.695 1.00 82.74  ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 216.409 313.005 232.133 1.00 69.25  ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 215.423 312.190 232.830 1.00 67.40  ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 215.637 310.695 232.636 1.00 69.98  ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 215.002 309.902 233.338 1.00 72.33  ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 214.012 312.566 232.369 1.00 69.64  ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 213.620 314.002 232.672 1.00 68.02  ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 212.995 314.124 234.052 1.00 70.41  ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 212.950 315.572 234.511 1.00 71.91  ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 214.288 316.058 234.949 1.00 69.80  ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 216.501 310.295 231.712 1.00 57.62  ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 216.763 308.869 231.491 1.00 56.41  ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 217.466 308.293 232.716 1.00 66.06  ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 218.426 308.904 233.219 1.00 65.26  ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 217.605 308.673 230.228 1.00 58.26  ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 216.853 309.197 229.003 1.00 62.61  ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 217.969 307.208 230.041 1.00 57.73  ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 217.609 309.031 227.704 1.00 59.82  ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 217.035 307.139 233.235 1.00 61.49  ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 217.692 306.576 234.423 1.00 54.88  ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 219.072 306.019 234.112 1.00 52.87  ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 219.244 304.806 233.956 1.00 60.73  ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 216.725 305.472 234.866 1.00 56.83  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 216.013 305.079 233.617 1.00 54.55  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 215.872 306.340 232.813 1.00 56.34  ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 220.063 306.908 234.017 1.00 47.35  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 221.425 306.478 233.718 1.00 45.19  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 222.006 305.642 234.851 1.00 49.84  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 222.725 304.667 234.603 1.00 50.85  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 222.306 307.695 233.442 1.00 47.79  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 221.886 308.471 232.236 1.00 53.61  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 221.320 309.712 232.216 1.00 52.52  ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 221.996 308.058 230.869 1.00 53.92  ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 221.071 310.098 230.922 1.00 60.39  ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 221.478 309.100 230.076 1.00 55.43  ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 222.483 306.909 230.240 1.00 48.69  ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 221.432 309.027 228.686 1.00 53.97  ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 222.438 306.839 228.861 1.00 50.45  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 221.917 307.891 228.099 1.00 54.16  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 221.715 306.014 236.100 1.00 52.48  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 222.253 305.277 237.239 1.00 44.76  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 221.739 303.842 237.266 1.00 45.86  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 222.496 302.911 237.565 1.00 46.33  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 221.903 305.997 238.540 1.00 45.76  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 220.501 306.037 238.739 1.00 54.57  ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 220.454 303.646 236.966 1.00 41.68  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 219.888 302.300 236.964 1.00 34.65  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 220.546 301.428 235.902 1.00 42.11  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 220.859 300.258 236.149 1.00 46.83  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 218.377 302.368 236.749 1.00 35.04  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 220.757 301.981 234.706 1.00 46.79  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 221.395 301.219 233.637 1.00 44.91  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 222.852 300.921 233.968 1.00 44.19  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 223.339 299.807 233.739 1.00 48.71  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 221.286 301.979 232.315 1.00 42.38  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 219.874 302.318 231.834 1.00 40.13  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 219.919 302.966 230.460 1.00 42.72  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 219.000 301.075 231.815 1.00 43.60  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 223.568 301.911 234.504 1.00 39.17  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 224.987 301.730 234.794 1.00 37.01  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 225.199 300.730 235.924 1.00 44.48  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 226.038 299.828 235.820 1.00 48.06  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 225.626 303.075 235.141 1.00 37.28  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 226.082 303.878 233.937 1.00 37.49  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 226.783 305.155 234.366 1.00 41.25  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 225.812 306.128 235.012 1.00 37.61  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 226.441 307.453 235.265 1.00 42.52  ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 224.448 300.878 237.018 1.00 37.23  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 224.652 300.013 238.177 1.00 32.92  ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 224.284 298.567 237.869 1.00 36.17  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 225.007 297.643 238.259 1.00 47.53  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 223.843 300.527 239.367 1.00 39.20  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 224.036 301.940 239.504 1.00 47.41  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 224.283 299.834 240.648 1.00 36.03  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 223.165 298.348 237.176 1.00 33.97  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 222.755 296.984 236.857 1.00 31.78  ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 223.750 296.310 235.920 1.00 41.77  ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 224.060 295.125 236.085 1.00 50.28  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 221.354 296.984 236.247 1.00 31.17  ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 220.202 297.152 237.238 1.00 32.89  ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 218.872 296.913 236.553 1.00 38.53  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 220.370 296.216 238.425 1.00 42.01  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 224.261 297.047 234.931 1.00 37.94  ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 225.262 296.480 234.035 1.00 35.33  ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 226.587 296.244 234.749 1.00 38.52  ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 227.283 295.266 234.453 1.00 40.51  ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 225.464 297.395 232.827 1.00 36.04  ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 224.580 297.053 231.639 1.00 32.99  ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 224.526 298.367 230.406 1.00 61.33  ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 222.758 298.617 230.259 1.00 46.90  ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 226.952 297.121 235.686 1.00 38.43  ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 228.214 296.974 236.401 1.00 37.34  ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 228.168 295.864 237.442 1.00 43.97  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 229.209 295.280 237.761 1.00 50.79  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 228.599 298.292 237.073 1.00 33.02  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 226.991 295.566 237.987 1.00 36.18  ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 226.857 294.611 239.081 1.00 34.53  ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 226.183 293.308 238.683 1.00 47.02  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 226.569 292.248 239.180 1.00 49.58  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 226.074 295.244 240.237 1.00 36.95  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 226.669 296.541 240.761 1.00 38.48  ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 227.871 296.314 241.655 1.00 47.65  ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 227.739 295.842 242.784 1.00 50.61  ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 229.053 296.654 241.155 1.00 45.96  ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 225.186 293.351 237.801 1.00 40.44  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 224.367 292.184 237.497 1.00 33.10  ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 224.578 291.643 236.091 1.00 36.96  ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 224.853 290.451 235.924 1.00 38.77  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 222.883 292.524 237.699 1.00 32.27  ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 222.611 292.836 239.054 1.00 42.97  ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 224.455 292.488 235.069 1.00 40.39  ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 224.436 291.999 233.693 1.00 36.13  ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 225.839 291.630 233.227 1.00 39.31  ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 226.119 290.471 232.900 1.00 44.66  ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 223.794 293.043 232.763 1.00 31.74  ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 222.392 293.402 233.255 1.00 30.79  ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 223.742 292.523 231.339 1.00 36.49  ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 221.848 294.676 232.657 1.00 42.30  ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 226.741 292.609 233.190 1.00 39.54  ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 228.101 292.378 232.720 1.00 40.36  ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 229.099 292.166 233.846 1.00 40.09  ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 230.097 291.465 233.650 1.00 47.11  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 228.568 293.550 231.850 1.00 34.54  ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 227.912 293.604 230.490 1.00 36.00  ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 228.403 292.853 229.430 1.00 34.29  ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 226.802 294.407 230.264 1.00 40.66  ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 227.808 292.901 228.185 1.00 32.46  ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 226.200 294.460 229.021 1.00 44.36  ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 226.707 293.705 227.986 1.00 43.66  ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 226.111 293.756 226.747 1.00 48.53  ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 228.858 292.753 235.018 1.00 37.12  ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 229.764 292.591 236.138 1.00 36.71  ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 229.618 291.299 236.906 1.00 44.94  ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 230.416 291.042 237.813 1.00 55.49  ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 228.617 290.482 236.574 1.00 38.80  ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 228.465 289.206 237.253 1.00 38.13  ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 229.618 288.260 236.979 1.00 41.29  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 230.100 287.575 237.885 1.00 55.23  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 230.079 288.211 235.727 1.00 38.34  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 231.194 287.341 235.375 1.00 42.76  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 232.528 287.869 235.882 1.00 48.16  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 233.482 287.092 236.000 1.00 56.93  ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 231.259 287.159 233.858 1.00 49.86  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 229.907 286.973 233.195 1.00 51.19  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 230.039 286.960 231.682 1.00 46.48  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 228.805 286.544 231.027 1.00 45.98  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 228.401 285.286 230.916 1.00 49.54  ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 229.112 284.285 231.409 1.00 48.33  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 227.256 285.025 230.293 1.00 49.72  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 232.619 289.162 236.184 1.00 39.84  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 233.891 289.762 236.572 1.00 38.95  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 234.226 289.350 238.000 1.00 43.74  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 233.447 289.587 238.930 1.00 45.84  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 233.842 291.288 236.427 1.00 38.06  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 235.057 291.921 237.080 1.00 44.61  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 233.762 291.678 234.958 1.00 35.01  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 235.396 288.732 238.177 1.00 47.29  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 235.872 288.301 239.487 1.00 46.18  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 237.131 289.045 239.921 1.00 47.84  ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 237.810 288.615 240.860 1.00 57.02  ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 236.102 286.785 239.497 1.00 54.99  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 237.194 286.335 238.532 1.00 55.24  ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 238.021 287.160 238.091 1.00 58.44  ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 237.214 285.132 238.198 1.00 56.49  ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 237.456 290.150 239.258 1.00 51.53  ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 238.672 290.903 239.520 1.00 49.46  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 238.320 292.350 239.836 1.00 52.64  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 237.419 292.927 239.220 1.00 62.86  ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 239.622 290.838 238.320 1.00 47.15  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 240.996 291.388 238.633 1.00 55.78  ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 241.177 292.595 238.773 1.00 62.58  ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 241.977 290.500 238.745 1.00 58.11  ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 239.034 292.932 240.802 1.00 48.16  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 238.745 294.305 241.204 1.00 49.68  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 239.207 295.303 240.149 1.00 52.49  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 238.672 296.414 240.062 1.00 52.21  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 239.395 294.605 242.556 1.00 51.68  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 240.836 295.084 242.472 1.00 55.39  ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 241.563 294.983 243.798 1.00 63.88  ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 241.870 293.850 244.224 1.00 60.26  ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 241.829 296.037 244.413 1.00 61.66  ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 240.199 294.928 239.339 1.00 53.30  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 240.672 295.820 238.286 1.00 48.65  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 239.847 295.665 237.015 1.00 55.35  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 239.655 296.635 236.274 1.00 60.04  ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 242.153 295.563 238.012 1.00 43.59  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 243.008 295.606 239.246 1.00 54.64  ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 243.396 296.816 239.794 1.00 55.72  ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 243.408 294.436 239.869 1.00 51.77  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 244.176 296.860 240.933 1.00 50.56  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 244.186 294.473 241.009 1.00 52.46  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 244.570 295.687 241.542 1.00 52.62  ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 239.358 294.452 236.744 1.00 53.36  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 238.424 294.264 235.639 1.00 42.89  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 237.108 294.979 235.911 1.00 46.83  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 236.521 295.583 235.005 1.00 56.39  ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 238.188 292.774 235.401 1.00 46.52  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 239.363 292.100 234.732 1.00 52.96  ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 240.174 292.804 234.095 1.00 50.97  ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 239.479 290.863 234.849 1.00 59.94  ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 236.625 294.914 237.154 1.00 42.54  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 235.436 295.673 237.526 1.00 38.85  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 235.688 297.169 237.406 1.00 36.99  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 234.814 297.921 236.960 1.00 49.16  ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 235.005 295.311 238.947 1.00 38.76  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 233.696 295.948 239.381 1.00 42.01  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 232.514 295.460 238.569 1.00 43.28  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 232.311 294.257 238.407 1.00 45.61  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 231.724 296.395 238.053 1.00 42.44  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 236.881 297.619 237.801 1.00 47.52  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 237.245 299.019 237.621 1.00 46.96  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 237.280 299.389 236.143 1.00 46.33  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 236.845 300.480 235.756 1.00 49.25  ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 238.596 299.291 238.281 1.00 48.06  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 239.183 300.658 237.985 1.00 51.90  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 240.509 300.845 238.702 1.00 51.01  ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 241.608 300.204 237.990 1.00 56.68  ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 242.794 299.939 238.522 1.00 56.59  ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 243.071 300.244 239.779 1.00 53.80  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 243.725 299.355 237.773 1.00 53.18  ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 237.797 298.490 235.302 1.00 45.85  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 237.800 298.736 233.864 1.00 38.92  ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 236.390 298.676 233.291 1.00 45.95  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 236.031 299.481 232.423 1.00 53.83  ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 238.708 297.726 233.164 1.00 39.60  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 238.764 297.806 231.638 1.00 41.39  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 239.131 299.210 231.189 1.00 47.64  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 239.748 296.791 231.089 1.00 41.94  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 235.578 297.725 233.760 1.00 46.43  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 234.206 297.619 233.274 1.00 36.72  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 233.400 298.864 233.613 1.00 38.32  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 232.598 299.335 232.797 1.00 44.63  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 233.534 296.376 233.855 1.00 39.20  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 232.239 295.944 233.164 1.00 40.59  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 232.523 295.197 231.872 1.00 49.46  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 231.404 295.096 234.103 1.00 42.14  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 233.589 299.405 234.818 1.00 42.22  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 232.906 300.641 235.182 1.00 38.31  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 233.328 301.791 234.276 1.00 50.34  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 232.478 302.532 233.773 1.00 62.95  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 233.179 300.982 236.647 1.00 35.33  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 232.663 299.922 237.599 1.00 48.23  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 232.054 298.938 237.181 1.00 50.49  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 232.912 300.114 238.889 1.00 51.67  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 234.633 301.922 234.019 1.00 48.02  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 235.153 303.085 233.301 1.00 46.66  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 234.430 303.299 231.976 1.00 49.32  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 234.191 304.439 231.562 1.00 55.49  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 236.657 302.923 233.069 1.00 47.61  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 237.312 302.677 234.320 1.00 56.65  ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 237.241 304.173 232.431 1.00 49.52  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 234.063 302.210 231.300 1.00 41.90  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 233.305 302.334 230.059 1.00 37.68  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 231.876 302.789 230.331 1.00 45.39  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 231.233 303.403 229.472 1.00 59.29  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 233.309 301.003 229.308 1.00 47.67  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 234.668 300.576 228.834 1.00 47.81  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 235.416 301.391 228.001 1.00 51.29  ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 235.194 299.354 229.216 1.00 48.11  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 236.665 300.995 227.563 1.00 49.33  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 236.441 298.954 228.781 1.00 45.68  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 237.178 299.775 227.954 1.00 45.81  ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 231.358 302.493 231.525 1.00 43.78  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 229.937 302.708 231.789 1.00 43.77  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 229.634 304.170 232.105 1.00 45.87  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 228.695 304.749 231.548 1.00 52.76  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 229.475 301.794 232.923 1.00 44.70  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 229.281 300.336 232.499 1.00 42.67  ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 229.123 299.436 233.708 1.00 41.21  ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 228.090 300.198 231.562 1.00 42.16  ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 230.413 304.789 232.998 1.00 41.40  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 230.177 306.201 233.292 1.00 47.68  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 230.690 307.120 232.191 1.00 54.34  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 230.594 308.344 232.330 1.00 57.16  ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 230.791 306.617 234.637 1.00 52.14  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 230.144 305.996 235.879 1.00 61.36  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 230.650 304.610 236.200 1.00 67.67  ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 231.559 304.142 235.498 1.00 65.27  ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 230.135 303.989 237.153 1.00 59.83  ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 231.248 306.569 231.114 1.00 51.34  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 231.602 307.378 229.954 1.00 50.62  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 230.550 307.288 228.853 1.00 50.31  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 230.086 308.316 228.349 1.00 55.27  ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 232.974 306.961 229.417 1.00 48.63  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 233.661 308.042 228.596 1.00 53.12  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 235.134 307.731 228.378 1.00 58.91  ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 235.369 306.349 227.977 1.00 57.24  ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 235.016 305.830 226.808 1.00 57.48  ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 234.435 306.562 225.872 1.00 53.65  ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 235.262 304.545 226.569 1.00 51.49  ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 230.168 306.069 228.466 1.00 44.78  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 229.197 305.904 227.389 1.00 51.35  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 227.781 306.229 227.850 1.00 49.86  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 227.020 306.877 227.123 1.00 52.85  ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 229.266 304.480 226.839 1.00 46.27  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 230.624 304.031 226.300 1.00 43.05  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 230.512 302.668 225.644 1.00 48.14  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 231.171 305.056 225.319 1.00 46.47  ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 227.406 305.787 229.052 1.00 42.69  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 226.027 305.906 229.530 1.00 46.49  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 225.893 307.157 230.395 1.00 50.27  ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 225.841 307.104 231.625 1.00 54.88  ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 225.612 304.653 230.291 1.00 41.64  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 225.536 303.420 229.438 1.00 49.00  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 226.688 302.755 229.048 1.00 53.20  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 224.312 302.927 229.022 1.00 49.53  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 226.618 301.623 228.263 1.00 45.89  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 224.237 301.794 228.236 1.00 48.24  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 225.391 301.141 227.857 1.00 48.27  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 225.825 308.305 229.724 1.00 55.42  ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 225.591 309.586 230.376 1.00 56.12  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 224.664 310.426 229.511 1.00 60.18  ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 224.433 310.127 228.337 1.00 63.00  ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 226.890 310.370 230.630 1.00 55.37  ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 227.536 310.655 229.383 1.00 62.84  ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 227.832 309.603 231.539 1.00 57.75  ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 224.125 311.487 230.114 1.00 65.85  ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 223.331 312.444 229.355 1.00 66.26  ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 224.170 313.206 228.337 1.00 71.91  ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 223.609 313.786 227.401 1.00 73.93  ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 222.635 313.425 230.302 1.00 66.13  ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 221.738 314.256 229.556 1.00 72.12  ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 223.654 314.298 231.016 1.00 65.36  ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 225.496 313.217 228.497 1.00 72.22  ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 226.360 313.851 227.507 1.00 67.44  ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 226.442 313.033 226.225 1.00 66.25  ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 226.870 313.553 225.188 1.00 73.90  ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 227.759 314.065 228.087 1.00 70.20  ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 227.832 314.999 229.294 1.00 71.35  ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 227.689 316.472 228.906 1.00 74.40  ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 226.323 316.851 228.560 1.00 74.72  ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 225.363 317.083 229.445 1.00 76.39  ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 225.587 317.002 230.746 1.00 76.11  ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 224.148 317.410 229.013 1.00 74.75  ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 226.043 311.760 226.272 1.00 63.53  ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 226.069 310.927 225.076 1.00 65.55  ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 225.038 311.367 224.047 1.00 65.87  ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 225.124 310.958 222.884 1.00 70.79  ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 225.841 309.461 225.448 1.00 62.55  ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 224.526 309.258 225.934 1.00 63.98  ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 224.068 312.185 224.445 1.00 63.19  ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 223.078 312.726 223.526 1.00 64.44  ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 223.503 314.059 222.924 1.00 67.56  ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 222.734 314.650 222.158 1.00 66.18  ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 221.729 312.882 224.235 1.00 63.89  ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 220.952 311.602 224.342 1.00 65.48  ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 221.393 310.574 225.158 1.00 65.60  ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 219.785 311.425 223.621 1.00 66.50  ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 220.682 309.394 225.254 1.00 66.16  ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 219.071 310.247 223.713 1.00 64.04  ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 219.519 309.231 224.532 1.00 65.10  ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 224.698 314.542 223.250 1.00 81.24  ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 225.204 315.769 222.662 1.00 81.89  ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 225.643 315.523 221.219 1.00 87.06  ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 225.811 314.385 220.772 1.00 87.71  ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 226.368 316.319 223.486 1.00 79.77  ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 225.919 316.905 224.809 1.00 84.32  ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 224.695 316.979 225.044 1.00 85.64  ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 226.791 317.291 225.616 1.00 82.37  ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 225.831 316.618 220.485 1.00 93.65  ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 226.236 316.547 219.089 1.00 94.09  ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 227.745 316.451 218.907 1.00 94.87  ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 228.207 316.308 217.770 1.00 93.80  ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 225.708 317.766 218.325 1.00 91.95  ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 224.300 317.868 218.441 1.00 91.56  ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 228.521 316.525 219.990 1.00 85.74  ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 229.977 316.482 219.913 1.00 83.48  ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 230.570 315.378 220.784 1.00 82.98  ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 231.769 315.405 221.079 1.00 83.37  ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 230.571 317.839 220.297 1.00 84.60  ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 230.388 318.205 221.762 1.00 84.89  ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 230.289 319.702 221.979 1.00 85.93  ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 230.325 320.453 220.982 1.00 84.74  ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 230.176 320.128 223.148 1.00 85.03  ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 229.759 314.409 221.199 1.00 69.68  ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 230.256 313.321 222.028 1.00 66.06  ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 231.236 312.454 221.247 1.00 67.16  ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 231.049 312.194 220.056 1.00 74.18  ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 229.095 312.471 222.542 1.00 66.76  ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 229.501 311.439 223.554 1.00 69.46  ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 230.166 311.808 224.710 1.00 70.38  ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 229.219 310.099 223.347 1.00 67.60  ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 230.542 310.860 225.643 1.00 68.26  ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 229.592 309.147 224.276 1.00 66.82  ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 230.255 309.528 225.425 1.00 64.74  ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 232.291 312.010 221.927 1.00 64.35  ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 233.333 311.188 221.321 1.00 62.23  ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 233.184 309.756 221.824 1.00 67.26  ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 233.397 309.483 223.009 1.00 73.93  ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 234.718 311.738 221.651 1.00 65.56  ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 234.816 313.253 221.617 1.00 66.34  ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 234.918 313.767 220.193 1.00 70.46  ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 235.367 315.219 220.163 1.00 72.37  ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 236.692 315.402 220.818 1.00 70.54  ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 232.815 308.844 220.921 1.00 60.32  ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 232.771 307.431 221.283 1.00 59.80  ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 234.165 306.907 221.604 1.00 61.96  ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 234.348 306.150 222.565 1.00 60.27  ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 232.136 306.619 220.155 1.00 53.46  ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 230.612 306.693 220.043 1.00 50.54  ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 230.111 305.786 218.931 1.00 61.82  ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 229.961 306.333 221.367 1.00 55.34  ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 235.158 307.299 220.811 1.00 68.51  ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 236.548 306.951 221.057 1.00 67.64  ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 237.407 308.182 220.813 1.00 73.58  ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 237.033 309.084 220.059 1.00 78.49  ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 237.010 305.787 220.171 1.00 67.82  ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 238.567 308.214 221.462 1.00 88.11  ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 239.473 309.349 221.382 1.00 88.65  ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 240.840 308.900 220.884 1.00 90.30  ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 241.291 307.790 221.181 1.00 90.62  ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 239.619 310.040 222.745 1.00 88.60  ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 238.126 310.879 223.322 1.00 94.10  ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 241.486 309.788 220.128 1.00 96.50  ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 242.832 309.602 219.577 1.00 99.54  ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 243.038 308.183 219.038 1.00 99.95  ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 243.983 307.473 219.385 1.00 98.17  ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 243.903 309.990 220.606 1.00 98.19  ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 243.989 309.137 221.871 1.00 96.82  ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 245.112 309.606 222.781 1.00 96.21  ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 244.766 310.928 223.447 1.00 98.13  ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 243.623 310.793 224.391 1.00 97.63  ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 242.127 307.785 218.146 1.00 90.35  ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 242.209 306.456 217.548 1.00 89.21  ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 243.451 306.337 216.671 1.00 91.13  ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 244.106 305.288 216.638 1.00 92.37  ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 240.922 306.135 216.766 1.00 86.96  ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 239.768 305.896 217.726 1.00 85.49  ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 240.583 307.251 215.791 1.00 87.87  ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 243.793 307.400 215.943 1.00 104.47 ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 245.000 307.434 215.127 1.00 106.42 ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 245.961 308.532 215.571 1.00 109.15 ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 246.849 308.922 214.807 1.00 110.12 ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 244.640 307.607 213.651 1.00 107.03 ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 243.646 308.729 213.418 1.00 109.19 ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 243.975 309.894 213.724 1.00 110.02 ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 242.533 308.444 212.928 1.00 107.23 ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 245.800 309.036 216.795 1.00 112.54 ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 246.596 310.137 217.289 1.00 113.26 ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 246.130 311.509 216.858 1.00 115.80 ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 246.469 312.498 217.519 1.00 114.64 ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 245.365 311.606 215.772 1.00 118.25 ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 244.842 312.876 215.285 1.00 116.34 ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 243.323 312.919 215.290 1.00 115.91 ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 242.734 313.865 215.825 1.00 113.70 ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 245.369 313.150 213.867 1.00 114.59 ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 246.853 313.340 213.801 1.00 117.29 ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 247.730 312.292 213.629 1.00 116.34 ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 247.613 314.457 213.883 1.00 117.42 ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 248.967 312.754 213.608 1.00 116.40 ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 248.924 314.065 213.761 1.00 117.60 ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 242.671 311.918 214.708 1.00 105.90 ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 241.222 311.870 214.591 1.00 102.21 ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 240.628 311.062 215.743 1.00 104.06 ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 241.311 310.280 216.408 1.00 103.27 ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 240.829 311.272 213.232 1.00 99.71  ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 239.337 311.241 212.929 1.00 102.34 ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 239.064 310.681 211.544 1.00 103.77 ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 237.582 310.738 211.211 1.00 102.21 ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 236.787 309.813 212.065 1.00 101.62 ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 239.335 311.275 215.986 1.00 90.43  ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 238.605 310.525 216.996 1.00 84.66  ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 237.232 310.165 216.447 1.00 81.87  ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 236.699 310.838 215.561 1.00 84.06  ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 238.478 311.316 218.304 1.00 83.48  ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 238.072 312.759 218.077 1.00 86.91  ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 237.803 313.130 216.916 1.00 89.16  ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 238.023 313.523 219.063 1.00 84.65  ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 236.665 309.088 216.983 1.00 68.81  ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 235.368 308.595 216.529 1.00 71.66  ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 234.265 309.430 217.166 1.00 66.30  ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 234.248 309.634 218.385 1.00 69.28  ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 235.204 307.105 216.866 1.00 66.39  ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 236.301 306.280 216.190 1.00 64.36  ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 233.833 306.610 216.438 1.00 63.50  ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 236.225 304.801 216.495 1.00 64.65  ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 233.341 309.914 216.342 1.00 65.78  ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 232.260 310.782 216.786 1.00 63.88  ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 230.973 309.995 217.012 1.00 67.10  ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 230.752 308.929 216.432 1.00 71.25  ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 232.009 311.898 215.769 1.00 69.37  ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 233.207 312.792 215.507 1.00 71.37  ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 233.597 313.609 216.722 1.00 73.54  ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 232.740 314.051 217.488 1.00 72.67  ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 234.895 313.817 216.903 1.00 73.62  ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 230.117 310.550 217.874 1.00 67.47  ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 228.782 310.044 218.179 1.00 65.90  ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 227.812 310.427 217.069 1.00 70.80  ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 227.741 311.606 216.700 1.00 75.38  ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 228.286 310.602 219.505 1.00 67.89  ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 226.966 310.021 219.991 1.00 67.43  ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 227.030 308.272 220.412 1.00 73.37  ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 225.307 307.827 220.218 1.00 65.11  ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 227.070 309.474 216.510 1.00 70.34  ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 226.082 309.815 215.479 1.00 69.77  ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 225.032 310.779 216.011 1.00 75.39  ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 224.614 310.697 217.168 1.00 82.51  ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 225.469 308.459 215.114 1.00 69.09  ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 226.478 307.453 215.521 1.00 72.21  ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 227.207 308.021 216.699 1.00 72.27  ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 224.604 311.699 215.152 1.00 80.42  ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 223.600 312.692 215.504 1.00 82.42  ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 222.186 312.253 215.145 1.00 81.72  ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 221.244 313.030 215.330 1.00 82.05  ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 223.919 314.026 214.824 1.00 83.34  ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 225.165 314.682 215.386 1.00 87.36  ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 225.467 314.464 216.579 1.00 86.17  ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 225.843 315.414 214.635 1.00 84.07  ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 222.017 311.034 214.638 1.00 77.57  ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 220.700 310.570 214.262 1.00 80.06  ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 219.821 310.275 215.462 1.00 81.91  ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 220.271 310.198 216.605 1.00 81.17  ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 218.526 310.113 215.185 1.00 82.36  ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 217.528 309.825 216.203 1.00 79.42  ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 216.706 308.587 215.866 1.00 78.91  ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 215.779 308.245 216.600 1.00 78.96  ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 216.606 311.038 216.441 1.00 83.11  ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 215.835 311.380 215.165 1.00 84.79  ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 217.408 312.236 216.928 1.00 79.81  ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 214.741 312.405 215.369 1.00 82.64  ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 217.028 307.906 214.769 1.00 80.87  ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 216.300 306.722 214.339 1.00 81.49  ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 217.272 305.568 214.147 1.00 80.92  ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 218.483 305.764 214.016 1.00 88.13  ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 215.518 306.978 213.044 1.00 79.99  ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 214.487 308.090 213.153 1.00 82.68  ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 213.967 308.499 211.785 1.00 82.62  ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 215.050 308.765 210.845 1.00 86.77  ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 214.873 309.092 209.573 1.00 85.99  ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 213.663 309.203 209.050 1.00 84.09  ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 215.936 309.314 208.806 1.00 83.66  ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 216.720 304.352 214.132 1.00 63.06  ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 217.551 303.155 214.046 1.00 67.04  ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 218.367 303.135 212.760 1.00 71.74  ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 219.563 302.824 212.775 1.00 73.43  ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 216.679 301.903 214.142 1.00 67.97  ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 217.430 300.612 213.861 1.00 65.22  ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 216.482 299.430 213.726 1.00 69.90  ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 217.175 298.206 213.337 1.00 70.51  ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 217.726 297.995 212.149 1.00 72.73  ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 217.667 298.900 211.185 1.00 68.58  ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 218.347 296.841 211.919 1.00 72.45  ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 217.735 303.468 211.632 1.00 80.54  ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 218.436 303.424 210.353 1.00 78.61  ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 219.585 304.424 210.315 1.00 76.18  ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 220.628 304.159 209.707 1.00 76.16  ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 217.460 303.678 209.203 1.00 79.78  ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 216.632 304.947 209.334 1.00 80.23  ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 215.343 304.728 210.102 1.00 86.21  ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 215.131 303.604 210.604 1.00 84.08  ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 214.539 305.679 210.199 1.00 87.15  ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 219.414 305.580 210.961 1.00 76.20  ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 220.483 306.573 210.989 1.00 74.31  ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 221.701 306.051 211.742 1.00 78.08  ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 222.843 306.313 211.348 1.00 78.59  ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 219.972 307.873 211.612 1.00 73.53  ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 218.925 308.583 210.765 1.00 79.11  ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 218.436 309.874 211.392 1.00 82.78  ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 219.212 310.851 211.427 1.00 81.30  ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 217.274 309.911 211.849 1.00 81.15  ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 221.478 305.313 212.832 1.00 71.64  ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 222.594 304.711 213.556 1.00 66.70  ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 223.225 303.574 212.761 1.00 67.34  ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 224.451 303.411 212.769 1.00 72.97  ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 222.129 304.212 214.924 1.00 65.09  ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 221.736 305.309 215.870 1.00 63.00  ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 222.662 306.253 216.279 1.00 64.99  ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 220.444 305.391 216.359 1.00 64.43  ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 222.305 307.262 217.151 1.00 65.23  ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 220.080 306.398 217.230 1.00 68.85  ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 221.012 307.334 217.627 1.00 69.44  ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 222.406 302.773 212.076 1.00 67.58  ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 222.930 301.639 211.319 1.00 68.26  ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 223.796 302.121 210.161 1.00 70.52  ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 224.871 301.569 209.898 1.00 71.95  ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 221.779 300.740 210.832 1.00 70.28  ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 222.304 299.669 209.890 1.00 67.81  ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 221.072 300.102 212.015 1.00 69.67  ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 223.342 303.158 209.450 1.00 72.24  ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 224.123 303.691 208.337 1.00 68.46  ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 225.475 304.210 208.809 1.00 72.32  ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 226.462 304.164 208.066 1.00 79.88  ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 223.342 304.797 207.626 1.00 71.27  ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 222.086 304.317 206.918 1.00 74.72  ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 221.138 305.451 206.579 1.00 79.80  ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 221.244 306.549 207.125 1.00 79.09  ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 220.201 305.188 205.674 1.00 76.20  ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 225.537 304.715 210.043 1.00 57.98  ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 226.818 305.113 210.615 1.00 59.04  ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 227.734 303.910 210.802 1.00 58.37  ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 228.944 303.997 210.565 1.00 59.10  ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 226.594 305.835 211.944 1.00 61.00  ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 227.854 306.286 212.616 1.00 65.35  ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 228.458 307.503 212.494 1.00 62.30  ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 228.657 305.530 213.531 1.00 63.37  ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 229.591 307.550 213.268 1.00 62.94  ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 229.735 306.351 213.916 1.00 60.29  ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 228.572 304.238 214.058 1.00 58.33  ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 230.720 305.922 214.803 1.00 58.35  ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 229.550 303.815 214.939 1.00 55.12  ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 230.609 304.654 215.302 1.00 56.73  ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 227.173 302.779 211.236 1.00 57.70  ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 227.971 301.568 211.419 1.00 58.09  ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 228.515 301.084 210.080 1.00 63.60  ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 229.687 300.706 209.965 1.00 66.47  ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 227.138 300.478 212.117 1.00 56.91  ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 227.962 299.212 212.295 1.00 57.30  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 226.624 300.980 213.455 1.00 57.43  ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 227.668 301.087 209.048 1.00 66.49  ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 228.104 300.671 207.719 1.00 63.50  ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 229.148 301.610 207.129 1.00 63.79  ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 229.895 301.201 206.234 1.00 68.05  ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 226.904 300.578 206.775 1.00 64.13  ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 225.720 299.811 207.339 1.00 65.87  ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 225.618 298.405 206.783 1.00 71.27  ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 226.467 298.032 205.946 1.00 70.55  ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 224.687 297.673 207.180 1.00 74.83  ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 229.217 302.853 207.607 1.00 64.84  ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 230.156 303.843 207.099 1.00 66.25  ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 231.420 303.938 207.946 1.00 71.24  ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 232.164 304.918 207.829 1.00 68.71  ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 229.480 305.211 207.005 1.00 65.45  ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 228.566 305.426 205.798 1.00 69.34  ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 227.685 306.648 206.001 1.00 67.23  ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 229.386 305.555 204.524 1.00 70.74  ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 231.673 302.949 208.798 1.00 66.58  ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 232.871 302.964 209.619 1.00 64.74  ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 234.115 302.850 208.736 1.00 67.17  ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 234.072 302.238 207.666 1.00 66.20  ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 232.835 301.827 210.637 1.00 66.28  ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 232.073 302.144 211.928 1.00 64.50  ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 232.020 300.937 212.849 1.00 62.88  ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 232.689 303.337 212.643 1.00 60.35  ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 235.237 303.439 209.163 1.00 72.57  ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 236.407 303.531 208.272 1.00 69.60  ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 236.988 302.192 207.854 1.00 74.05  ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 237.759 302.154 206.886 1.00 80.40  ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 237.417 304.335 209.103 1.00 70.47  ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 236.587 305.091 210.085 1.00 74.88  ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 235.436 304.191 210.413 1.00 75.24  ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 236.663 301.102 208.552 1.00 72.77  ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 237.213 299.773 208.283 1.00 75.83  ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 238.727 299.736 208.474 1.00 74.73  ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 239.417 298.897 207.886 1.00 73.21  ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 236.832 299.283 206.879 1.00 74.35  ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 236.966 297.779 206.725 1.00 81.23  ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 236.123 297.046 207.283 1.00 78.36  ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 237.911 297.331 206.042 1.00 80.64  ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 239.255 300.644 209.294 1.00 71.35  ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 240.674 300.677 209.621 1.00 70.62  ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 240.849 300.514 211.125 1.00 72.89  ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 241.601 301.264 211.755 1.00 74.73  ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 241.316 301.983 209.146 1.00 70.79  ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 240.776 303.081 209.891 1.00 69.04  ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 241.050 302.202 207.664 1.00 68.65  ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 240.144 299.543 211.702 1.00 55.81  ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 240.102 299.397 213.150 1.00 50.28  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 241.484 299.107 213.720 1.00 56.05  ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 242.255 298.317 213.168 1.00 58.56  ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 239.134 298.281 213.542 1.00 52.93  ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 238.872 298.195 215.036 1.00 53.60  ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 238.375 296.832 215.463 1.00 56.00  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 237.413 296.309 214.905 1.00 64.69  ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 239.030 296.248 216.460 1.00 48.53  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 241.786 299.757 214.833 1.00 60.65  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 243.013 299.595 215.594 1.00 55.74  ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 242.643 299.410 217.056 1.00 55.70  ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 241.537 299.773 217.472 1.00 62.40  ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 243.934 300.814 215.430 1.00 56.57  ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 243.188 302.015 215.660 1.00 56.77  ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 244.527 300.850 214.031 1.00 58.53  ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 243.539 298.834 217.866 1.00 50.97  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 243.237 298.684 219.300 1.00 47.71  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 242.980 300.002 220.011 1.00 47.56  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 242.452 299.984 221.130 1.00 57.85  ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 244.486 297.987 219.855 1.00 48.20  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 245.084 297.299 218.683 1.00 55.81  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 244.805 298.176 217.501 1.00 56.80  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 243.336 301.138 219.407 1.00 48.05  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 242.999 302.431 219.988 1.00 52.54  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 241.500 302.699 219.971 1.00 58.10  ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 241.029 303.552 220.731 1.00 59.94  ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 243.741 303.544 219.251 1.00 56.70  ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 243.539 303.445 217.852 1.00 66.93  ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 240.743 302.000 219.120 1.00 52.67  ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 239.288 302.087 219.188 1.00 53.20  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 238.767 301.555 220.515 1.00 56.91  ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 237.738 302.022 221.014 1.00 61.34  ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 238.648 301.313 218.034 1.00 51.08  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 238.817 301.940 216.682 1.00 54.82  ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 239.820 302.771 216.279 1.00 58.57  ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 237.947 301.786 215.554 1.00 59.04  ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 239.631 303.142 214.970 1.00 60.04  ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 238.487 302.551 214.502 1.00 57.93  ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 236.763 301.075 215.332 1.00 56.90  ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 237.885 302.625 213.248 1.00 55.87  ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 236.168 301.150 214.086 1.00 52.47  ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 236.729 301.919 213.061 1.00 55.46  ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 239.463 300.582 221.096 1.00 48.47  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 239.063 299.949 222.344 1.00 43.60  ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 239.648 300.638 223.568 1.00 49.39  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 239.401 300.188 224.692 1.00 55.45  ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 239.491 298.479 222.338 1.00 44.28  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 239.188 297.697 221.059 1.00 42.50  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 239.711 296.275 221.166 1.00 47.60  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 237.702 297.706 220.760 1.00 45.41  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 240.413 301.711 223.380 1.00 49.30  ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 241.130 302.346 224.462 1.00 43.64  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 242.501 301.769 224.732 1.00 49.58  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 243.238 302.326 225.554 1.00 65.76  ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 242.864 300.676 224.070 1.00 44.76  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 244.167 300.055 224.228 1.00 39.97  ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 245.197 300.730 223.328 1.00 47.67  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 244.843 301.376 222.340 1.00 57.25  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 244.078 298.569 223.894 1.00 46.10  ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 243.383 297.667 224.913 1.00 50.10  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 242.998 296.345 224.274 1.00 45.43  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 244.280 297.438 226.118 1.00 50.31  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 246.482 300.607 223.653 1.00 52.03  ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 247.515 301.090 222.732 1.00 49.52  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 247.526 300.280 221.445 1.00 52.65  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 247.208 299.089 221.429 1.00 57.24  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 248.815 300.903 223.522 1.00 50.22  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 248.499 299.841 224.521 1.00 50.85  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 247.063 300.058 224.891 1.00 53.87  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 247.900 300.950 220.352 1.00 57.09  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 247.922 300.295 219.049 1.00 57.53  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 248.987 299.210 218.958 1.00 66.61  ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 248.885 298.332 218.095 1.00 70.60  ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 248.142 301.328 217.943 1.00 59.03  ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 247.253 302.545 218.097 1.00 64.89  ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 247.323 303.256 219.099 1.00 68.47  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 246.410 302.791 217.102 1.00 64.71  ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 250.001 299.247 219.825 1.00 63.38  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 251.055 298.242 219.788 1.00 64.97  ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 250.608 296.902 220.359 1.00 63.49  ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 251.349 295.920 220.250 1.00 65.60  ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 252.287 298.747 220.542 1.00 65.78  ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 251.964 299.208 221.950 1.00 69.40  ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 251.485 298.434 222.779 1.00 70.59  ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 252.226 300.480 222.229 1.00 70.71  ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 249.421 296.842 220.969 1.00 61.76  ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 248.953 295.591 221.559 1.00 65.87  ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 248.717 294.520 220.503 1.00 70.44  ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 248.852 293.325 220.791 1.00 68.85  ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 247.676 295.835 222.362 1.00 65.81  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 248.362 294.920 219.281 1.00 70.55  ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 248.094 293.953 218.223 1.00 62.14  ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 249.334 293.595 217.416 1.00 66.63  ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 249.262 292.696 216.573 1.00 75.77  ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 247.022 294.491 217.273 1.00 61.20  ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 247.477 295.689 216.454 1.00 65.46  ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 246.490 296.063 215.366 1.00 73.48  ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 245.464 295.365 215.226 1.00 72.02  ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 246.741 297.055 214.651 1.00 71.53  ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 250.460 294.273 217.649 1.00 71.91  ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 251.639 294.085 216.810 1.00 69.37  ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 252.152 292.651 216.880 1.00 72.26  ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 252.446 292.029 215.853 1.00 77.93  ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 252.733 295.071 217.224 1.00 74.01  ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 254.014 294.948 216.418 1.00 73.94  ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 254.949 296.113 216.691 1.00 74.65  ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 255.077 296.382 218.118 1.00 79.53  ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 255.663 297.456 218.628 1.00 79.75  ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 256.187 298.391 217.853 1.00 76.82  ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 255.723 297.596 219.950 1.00 74.96  ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 252.269 292.108 218.093 1.00 68.58  ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 252.743 290.735 218.248 1.00 69.62  ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 251.692 289.752 217.747 1.00 68.70  ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 252.010 288.760 217.080 1.00 71.70  ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 253.126 290.461 219.714 1.00 73.36  ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 253.520 289.004 219.899 1.00 68.05  ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 254.257 291.381 220.144 1.00 72.55  ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 250.422 290.013 218.065 1.00 67.40  ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 249.348 289.124 217.633 1.00 66.78  ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 249.235 289.095 216.113 1.00 65.20  ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 249.059 288.030 215.512 1.00 67.60  ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 248.025 289.555 218.266 1.00 65.54  ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 246.771 288.815 217.797 1.00 68.74  ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 246.898 287.321 218.057 1.00 66.44  ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 245.531 289.377 218.475 1.00 66.82  ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 249.332 290.263 215.473 1.00 62.48  ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 249.276 290.315 214.017 1.00 58.73  ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 250.484 289.650 213.373 1.00 62.45  ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 250.350 289.055 212.298 1.00 67.81  ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 249.163 291.765 213.543 1.00 62.08  ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 247.779 292.412 213.638 1.00 58.70  ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 247.724 293.683 212.807 1.00 62.12  ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 246.696 291.438 213.203 1.00 62.40  ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 251.658 289.746 213.998 1.00 65.42  ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 252.844 289.081 213.468 1.00 65.72  ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 252.682 287.566 213.505 1.00 64.28  ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 252.999 286.869 212.534 1.00 69.30  ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 254.083 289.510 