data_9BM2
# 
_entry.id   9BM2 
# 
_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   9BM2         pdb_00009bm2 10.2210/pdb9bm2/pdb 
WWPDB D_1000283517 ?            ?                   
EMDB  EMD-44685    ?            ?                   
# 
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                        9BM2 
_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-4 of motor domain from full-length human dynein-1 in 5 mM ATP' 
_pdbx_database_related.db_id          EMD-44685 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    3 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     2 ? ? ? ? 
5 water       nat water                                18.015     7 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
5 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ? 'H2 O'              18.015  
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 ?    ?   ?   A . n 
A 1 1458 ALA 1458 1458 ?    ?   ?   A . n 
A 1 1459 LEU 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLU 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 LEU 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLN 1465 1465 ?    ?   ?   A . n 
A 1 1466 ILE 1466 1466 ?    ?   ?   A . n 
A 1 1467 ARG 1467 1467 ?    ?   ?   A . n 
A 1 1468 GLU 1468 1468 ?    ?   ?   A . n 
A 1 1469 VAL 1469 1469 ?    ?   ?   A . n 
A 1 1470 TRP 1470 1470 ?    ?   ?   A . n 
A 1 1471 ASN 1471 1471 ?    ?   ?   A . n 
A 1 1472 THR 1472 1472 ?    ?   ?   A . n 
A 1 1473 TYR 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLU 1474 1474 ?    ?   ?   A . n 
A 1 1475 LEU 1475 1475 ?    ?   ?   A . n 
A 1 1476 ASP 1476 1476 ?    ?   ?   A . n 
A 1 1477 LEU 1477 1477 ?    ?   ?   A . n 
A 1 1478 VAL 1478 1478 ?    ?   ?   A . n 
A 1 1479 ASN 1479 1479 ?    ?   ?   A . n 
A 1 1480 TYR 1480 1480 ?    ?   ?   A . n 
A 1 1481 GLN 1481 1481 ?    ?   ?   A . n 
A 1 1482 ASN 1482 1482 ?    ?   ?   A . n 
A 1 1483 LYS 1483 1483 ?    ?   ?   A . n 
A 1 1484 CYS 1484 1484 ?    ?   ?   A . n 
A 1 1485 ARG 1485 1485 ?    ?   ?   A . n 
A 1 1486 LEU 1486 1486 ?    ?   ?   A . n 
A 1 1487 ILE 1487 1487 ?    ?   ?   A . n 
A 1 1488 ARG 1488 1488 ?    ?   ?   A . n 
A 1 1489 GLY 1489 1489 ?    ?   ?   A . n 
A 1 1490 TRP 1490 1490 ?    ?   ?   A . n 
A 1 1491 ASP 1491 1491 ?    ?   ?   A . n 
A 1 1492 ASP 1492 1492 ?    ?   ?   A . n 
A 1 1493 LEU 1493 1493 ?    ?   ?   A . n 
A 1 1494 PHE 1494 1494 ?    ?   ?   A . n 
A 1 1495 ASN 1495 1495 ?    ?   ?   A . n 
A 1 1496 LYS 1496 1496 ?    ?   ?   A . n 
A 1 1497 VAL 1497 1497 ?    ?   ?   A . n 
A 1 1498 LYS 1498 1498 ?    ?   ?   A . n 
A 1 1499 GLU 1499 1499 ?    ?   ?   A . n 
A 1 1500 HIS 1500 1500 ?    ?   ?   A . n 
A 1 1501 ILE 1501 1501 ?    ?   ?   A . n 
A 1 1502 ASN 1502 1502 ?    ?   ?   A . n 
A 1 1503 SER 1503 1503 ?    ?   ?   A . n 
A 1 1504 VAL 1504 1504 ?    ?   ?   A . n 
A 1 1505 SER 1505 1505 ?    ?   ?   A . n 
A 1 1506 ALA 1506 1506 ?    ?   ?   A . n 
A 1 1507 MET 1507 1507 ?    ?   ?   A . n 
A 1 1508 LYS 1508 1508 ?    ?   ?   A . n 
A 1 1509 LEU 1509 1509 ?    ?   ?   A . n 
A 1 1510 SER 1510 1510 ?    ?   ?   A . n 
A 1 1511 PRO 1511 1511 ?    ?   ?   A . n 
A 1 1512 TYR 1512 1512 ?    ?   ?   A . n 
A 1 1513 TYR 1513 1513 ?    ?   ?   A . n 
A 1 1514 LYS 1514 1514 ?    ?   ?   A . n 
A 1 1515 VAL 1515 1515 ?    ?   ?   A . n 
A 1 1516 PHE 1516 1516 ?    ?   ?   A . n 
A 1 1517 GLU 1517 1517 ?    ?   ?   A . n 
A 1 1518 GLU 1518 1518 ?    ?   ?   A . n 
A 1 1519 ASP 1519 1519 ?    ?   ?   A . n 
A 1 1520 ALA 1520 1520 ?    ?   ?   A . n 
A 1 1521 LEU 1521 1521 ?    ?   ?   A . n 
A 1 1522 SER 1522 1522 ?    ?   ?   A . n 
A 1 1523 TRP 1523 1523 ?    ?   ?   A . n 
A 1 1524 GLU 1524 1524 ?    ?   ?   A . n 
A 1 1525 ASP 1525 1525 ?    ?   ?   A . n 
A 1 1526 LYS 1526 1526 ?    ?   ?   A . n 
A 1 1527 LEU 1527 1527 ?    ?   ?   A . n 
A 1 1528 ASN 1528 1528 ?    ?   ?   A . n 
A 1 1529 ARG 1529 1529 ?    ?   ?   A . n 
A 1 1530 ILE 1530 1530 ?    ?   ?   A . n 
A 1 1531 MET 1531 1531 ?    ?   ?   A . n 
A 1 1532 ALA 1532 1532 ?    ?   ?   A . n 
A 1 1533 LEU 1533 1533 ?    ?   ?   A . n 
A 1 1534 PHE 1534 1534 ?    ?   ?   A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 2389 GLU GLU A . n 
A 1 2390 GLY 2390 2390 ?    ?   ?   A . n 
A 1 2391 GLU 2391 2391 ?    ?   ?   A . n 
A 1 2392 ASP 2392 2392 ?    ?   ?   A . n 
A 1 2393 GLU 2393 2393 ?    ?   ?   A . n 
A 1 2394 ALA 2394 2394 ?    ?   ?   A . n 
A 1 2395 GLN 2395 2395 ?    ?   ?   A . n 
A 1 2396 ARG 2396 2396 ?    ?   ?   A . n 
A 1 2397 ARG 2397 2397 ?    ?   ?   A . n 
A 1 2398 ARG 2398 2398 ?    ?   ?   A . n 
A 1 2399 LYS 2399 2399 ?    ?   ?   A . n 
A 1 2400 GLY 2400 2400 ?    ?   ?   A . n 
A 1 2401 LYS 2401 2401 ?    ?   ?   A . n 
A 1 2402 GLU 2402 2402 ?    ?   ?   A . n 
A 1 2403 ASP 2403 2403 ?    ?   ?   A . n 
A 1 2404 GLU 2404 2404 ?    ?   ?   A . n 
A 1 2405 GLY 2405 2405 ?    ?   ?   A . n 
A 1 2406 GLU 2406 2406 ?    ?   ?   A . n 
A 1 2407 GLU 2407 2407 ?    ?   ?   A . n 
A 1 2408 ALA 2408 2408 ?    ?   ?   A . n 
A 1 2409 ALA 2409 2409 ?    ?   ?   A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET MET A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 3221 ASP ASP A . n 
A 1 3222 LEU 3222 3222 3222 LEU LEU A . n 
A 1 3223 ARG 3223 3223 3223 ARG ARG A . n 
A 1 3224 ILE 3224 3224 3224 ILE ILE A . n 
A 1 3225 LYS 3225 3225 3225 LYS LYS A . n 
A 1 3226 SER 3226 3226 3226 SER SER A . n 
A 1 3227 GLN 3227 3227 3227 GLN GLN A . n 
A 1 3228 GLU 3228 3228 3228 GLU GLU A . n 
A 1 3229 LEU 3229 3229 3229 LEU LEU A . n 
A 1 3230 GLU 3230 3230 3230 GLU GLU A . n 
A 1 3231 VAL 3231 3231 3231 VAL VAL A . n 
A 1 3232 LYS 3232 3232 3232 LYS LYS A . n 
A 1 3233 ASN 3233 3233 3233 ASN ASN A . n 
A 1 3234 ALA 3234 3234 3234 ALA ALA A . n 
A 1 3235 ALA 3235 3235 3235 ALA ALA A . n 
A 1 3236 ALA 3236 3236 3236 ALA ALA A . n 
A 1 3237 ASN 3237 3237 3237 ASN ASN A . n 
A 1 3238 ASP 3238 3238 3238 ASP ASP A . n 
A 1 3239 LYS 3239 3239 3239 LYS LYS A . n 
A 1 3240 LEU 3240 3240 3240 LEU LEU A . n 
A 1 3241 LYS 3241 3241 3241 LYS LYS A . n 
A 1 3242 LYS 3242 3242 3242 LYS LYS A . n 
A 1 3243 MET 3243 3243 ?    ?   ?   A . n 
A 1 3244 VAL 3244 3244 ?    ?   ?   A . n 
A 1 3245 LYS 3245 3245 ?    ?   ?   A . n 
A 1 3246 ASP 3246 3246 ?    ?   ?   A . n 
A 1 3247 GLN 3247 3247 ?    ?   ?   A . n 
A 1 3248 GLN 3248 3248 ?    ?   ?   A . n 
A 1 3249 GLU 3249 3249 ?    ?   ?   A . n 
A 1 3250 ALA 3250 3250 ?    ?   ?   A . n 
A 1 3251 GLU 3251 3251 ?    ?   ?   A . n 
A 1 3252 LYS 3252 3252 ?    ?   ?   A . n 
A 1 3253 LYS 3253 3253 ?    ?   ?   A . n 
A 1 3254 LYS 3254 3254 ?    ?   ?   A . n 
A 1 3255 VAL 3255 3255 ?    ?   ?   A . n 
A 1 3256 MET 3256 3256 ?    ?   ?   A . n 
A 1 3257 SER 3257 3257 ?    ?   ?   A . n 
A 1 3258 GLN 3258 3258 ?    ?   ?   A . n 
A 1 3259 GLU 3259 3259 ?    ?   ?   A . n 
A 1 3260 ILE 3260 3260 ?    ?   ?   A . n 
A 1 3261 GLN 3261 3261 ?    ?   ?   A . n 
A 1 3262 GLU 3262 3262 ?    ?   ?   A . n 
A 1 3263 GLN 3263 3263 ?    ?   ?   A . n 
A 1 3264 LEU 3264 3264 ?    ?   ?   A . n 
A 1 3265 HIS 3265 3265 ?    ?   ?   A . n 
A 1 3266 LYS 3266 3266 ?    ?   ?   A . n 
A 1 3267 GLN 3267 3267 ?    ?   ?   A . n 
A 1 3268 GLN 3268 3268 ?    ?   ?   A . n 
A 1 3269 GLU 3269 3269 ?    ?   ?   A . n 
A 1 3270 VAL 3270 3270 ?    ?   ?   A . n 
A 1 3271 ILE 3271 3271 ?    ?   ?   A . n 
A 1 3272 ALA 3272 3272 ?    ?   ?   A . n 
A 1 3273 ASP 3273 3273 ?    ?   ?   A . n 
A 1 3274 LYS 3274 3274 ?    ?   ?   A . n 
A 1 3275 GLN 3275 3275 ?    ?   ?   A . n 
A 1 3276 MET 3276 3276 ?    ?   ?   A . n 
A 1 3277 SER 3277 3277 ?    ?   ?   A . n 
A 1 3278 VAL 3278 3278 ?    ?   ?   A . n 
A 1 3279 LYS 3279 3279 ?    ?   ?   A . n 
A 1 3280 GLU 3280 3280 ?    ?   ?   A . n 
A 1 3281 ASP 3281 3281 ?    ?   ?   A . n 
A 1 3282 LEU 3282 3282 ?    ?   ?   A . n 
A 1 3283 ASP 3283 3283 ?    ?   ?   A . n 
A 1 3284 LYS 3284 3284 ?    ?   ?   A . n 
A 1 3285 VAL 3285 3285 ?    ?   ?   A . n 
A 1 3286 GLU 3286 3286 ?    ?   ?   A . n 
A 1 3287 PRO 3287 3287 ?    ?   ?   A . n 
A 1 3288 ALA 3288 3288 ?    ?   ?   A . n 
A 1 3289 VAL 3289 3289 ?    ?   ?   A . n 
A 1 3290 ILE 3290 3290 ?    ?   ?   A . n 
A 1 3291 GLU 3291 3291 ?    ?   ?   A . n 
A 1 3292 ALA 3292 3292 ?    ?   ?   A . n 
A 1 3293 GLN 3293 3293 ?    ?   ?   A . n 
A 1 3294 ASN 3294 3294 ?    ?   ?   A . n 
A 1 3295 ALA 3295 3295 ?    ?   ?   A . n 
A 1 3296 VAL 3296 3296 ?    ?   ?   A . n 
A 1 3297 LYS 3297 3297 ?    ?   ?   A . n 
A 1 3298 SER 3298 3298 ?    ?   ?   A . n 
A 1 3299 ILE 3299 3299 ?    ?   ?   A . n 
A 1 3300 LYS 3300 3300 ?    ?   ?   A . n 
A 1 3301 LYS 3301 3301 ?    ?   ?   A . n 
A 1 3302 GLN 3302 3302 ?    ?   ?   A . n 
A 1 3303 HIS 3303 3303 ?    ?   ?   A . n 
A 1 3304 LEU 3304 3304 ?    ?   ?   A . n 
A 1 3305 VAL 3305 3305 ?    ?   ?   A . n 
A 1 3306 GLU 3306 3306 ?    ?   ?   A . n 
A 1 3307 VAL 3307 3307 ?    ?   ?   A . n 
A 1 3308 ARG 3308 3308 ?    ?   ?   A . n 
A 1 3309 SER 3309 3309 ?    ?   ?   A . n 
A 1 3310 MET 3310 3310 ?    ?   ?   A . n 
A 1 3311 ALA 3311 3311 ?    ?   ?   A . n 
A 1 3312 ASN 3312 3312 ?    ?   ?   A . n 
A 1 3313 PRO 3313 3313 ?    ?   ?   A . n 
A 1 3314 PRO 3314 3314 ?    ?   ?   A . n 
A 1 3315 ALA 3315 3315 ?    ?   ?   A . n 
A 1 3316 ALA 3316 3316 ?    ?   ?   A . n 
A 1 3317 VAL 3317 3317 ?    ?   ?   A . n 
A 1 3318 LYS 3318 3318 ?    ?   ?   A . n 
A 1 3319 LEU 3319 3319 ?    ?   ?   A . n 
A 1 3320 ALA 3320 3320 ?    ?   ?   A . n 
A 1 3321 LEU 3321 3321 ?    ?   ?   A . n 
A 1 3322 GLU 3322 3322 ?    ?   ?   A . n 
A 1 3323 SER 3323 3323 ?    ?   ?   A . n 
A 1 3324 ILE 3324 3324 ?    ?   ?   A . n 
A 1 3325 CYS 3325 3325 ?    ?   ?   A . n 
A 1 3326 LEU 3326 3326 ?    ?   ?   A . n 
A 1 3327 LEU 3327 3327 ?    ?   ?   A . n 
A 1 3328 LEU 3328 3328 ?    ?   ?   A . n 
A 1 3329 GLY 3329 3329 ?    ?   ?   A . n 
A 1 3330 GLU 3330 3330 ?    ?   ?   A . n 
A 1 3331 SER 3331 3331 ?    ?   ?   A . n 
A 1 3332 THR 3332 3332 ?    ?   ?   A . n 
A 1 3333 THR 3333 3333 ?    ?   ?   A . n 
A 1 3334 ASP 3334 3334 ?    ?   ?   A . n 
A 1 3335 TRP 3335 3335 ?    ?   ?   A . n 
A 1 3336 LYS 3336 3336 ?    ?   ?   A . n 
A 1 3337 GLN 3337 3337 ?    ?   ?   A . n 
A 1 3338 ILE 3338 3338 ?    ?   ?   A . n 
A 1 3339 ARG 3339 3339 ?    ?   ?   A . n 
A 1 3340 SER 3340 3340 ?    ?   ?   A . n 
A 1 3341 ILE 3341 3341 ?    ?   ?   A . n 
A 1 3342 ILE 3342 3342 ?    ?   ?   A . n 
A 1 3343 MET 3343 3343 ?    ?   ?   A . n 
A 1 3344 ARG 3344 3344 ?    ?   ?   A . n 
A 1 3345 GLU 3345 3345 ?    ?   ?   A . n 
A 1 3346 ASN 3346 3346 ?    ?   ?   A . n 
A 1 3347 PHE 3347 3347 ?    ?   ?   A . n 
A 1 3348 ILE 3348 3348 ?    ?   ?   A . n 
A 1 3349 PRO 3349 3349 ?    ?   ?   A . n 
A 1 3350 THR 3350 3350 ?    ?   ?   A . n 
A 1 3351 ILE 3351 3351 ?    ?   ?   A . n 
A 1 3352 VAL 3352 3352 ?    ?   ?   A . n 
A 1 3353 ASN 3353 3353 ?    ?   ?   A . n 
A 1 3354 PHE 3354 3354 ?    ?   ?   A . n 
A 1 3355 SER 3355 3355 ?    ?   ?   A . n 
A 1 3356 ALA 3356 3356 ?    ?   ?   A . n 
A 1 3357 GLU 3357 3357 ?    ?   ?   A . n 
A 1 3358 GLU 3358 3358 ?    ?   ?   A . n 
A 1 3359 ILE 3359 3359 ?    ?   ?   A . n 
A 1 3360 SER 3360 3360 ?    ?   ?   A . n 
A 1 3361 ASP 3361 3361 ?    ?   ?   A . n 
A 1 3362 ALA 3362 3362 ?    ?   ?   A . n 
A 1 3363 ILE 3363 3363 ?    ?   ?   A . n 
A 1 3364 ARG 3364 3364 ?    ?   ?   A . n 
A 1 3365 GLU 3365 3365 ?    ?   ?   A . n 
A 1 3366 LYS 3366 3366 ?    ?   ?   A . n 
A 1 3367 MET 3367 3367 ?    ?   ?   A . n 
A 1 3368 LYS 3368 3368 ?    ?   ?   A . n 
A 1 3369 LYS 3369 3369 ?    ?   ?   A . n 
A 1 3370 ASN 3370 3370 ?    ?   ?   A . n 
A 1 3371 TYR 3371 3371 ?    ?   ?   A . n 
A 1 3372 MET 3372 3372 ?    ?   ?   A . n 
A 1 3373 SER 3373 3373 ?    ?   ?   A . n 
A 1 3374 ASN 3374 3374 ?    ?   ?   A . n 
A 1 3375 PRO 3375 3375 ?    ?   ?   A . n 
A 1 3376 SER 3376 3376 ?    ?   ?   A . n 
A 1 3377 TYR 3377 3377 ?    ?   ?   A . n 
A 1 3378 ASN 3378 3378 ?    ?   ?   A . n 
A 1 3379 TYR 3379 3379 ?    ?   ?   A . n 
A 1 3380 GLU 3380 3380 ?    ?   ?   A . n 
A 1 3381 ILE 3381 3381 ?    ?   ?   A . n 
A 1 3382 VAL 3382 3382 ?    ?   ?   A . n 
A 1 3383 ASN 3383 3383 ?    ?   ?   A . n 
A 1 3384 ARG 3384 3384 ?    ?   ?   A . n 
A 1 3385 ALA 3385 3385 ?    ?   ?   A . n 
A 1 3386 SER 3386 3386 ?    ?   ?   A . n 
A 1 3387 LEU 3387 3387 ?    ?   ?   A . n 
A 1 3388 ALA 3388 3388 ?    ?   ?   A . n 
A 1 3389 CYS 3389 3389 ?    ?   ?   A . n 
A 1 3390 GLY 3390 3390 ?    ?   ?   A . n 
A 1 3391 PRO 3391 3391 ?    ?   ?   A . n 
A 1 3392 MET 3392 3392 ?    ?   ?   A . n 
A 1 3393 VAL 3393 3393 ?    ?   ?   A . n 
A 1 3394 LYS 3394 3394 ?    ?   ?   A . n 
A 1 3395 TRP 3395 3395 ?    ?   ?   A . n 
A 1 3396 ALA 3396 3396 ?    ?   ?   A . n 
A 1 3397 ILE 3397 3397 ?    ?   ?   A . n 
A 1 3398 ALA 3398 3398 ?    ?   ?   A . n 
A 1 3399 GLN 3399 3399 ?    ?   ?   A . n 
A 1 3400 LEU 3400 3400 ?    ?   ?   A . n 
A 1 3401 ASN 3401 3401 ?    ?   ?   A . n 
A 1 3402 TYR 3402 3402 ?    ?   ?   A . n 
A 1 3403 ALA 3403 3403 ?    ?   ?   A . n 
A 1 3404 ASP 3404 3404 ?    ?   ?   A . n 
A 1 3405 MET 3405 3405 ?    ?   ?   A . n 
A 1 3406 LEU 3406 3406 ?    ?   ?   A . n 
A 1 3407 LYS 3407 3407 ?    ?   ?   A . n 
A 1 3408 ARG 3408 3408 ?    ?   ?   A . n 
A 1 3409 VAL 3409 3409 ?    ?   ?   A . n 
A 1 3410 GLU 3410 3410 ?    ?   ?   A . n 
A 1 3411 PRO 3411 3411 ?    ?   ?   A . n 
A 1 3412 LEU 3412 3412 ?    ?   ?   A . n 
A 1 3413 ARG 3413 3413 ?    ?   ?   A . n 
A 1 3414 ASN 3414 3414 ?    ?   ?   A . n 
A 1 3415 GLU 3415 3415 ?    ?   ?   A . n 
A 1 3416 LEU 3416 3416 ?    ?   ?   A . n 
A 1 3417 GLN 3417 3417 ?    ?   ?   A . n 
A 1 3418 LYS 3418 3418 ?    ?   ?   A . n 
A 1 3419 LEU 3419 3419 ?    ?   ?   A . n 
A 1 3420 GLU 3420 3420 ?    ?   ?   A . n 
A 1 3421 ASP 3421 3421 ?    ?   ?   A . n 
A 1 3422 ASP 3422 3422 ?    ?   ?   A . n 
A 1 3423 ALA 3423 3423 ?    ?   ?   A . n 
A 1 3424 LYS 3424 3424 ?    ?   ?   A . n 
A 1 3425 ASP 3425 3425 ?    ?   ?   A . n 
A 1 3426 ASN 3426 3426 ?    ?   ?   A . n 
A 1 3427 GLN 3427 3427 ?    ?   ?   A . n 
A 1 3428 GLN 3428 3428 ?    ?   ?   A . n 
A 1 3429 LYS 3429 3429 ?    ?   ?   A . n 
A 1 3430 ALA 3430 3430 ?    ?   ?   A . n 
A 1 3431 ASN 3431 3431 ?    ?   ?   A . n 
A 1 3432 GLU 3432 3432 ?    ?   ?   A . n 
A 1 3433 VAL 3433 3433 ?    ?   ?   A . n 
A 1 3434 GLU 3434 3434 ?    ?   ?   A . n 
A 1 3435 GLN 3435 3435 ?    ?   ?   A . n 
A 1 3436 MET 3436 3436 ?    ?   ?   A . n 
A 1 3437 ILE 3437 3437 ?    ?   ?   A . n 
A 1 3438 ARG 3438 3438 ?    ?   ?   A . n 
A 1 3439 ASP 3439 3439 ?    ?   ?   A . n 
A 1 3440 LEU 3440 3440 ?    ?   ?   A . n 
A 1 3441 GLU 3441 3441 ?    ?   ?   A . n 
A 1 3442 ALA 3442 3442 ?    ?   ?   A . n 
A 1 3443 SER 3443 3443 ?    ?   ?   A . n 
A 1 3444 ILE 3444 3444 ?    ?   ?   A . n 
A 1 3445 ALA 3445 3445 ?    ?   ?   A . n 
A 1 3446 ARG 3446 3446 ?    ?   ?   A . n 
A 1 3447 TYR 3447 3447 ?    ?   ?   A . n 
A 1 3448 LYS 3448 3448 ?    ?   ?   A . n 
A 1 3449 GLU 3449 3449 3449 GLU GLU A . n 
A 1 3450 GLU 3450 3450 3450 GLU GLU A . n 
A 1 3451 TYR 3451 3451 3451 TYR TYR A . n 
A 1 3452 ALA 3452 3452 3452 ALA ALA A . n 
A 1 3453 VAL 3453 3453 3453 VAL VAL A . n 
A 1 3454 LEU 3454 3454 3454 LEU LEU A . n 
A 1 3455 ILE 3455 3455 3455 ILE ILE A . n 
A 1 3456 SER 3456 3456 3456 SER SER A . n 
A 1 3457 GLU 3457 3457 3457 GLU GLU A . n 
A 1 3458 ALA 3458 3458 3458 ALA ALA A . n 
A 1 3459 GLN 3459 3459 3459 GLN GLN A . n 
A 1 3460 ALA 3460 3460 3460 ALA ALA A . n 
A 1 3461 ILE 3461 3461 3461 ILE ILE A . n 
A 1 3462 LYS 3462 3462 3462 LYS LYS A . n 
A 1 3463 ALA 3463 3463 3463 ALA ALA A . n 
A 1 3464 ASP 3464 3464 3464 ASP ASP A . n 
A 1 3465 LEU 3465 3465 3465 LEU LEU A . n 
A 1 3466 ALA 3466 3466 3466 ALA ALA A . n 
A 1 3467 ALA 3467 3467 3467 ALA ALA A . n 
A 1 3468 VAL 3468 3468 3468 VAL VAL A . n 
A 1 3469 GLU 3469 3469 3469 GLU GLU A . n 
A 1 3470 ALA 3470 3470 3470 ALA ALA A . n 
A 1 3471 LYS 3471 3471 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ASP A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 ?    ?   ?   A . n 
A 1 4349 LEU 4349 4349 ?    ?   ?   A . n 
A 1 4350 GLU 4350 4350 ?    ?   ?   A . n 
A 1 4351 ASP 4351 4351 ?    ?   ?   A . n 
A 1 4352 GLU 4352 4352 ?    ?   ?   A . n 
A 1 4353 ASP 4353 4353 ?    ?   ?   A . n 
A 1 4354 ASP 4354 4354 ?    ?   ?   A . n 
A 1 4355 LEU 4355 4355 ?    ?   ?   A . n 
A 1 4356 ALA 4356 4356 ?    ?   ?   A . n 
A 1 4357 TYR 4357 4357 ?    ?   ?   A . n 
A 1 4358 ALA 4358 4358 ?    ?   ?   A . n 
A 1 4359 GLU 4359 4359 ?    ?   ?   A . n 
A 1 4360 THR 4360 4360 ?    ?   ?   A . n 
A 1 4361 GLU 4361 4361 ?    ?   ?   A . n 
A 1 4362 LYS 4362 4362 ?    ?   ?   A . n 
A 1 4363 LYS 4363 4363 ?    ?   ?   A . n 
A 1 4364 THR 4364 4364 ?    ?   ?   A . n 
A 1 4365 ARG 4365 4365 ?    ?   ?   A . n 
A 1 4366 THR 4366 4366 ?    ?   ?   A . n 
A 1 4367 ASP 4367 4367 ?    ?   ?   A . n 
A 1 4368 SER 4368 4368 ?    ?   ?   A . n 
A 1 4369 THR 4369 4369 ?    ?   ?   A . n 
A 1 4370 SER 4370 4370 ?    ?   ?   A . n 
A 1 4371 ASP 4371 4371 ?    ?   ?   A . n 
A 1 4372 GLY 4372 4372 ?    ?   ?   A . n 
A 1 4373 ARG 4373 4373 ?    ?   ?   A . n 
A 1 4374 PRO 4374 4374 4374 PRO PRO A . n 
A 1 4375 ALA 4375 4375 4375 ALA ALA A . n 
A 1 4376 TRP 4376 4376 4376 TRP TRP A . n 
A 1 4377 MET 4377 4377 4377 MET MET A . n 
A 1 4378 ARG 4378 4378 4378 ARG ARG A . n 
A 1 4379 THR 4379 4379 4379 THR THR A . n 
A 1 4380 LEU 4380 4380 4380 LEU LEU A . n 
A 1 4381 HIS 4381 4381 4381 HIS HIS A . n 
A 1 4382 THR 4382 4382 4382 THR THR A . n 
A 1 4383 THR 4383 4383 4383 THR THR A . n 
A 1 4384 ALA 4384 4384 4384 ALA ALA A . n 
A 1 4385 SER 4385 4385 4385 SER SER A . n 
A 1 4386 ASN 4386 4386 4386 ASN ASN A . n 
A 1 4387 TRP 4387 4387 4387 TRP TRP A . n 
A 1 4388 LEU 4388 4388 4388 LEU LEU A . n 
A 1 4389 HIS 4389 4389 4389 HIS HIS A . n 
A 1 4390 LEU 4390 4390 4390 LEU LEU A . n 
A 1 4391 ILE 4391 4391 4391 ILE ILE A . n 
A 1 4392 PRO 4392 4392 4392 PRO PRO A . n 
A 1 4393 GLN 4393 4393 4393 GLN GLN A . n 
A 1 4394 THR 4394 4394 4394 THR THR A . n 
A 1 4395 LEU 4395 4395 4395 LEU LEU A . n 
A 1 4396 SER 4396 4396 4396 SER SER A . n 
A 1 4397 HIS 4397 4397 4397 HIS HIS A . n 
A 1 4398 LEU 4398 4398 4398 LEU LEU A . n 
A 1 4399 LYS 4399 4399 4399 LYS LYS A . n 
A 1 4400 ARG 4400 4400 4400 ARG ARG A . n 
A 1 4401 THR 4401 4401 4401 THR THR A . n 
A 1 4402 VAL 4402 4402 4402 VAL VAL A . n 
A 1 4403 GLU 4403 4403 4403 GLU GLU A . n 
A 1 4404 ASN 4404 4404 4404 ASN ASN A . n 
A 1 4405 ILE 4405 4405 4405 ILE ILE A . n 
A 1 4406 LYS 4406 4406 4406 LYS LYS A . n 
A 1 4407 ASP 4407 4407 4407 ASP ASP A . n 
A 1 4408 PRO 4408 4408 4408 PRO PRO A . n 
A 1 4409 LEU 4409 4409 4409 LEU LEU A . n 
A 1 4410 PHE 4410 4410 4410 PHE PHE A . n 
A 1 4411 ARG 4411 4411 4411 ARG ARG A . n 
A 1 4412 PHE 4412 4412 4412 PHE PHE A . n 
A 1 4413 PHE 4413 4413 4413 PHE PHE A . n 
A 1 4414 GLU 4414 4414 4414 GLU GLU A . n 
A 1 4415 ARG 4415 4415 4415 ARG ARG A . n 
A 1 4416 GLU 4416 4416 4416 GLU GLU A . n 
A 1 4417 VAL 4417 4417 4417 VAL VAL A . n 
A 1 4418 LYS 4418 4418 4418 LYS LYS A . n 
A 1 4419 MET 4419 4419 4419 MET MET A . n 
A 1 4420 GLY 4420 4420 4420 GLY GLY A . n 
A 1 4421 ALA 4421 4421 4421 ALA ALA A . n 
A 1 4422 LYS 4422 4422 4422 LYS LYS A . n 
A 1 4423 LEU 4423 4423 4423 LEU LEU A . n 
A 1 4424 LEU 4424 4424 4424 LEU LEU A . n 
A 1 4425 GLN 4425 4425 4425 GLN GLN A . n 
A 1 4426 ASP 4426 4426 4426 ASP ASP A . n 
A 1 4427 VAL 4427 4427 4427 VAL VAL A . n 
A 1 4428 ARG 4428 4428 4428 ARG ARG A . n 
A 1 4429 GLN 4429 4429 4429 GLN GLN A . n 
A 1 4430 ASP 4430 4430 4430 ASP ASP A . n 
A 1 4431 LEU 4431 4431 4431 LEU LEU A . n 
A 1 4432 ALA 4432 4432 4432 ALA ALA A . n 
A 1 4433 ASP 4433 4433 4433 ASP ASP A . n 
A 1 4434 VAL 4434 4434 4434 VAL VAL A . n 
A 1 4435 VAL 4435 4435 4435 VAL VAL A . n 
A 1 4436 GLN 4436 4436 4436 GLN GLN A . n 
A 1 4437 VAL 4437 4437 4437 VAL VAL A . n 
A 1 4438 CYS 4438 4438 4438 CYS CYS A . n 
A 1 4439 GLU 4439 4439 4439 GLU GLU A . n 
A 1 4440 GLY 4440 4440 4440 GLY GLY A . n 
A 1 4441 LYS 4441 4441 4441 LYS LYS A . n 
A 1 4442 LYS 4442 4442 4442 LYS LYS A . n 
A 1 4443 LYS 4443 4443 4443 LYS LYS A . n 
A 1 4444 GLN 4444 4444 4444 GLN GLN A . n 
A 1 4445 THR 4445 4445 4445 THR THR A . n 
A 1 4446 ASN 4446 4446 4446 ASN ASN A . n 
A 1 4447 TYR 4447 4447 4447 TYR TYR A . n 
A 1 4448 LEU 4448 4448 4448 LEU LEU A . n 
A 1 4449 ARG 4449 4449 4449 ARG ARG A . n 
A 1 4450 THR 4450 4450 4450 THR THR A . n 
A 1 4451 LEU 4451 4451 4451 LEU LEU A . n 
A 1 4452 ILE 4452 4452 4452 ILE ILE A . n 
A 1 4453 ASN 4453 4453 4453 ASN ASN A . n 
A 1 4454 GLU 4454 4454 4454 GLU GLU A . n 
A 1 4455 LEU 4455 4455 4455 LEU LEU A . n 
A 1 4456 VAL 4456 4456 4456 VAL VAL A . n 
A 1 4457 LYS 4457 4457 4457 LYS LYS A . n 
A 1 4458 GLY 4458 4458 4458 GLY GLY A . n 
A 1 4459 ILE 4459 4459 4459 ILE ILE A . n 
A 1 4460 LEU 4460 4460 4460 LEU LEU A . n 
A 1 4461 PRO 4461 4461 4461 PRO PRO A . n 
A 1 4462 ARG 4462 4462 4462 ARG ARG A . n 
A 1 4463 SER 4463 4463 4463 SER SER A . n 
A 1 4464 TRP 4464 4464 4464 TRP TRP A . n 
A 1 4465 SER 4465 4465 4465 SER SER A . n 
A 1 4466 HIS 4466 4466 4466 HIS HIS A . n 
A 1 4467 TYR 4467 4467 4467 TYR TYR A . n 
A 1 4468 THR 4468 4468 4468 THR THR A . n 
A 1 4469 VAL 4469 4469 4469 VAL VAL A . n 
A 1 4470 PRO 4470 4470 4470 PRO PRO A . n 
A 1 4471 ALA 4471 4471 4471 ALA ALA A . n 
A 1 4472 GLY 4472 4472 4472 GLY GLY A . n 
A 1 4473 MET 4473 4473 4473 MET MET A . n 
A 1 4474 THR 4474 4474 4474 THR THR A . n 
A 1 4475 VAL 4475 4475 4475 VAL VAL A . n 
A 1 4476 ILE 4476 4476 4476 ILE ILE A . n 
A 1 4477 GLN 4477 4477 4477 GLN GLN A . n 
A 1 4478 TRP 4478 4478 4478 TRP TRP A . n 
A 1 4479 VAL 4479 4479 4479 VAL VAL A . n 
A 1 4480 SER 4480 4480 4480 SER SER A . n 
A 1 4481 ASP 4481 4481 4481 ASP ASP A . n 
A 1 4482 PHE 4482 4482 4482 PHE PHE A . n 
A 1 4483 SER 4483 4483 4483 SER SER A . n 
A 1 4484 GLU 4484 4484 4484 GLU GLU A . n 
A 1 4485 ARG 4485 4485 4485 ARG ARG A . n 
A 1 4486 ILE 4486 4486 4486 ILE ILE A . n 
A 1 4487 LYS 4487 4487 4487 LYS LYS A . n 
A 1 4488 GLN 4488 4488 4488 GLN GLN A . n 
A 1 4489 LEU 4489 4489 4489 LEU LEU A . n 
A 1 4490 GLN 4490 4490 4490 GLN GLN A . n 
A 1 4491 ASN 4491 4491 4491 ASN ASN A . n 
A 1 4492 ILE 4492 4492 4492 ILE ILE A . n 
A 1 4493 SER 4493 4493 4493 SER SER A . n 
A 1 4494 LEU 4494 4494 4494 LEU LEU A . n 
A 1 4495 ALA 4495 4495 4495 ALA ALA A . n 
A 1 4496 ALA 4496 4496 4496 ALA ALA A . n 
A 1 4497 ALA 4497 4497 4497 ALA ALA A . n 
A 1 4498 SER 4498 4498 4498 SER SER A . n 
A 1 4499 GLY 4499 4499 4499 GLY GLY A . n 
A 1 4500 GLY 4500 4500 4500 GLY GLY A . n 
A 1 4501 ALA 4501 4501 4501 ALA ALA A . n 
A 1 4502 LYS 4502 4502 4502 LYS LYS A . n 
A 1 4503 GLU 4503 4503 4503 GLU GLU A . n 
A 1 4504 LEU 4504 4504 4504 LEU LEU A . n 
A 1 4505 LYS 4505 4505 4505 LYS LYS A . n 
A 1 4506 ASN 4506 4506 4506 ASN ASN A . n 
A 1 4507 ILE 4507 4507 4507 ILE ILE A . n 
A 1 4508 HIS 4508 4508 4508 HIS HIS A . n 
A 1 4509 VAL 4509 4509 4509 VAL VAL A . n 
A 1 4510 CYS 4510 4510 4510 CYS CYS A . n 
A 1 4511 LEU 4511 4511 4511 LEU LEU A . n 
A 1 4512 GLY 4512 4512 4512 GLY GLY A . n 
A 1 4513 GLY 4513 4513 4513 GLY GLY A . n 
A 1 4514 LEU 4514 4514 4514 LEU LEU A . n 
A 1 4515 PHE 4515 4515 4515 PHE PHE A . n 
A 1 4516 VAL 4516 4516 4516 VAL VAL A . n 
A 1 4517 PRO 4517 4517 4517 PRO PRO A . n 
A 1 4518 GLU 4518 4518 4518 GLU GLU A . n 
A 1 4519 ALA 4519 4519 4519 ALA ALA A . n 
A 1 4520 TYR 4520 4520 4520 TYR TYR A . n 
A 1 4521 ILE 4521 4521 4521 ILE ILE A . n 
A 1 4522 THR 4522 4522 4522 THR THR A . n 
A 1 4523 ALA 4523 4523 4523 ALA ALA A . n 
A 1 4524 THR 4524 4524 4524 THR THR A . n 
A 1 4525 ARG 4525 4525 4525 ARG ARG A . n 
A 1 4526 GLN 4526 4526 4526 GLN GLN A . n 
A 1 4527 TYR 4527 4527 4527 TYR TYR A . n 
A 1 4528 VAL 4528 4528 4528 VAL VAL A . n 
A 1 4529 ALA 4529 4529 4529 ALA ALA A . n 
A 1 4530 GLN 4530 4530 4530 GLN GLN A . n 
A 1 4531 ALA 4531 4531 4531 ALA ALA A . n 
A 1 4532 ASN 4532 4532 4532 ASN ASN A . n 
A 1 4533 SER 4533 4533 4533 SER SER A . n 
A 1 4534 TRP 4534 4534 4534 TRP TRP A . n 
A 1 4535 SER 4535 4535 4535 SER SER A . n 
A 1 4536 LEU 4536 4536 4536 LEU LEU A . n 
A 1 4537 GLU 4537 4537 4537 GLU GLU A . n 
A 1 4538 GLU 4538 4538 4538 GLU GLU A . n 
A 1 4539 LEU 4539 4539 4539 LEU LEU A . n 
A 1 4540 CYS 4540 4540 4540 CYS CYS A . n 
A 1 4541 LEU 4541 4541 4541 LEU LEU A . n 
A 1 4542 GLU 4542 4542 4542 GLU GLU A . n 
A 1 4543 VAL 4543 4543 4543 VAL VAL A . n 
A 1 4544 ASN 4544 4544 4544 ASN ASN A . n 
A 1 4545 VAL 4545 4545 4545 VAL VAL A . n 
A 1 4546 THR 4546 4546 4546 THR THR A . n 
A 1 4547 THR 4547 4547 4547 THR THR A . n 
A 1 4548 SER 4548 4548 4548 SER SER A . n 
A 1 4549 GLN 4549 4549 4549 GLN GLN A . n 
A 1 4550 GLY 4550 4550 4550 GLY GLY A . n 
A 1 4551 ALA 4551 4551 4551 ALA ALA A . n 
A 1 4552 THR 4552 4552 4552 THR THR A . n 
A 1 4553 LEU 4553 4553 4553 LEU LEU A . n 
A 1 4554 ASP 4554 4554 4554 ASP ASP A . n 
A 1 4555 ALA 4555 4555 4555 ALA ALA A . n 
A 1 4556 CYS 4556 4556 4556 CYS CYS A . n 
A 1 4557 SER 4557 4557 4557 SER SER A . n 
A 1 4558 PHE 4558 4558 4558 PHE PHE A . n 
A 1 4559 GLY 4559 4559 4559 GLY GLY A . n 
A 1 4560 VAL 4560 4560 4560 VAL VAL A . n 
A 1 4561 THR 4561 4561 4561 THR THR A . n 
A 1 4562 GLY 4562 4562 4562 GLY GLY A . n 
A 1 4563 LEU 4563 4563 4563 LEU LEU A . n 
A 1 4564 LYS 4564 4564 4564 LYS LYS A . n 
A 1 4565 LEU 4565 4565 4565 LEU LEU A . n 
A 1 4566 GLN 4566 4566 4566 GLN GLN A . n 
A 1 4567 GLY 4567 4567 4567 GLY GLY A . n 
A 1 4568 ALA 4568 4568 4568 ALA ALA A . n 
A 1 4569 THR 4569 4569 4569 THR THR A . n 
A 1 4570 CYS 4570 4570 4570 CYS CYS A . n 
A 1 4571 ASN 4571 4571 4571 ASN ASN A . n 
A 1 4572 ASN 4572 4572 4572 ASN ASN A . n 
A 1 4573 ASN 4573 4573 4573 ASN ASN A . n 
A 1 4574 LYS 4574 4574 4574 LYS LYS A . n 
A 1 4575 LEU 4575 4575 4575 LEU LEU A . n 
A 1 4576 SER 4576 4576 4576 SER SER A . n 
A 1 4577 LEU 4577 4577 4577 LEU LEU A . n 
A 1 4578 SER 4578 4578 4578 SER SER A . n 
A 1 4579 ASN 4579 4579 4579 ASN ASN A . n 
A 1 4580 ALA 4580 4580 4580 ALA ALA A . n 
A 1 4581 ILE 4581 4581 4581 ILE ILE A . n 
A 1 4582 SER 4582 4582 4582 SER SER A . n 
A 1 4583 THR 4583 4583 4583 THR THR A . n 
A 1 4584 ALA 4584 4584 4584 ALA ALA A . n 
A 1 4585 LEU 4585 4585 4585 LEU LEU A . n 
A 1 4586 PRO 4586 4586 4586 PRO PRO A . n 
A 1 4587 LEU 4587 4587 4587 LEU LEU A . n 
A 1 4588 THR 4588 4588 4588 THR THR A . n 
A 1 4589 GLN 4589 4589 4589 GLN GLN A . n 
A 1 4590 LEU 4590 4590 4590 LEU LEU A . n 
A 1 4591 ARG 4591 4591 4591 ARG ARG A . n 
A 1 4592 TRP 4592 4592 4592 TRP TRP A . n 
A 1 4593 VAL 4593 4593 4593 VAL VAL A . n 