214.258 1.00 65.67  ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 254.340 290.902 214.035 1.00 70.83  ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 255.299 288.702 213.832 1.00 62.81  ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 252.180 287.039 214.624 1.00 60.20  ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 252.026 285.595 214.767 1.00 60.00  ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 251.009 285.047 213.772 1.00 63.95  ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 251.223 283.991 213.165 1.00 69.81  ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 251.617 285.253 216.201 1.00 63.74  ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 252.628 285.710 217.108 1.00 65.85  ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 251.445 283.751 216.364 1.00 63.42  ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 249.892 285.755 213.592 1.00 62.72  ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 248.870 285.306 212.652 1.00 56.56  ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 249.395 285.315 211.222 1.00 58.28  ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 249.085 284.421 210.427 1.00 65.44  ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 247.621 286.180 212.778 1.00 57.06  ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 246.904 286.047 214.110 1.00 64.53  ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 245.540 286.709 214.107 1.00 69.23  ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 245.421 287.914 213.883 1.00 67.57  ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 244.500 285.922 214.357 1.00 66.45  ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 250.189 286.330 210.874 1.00 60.72  ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 250.783 286.367 209.547 1.00 60.39  ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 251.735 285.211 209.307 1.00 62.24  ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 251.753 284.619 208.225 1.00 61.04  ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 252.542 284.877 210.316 1.00 63.28  ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 253.443 283.732 210.203 1.00 59.93  ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 252.646 282.436 210.133 1.00 61.49  ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 253.013 281.500 209.411 1.00 63.03  ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 254.445 283.726 211.372 1.00 60.56  ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 255.304 282.471 211.338 1.00 62.75  ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 255.319 284.969 211.325 1.00 62.26  ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 251.541 282.361 210.879 1.00 67.46  ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 250.696 281.172 210.841 1.00 61.48  ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 250.100 280.960 209.455 1.00 62.83  ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 249.952 279.819 209.003 1.00 68.53  ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 249.588 281.283 211.889 1.00 62.81  ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 249.172 279.934 212.441 1.00 70.66  ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 249.639 278.903 211.912 1.00 71.84  ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 248.378 279.903 213.405 1.00 71.04  ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 249.751 282.050 208.767 1.00 62.13  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 249.204 281.935 207.418 1.00 61.90  ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 250.219 281.310 206.468 1.00 65.93  ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 249.866 280.485 205.617 1.00 68.50  ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 248.763 283.311 206.915 1.00 61.02  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 248.805 283.468 205.402 1.00 62.19  ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 248.370 285.129 204.854 1.00 76.42  ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 249.978 285.918 204.854 1.00 68.24  ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 251.491 281.695 206.600 1.00 67.49  ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 252.537 281.116 205.760 1.00 62.01  ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 252.655 279.620 206.018 1.00 59.01  ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 252.792 278.818 205.086 1.00 66.34  ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 253.877 281.835 205.999 1.00 63.61  ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 253.687 283.351 205.938 1.00 63.71  ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 254.914 281.381 204.984 1.00 67.70  ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 253.473 283.881 204.543 1.00 62.68  ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 252.613 279.222 207.292 1.00 60.29  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 252.683 277.804 207.630 1.00 61.94  ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 251.477 277.050 207.085 1.00 63.64  ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 251.610 275.937 206.564 1.00 67.34  ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 252.788 277.633 209.146 1.00 65.68  ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 253.898 278.346 209.663 1.00 67.95  ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 250.284 277.641 207.203 1.00 59.41  ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 249.085 276.991 206.683 1.00 54.89  ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 249.137 276.864 205.167 1.00 59.47  ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 248.801 275.810 204.615 1.00 65.32  ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 247.838 277.762 207.116 1.00 57.09  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 247.583 277.727 208.612 1.00 58.21  ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 246.415 278.617 208.996 1.00 58.51  ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 246.298 278.739 210.505 1.00 60.97  ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 246.235 277.404 211.160 1.00 57.96  ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 249.557 277.925 204.474 1.00 63.43  ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 249.683 277.864 203.023 1.00 58.67  ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 250.731 276.854 202.578 1.00 61.80  ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 250.530 276.176 201.565 1.00 69.92  ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 250.022 279.245 202.463 1.00 56.04  ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 248.845 280.201 202.426 1.00 54.70  ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 248.834 281.209 200.933 1.00 73.17  ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 250.009 282.482 201.380 1.00 64.66  ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 251.840 276.742 203.306 1.00 62.67  ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 252.856 275.744 203.010 1.00 64.58  ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 252.421 274.331 203.370 1.00 65.34  ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 252.813 273.382 202.681 1.00 68.64  ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 254.153 276.081 203.753 1.00 64.28  ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 255.362 275.185 203.486 1.00 65.09  ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 255.774 275.270 202.026 1.00 68.47  ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 256.516 275.560 204.401 1.00 64.41  ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 251.620 274.171 204.426 1.00 62.68  ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 251.181 272.841 204.835 1.00 63.40  ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 250.285 272.200 203.782 1.00 61.70  ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 250.410 271.003 203.499 1.00 64.58  ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 250.453 272.921 206.177 1.00 60.25  ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 250.292 271.585 206.881 1.00 58.83  ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 249.407 271.714 208.112 1.00 64.51  ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 249.817 272.899 208.972 1.00 63.72  ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 248.871 273.120 210.102 1.00 61.37  ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 249.377 272.978 203.192 1.00 61.55  ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 248.413 272.471 202.224 1.00 64.13  ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 248.776 272.846 200.789 1.00 65.61  ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 247.888 273.081 199.962 1.00 68.03  ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 247.009 272.960 202.582 1.00 62.65  ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 246.840 274.471 202.576 1.00 61.78  ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 245.114 274.992 202.589 1.00 68.54  ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 244.514 274.257 201.073 1.00 62.33  ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 250.067 272.894 200.475 1.00 73.20  ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 250.516 273.152 199.112 1.00 75.79  ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 250.833 271.845 198.395 1.00 75.36  ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 251.641 271.046 198.870 1.00 74.43  ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 251.744 274.064 199.109 1.00 69.88  ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 252.218 274.450 197.717 1.00 72.64  ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 253.399 275.398 197.744 1.00 75.85  ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 253.903 275.749 198.811 1.00 79.63  ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 253.847 275.820 196.568 1.00 75.42  ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 271.035 255.575 220.648 1.00 106.15 ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 270.474 256.311 219.513 1.00 109.06 ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 270.840 257.792 219.526 1.00 108.41 ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 271.630 258.224 220.365 1.00 108.50 ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 268.969 256.120 219.694 1.00 106.93 ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 268.853 254.774 220.326 1.00 107.89 ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 270.090 254.575 221.175 1.00 107.91 ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 270.266 258.557 218.595 1.00 108.22 ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 270.587 259.976 218.501 1.00 108.12 ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 270.030 260.768 219.677 1.00 108.87 ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 270.655 261.740 220.117 1.00 109.39 ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 270.063 260.548 217.184 1.00 107.48 ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 268.862 260.378 220.194 1.00 103.03 ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 268.243 261.147 221.269 1.00 102.17 ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 269.043 261.042 222.563 1.00 99.76  ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 269.017 261.959 223.392 1.00 99.76  ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 266.797 260.694 221.482 1.00 100.84 ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 266.652 259.263 221.895 1.00 102.51 ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 266.522 258.182 221.073 1.00 102.06 ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 266.606 258.757 223.234 1.00 103.38 ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 266.405 257.033 221.817 1.00 105.56 ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 266.454 257.359 223.147 1.00 104.59 ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 266.684 259.350 224.498 1.00 100.94 ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 266.377 256.545 224.274 1.00 101.49 ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 266.607 258.540 225.616 1.00 99.91  ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 266.455 257.153 225.497 1.00 100.88 ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 269.749 259.927 222.760 1.00 96.85  ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 270.597 259.791 223.941 1.00 96.55  ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 271.759 260.777 223.902 1.00 97.82  ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 272.126 261.364 224.927 1.00 98.97  ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 271.111 258.355 224.059 1.00 98.24  ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 270.063 257.353 224.515 1.00 99.35  ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 270.678 255.657 224.545 1.00 103.70 ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 272.043 255.804 225.694 1.00 98.11  ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 272.354 260.971 222.723 1.00 103.05 ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 273.534 261.825 222.619 1.00 102.59 ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 273.169 263.300 222.752 1.00 101.20 ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 273.880 264.066 223.413 1.00 101.23 ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 274.261 261.565 221.298 1.00 101.04 ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 275.260 260.413 221.344 1.00 100.36 ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 274.568 259.063 221.441 1.00 102.56 ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 275.506 257.983 221.726 1.00 105.93 ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 275.160 256.712 221.878 1.00 104.69 ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 273.900 256.322 221.776 1.00 100.75 ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 276.102 255.810 222.140 1.00 103.74 ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 272.066 263.719 222.127 1.00 94.65  ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 271.681 265.126 222.197 1.00 96.62  ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 271.156 265.489 223.581 1.00 96.22  ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 271.317 266.629 224.032 1.00 96.70  ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 270.646 265.451 221.116 1.00 94.81  ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 270.321 266.846 221.167 1.00 93.85  ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 269.379 264.629 221.303 1.00 93.65  ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 270.526 264.535 224.273 1.00 85.71  ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 270.074 264.793 225.635 1.00 84.38  ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 271.238 264.794 226.617 1.00 84.37  ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 271.211 265.535 227.606 1.00 87.33  ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 269.028 263.758 226.048 1.00 86.31  ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 268.417 263.911 227.442 1.00 85.48  ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 267.644 265.215 227.552 1.00 83.50  ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 267.525 262.725 227.765 1.00 86.75  ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 272.260 263.973 226.366 1.00 85.26  ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 273.438 263.966 227.227 1.00 86.84  ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 274.144 265.315 227.193 1.00 87.40  ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 274.563 265.837 228.232 1.00 88.42  ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 274.386 262.843 226.803 1.00 87.28  ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 275.693 262.841 227.534 1.00 87.67  ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 276.724 263.701 227.223 1.00 88.32  ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 276.134 262.083 228.565 1.00 88.25  ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 277.744 263.473 228.030 1.00 87.60  ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 277.412 262.495 228.854 1.00 86.39  ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 274.291 265.892 225.998 1.00 86.87  ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 274.887 267.219 225.888 1.00 86.34  ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 274.006 268.274 226.543 1.00 85.92  ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 274.505 269.162 227.244 1.00 87.17  ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 275.135 267.565 224.420 1.00 88.12  ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 273.984 267.211 223.643 1.00 90.14  ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 276.348 266.812 223.893 1.00 87.05  ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 272.691 268.193 226.325 1.00 83.58  ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 271.779 269.171 226.911 1.00 85.14  ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 271.795 269.103 228.433 1.00 84.96  ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 271.819 270.139 229.108 1.00 87.99  ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 270.362 268.949 226.382 1.00 84.26  ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 270.394 268.844 224.953 1.00 83.39  ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 269.459 270.106 226.778 1.00 82.91  ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 271.780 267.891 228.991 1.00 82.70  ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 271.831 267.746 230.442 1.00 78.30  ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 273.173 268.206 230.998 1.00 78.43  ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 273.229 268.824 232.067 1.00 82.32  ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 271.552 266.297 230.836 1.00 80.77  ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 274.266 267.905 230.291 1.00 80.12  ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 275.583 268.338 230.745 1.00 81.62  ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 275.698 269.857 230.741 1.00 82.16  ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 276.262 270.446 231.670 1.00 80.99  ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 276.671 267.714 229.872 1.00 82.90  ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 276.562 266.301 229.853 1.00 81.78  ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 275.175 270.508 229.699 1.00 82.74  ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 275.178 271.967 229.666 1.00 82.16  ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 274.311 272.544 230.777 1.00 84.34  ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 274.688 273.531 231.419 1.00 84.81  ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 274.702 272.466 228.301 1.00 81.85  ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 275.581 271.984 227.166 1.00 84.70  ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 276.739 271.620 227.373 1.00 85.52  ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 275.034 271.978 225.956 1.00 83.36  ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 273.145 271.939 231.021 1.00 79.38  ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 272.270 272.418 232.086 1.00 74.65  ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 272.943 272.307 233.447 1.00 76.39  ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 272.820 273.209 234.283 1.00 80.10  ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 270.953 271.641 232.074 1.00 74.63  ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 270.016 272.063 230.988 1.00 77.56  ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 270.126 273.165 230.193 1.00 78.20  ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 268.819 271.391 230.579 1.00 78.83  ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 269.073 273.221 229.312 1.00 79.72  ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 268.256 272.143 229.529 1.00 80.22  ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 268.169 270.226 230.998 1.00 78.59  ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 267.076 271.768 228.892 1.00 79.79  ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 266.997 269.856 230.365 1.00 77.45  ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 266.463 270.624 229.323 1.00 78.02  ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 273.660 271.206 233.688 1.00 78.34  ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 274.356 271.042 234.959 1.00 79.31  ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 275.424 272.114 235.147 1.00 80.63  ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 275.707 272.528 236.277 1.00 80.05  ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 274.974 269.647 235.042 1.00 81.08  ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 274.048 268.520 235.503 1.00 79.30  ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 274.744 267.173 235.387 1.00 79.43  ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 273.577 268.762 236.928 1.00 77.46  ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 276.030 272.573 234.049 1.00 87.61  ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 277.039 273.623 234.150 1.00 87.79  ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 276.404 274.980 234.428 1.00 86.61  ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 276.906 275.746 235.259 1.00 87.36  ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 277.873 273.671 232.870 1.00 87.22  ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 278.888 272.576 232.769 1.00 89.87  ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 279.772 272.285 233.786 1.00 88.04  ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 279.158 271.699 231.774 1.00 90.90  ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 280.544 271.277 233.420 1.00 90.87  ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 280.192 270.903 232.203 1.00 92.35  ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 275.304 275.299 233.741 1.00 78.48  ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 274.637 276.580 233.962 1.00 79.74  ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 274.023 276.650 235.355 1.00 81.80  ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 274.134 277.672 236.042 1.00 82.60  ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 273.570 276.811 232.891 1.00 78.82  ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 273.996 276.637 231.432 1.00 82.72  ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 272.782 276.633 230.516 1.00 80.62  ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 274.978 277.723 231.022 1.00 80.86  ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 273.369 275.579 235.783 1.00 78.17  ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 272.734 275.561 237.106 1.00 76.11  ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 273.815 275.561 238.182 1.00 76.05  ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 274.777 274.778 238.089 1.00 75.99  ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 271.818 274.343 237.240 1.00 73.27  ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 270.663 274.434 236.241 1.00 76.18  ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 271.283 274.227 238.655 1.00 73.21  ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 269.743 273.234 236.261 1.00 75.67  ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 273.715 276.413 239.202 1.00 75.93  ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 274.725 276.419 240.266 1.00 75.00  ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 274.747 275.100 241.025 1.00 77.51  ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 273.753 274.377 241.107 1.00 79.98  ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 274.283 277.576 241.170 1.00 74.41  ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 273.461 278.454 240.281 1.00 76.09  ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 272.752 277.517 239.351 1.00 75.39  ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 275.917 274.790 241.583 1.00 82.65  ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 276.153 273.488 242.201 1.00 85.15  ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 275.590 273.406 243.619 1.00 85.05  ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 274.718 272.577 243.899 1.00 87.36  ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 277.654 273.179 242.200 1.00 83.75  ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 278.258 273.067 240.810 1.00 83.76  ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 279.709 272.634 240.837 1.00 86.17  ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 280.593 273.354 240.373 1.00 84.72  ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 279.962 271.449 241.382 1.00 86.79  ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 276.078 274.254 244.520 1.00 82.19  ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 275.750 274.164 245.937 1.00 83.37  ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 275.156 275.473 246.436 1.00 82.99  ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 275.609 276.558 246.059 1.00 85.62  ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 276.989 273.814 246.771 1.00 86.05  ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 277.966 274.854 246.639 1.00 86.89  ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 277.592 272.495 246.310 1.00 84.10  ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 274.138 275.359 247.287 1.00 78.34  ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 273.507 276.498 247.948 1.00 80.18  ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 273.571 276.264 249.452 1.00 78.99  ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 272.941 275.333 249.967 1.00 78.36  ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 272.064 276.677 247.477 1.00 79.46  ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 271.239 277.750 248.189 1.00 76.93  ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 271.857 279.123 247.991 1.00 78.85  ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 269.800 277.733 247.697 1.00 75.82  ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 274.328 277.103 250.153 1.00 85.38  ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 274.529 276.932 251.585 1.00 86.67  ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 273.328 277.443 252.369 1.00 86.67  ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 272.756 278.490 252.051 1.00 91.25  ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 275.795 277.660 252.036 1.00 85.61  ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 275.648 279.064 251.915 1.00 89.81  ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 272.949 276.695 253.402 1.00 83.38  ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 271.835 277.070 254.257 1.00 84.43  ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 272.232 278.202 255.200 1.00 84.21  ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 273.406 278.396 255.527 1.00 82.63  ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 271.346 275.869 255.070 1.00 84.41  ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 270.792 274.754 254.239 1.00 85.69  ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 269.667 274.045 254.602 1.00 84.85  ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 271.209 274.220 253.066 1.00 88.87  ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 269.413 273.126 253.688 1.00 85.42  ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 270.334 273.211 252.745 1.00 89.18  ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 271.228 278.958 255.636 1.00 88.71  ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 271.452 279.998 256.629 1.00 91.22  ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 271.687 279.380 258.003 1.00 92.51  ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 271.065 278.381 258.375 1.00 90.98  ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 270.262 280.957 256.684 1.00 92.85  ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 269.924 281.749 255.418 1.00 89.94  ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 269.108 282.984 255.764 1.00 88.95  ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 271.186 282.138 254.668 1.00 89.27  ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 272.595 279.988 258.762 1.00 98.78  ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 272.936 279.509 260.096 1.00 97.40  ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 271.996 280.142 261.116 1.00 96.28  ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 271.855 281.369 261.164 1.00 97.10  ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 274.397 279.816 260.425 1.00 96.27  ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 274.788 281.282 260.303 1.00 98.16  ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 276.251 281.495 260.652 1.00 98.02  ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 276.531 281.135 262.102 1.00 98.69  ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 277.578 282.009 262.699 1.00 95.70  ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 271.347 279.305 261.921 1.00 96.34  ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 270.397 279.805 262.904 1.00 98.96  ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 271.120 280.328 264.140 1.00 100.36 ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 272.026 279.683 264.674 1.00 98.05  ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 269.409 278.707 263.299 1.00 96.32  ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 268.673 278.084 262.125 1.00 96.06  ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 267.389 277.406 262.576 1.00 97.95  ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 266.289 278.354 262.713 1.00 100.97 ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 265.007 278.017 262.727 1.00 100.27 ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 264.622 276.756 262.611 1.00 97.28  ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 264.086 278.968 262.859 1.00 97.88  ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 270.707 281.510 264.591 1.00 108.49 ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 271.250 282.137 265.785 1.00 107.02 ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 270.079 282.620 266.630 1.00 107.06 ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 268.969 282.812 266.126 1.00 110.11 ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 272.200 283.294 265.428 1.00 108.25 ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 273.121 282.856 264.422 1.00 107.27 ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 273.002 283.742 266.643 1.00 107.15 ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 270.329 282.804 267.926 1.00 109.43 ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 269.275 283.125 268.885 1.00 111.46 ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 268.559 284.415 268.497 1.00 110.93 ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 267.338 284.522 268.657 1.00 111.37 ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 269.829 283.200 270.321 1.00 111.02 ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 270.224 281.813 270.804 1.00 108.80 ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 271.021 284.135 270.394 1.00 110.01 ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 269.299 285.406 267.991 1.00 108.17 ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 268.638 286.620 267.520 1.00 108.63 ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 268.176 286.470 266.075 1.00 109.94 ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 267.310 287.222 265.613 1.00 108.37 ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 269.558 287.836 267.660 1.00 107.60 ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 270.760 287.861 266.721 1.00 110.68 ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 271.950 287.086 267.249 1.00 112.51 ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 271.773 286.284 268.187 1.00 111.24 ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 273.067 287.286 266.727 1.00 110.81 ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 268.746 285.508 265.345 1.00 103.68 ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 268.345 285.290 263.959 1.00 101.78 ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 266.920 284.758 263.873 1.00 101.82 ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 266.147 285.160 262.995 1.00 104.50 ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 269.319 284.329 263.275 1.00 101.19 ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 270.605 285.008 262.847 1.00 102.77 ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 270.782 286.209 263.045 1.00 102.24 ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 271.510 284.238 262.253 1.00 102.23 ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 266.554 283.849 264.781 1.00 99.51  ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 265.238 283.214 264.718 1.00 100.15 ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 264.132 284.246 264.888 1.00 100.18 ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 263.099 284.189 264.210 1.00 100.53 ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 265.134 282.095 265.772 1.00 100.94 ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 266.295 281.109 265.623 1.00 100.32 ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 263.802 281.370 265.653 1.00 100.89 ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 266.283 279.994 266.645 1.00 99.15  ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 264.331 285.209 265.790 1.00 100.07 ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 263.292 286.196 266.069 1.00 99.92  ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 263.046 287.103 264.868 1.00 98.77  ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 261.933 287.607 264.678 1.00 98.03  ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 263.669 287.023 267.299 1.00 102.27 ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 263.278 286.391 268.629 1.00 101.19 ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 264.217 285.259 269.014 1.00 100.45 ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 263.872 284.696 270.382 1.00 99.12  ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 264.716 283.518 270.724 1.00 98.42  ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 264.070 287.326 264.050 1.00 95.57  ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 263.961 288.238 262.923 1.00 94.34  ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 263.043 287.648 261.852 1.00 95.66  ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 263.326 286.555 261.337 1.00 95.08  ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 265.346 288.513 262.339 1.00 95.60  ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 265.345 289.645 261.327 1.00 97.25  ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 264.303 290.314 261.170 1.00 95.78  ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 266.392 289.866 260.684 1.00 96.86  ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 261.942 288.323 261.502 1.00 90.92  ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 261.075 287.794 260.433 1.00 90.62  ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 261.772 287.680 259.088 1.00 88.28  ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 261.480 286.752 258.323 1.00 87.84  ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 259.916 288.803 260.391 1.00 86.93  ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 260.435 290.029 261.075 1.00 83.41  ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 261.389 289.541 262.114 1.00 86.85  ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 262.683 288.604 258.774 1.00 80.18  ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 263.392 288.536 257.499 1.00 82.66  ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 264.287 287.307 257.429 1.00 85.65  ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 264.374 286.653 256.383 1.00 87.94  ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 264.206 289.810 257.278 1.00 83.00  ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 263.561 290.854 256.364 1.00 82.03  ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 262.264 291.374 256.959 1.00 84.54  ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 264.523 291.996 256.095 1.00 82.75  ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 264.966 286.978 258.530 1.00 88.31  ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 265.777 285.766 258.551 1.00 86.59  ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 264.905 284.524 258.418 1.00 88.28  ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 265.300 283.547 257.773 1.00 93.04  ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 266.609 285.702 259.831 1.00 87.19  ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 267.477 284.481 259.925 1.00 89.40  ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 268.700 284.435 259.278 1.00 90.81  ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 267.068 283.375 260.651 1.00 89.09  ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 269.501 283.312 259.359 1.00 90.01  ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 267.864 282.251 260.736 1.00 89.38  ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 269.080 282.219 260.088 1.00 90.14  ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 263.718 284.541 259.029 1.00 84.89  ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 262.799 283.415 258.898 1.00 83.96  ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 262.400 283.203 257.443 1.00 84.85  ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 262.368 282.068 256.954 1.00 85.27  ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 261.558 283.646 259.761 1.00 87.00  ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 261.787 283.535 261.260 1.00 85.61  ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 260.472 283.697 262.007 1.00 85.47  ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 260.554 283.261 263.395 1.00 86.93  ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 260.132 283.974 264.430 1.00 87.33  ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 259.591 285.171 264.271 1.00 86.17  ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 260.256 283.474 265.657 1.00 85.41  ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 262.089 284.290 256.734 1.00 81.34  ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 261.701 284.173 255.333 1.00 79.54  ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 262.884 283.768 254.462 1.00 80.35  ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 262.763 282.873 253.617 1.00 85.41  ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 261.098 285.490 254.844 1.00 76.69  ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 261.051 285.619 253.348 1.00 81.20  ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 260.037 285.019 252.621 1.00 81.88  ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 262.025 286.331 252.666 1.00 82.40  ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 259.991 285.132 251.245 1.00 79.83  ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 261.984 286.447 251.290 1.00 81.97  ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 260.966 285.845 250.580 1.00 79.74  ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 264.035 284.418 254.650 1.00 78.63  ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 265.192 284.127 253.809 1.00 75.84  ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 265.721 282.720 254.054 1.00 81.28  ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 266.173 282.052 253.116 1.00 86.87  ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 266.286 285.169 254.038 1.00 76.59  ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 266.015 286.485 253.365 1.00 80.57  ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 265.563 286.526 252.056 1.00 79.09  ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 266.214 287.679 254.036 1.00 84.10  ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 265.312 287.732 251.431 1.00 76.80  ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 265.965 288.889 253.416 1.00 82.39  ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 265.514 288.915 252.111 1.00 77.62  ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 265.684 282.252 255.305 1.00 83.24  ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 266.066 280.869 255.575 1.00 80.79  ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 265.136 279.897 254.863 1.00 84.04  ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 265.592 278.917 254.264 1.00 86.19  ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 266.061 280.593 257.078 1.00 81.98  ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 266.526 279.190 257.436 1.00 85.32  ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 266.563 278.945 258.930 1.00 88.54  ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 266.204 279.863 259.695 1.00 90.64  ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 266.948 277.830 259.339 1.00 89.27  ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 263.827 280.158 254.913 1.00 75.50  ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 262.871 279.275 254.255 1.00 72.87  ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 263.096 279.243 252.749 1.00 78.85  ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 263.054 278.173 252.132 1.00 82.28  ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 261.442 279.714 254.577 1.00 72.33  ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 260.372 278.979 253.788 1.00 75.02  ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 259.037 278.998 254.514 1.00 75.11  ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 258.518 280.351 254.671 1.00 76.01  ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 257.371 280.777 254.160 1.00 73.45  ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 256.594 279.979 253.446 1.00 71.69  ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 256.994 282.035 254.371 1.00 76.61  ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 263.353 280.405 252.143 1.00 76.45  ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 263.609 280.452 250.706 1.00 73.89  ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 264.841 279.636 250.340 1.00 77.77  ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 264.863 278.960 249.305 1.00 85.44  ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 263.771 281.901 250.249 1.00 76.15  ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 262.499 282.723 250.332 1.00 81.61  ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 261.441 282.262 249.350 1.00 83.31  ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 261.670 282.387 248.129 1.00 84.06  ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 260.382 281.776 249.798 1.00 82.06  ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 265.880 279.692 251.175 1.00 75.99  ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 267.077 278.896 250.927 1.00 76.42  ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 266.768 277.409 251.063 1.00 79.26  ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 267.271 276.586 250.289 1.00 83.02  ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 268.211 279.337 251.870 1.00 78.69  ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 269.360 278.343 251.833 1.00 79.40  ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 268.697 280.729 251.498 1.00 77.58  ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 265.933 277.042 252.040 1.00 79.38  ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 265.592 275.635 252.238 1.00 80.26  ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 264.898 275.055 251.011 1.00 84.73  ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 265.269 273.980 250.524 1.00 83.86  ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 264.710 275.475 253.477 1.00 82.04  ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 265.383 275.851 254.787 1.00 82.29  ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 266.448 274.844 255.180 1.00 82.75  ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 267.157 275.269 256.455 1.00 83.79  ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 266.247 275.242 257.633 1.00 81.60  ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 263.880 275.751 250.497 1.00 83.11  ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 263.217 275.291 249.280 1.00 79.85  ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 264.161 275.340 248.087 1.00 78.28  ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 264.157 274.435 247.244 1.00 83.25  ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 261.963 276.122 249.006 1.00 78.13  ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 261.220 276.570 250.249 1.00 79.50  ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 259.867 277.703 249.883 1.00 89.66  ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 258.923 276.734 248.711 1.00 83.12  ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 264.974 276.394 247.994 1.00 70.30  ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 265.909 276.496 246.886 1.00 73.31  ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 266.959 275.402 246.900 1.00 73.13  ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 267.251 274.797 245.866 1.00 77.11  ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 267.542 275.134 248.071 1.00 74.95  ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 268.559 274.091 248.169 1.00 73.53  ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 267.972 272.712 247.891 1.00 76.02  ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 268.599 271.891 247.211 1.00 80.08  ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 269.217 274.125 249.548 1.00 73.98  ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 266.776 272.436 248.415 1.00 75.79  ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 266.141 271.143 248.174 1.00 75.19  ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 265.809 270.962 246.699 1.00 77.02  ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 266.034 269.890 246.126 1.00 75.42  ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 264.883 271.010 249.032 1.00 75.48  ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 264.169 269.677 248.882 1.00 76.71  ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 263.008 269.561 249.855 1.00 77.03  ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 261.845 270.443 249.433 1.00 78.85  ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 260.658 270.253 250.310 1.00 78.04  ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 265.270 272.006 246.065 1.00 75.25  ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 264.976 271.931 244.638 1.00 69.17  ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 266.256 271.850 243.818 1.00 70.76  ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 266.308 271.151 242.800 1.00 78.15  ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 264.135 273.134 244.211 1.00 70.35  ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 263.684 273.174 242.750 1.00 73.43  ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 263.055 271.851 242.343 1.00 72.90  ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 262.714 274.321 242.524 1.00 75.36  ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 267.300 272.565 244.244 1.00 68.82  ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 268.577 272.512 243.539 1.00 65.22  ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 269.169 271.109 243.584 1.00 69.33  ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 269.665 270.599 242.574 1.00 76.70  ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 269.549 273.525 244.145 1.00 68.26  ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 270.890 273.704 243.437 1.00 70.28  ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 270.715 274.566 242.203 1.00 73.58  ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 271.916 274.312 244.379 1.00 70.33  ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 269.126 270.471 244.756 1.00 74.09  ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 269.655 269.117 244.881 1.00 72.59  ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 268.852 268.129 244.046 1.00 73.98  ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 269.423 267.244 243.398 1.00 75.29  ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 269.666 268.692 246.349 1.00 72.52  ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 270.284 267.326 246.594 1.00 76.26  ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 270.330 266.964 248.064 1.00 79.74  ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 269.864 267.720 248.916 1.00 77.29  ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 270.892 265.800 248.370 1.00 78.52  ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 267.523 268.260 244.052 1.00 73.76  ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 266.684 267.348 243.281 1.00 71.07  ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 266.935 267.501 241.786 1.00 72.00  ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 267.071 266.507 241.064 1.00 74.06  ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 265.210 267.589 243.608 1.00 72.60  ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 264.849 267.169 245.019 1.00 77.71  ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 265.493 266.238 245.547 1.00 78.28  ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 263.919 267.767 245.599 1.00 77.52  ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 267.005 268.744 241.304 1.00 73.66  ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 267.203 268.977 239.877 1.00 68.88  ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 268.572 268.475 239.433 1.00 70.13  ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 268.697 267.808 238.398 1.00 73.77  ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 267.011 270.470 239.551 1.00 68.36  ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 267.580 270.797 238.180 1.00 69.75  ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 265.538 270.840 239.620 1.00 68.89  ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 269.618 268.780 240.205 1.00 71.27  ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 270.961 268.342 239.837 1.00 70.71  ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 271.083 266.824 239.875 1.00 73.48  ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 271.716 266.226 238.997 1.00 76.53  ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 271.996 268.989 240.757 1.00 72.76  ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 272.181 270.478 240.523 1.00 72.08  ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 273.384 271.009 241.285 1.00 73.14  ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 274.638 270.463 240.779 1.00 76.56  ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 275.202 270.809 239.629 1.00 74.14  ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 274.656 271.715 238.834 1.00 73.64  ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 276.344 270.232 239.267 1.00 73.22  ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 270.494 266.184 240.887 1.00 74.80  ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 270.520 264.726 240.953 1.00 73.92  ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 269.765 264.111 239.781 1.00 75.38  ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 270.203 263.108 239.207 1.00 79.20  ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 269.932 264.248 242.280 1.00 73.70  ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 270.170 262.775 242.574 1.00 77.92  ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 271.628 262.465 242.855 1.00 81.43  ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 272.131 262.728 243.947 1.00 78.50  ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 272.314 261.900 241.868 1.00 77.37  ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 268.623 264.699 239.417 1.00 72.30  ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 267.854 264.191 238.286 1.00 66.54  ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 268.629 264.332 236.983 1.00 69.61  ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 268.627 263.420 236.149 1.00 72.43  ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 266.518 264.926 238.195 1.00 70.56  ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 265.602 264.607 239.354 1.00 75.85  ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 265.968 263.749 240.185 1.00 77.32  ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 264.515 265.215 239.437 1.00 71.86  ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 269.294 265.473 236.790 1.00 73.83  ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 270.082 265.674 235.579 1.00 72.28  ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 271.283 264.738 235.541 1.00 72.86  ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 271.660 264.246 234.471 1.00 73.53  ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 270.528 267.131 235.480 1.00 73.88  ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 269.442 268.129 235.072 1.00 69.69  ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 270.025 269.523 234.914 1.00 73.76  ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 268.755 267.681 233.791 1.00 70.92  ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 271.902 264.485 236.698 1.00 74.25  ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 273.018 263.547 236.750 1.00 72.78  ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 272.571 262.139 236.374 1.00 78.28  ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 273.297 261.412 235.687 1.00 79.52  ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 273.651 263.558 238.140 1.00 69.92  ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 271.380 261.736 236.824 1.00 76.37  ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 270.850 260.429 236.447 1.00 70.84  ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 270.582 260.355 234.950 1.00 73.02  ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 270.813 259.315 234.321 1.00 78.04  ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 269.576 260.131 237.237 1.00 74.23  ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 269.833 259.987 238.723 1.00 78.40  ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 271.000 260.129 239.143 1.00 78.45  ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 268.867 259.733 239.473 1.00 78.07  ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 270.089 261.448 234.362 1.00 72.99  ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 269.841 261.477 232.923 1.00 75.62  ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 271.143 261.292 232.154 1.00 77.90  ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 271.192 260.570 231.150 1.00 81.54  ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 269.129 262.786 232.532 1.00 77.80  ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 269.147 262.977 231.026 1.00 77.92  ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 267.702 262.783 233.049 1.00 74.73  ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 272.217 261.938 232.613 1.00 81.45  ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 273.521 261.763 231.979 1.00 79.15  ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 273.966 260.309 232.068 1.00 81.17  ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 274.489 259.744 231.100 1.00 83.53  ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 274.555 262.713 232.613 1.00 81.27  ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 275.937 262.461 232.032 1.00 80.22  ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 274.145 264.160 232.398 1.00 83.36  ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 273.766 259.681 233.230 1.00 81.42  ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 274.162 258.286 233.397 1.00 80.04  ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 273.386 257.370 232.459 1.00 78.43  ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 273.960 256.451 231.862 1.00 80.04  ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 273.967 257.858 234.851 1.00 79.88  ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 274.958 258.484 235.818 1.00 80.22  ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 276.390 258.376 235.335 1.00 84.52  ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 276.899 257.279 235.106 1.00 85.07  ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 277.049 259.518 235.176 1.00 84.20  ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 272.077 257.598 232.319 1.00 76.60  ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 271.279 256.792 231.398 1.00 78.72  ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 271.731 257.021 229.962 1.00 81.27  ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 271.883 256.072 229.184 1.00 83.59  ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 269.780 257.099 231.574 1.00 78.99  ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 268.959 256.315 230.563 1.00 78.77  ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 269.335 256.775 232.987 1.00 78.10  ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 271.954 258.283 229.589 1.00 90.14  ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 272.413 258.593 228.240 1.00 86.82  ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 273.834 258.109 227.987 1.00 87.97  ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 274.223 257.950 226.825 1.00 88.42  ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 272.319 260.098 227.987 1.00 87.47  ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 270.630 260.740 227.942 1.00 86.26  ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 274.615 257.879 229.039 1.00 89.34  ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 275.954 257.322 228.910 1.00 88.07  ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 275.964 255.800 228.941 1.00 90.04  ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 277.032 255.199 228.781 1.00 91.64  ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 276.860 257.861 230.022 1.00 87.96  ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 277.558 259.165 229.682 1.00 88.98  ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 278.381 259.704 230.835 1.00 93.45  ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 278.426 259.044 231.895 1.00 89.36  ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 278.981 260.789 230.683 1.00 93.31  ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 274.812 255.169 229.136 1.00 91.04  ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 274.751 253.721 229.239 1.00 88.10  ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 275.462 253.165 230.453 1.00 88.08  ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 276.095 252.106 230.364 1.00 89.81  ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 275.374 253.855 231.590 1.00 86.48  ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 276.049 253.434 232.808 1.00 88.07  ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 275.092 253.088 233.939 1.00 89.35  ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 275.544 252.607 234.985 1.00 89.45  ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 277.024 254.523 233.277 1.00 88.54  ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 278.010 254.971 232.209 1.00 88.15  ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 279.271 254.123 232.227 1.00 86.92  ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 280.458 254.886 231.659 1.00 88.84  ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 281.089 255.774 232.674 1.00 89.96  ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 273.791 253.319 233.770 1.00 79.64  ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 272.814 252.960 234.786 1.00 76.62  ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 271.511 252.571 234.104 1.00 78.88  ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 271.231 252.992 232.978 1.00 76.98  ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 272.585 254.105 235.782 1.00 76.44  ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 271.496 255.084 235.379 1.00 77.74  ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 271.121 255.998 236.533 1.00 77.08  ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 270.719 255.199 237.762 1.00 76.29  ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 270.339 256.081 238.899 1.00 75.09  ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 270.720 251.756 234.796 1.00 79.30  ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 269.465 251.268 234.246 1.00 78.07  ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 268.387 252.344 234.325 1.00 78.73  ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 268.374 253.178 235.235 1.00 76.67  ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 269.011 250.009 234.988 1.00 74.87  ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 267.762 249.354 234.417 1.00 78.19  ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 267.420 248.069 235.150 1.00 80.13  ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 266.167 247.427 234.577 1.00 78.58  ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 265.813 246.166 235.284 1.00 75.09  ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 267.475 252.314 233.357 1.00 67.45  ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 266.373 253.264 233.292 1.00 64.41  ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 265.200 252.749 234.118 1.00 69.24  ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 264.781 251.597 233.962 1.00 70.54  ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 265.944 253.483 231.841 1.00 66.25  ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 265.135 254.746 231.608 1.00 68.14  ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 265.024 255.098 230.137 1.00 71.99  ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 264.800 256.254 229.778 1.00 71.27  ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 265.177 254.098 229.277 1.00 68.29  ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 264.677 253.602 234.994 1.00 61.85  ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 263.558 253.255 235.855 1.00 55.80  ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 262.272 253.884 235.322 1.00 51.78  ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 262.265 254.589 234.310 1.00 58.37  ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 263.828 253.701 237.294 1.00 55.13  ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 263.787 255.131 237.369 1.00 62.65  ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 265.194 253.215 237.753 1.00 55.60  ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 261.163 253.619 236.018 1.00 50.32  ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 259.882 254.192 235.616 1.00 52.64  ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 259.911 255.712 235.692 1.00 57.53  ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 259.430 256.401 234.785 1.00 58.13  ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 258.755 253.639 236.488 1.00 55.18  ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 258.205 252.330 235.970 1.00 57.00  ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 257.968 252.174 234.772 1.00 58.51  ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 257.981 251.384 236.873 1.00 50.97  ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 260.470 256.257 236.775 1.00 65.66  ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 260.521 257.708 236.914 1.00 60.93  ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 261.507 258.316 235.925 1.00 58.52  ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 261.263 259.400 235.384 1.00 63.17  ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 260.882 258.089 238.351 1.00 59.47  ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 261.490 259.468 238.486 1.00 64.72  ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 260.676 260.583 238.624 1.00 61.86  ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 262.867 259.660 238.461 1.00 64.95  ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 261.208 261.845 238.741 1.00 62.17  ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 263.410 260.925 238.577 1.00 64.31  ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 262.573 262.012 238.718 1.00 66.56  ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 263.091 263.277 238.835 1.00 67.79  ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 262.631 257.635 235.685 1.00 56.98  ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 263.605 258.132 234.719 1.00 55.09  ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 263.027 258.143 233.310 1.00 60.55  ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 263.338 259.034 232.512 1.00 69.53  ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 264.879 257.288 234.775 1.00 62.23  ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 265.813 257.561 235.956 1.00 58.86  ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 267.060 256.696 235.871 1.00 56.81  ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 266.185 259.034 236.015 1.00 57.67  ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 262.189 257.156 232.983 1.00 61.49  ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 261.526 257.149 231.682 1.00 54.18  ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 260.623 258.366 231.525 1.00 57.88  ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 260.599 259.005 230.468 1.00 65.53  ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 260.723 255.859 231.508 1.00 56.14  ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 261.557 254.645 231.144 1.00 60.88  ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 260.678 253.429 230.896 1.00 60.86  ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 260.665 252.521 232.036 1.00 62.80  ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 261.663 251.712 232.365 1.00 65.61  ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 262.772 251.654 231.647 1.00 63.57  ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 261.543 250.939 233.440 1.00 62.97  ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 259.865 258.697 232.573 1.00 63.75  ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 259.012 259.880 232.530 1.00 62.26  ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 259.846 261.152 232.436 1.00 63.83  ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 259.544 262.051 231.642 1.00 64.91  ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 258.106 259.914 233.763 1.00 59.50  ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 257.045 258.965 233.605 1.00 63.31  ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 257.511 261.301 233.959 1.00 63.32  ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 260.911 261.239 233.236 1.00 66.46  ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 261.749 262.434 233.234 1.00 62.79  ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 262.446 262.624 231.892 1.00 61.88  ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 262.494 263.740 231.362 1.00 72.80  ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 262.773 262.354 234.365 1.00 61.90  ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 263.665 263.576 234.585 1.00 57.72  ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 262.905 264.667 235.316 1.00 65.44  ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 264.911 263.184 235.356 1.00 64.99  ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 262.992 261.545 231.328 1.00 60.74  ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 263.690 261.648 230.049 1.00 61.36  ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 262.713 261.980 228.928 1.00 68.05  ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 263.023 262.773 228.031 1.00 73.85  ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 264.472 260.352 229.767 1.00 62.58  ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 265.712 260.282 230.659 1.00 62.63  ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 264.858 260.256 228.299 1.00 64.86  ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 266.433 258.959 230.600 1.00 65.73  ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 261.515 261.390 228.965 1.00 69.71  ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 260.523 261.660 227.928 1.00 66.74  ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 260.132 263.133 227.908 1.00 69.74  ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 259.977 263.727 226.835 1.00 76.59  ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 259.292 260.779 228.140 1.00 69.35  ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 258.368 260.763 226.937 1.00 75.96  ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 258.654 261.377 225.909 1.00 77.26  ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 257.251 260.055 227.061 1.00 74.40  ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 259.959 263.737 229.085 1.00 70.67  ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 259.630 265.157 229.141 1.00 67.24  ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 260.792 266.017 228.659 1.00 67.76  ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 260.585 267.018 227.964 1.00 76.67  ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 259.225 265.546 230.563 1.00 65.94  ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 258.000 264.811 231.077 1.00 69.16  ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 257.410 265.456 232.315 1.00 74.72  ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 256.821 266.550 232.193 1.00 77.11  ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 257.536 264.869 233.410 1.00 73.28  ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 262.022 265.645 229.022 1.00 62.61  ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 263.179 266.453 228.645 1.00 65.86  ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 263.408 266.441 227.138 1.00 70.94  ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 263.689 267.488 226.542 1.00 73.64  ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 264.426 265.964 229.381 1.00 67.40  ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 264.478 266.235 230.886 1.00 68.72  ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 265.886 266.026 231.422 1.00 68.23  ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 263.984 267.639 231.200 1.00 67.53  ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 263.300 265.271 226.504 1.00 73.22  ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 263.523 265.198 225.063 1.00 74.84  ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 262.412 