A 1 4594 LYS 4594 4594 4594 LYS LYS A . n 
A 1 4595 GLN 4595 4595 4595 GLN GLN A . n 
A 1 4596 THR 4596 4596 4596 THR THR A . n 
A 1 4597 ASN 4597 4597 4597 ASN ASN A . n 
A 1 4598 THR 4598 4598 4598 THR THR A . n 
A 1 4599 GLU 4599 4599 4599 GLU GLU A . n 
A 1 4600 LYS 4600 4600 4600 LYS LYS A . n 
A 1 4601 LYS 4601 4601 4601 LYS LYS A . n 
A 1 4602 ALA 4602 4602 4602 ALA ALA A . n 
A 1 4603 SER 4603 4603 4603 SER SER A . n 
A 1 4604 VAL 4604 4604 4604 VAL VAL A . n 
A 1 4605 VAL 4605 4605 4605 VAL VAL A . n 
A 1 4606 THR 4606 4606 4606 THR THR A . n 
A 1 4607 LEU 4607 4607 4607 LEU LEU A . n 
A 1 4608 PRO 4608 4608 4608 PRO PRO A . n 
A 1 4609 VAL 4609 4609 4609 VAL VAL A . n 
A 1 4610 TYR 4610 4610 4610 TYR TYR A . n 
A 1 4611 LEU 4611 4611 4611 LEU LEU A . n 
A 1 4612 ASN 4612 4612 4612 ASN ASN A . n 
A 1 4613 PHE 4613 4613 4613 PHE PHE A . n 
A 1 4614 THR 4614 4614 4614 THR THR A . n 
A 1 4615 ARG 4615 4615 4615 ARG ARG A . n 
A 1 4616 ALA 4616 4616 4616 ALA ALA A . n 
A 1 4617 ASP 4617 4617 4617 ASP ASP A . n 
A 1 4618 LEU 4618 4618 4618 LEU LEU A . n 
A 1 4619 ILE 4619 4619 4619 ILE ILE A . n 
A 1 4620 PHE 4620 4620 4620 PHE PHE A . n 
A 1 4621 THR 4621 4621 4621 THR THR A . n 
A 1 4622 VAL 4622 4622 4622 VAL VAL A . n 
A 1 4623 ASP 4623 4623 4623 ASP ASP A . n 
A 1 4624 PHE 4624 4624 4624 PHE PHE A . n 
A 1 4625 GLU 4625 4625 4625 GLU GLU A . n 
A 1 4626 ILE 4626 4626 4626 ILE ILE A . n 
A 1 4627 ALA 4627 4627 4627 ALA ALA A . n 
A 1 4628 THR 4628 4628 4628 THR THR A . n 
A 1 4629 LYS 4629 4629 4629 LYS LYS A . n 
A 1 4630 GLU 4630 4630 4630 GLU GLU A . n 
A 1 4631 ASP 4631 4631 4631 ASP ASP A . n 
A 1 4632 PRO 4632 4632 4632 PRO PRO A . n 
A 1 4633 ARG 4633 4633 4633 ARG ARG A . n 
A 1 4634 SER 4634 4634 4634 SER SER A . n 
A 1 4635 PHE 4635 4635 4635 PHE PHE A . n 
A 1 4636 TYR 4636 4636 4636 TYR TYR A . n 
A 1 4637 GLU 4637 4637 4637 GLU GLU A . n 
A 1 4638 ARG 4638 4638 4638 ARG ARG A . n 
A 1 4639 GLY 4639 4639 4639 GLY GLY A . n 
A 1 4640 VAL 4640 4640 4640 VAL VAL A . n 
A 1 4641 ALA 4641 4641 4641 ALA ALA A . n 
A 1 4642 VAL 4642 4642 4642 VAL VAL A . n 
A 1 4643 LEU 4643 4643 4643 LEU LEU A . n 
A 1 4644 CYS 4644 4644 4644 CYS CYS A . n 
A 1 4645 THR 4645 4645 4645 THR THR A . n 
A 1 4646 GLU 4646 4646 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1 4701 4701 ADP ADP A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 2 ADP 1 4703 4703 ADP ADP A . 
E 2 ADP 1 4704 4704 ADP ADP A . 
F 4 MG  1 4705 4705 MG  MG  A . 
G 4 MG  1 4706 4706 MG  MG  A . 
H 5 HOH 1 4801 4    HOH HOH A . 
H 5 HOH 2 4802 2    HOH HOH A . 
H 5 HOH 3 4803 3    HOH HOH A . 
H 5 HOH 4 4804 7    HOH HOH A . 
H 5 HOH 5 4805 5    HOH HOH A . 
H 5 HOH 6 4806 6    HOH HOH A . 
H 5 HOH 7 4807 1    HOH HOH 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                   9BM2 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BM2 
_struct.title                        'State-4 of motor domain from full-length human dynein-1 in 5 mM ATP' 
_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        9BM2 
_struct_keywords.text            'dynein-1, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
H 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              9BM2 
_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,H 
# 
_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 VAL A 1536 ? SER A 1554 ? VAL A 1536 SER A 1554 1 ? 19 
HELX_P HELX_P2   AA2 LEU A 1561 ? SER A 1583 ? LEU A 1561 SER A 1583 1 ? 23 
HELX_P HELX_P3   AA3 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P4   AA4 GLY A 1596 ? SER A 1625 ? GLY A 1596 SER A 1625 1 ? 30 
HELX_P HELX_P5   AA5 PHE A 1626 ? VAL A 1632 ? PHE A 1626 VAL A 1632 5 ? 7  
HELX_P HELX_P6   AA6 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P7   AA7 ALA A 1648 ? HIS A 1653 ? ALA A 1648 HIS A 1653 5 ? 6  
HELX_P HELX_P8   AA8 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P9   AA9 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P10  AB1 GLN A 1746 ? GLY A 1770 ? GLN A 1746 GLY A 1770 1 ? 25 
HELX_P HELX_P11  AB2 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P12  AB3 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P13  AB4 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P14  AB5 VAL A 1853 ? GLN A 1855 ? VAL A 1853 GLN A 1855 5 ? 3  
HELX_P HELX_P15  AB6 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P16  AB7 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P17  AB8 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P18  AB9 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P19  AC1 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P20  AC2 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P21  AC3 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P22  AC4 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P23  AC5 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P24  AC6 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P25  AC7 PRO A 2132 ? MET A 2145 ? PRO A 2132 MET A 2145 1 ? 14 
HELX_P HELX_P26  AC8 VAL A 2146 ? LEU A 2149 ? VAL A 2146 LEU A 2149 5 ? 4  
HELX_P HELX_P27  AC9 VAL A 2150 ? GLU A 2152 ? VAL A 2150 GLU A 2152 5 ? 3  
HELX_P HELX_P28  AD1 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P29  AD2 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P30  AD3 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P31  AD4 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P32  AD5 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P33  AD6 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P34  AD7 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P35  AD8 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P36  AD9 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P37  AE1 ASN A 2314 ? ASN A 2316 ? ASN A 2314 ASN A 2316 5 ? 3  
HELX_P HELX_P38  AE2 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P39  AE3 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P40  AE4 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P41  AE5 PRO A 2425 ? PHE A 2427 ? PRO A 2425 PHE A 2427 5 ? 3  
HELX_P HELX_P42  AE6 GLY A 2431 ? PHE A 2441 ? GLY A 2431 PHE A 2441 1 ? 11 
HELX_P HELX_P43  AE7 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P44  AE8 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P45  AE9 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P46  AF1 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P47  AF2 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P48  AF3 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P49  AF4 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P50  AF5 GLY A 2600 ? ALA A 2611 ? GLY A 2600 ALA A 2611 1 ? 12 
HELX_P HELX_P51  AF6 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P52  AF7 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P53  AF8 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P54  AF9 GLY A 2740 ? ARG A 2757 ? GLY A 2740 ARG A 2757 1 ? 18 
HELX_P HELX_P55  AG1 LEU A 2758 ? THR A 2764 ? LEU A 2758 THR A 2764 5 ? 7  
HELX_P HELX_P56  AG2 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P57  AG3 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P58  AG4 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P59  AG5 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P60  AG6 ASP A 2862 ? MET A 2867 ? ASP A 2862 MET A 2867 1 ? 6  
HELX_P HELX_P61  AG7 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P62  AG8 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P63  AG9 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P64  AH1 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P65  AH2 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P66  AH3 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P67  AH4 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P68  AH5 SER A 3046 ? LEU A 3062 ? SER A 3046 LEU A 3062 1 ? 17 
HELX_P HELX_P69  AH6 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P70  AH7 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P71  AH8 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P72  AH9 SER A 3111 ? MET A 3113 ? SER A 3111 MET A 3113 5 ? 3  
HELX_P HELX_P73  AI1 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P74  AI2 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P75  AI3 GLU A 3450 ? THR A 3495 ? GLU A 3450 THR A 3495 1 ? 46 
HELX_P HELX_P76  AI4 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P77  AI5 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P78  AI6 ALA A 3548 ? SER A 3554 ? ALA A 3548 SER A 3554 1 ? 7  
HELX_P HELX_P79  AI7 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P80  AI8 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P81  AI9 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P82  AJ1 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P83  AJ2 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P84  AJ3 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P85  AJ4 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P86  AJ5 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P87  AJ6 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P88  AJ7 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P89  AJ8 ASP A 3763 ? LEU A 3818 ? ASP A 3763 LEU A 3818 1 ? 56 
HELX_P HELX_P90  AJ9 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P91  AK1 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P92  AK2 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P93  AK3 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P94  AK4 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P95  AK5 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P96  AK6 ASP A 3879 ? GLY A 3894 ? ASP A 3879 GLY A 3894 1 ? 16 
HELX_P HELX_P97  AK7 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P98  AK8 ASN A 3912 ? ILE A 3914 ? ASN A 3912 ILE A 3914 5 ? 3  
HELX_P HELX_P99  AK9 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P100 AL1 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P101 AL2 LEU A 3947 ? ASP A 3954 ? LEU A 3947 ASP A 3954 1 ? 8  
HELX_P HELX_P102 AL3 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P103 AL4 SER A 3965 ? THR A 3969 ? SER A 3965 THR A 3969 5 ? 5  
HELX_P HELX_P104 AL5 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P105 AL6 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P106 AL7 ASP A 4026 ? THR A 4033 ? ASP A 4026 THR A 4033 1 ? 8  
HELX_P HELX_P107 AL8 ALA A 4051 ? GLN A 4062 ? ALA A 4051 GLN A 4062 1 ? 12 
HELX_P HELX_P108 AL9 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P109 AM1 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P110 AM2 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P111 AM3 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P112 AM4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P113 AM5 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P114 AM6 ASN A 4174 ? LEU A 4194 ? ASN A 4174 LEU A 4194 1 ? 21 
HELX_P HELX_P115 AM7 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P116 AM8 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P117 AM9 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P118 AN1 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P119 AN2 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P120 AN3 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P121 AN4 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P122 AN5 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P123 AN6 ASN A 4326 ? MET A 4346 ? ASN A 4326 MET A 4346 1 ? 21 
HELX_P HELX_P124 AN7 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P125 AN8 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P126 AN9 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P127 AO1 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P128 AO2 THR A 4474 ? GLY A 4499 ? THR A 4474 GLY A 4499 1 ? 26 
HELX_P HELX_P129 AO3 LYS A 4502 ? ASN A 4506 ? LYS A 4502 ASN A 4506 5 ? 5  
HELX_P HELX_P130 AO4 GLY A 4512 ? LEU A 4514 ? GLY A 4512 LEU A 4514 5 ? 3  
HELX_P HELX_P131 AO5 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P132 AO6 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P133 AO7 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 1913 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 1913 A MG  4705 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc2 metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG  . MG ? ? A SER 2231 A MG  4706 1_555 ? ? ? ? ? ? ? 1.891 ? ? 
metalc3 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG  . MG ? ? A GLU 2344 A MG  4706 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc4 metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG  . MG ? ? A ADP 4701 A MG  4705 1_555 ? ? ? ? ? ? ? 2.845 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.732 ? ? 
metalc7 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 4802 1_555 ? ? ? ? ? ? ? 2.554 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O3B ? B ADP .    ? A ADP 4701 ? 1_555 78.0  ? 
2 OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4802 ? 1_555 110.2 ? 
3 O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4802 ? 1_555 162.8 ? 
4 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 78.7  ? 
5 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 156.4 ? 
6 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 84.9  ? 
7 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 74.9  ? 
8 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 72.2  ? 