265.912 224.303 1.00 77.87  ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 262.665 266.538 223.266 1.00 75.62  ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 263.679 263.733 224.605 1.00 75.28  ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 264.852 263.080 225.315 1.00 74.31  ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 262.402 262.941 224.847 1.00 72.21  ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 261.173 265.838 224.792 1.00 78.35  ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 260.059 266.497 224.125 1.00 76.70  ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 259.999 267.990 224.433 1.00 76.18  ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 259.342 268.735 223.697 1.00 77.53  ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 258.747 265.806 224.518 1.00 73.67  ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 257.503 266.318 223.806 1.00 79.79  ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 256.273 265.515 224.198 1.00 77.75  ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 255.031 266.030 223.491 1.00 80.31  ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 253.818 265.254 223.867 1.00 79.38  ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 260.690 268.446 225.477 1.00 74.55  ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 260.796 269.859 225.770 1.00 75.36  ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 259.895 270.377 226.869 1.00 73.73  ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 260.041 271.541 227.263 1.00 72.94  ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 258.976 269.566 227.380 1.00 73.14  ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 258.066 270.018 228.426 1.00 73.96  ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 258.757 269.919 229.779 1.00 74.23  ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 259.531 268.988 230.037 1.00 77.11  ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 256.754 269.212 228.391 1.00 76.23  ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 255.706 269.848 229.308 1.00 76.84  ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 256.993 267.756 228.761 1.00 73.56  ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 254.305 269.320 229.096 1.00 73.60  ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 258.506 270.903 230.634 1.00 74.15  ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 259.089 270.910 231.970 1.00 73.47  ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 258.565 269.728 232.779 1.00 74.55  ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 257.352 269.489 232.799 1.00 74.17  ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 258.756 272.217 232.686 1.00 72.62  ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 259.347 272.417 234.083 1.00 72.97  ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 260.868 272.448 234.039 1.00 76.86  ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 258.794 273.677 234.726 1.00 70.79  ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 259.433 268.964 233.441 1.00 71.41  ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 258.944 267.922 234.350 1.00 68.89  ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 258.127 268.524 235.483 1.00 70.80  ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 258.440 269.599 235.998 1.00 77.75  ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 260.231 267.268 234.866 1.00 69.86  ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 261.262 267.593 233.833 1.00 70.18  ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 260.900 268.954 233.327 1.00 70.94  ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 257.071 267.812 235.874 1.00 75.96  ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 256.194 268.282 236.938 1.00 80.10  ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 256.802 268.127 238.324 1.00 81.23  ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 256.277 268.706 239.280 1.00 80.21  ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 254.855 267.542 236.875 1.00 78.23  ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 254.063 267.775 235.592 1.00 79.63  ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 253.402 269.154 235.565 1.00 84.28  ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 254.342 270.242 235.319 1.00 83.27  ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 254.837 270.554 234.129 1.00 84.22  ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 254.492 269.887 233.040 1.00 83.30  ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 255.700 271.561 234.030 1.00 83.07  ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 257.894 267.375 238.455 1.00 74.50  ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 258.572 267.236 239.737 1.00 73.39  ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 259.531 268.383 240.023 1.00 75.95  ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 260.082 268.446 241.127 1.00 76.19  ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 259.329 265.907 239.790 1.00 72.50  ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 260.151 265.743 238.648 1.00 74.10  ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 259.743 269.283 239.063 1.00 71.47  ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 260.623 270.428 239.250 1.00 70.27  ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 259.872 271.727 239.500 1.00 72.39  ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 260.450 272.658 240.071 1.00 72.81  ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 261.529 270.607 238.025 1.00 68.70  ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 262.485 269.476 237.798 1.00 69.00  ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 262.634 268.358 238.566 1.00 73.54  ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 263.418 269.347 236.719 1.00 69.05  ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 263.606 267.545 238.036 1.00 74.53  ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 264.103 268.130 236.902 1.00 72.97  ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 263.743 270.145 235.618 1.00 70.07  ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 265.092 267.692 236.025 1.00 72.00  ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 264.726 269.708 234.749 1.00 69.93  ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 265.389 268.493 234.957 1.00 71.35  ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 258.608 271.812 239.091 1.00 70.42  ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 257.820 273.036 239.218 1.00 72.93  ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 257.295 273.139 240.644 1.00 70.48  ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 256.166 272.749 240.947 1.00 70.58  ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 256.683 273.048 238.203 1.00 73.93  ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 255.956 274.262 238.266 1.00 73.43  ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 258.129 273.675 241.534 1.00 69.93  ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 257.757 273.892 242.926 1.00 68.90  ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 257.420 275.348 243.219 1.00 72.68  ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 257.259 275.715 244.388 1.00 72.74  ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 258.873 273.410 243.854 1.00 69.95  ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 259.024 271.921 243.892 1.00 73.04  ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 258.158 271.069 243.242 1.00 70.80  ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 259.939 271.132 244.504 1.00 73.97  ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 258.532 269.819 243.451 1.00 69.54  ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 259.611 269.830 244.214 1.00 73.57  ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 257.312 276.184 242.189 1.00 74.12  ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 256.903 277.570 242.354 1.00 68.89  ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 256.110 277.988 241.124 1.00 69.10  ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 256.156 277.331 240.081 1.00 73.85  ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 258.104 278.500 242.576 1.00 68.99  ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 259.255 278.285 241.617 1.00 68.50  ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 259.219 278.805 240.330 1.00 68.40  ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 260.381 277.569 242.002 1.00 69.84  ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 260.268 278.615 239.452 1.00 67.62  ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 261.436 277.373 241.129 1.00 69.16  ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 261.374 277.898 239.856 1.00 67.59  ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 262.419 277.708 238.983 1.00 71.61  ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 255.370 279.086 241.264 1.00 70.57  ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 254.504 279.550 240.188 1.00 70.09  ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 255.323 279.949 238.966 1.00 73.79  ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 256.303 280.692 239.077 1.00 72.64  ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 253.667 280.739 240.662 1.00 71.54  ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 252.982 280.396 241.873 1.00 73.29  ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 252.648 281.122 239.601 1.00 69.72  ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 254.914 279.463 237.798 1.00 75.87  ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 255.551 279.833 236.536 1.00 73.47  ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 254.461 280.148 235.517 1.00 72.37  ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 253.341 279.631 235.636 1.00 72.38  ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 256.487 278.722 236.031 1.00 74.99  ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 257.742 278.651 236.888 1.00 71.52  ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 255.769 277.383 236.028 1.00 69.82  ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 254.728 280.992 234.519 1.00 74.43  ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 253.731 281.221 233.467 1.00 73.63  ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 253.395 279.932 232.736 1.00 76.22  ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 254.250 279.067 232.538 1.00 77.05  ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 254.411 282.236 232.540 1.00 69.68  ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 255.856 282.184 232.883 1.00 71.22  ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 255.928 281.823 234.331 1.00 75.28  ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 252.130 279.809 232.342 1.00 83.10  ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 251.679 278.617 231.641 1.00 83.12  ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 252.407 278.476 230.311 1.00 84.40  ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 252.564 279.447 229.566 1.00 82.91  ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 250.168 278.674 231.415 1.00 81.34  ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 252.853 277.258 230.018 1.00 85.82  ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 253.490 276.983 228.747 1.00 86.08  ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 254.942 277.385 228.637 1.00 87.11  ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 255.437 277.580 227.523 1.00 86.70  ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 255.647 277.521 229.758 1.00 81.29  ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 257.086 277.746 229.714 1.00 81.61  ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 257.817 276.459 229.356 1.00 82.72  ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 257.526 275.392 229.906 1.00 82.27  ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 257.600 278.288 231.049 1.00 79.27  ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 259.082 278.637 231.007 1.00 83.00  ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 259.782 279.301 232.527 1.00 83.85  ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 259.060 280.929 232.541 1.00 83.18  ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 258.759 276.560 228.423 1.00 74.23  ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 259.586 275.418 228.072 1.00 72.03  ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 260.598 275.138 229.183 1.00 71.67  ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 260.818 275.950 230.086 1.00 73.79  ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 260.303 275.658 226.743 1.00 77.23  ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 261.450 276.491 226.955 1.00 75.83  ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 259.366 276.333 225.746 1.00 75.06  ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 261.216 273.958 229.111 1.00 74.85  ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 262.195 273.583 230.125 1.00 72.95  ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 263.436 274.467 230.038 1.00 73.99  ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 264.054 274.779 231.063 1.00 78.42  ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 262.540 272.085 230.008 1.00 72.67  ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 263.126 271.767 228.642 1.00 71.55  ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 263.490 271.663 231.121 1.00 72.89  ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 263.818 274.888 228.829 1.00 72.05  ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 265.006 275.724 228.671 1.00 70.68  ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 264.825 277.056 229.388 1.00 69.23  ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 265.728 277.523 230.094 1.00 70.28  ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 265.333 275.928 227.179 1.00 73.45  ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 265.670 274.599 226.493 1.00 73.10  ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 266.478 276.916 227.012 1.00 74.07  ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 264.476 273.864 225.917 1.00 71.07  ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 263.662 277.689 229.223 1.00 71.01  ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 263.405 278.953 229.907 1.00 71.88  ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 263.369 278.764 231.418 1.00 73.22  ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 263.869 279.610 232.169 1.00 75.60  ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 262.095 279.564 229.410 1.00 70.34  ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 261.971 279.644 227.898 1.00 74.14  ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 260.602 280.120 227.451 1.00 75.63  ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 259.580 279.541 227.820 1.00 76.54  ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 260.575 281.181 226.653 1.00 73.87  ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 262.772 277.663 231.884 1.00 68.54  ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 262.723 277.397 233.318 1.00 64.78  ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 264.117 277.178 233.891 1.00 65.73  ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 264.424 277.651 234.991 1.00 74.18  ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 261.829 276.190 233.599 1.00 63.95  ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 261.620 275.924 235.060 1.00 67.40  ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 260.600 276.385 235.840 1.00 67.12  ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 262.445 275.120 235.913 1.00 67.77  ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 260.743 275.925 237.127 1.00 69.50  ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 261.868 275.146 237.198 1.00 68.80  ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 263.617 274.384 235.716 1.00 65.80  ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 262.422 274.465 238.279 1.00 66.91  ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 264.166 273.709 236.790 1.00 63.94  ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 263.569 273.755 238.055 1.00 67.57  ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 264.974 276.458 233.163 1.00 62.91  ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 266.331 276.208 233.644 1.00 66.28  ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 267.097 277.517 233.782 1.00 69.28  ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 267.788 277.747 234.782 1.00 71.87  ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 267.055 275.220 232.710 1.00 68.36  ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 268.560 275.290 232.919 1.00 69.39  ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 266.549 273.805 232.942 1.00 68.30  ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 266.985 278.397 232.784 1.00 69.46  ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 267.630 279.703 232.874 1.00 65.35  ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 267.055 280.524 234.021 1.00 66.57  ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 267.799 281.182 234.758 1.00 68.94  ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 267.484 280.452 231.550 1.00 66.95  ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 268.088 279.733 230.490 1.00 66.55  ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 265.729 280.505 234.184 1.00 72.25  ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 265.110 281.215 235.298 1.00 70.68  ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 265.515 280.606 236.634 1.00 72.45  ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 265.778 281.331 237.601 1.00 77.60  ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 263.589 281.210 235.145 1.00 70.99  ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 262.913 282.260 236.005 1.00 76.86  ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 263.628 283.075 236.625 1.00 78.20  ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 261.665 282.270 236.062 1.00 74.81  ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 265.569 279.274 236.708 1.00 66.18  ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 265.953 278.612 237.951 1.00 64.08  ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 267.386 278.954 238.339 1.00 63.84  ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 267.689 279.137 239.524 1.00 68.29  ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 265.780 277.100 237.817 1.00 65.93  ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 266.154 276.334 239.053 1.00 70.28  ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 265.500 276.564 240.251 1.00 67.85  ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 267.159 275.382 239.015 1.00 65.02  ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 265.841 275.860 241.390 1.00 64.97  ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 267.505 274.675 240.150 1.00 64.55  ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 266.845 274.914 241.338 1.00 68.70  ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 268.284 279.034 237.355 1.00 64.23  ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 269.672 279.381 237.645 1.00 65.54  ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 269.780 280.782 238.234 1.00 69.23  ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 270.555 281.012 239.169 1.00 68.72  ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 270.517 279.264 236.377 1.00 67.11  ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 270.320 278.010 235.748 1.00 70.01  ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 269.012 281.733 237.697 1.00 73.79  ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 269.033 283.091 238.232 1.00 69.51  ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 268.498 283.132 239.658 1.00 72.41  ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 269.023 283.867 240.504 1.00 71.87  ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 268.225 284.024 237.329 1.00 68.01  ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 268.773 284.152 235.919 1.00 72.48  ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 267.943 285.080 235.054 1.00 76.55  ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 266.746 284.790 234.848 1.00 77.02  ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 268.487 286.099 234.580 1.00 72.11  ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 267.448 282.358 239.941 1.00 68.89  ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 266.887 282.331 241.288 1.00 64.20  ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 267.891 281.785 242.296 1.00 67.84  ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 268.001 282.300 243.415 1.00 68.17  ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 265.604 281.500 241.307 1.00 63.19  ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 264.488 282.066 240.448 1.00 63.53  ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 263.231 281.219 240.549 1.00 63.57  ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 262.145 281.757 239.739 1.00 64.80  ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 260.992 282.192 240.227 1.00 68.78  ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 260.738 282.169 241.525 1.00 67.59  ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 260.071 282.664 239.391 1.00 67.42  ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 268.629 280.739 241.919 1.00 69.14  ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 269.620 280.166 242.825 1.00 65.93  ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 270.761 281.149 243.061 1.00 67.59  ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 271.294 281.246 244.173 1.00 73.01  ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 270.127 278.820 242.277 1.00 65.23  ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 268.977 277.815 242.196 1.00 64.36  ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 271.235 278.265 243.155 1.00 65.69  ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 268.209 277.661 243.490 1.00 65.16  ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 271.150 281.896 242.024 1.00 66.66  ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 272.196 282.901 242.190 1.00 64.46  ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 271.774 283.977 243.180 1.00 65.16  ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 272.583 284.433 243.997 1.00 71.82  ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 272.551 283.523 240.839 1.00 65.80  ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 273.267 282.582 239.885 1.00 66.15  ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 273.641 283.292 238.594 1.00 65.10  ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 274.418 282.376 237.663 1.00 67.58  ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 273.564 281.285 237.119 1.00 69.34  ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 270.510 284.405 243.118 1.00 63.34  ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 270.004 285.350 244.108 1.00 63.93  ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 270.022 284.742 245.504 1.00 67.02  ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 270.388 285.412 246.477 1.00 69.95  ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 268.590 285.797 243.736 1.00 66.05  ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 267.873 286.557 244.839 1.00 66.86  ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 266.514 287.070 244.409 1.00 66.81  ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 266.247 288.270 244.458 1.00 68.53  ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 265.645 286.160 243.986 1.00 71.14  ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 269.633 283.470 245.621 1.00 70.33  ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 269.673 282.799 246.917 1.00 65.05  ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 271.104 282.662 247.422 1.00 64.83  ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 271.360 282.785 248.625 1.00 71.51  ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 269.001 281.430 246.819 1.00 66.05  ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 267.492 281.441 246.569 1.00 68.70  ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 266.923 280.035 246.656 1.00 67.64  ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 266.789 282.368 247.549 1.00 66.38  ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 272.049 282.398 246.517 1.00 65.22  ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 273.453 282.331 246.911 1.00 66.08  ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 273.945 283.676 247.428 1.00 69.47  ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 274.686 283.737 248.416 1.00 73.14  ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 274.308 281.863 245.734 1.00 65.92  ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 274.285 280.362 245.508 1.00 67.96  ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 275.095 279.943 244.299 1.00 71.12  ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 275.538 280.780 243.513 1.00 67.89  ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 275.298 278.640 244.146 1.00 74.39  ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 273.550 284.767 246.767 1.00 65.70  ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 273.935 286.095 247.234 1.00 65.77  ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 273.314 286.405 248.590 1.00 68.33  ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 273.961 287.009 249.454 1.00 72.38  ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 273.534 287.150 246.204 1.00 67.93  ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 274.283 286.999 244.895 1.00 72.26  ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 275.095 286.089 244.733 1.00 73.82  ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 274.012 287.894 243.952 1.00 70.58  ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 272.056 286.007 248.792 1.00 71.41  ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 271.409 286.209 250.086 1.00 69.31  ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 272.108 285.390 251.163 1.00 73.44  ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 272.347 285.875 252.276 1.00 75.88  ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 269.910 285.867 249.993 1.00 70.21  ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 269.189 286.867 249.088 1.00 72.69  ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 269.277 285.848 251.376 1.00 67.85  ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 267.730 286.541 248.858 1.00 74.56  ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 272.447 284.137 250.851 1.00 76.67  ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 273.143 283.294 251.817 1.00 74.50  ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 274.523 283.849 252.145 1.00 75.75  ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 274.960 283.799 253.301 1.00 77.77  ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 273.250 281.865 251.285 1.00 73.17  ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 274.161 281.791 250.202 1.00 78.72  ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 275.229 284.371 251.139 1.00 78.61  ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 276.541 284.961 251.383 1.00 79.55  ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 276.432 286.188 252.281 1.00 82.45  ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 277.234 286.362 253.207 1.00 82.50  ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 277.203 285.321 250.051 1.00 79.14  ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 278.396 286.282 250.027 1.00 83.05  ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 279.502 285.835 250.977 1.00 81.66  ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 278.930 286.433 248.610 1.00 81.66  ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 275.444 287.049 252.026 1.00 87.53  ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 275.272 288.244 252.846 1.00 86.59  ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 274.860 287.889 254.270 1.00 88.54  ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 275.350 288.491 255.232 1.00 89.79  ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 274.245 289.176 252.206 1.00 84.71  ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 273.954 286.920 254.423 1.00 85.26  ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 273.507 286.528 255.756 1.00 86.55  ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 274.637 285.901 256.563 1.00 89.49  ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 274.774 286.170 257.763 1.00 90.12  ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 272.325 285.565 255.652 1.00 86.88  ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 275.451 285.056 255.926 1.00 93.27  ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 276.539 284.393 256.639 1.00 92.18  ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 277.575 285.397 257.131 1.00 92.79  ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 278.060 285.294 258.264 1.00 91.34  ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 277.192 283.343 255.742 1.00 88.95  ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 277.926 286.372 256.297 1.00 97.77  ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 278.921 287.389 256.628 1.00 97.85  ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 278.216 288.741 256.675 1.00 97.54  ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 278.103 289.433 255.660 1.00 96.30  ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 280.067 287.386 255.616 1.00 97.12  ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 280.698 286.118 255.564 1.00 98.29  ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 277.743 289.116 257.861 1.00 101.62 ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 277.065 290.385 258.036 1.00 100.87 ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 275.878 290.307 258.973 1.00 102.46 ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 275.311 291.335 259.354 1.00 102.59 ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 275.492 289.092 259.349 1.00 101.67 ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 274.376 288.904 260.249 1.00 100.86 ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 273.038 289.169 259.585 1.00 101.73 ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 272.912 289.270 258.361 1.00 100.09 ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 272.013 289.284 260.431 1.00 101.62 ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 270.660 289.540 259.957 1.00 102.57 ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 270.426 290.996 259.580 1.00 103.61 ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 269.427 291.291 258.916 1.00 102.66 ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 269.642 289.117 261.020 1.00 102.19 ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 271.311 291.909 259.990 1.00 104.59 ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 271.153 293.311 259.617 1.00 105.50 ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 271.299 293.504 258.113 1.00 103.96 ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 270.571 294.302 257.510 1.00 103.40 ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 272.163 294.175 260.371 1.00 103.36 ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 272.053 295.659 260.061 1.00 103.61 ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 270.768 296.246 260.623 1.00 103.42 ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 270.707 297.750 260.408 1.00 102.74 ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 269.423 298.328 260.893 1.00 102.69 ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 272.236 292.785 257.489 1.00 101.62 ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 272.417 292.893 256.047 1.00 102.85 ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 271.198 292.410 255.274 1.00 102.73 ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 270.943 292.908 254.173 1.00 104.01 ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 273.653 292.108 255.606 1.00 103.35 ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 274.971 292.724 256.040 1.00 103.90 ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 276.141 292.231 255.213 1.00 104.16 ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 275.912 291.449 254.266 1.00 102.18 ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 277.288 292.626 255.508 1.00 103.17 ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 270.437 291.461 255.827 1.00 91.55  ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 269.249 290.964 255.140 1.00 92.91  ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 268.235 292.072 254.894 1.00 92.79  ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 267.442 291.987 253.949 1.00 93.06  ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 268.612 289.833 255.948 1.00 91.77  ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 269.403 288.526 256.023 1.00 92.70  ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 268.596 287.451 256.732 1.00 89.86  ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 269.804 288.067 254.631 1.00 91.60  ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 268.240 293.111 255.729 1.00 87.07  ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 267.345 294.242 255.519 1.00 85.20  ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 267.836 295.144 254.392 1.00 86.24  ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 267.026 295.765 253.694 1.00 88.09  ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 267.197 295.035 256.820 1.00 86.26  ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 266.101 296.089 256.796 1.00 85.74  ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 266.667 297.462 256.479 1.00 86.21  ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 265.576 298.424 256.054 1.00 85.01  ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 266.154 299.663 255.470 1.00 87.01  ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 269.152 295.224 254.192 1.00 91.30  ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 269.751 296.164 253.253 1.00 91.91  ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 270.185 295.502 251.948 1.00 91.73  ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 271.141 295.958 251.312 1.00 92.05  ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 270.935 296.877 253.905 1.00 91.64  ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 270.514 297.783 255.044 1.00 93.69  ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 270.901 297.575 256.194 1.00 91.06  ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 269.714 298.796 254.730 1.00 94.90  ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 269.507 294.436 251.535 1.00 86.16  ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 269.764 293.805 250.247 1.00 86.81  ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 268.606 294.108 249.308 1.00 86.52  ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 267.448 294.228 249.725 1.00 87.53  ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 269.984 292.282 250.377 1.00 85.46  ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 268.734 291.598 250.937 1.00 85.40  ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 271.215 291.983 251.216 1.00 85.96  ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 268.786 290.089 250.877 1.00 86.16  ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 268.926 294.246 248.025 1.00 79.18  ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 267.919 294.445 246.993 1.00 75.80  ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 267.457 293.086 246.485 1.00 78.51  ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 268.275 292.266 246.054 1.00 82.12  ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 268.475 295.292 245.849 1.00 75.79  ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 268.872 296.676 246.263 1.00 78.06  ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 268.637 297.170 247.528 1.00 77.45  ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 269.489 297.668 245.580 1.00 78.45  ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 269.091 298.408 247.606 1.00 78.66  ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 269.613 298.734 246.437 1.00 78.97  ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 266.150 292.853 246.536 1.00 68.13  ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 265.570 291.538 246.295 1.00 66.44  ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 264.763 291.584 245.006 1.00 69.72  ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 263.910 292.461 244.832 1.00 74.65  ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 264.687 291.090 247.474 1.00 69.12  ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 263.960 289.806 247.131 1.00 68.49  ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 265.527 290.915 248.728 1.00 77.80  ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 265.030 290.638 244.109 1.00 69.31  ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 264.241 290.485 242.892 1.00 66.67  ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 262.967 289.724 243.238 1.00 68.65  ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 263.018 288.538 243.580 1.00 66.27  ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 265.046 289.760 241.817 1.00 69.70  ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 264.143 289.457 240.281 1.00 82.26  ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 261.823 290.409 243.157 1.00 69.78  ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 260.559 289.789 243.544 1.00 68.26  ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 260.205 288.627 242.625 1.00 66.70  ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 259.661 287.613 243.077 1.00 70.04  ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 259.443 290.834 243.546 1.00 66.86  ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 259.173 291.528 244.882 1.00 66.35  ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 257.879 292.323 244.820 1.00 66.67  ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 259.131 290.518 246.018 1.00 65.89  ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 260.496 288.760 241.330 1.00 65.48  ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 260.199 287.684 240.400 1.00 70.97  ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 260.971 286.412 240.687 1.00 72.20  ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 260.457 285.310 240.478 1.00 69.19  ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 262.210 286.541 241.166 1.00 67.91  ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 263.022 285.372 241.456 1.00 64.13  ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 262.668 284.673 242.751 1.00 64.74  ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 263.099 283.535 242.965 1.00 68.46  ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 261.902 285.324 243.620 1.00 67.66  ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 261.516 284.711 244.883 1.00 68.68  ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 260.529 283.574 244.653 1.00 71.85  ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 259.657 283.652 243.783 1.00 76.15  ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 260.899 285.752 245.814 1.00 67.31  ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 261.839 286.823 246.363 1.00 69.78  ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 261.128 287.625 247.432 1.00 69.86  ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 263.108 286.194 246.915 1.00 69.04  ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 260.674 282.507 245.442 1.00 74.14  ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 259.729 281.399 245.360 1.00 71.55  ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 258.342 281.826 245.824 1.00 74.38  ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 257.336 281.483 245.191 1.00 75.16  ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 260.228 280.208 246.183 1.00 73.54  ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 261.383 279.463 245.556 1.00 74.52  ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 262.315 280.116 244.763 1.00 71.78  ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 261.531 278.102 245.763 1.00 75.47  ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 263.368 279.428 244.193 1.00 70.91  ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 262.582 277.409 245.195 1.00 77.89  ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 263.501 278.073 244.409 1.00 77.36  ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 258.268 282.572 246.922 1.00 77.87  ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 257.005 283.116 247.416 1.00 73.92  ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 257.201 284.615 247.618 1.00 75.49  ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 257.605 285.047 248.707 1.00 74.90  ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 256.554 282.416 248.709 1.00 75.64  ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 255.290 283.065 249.260 1.00 78.40  ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 256.330 280.931 248.462 1.00 76.44  ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 256.969 285.436 246.589 1.00 76.84  ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 257.209 286.881 246.747 1.00 75.73  ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 256.332 287.533 247.801 1.00 75.10  ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 256.764 288.496 248.446 1.00 78.22  ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 256.926 287.435 245.344 1.00 73.02  ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 256.004 286.439 244.723 1.00 74.33  ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 256.421 285.103 245.264 1.00 73.13  ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 255.106 287.039 247.995 1.00 75.64  ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 254.199 287.677 248.943 1.00 75.78  ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 254.671 287.514 250.381 1.00 74.06  ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 254.407 288.381 251.222 1.00 76.15  ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 252.786 287.119 248.772 1.00 77.07  ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 251.755 287.753 249.691 1.00 81.58  ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 251.540 289.223 249.399 1.00 83.28  ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 251.780 289.642 248.249 1.00 78.72  ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 251.133 289.962 250.320 1.00 80.89  ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 255.373 286.420 250.685 1.00 73.42  ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 255.906 286.246 252.031 1.00 72.29  ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 256.935 287.320 252.356 1.00 75.46  ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 257.029 287.774 253.502 1.00 77.23  ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 256.514 284.852 252.183 1.00 71.24  ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 257.720 287.737 251.358 1.00 71.85  ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 258.690 288.806 251.574 1.00 68.90  ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 258.002 290.115 251.938 1.00 69.91  ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 258.438 290.814 252.860 1.00 77.85  ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 259.555 288.992 250.329 1.00 71.06  ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 260.557 290.118 250.443 1.00 71.99  ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 261.699 289.980 251.220 1.00 71.76  ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 260.361 291.319 249.773 1.00 70.23  ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 262.618 291.006 251.327 1.00 72.45  ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 261.275 292.350 249.875 1.00 68.97  ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 262.401 292.188 250.653 1.00 72.12  ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 263.314 293.212 250.757 1.00 69.33  ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 256.928 290.463 251.226 1.00 63.37  ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 256.201 291.693 251.531 1.00 65.90  ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 255.631 291.633 252.941 1.00 71.54  ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 255.680 292.616 253.691 1.00 77.22  ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 255.101 291.939 250.482 1.00 70.07  ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 255.662 291.761 249.070 1.00 72.78  ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 254.505 293.327 250.650 1.00 68.34  ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 256.774 292.728 248.728 1.00 69.96  ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 255.076 290.481 253.321 1.00 73.75  ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 254.601 290.303 254.689 1.00 71.93  ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 255.759 290.340 255.681 1.00 71.80  ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 255.643 290.933 256.760 1.00 73.74  ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 253.827 288.989 254.806 1.00 72.74  ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 252.619 289.077 254.040 1.00 75.28  ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 253.468 288.703 256.254 1.00 69.48  ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 256.888 289.718 255.328 1.00 73.37  ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 258.041 289.701 256.226 1.00 71.13  ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 258.586 291.104 256.459 1.00 75.63  ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 258.936 291.458 257.591 1.00 80.12  ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 259.132 288.789 255.667 1.00 72.75  ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 258.677 291.915 255.401 1.00 73.70  ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 259.105 293.300 255.571 1.00 69.19  ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 258.099 294.083 256.403 1.00 73.35  ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 258.479 294.952 257.197 1.00 79.53  ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 259.309 293.965 254.210 1.00 71.85  ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 258.079 293.944 253.474 1.00 71.84  ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 260.386 293.241 253.418 1.00 73.90  ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 256.807 293.794 256.228 1.00 70.42  ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 255.785 294.429 257.052 1.00 73.02  ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 255.957 294.060 258.520 1.00 74.17  ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 255.800 294.910 259.405 1.00 72.34  ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 254.396 294.027 256.555 1.00 76.12  ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 253.245 294.747 257.236 1.00 72.46  ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 251.931 294.033 256.967 1.00 70.67  ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 250.782 294.794 257.442 1.00 74.05  ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 249.764 295.166 256.677 1.00 75.08  ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 249.719 294.861 255.391 1.00 76.40  ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 248.766 295.860 257.217 1.00 75.53  ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 256.274 292.794 258.798 1.00 79.02  ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 256.475 292.363 260.178 1.00 74.63  ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 257.692 293.037 260.799 1.00 75.67  ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 257.662 293.428 261.972 1.00 79.85  ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 256.612 290.842 260.236 1.00 70.84  ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 256.279 290.242 261.591 1.00 77.34  ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 255.927 288.770 261.507 1.00 74.65  ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 255.794 288.214 260.417 1.00 72.12  ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 255.774 288.131 262.660 1.00 74.32  ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 258.776 293.175 260.031 1.00 73.94  ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 259.998 293.770 260.567 1.00 75.02  ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 259.779 295.225 260.964 1.00 76.92  ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 260.249 295.664 262.021 1.00 78.11  ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 261.129 293.642 259.543 1.00 73.45  ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 262.311 294.569 259.755 1.00 73.77  ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 262.307 295.868 259.257 1.00 74.78  ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 263.451 294.128 260.413 1.00 73.15  ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 263.387 296.708 259.441 1.00 77.09  ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 264.537 294.962 260.602 1.00 73.41  ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 264.500 296.250 260.112 1.00 77.90  ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 265.579 297.083 260.294 1.00 81.64  ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 259.077 295.991 260.126 1.00 72.92  ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 258.849 297.404 260.421 1.00 73.47  ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 257.993 297.557 261.671 1.00 77.69  ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 258.282 298.386 262.543 1.00 79.91  ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 258.211 298.107 259.209 1.00 72.19  ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 257.858 299.545 259.554 1.00 72.17  ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 259.149 298.059 258.017 1.00 76.92  ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 256.926 296.762 261.779 1.00 79.52  ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 256.048 296.856 262.940 1.00 75.51  ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 256.776 296.469 264.221 1.00 76.27  ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 256.606 297.117 265.260 1.00 81.40  ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 254.815 295.977 262.734 1.00 76.42  ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 257.588 295.411 264.167 1.00 76.24  ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 258.337 294.992 265.348 1.00 73.56  ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 259.361 296.043 265.759 1.00 76.33  ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 259.529 296.322 266.952 1.00 77.12  ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 259.020 293.651 265.087 1.00 71.06  ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 258.068 292.468 265.035 1.00 72.85  ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 258.794 291.137 265.023 1.00 77.33  ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 260.024 291.088 265.028 1.00 78.46  ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 258.034 290.048 265.007 1.00 74.11  ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 260.059 296.634 264.786 1.00 76.96  ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 261.076 297.631 265.105 1.00 76.72  ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 260.453 298.915 265.638 1.00 79.08  ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 260.974 299.518 266.584 1.00 76.76  ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 261.931 297.921 263.872 1.00 74.66  ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 259.342 299.350 265.048 1.00 81.41  ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 258.697 300.599 265.426 1.00 78.19  ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 257.606 300.419 266.474 1.00 83.31  ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 256.928 301.396 266.811 1.00 83.05  ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 258.111 301.284 264.187 1.00 76.99  ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 259.169 301.633 263.159 1.00 83.37  ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 259.884 300.761 262.666 1.00 85.13  ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 259.274 302.915 262.831 1.00 81.53  ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 257.422 299.201 266.991 1.00 87.10  ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 256.409 298.911 268.008 1.00 83.69  ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 255.009 299.290 267.528 1.00 86.08  ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 254.180 299.782 268.295 1.00 84.81  ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 256.737 299.605 269.333 1.00 83.21  ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 255.745 299.337 270.308 1.00 84.46  ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 254.747 299.060 266.246 1.00 88.37  ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 253.446 299.317 265.648 1.00 84.71  ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 252.718 298.002 265.401 1.00 88.62  ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 253.327 296.930 265.375 1.00 90.45  ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 253.590 300.087 264.333 1.00 84.72  ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 254.162 301.463 264.495 1.00 85.75  ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 254.146 302.231 265.622 1.00 87.50  ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 254.837 302.234 263.494 1.00 88.35  ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 254.768 303.433 265.385 1.00 88.85  ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 255.202 303.459 264.085 1.00 90.28  ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 255.170 302.007 262.154 1.00 86.27  ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 255.881 304.454 263.385 1.00 89.69  ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 255.843 302.996 261.461 1.00 86.00  ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 256.192 304.204 262.077 1.00 88.08  ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 251.402 298.092 265.237 1.00 88.74  ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 250.616 296.911 264.912 1.00 91.29  ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 250.703 296.611 263.419 1.00 91.79  ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 250.886 297.509 262.592 1.00 91.11  ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 249.160 297.103 265.331 1.00 90.35  ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 248.437 295.891 265.218 1.00 90.08  ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 250.573 295.326 263.076 1.00 82.90  ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 250.729 294.913 261.684 1.00 81.21  ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 249.657 295.525 260.790 1.00 81.36  ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 249.958 295.997 259.687 1.00 86.56  ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 250.705 293.387 261.574 1.00 81.38  ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 251.857 292.615 262.219 1.00 82.93  ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 251.613 291.118 262.142 1.00 83.40  ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 253.166 292.970 261.544 1.00 81.51  ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 248.401 295.529 261.243 1.00 81.86  ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 247.324 296.038 260.401 1.00 85.11  ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 247.402 297.546 260.206 1.00 85.04  ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 246.850 298.060 259.228 1.00 86.04  ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 245.959 295.661 260.982 1.00 81.03  ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 245.559 296.446 262.221 1.00 82.71  ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 245.999 295.781 263.507 1.00 85.40  ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 246.812 294.835 263.443 1.00 84.83  ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 245.537 296.209 264.585 1.00 84.54  ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 248.072 298.265 261.109 1.00 85.88  ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 248.186 299.713 260.988 1.00 89.45  ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 249.191 300.143 259.929 1.00 93.36  ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 249.230 301.330 259.586 1.00 94.55  ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 248.575 300.322 262.336 1.00 90.77  ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 247.565 300.081 263.445 1.00 92.52  ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 248.123 300.404 264.817 1.00 94.64  ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 249.322 300.743 264.907 1.00 94.98  ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 247.364 300.318 265.805 1.00 91.25  ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 249.997 299.223 259.406 1.00 87.24  ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 251.030 299.580 258.445 1.00 84.10  ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 250.450 299.694 257.041 1.00 87.84  ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 249.570 298.922 256.649 1.00 87.29  ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 252.156 298.546 258.461 1.00 84.94  ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 252.947 298.387 259.761 1.00 83.24  ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 254.326 297.818 259.475 1.00 87.04  ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 253.060 299.711 260.498 1.00 85.62  ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 250.955 300.666 256.285 1.00 87.72  ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 250.569 300.874 254.898 1.00 85.65  ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 251.822 300.952 254.038 1.00 88.34  ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 252.874 301.412 254.489 1.00 89.07  ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 249.734 302.151 254.730 1.00 83.96  ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 249.154 302.450 253.044 1.00 93.85  ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 251.699 300.502 252.794 1.00 85.59  ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 252.825 300.433 251.873 1.00 84.39  ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 252.786 301.597 250.891 1.00 84.94  ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 251.753 301.868 250.272 1.00 83.64  ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 252.819 299.106 251.111 1.00 82.28  ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 254.106 298.729 250.375 1.00 80.32  ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 255.284 298.651 251.334 1.00 82.33  ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 253.933 297.415 249.626 1.00 82.51  ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 253.920 302.283 250.754 1.00 86.83  ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 254.079 303.365 249.793 1.00 85.93  ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 255.292 303.076 248.922 1.00 84.83  ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 256.297 302.542 249.399 1.00 86.74  ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 254.232 304.725 250.490 1.00 87.20  ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 254.358 305.906 249.534 1.00 92.23  ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 253.102 306.131 248.710 1.00 92.82  ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 252.009 305.743 249.172 1.00 90.70  ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 253.209 306.694 247.600 1.00 90.07  ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 255.192 303.428 247.644 1.00 80.78  ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 256.156 303.023 246.629 1.00 80.48  ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 256.966 304.235 246.191 1.00 81.10  ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 256.408 305.316 245.967 1.00 81.04  ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 255.444 302.366 245.436 1.00 79.92  ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 256.429 302.032 244.325 1.00 79.73  ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 254.715 301.130 245.913 1.00 83.83  ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 258.280 304.049 246.060 1.00 79.67  ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 259.186 305.095 245.596 1.00 76.39  ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 260.201 304.469 244.653 1.00 78.64  ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 260.949 303.572 245.053 1.00 79.86  ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 259.895 305.778 246.769 1.00 75.94  ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 260.558 307.086 246.372 1.00 81.00  ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 261.447 307.113 245.521 1.00 85.89  ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 260.137 308.177 247.001 1.00 79.90  ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 260.236 304.945 243.412 1.00 78.43  ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 261.140 304.419 242.395 1.00 81.03  ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 262.285 305.404 242.213 1.00 82.30  ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 262.062 306.576 241.885 1.00 80.17  ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 260.408 304.170 241.068 1.00 78.90  ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 261.374 303.622 240.032 1.00 78.68  ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 259.244 303.215 241.279 1.00 78.01  ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 263.511 304.928 242.416 1.00 90.61  ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 264.714 305.743 242.298 1.00 90.41  ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 265.568 305.195 241.165 1.00 89.79  ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 265.821 303.987 241.102 1.00 87.72  ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 265.504 305.754 243.608 1.00 90.15  ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 265.837 304.410 243.977 1.00 91.35  ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 264.685 306.392 244.719 1.00 87.97  ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 266.009 306.085 240.271 1.00 102.39 ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 266.833 305.659 239.144 1.00 106.12 ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 268.166 305.090 239.615 1.00 104.17 ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 268.640 304.078 239.085 1.00 101.45 ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 267.060 306.830 238.187 1.00 104.99 ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 265.797 307.386 237.802 1.00 102.87 ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 267.802 306.366 236.943 1.00 102.64 ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 268.784 305.723 240.610 1.00 108.74 ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 270.075 305.272 241.111 1.00 109.48 ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 269.924 304.020 241.965 1.00 109.24 ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 269.528 304.101 243.132 1.00 108.23 ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 270.754 306.383 241.916 1.00 107.69 ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 270.003 306.706 243.074 1.00 106.61 ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 270.230 302.859 241.390 1.00 103.60 ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 270.198 301.619 242.148 1.00 102.61 ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 271.283 301.627 243.222 1.00 103.61 ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 272.336 302.254 243.079 1.00 101.44 ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 270.381 300.415 241.222 1.00 101.15 ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 269.423 300.379 240.041 1.00 102.11 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 269.967 301.101 238.823 1.00 103.89 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 271.033 301.715 238.876 1.00 104.14 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 269.237 301.029 237.717 1.00 102.68 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 271.012 300.915 244.313 1.00 105.89 ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 271.920 300.902 245.440 1.00 104.98 ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 271.793 302.082 246.374 1.00 107.69 ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 272.650 302.253 247.249 1.00 107.93 ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 270.758 302.905 246.214 1.00 109.38 ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 270.570 304.054 247.089 1.00 108.84 ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 270.279 303.600 248.513 1.00 108.34 ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 269.736 302.514 248.739 1.00 107.21 ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 269.432 304.934 246.571 1.00 105.50 ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 270.652 304.439 249.477 1.00 102.88 ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 270.476 304.097 250.882 1.00 103.56 ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 268.998 303.944 251.222 1.00 104.57 ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 268.166 304.765 250.826 1.00 101.89 ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 271.110 305.167 251.770 1.00 104.08 ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 270.410 306.406 251.603 1.00 104.89 ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 272.573 305.364 251.402 1.00 102.32 ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 268.679 302.886 251.961 1.00 98.30  ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 267.324 302.621 252.423 1.00 95.66  ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 267.220 302.997 253.894 1.00 95.13  ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 268.105 302.658 254.687 1.00 94.92  ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 266.958 301.147 252.231 1.00 93.87  ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 267.359 300.473 250.918 1.00 92.35  ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 266.986 298.999 250.943 1.00 94.11  ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 266.714 301.166 249.732 1.00 91.25  ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 266.146 303.694 254.258 1.00 90.17  ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 265.970 304.070 255.651 1.00 90.95  ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 265.488 302.869 256.466 1.00 93.36  ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 265.467 301.728 255.995 1.00 94.45  ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 265.025 305.273 255.774 1.00 88.13  ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 263.547 304.907 255.649 1.00 92.52  ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 263.207 303.783 255.231 1.00 95.60  ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 262.707 305.771 255.979 1.00 92.23  ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 265.099 303.140 257.714 1.00 91.93  ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 264.732 302.064 258.630 1.00 93.36  ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 263.546 301.254 258.116 1.00 93.02  ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 263.429 300.059 258.410 1.00 92.81  ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 264.425 302.639 260.013 1.00 91.64  ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 262.656 301.882 257.349 1.00 86.74  ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 261.421 301.241 256.918 1.00 87.18  ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 261.319 301.069 255.405 1.00 86.77  ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 260.252 300.693 254.911 1.00 89.75  ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 260.216 302.031 257.434 1.00 88.16  ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 260.240 303.789 257.017 1.00 89.49  ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 262.391 301.324 254.660 1.00 80.96  ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 262.381 301.179 253.209 1.00 78.40  ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 263.091 299.894 252.808 1.00 78.69  ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 264.152 299.570 253.350 1.00 84.28  ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 263.044 302.376 252.525 1.00 81.54  ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 262.268 303.550 252.686 1.00 81.77  ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 262.503 299.170 251.859 1.00 73.98  ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 263.092 297.958 251.306 1.00 71.91  ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 263.163 298.092 249.793 1.00 74.78  ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 262.206 298.552 249.161 1.00 78.93  ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 262.286 296.714 251.690 1.00 70.44  ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 262.172 296.495 253.171 1.00 74.67  ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 261.260 297.214 253.926 1.00 75.48  ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 262.986 295.576 253.811 1.00 75.47  ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 261.157 297.015 255.286 1.00 75.65  ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 262.887 295.373 255.172 1.00 74.63  ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 261.972 296.094 255.910 1.00 77.78  ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 264.292 297.691 249.218 1.00 70.30  ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 264.485 297.805 247.787 1.00 67.49  ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 264.193 296.525 247.035 1.00 68.18  ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 264.807 295.487 247.299 1.00 71.91  ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 263.254 296.585 246.095 1.00 65.67  ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 262.911 295.456 245.239 1.00 65.64  ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 263.214 295.839 243.797 1.00 66.12  ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 262.860 296.937 243.348 1.00 69.18  ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 261.443 295.025 245.421 1.00 61.39  ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 261.211 