9 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 83.9  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 5 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 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 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? parallel      
AB8 3 4 ? anti-parallel 
AB8 4 5 ? parallel      
AB8 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 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA1 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA1 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA2 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA2 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA2 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA3 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA3 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA4 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA4 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA4 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA5 1 THR A 1998 ? GLU A 2000 ? THR A 1998 GLU A 2000 
AA5 2 GLN A 2005 ? LYS A 2007 ? GLN A 2005 LYS A 2007 
AA6 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA6 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA6 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA6 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA6 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA7 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA7 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA8 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA8 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AA9 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AA9 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB1 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB1 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB1 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB1 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB1 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB2 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB2 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB2 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB2 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB3 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB3 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB3 3 HIS A 3063 ? MET A 3068 ? HIS A 3063 MET A 3068 
AB3 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB3 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB4 1 THR A 3610 ? THR A 3612 ? THR A 3610 THR A 3612 
AB4 2 PRO A 3632 ? VAL A 3635 ? PRO A 3632 VAL A 3635 
AB4 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB4 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB4 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB5 1 VAL A 3653 ? THR A 3656 ? VAL A 3653 THR A 3656 
AB5 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB5 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB6 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB6 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB6 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB6 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB6 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB7 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AB7 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AB7 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AB7 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AB8 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AB8 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AB8 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AB8 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AB8 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AB8 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 SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA1 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA2 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA2 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA3 1 2 N PHE A 1905 ? N PHE A 1905 O LEU A 2039 ? O LEU A 2039 
AA4 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA4 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA5 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA6 1 2 N VAL A 2250 ? N VAL A 2250 O TRP A 2300 ? O TRP A 2300 
AA6 2 3 N ILE A 2301 ? N ILE A 2301 O MET A 2342 ? O MET A 2342 
AA6 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA6 4 5 N GLY A 2219 ? N GLY A 2219 O GLY A 2360 ? O GLY A 2360 
AA7 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA8 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AA9 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB1 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB1 2 3 N CYS A 2663 ? N CYS A 2663 O VAL A 2709 ? O VAL A 2709 
AB1 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB1 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB2 1 2 N ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB2 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB2 3 4 O THR A 2699 ? O THR A 2699 N ARG A 2694 ? N ARG A 2694 
AB3 1 2 N TYR A 2959 ? N TYR A 2959 O ALA A 2991 ? O ALA A 2991 
AB3 2 3 N MET A 2994 ? N MET A 2994 O VAL A 3065 ? O VAL A 3065 
AB3 3 4 O VAL A 3064 ? O VAL A 3064 N LEU A 2933 ? N LEU A 2933 
AB3 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB4 1 2 N THR A 3610 ? N THR A 3610 O LEU A 3634 ? O LEU A 3634 
AB4 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB4 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB4 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB5 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB5 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB6 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB6 2 3 N VAL A 4094 ? N VAL A 4094 O PHE A 4125 ? O PHE A 4125 
AB6 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB6 4 5 N CYS A 4044 ? N CYS A 4044 O PHE A 4147 ? O PHE A 4147 
AB7 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AB7 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AB7 3 4 O ARG A 4591 ? O ARG A 4591 N GLU A 4542 ? N GLU A 4542 
AB8 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AB8 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AB8 3 4 O VAL A 4622 ? O VAL A 4622 N LEU A 4607 ? N LEU A 4607 
AB8 4 5 N TYR A 4610 ? N TYR A 4610 O VAL A 4642 ? O VAL A 4642 
AB8 5 6 O ALA A 4641 ? O ALA A 4641 N GLN A 4566 ? N GLN A 4566 
# 
_pdbx_entry_details.entry_id                   9BM2 
_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   OH 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   TYR 
_pdbx_validate_close_contact.auth_seq_id_1    2967 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    2975 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
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 PRO A 1586 ? ? -82.94  49.12   
2  1 PHE A 1626 ? ? 52.49   74.20   
3  1 ALA A 1862 ? ? 56.33   -122.22 
4  1 ASN A 2130 ? ? -94.57  53.93   
5  1 LYS A 2673 ? ? -69.29  2.63    
6  1 TYR A 2881 ? ? -90.09  57.67   
7  1 GLU A 2904 ? ? -126.58 -164.37 
8  1 LEU A 2905 ? ? -37.42  127.61  
9  1 GLU A 3842 ? ? 40.00   42.53   
10 1 LEU A 3973 ? ? -95.02  52.25   
11 1 GLU A 4034 ? ? 67.18   -2.72   
12 1 GLU A 4206 ? ? -94.90  56.51   
13 1 LYS A 4287 ? ? 39.71   56.82   
14 1 GLU A 4599 ? ? 58.81   -147.56 
15 1 PHE A 4620 ? ? -161.30 -169.88 
16 1 LYS A 4629 ? ? 70.13   -7.84   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BM2 
_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                    9BM2 
_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                  2.82 
_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               122798 
_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 ATP' 
_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-4 of motor domain from full-length human dynein-1 in 5mM ATP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BM2 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BM2 
_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                9BM2 
_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 MET 1457 ? A MET 1457 
1458 1 Y 1 A ALA 1458 ? A ALA 1458 
1459 1 Y 1 A LEU 1459 ? A LEU 1459 
1460 1 Y 1 A GLU 1460 ? A GLU 1460 
1461 1 Y 1 A GLU 1461 ? A GLU 1461 
1462 1 Y 1 A PHE 1462 ? A PHE 1462 
1463 1 Y 1 A LEU 1463 ? A LEU 1463 
1464 1 Y 1 A LYS 1464 ? A LYS 1464 
1465 1 Y 1 A GLN 1465 ? A GLN 1465 
1466 1 Y 1 A ILE 1466 ? A ILE 1466 
1467 1 Y 1 A ARG 1467 ? A ARG 1467 
1468 1 Y 1 A GLU 1468 ? A GLU 1468 
1469 1 Y 1 A VAL 1469 ? A VAL 1469 
1470 1 Y 1 A TRP 1470 ? A TRP 1470 
1471 1 Y 1 A ASN 1471 ? A ASN 1471 
1472 1 Y 1 A THR 1472 ? A THR 1472 
1473 1 Y 1 A TYR 1473 ? A TYR 1473 
1474 1 Y 1 A GLU 1474 ? A GLU 1474 
1475 1 Y 1 A LEU 1475 ? A LEU 1475 
1476 1 Y 1 A ASP 1476 ? A ASP 1476 
1477 1 Y 1 A LEU 1477 ? A LEU 1477 
1478 1 Y 1 A VAL 1478 ? A VAL 1478 
1479 1 Y 1 A ASN 1479 ? A ASN 1479 
1480 1 Y 1 A TYR 1480 ? A TYR 1480 
1481 1 Y 1 A GLN 1481 ? A GLN 1481 
1482 1 Y 1 A ASN 1482 ? A ASN 1482 
1483 1 Y 1 A LYS 1483 ? A LYS 1483 
1484 1 Y 1 A CYS 1484 ? A CYS 1484 
1485 1 Y 1 A ARG 1485 ? A ARG 1485 
1486 1 Y 1 A LEU 1486 ? A LEU 1486 
1487 1 Y 1 A ILE 1487 ? A ILE 1487 
1488 1 Y 1 A ARG 1488 ? A ARG 1488 
1489 1 Y 1 A GLY 1489 ? A GLY 1489 
1490 1 Y 1 A TRP 1490 ? A TRP 1490 
1491 1 Y 1 A ASP 1491 ? A ASP 1491 
1492 1 Y 1 A ASP 1492 ? A ASP 1492 
1493 1 Y 1 A LEU 1493 ? A LEU 1493 
1494 1 Y 1 A PHE 1494 ? A PHE 1494 
1495 1 Y 1 A ASN 1495 ? A ASN 1495 
1496 1 Y 1 A LYS 1496 ? A LYS 1496 
1497 1 Y 1 A VAL 1497 ? A VAL 1497 
1498 1 Y 1 A LYS 1498 ? A LYS 1498 
1499 1 Y 1 A GLU 1499 ? A GLU 1499 
1500 1 Y 1 A HIS 1500 ? A HIS 1500 
1501 1 Y 1 A ILE 1501 ? A ILE 1501 
1502 1 Y 1 A ASN 1502 ? A ASN 1502 
1503 1 Y 1 A SER 1503 ? A SER 1503 
1504 1 Y 1 A VAL 1504 ? A VAL 1504 
1505 1 Y 1 A SER 1505 ? A SER 1505 
1506 1 Y 1 A ALA 1506 ? A ALA 1506 
1507 1 Y 1 A MET 1507 ? A MET 1507 
1508 1 Y 1 A LYS 1508 ? A LYS 1508 
1509 1 Y 1 A LEU 1509 ? A LEU 1509 
1510 1 Y 1 A SER 1510 ? A SER 1510 
1511 1 Y 1 A PRO 1511 ? A PRO 1511 
1512 1 Y 1 A TYR 1512 ? A TYR 1512 
1513 1 Y 1 A TYR 1513 ? A TYR 1513 
1514 1 Y 1 A LYS 1514 ? A LYS 1514 
1515 1 Y 1 A VAL 1515 ? A VAL 1515 
1516 1 Y 1 A PHE 1516 ? A PHE 1516 
1517 1 Y 1 A GLU 1517 ? A GLU 1517 
1518 1 Y 1 A GLU 1518 ? A GLU 1518 
1519 1 Y 1 A ASP 1519 ? A ASP 1519 
1520 1 Y 1 A ALA 1520 ? A ALA 1520 
1521 1 Y 1 A LEU 1521 ? A LEU 1521 
1522 1 Y 1 A SER 1522 ? A SER 1522 
1523 1 Y 1 A TRP 1523 ? A TRP 1523 
1524 1 Y 1 A GLU 1524 ? A GLU 1524 
1525 1 Y 1 A ASP 1525 ? A ASP 1525 
1526 1 Y 1 A LYS 1526 ? A LYS 1526 
1527 1 Y 1 A LEU 1527 ? A LEU 1527 
1528 1 Y 1 A ASN 1528 ? A ASN 1528 
1529 1 Y 1 A ARG 1529 ? A ARG 1529 
1530 1 Y 1 A ILE 1530 ? A ILE 1530 
1531 1 Y 1 A MET 1531 ? A MET 1531 
1532 1 Y 1 A ALA 1532 ? A ALA 1532 
1533 1 Y 1 A LEU 1533 ? A LEU 1533 
1534 1 Y 1 A PHE 1534 ? A PHE 1534 
1535 1 Y 1 A GLY 2390 ? A GLY 2390 
1536 1 Y 1 A GLU 2391 ? A GLU 2391 
1537 1 Y 1 A ASP 2392 ? A ASP 2392 
1538 1 Y 1 A GLU 2393 ? A GLU 2393 
1539 1 Y 1 A ALA 2394 ? A ALA 2394 
1540 1 Y 1 A GLN 2395 ? A GLN 2395 
1541 1 Y 1 A ARG 2396 ? A ARG 2396 
1542 1 Y 1 A ARG 2397 ? A ARG 2397 
1543 1 Y 1 A ARG 2398 ? A ARG 2398 
1544 1 Y 1 A LYS 2399 ? A LYS 2399 
1545 1 Y 1 A GLY 2400 ? A GLY 2400 
1546 1 Y 1 A LYS 2401 ? A LYS 2401 
1547 1 Y 1 A GLU 2402 ? A GLU 2402 
1548 1 Y 1 A ASP 2403 ? A ASP 2403 
1549 1 Y 1 A GLU 2404 ? A GLU 2404 
1550 1 Y 1 A GLY 2405 ? A GLY 2405 
1551 1 Y 1 A GLU 2406 ? A GLU 2406 
1552 1 Y 1 A GLU 2407 ? A GLU 2407 
1553 1 Y 1 A ALA 2408 ? A ALA 2408 
1554 1 Y 1 A ALA 2409 ? A ALA 2409 
1555 1 Y 1 A MET 3243 ? A MET 3243 
1556 1 Y 1 A VAL 3244 ? A VAL 3244 
1557 1 Y 1 A LYS 3245 ? A LYS 3245 
1558 1 Y 1 A ASP 3246 ? A ASP 3246 
1559 1 Y 1 A GLN 3247 ? A GLN 3247 
1560 1 Y 1 A GLN 3248 ? A GLN 3248 
1561 1 Y 1 A GLU 3249 ? A GLU 3249 
1562 1 Y 1 A ALA 3250 ? A ALA 3250 
1563 1 Y 1 A GLU 3251 ? A GLU 3251 
1564 1 Y 1 A LYS 3252 ? A LYS 3252 
1565 1 Y 1 A LYS 3253 ? A LYS 3253 
1566 1 Y 1 A LYS 3254 ? A LYS 3254 
1567 1 Y 1 A VAL 3255 ? A VAL 3255 
1568 1 Y 1 A MET 3256 ? A MET 3256 
1569 1 Y 1 A SER 3257 ? A SER 3257 
1570 1 Y 1 A GLN 3258 ? A GLN 3258 
1571 1 Y 1 A GLU 3259 ? A GLU 3259 
1572 1 Y 1 A ILE 3260 ? A ILE 3260 
1573 1 Y 1 A GLN 3261 ? A GLN 3261 
1574 1 Y 1 A GLU 3262 ? A GLU 3262 
1575 1 Y 1 A GLN 3263 ? A GLN 3263 
1576 1 Y 1 A LEU 3264 ? A LEU 3264 
1577 1 Y 1 A HIS 3265 ? A HIS 3265 
1578 1 Y 1 A LYS 3266 ? A LYS 3266 
1579 1 Y 1 A GLN 3267 ? A GLN 3267 
1580 1 Y 1 A GLN 3268 ? A GLN 3268 
1581 1 Y 1 A GLU 3269 ? A GLU 3269 
1582 1 Y 1 A VAL 3270 ? A VAL 3270 
1583 1 Y 1 A ILE 3271 ? A ILE 3271 
1584 1 Y 1 A ALA 3272 ? A ALA 3272 
1585 1 Y 1 A ASP 3273 ? A ASP 3273 
1586 1 Y 1 A LYS 3274 ? A LYS 3274 
1587 1 Y 1 A GLN 3275 ? A GLN 3275 
1588 1 Y 1 A MET 3276 ? A MET 3276 
1589 1 Y 1 A SER 3277 ? A SER 3277 
1590 1 Y 1 A VAL 3278 ? A VAL 3278 
1591 1 Y 1 A LYS 3279 ? A LYS 3279 
1592 1 Y 1 A GLU 3280 ? A GLU 3280 
1593 1 Y 1 A ASP 3281 ? A ASP 3281 
1594 1 Y 1 A LEU 3282 ? A LEU 3282 
1595 1 Y 1 A ASP 3283 ? A ASP 3283 
1596 1 Y 1 A LYS 3284 ? A LYS 3284 
1597 1 Y 1 A VAL 3285 ? A VAL 3285 
1598 1 Y 1 A GLU 3286 ? A GLU 3286 
1599 1 Y 1 A PRO 3287 ? A PRO 3287 
1600 1 Y 1 A ALA 3288 ? A ALA 3288 
1601 1 Y 1 A VAL 3289 ? A VAL 3289 
1602 1 Y 1 A ILE 3290 ? A ILE 3290 
1603 1 Y 1 A GLU 3291 ? A GLU 3291 
1604 1 Y 1 A ALA 3292 ? A ALA 3292 
1605 1 Y 1 A GLN 3293 ? A GLN 3293 
1606 1 Y 1 A ASN 3294 ? A ASN 3294 
1607 1 Y 1 A ALA 3295 ? A ALA 3295 
1608 1 Y 1 A VAL 3296 ? A VAL 3296 
1609 1 Y 1 A LYS 3297 ? A LYS 3297 
1610 1 Y 1 A SER 3298 ? A SER 3298 
1611 1 Y 1 A ILE 3299 ? A ILE 3299 
1612 1 Y 1 A LYS 3300 ? A LYS 3300 
1613 1 Y 1 A LYS 3301 ? A LYS 3301 
1614 1 Y 1 A GLN 3302 ? A GLN 3302 
1615 1 Y 1 A HIS 3303 ? A HIS 3303 
1616 1 Y 1 A LEU 3304 ? A LEU 3304 
1617 1 Y 1 A VAL 3305 ? A VAL 3305 
1618 1 Y 1 A GLU 3306 ? A GLU 3306 
1619 1 Y 1 A VAL 3307 ? A VAL 3307 
1620 1 Y 1 A ARG 3308 ? A ARG 3308 
1621 1 Y 1 A SER 3309 ? A SER 3309 
1622 1 Y 1 A MET 3310 ? A MET 3310 
1623 1 Y 1 A ALA 3311 ? A ALA 3311 
1624 1 Y 1 A ASN 3312 ? A ASN 3312 
1625 1 Y 1 A PRO 3313 ? A PRO 3313 
1626 1 Y 1 A PRO 3314 ? A PRO 3314 
1627 1 Y 1 A ALA 3315 ? A ALA 3315 
1628 1 Y 1 A ALA 3316 ? A ALA 3316 
1629 1 Y 1 A VAL 3317 ? A VAL 3317 
1630 1 Y 1 A LYS 3318 ? A LYS 3318 
1631 1 Y 1 A LEU 3319 ? A LEU 3319 
1632 1 Y 1 A ALA 3320 ? A ALA 3320 
1633 1 Y 1 A LEU 3321 ? A LEU 3321 
1634 1 Y 1 A GLU 3322 ? A GLU 3322 
1635 1 Y 1 A SER 3323 ? A SER 3323 
1636 1 Y 1 A ILE 3324 ? A ILE 3324 
1637 1 Y 1 A CYS 3325 ? A CYS 3325 
1638 1 Y 1 A LEU 3326 ? A LEU 3326 
1639 1 Y 1 A LEU 3327 ? A LEU 3327 
1640 1 Y 1 A LEU 3328 ? A LEU 3328 
1641 1 Y 1 A GLY 3329 ? A GLY 3329 
1642 1 Y 1 A GLU 3330 ? A GLU 3330 
1643 1 Y 1 A SER 3331 ? A SER 3331 
1644 1 Y 1 A THR 3332 ? A THR 3332 
1645 1 Y 1 A THR 3333 ? A THR 3333 
1646 1 Y 1 A ASP 3334 ? A ASP 3334 
1647 1 Y 1 A TRP 3335 ? A TRP 3335 
1648 1 Y 1 A LYS 3336 ? A LYS 3336 
1649 1 Y 1 A GLN 3337 ? A GLN 3337 
1650 1 Y 1 A ILE 3338 ? A ILE 3338 
1651 1 Y 1 A ARG 3339 ? A ARG 3339 
1652 1 Y 1 A SER 3340 ? A SER 3340 
1653 1 Y 1 A ILE 3341 ? A ILE 3341 
1654 1 Y 1 A ILE 3342 ? A ILE 3342 
1655 1 Y 1 A MET 3343 ? A MET 3343 
1656 1 Y 1 A ARG 3344 ? A ARG 3344 
1657 1 Y 1 A GLU 3345 ? A GLU 3345 
1658 1 Y 1 A ASN 3346 ? A ASN 3346 
1659 1 Y 1 A PHE 3347 ? A PHE 3347 
1660 1 Y 1 A ILE 3348 ? A ILE 3348 
1661 1 Y 1 A PRO 3349 ? A PRO 3349 
1662 1 Y 1 A THR 3350 ? A THR 3350 
1663 1 Y 1 A ILE 3351 ? A ILE 3351 
1664 1 Y 1 A VAL 3352 ? A VAL 3352 
1665 1 Y 1 A ASN 3353 ? A ASN 3353 
1666 1 Y 1 A PHE 3354 ? A PHE 3354 
1667 1 Y 1 A SER 3355 ? A SER 3355 
1668 1 Y 1 A ALA 3356 ? A ALA 3356 
1669 1 Y 1 A GLU 3357 ? A GLU 3357 
1670 1 Y 1 A GLU 3358 ? A GLU 3358 
1671 1 Y 1 A ILE 3359 ? A ILE 3359 
1672 1 Y 1 A SER 3360 ? A SER 3360 
1673 1 Y 1 A ASP 3361 ? A ASP 3361 
1674 1 Y 1 A ALA 3362 ? A ALA 3362 
1675 1 Y 1 A ILE 3363 ? A ILE 3363 
1676 1 Y 1 A ARG 3364 ? A ARG 3364 
1677 1 Y 1 A GLU 3365 ? A GLU 3365 
1678 1 Y 1 A LYS 3366 ? A LYS 3366 
1679 1 Y 1 A MET 3367 ? A MET 3367 
1680 1 Y 1 A LYS 3368 ? A LYS 3368 
1681 1 Y 1 A LYS 3369 ? A LYS 3369 
1682 1 Y 1 A ASN 3370 ? A ASN 3370 
1683 1 Y 1 A TYR 3371 ? A TYR 3371 
1684 1 Y 1 A MET 3372 ? A MET 3372 
1685 1 Y 1 A SER 3373 ? A SER 3373 
1686 1 Y 1 A ASN 3374 ? A ASN 3374 
1687 1 Y 1 A PRO 3375 ? A PRO 3375 
1688 1 Y 1 A SER 3376 ? A SER 3376 
1689 1 Y 1 A TYR 3377 ? A TYR 3377 
1690 1 Y 1 A ASN 3378 ? A ASN 3378 
1691 1 Y 1 A TYR 3379 ? A TYR 3379 
1692 1 Y 1 A GLU 3380 ? A GLU 3380 
1693 1 Y 1 A ILE 3381 ? A ILE 3381 
1694 1 Y 1 A VAL 3382 ? A VAL 3382 
1695 1 Y 1 A ASN 3383 ? A ASN 3383 
1696 1 Y 1 A ARG 3384 ? A ARG 3384 
1697 1 Y 1 A ALA 3385 ? A ALA 3385 
1698 1 Y 1 A SER 3386 ? A SER 3386 
1699 1 Y 1 A LEU 3387 ? A LEU 3387 
1700 1 Y 1 A ALA 3388 ? A ALA 3388 
1701 1 Y 1 A CYS 3389 ? A CYS 3389 
1702 1 Y 1 A GLY 3390 ? A GLY 3390 
1703 1 Y 1 A PRO 3391 ? A PRO 3391 
1704 1 Y 1 A MET 3392 ? A MET 3392 
1705 1 Y 1 A VAL 3393 ? A VAL 3393 
1706 1 Y 1 A LYS 3394 ? A LYS 3394 
1707 1 Y 1 A TRP 3395 ? A TRP 3395 
1708 1 Y 1 A ALA 3396 ? A ALA 3396 
1709 1 Y 1 A ILE 3397 ? A ILE 3397 
1710 1 Y 1 A ALA 3398 ? A ALA 3398 
1711 1 Y 1 A GLN 3399 ? A GLN 3399 
1712 1 Y 1 A LEU 3400 ? A LEU 3400 
1713 1 Y 1 A ASN 3401 ? A ASN 3401 
1714 1 Y 1 A TYR 3402 ? A TYR 3402 
1715 1 Y 1 A ALA 3403 ? A ALA 3403 
1716 1 Y 1 A ASP 3404 ? A ASP 3404 
1717 1 Y 1 A MET 3405 ? A MET 3405 
1718 1 Y 1 A LEU 3406 ? A LEU 3406 
1719 1 Y 1 A LYS 3407 ? A LYS 3407 
1720 1 Y 1 A ARG 3408 ? A ARG 3408 
1721 1 Y 1 A VAL 3409 ? A VAL 3409 
1722 1 Y 1 A GLU 3410 ? A GLU 3410 
1723 1 Y 1 A PRO 3411 ? A PRO 3411 
1724 1 Y 1 A LEU 3412 ? A LEU 3412 
1725 1 Y 1 A ARG 3413 ? A ARG 3413 
1726 1 Y 1 A ASN 3414 ? A ASN 3414 
1727 1 Y 1 A GLU 3415 ? A GLU 3415 
1728 1 Y 1 A LEU 3416 ? A LEU 3416 
1729 1 Y 1 A GLN 3417 ? A GLN 3417 
1730 1 Y 1 A LYS 3418 ? A LYS 3418 
1731 1 Y 1 A LEU 3419 ? A LEU 3419 
1732 1 Y 1 A GLU 3420 ? A GLU 3420 
1733 1 Y 1 A ASP 3421 ? A ASP 3421 
1734 1 Y 1 A ASP 3422 ? A ASP 3422 
1735 1 Y 1 A ALA 3423 ? A ALA 3423 
1736 1 Y 1 A LYS 3424 ? A LYS 3424 
1737 1 Y 1 A ASP 3425 ? A ASP 3425 
1738 1 Y 1 A ASN 3426 ? A ASN 3426 
1739 1 Y 1 A GLN 3427 ? A GLN 3427 
1740 1 Y 1 A GLN 3428 ? A GLN 3428 
1741 1 Y 1 A LYS 3429 ? A LYS 3429 
1742 1 Y 1 A ALA 3430 ? A ALA 3430 
1743 1 Y 1 A ASN 3431 ? A ASN 3431 
1744 1 Y 1 A GLU 3432 ? A GLU 3432 
1745 1 Y 1 A VAL 3433 ? A VAL 3433 
1746 1 Y 1 A GLU 3434 ? A GLU 3434 
1747 1 Y 1 A GLN 3435 ? A GLN 3435 
1748 1 Y 1 A MET 3436 ? A MET 3436 
1749 1 Y 1 A ILE 3437 ? A ILE 3437 
1750 1 Y 1 A ARG 3438 ? A ARG 3438 
1751 1 Y 1 A ASP 3439 ? A ASP 3439 
1752 1 Y 1 A LEU 3440 ? A LEU 3440 
1753 1 Y 1 A GLU 3441 ? A GLU 3441 
1754 1 Y 1 A ALA 3442 ? A ALA 3442 
1755 1 Y 1 A SER 3443 ? A SER 3443 
1756 1 Y 1 A ILE 3444 ? A ILE 3444 
1757 1 Y 1 A ALA 3445 ? A ALA 3445 
1758 1 Y 1 A ARG 3446 ? A ARG 3446 
1759 1 Y 1 A TYR 3447 ? A TYR 3447 
1760 1 Y 1 A LYS 3448 ? A LYS 3448 
1761 1 Y 1 A MET 4348 ? A MET 4348 
1762 1 Y 1 A LEU 4349 ? A LEU 4349 
1763 1 Y 1 A GLU 4350 ? A GLU 4350 
1764 1 Y 1 A ASP 4351 ? A ASP 4351 
1765 1 Y 1 A GLU 4352 ? A GLU 4352 
1766 1 Y 1 A ASP 4353 ? A ASP 4353 
1767 1 Y 1 A ASP 4354 ? A ASP 4354 
1768 1 Y 1 A LEU 4355 ? A LEU 4355 
1769 1 Y 1 A ALA 4356 ? A ALA 4356 
1770 1 Y 1 A TYR 4357 ? A TYR 4357 
1771 1 Y 1 A ALA 4358 ? A ALA 4358 
1772 1 Y 1 A GLU 4359 ? A GLU 4359 
1773 1 Y 1 A THR 4360 ? A THR 4360 
1774 1 Y 1 A GLU 4361 ? A GLU 4361 
1775 1 Y 1 A LYS 4362 ? A LYS 4362 
1776 1 Y 1 A LYS 4363 ? A LYS 4363 
1777 1 Y 1 A THR 4364 ? A THR 4364 
1778 1 Y 1 A ARG 4365 ? A ARG 4365 
1779 1 Y 1 A THR 4366 ? A THR 4366 
1780 1 Y 1 A ASP 4367 ? A ASP 4367 
1781 1 Y 1 A SER 4368 ? A SER 4368 
1782 1 Y 1 A THR 4369 ? A THR 4369 
1783 1 Y 1 A SER 4370 ? A SER 4370 
1784 1 Y 1 A ASP 4371 ? A ASP 4371 
1785 1 Y 1 A GLY 4372 ? A GLY 4372 
1786 1 Y 1 A ARG 4373 ? A ARG 4373 
1787 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
ATP PG     P  N N 116 
ATP O1G    O  N N 117 
ATP O2G    O  N N 118 
ATP O3G    O  N N 119 
ATP PB     P  N R 120 
ATP O1B    O  N N 121 
ATP O2B    O  N N 122 
ATP O3B    O  N N 123 
ATP PA     P  N R 124 
ATP O1A    O  N N 125 
ATP O2A    O  N N 126 
ATP O3A    O  N N 127 
ATP "O5'"  O  N N 128 
ATP "C5'"  C  N N 129 
ATP "C4'"  C  N R 130 
ATP "O4'"  O  N N 131 
ATP "C3'"  C  N S 132 
ATP "O3'"  O  N N 133 
ATP "C2'"  C  N R 134 
ATP "O2'"  O  N N 135 
ATP "C1'"  C  N R 136 
ATP N9     N  Y N 137 
ATP C8     C  Y N 138 
ATP N7     N  Y N 139 
ATP C5     C  Y N 140 
ATP C6     C  Y N 141 
ATP N6     N  N N 142 
ATP N1     N  Y N 143 
ATP C2     C  Y N 144 
ATP N3     N  Y N 145 
ATP C4     C  Y N 146 
ATP HOG2   H  N N 147 
ATP HOG3   H  N N 148 
ATP HOB2   H  N N 149 
ATP HOA2   H  N N 150 
ATP "H5'1" H  N N 151 
ATP "H5'2" H  N N 152 
ATP "H4'"  H  N N 153 
ATP "H3'"  H  N N 154 
ATP "HO3'" H  N N 155 
ATP "H2'"  H  N N 156 
ATP "HO2'" H  N N 157 
ATP "H1'"  H  N N 158 
ATP H8     H  N N 159 
ATP HN61   H  N N 160 
ATP HN62   H  N N 161 
ATP H2     H  N N 162 
CYS N      N  N N 163 
CYS CA     C  N R 164 
CYS C      C  N N 165 
CYS O      O  N N 166 
CYS CB     C  N N 167 
CYS SG     S  N N 168 
CYS OXT    O  N N 169 
CYS H      H  N N 170 
CYS H2     H  N N 171 
CYS HA     H  N N 172 
CYS HB2    H  N N 173 
CYS HB3    H  N N 174 
CYS HG     H  N N 175 
CYS HXT    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
HOH O      O  N N 247 
HOH H1     H  N N 248 
HOH H2     H  N N 249 
ILE N      N  N N 250 
ILE CA     C  N S 251 
ILE C      C  N N 252 
ILE O      O  N N 253 
ILE CB     C  N S 254 
ILE CG1    C  N N 255 
ILE CG2    C  N N 256 
ILE CD1    C  N N 257 
ILE OXT    O  N N 258 
ILE H      H  N N 259 
ILE H2     H  N N 260 
ILE HA     H  N N 261 
ILE HB     H  N N 262 
ILE HG12   H  N N 263 
ILE HG13   H  N N 264 
ILE HG21   H  N N 265 
ILE HG22   H  N N 266 
ILE HG23   H  N N 267 
ILE HD11   H  N N 268 
ILE HD12   H  N N 269 
ILE HD13   H  N N 270 
ILE HXT    H  N N 271 
LEU N      N  N N 272 
LEU CA     C  N S 273 
LEU C      C  N N 274 
LEU O      O  N N 275 
LEU CB     C  N N 276 
LEU CG     C  N N 277 
LEU CD1    C  N N 278 
LEU CD2    C  N N 279 
LEU OXT    O  N N 280 
LEU H      H  N N 281 
LEU H2     H  N N 282 
LEU HA     H  N N 283 
LEU HB2    H  N N 284 
LEU HB3    H  N N 285 
LEU HG     H  N N 286 
LEU HD11   H  N N 287 
LEU HD12   H  N N 288 
LEU HD13   H  N N 289 
LEU HD21   H  N N 290 
LEU HD22   H  N N 291 
LEU HD23   H  N N 292 
LEU HXT    H  N N 293 
LYS N      N  N N 294 
LYS CA     C  N S 295 
LYS C      C  N N 296 
LYS O      O  N N 297 
LYS CB     C  N N 298 
LYS CG     C  N N 299 
LYS CD     C  N N 300 
LYS CE     C  N N 301 
LYS NZ     N  N N 302 
LYS OXT    O  N N 303 
LYS H      H  N N 304 
LYS H2     H  N N 305 
LYS HA     H  N N 306 
LYS HB2    H  N N 307 
LYS HB3    H  N N 308 
LYS HG2    H  N N 309 
LYS HG3    H  N N 310 
LYS HD2    H  N N 311 
LYS HD3    H  N N 312 
LYS HE2    H  N N 313 
LYS HE3    H  N N 314 
LYS HZ1    H  N N 315 
LYS HZ2    H  N N 316 
LYS HZ3    H  N N 317 
LYS HXT    H  N N 318 
MET N      N  N N 319 
MET CA     C  N S 320 
MET C      C  N N 321 
MET O      O  N N 322 
MET CB     C  N N 323 
MET CG     C  N N 324 
MET SD     S  N N 325 
MET CE     C  N N 326 
MET OXT    O  N N 327 
MET H      H  N N 328 
MET H2     H  N N 329 
MET HA     H  N N 330 
MET HB2    H  N N 331 
MET HB3    H  N N 332 
MET HG2    H  N N 333 
MET HG3    H  N N 334 
MET HE1    H  N N 335 
MET HE2    H  N N 336 
MET HE3    H  N N 337 
MET HXT    H  N N 338 
MG  MG     MG N N 339 
PHE N      N  N N 340 
PHE CA     C  N S 341 
PHE C      C  N N 342 
PHE O      O  N N 343 
PHE CB     C  N N 344 
PHE CG     C  Y N 345 
PHE CD1    C  Y N 346 
PHE CD2    C  Y N 347 
PHE CE1    C  Y N 348 
PHE CE2    C  Y N 349 
PHE CZ     C  Y N 350 
PHE OXT    O  N N 351 
PHE H      H  N N 352 
PHE H2     H  N N 353 
PHE HA     H  N N 354 
PHE HB2    H  N N 355 
PHE HB3    H  N N 356 
PHE HD1    H  N N 357 
PHE HD2    H  N N 358 
PHE HE1    H  N N 359 
PHE HE2    H  N N 360 
PHE HZ     H  N N 361 
PHE HXT    H  N N 362 
PRO N      N  N N 363 
PRO CA     C  N S 364 
PRO C      C  N N 365 
PRO O      O  N N 366 
PRO CB     C  N N 367 
PRO CG     C  N N 368 
PRO CD     C  N N 369 
PRO OXT    O  N N 370 
PRO H      H  N N 371 
PRO HA     H  N N 372 
PRO HB2    H  N N 373 
PRO HB3    H  N N 374 
PRO HG2    H  N N 375 
PRO HG3    H  N N 376 
PRO HD2    H  N N 377 
PRO HD3    H  N N 378 
PRO HXT    H  N N 379 
SER N      N  N N 380 
SER CA     C  N S 381 
SER C      C  N N 382 
SER O      O  N N 383 
SER CB     C  N N 384 
SER OG     O  N N 385 
SER OXT    O  N N 386 
SER H      H  N N 387 
SER H2     H  N N 388 
SER HA     H  N N 389 
SER HB2    H  N N 390 
SER HB3    H  N N 391 
SER HG     H  N N 392 
SER HXT    H  N N 393 
THR N      N  N N 394 
THR CA     C  N S 395 
THR C      C  N N 396 
THR O      O  N N 397 
THR CB     C  N R 398 
THR OG1    O  N N 399 
THR CG2    C  N N 400 
THR OXT    O  N N 401 
THR H      H  N N 402 
THR H2     H  N N 403 
THR HA     H  N N 404 
THR HB     H  N N 405 
THR HG1    H  N N 406 
THR HG21   H  N N 407 
THR HG22   H  N N 408 
THR HG23   H  N N 409 
THR HXT    H  N N 410 
TRP N      N  N N 411 
TRP CA     C  N S 412 
TRP C      C  N N 413 
TRP O      O  N N 414 
TRP CB     C  N N 415 
TRP CG     C  Y N 416 
TRP CD1    C  Y N 417 
TRP CD2    C  Y N 418 
TRP NE1    N  Y N 419 
TRP CE2    C  Y N 420 
TRP CE3    C  Y N 421 
TRP CZ2    C  Y N 422 
TRP CZ3    C  Y N 423 
TRP CH2    C  Y N 424 
TRP OXT    O  N N 425 
TRP H      H  N N 426 
TRP H2     H  N N 427 
TRP HA     H  N N 428 
TRP HB2    H  N N 429 
TRP HB3    H  N N 430 
TRP HD1    H  N N 431 
TRP HE1    H  N N 432 
TRP HE3    H  N N 433 
TRP HZ2    H  N N 434 
TRP HZ3    H  N N 435 
TRP HH2    H  N N 436 
TRP HXT    H  N N 437 
TYR N      N  N N 438 
TYR CA     C  N S 439 
TYR C      C  N N 440 
TYR O      O  N N 441 
TYR CB     C  N N 442 
TYR CG     C  Y N 443 
TYR CD1    C  Y N 444 
TYR CD2    C  Y N 445 
TYR CE1    C  Y N 446 
TYR CE2    C  Y N 447 
TYR CZ     C  Y N 448 
TYR OH     O  N N 449 
TYR OXT    O  N N 450 
TYR H      H  N N 451 
TYR H2     H  N N 452 
TYR HA     H  N N 453 
TYR HB2    H  N N 454 
TYR HB3    H  N N 455 
TYR HD1    H  N N 456 
TYR HD2    H  N N 457 
TYR HE1    H  N N 458 
TYR HE2    H  N N 459 
TYR HH     H  N N 460 
TYR HXT    H  N N 461 
VAL N      N  N N 462 
VAL CA     C  N S 463 
VAL C      C  N N 464 
VAL O      O  N N 465 
VAL CB     C  N N 466 
VAL CG1    C  N N 467 
VAL CG2    C  N N 468 
VAL OXT    O  N N 469 
VAL H      H  N N 470 
VAL H2     H  N N 471 
VAL HA     H  N N 472 
VAL HB     H  N N 473 
VAL HG11   H  N N 474 
VAL HG12   H  N N 475 
VAL HG13   H  N N 476 
VAL HG21   H  N N 477 
VAL HG22   H  N N 478 
VAL HG23   H  N N 479 
VAL HXT    H  N N 480 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
HOH O     H1     sing N N 243 
HOH O     H2     sing N N 244 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
PHE N     CA     sing N N 330 