294.547 246.844 1.00 69.43  ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 260.492 296.166 245.100 1.00 62.86  ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 263.899 294.951 243.085 1.00 70.45  ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 264.331 295.195 241.718 1.00 69.00  ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 263.671 294.196 240.776 1.00 71.67  ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 263.013 293.242 241.198 1.00 73.79  ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 265.858 295.106 241.595 1.00 70.62  ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 266.289 293.776 241.910 1.00 67.87  ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 266.526 296.088 242.545 1.00 70.80  ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 263.856 294.432 239.478 1.00 66.33  ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 263.297 293.583 238.452 1.00 62.84  ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 261.872 293.904 238.058 1.00 64.69  ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 261.339 293.256 237.148 1.00 68.57  ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 261.240 294.876 238.709 1.00 61.95  ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 259.873 295.241 238.366 1.00 54.61  ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 259.821 295.879 236.983 1.00 61.07  ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 260.681 296.685 236.619 1.00 64.59  ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 259.300 296.200 239.409 1.00 56.43  ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 259.193 295.676 240.843 1.00 60.39  ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 258.262 296.552 241.664 1.00 61.54  ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 258.720 294.231 240.857 1.00 63.84  ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 258.803 295.510 236.211 1.00 64.55  ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 258.597 296.035 234.870 1.00 61.53  ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 257.262 296.763 234.809 1.00 63.40  ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 256.239 296.243 235.265 1.00 67.39  ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 258.633 294.916 233.824 1.00 60.15  ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 259.934 294.131 233.798 1.00 60.91  ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 261.130 295.049 233.609 1.00 64.25  ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 262.426 294.259 233.523 1.00 63.87  ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 262.677 293.463 234.755 1.00 65.32  ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 257.278 297.965 234.242 1.00 59.25  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 256.086 298.792 234.115 1.00 56.68  ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 255.513 298.620 232.714 1.00 60.68  ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 256.214 298.845 231.721 1.00 65.02  ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 256.412 300.259 234.393 1.00 57.63  ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 255.227 301.220 234.488 1.00 57.20  ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 254.220 300.722 235.507 1.00 60.07  ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 255.710 302.612 234.852 1.00 64.26  ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 254.246 298.224 232.636 1.00 64.27  ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 253.588 297.929 231.370 1.00 59.88  ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 252.781 299.140 230.921 1.00 62.35  ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 251.885 299.595 231.640 1.00 64.77  ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 252.681 296.706 231.502 1.00 59.52  ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 253.414 295.410 231.796 1.00 63.69  ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 254.370 295.014 230.690 1.00 69.71  ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 255.587 295.077 230.855 1.00 70.34  ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 253.822 294.601 229.553 1.00 68.63  ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 253.098 299.657 229.738 1.00 67.43  ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 252.329 300.729 229.142 1.00 65.80  ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 252.528 302.098 229.748 1.00 69.70  ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 251.748 303.008 229.442 1.00 74.11  ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 253.538 302.280 230.595 1.00 69.64  ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 253.765 303.571 231.228 1.00 66.26  ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 255.244 303.715 231.547 1.00 67.25  ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 255.987 302.732 231.598 1.00 71.78  ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 252.920 303.733 232.496 1.00 63.42  ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 255.661 304.963 231.758 1.00 75.64  ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 257.029 305.288 232.138 1.00 75.89  ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 257.005 306.069 233.442 1.00 76.16  ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 256.168 306.959 233.619 1.00 80.72  ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 257.738 306.101 231.049 1.00 75.15  ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 256.918 307.213 230.668 1.00 75.89  ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 258.015 305.236 229.830 1.00 74.17  ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 257.921 305.737 234.347 1.00 79.41  ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 257.993 306.385 235.650 1.00 80.72  ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 259.124 307.407 235.649 1.00 83.29  ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 260.285 307.058 235.408 1.00 82.89  ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 258.204 305.351 236.755 1.00 80.80  ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 258.197 306.034 238.428 1.00 85.00  ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 258.783 308.666 235.916 1.00 89.25  ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 259.756 309.748 236.008 1.00 88.94  ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 259.402 310.612 237.208 1.00 89.65  ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 258.272 311.100 237.311 1.00 94.98  ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 259.783 310.581 234.721 1.00 89.32  ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 258.419 311.134 234.352 1.00 92.17  ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 257.478 310.381 234.100 1.00 89.91  ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 258.306 312.457 234.317 1.00 90.00  ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 260.366 310.794 238.114 1.00 89.13  ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 260.163 311.544 239.354 1.00 91.83  ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 258.987 310.994 240.157 1.00 91.34  ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 258.231 311.754 240.767 1.00 92.68  ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 259.966 313.038 239.078 1.00 90.96  ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 260.953 313.578 238.062 1.00 93.92  ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 262.078 313.940 238.403 1.00 93.30  ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 260.533 313.634 236.804 1.00 93.34  ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 258.829 309.670 240.152 1.00 81.40  ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 257.738 308.943 240.796 1.00 81.61  ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 256.388 309.334 240.199 1.00 85.05  ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 255.346 309.150 240.836 1.00 84.90  ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 257.747 309.156 242.319 1.00 81.65  ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 256.841 308.184 243.070 1.00 83.29  ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 256.180 307.332 242.475 1.00 82.31  ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 256.813 308.313 244.391 1.00 83.96  ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 256.377 309.884 238.989 1.00 86.09  ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 255.151 310.242 238.289 1.00 80.69  ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 254.994 309.339 237.075 1.00 83.80  ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 255.937 309.179 236.292 1.00 83.87  ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 255.170 311.709 237.856 1.00 80.16  ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 255.827 312.650 238.849 1.00 85.91  ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 254.958 312.868 240.075 1.00 84.34  ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 253.671 313.596 239.719 1.00 84.11  ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 253.936 314.892 239.035 1.00 81.35  ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 253.810 308.757 236.917 1.00 81.91  ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 253.549 307.848 235.811 1.00 78.60  ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 253.034 308.612 234.599 1.00 78.29  ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 252.205 309.517 234.724 1.00 83.46  ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 252.537 306.774 236.211 1.00 75.10  ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 253.007 305.707 237.200 1.00 78.07  ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 252.114 304.479 237.110 1.00 79.22  ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 254.462 305.343 236.965 1.00 77.33  ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 253.532 308.235 233.424 1.00 72.73  ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 253.104 308.828 232.165 1.00 74.54  ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 252.827 307.714 231.169 1.00 77.63  ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 253.600 306.757 231.077 1.00 81.72  ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 254.165 309.787 231.611 1.00 78.37  ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 254.407 310.857 232.509 1.00 80.95  ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 251.726 307.839 230.429 1.00 75.37  ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 251.387 306.832 229.432 1.00 72.68  ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 252.440 306.804 228.333 1.00 69.82  ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 252.911 307.847 227.872 1.00 71.95  ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 250.007 307.113 228.835 1.00 72.49  ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 248.812 306.928 229.771 1.00 70.74  ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 247.518 307.329 229.077 1.00 70.42  ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 248.737 305.495 230.274 1.00 68.18  ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 252.811 305.597 227.914 1.00 71.95  ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 253.850 305.404 226.917 1.00 74.33  ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 253.391 304.392 225.879 1.00 77.34  ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 252.522 303.554 226.135 1.00 78.76  ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 255.164 304.937 227.556 1.00 72.33  ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 256.109 304.571 226.566 1.00 77.37  ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 253.990 304.483 224.695 1.00 76.28  ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 253.700 303.569 223.600 1.00 76.23  ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 254.566 302.317 223.631 1.00 77.02  ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 254.396 301.443 222.776 1.00 80.50  ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 253.877 304.284 222.257 1.00 76.63  ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 252.561 304.754 221.669 1.00 80.94  ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 251.489 304.439 222.185 1.00 78.52  ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 252.637 305.511 220.581 1.00 79.17  ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 255.486 302.212 224.585 1.00 71.75  ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 256.336 301.037 224.694 1.00 74.25  ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 255.614 299.918 225.433 1.00 77.45  ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 254.722 300.157 226.252 1.00 75.73  ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 257.642 301.381 225.411 1.00 72.35  ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 256.009 298.680 225.129 1.00 74.29  ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 255.379 297.524 225.760 1.00 72.08  ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 255.729 297.461 227.241 1.00 70.04  ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 254.863 297.205 228.087 1.00 73.41  ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 255.782 296.230 225.030 1.00 73.16  ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 255.606 296.389 223.520 1.00 72.22  ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 254.964 295.054 225.542 1.00 72.85  ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 254.175 296.615 223.095 1.00 71.72  ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 256.995 297.692 227.582 1.00 67.82  ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 257.458 297.560 228.954 1.00 66.87  ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 258.445 298.673 229.273 1.00 68.97  ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 259.068 299.258 228.383 1.00 71.20  ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 258.110 296.192 229.198 1.00 63.50  ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 258.507 296.051 230.551 1.00 65.99  ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 258.579 298.959 230.567 1.00 68.65  ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 259.531 299.949 231.064 1.00 66.20  ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 260.117 299.419 232.364 1.00 69.04  ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 259.381 299.185 233.328 1.00 74.39  ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 258.866 301.308 231.281 1.00 67.94  ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 258.275 301.755 230.054 1.00 69.84  ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 259.889 302.333 231.747 1.00 66.89  ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 261.433 299.227 232.391 1.00 65.92  ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 262.081 298.673 233.571 1.00 67.57  ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 262.180 299.719 234.674 1.00 64.50  ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 262.614 300.850 234.439 1.00 65.07  ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 263.471 298.149 233.211 1.00 67.26  ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 261.777 299.333 235.884 1.00 65.94  ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 261.907 300.199 237.048 1.00 68.55  ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 263.270 299.953 237.681 1.00 72.80  ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 263.551 298.816 238.092 1.00 74.72  ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 260.793 299.930 238.049 1.00 68.96  ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 259.366 300.179 237.553 1.00 67.86  ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 258.376 300.118 238.705 1.00 68.52  ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 259.271 301.515 236.834 1.00 67.00  ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 264.145 300.962 237.768 1.00 78.90  ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 265.510 300.730 238.262 1.00 77.42  ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 265.565 300.120 239.654 1.00 83.28  ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 266.155 299.053 239.847 1.00 84.18  ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 266.122 302.136 238.252 1.00 80.19  ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 265.372 302.859 237.188 1.00 80.42  ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 263.966 302.328 237.247 1.00 80.17  ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 264.954 300.788 240.630 1.00 78.22  ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 264.948 300.315 242.010 1.00 76.78  ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 263.687 300.821 242.690 1.00 77.99  ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 263.516 302.032 242.859 1.00 83.20  ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 266.195 300.786 242.764 1.00 78.28  ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 266.175 300.636 244.286 1.00 76.85  ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 266.255 299.171 244.685 1.00 78.34  ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 267.306 301.430 244.920 1.00 78.15  ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 262.811 299.898 243.078 1.00 69.00  ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 261.556 300.242 243.738 1.00 70.45  ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 261.757 300.146 245.246 1.00 71.25  ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 262.121 299.087 245.766 1.00 77.82  ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 260.431 299.323 243.272 1.00 74.14  ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 260.193 299.526 241.873 1.00 78.46  ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 259.155 299.611 244.044 1.00 72.23  ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 261.518 301.252 245.946 1.00 77.82  ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 261.707 301.323 247.393 1.00 75.73  ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 260.351 301.133 248.061 1.00 76.72  ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 259.485 302.008 247.996 1.00 80.42  ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 262.340 302.653 247.786 1.00 80.05  ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 263.854 302.687 247.672 1.00 82.66  ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 264.426 304.054 247.996 1.00 86.86  ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 265.500 304.164 248.588 1.00 90.02  ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 263.710 305.103 247.612 1.00 82.39  ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 260.164 299.986 248.708 1.00 74.95  ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 258.922 299.704 249.416 1.00 74.15  ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 259.047 300.174 250.860 1.00 75.75  ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 259.895 299.679 251.610 1.00 82.06  ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 258.599 298.213 249.357 1.00 76.51  ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 258.312 297.639 247.969 1.00 78.03  ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 257.713 296.247 248.080 1.00 75.96  ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 257.391 298.560 247.184 1.00 78.05  ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 258.203 301.127 251.247 1.00 80.55  ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 258.249 301.735 252.571 1.00 80.06  ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 256.950 301.435 253.304 1.00 80.34  ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 255.862 301.646 252.757 1.00 84.88  ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 258.475 303.244 252.471 1.00 81.43  ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 258.647 303.933 253.813 1.00 84.19  ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 259.012 305.397 253.643 1.00 83.96  ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 259.137 306.078 254.926 1.00 86.25  ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 259.509 307.342 255.071 1.00 87.10  ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 259.811 308.098 254.027 1.00 84.07  ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 259.581 307.861 256.293 1.00 85.68  ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 257.066 300.947 254.535 1.00 72.80  ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 255.909 300.667 255.376 1.00 73.69  ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 255.688 301.843 256.320 1.00 78.82  ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 256.564 302.168 257.129 1.00 81.39  ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 256.111 299.371 256.160 1.00 78.31  ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 255.966 298.136 255.324 1.00 79.25  ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 256.963 297.293 254.929 1.00 74.31  ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 254.752 297.601 254.786 1.00 79.67  ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 256.445 296.268 254.175 1.00 71.51  ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 255.089 296.434 254.073 1.00 76.46  ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 253.411 297.997 254.837 1.00 76.00  ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 254.136 295.660 253.415 1.00 75.90  ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 252.467 297.226 254.184 1.00 74.31  ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 252.834 296.071 253.483 1.00 77.75  ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 254.519 302.476 256.218 1.00 87.12  ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 254.201 303.664 256.996 1.00 88.09  ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 252.838 303.486 257.651 1.00 89.67  ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 252.038 302.632 257.261 1.00 88.86  ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 254.214 304.949 256.138 1.00 83.24  ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 255.595 305.184 255.548 1.00 85.26  ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 253.168 304.862 255.038 1.00 83.76  ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 252.586 304.308 258.666 1.00 96.20  ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 251.297 304.305 259.339 1.00 95.39  ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 250.211 304.854 258.417 1.00 97.44  ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 250.460 305.687 257.541 1.00 96.47  ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 251.361 305.132 260.623 1.00 94.29  ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 252.281 304.559 261.688 1.00 94.11  ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 251.746 303.244 262.227 1.00 96.98  ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 250.466 303.454 263.018 1.00 96.46  ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 250.696 304.288 264.230 1.00 92.32  ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 248.988 304.373 258.626 1.00 102.43 ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 247.851 304.815 257.829 1.00 103.88 ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 247.376 306.174 258.327 1.00 104.65 ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 247.033 306.326 259.505 1.00 103.59 ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 246.719 303.793 257.893 1.00 102.32 ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 247.075 302.432 257.323 1.00 102.51 ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 245.905 301.469 257.348 1.00 103.09 ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 245.957 300.428 258.001 1.00 103.94 ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 244.841 301.814 256.634 1.00 102.83 ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 247.358 307.160 257.432 1.00 120.92 ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 246.911 308.506 257.761 1.00 122.43 ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 245.569 308.856 257.136 1.00 122.48 ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 245.117 309.995 257.288 1.00 121.89 ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 247.962 309.535 257.326 1.00 122.67 ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 248.050 309.556 255.896 1.00 120.96 ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 249.323 309.186 257.909 1.00 120.29 ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 244.956 307.920 256.401 1.00 125.25 ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 243.630 308.016 255.786 1.00 125.49 ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 243.284 309.418 255.290 1.00 125.90 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 242.177 309.917 255.523 1.00 125.60 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 242.550 307.465 256.741 1.00 123.80 ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 242.363 308.287 258.019 1.00 124.93 ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 242.764 309.442 258.118 1.00 124.87 ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 241.738 307.667 259.013 1.00 123.88 ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 244.216 310.045 254.573 1.00 129.63 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 244.031 311.389 254.043 1.00 130.53 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 243.365 311.394 252.671 1.00 131.07 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 243.525 312.365 251.921 1.00 130.26 ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 245.375 312.118 253.971 1.00 131.18 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 246.364 311.249 253.404 1.00 131.41 ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 245.823 312.552 255.359 1.00 128.01 ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 242.640 310.326 252.327 1.00 127.90 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 241.915 310.209 251.064 1.00 127.11 ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 242.857 310.226 249.865 1.00 127.42 ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 244.075 310.362 250.019 1.00 127.06 ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 240.870 311.322 250.932 1.00 127.17 ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 239.907 311.414 252.104 1.00 127.93 ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 239.246 312.774 252.209 1.00 128.65 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 238.587 313.193 251.234 1.00 128.34 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 239.386 313.425 253.265 1.00 127.16 ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 242.301 310.072 248.667 1.00 115.67 ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 243.104 310.091 247.457 1.00 114.75 ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 243.389 311.526 247.021 1.00 115.18 ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 242.707 312.474 247.418 1.00 115.43 ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 242.404 309.327 246.333 1.00 113.64 ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 242.446 307.816 246.494 1.00 115.14 ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 243.875 307.316 246.636 1.00 114.57 ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 243.925 305.801 246.740 1.00 111.34 ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 245.302 305.309 247.016 1.00 111.97 ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 244.418 311.672 246.190 1.00 110.73 ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 244.843 312.966 245.676 1.00 111.96 ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 244.170 313.310 244.350 1.00 112.89 ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 244.460 314.362 243.771 1.00 112.69 ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 246.369 312.983 245.527 1.00 111.49 ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 246.998 314.364 245.386 1.00 111.69 ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 248.507 314.268 245.231 1.00 111.18 ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 249.145 315.645 245.167 1.00 110.81 ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 248.747 316.383 243.936 1.00 111.51 ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 243.279 312.444 243.862 1.00 104.67 ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 242.588 312.534 242.578 1.00 103.59 ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 243.532 312.361 241.395 1.00 103.89 ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 243.076 312.395 240.245 1.00 98.86  ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 241.807 313.847 242.410 1.00 101.64 ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 244.833 312.178 241.635 1.00 100.46 ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 245.795 311.864 240.586 1.00 95.96  ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 246.551 310.578 240.901 1.00 93.95  ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 247.612 310.329 240.321 1.00 95.87  ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 246.777 313.020 240.381 1.00 93.15  ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 247.541 313.253 241.551 1.00 92.61  ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 246.023 309.762 241.810 1.00 87.93  ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 246.670 308.537 242.263 1.00 86.25  ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 245.924 307.351 241.671 1.00 86.50  ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 244.695 307.263 241.781 1.00 86.95  ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 246.704 308.455 243.799 1.00 87.83  ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 247.283 307.123 244.252 1.00 88.10  ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 247.504 309.614 244.373 1.00 88.92  ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 246.666 306.443 241.043 1.00 78.92  ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 246.113 305.242 240.428 1.00 76.08  ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 246.725 304.018 241.094 1.00 74.36  ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 247.942 303.955 241.304 1.00 78.16  ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 246.346 305.225 238.908 1.00 72.79  ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 245.454 306.238 238.245 1.00 76.84  ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 247.795 305.557 238.595 1.00 74.26  ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 245.873 303.054 241.436 1.00 66.42  ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 246.297 301.816 242.085 1.00 68.14  ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 246.619 300.796 240.999 1.00 70.74  ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 245.719 300.198 240.404 1.00 79.01  ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 245.210 301.310 243.026 1.00 65.03  ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 244.942 302.301 244.025 1.00 69.73  ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 245.648 300.029 243.704 1.00 65.91  ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 247.909 300.598 240.735 1.00 60.00  ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 248.337 299.656 239.704 1.00 56.78  ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 248.495 298.262 240.293 1.00 62.84  ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 249.168 298.103 241.319 1.00 68.20  ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 249.654 300.088 239.079 1.00 58.71  ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 249.617 300.943 237.815 1.00 58.19  ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 249.114 302.331 238.129 1.00 60.63  ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 250.999 301.002 237.198 1.00 65.42  ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 247.889 297.242 239.693 1.00 58.25  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 248.167 295.869 240.125 1.00 54.65  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 249.608 295.485 239.838 1.00 50.17  ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 250.210 295.921 238.854 1.00 57.27  ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 247.193 295.030 239.291 1.00 57.37  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 246.901 295.869 238.093 1.00 56.24  ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 246.953 297.293 238.557 1.00 52.65  ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 250.162 294.658 240.715 1.00 52.53  ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 251.509 294.116 240.546 1.00 56.60  ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 251.345 292.619 240.322 1.00 54.52  ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 251.278 291.828 241.267 1.00 53.70  ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 252.420 294.412 241.739 1.00 52.47  ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 253.806 293.830 241.505 1.00 53.36  ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 252.504 295.903 241.969 1.00 55.47  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 251.274 292.220 239.058 1.00 56.71  ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 251.152 290.814 238.716 1.00 55.48  ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 252.522 290.151 238.718 1.00 60.03  ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 253.547 290.789 238.463 1.00 62.18  ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 250.484 290.652 237.352 1.00 56.66  ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 249.083 291.213 237.301 1.00 57.99  ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 248.070 290.676 238.085 1.00 57.11  ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 248.774 292.287 236.478 1.00 58.09  ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 246.788 291.188 238.044 1.00 58.28  ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 247.495 292.805 236.430 1.00 54.50  ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 246.507 292.252 237.216 1.00 56.12  ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 245.231 292.766 237.172 1.00 63.29  ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 252.531 288.853 239.022 1.00 63.31  ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 253.787 288.115 239.089 1.00 63.51  ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 254.467 288.061 237.726 1.00 67.18  ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 255.694 288.171 237.628 1.00 70.86  ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 253.536 286.704 239.622 1.00 64.78  ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 254.771 285.822 239.807 1.00 67.79  ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 255.642 286.348 240.937 1.00 66.51  ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 254.365 284.382 240.065 1.00 67.85  ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 253.684 287.895 236.663 1.00 67.51  ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 254.215 287.686 235.325 1.00 68.34  ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 253.240 288.248 234.296 1.00 68.65  ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 252.202 288.823 234.639 1.00 68.75  ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 254.522 286.199 235.105 1.00 61.44  ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 253.280 285.322 235.172 1.00 64.42  ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 252.153 285.810 235.262 1.00 72.13  ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 253.490 284.014 235.154 1.00 66.15  ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 253.583 288.074 233.016 1.00 60.95  ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 252.781 288.639 231.936 1.00 59.36  ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 251.407 287.993 231.823 1.00 59.89  ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 250.510 288.584 231.213 1.00 65.97  ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 253.523 288.513 230.602 1.00 60.92  ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 253.733 287.094 230.150 1.00 64.78  ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 254.775 286.336 230.658 1.00 63.86  ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 252.889 286.520 229.213 1.00 65.89  ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 254.970 285.033 230.243 1.00 65.63  ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 253.078 285.217 228.795 1.00 65.51  ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 254.120 284.473 229.310 1.00 66.02  ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 251.220 286.798 232.387 1.00 58.32  ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 249.917 286.146 232.331 1.00 57.83  ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 248.860 286.892 233.134 1.00 65.49  ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 247.665 286.703 232.882 1.00 63.66  ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 250.020 284.704 232.830 1.00 57.42  ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 250.031 284.692 234.263 1.00 64.19  ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 251.290 284.053 232.313 1.00 56.36  ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 249.275 287.729 234.089 1.00 58.43  ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 248.356 288.523 234.907 1.00 56.12  ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 247.353 287.633 235.637 1.00 58.17  ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 246.176 287.973 235.775 1.00 62.36  ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 247.637 289.576 234.062 1.00 48.11  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 248.573 290.502 233.303 1.00 52.24  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 247.915 291.838 233.011 1.00 53.42  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 248.827 292.760 232.345 1.00 50.60  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 248.541 294.024 232.066 1.00 54.65  ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 247.372 294.554 232.383 1.00 53.45  ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 249.452 294.774 231.452 1.00 55.63  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 247.824 286.480 236.110 1.00 64.55  ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 246.984 285.515 236.809 1.00 66.97  ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 247.068 285.655 238.324 1.00 72.27  ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 246.038 285.665 239.003 1.00 73.53  ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 247.365 284.089 236.394 1.00 63.30  ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 248.277 285.764 238.867 1.00 74.45  ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 248.484 285.898 240.303 1.00 73.27  ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 248.869 287.336 240.624 1.00 70.52  ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 249.810 287.879 240.034 1.00 75.44  ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 249.560 284.930 240.792 1.00 76.27  ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 249.116 283.483 240.723 1.00 78.03  ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 247.899 283.227 240.844 1.00 77.21  ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 249.981 282.601 240.551 1.00 77.02  ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 248.143 287.945 241.556 1.00 64.76  ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 248.395 289.312 241.990 1.00 67.94  ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 249.170 289.281 243.300 1.00 69.56  ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 248.726 288.662 244.273 1.00 69.69  ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 247.084 290.078 242.162 1.00 66.59  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 247.203 291.502 242.705 1.00 65.45  ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 247.942 292.391 241.723 1.00 66.93  ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 245.831 292.071 243.027 1.00 65.48  ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 250.324 289.947 243.325 1.00 66.74  ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 251.109 290.009 244.553 1.00 69.43  ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 250.574 291.097 245.473 1.00 68.91  ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 250.072 290.816 246.567 1.00 70.74  ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 252.598 290.226 244.225 1.00 67.26  ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 253.031 289.330 243.063 1.00 65.64  ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 253.457 289.946 245.447 1.00 68.02  ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 252.851 287.850 243.326 1.00 67.56  ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 250.639 292.349 245.035 1.00 61.76  ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 250.130 293.470 245.814 1.00 62.55  ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 249.780 294.594 244.845 1.00 63.12  ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 249.832 294.421 243.623 1.00 72.20  ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 251.139 293.908 246.886 1.00 66.50  ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 252.467 294.361 246.338 1.00 68.28  ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 253.386 293.446 245.851 1.00 66.18  ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 252.800 295.705 246.325 1.00 67.46  ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 254.605 293.862 245.352 1.00 63.69  ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 254.019 296.126 245.827 1.00 64.17  ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 254.922 295.203 245.341 1.00 63.63  ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 249.410 295.749 245.391 1.00 64.34  ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 248.991 296.890 244.593 1.00 69.12  ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 249.828 298.104 244.962 1.00 72.40  ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 250.183 298.302 246.128 1.00 74.45  ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 247.504 297.205 244.795 1.00 75.82  ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 247.297 297.721 246.116 1.00 78.43  ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 246.657 295.955 244.601 1.00 70.09  ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 250.135 298.922 243.959 1.00 72.85  ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 250.992 300.089 244.129 1.00 71.30  ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 250.182 301.342 243.823 1.00 75.25  ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 249.445 301.390 242.830 1.00 82.39  ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 252.251 300.006 243.244 1.00 73.35  ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 253.157 298.889 243.734 1.00 71.53  ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 251.887 299.794 241.784 1.00 75.51  ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 250.306 302.344 244.692 1.00 82.10  ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 249.596 303.614 244.548 1.00 82.59  ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 250.562 304.646 243.978 1.00 82.99  ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 251.207 305.399 244.708 1.00 89.48  ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 249.021 304.059 245.887 1.00 86.10  ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 247.827 303.227 246.314 1.00 88.00  ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 247.084 302.754 245.429 1.00 89.68  ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 247.639 303.038 247.534 1.00 85.50  ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 250.665 304.674 242.655 1.00 76.44  ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 251.461 305.666 241.949 1.00 78.25  ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 250.639 306.928 241.704 1.00 79.69  ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 249.408 306.917 241.763 1.00 83.83  ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 251.958 305.102 240.619 1.00 82.44  ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 253.274 304.384 240.712 1.00 82.27  ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 254.466 305.089 240.727 1.00 79.19  ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 253.318 303.001 240.781 1.00 79.83  ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 255.677 304.428 240.809 1.00 81.55  ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 254.526 302.335 240.865 1.00 78.41  ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 255.706 303.050 240.879 1.00 80.31  ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 251.337 308.024 241.422 1.00 84.80  ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 250.706 309.300 241.110 1.00 85.82  ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 251.001 309.681 239.665 1.00 83.11  ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 252.082 309.385 239.146 1.00 84.02  ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 251.172 310.398 242.073 1.00 86.93  ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 252.626 310.803 241.932 1.00 88.61  ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 253.512 310.139 242.967 1.00 90.70  ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 254.296 310.853 243.627 1.00 88.92  ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 253.424 308.903 243.121 1.00 90.44  ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 250.026 310.320 239.016 1.00 86.34  ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 250.098 310.648 237.595 1.00 84.34  ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 250.734 312.023 237.424 1.00 86.12  ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 250.716 312.845 238.346 1.00 86.75  ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 248.693 310.594 236.961 1.00 84.67  ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 248.096 309.199 237.101 1.00 83.62  ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 248.720 310.941 235.482 1.00 86.49  ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 246.638 309.157 236.738 1.00 84.99  ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 251.296 312.284 236.245 1.00 92.13  ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 251.858 313.578 235.899 1.00 94.64  ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 250.997 314.259 234.843 1.00 96.34  ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 250.199 313.619 234.151 1.00 96.23  ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 253.296 313.444 235.383 1.00 93.56  ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 251.177 315.577 234.732 1.00 104.14 ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 250.515 316.415 233.736 1.00 106.82 ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 248.998 316.263 233.757 1.00 104.50 ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 248.394 316.128 234.826 1.00 100.78 ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 251.047 316.105 232.333 1.00 106.45 ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 250.546 314.836 231.897 1.00 105.43 ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 252.569 316.066 232.337 1.00 101.54 ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 248.378 316.272 232.576 1.00 103.50 ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 246.927 316.271 232.439 1.00 103.22 ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 246.377 314.899 232.067 1.00 106.08 ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 245.245 314.801 231.582 1.00 106.57 ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 246.497 317.310 231.401 1.00 103.82 ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 246.966 317.002 229.984 1.00 104.49 ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 246.719 318.168 229.034 1.00 104.39 ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 247.534 319.390 229.434 1.00 103.48 ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 247.341 320.535 228.499 1.00 102.53 ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 247.154 313.842 232.285 1.00 96.70  ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 246.727 312.506 231.898 1.00 94.35  ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 245.546 312.046 232.746 1.00 94.74  ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 245.386 312.442 233.904 1.00 93.41  ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 247.895 311.531 232.028 1.00 93.00  ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 249.014 311.798 231.034 1.00 95.50  ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 250.170 310.838 231.192 1.00 95.68  ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 250.150 310.047 232.157 1.00 96.80  ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 251.096 310.873 230.355 1.00 93.51  ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 244.709 311.189 232.148 1.00 83.26  ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 243.461 310.705 232.729 1.00 80.57  ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 243.701 309.397 233.464 1.00 81.03  ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 244.224 308.446 232.864 1.00 80.59  ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 242.414 310.497 231.636 1.00 81.64  ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 241.029 310.198 232.189 1.00 83.69  ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 240.852 310.210 233.424 1.00 84.44  ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 240.112 309.941 231.382 1.00 83.80  ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 243.353 309.305 234.751 1.00 76.38  ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 243.435 308.004 235.435 1.00 76.99  ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 242.580 306.935 234.783 1.00 75.09  ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 242.901 305.745 234.884 1.00 72.93  ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 242.956 308.323 236.860 1.00 72.84  ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 242.287 309.660 236.769 1.00 73.96  ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 242.992 310.390 235.677 1.00 72.56  ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 241.489 307.328 234.123 1.00 70.25  ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 240.701 306.370 233.357 1.00 67.52  ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 241.508 305.802 232.197 1.00 66.39  ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 241.391 304.615 231.872 1.00 69.74  ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 239.424 307.040 232.851 1.00 70.44  ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 238.673 307.822 233.917 1.00 69.62  ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 237.198 308.053 233.575 1.00 69.31  ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 236.973 309.148 232.635 1.00 73.48  ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 237.105 309.069 231.317 1.00 74.57  ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 237.409 307.931 230.715 1.00 71.96  ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 236.908 310.159 230.580 1.00 66.97  ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 242.336 306.637 231.563 1.00 65.90  ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 243.141 306.177 230.435 1.00 64.50  ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 244.122 305.093 230.859 1.00 64.71  ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 244.396 304.161 230.093 1.00 74.92  ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 243.881 307.355 229.803 1.00 67.56  ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 242.975 308.280 229.227 1.00 72.38  ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 244.676 305.203 232.069 1.00 61.93  ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 245.525 304.135 232.587 1.00 58.26  ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 244.740 302.839 232.740 1.00 59.95  ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 245.246 301.755 232.428 1.00 63.53  ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 246.139 304.547 233.925 1.00 60.80  ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 247.287 305.508 233.802 1.00 63.44  ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 247.076 306.824 233.429 1.00 66.66  ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 248.581 305.093 234.069 1.00 63.60  ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 248.134 307.706 233.319 1.00 62.61  ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 249.643 305.970 233.961 1.00 63.95  ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 249.419 307.278 233.587 1.00 63.02  ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 243.501 302.934 233.226 1.00 66.42  ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 242.671 301.746 233.394 1.00 60.97  ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 242.328 301.118 232.049 1.00 63.31  ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 242.326 299.890 231.910 1.00 64.67  ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 241.394 302.102 234.156 1.00 56.52  ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 241.624 302.754 235.504 1.00 61.64  ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 242.812 302.568 236.200 1.00 64.61  ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 240.649 303.559 236.078 1.00 64.42  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 243.021 303.165 237.429 1.00 63.04  ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 240.849 304.159 237.306 1.00 66.24  ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 242.036 303.958 237.977 1.00 64.59  ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 242.236 304.555 239.201 1.00 64.74  ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 242.028 301.949 231.048 1.00 56.99  ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 241.636 301.444 229.738 1.00 49.75  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 242.802 300.824 228.979 1.00 54.79  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 242.601 299.868 228.222 1.00 61.70  ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 241.014 302.569 228.910 1.00 50.67  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 239.664 303.042 229.420 1.00 58.80  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 239.035 304.085 228.519 1.00 63.35  ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 239.684 305.121 228.266 1.00 65.53  ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 237.893 303.870 228.062 1.00 58.83  ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 244.014 301.340 229.163 1.00 48.90  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 245.179 300.852 228.437 1.00 49.04  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 245.849 299.666 229.117 1.00 53.26  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 246.876 299.188 228.623 1.00 56.11  ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 246.198 301.981 228.247 1.00 49.72  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 245.711 303.101 227.342 1.00 49.40  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 246.749 304.199 227.187 1.00 56.63  ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 248.047 303.672 226.783 1.00 57.27  ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 248.717 304.076 225.713 1.00 53.68  ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 248.240 305.014 224.912 1.00 52.71  ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 249.896 303.525 225.439 1.00 57.46  ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 245.300 299.182 230.226 1.00 51.98  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 245.864 298.030 230.909 1.00 52.66  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 247.236 298.262 231.502 1.00 57.09  ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 248.103 297.384 231.408 1.00 56.06  ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 247.457 299.426 232.111 1.00 56.14  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 248.743 299.717 232.731 1.00 47.23  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 248.872 298.920 234.021 1.00 53.23  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 247.991 298.965 234.889 1.00 54.51  ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 248.885 301.225 232.986 1.00 45.49  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 250.189 301.521 233.703 1.00 52.13  ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 248.806 301.993 231.677 1.00 52.32  ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 249.972 298.182 234.152 1.00 55.93  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 250.196 297.336 235.314 1.00 47.88  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 251.695 297.210 235.554 1.00 49.68  ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 252.514 297.748 234.803 1.00 58.13  ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 249.543 295.963 235.131 1.00 49.30  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 252.049 296.490 236.616 1.00 55.54  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 253.436 296.252 236.997 1.00 54.70  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 253.662 294.749 237.049 1.00 54.70  ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 252.848 294.015 237.619 1.00 55.15  ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 253.778 296.899 238.354 1.00 51.93  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 255.247 296.692 238.687 1.00 54.54  ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 253.434 298.379 238.341 1.00 49.72  ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 254.758 294.291 236.450 1.00 56.28  ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 255.092 292.875 236.392 1.00 57.57  ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 256.358 292.619 237.195 1.00 56.70  ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 257.355 293.330 237.034 1.00 58.33  ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 255.282 292.412 234.945 1.00 58.86  ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 254.078 292.582 234.018 1.00 57.29  ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 254.344 291.925 232.674 1.00 59.78  ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 252.818 292.021 234.656 1.00 54.43  ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 256.311 291.605 238.063 1.00 61.42  ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 257.484 291.256 238.858 1.00 61.41  ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 258.618 290.740 237.980 1.00 60.88  ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 259.786 291.076 238.204 1.00 65.52  ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 257.112 290.220 239.918 1.00 63.01  ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 255.883 290.785 241.117 1.00 64.64  ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 258.296 289.924 236.981 1.00 65.21  ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 259.309 289.380 236.084 1.00 68.77  ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 258.900 289.548 234.624 1.00 65.55  ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 257.737 289.818 234.323 1.00 67.41  ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 259.573 287.888 236.364 1.00 68.67  ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 260.628 287.420 235.515 1.00 71.94  ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 258.321 287.067 236.102 1.00 64.10  ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . AOV B 2 .    ? 230.289 278.253 249.598 1.00 42.42  ? 4701 AOV A PB    1 
HETATM 23595 O  O1B   . AOV B 2 .    ? 231.614 278.576 248.986 1.00 40.67  ? 4701 AOV A O1B   1 
HETATM 23596 O  O2B   . AOV B 2 .    ? 229.167 278.761 248.759 1.00 38.55  ? 4701 AOV A O2B   1 
HETATM 23597 O  O3B   . AOV B 2 .    ? 230.130 276.677 249.706 1.00 45.06  ? 4701 AOV A O3B   1 
HETATM 23598 P  PA    . AOV B 2 .    ? 229.182 278.600 252.037 1.00 48.54  ? 4701 AOV A PA    1 
HETATM 23599 O  O1A   . AOV B 2 .    ? 228.054 279.299 251.352 1.00 27.84  ? 4701 AOV A O1A   1 
HETATM 23600 O  O2A   . AOV B 2 .    ? 228.936 277.126 252.314 1.00 50.13  ? 4701 AOV A O2A   1 
HETATM 23601 O  O3A   . AOV B 2 .    ? 230.394 278.810 251.074 1.00 49.20  ? 4701 AOV A O3A   1 
HETATM 23602 O  "O5'" . AOV B 2 .    ? 229.567 279.418 253.343 1.00 48.70  ? 4701 AOV A "O5'" 1 
HETATM 23603 C  "C5'" . AOV B 2 .    ? 230.917 279.339 253.760 1.00 41.41  ? 4701 AOV A "C5'" 1 
HETATM 23604 C  "C4'" . AOV B 2 .    ? 231.019 279.845 255.175 1.00 41.22  ? 4701 AOV A "C4'" 1 
HETATM 23605 O  "O4'" . AOV B 2 .    ? 231.049 281.268 255.155 1.00 51.23  ? 4701 AOV A "O4'" 1 
HETATM 23606 C  "C3'" . AOV B 2 .    ? 229.805 279.416 255.978 1.00 45.92  ? 4701 AOV A "C3'" 1 
HETATM 23607 O  "O3'" . AOV B 2 .    ? 230.206 279.071 257.309 1.00 58.33  ? 4701 AOV A "O3'" 1 
HETATM 23608 C  "C2'" . AOV B 2 .    ? 228.960 280.661 255.934 1.00 52.38  ? 4701 AOV A "C2'" 1 
HETATM 23609 O  "O2'" . AOV B 2 .    ? 228.034 280.724 257.010 1.00 57.14  ? 4701 AOV A "O2'" 1 
HETATM 23610 C  "C1'" . AOV B 2 .    ? 230.029 281.712 256.029 1.00 35.31  ? 4701 AOV A "C1'" 1 
HETATM 23611 N  N9    . AOV B 2 .    ? 229.453 282.972 255.576 1.00 36.88  ? 4701 AOV A N9    1 
HETATM 23612 C  C8    . AOV B 2 .    ? 229.396 283.351 254.307 1.00 38.71  ? 4701 AOV A C8    1 
HETATM 23613 N  N7    . AOV B 2 .    ? 228.810 284.568 254.199 1.00 34.77  ? 4701 AOV A N7    1 
HETATM 23614 C  C5    . AOV B 2 .    ? 228.474 284.996 255.422 1.00 36.61  ? 4701 AOV A C5    1 
HETATM 23615 C  C6    . AOV B 2 .    ? 227.825 286.197 255.997 1.00 42.63  ? 4701 AOV A C6    1 
HETATM 23616 N  N6    . AOV B 2 .    ? 227.413 287.198 255.203 1.00 42.28  ? 4701 AOV A N6    1 
HETATM 23617 N  N1    . AOV B 2 .    ? 227.659 286.257 257.334 1.00 39.60  ? 4701 AOV A N1    1 
HETATM 23618 C  C2    . AOV B 2 .    ? 228.070 285.256 258.132 1.00 38.45  ? 4701 AOV A C2    1 
HETATM 23619 N  N3    . AOV B 2 .    ? 228.669 284.135 257.666 1.00 42.93  ? 4701 AOV A N3    1 
HETATM 23620 C  C4    . AOV B 2 .    ? 228.904 283.933 256.339 1.00 38.03  ? 4701 AOV A C4    1 
HETATM 23621 V  VG    . AOV B 2 .    ? 231.416 275.741 248.530 1.00 51.28  ? 4701 AOV A VG    1 
HETATM 23622 O  O1G   . AOV B 2 .    ? 233.026 276.064 249.824 1.00 45.66  ? 4701 AOV A O1G   1 
HETATM 23623 O  O2G   . AOV B 2 .    ? 232.777 274.768 247.337 1.00 39.18  ? 4701 AOV A O2G   1 
HETATM 23624 O  O3G   . AOV B 2 .    ? 230.448 273.930 248.899 1.00 51.26  ? 4701 AOV A O3G   1 
HETATM 23625 O  O4G   . AOV B 2 .    ? 230.893 276.998 246.921 1.00 49.53  ? 4701 AOV A O4G   1 
HETATM 23626 P  PG    . ATP C 3 .    ? 248.350 254.624 259.566 1.00 59.64  ? 4702 ATP A PG    1 
HETATM 23627 O  O1G   . ATP C 3 .    ? 248.724 255.754 258.670 1.00 56.34  ? 4702 ATP A O1G   1 
HETATM 23628 O  O2G   . ATP C 3 .    ? 246.840 254.472 259.764 1.00 59.88  ? 4702 ATP A O2G   1 
HETATM 23629 O  O3G   . ATP C 3 .    ? 248.936 253.276 259.135 1.00 58.90  ? 4702 ATP A O3G   1 
HETATM 23630 P  PB    . ATP C 3 .    ? 248.653 255.759 262.320 1.00 34.72  ? 4702 ATP A PB    1 
HETATM 23631 O  O1B   . ATP C 3 .    ? 249.268 257.095 262.199 1.00 53.75  ? 4702 ATP A O1B   1 
HETATM 23632 O  O2B   . ATP C 3 .    ? 247.146 255.750 262.566 1.00 55.89  ? 4702 ATP A O2B   1 
HETATM 23633 O  O3B   . ATP C 3 .    ? 248.924 254.859 261.038 1.00 53.28  ? 4702 ATP A O3B   1 
HETATM 23634 P  PA    . ATP C 3 .    ? 248.828 253.919 264.631 1.00 45.13  ? 4702 ATP A PA    1 
HETATM 23635 O  O1A   . ATP C 3 .    ? 247.656 253.124 264.211 1.00 58.76  ? 4702 ATP A O1A   1 
HETATM 23636 O  O2A   . ATP C 3 .    ? 248.621 254.775 265.878 1.00 50.65  ? 4702 ATP A O2A   1 
HETATM 23637 O  O3A   . ATP C 3 .    ? 249.324 254.889 263.472 1.00 53.23  ? 4702 ATP A O3A   1 
HETATM 23638 O  "O5'" . ATP C 3 .    ? 250.077 252.984 264.870 1.00 55.52  ? 4702 ATP A "O5'" 1 
HETATM 23639 C  "C5'" . ATP C 3 .    ? 251.369 253.532 265.206 1.00 47.99  ? 4702 ATP A "C5'" 1 
HETATM 23640 C  "C4'" . ATP C 3 .    ? 252.188 252.468 265.893 1.00 53.65  ? 4702 ATP A "C4'" 1 
HETATM 23641 O  "O4'" . ATP C 3 .    ? 252.742 253.001 267.115 1.00 60.68  ? 4702 ATP A "O4'" 1 
HETATM 23642 C  "C3'" . ATP C 3 .    ? 251.416 251.227 266.323 1.00 54.92  ? 4702 ATP A "C3'" 1 
HETATM 23643 O  "O3'" . ATP C 3 .    ? 252.273 250.094 266.403 1.00 58.84  ? 4702 ATP A "O3'" 1 
HETATM 23644 C  "C2'" . ATP C 3 .    ? 250.886 251.635 267.699 1.00 52.75  ? 4702 ATP A "C2'" 1 
HETATM 23645 O  "O2'" . ATP C 3 .    ? 250.670 250.507 268.538 1.00 61.09  ? 4702 ATP A "O2'" 1 
HETATM 23646 C  "C1'" . ATP C 3 .    ? 252.036 252.495 268.236 1.00 49.63  ? 4702 ATP A "C1'" 1 
HETATM 23647 N  N9    . ATP C 3 .    ? 251.599 253.624 269.049 1.00 55.06  ? 4702 ATP A N9    1 
HETATM 23648 C  C8    . ATP C 3 .    ? 250.720 254.611 268.688 1.00 52.27  ? 4702 ATP A C8    1 
HETATM 23649 N  N7    . ATP C 3 .    ? 250.506 255.506 269.621 1.00 45.19  ? 4702 ATP A N7    1 
HETATM 23650 C  C5    . ATP C 3 .    ? 251.303 255.079 270.672 1.00 47.94  ? 4702 ATP A C5    1 
HETATM 23651 C  C6    . ATP C 3 .    ? 251.530 255.594 271.963 1.00 50.49  ? 4702 ATP A C6    1 
HETATM 23652 N  N6    . ATP C 3 .    ? 250.949 256.701 272.435 1.00 54.26  ? 4702 ATP A N6    1 
HETATM 23653 N  N1    . ATP C 3 .    ? 252.387 254.925 272.765 1.00 51.88  ? 4702 ATP A N1    1 
HETATM 23654 C  C2    . ATP C 3 .    ? 252.971 253.817 272.300 1.00 46.86  ? 4702 ATP A C2    1 
HETATM 23655 N  N3    . ATP C 3 .    ? 252.834 253.238 271.106 1.00 52.45  ? 4702 ATP A N3    1 
HETATM 23656 C  C4    . ATP C 3 .    ? 251.983 253.920 270.334 1.00 53.29  ? 4702 ATP A C4    1 
HETATM 23657 P  PB    . ADP D 4 .    ? 258.932 233.984 240.528 1.00 37.21  ? 4703 ADP A PB    1 
HETATM 23658 O  O1B   . ADP D 4 .    ? 258.900 233.558 241.975 1.00 40.11  ? 4703 ADP A O1B   1 
HETATM 23659 O  O2B   . ADP D 4 .    ? 257.646 233.748 239.774 1.00 49.78  ? 4703 ADP A O2B   1 
HETATM 23660 O  O3B   . ADP D 4 .    ? 259.548 235.342 240.298 1.00 47.51  ? 4703 ADP A O3B   1 
HETATM 23661 P  PA    . ADP D 4 .    ? 259.859 231.379 240.023 1.00 52.32  ? 4703 ADP A PA    1 
HETATM 23662 O  O1A   . ADP D 4 .    ? 260.157 231.036 241.462 1.00 37.37  ? 4703 ADP A O1A   1 
HETATM 23663 O  O2A   . ADP D 4 .    ? 258.572 230.888 239.406 1.00 39.20  ? 4703 ADP A O2A   1 
HETATM 23664 O  O3A   . ADP D 4 .    ? 259.979 232.974 239.842 1.00 49.82  ? 4703 ADP A O3A   1 
HETATM 23665 O  "O5'" . ADP D 4 .    ? 261.088 230.848 239.131 1.00 47.49  ? 4703 ADP A "O5'" 1 
HETATM 23666 C  "C5'" . ADP D 4 .    ? 262.314 230.487 239.758 1.00 32.55  ? 4703 ADP A "C5'" 1 
HETATM 23667 C  "C4'" . ADP D 4 .    ? 263.086 229.510 238.884 1.00 33.17  ? 4703 ADP A "C4'" 1 
HETATM 23668 O  "O4'" . ADP D 4 .    ? 264.465 229.509 239.259 1.00 48.02  ? 4703 ADP A "O4'" 1 
HETATM 23669 C  "C3'" . ADP D 4 .    ? 262.552 228.102 239.071 1.00 37.44  ? 4703 ADP A "C3'" 1 
HETATM 23670 O  "O3'" . ADP D 4 .    ? 262.088 227.588 237.820 1.00 42.21  ? 4703 ADP A "O3'" 1 
HETATM 23671 C  "C2'" . ADP D 4 .    ? 263.724 227.283 239.567 1.00 41.96  ? 4703 ADP A "C2'" 1 
HETATM 23672 O  "O2'" . ADP D 4 .    ? 263.894 226.125 238.744 1.00 52.66  ? 4703 ADP A "O2'" 1 
HETATM 23673 C  "C1'" . ADP D 4 .    ? 264.947 228.179 239.459 1.00 41.94  ? 4703 ADP A "C1'" 1 
HETATM 23674 N  N9    . ADP D 4 .    ? 265.745 228.144 240.712 1.00 43.34  ? 4703 ADP A N9    1 
HETATM 23675 C  C8    . ADP D 4 .    ? 266.217 229.229 241.352 1.00 42.40  ? 4703 ADP A C8    1 
HETATM 23676 N  N7    . ADP D 4 .    ? 266.916 228.882 242.461 1.00 48.48  ? 4703 ADP A N7    1 
HETATM 23677 C  C5    . ADP D 4 .    ? 266.903 227.540 242.541 1.00 38.33  ? 4703 ADP A C5    1 
HETATM 23678 C  C6    . ADP D 4 .    ? 267.452 226.524 243.469 1.00 35.51  ? 4703 ADP A C6    1 
HETATM 23679 N  N6    . ADP D 4 .    ? 268.172 226.885 244.558 1.00 40.42  ? 4703 ADP A N6    1 
HETATM 23680 N  N1    . ADP D 4 .    ? 267.210 225.224 243.193 1.00 44.42  ? 4703 ADP A N1    1 
HETATM 23681 C  C2    . ADP D 4 .    ? 266.497 224.851 242.116 1.00 40.21  ? 4703 ADP A C2    1 
HETATM 23682 N  N3    . ADP D 4 .    ? 265.972 225.718 241.234 1.00 34.08  ? 4703 ADP A N3    1 
HETATM 23683 C  C4    . ADP D 4 .    ? 266.136 227.055 241.383 1.00 41.92  ? 4703 ADP A C4    1 
HETATM 23684 P  PB    . ADP E 4 .    ? 246.972 234.865 210.929 1.00 41.59  ? 4704 ADP A PB    1 
HETATM 23685 O  O1B   . ADP E 4 .    ? 248.344 234.284 210.690 1.00 45.46  ? 4704 ADP A O1B   1 
HETATM 23686 O  O2B   . ADP E 4 .    ? 246.126 234.077 211.898 1.00 41.56  ? 4704 ADP A O2B   1 
HETATM 23687 O  O3B   . ADP E 4 .    ? 246.953 236.355 211.163 1.00 50.07  ? 4704 ADP A O3B   1 
HETATM 23688 P  PA    . ADP E 4 .    ? 245.689 233.240 209.042 1.00 51.90  ? 4704 ADP A PA    1 
HETATM 23689 O  O1A   . ADP E 4 .    ? 246.768 232.222 209.311 1.00 27.68  ? 4704 ADP A O1A   1 
HETATM 23690 O  O2A   . ADP E 4 .    ? 244.309 233.030 209.618 1.00 36.82  ? 4704 ADP A O2A   1 
HETATM 23691 O  O3A   . ADP E 4 .    ? 246.225 234.682 209.516 1.00 49.60  ? 4704 ADP A O3A   1 
HETATM 23692 O  "O5'" . ADP E 4 .    ? 245.563 233.422 207.448 1.00 51.29  ? 4704 ADP A "O5'" 1 
HETATM 23693 C  "C5'" . ADP E 4 .    ? 245.014 232.381 206.646 1.00 47.95  ? 4704 ADP A "C5'" 1 
HETATM 23694 C  "C4'" . ADP E 4 .    ? 245.360 232.624 205.184 1.00 36.56  ? 4704 ADP A "C4'" 1 
HETATM 23695 O  "O4'" . ADP E 4 .    ? 246.768 232.815 205.035 1.00 37.52  ? 4704 ADP A "O4'" 1 
HETATM 23696 C  "C3'" . ADP E 4 .    ? 244.972 231.433 204.324 1.00 45.24  ? 4704 ADP A "C3'" 1 
HETATM 23697 O  "O3'" . ADP E 4 .    ? 243.902 231.790 203.444 1.00 51.87  ? 4704 ADP A "O3'" 1 
HETATM 23698 C  "C2'" . ADP E 4 .    ? 246.207 231.081 203.521 1.00 51.30  ? 4704 ADP A "C2'" 1 
HETATM 23699 O  "O2'" . ADP E 4 .    ? 245.918 231.151 202.122 1.00 55.83  ? 4704 ADP A "O2'" 1 
HETATM 23700 C  "C1'" . ADP E 4 .    ? 247.255 232.118 203.887 1.00 42.81  ? 4704 ADP A "C1'" 1 
HETATM 23701 N  N9    . ADP E 4 .    ? 248.540 231.450 204.211 1.00 46.32  ? 4704 ADP A N9    1 
HETATM 23702 C  C8    . ADP E 4 .    ? 249.145 231.456 205.412 1.00 47.19  ? 4704 ADP A C8    1 
HETATM 23703 N  N7    . ADP E 4 .    ? 250.309 230.759 205.379 1.00 46.36  ? 4704 ADP A N7    1 
HETATM 23704 C  C5    . ADP E 4 .    ? 250.464 230.293 204.127 1.00 40.89  ? 4704 ADP A C5    1 
HETATM 23705 C  C6    . ADP E 4 .    ? 251.474 229.482 203.408 1.00 39.94  ? 4704 ADP A C6    1 
HETATM 23706 N  N6    . ADP E 4 .    ? 252.579 229.018 204.039 1.00 43.07  ? 4704 ADP A N6    1 
HETATM 23707 N  N1    . ADP E 4 .    ? 251.254 229.220 202.101 1.00 41.85  ? 4704 ADP A N1    1 
HETATM 23708 C  C2    . ADP E 4 .    ? 250.161 229.675 201.462 1.00 34.87  ? 4704 ADP A C2    1 
HETATM 23709 N  N3    . ADP E 4 .    ? 249.206 230.415 202.052 1.00 37.51  ? 4704 ADP A N3    1 
HETATM 23710 C  C4    . ADP E 4 .    ? 249.298 230.754 203.359 1.00 42.96  ? 4704 ADP A C4    1 
HETATM 23711 MG MG    . MG  F 5 .    ? 245.354 254.062 261.039 1.00 26.96  ? 4705 MG  A MG    1 
HETATM 23712 MG MG    . MG  G 5 .    ? 227.995 275.518 248.827 1.00 18.67  ? 4706 MG  A MG    1 
# 