PHE N     H      sing N N 331 
PHE N     H2     sing N N 332 
PHE CA    C      sing N N 333 
PHE CA    CB     sing N N 334 
PHE CA    HA     sing N N 335 
PHE C     O      doub N N 336 
PHE C     OXT    sing N N 337 
PHE CB    CG     sing N N 338 
PHE CB    HB2    sing N N 339 
PHE CB    HB3    sing N N 340 
PHE CG    CD1    doub Y N 341 
PHE CG    CD2    sing Y N 342 
PHE CD1   CE1    sing Y N 343 
PHE CD1   HD1    sing N N 344 
PHE CD2   CE2    doub Y N 345 
PHE CD2   HD2    sing N N 346 
PHE CE1   CZ     doub Y N 347 
PHE CE1   HE1    sing N N 348 
PHE CE2   CZ     sing Y N 349 
PHE CE2   HE2    sing N N 350 
PHE CZ    HZ     sing N N 351 
PHE OXT   HXT    sing N N 352 
PRO N     CA     sing N N 353 
PRO N     CD     sing N N 354 
PRO N     H      sing N N 355 
PRO CA    C      sing N N 356 
PRO CA    CB     sing N N 357 
PRO CA    HA     sing N N 358 
PRO C     O      doub N N 359 
PRO C     OXT    sing N N 360 
PRO CB    CG     sing N N 361 
PRO CB    HB2    sing N N 362 
PRO CB    HB3    sing N N 363 
PRO CG    CD     sing N N 364 
PRO CG    HG2    sing N N 365 
PRO CG    HG3    sing N N 366 
PRO CD    HD2    sing N N 367 
PRO CD    HD3    sing N N 368 
PRO OXT   HXT    sing N N 369 
SER N     CA     sing N N 370 
SER N     H      sing N N 371 
SER N     H2     sing N N 372 
SER CA    C      sing N N 373 
SER CA    CB     sing N N 374 
SER CA    HA     sing N N 375 
SER C     O      doub N N 376 
SER C     OXT    sing N N 377 
SER CB    OG     sing N N 378 
SER CB    HB2    sing N N 379 
SER CB    HB3    sing N N 380 
SER OG    HG     sing N N 381 
SER OXT   HXT    sing N N 382 
THR N     CA     sing N N 383 
THR N     H      sing N N 384 
THR N     H2     sing N N 385 
THR CA    C      sing N N 386 
THR CA    CB     sing N N 387 
THR CA    HA     sing N N 388 
THR C     O      doub N N 389 
THR C     OXT    sing N N 390 
THR CB    OG1    sing N N 391 
THR CB    CG2    sing N N 392 
THR CB    HB     sing N N 393 
THR OG1   HG1    sing N N 394 
THR CG2   HG21   sing N N 395 
THR CG2   HG22   sing N N 396 
THR CG2   HG23   sing N N 397 
THR OXT   HXT    sing N N 398 
TRP N     CA     sing N N 399 
TRP N     H      sing N N 400 
TRP N     H2     sing N N 401 
TRP CA    C      sing N N 402 
TRP CA    CB     sing N N 403 
TRP CA    HA     sing N N 404 
TRP C     O      doub N N 405 
TRP C     OXT    sing N N 406 
TRP CB    CG     sing N N 407 
TRP CB    HB2    sing N N 408 
TRP CB    HB3    sing N N 409 
TRP CG    CD1    doub Y N 410 
TRP CG    CD2    sing Y N 411 
TRP CD1   NE1    sing Y N 412 
TRP CD1   HD1    sing N N 413 
TRP CD2   CE2    doub Y N 414 
TRP CD2   CE3    sing Y N 415 
TRP NE1   CE2    sing Y N 416 
TRP NE1   HE1    sing N N 417 
TRP CE2   CZ2    sing Y N 418 
TRP CE3   CZ3    doub Y N 419 
TRP CE3   HE3    sing N N 420 
TRP CZ2   CH2    doub Y N 421 
TRP CZ2   HZ2    sing N N 422 
TRP CZ3   CH2    sing Y N 423 
TRP CZ3   HZ3    sing N N 424 
TRP CH2   HH2    sing N N 425 
TRP OXT   HXT    sing N N 426 
TYR N     CA     sing N N 427 
TYR N     H      sing N N 428 
TYR N     H2     sing N N 429 
TYR CA    C      sing N N 430 
TYR CA    CB     sing N N 431 
TYR CA    HA     sing N N 432 
TYR C     O      doub N N 433 
TYR C     OXT    sing N N 434 
TYR CB    CG     sing N N 435 
TYR CB    HB2    sing N N 436 
TYR CB    HB3    sing N N 437 
TYR CG    CD1    doub Y N 438 
TYR CG    CD2    sing Y N 439 
TYR CD1   CE1    sing Y N 440 
TYR CD1   HD1    sing N N 441 
TYR CD2   CE2    doub Y N 442 
TYR CD2   HD2    sing N N 443 
TYR CE1   CZ     doub Y N 444 
TYR CE1   HE1    sing N N 445 
TYR CE2   CZ     sing Y N 446 
TYR CE2   HE2    sing N N 447 
TYR CZ    OH     sing N N 448 
TYR OH    HH     sing N N 449 
TYR OXT   HXT    sing N N 450 
VAL N     CA     sing N N 451 
VAL N     H      sing N N 452 
VAL N     H2     sing N N 453 
VAL CA    C      sing N N 454 
VAL CA    CB     sing N N 455 
VAL CA    HA     sing N N 456 
VAL C     O      doub N N 457 
VAL C     OXT    sing N N 458 
VAL CB    CG1    sing N N 459 
VAL CB    CG2    sing N N 460 
VAL CB    HB     sing N N 461 
VAL CG1   HG11   sing N N 462 
VAL CG1   HG12   sing N N 463 
VAL CG1   HG13   sing N N 464 
VAL CG2   HG21   sing N N 465 
VAL CG2   HG22   sing N N 466 
VAL CG2   HG23   sing N N 467 
VAL OXT   HXT    sing N N 468 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BM2 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-4 of motor domain from full-length human dynein-1 in 5 mM ATP' 
# 
_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                    9BM2 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . ASP A 1 1535 ? 123.957 175.604 178.175 1.00 125.88 ? 1535 ASP A N     1 
ATOM   2     C  CA    . ASP A 1 1535 ? 124.826 175.031 177.154 1.00 129.72 ? 1535 ASP A CA    1 
ATOM   3     C  C     . ASP A 1 1535 ? 124.113 174.957 175.808 1.00 133.85 ? 1535 ASP A C     1 
ATOM   4     O  O     . ASP A 1 1535 ? 124.684 174.509 174.815 1.00 132.16 ? 1535 ASP A O     1 
ATOM   5     C  CB    . ASP A 1 1535 ? 125.301 173.639 177.574 1.00 125.63 ? 1535 ASP A CB    1 
ATOM   6     C  CG    . ASP A 1 1535 ? 126.245 173.678 178.760 1.00 120.78 ? 1535 ASP A CG    1 
ATOM   7     O  OD1   . ASP A 1 1535 ? 126.937 174.702 178.937 1.00 120.30 ? 1535 ASP A OD1   1 
ATOM   8     O  OD2   . ASP A 1 1535 ? 126.295 172.684 179.515 1.00 116.96 ? 1535 ASP A OD2   1 
ATOM   9     N  N     . VAL A 1 1536 ? 122.858 175.401 175.785 1.00 135.86 ? 1536 VAL A N     1 
ATOM   10    C  CA    . VAL A 1 1536 ? 122.040 175.376 174.584 1.00 133.66 ? 1536 VAL A CA    1 
ATOM   11    C  C     . VAL A 1 1536 ? 121.752 176.782 174.070 1.00 136.10 ? 1536 VAL A C     1 
ATOM   12    O  O     . VAL A 1 1536 ? 121.722 177.008 172.859 1.00 135.67 ? 1536 VAL A O     1 
ATOM   13    C  CB    . VAL A 1 1536 ? 120.728 174.600 174.837 1.00 126.15 ? 1536 VAL A CB    1 
ATOM   14    C  CG1   . VAL A 1 1536 ? 119.821 174.653 173.616 1.00 128.22 ? 1536 VAL A CG1   1 
ATOM   15    C  CG2   . VAL A 1 1536 ? 121.030 173.160 175.220 1.00 115.32 ? 1536 VAL A CG2   1 
ATOM   16    N  N     . TRP A 1 1537 ? 121.555 177.743 174.978 1.00 135.52 ? 1537 TRP A N     1 
ATOM   17    C  CA    . TRP A 1 1537 ? 121.194 179.097 174.566 1.00 136.52 ? 1537 TRP A CA    1 
ATOM   18    C  C     . TRP A 1 1537 ? 122.291 179.737 173.723 1.00 138.24 ? 1537 TRP A C     1 
ATOM   19    O  O     . TRP A 1 1537 ? 122.004 180.384 172.710 1.00 138.00 ? 1537 TRP A O     1 
ATOM   20    C  CB    . TRP A 1 1537 ? 120.892 179.954 175.797 1.00 134.02 ? 1537 TRP A CB    1 
ATOM   21    C  CG    . TRP A 1 1537 ? 120.083 181.191 175.510 1.00 138.80 ? 1537 TRP A CG    1 
ATOM   22    C  CD1   . TRP A 1 1537 ? 120.275 182.082 174.493 1.00 135.21 ? 1537 TRP A CD1   1 
ATOM   23    C  CD2   . TRP A 1 1537 ? 118.957 181.672 176.255 1.00 144.38 ? 1537 TRP A CD2   1 
ATOM   24    N  NE1   . TRP A 1 1537 ? 119.339 183.085 174.558 1.00 134.31 ? 1537 TRP A NE1   1 
ATOM   25    C  CE2   . TRP A 1 1537 ? 118.518 182.857 175.630 1.00 142.19 ? 1537 TRP A CE2   1 
ATOM   26    C  CE3   . TRP A 1 1537 ? 118.278 181.216 177.389 1.00 140.70 ? 1537 TRP A CE3   1 
ATOM   27    C  CZ2   . TRP A 1 1537 ? 117.431 183.590 176.101 1.00 139.16 ? 1537 TRP A CZ2   1 
ATOM   28    C  CZ3   . TRP A 1 1537 ? 117.198 181.946 177.855 1.00 136.34 ? 1537 TRP A CZ3   1 
ATOM   29    C  CH2   . TRP A 1 1537 ? 116.786 183.120 177.212 1.00 138.41 ? 1537 TRP A CH2   1 
ATOM   30    N  N     . ILE A 1 1538 ? 123.554 179.568 174.122 1.00 138.04 ? 1538 ILE A N     1 
ATOM   31    C  CA    . ILE A 1 1538 ? 124.649 180.229 173.415 1.00 134.39 ? 1538 ILE A CA    1 
ATOM   32    C  C     . ILE A 1 1538 ? 124.803 179.668 172.004 1.00 136.02 ? 1538 ILE A C     1 
ATOM   33    O  O     . ILE A 1 1538 ? 125.032 180.418 171.045 1.00 132.29 ? 1538 ILE A O     1 
ATOM   34    C  CB    . ILE A 1 1538 ? 125.955 180.125 174.231 1.00 125.12 ? 1538 ILE A CB    1 
ATOM   35    C  CG1   . ILE A 1 1538 ? 127.045 181.009 173.619 1.00 119.75 ? 1538 ILE A CG1   1 
ATOM   36    C  CG2   . ILE A 1 1538 ? 126.416 178.676 174.384 1.00 118.42 ? 1538 ILE A CG2   1 
ATOM   37    C  CD1   . ILE A 1 1538 ? 128.241 181.217 174.522 1.00 106.26 ? 1538 ILE A CD1   1 
ATOM   38    N  N     . ASP A 1 1539 ? 124.670 178.347 171.850 1.00 137.30 ? 1539 ASP A N     1 
ATOM   39    C  CA    . ASP A 1 1539 ? 124.806 177.739 170.530 1.00 134.49 ? 1539 ASP A CA    1 
ATOM   40    C  C     . ASP A 1 1539 ? 123.698 178.207 169.596 1.00 134.44 ? 1539 ASP A C     1 
ATOM   41    O  O     . ASP A 1 1539 ? 123.955 178.578 168.444 1.00 132.18 ? 1539 ASP A O     1 
ATOM   42    C  CB    . ASP A 1 1539 ? 124.799 176.214 170.652 1.00 130.80 ? 1539 ASP A CB    1 
ATOM   43    C  CG    . ASP A 1 1539 ? 125.995 175.685 171.418 1.00 128.88 ? 1539 ASP A CG    1 
ATOM   44    O  OD1   . ASP A 1 1539 ? 127.078 176.300 171.332 1.00 125.14 ? 1539 ASP A OD1   1 
ATOM   45    O  OD2   . ASP A 1 1539 ? 125.851 174.653 172.107 1.00 125.96 ? 1539 ASP A OD2   1 
ATOM   46    N  N     . VAL A 1 1540 ? 122.455 178.206 170.084 1.00 136.58 ? 1540 VAL A N     1 
ATOM   47    C  CA    . VAL A 1 1540 ? 121.333 178.662 169.270 1.00 136.63 ? 1540 VAL A CA    1 
ATOM   48    C  C     . VAL A 1 1540 ? 121.498 180.133 168.918 1.00 137.87 ? 1540 VAL A C     1 
ATOM   49    O  O     . VAL A 1 1540 ? 121.217 180.552 167.789 1.00 138.54 ? 1540 VAL A O     1 
ATOM   50    C  CB    . VAL A 1 1540 ? 120.001 178.400 169.997 1.00 134.63 ? 1540 VAL A CB    1 
ATOM   51    C  CG1   . VAL A 1 1540 ? 118.833 178.936 169.182 1.00 131.63 ? 1540 VAL A CG1   1 
ATOM   52    C  CG2   . VAL A 1 1540 ? 119.829 176.917 170.266 1.00 131.96 ? 1540 VAL A CG2   1 
ATOM   53    N  N     . GLN A 1 1541 ? 121.958 180.939 169.878 1.00 137.66 ? 1541 GLN A N     1 
ATOM   54    C  CA    . GLN A 1 1541 ? 122.163 182.359 169.621 1.00 135.71 ? 1541 GLN A CA    1 
ATOM   55    C  C     . GLN A 1 1541 ? 123.190 182.574 168.517 1.00 137.02 ? 1541 GLN A C     1 
ATOM   56    O  O     . GLN A 1 1541 ? 122.948 183.333 167.572 1.00 137.35 ? 1541 GLN A O     1 
ATOM   57    C  CB    . GLN A 1 1541 ? 122.597 183.065 170.907 1.00 134.35 ? 1541 GLN A CB    1 
ATOM   58    C  CG    . GLN A 1 1541 ? 122.880 184.549 170.738 1.00 128.59 ? 1541 GLN A CG    1 
ATOM   59    C  CD    . GLN A 1 1541 ? 123.198 185.235 172.052 1.00 126.35 ? 1541 GLN A CD    1 
ATOM   60    O  OE1   . GLN A 1 1541 ? 122.348 185.332 172.938 1.00 122.65 ? 1541 GLN A OE1   1 
ATOM   61    N  NE2   . GLN A 1 1541 ? 124.429 185.715 172.186 1.00 123.52 ? 1541 GLN A NE2   1 
ATOM   62    N  N     . ARG A 1 1542 ? 124.341 181.902 168.612 1.00 137.16 ? 1542 ARG A N     1 
ATOM   63    C  CA    . ARG A 1 1542 ? 125.374 182.067 167.593 1.00 136.79 ? 1542 ARG A CA    1 
ATOM   64    C  C     . ARG A 1 1542 ? 124.888 181.584 166.231 1.00 137.01 ? 1542 ARG A C     1 
ATOM   65    O  O     . ARG A 1 1542 ? 125.121 182.245 165.205 1.00 135.05 ? 1542 ARG A O     1 
ATOM   66    C  CB    . ARG A 1 1542 ? 126.644 181.321 168.006 1.00 132.50 ? 1542 ARG A CB    1 
ATOM   67    C  CG    . ARG A 1 1542 ? 127.584 181.006 166.851 1.00 129.18 ? 1542 ARG A CG    1 
ATOM   68    C  CD    . ARG A 1 1542 ? 128.765 180.158 167.301 1.00 130.94 ? 1542 ARG A CD    1 
ATOM   69    N  NE    . ARG A 1 1542 ? 128.366 179.078 168.196 1.00 132.96 ? 1542 ARG A NE    1 
ATOM   70    C  CZ    . ARG A 1 1542 ? 127.845 177.926 167.795 1.00 131.06 ? 1542 ARG A CZ    1 
ATOM   71    N  NH1   . ARG A 1 1542 ? 127.643 177.668 166.513 1.00 129.97 ? 1542 ARG A NH1   1 
ATOM   72    N  NH2   . ARG A 1 1542 ? 127.523 177.009 168.702 1.00 125.91 ? 1542 ARG A NH2   1 
ATOM   73    N  N     . ARG A 1 1543 ? 124.207 180.434 166.202 1.00 136.60 ? 1543 ARG A N     1 
ATOM   74    C  CA    . ARG A 1 1543 ? 123.696 179.903 164.944 1.00 131.61 ? 1543 ARG A CA    1 
ATOM   75    C  C     . ARG A 1 1543 ? 122.721 180.878 164.303 1.00 132.38 ? 1543 ARG A C     1 
ATOM   76    O  O     . ARG A 1 1543 ? 122.809 181.163 163.102 1.00 133.48 ? 1543 ARG A O     1 
ATOM   77    C  CB    . ARG A 1 1543 ? 123.026 178.549 165.179 1.00 127.62 ? 1543 ARG A CB    1 
ATOM   78    C  CG    . ARG A 1 1543 ? 123.985 177.417 165.516 1.00 127.12 ? 1543 ARG A CG    1 
ATOM   79    C  CD    . ARG A 1 1543 ? 123.234 176.210 166.057 1.00 127.87 ? 1543 ARG A CD    1 
ATOM   80    N  NE    . ARG A 1 1543 ? 124.123 175.242 166.688 1.00 125.63 ? 1543 ARG A NE    1 
ATOM   81    C  CZ    . ARG A 1 1543 ? 124.640 174.187 166.073 1.00 122.79 ? 1543 ARG A CZ    1 
ATOM   82    N  NH1   . ARG A 1 1543 ? 124.375 173.929 164.804 1.00 123.15 ? 1543 ARG A NH1   1 
ATOM   83    N  NH2   . ARG A 1 1543 ? 125.441 173.370 166.750 1.00 116.85 ? 1543 ARG A NH2   1 
ATOM   84    N  N     . TRP A 1 1544 ? 121.795 181.420 165.099 1.00 134.63 ? 1544 TRP A N     1 
ATOM   85    C  CA    . TRP A 1 1544 ? 120.823 182.359 164.559 1.00 138.08 ? 1544 TRP A CA    1 
ATOM   86    C  C     . TRP A 1 1544 ? 121.501 183.631 164.074 1.00 136.65 ? 1544 TRP A C     1 
ATOM   87    O  O     . TRP A 1 1544 ? 121.129 184.172 163.030 1.00 134.68 ? 1544 TRP A O     1 
ATOM   88    C  CB    . TRP A 1 1544 ? 119.755 182.686 165.602 1.00 140.75 ? 1544 TRP A CB    1 
ATOM   89    C  CG    . TRP A 1 1544 ? 118.642 183.532 165.054 1.00 142.56 ? 1544 TRP A CG    1 
ATOM   90    C  CD1   . TRP A 1 1544 ? 117.444 183.093 164.571 1.00 140.41 ? 1544 TRP A CD1   1 
ATOM   91    C  CD2   . TRP A 1 1544 ? 118.625 184.961 164.929 1.00 141.36 ? 1544 TRP A CD2   1 
ATOM   92    N  NE1   . TRP A 1 1544 ? 116.683 184.158 164.152 1.00 140.36 ? 1544 TRP A NE1   1 
ATOM   93    C  CE2   . TRP A 1 1544 ? 117.385 185.315 164.361 1.00 139.51 ? 1544 TRP A CE2   1 
ATOM   94    C  CE3   . TRP A 1 1544 ? 119.537 185.975 165.241 1.00 136.62 ? 1544 TRP A CE3   1 
ATOM   95    C  CZ2   . TRP A 1 1544 ? 117.033 186.638 164.101 1.00 133.42 ? 1544 TRP A CZ2   1 
ATOM   96    C  CZ3   . TRP A 1 1544 ? 119.187 187.287 164.981 1.00 133.76 ? 1544 TRP A CZ3   1 
ATOM   97    C  CH2   . TRP A 1 1544 ? 117.945 187.607 164.417 1.00 130.85 ? 1544 TRP A CH2   1 
ATOM   98    N  N     . VAL A 1 1545 ? 122.501 184.123 164.810 1.00 136.07 ? 1545 VAL A N     1 
ATOM   99    C  CA    . VAL A 1 1545 ? 123.182 185.348 164.395 1.00 134.19 ? 1545 VAL A CA    1 
ATOM   100   C  C     . VAL A 1 1545 ? 123.856 185.156 163.043 1.00 134.29 ? 1545 VAL A C     1 
ATOM   101   O  O     . VAL A 1 1545 ? 123.663 185.957 162.117 1.00 129.94 ? 1545 VAL A O     1 
ATOM   102   C  CB    . VAL A 1 1545 ? 124.187 185.808 165.467 1.00 130.40 ? 1545 VAL A CB    1 
ATOM   103   C  CG1   . VAL A 1 1545 ? 124.986 186.993 164.955 1.00 121.97 ? 1545 VAL A CG1   1 
ATOM   104   C  CG2   . VAL A 1 1545 ? 123.455 186.215 166.732 1.00 124.19 ? 1545 VAL A CG2   1 
ATOM   105   N  N     . TYR A 1 1546 ? 124.643 184.083 162.891 1.00 136.22 ? 1546 TYR A N     1 
ATOM   106   C  CA    . TYR A 1 1546 ? 125.362 183.966 161.624 1.00 133.20 ? 1546 TYR A CA    1 
ATOM   107   C  C     . TYR A 1 1546 ? 124.429 183.577 160.482 1.00 131.20 ? 1546 TYR A C     1 
ATOM   108   O  O     . TYR A 1 1546 ? 124.638 184.015 159.343 1.00 127.65 ? 1546 TYR A O     1 
ATOM   109   C  CB    . TYR A 1 1546 ? 126.564 183.009 161.725 1.00 132.95 ? 1546 TYR A CB    1 
ATOM   110   C  CG    . TYR A 1 1546 ? 126.327 181.543 162.044 1.00 132.40 ? 1546 TYR A CG    1 
ATOM   111   C  CD1   . TYR A 1 1546 ? 125.598 180.724 161.191 1.00 131.26 ? 1546 TYR A CD1   1 
ATOM   112   C  CD2   . TYR A 1 1546 ? 126.921 180.957 163.155 1.00 130.54 ? 1546 TYR A CD2   1 
ATOM   113   C  CE1   . TYR A 1 1546 ? 125.411 179.384 161.470 1.00 130.99 ? 1546 TYR A CE1   1 
ATOM   114   C  CE2   . TYR A 1 1546 ? 126.746 179.617 163.439 1.00 130.07 ? 1546 TYR A CE2   1 
ATOM   115   C  CZ    . TYR A 1 1546 ? 125.989 178.836 162.593 1.00 131.14 ? 1546 TYR A CZ    1 
ATOM   116   O  OH    . TYR A 1 1546 ? 125.808 177.500 162.872 1.00 130.52 ? 1546 TYR A OH    1 
ATOM   117   N  N     . LEU A 1 1547 ? 123.369 182.809 160.758 1.00 134.10 ? 1547 LEU A N     1 
ATOM   118   C  CA    . LEU A 1 1547 ? 122.433 182.469 159.692 1.00 132.07 ? 1547 LEU A CA    1 
ATOM   119   C  C     . LEU A 1 1547 ? 121.610 183.680 159.271 1.00 131.91 ? 1547 LEU A C     1 
ATOM   120   O  O     . LEU A 1 1547 ? 121.300 183.840 158.086 1.00 131.29 ? 1547 LEU A O     1 
ATOM   121   C  CB    . LEU A 1 1547 ? 121.529 181.319 160.131 1.00 130.67 ? 1547 LEU A CB    1 
ATOM   122   C  CG    . LEU A 1 1547 ? 122.145 179.929 159.954 1.00 127.85 ? 1547 LEU A CG    1 
ATOM   123   C  CD1   . LEU A 1 1547 ? 121.103 178.848 160.152 1.00 121.14 ? 1547 LEU A CD1   1 
ATOM   124   C  CD2   . LEU A 1 1547 ? 122.802 179.796 158.588 1.00 129.45 ? 1547 LEU A CD2   1 
ATOM   125   N  N     . GLU A 1 1548 ? 121.253 184.549 160.221 1.00 133.13 ? 1548 GLU A N     1 
ATOM   126   C  CA    . GLU A 1 1548 ? 120.573 185.790 159.870 1.00 133.28 ? 1548 GLU A CA    1 
ATOM   127   C  C     . GLU A 1 1548 ? 121.483 186.694 159.055 1.00 133.75 ? 1548 GLU A C     1 
ATOM   128   O  O     . GLU A 1 1548 ? 121.037 187.322 158.089 1.00 130.67 ? 1548 GLU A O     1 
ATOM   129   C  CB    . GLU A 1 1548 ? 120.096 186.506 161.134 1.00 132.20 ? 1548 GLU A CB    1 
ATOM   130   C  CG    . GLU A 1 1548 ? 119.073 187.603 160.874 1.00 127.53 ? 1548 GLU A CG    1 
ATOM   131   C  CD    . GLU A 1 1548 ? 119.711 188.966 160.683 1.00 127.04 ? 1548 GLU A CD    1 
ATOM   132   O  OE1   . GLU A 1 1548 ? 120.911 189.112 160.998 1.00 130.90 ? 1548 GLU A OE1   1 
ATOM   133   O  OE2   . GLU A 1 1548 ? 119.012 189.890 160.218 1.00 119.90 ? 1548 GLU A OE2   1 
ATOM   134   N  N     . GLY A 1 1549 ? 122.762 186.776 159.429 1.00 134.91 ? 1549 GLY A N     1 
ATOM   135   C  CA    . GLY A 1 1549 ? 123.703 187.528 158.617 1.00 134.70 ? 1549 GLY A CA    1 
ATOM   136   C  C     . GLY A 1 1549 ? 123.801 186.991 157.202 1.00 131.72 ? 1549 GLY A C     1 
ATOM   137   O  O     . GLY A 1 1549 ? 123.821 187.757 156.235 1.00 125.06 ? 1549 GLY A O     1 
ATOM   138   N  N     . ILE A 1 1550 ? 123.847 185.663 157.062 1.00 131.34 ? 1550 ILE A N     1 
ATOM   139   C  CA    . ILE A 1 1550 ? 123.918 185.048 155.738 1.00 128.67 ? 1550 ILE A CA    1 
ATOM   140   C  C     . ILE A 1 1550 ? 122.661 185.358 154.932 1.00 129.52 ? 1550 ILE A C     1 
ATOM   141   O  O     . ILE A 1 1550 ? 122.733 185.745 153.759 1.00 126.72 ? 1550 ILE A O     1 
ATOM   142   C  CB    . ILE A 1 1550 ? 124.148 183.531 155.868 1.00 128.36 ? 1550 ILE A CB    1 
ATOM   143   C  CG1   . ILE A 1 1550 ? 125.620 183.238 156.163 1.00 122.60 ? 1550 ILE A CG1   1 
ATOM   144   C  CG2   . ILE A 1 1550 ? 123.682 182.804 154.614 1.00 122.34 ? 1550 ILE A CG2   1 
ATOM   145   C  CD1   . ILE A 1 1550 ? 125.881 181.822 156.631 1.00 111.88 ? 1550 ILE A CD1   1 
ATOM   146   N  N     . PHE A 1 1551 ? 121.488 185.199 155.551 1.00 130.17 ? 1551 PHE A N     1 
ATOM   147   C  CA    . PHE A 1 1551 ? 120.231 185.366 154.829 1.00 126.93 ? 1551 PHE A CA    1 
ATOM   148   C  C     . PHE A 1 1551 ? 119.900 186.827 154.551 1.00 126.01 ? 1551 PHE A C     1 
ATOM   149   O  O     . PHE A 1 1551 ? 119.110 187.105 153.643 1.00 122.71 ? 1551 PHE A O     1 
ATOM   150   C  CB    . PHE A 1 1551 ? 119.087 184.715 155.609 1.00 127.13 ? 1551 PHE A CB    1 
ATOM   151   C  CG    . PHE A 1 1551 ? 118.889 183.259 155.293 1.00 130.83 ? 1551 PHE A CG    1 
ATOM   152   C  CD1   . PHE A 1 1551 ? 118.230 182.871 154.139 1.00 129.64 ? 1551 PHE A CD1   1 
ATOM   153   C  CD2   . PHE A 1 1551 ? 119.358 182.279 156.152 1.00 135.23 ? 1551 PHE A CD2   1 
ATOM   154   C  CE1   . PHE A 1 1551 ? 118.045 181.532 153.844 1.00 129.08 ? 1551 PHE A CE1   1 
ATOM   155   C  CE2   . PHE A 1 1551 ? 119.176 180.938 155.864 1.00 134.77 ? 1551 PHE A CE2   1 
ATOM   156   C  CZ    . PHE A 1 1551 ? 118.519 180.565 154.709 1.00 129.31 ? 1551 PHE A CZ    1 
ATOM   157   N  N     . THR A 1 1552 ? 120.476 187.762 155.305 1.00 127.63 ? 1552 THR A N     1 
ATOM   158   C  CA    . THR A 1 1552 ? 120.224 189.183 155.104 1.00 126.84 ? 1552 THR A CA    1 
ATOM   159   C  C     . THR A 1 1552 ? 121.232 189.837 154.170 1.00 125.48 ? 1552 THR A C     1 
ATOM   160   O  O     . THR A 1 1552 ? 120.850 190.679 153.351 1.00 120.16 ? 1552 THR A O     1 
ATOM   161   C  CB    . THR A 1 1552 ? 120.227 189.918 156.449 1.00 127.59 ? 1552 THR A CB    1 
ATOM   162   O  OG1   . THR A 1 1552 ? 119.483 189.159 157.411 1.00 127.01 ? 1552 THR A OG1   1 
ATOM   163   C  CG2   . THR A 1 1552 ? 119.601 191.298 156.307 1.00 120.46 ? 1552 THR A CG2   1 
ATOM   164   N  N     . GLY A 1 1553 ? 122.512 189.473 154.274 1.00 125.22 ? 1553 GLY A N     1 
ATOM   165   C  CA    . GLY A 1 1553 ? 123.489 189.988 153.329 1.00 121.81 ? 1553 GLY A CA    1 
ATOM   166   C  C     . GLY A 1 1553 ? 123.204 189.540 151.909 1.00 122.18 ? 1553 GLY A C     1 
ATOM   167   O  O     . GLY A 1 1553 ? 123.434 190.285 150.953 1.00 116.49 ? 1553 GLY A O     1 
ATOM   168   N  N     . SER A 1 1554 ? 122.699 188.320 151.753 1.00 125.73 ? 1554 SER A N     1 
ATOM   169   C  CA    . SER A 1 1554 ? 122.307 187.780 150.453 1.00 122.22 ? 1554 SER A CA    1 
ATOM   170   C  C     . SER A 1 1554 ? 120.788 187.878 150.354 1.00 124.44 ? 1554 SER A C     1 
ATOM   171   O  O     . SER A 1 1554 ? 120.059 186.983 150.783 1.00 124.21 ? 1554 SER A O     1 
ATOM   172   C  CB    . SER A 1 1554 ? 122.796 186.346 150.292 1.00 119.71 ? 1554 SER A CB    1 
ATOM   173   O  OG    . SER A 1 1554 ? 122.470 185.566 151.430 1.00 125.18 ? 1554 SER A OG    1 
ATOM   174   N  N     . ALA A 1 1555 ? 120.308 188.986 149.787 1.00 124.63 ? 1555 ALA A N     1 
ATOM   175   C  CA    . ALA A 1 1555 ? 118.874 189.178 149.613 1.00 121.01 ? 1555 ALA A CA    1 
ATOM   176   C  C     . ALA A 1 1555 ? 118.292 188.307 148.508 1.00 120.76 ? 1555 ALA A C     1 
ATOM   177   O  O     . ALA A 1 1555 ? 117.072 188.117 148.471 1.00 120.25 ? 1555 ALA A O     1 
ATOM   178   C  CB    . ALA A 1 1555 ? 118.572 190.649 149.322 1.00 109.33 ? 1555 ALA A CB    1 
ATOM   179   N  N     . ASP A 1 1556 ? 119.127 187.779 147.616 1.00 116.83 ? 1556 ASP A N     1 
ATOM   180   C  CA    . ASP A 1 1556 ? 118.678 186.919 146.530 1.00 116.73 ? 1556 ASP A CA    1 
ATOM   181   C  C     . ASP A 1 1556 ? 118.820 185.437 146.851 1.00 117.40 ? 1556 ASP A C     1 
ATOM   182   O  O     . ASP A 1 1556 ? 118.538 184.601 145.987 1.00 114.61 ? 1556 ASP A O     1 
ATOM   183   C  CB    . ASP A 1 1556 ? 119.452 187.246 145.250 1.00 114.45 ? 1556 ASP A CB    1 
ATOM   184   C  CG    . ASP A 1 1556 ? 119.102 188.612 144.693 1.00 111.43 ? 1556 ASP A CG    1 
ATOM   185   O  OD1   . ASP A 1 1556 ? 117.957 189.065 144.901 1.00 111.60 ? 1556 ASP A OD1   1 
ATOM   186   O  OD2   . ASP A 1 1556 ? 119.974 189.235 144.051 1.00 102.33 ? 1556 ASP A OD2   1 
ATOM   187   N  N     . ILE A 1 1557 ? 119.249 185.091 148.068 1.00 117.59 ? 1557 ILE A N     1 
ATOM   188   C  CA    . ILE A 1 1557 ? 119.420 183.690 148.432 1.00 116.44 ? 1557 ILE A CA    1 
ATOM   189   C  C     . ILE A 1 1557 ? 118.081 182.981 148.589 1.00 119.00 ? 1557 ILE A C     1 
ATOM   190   O  O     . ILE A 1 1557 ? 118.033 181.745 148.577 1.00 117.63 ? 1557 ILE A O     1 
ATOM   191   C  CB    . ILE A 1 1557 ? 120.255 183.572 149.722 1.00 116.61 ? 1557 ILE A CB    1 
ATOM   192   C  CG1   . ILE A 1 1557 ? 120.908 182.192 149.818 1.00 114.07 ? 1557 ILE A CG1   1 
ATOM   193   C  CG2   . ILE A 1 1557 ? 119.393 183.834 150.946 1.00 119.67 ? 1557 ILE A CG2   1 
ATOM   194   C  CD1   . ILE A 1 1557 ? 121.956 182.090 150.904 1.00 112.93 ? 1557 ILE A CD1   1 
ATOM   195   N  N     . LYS A 1 1558 ? 116.987 183.732 148.736 1.00 121.48 ? 1558 LYS A N     1 
ATOM   196   C  CA    . LYS A 1 1558 ? 115.679 183.108 148.900 1.00 123.69 ? 1558 LYS A CA    1 
ATOM   197   C  C     . LYS A 1 1558 ? 115.180 182.489 147.601 1.00 123.07 ? 1558 LYS A C     1 
ATOM   198   O  O     . LYS A 1 1558 ? 114.471 181.476 147.633 1.00 120.34 ? 1558 LYS A O     1 
ATOM   199   C  CB    . LYS A 1 1558 ? 114.671 184.132 149.419 1.00 119.82 ? 1558 LYS A CB    1 
ATOM   200   C  CG    . LYS A 1 1558 ? 114.684 185.458 148.674 1.00 113.73 ? 1558 LYS A CG    1 
ATOM   201   C  CD    . LYS A 1 1558 ? 113.825 186.494 149.379 1.00 110.79 ? 1558 LYS A CD    1 
ATOM   202   C  CE    . LYS A 1 1558 ? 112.465 185.923 149.757 1.00 108.00 ? 1558 LYS A CE    1 
ATOM   203   N  NZ    . LYS A 1 1558 ? 111.661 186.879 150.567 1.00 93.96  ? 1558 LYS A NZ    1 
ATOM   204   N  N     . HIS A 1 1559 ? 115.535 183.078 146.457 1.00 123.73 ? 1559 HIS A N     1 
ATOM   205   C  CA    . HIS A 1 1559 ? 115.058 182.575 145.175 1.00 123.22 ? 1559 HIS A CA    1 
ATOM   206   C  C     . HIS A 1 1559 ? 115.583 181.180 144.865 1.00 124.75 ? 1559 HIS A C     1 
ATOM   207   O  O     . HIS A 1 1559 ? 114.924 180.432 144.135 1.00 125.48 ? 1559 HIS A O     1 
ATOM   208   C  CB    . HIS A 1 1559 ? 115.447 183.545 144.060 1.00 120.01 ? 1559 HIS A CB    1 
ATOM   209   C  CG    . HIS A 1 1559 ? 115.170 184.980 144.387 1.00 121.19 ? 1559 HIS A CG    1 
ATOM   210   N  ND1   . HIS A 1 1559 ? 113.943 185.416 144.838 1.00 117.92 ? 1559 HIS A ND1   1 
ATOM   211   C  CD2   . HIS A 1 1559 ? 115.962 186.077 144.332 1.00 121.17 ? 1559 HIS A CD2   1 
ATOM   212   C  CE1   . HIS A 1 1559 ? 113.990 186.720 145.045 1.00 114.70 ? 1559 HIS A CE1   1 
ATOM   213   N  NE2   . HIS A 1 1559 ? 115.204 187.145 144.746 1.00 118.65 ? 1559 HIS A NE2   1 
ATOM   214   N  N     . LEU A 1 1560 ? 116.748 180.813 145.400 1.00 123.29 ? 1560 LEU A N     1 
ATOM   215   C  CA    . LEU A 1 1560 ? 117.295 179.478 145.220 1.00 120.14 ? 1560 LEU A CA    1 
ATOM   216   C  C     . LEU A 1 1560 ? 117.039 178.560 146.405 1.00 121.33 ? 1560 LEU A C     1 
ATOM   217   O  O     . LEU A 1 1560 ? 117.177 177.340 146.261 1.00 117.84 ? 1560 LEU A O     1 
ATOM   218   C  CB    . LEU A 1 1560 ? 118.807 179.553 144.958 1.00 112.58 ? 1560 LEU A CB    1 
ATOM   219   C  CG    . LEU A 1 1560 ? 119.424 178.401 144.159 1.00 110.44 ? 1560 LEU A CG    1 
ATOM   220   C  CD1   . LEU A 1 1560 ? 118.543 178.027 142.976 1.00 104.41 ? 1560 LEU A CD1   1 
ATOM   221   C  CD2   . LEU A 1 1560 ? 120.828 178.755 143.695 1.00 104.23 ? 1560 LEU A CD2   1 
ATOM   222   N  N     . LEU A 1 1561 ? 116.651 179.104 147.556 1.00 125.07 ? 1561 LEU A N     1 
ATOM   223   C  CA    . LEU A 1 1561 ? 116.450 178.327 148.780 1.00 122.55 ? 1561 LEU A CA    1 
ATOM   224   C  C     . LEU A 1 1561 ? 115.077 178.636 149.369 1.00 123.65 ? 1561 LEU A C     1 
ATOM   225   O  O     . LEU A 1 1561 ? 114.969 179.180 150.471 1.00 122.87 ? 1561 LEU A O     1 
ATOM   226   C  CB    . LEU A 1 1561 ? 117.555 178.636 149.790 1.00 119.87 ? 1561 LEU A CB    1 
ATOM   227   C  CG    . LEU A 1 1561 ? 119.022 178.409 149.418 1.00 110.92 ? 1561 LEU A CG    1 
ATOM   228   C  CD1   . LEU A 1 1561 ? 119.889 178.432 150.666 1.00 103.70 ? 1561 LEU A CD1   1 
ATOM   229   C  CD2   . LEU A 1 1561 ? 119.201 177.100 148.678 1.00 109.68 ? 1561 LEU A CD2   1 
ATOM   230   N  N     . PRO A 1 1562 ? 113.995 178.282 148.662 1.00 125.19 ? 1562 PRO A N     1 
ATOM   231   C  CA    . PRO A 1 1562 ? 112.660 178.750 149.071 1.00 123.19 ? 1562 PRO A CA    1 
ATOM   232   C  C     . PRO A 1 1562 ? 112.127 178.143 150.364 1.00 120.84 ? 1562 PRO A C     1 
ATOM   233   O  O     . PRO A 1 1562 ? 111.704 178.877 151.266 1.00 121.13 ? 1562 PRO A O     1 
ATOM   234   C  CB    . PRO A 1 1562 ? 111.778 178.363 147.876 1.00 123.81 ? 1562 PRO A CB    1 
ATOM   235   C  CG    . PRO A 1 1562 ? 112.468 177.200 147.254 1.00 119.15 ? 1562 PRO A CG    1 
ATOM   236   C  CD    . PRO A 1 1562 ? 113.941 177.372 147.503 1.00 120.15 ? 1562 PRO A CD    1 
ATOM   237   N  N     . VAL A 1 1563 ? 112.125 176.811 150.464 1.00 121.78 ? 1563 VAL A N     1 
ATOM   238   C  CA    . VAL A 1 1563 ? 111.505 176.161 151.616 1.00 122.63 ? 1563 VAL A CA    1 
ATOM   239   C  C     . VAL A 1 1563 ? 112.266 176.491 152.896 1.00 121.37 ? 1563 VAL A C     1 
ATOM   240   O  O     . VAL A 1 1563 ? 111.661 176.793 153.935 1.00 119.68 ? 1563 VAL A O     1 
ATOM   241   C  CB    . VAL A 1 1563 ? 111.377 174.643 151.378 1.00 113.26 ? 1563 VAL A CB    1 
ATOM   242   C  CG1   . VAL A 1 1563 ? 112.740 173.975 151.249 1.00 105.86 ? 1563 VAL A CG1   1 
ATOM   243   C  CG2   . VAL A 1 1563 ? 110.568 173.999 152.495 1.00 110.67 ? 1563 VAL A CG2   1 
ATOM   244   N  N     . GLU A 1 1564 ? 113.598 176.469 152.844 1.00 119.96 ? 1564 GLU A N     1 
ATOM   245   C  CA    . GLU A 1 1564 ? 114.363 176.879 154.011 1.00 117.59 ? 1564 GLU A CA    1 
ATOM   246   C  C     . GLU A 1 1564 ? 114.277 178.380 154.246 1.00 119.68 ? 1564 GLU A C     1 
ATOM   247   O  O     . GLU A 1 1564 ? 114.458 178.818 155.382 1.00 119.05 ? 1564 GLU A O     1 
ATOM   248   C  CB    . GLU A 1 1564 ? 115.821 176.435 153.886 1.00 119.46 ? 1564 GLU A CB    1 
ATOM   249   C  CG    . GLU A 1 1564 ? 116.535 176.939 152.655 1.00 122.38 ? 1564 GLU A CG    1 
ATOM   250   C  CD    . GLU A 1 1564 ? 116.724 175.853 151.616 1.00 120.70 ? 1564 GLU A CD    1 
ATOM   251   O  OE1   . GLU A 1 1564 ? 115.728 175.195 151.253 1.00 119.82 ? 1564 GLU A OE1   1 
ATOM   252   O  OE2   . GLU A 1 1564 ? 117.873 175.648 151.173 1.00 118.20 ? 1564 GLU A OE2   1 
ATOM   253   N  N     . THR A 1 1565 ? 113.977 179.175 153.215 1.00 123.93 ? 1565 THR A N     1 
ATOM   254   C  CA    . THR A 1 1565 ? 113.697 180.590 153.450 1.00 123.27 ? 1565 THR A CA    1 
ATOM   255   C  C     . THR A 1 1565 ? 112.430 180.769 154.276 1.00 123.09 ? 1565 THR A C     1 
ATOM   256   O  O     . THR A 1 1565 ? 112.400 181.582 155.206 1.00 123.12 ? 1565 THR A O     1 
ATOM   257   C  CB    . THR A 1 1565 ? 113.577 181.343 152.125 1.00 121.17 ? 1565 THR A CB    1 
ATOM   258   O  OG1   . THR A 1 1565 ? 114.860 181.395 151.488 1.00 122.51 ? 1565 THR A OG1   1 
ATOM   259   C  CG2   . THR A 1 1565 ? 113.075 182.762 152.357 1.00 115.29 ? 1565 THR A CG2   1 
ATOM   260   N  N     . GLN A 1 1566 ? 111.374 180.016 153.959 1.00 123.36 ? 1566 GLN A N     1 
ATOM   261   C  CA    . GLN A 1 1566 ? 110.161 180.078 154.772 1.00 119.74 ? 1566 GLN A CA    1 
ATOM   262   C  C     . GLN A 1 1566 ? 110.420 179.567 156.185 1.00 121.64 ? 1566 GLN A C     1 
ATOM   263   O  O     . GLN A 1 1566 ? 109.940 180.152 157.169 1.00 120.95 ? 1566 GLN A O     1 
ATOM   264   C  CB    . GLN A 1 1566 ? 109.038 179.280 154.110 1.00 117.60 ? 1566 GLN A CB    1 
ATOM   265   C  CG    . GLN A 1 1566 ? 108.896 179.521 152.616 1.00 121.38 ? 1566 GLN A CG    1 
ATOM   266   C  CD    . GLN A 1 1566 ? 108.739 180.989 152.275 1.00 119.54 ? 1566 GLN A CD    1 
ATOM   267   O  OE1   . GLN A 1 1566 ? 109.564 181.566 151.567 1.00 110.94 ? 1566 GLN A OE1   1 
ATOM   268   N  NE2   . GLN A 1 1566 ? 107.676 181.603 152.781 1.00 116.61 ? 1566 GLN A NE2   1 
ATOM   269   N  N     . ARG A 1 1567 ? 111.182 178.477 156.305 1.00 121.82 ? 1567 ARG A N     1 
ATOM   270   C  CA    . ARG A 1 1567 ? 111.519 177.956 157.627 1.00 119.83 ? 1567 ARG A CA    1 
ATOM   271   C  C     . ARG A 1 1567 ? 112.312 178.978 158.435 1.00 121.70 ? 1567 ARG A C     1 
ATOM   272   O  O     . ARG A 1 1567 ? 112.071 179.154 159.634 1.00 122.68 ? 1567 ARG A O     1 
ATOM   273   C  CB    . ARG A 1 1567 ? 112.299 176.649 157.493 1.00 115.20 ? 1567 ARG A CB    1 
ATOM   274   C  CG    . ARG A 1 1567 ? 111.499 175.514 156.876 1.00 109.55 ? 1567 ARG A CG    1 
ATOM   275   C  CD    . ARG A 1 1567 ? 112.354 174.270 156.691 1.00 110.28 ? 1567 ARG A CD    1 
ATOM   276   N  NE    . ARG A 1 1567 ? 111.717 173.291 155.818 1.00 115.87 ? 1567 ARG A NE    1 
ATOM   277   C  CZ    . ARG A 1 1567 ? 110.730 172.486 156.186 1.00 117.30 ? 1567 ARG A CZ    1 
ATOM   278   N  NH1   . ARG A 1 1567 ? 110.238 172.510 157.414 1.00 118.08 ? 1567 ARG A NH1   1 
ATOM   279   N  NH2   . ARG A 1 1567 ? 110.224 171.633 155.300 1.00 109.90 ? 1567 ARG A NH2   1 
ATOM   280   N  N     . PHE A 1 1568 ? 113.253 179.672 157.793 1.00 122.63 ? 1568 PHE A N     1 
ATOM   281   C  CA    . PHE A 1 1568 ? 114.033 180.680 158.496 1.00 125.64 ? 1568 PHE A CA    1 
ATOM   282   C  C     . PHE A 1 1568 ? 113.201 181.913 158.814 1.00 128.76 ? 1568 PHE A C     1 
ATOM   283   O  O     . PHE A 1 1568 ? 113.477 182.599 159.800 1.00 131.96 ? 1568 PHE A O     1 
ATOM   284   C  CB    . PHE A 1 1568 ? 115.263 181.072 157.681 1.00 128.13 ? 1568 PHE A CB    1 
ATOM   285   C  CG    . PHE A 1 1568 ? 116.249 181.900 158.449 1.00 132.97 ? 1568 PHE A CG    1 
ATOM   286   C  CD1   . PHE A 1 1568 ? 116.907 181.367 159.545 1.00 133.13 ? 1568 PHE A CD1   1 
ATOM   287   C  CD2   . PHE A 1 1568 ? 116.507 183.211 158.089 1.00 131.01 ? 1568 PHE A CD2   1 
ATOM   288   C  CE1   . PHE A 1 1568 ? 117.812 182.122 160.261 1.00 131.66 ? 1568 PHE A CE1   1 
ATOM   289   C  CE2   . PHE A 1 1568 ? 117.412 183.972 158.804 1.00 128.38 ? 1568 PHE A CE2   1 
ATOM   290   C  CZ    . PHE A 1 1568 ? 118.064 183.425 159.892 1.00 131.96 ? 1568 PHE A CZ    1 
ATOM   291   N  N     . GLN A 1 1569 ? 112.192 182.220 157.998 1.00 125.01 ? 1569 GLN A N     1 
ATOM   292   C  CA    . GLN A 1 1569 ? 111.260 183.284 158.359 1.00 123.97 ? 1569 GLN A CA    1 
ATOM   293   C  C     . GLN A 1 1569 ? 110.498 182.925 159.628 1.00 125.40 ? 1569 GLN A C     1 
ATOM   294   O  O     . GLN A 1 1569 ? 110.322 183.765 160.520 1.00 123.87 ? 1569 GLN A O     1 
ATOM   295   C  CB    . GLN A 1 1569 ? 110.293 183.552 157.206 1.00 117.58 ? 1569 GLN A CB    1 
ATOM   296   C  CG    . GLN A 1 1569 ? 109.256 184.620 157.507 1.00 118.99 ? 1569 GLN A CG    1 
ATOM   297   C  CD    . GLN A 1 1569 ? 109.879 185.919 157.977 1.00 117.42 ? 1569 GLN A CD    1 
ATOM   298   O  OE1   . GLN A 1 1569 ? 109.526 186.444 159.033 1.00 116.62 ? 1569 GLN A OE1   1 
ATOM   299   N  NE2   . GLN A 1 1569 ? 110.810 186.447 157.191 1.00 112.26 ? 1569 GLN A NE2   1 
ATOM   300   N  N     . SER A 1 1570 ? 110.048 181.672 159.727 1.00 125.03 ? 1570 SER A N     1 
ATOM   301   C  CA    . SER A 1 1570 ? 109.409 181.215 160.959 1.00 122.34 ? 1570 SER A CA    1 
ATOM   302   C  C     . SER A 1 1570 ? 110.376 181.282 162.138 1.00 127.61 ? 1570 SER A C     1 
ATOM   303   O  O     . SER A 1 1570 ? 109.997 181.685 163.247 1.00 127.94 ? 1570 SER A O     1 
ATOM   304   C  CB    . SER A 1 1570 ? 108.879 179.793 160.776 1.00 116.78 ? 1570 SER A CB    1 
ATOM   305   O  OG    . SER A 1 1570 ? 107.996 179.717 159.671 1.00 113.96 ? 1570 SER A OG    1 
ATOM   306   N  N     . ILE A 1 1571 ? 111.633 180.890 161.913 1.00 129.48 ? 1571 ILE A N     1 
ATOM   307   C  CA    . ILE A 1 1571 ? 112.641 180.943 162.970 1.00 130.48 ? 1571 ILE A CA    1 
ATOM   308   C  C     . ILE A 1 1571 ? 112.878 182.382 163.415 1.00 134.65 ? 1571 ILE A C     1 
ATOM   309   O  O     . ILE A 1 1571 ? 113.034 182.660 164.609 1.00 135.78 ? 1571 ILE A O     1 
ATOM   310   C  CB    . ILE A 1 1571 ? 113.946 180.274 162.497 1.00 130.69 ? 1571 ILE A CB    1 
ATOM   311   C  CG1   . ILE A 1 1571 ? 113.745 178.768 162.327 1.00 126.32 ? 1571 ILE A CG1   1 
ATOM   312   C  CG2   . ILE A 1 1571 ? 115.078 180.545 163.478 1.00 130.23 ? 1571 ILE A CG2   1 
ATOM   313   C  CD1   . ILE A 1 1571 ? 114.976 178.044 161.827 1.00 121.76 ? 1571 ILE A CD1   1 
ATOM   314   N  N     . SER A 1 1572 ? 112.920 183.316 162.463 1.00 133.34 ? 1572 SER A N     1 
ATOM   315   C  CA    . SER A 1 1572 ? 113.115 184.723 162.795 1.00 132.90 ? 1572 SER A CA    1 
ATOM   316   C  C     . SER A 1 1572 ? 111.927 185.278 163.568 1.00 133.44 ? 1572 SER A C     1 
ATOM   317   O  O     . SER A 1 1572 ? 112.102 186.086 164.486 1.00 132.87 ? 1572 SER A O     1 
ATOM   318   C  CB    . SER A 1 1572 ? 113.353 185.535 161.522 1.00 127.53 ? 1572 SER A CB    1 
ATOM   319   O  OG    . SER A 1 1572 ? 114.521 185.099 160.848 1.00 127.11 ? 1572 SER A OG    1 
ATOM   320   N  N     . THR A 1 1573 ? 110.709 184.870 163.202 1.00 133.43 ? 1573 THR A N     1 
ATOM   321   C  CA    . THR A 1 1573 ? 109.539 185.275 163.977 1.00 131.39 ? 1573 THR A CA    1 
ATOM   322   C  C     . THR A 1 1573 ? 109.622 184.750 165.406 1.00 135.76 ? 1573 THR A C     1 
ATOM   323   O  O     . THR A 1 1573 ? 109.326 185.476 166.365 1.00 134.02 ? 1573 THR A O     1 
ATOM   324   C  CB    . THR A 1 1573 ? 108.260 184.785 163.298 1.00 125.65 ? 1573 THR A CB    1 
ATOM   325   O  OG1   . THR A 1 1573 ? 108.311 185.094 161.900 1.00 123.70 ? 1573 THR A OG1   1 
ATOM   326   C  CG2   . THR A 1 1573 ? 107.041 185.453 163.915 1.00 118.23 ? 1573 THR A CG2   1 
ATOM   327   N  N     . GLU A 1 1574 ? 110.038 183.491 165.567 1.00 137.05 ? 1574 GLU A N     1 
ATOM   328   C  CA    . GLU A 1 1574 ? 110.227 182.943 166.907 1.00 134.75 ? 1574 GLU A CA    1 
ATOM   329   C  C     . GLU A 1 1574 ? 111.292 183.719 167.675 1.00 136.39 ? 1574 GLU A C     1 
ATOM   330   O  O     . GLU A 1 1574 ? 111.125 184.009 168.865 1.00 135.05 ? 1574 GLU A O     1 
ATOM   331   C  CB    . GLU A 1 1574 ? 110.602 181.464 166.821 1.00 127.63 ? 1574 GLU A CB    1 
ATOM   332   C  CG    . GLU A 1 1574 ? 109.471 180.560 166.363 1.00 124.63 ? 1574 GLU A CG    1 
ATOM   333   C  CD    . GLU A 1 1574 ? 108.551 180.161 167.499 1.00 121.03 ? 1574 GLU A CD    1 
ATOM   334   O  OE1   . GLU A 1 1574 ? 108.959 179.319 168.326 1.00 118.94 ? 1574 GLU A OE1   1 
ATOM   335   O  OE2   . GLU A 1 1574 ? 107.422 180.689 167.564 1.00 118.58 ? 1574 GLU A OE2   1 
ATOM   336   N  N     . PHE A 1 1575 ? 112.396 184.058 167.009 1.00 137.15 ? 1575 PHE A N     1 
ATOM   337   C  CA    . PHE A 1 1575 ? 113.473 184.803 167.652 1.00 135.80 ? 1575 PHE A CA    1 
ATOM   338   C  C     . PHE A 1 1575 ? 113.000 186.181 168.095 1.00 134.92 ? 1575 PHE A C     1 
ATOM   339   O  O     . PHE A 1 1575 ? 113.356 186.649 169.184 1.00 135.05 ? 1575 PHE A O     1 
ATOM   340   C  CB    . PHE A 1 1575 ? 114.656 184.912 166.691 1.00 134.46 ? 1575 PHE A CB    1 
ATOM   341   C  CG    . PHE A 1 1575 ? 115.985 185.057 167.370 1.00 137.88 ? 1575 PHE A CG    1 
ATOM   342   C  CD1   . PHE A 1 1575 ? 116.693 183.938 167.778 1.00 137.55 ? 1575 PHE A CD1   1 
ATOM   343   C  CD2   . PHE A 1 1575 ? 116.543 186.307 167.569 1.00 135.75 ? 1575 PHE A CD2   1 
ATOM   344   C  CE1   . PHE A 1 1575 ? 117.922 184.066 168.395 1.00 134.50 ? 1575 PHE A CE1   1 
ATOM   345   C  CE2   . PHE A 1 1575 ? 117.773 186.440 168.179 1.00 133.34 ? 1575 PHE A CE2   1 
ATOM   346   C  CZ    . PHE A 1 1575 ? 118.462 185.319 168.596 1.00 133.31 ? 1575 PHE A CZ    1 
ATOM   347   N  N     . LEU A 1 1576 ? 112.196 186.844 167.262 1.00 135.14 ? 1576 LEU A N     1 
ATOM   348   C  CA    . LEU A 1 1576 ? 111.602 188.117 167.655 1.00 134.32 ? 1576 LEU A CA    1 
ATOM   349   C  C     . LEU A 1 1576 ? 110.680 187.942 168.854 1.00 133.29 ? 1576 LEU A C     1 
ATOM   350   O  O     . LEU A 1 1576 ? 110.636 188.800 169.742 1.00 128.35 ? 1576 LEU A O     1 
ATOM   351   C  CB    . LEU A 1 1576 ? 110.843 188.732 166.479 1.00 130.39 ? 1576 LEU A CB    1 
ATOM   352   C  CG    . LEU A 1 1576 ? 111.673 189.194 165.279 1.00 126.80 ? 1576 LEU A CG    1 
ATOM   353   C  CD1   . LEU A 1 1576 ? 110.872 190.155 164.414 1.00 116.28 ? 1576 LEU A CD1   1 
ATOM   354   C  CD2   . LEU A 1 1576 ? 112.976 189.836 165.733 1.00 121.95 ? 1576 LEU A CD2   1 
ATOM   355   N  N     . ALA A 1 1577 ? 109.930 186.837 168.894 1.00 136.26 ? 1577 ALA A N     1 
ATOM   356   C  CA    . ALA A 1 1577 ? 109.079 186.570 170.051 1.00 134.31 ? 1577 ALA A CA    1 
ATOM   357   C  C     . ALA A 1 1577 ? 109.906 186.415 171.325 1.00 134.85 ? 1577 ALA A C     1 
ATOM   358   O  O     . ALA A 1 1577 ? 109.562 186.980 172.371 1.00 132.84 ? 1577 ALA A O     1 
ATOM   359   C  CB    . ALA A 1 1577 ? 108.232 185.322 169.805 1.00 125.35 ? 1577 ALA A CB    1 
ATOM   360   N  N     . LEU A 1 1578 ? 111.002 185.656 171.254 1.00 134.99 ? 1578 LEU A N     1 
ATOM   361   C  CA    . LEU A 1 1578 ? 111.874 185.515 172.421 1.00 132.07 ? 1578 LEU A CA    1 
ATOM   362   C  C     . LEU A 1 1578 ? 112.463 186.855 172.845 1.00 133.97 ? 1578 LEU A C     1 
ATOM   363   O  O     . LEU A 1 1578 ? 112.511 187.168 174.038 1.00 132.28 ? 1578 LEU A O     1 
ATOM   364   C  CB    . LEU A 1 1578 ? 112.989 184.495 172.163 1.00 125.75 ? 1578 LEU A CB    1 
ATOM   365   C  CG    . LEU A 1 1578 ? 112.716 182.992 172.330 1.00 121.03 ? 1578 LEU A CG    1 
ATOM   366   C  CD1   . LEU A 1 1578 ? 111.836 182.391 171.254 1.00 123.90 ? 1578 LEU A CD1   1 
ATOM   367   C  CD2   . LEU A 1 1578 ? 114.038 182.235 172.420 1.00 105.23 ? 1578 LEU A CD2   1 
ATOM   368   N  N     . MET A 1 1579 ? 112.921 187.662 171.886 1.00 136.24 ? 1579 MET A N     1 
ATOM   369   C  CA    . MET A 1 1579 ? 113.486 188.962 172.245 1.00 134.84 ? 1579 MET A CA    1 
ATOM   370   C  C     . MET A 1 1579 ? 112.436 189.895 172.838 1.00 130.50 ? 1579 MET A C     1 
ATOM   371   O  O     . MET A 1 1579 ? 112.751 190.725 173.698 1.00 126.01 ? 1579 MET A O     1 
ATOM   372   C  CB    . MET A 1 1579 ? 114.174 189.602 171.039 1.00 131.78 ? 1579 MET A CB    1 
ATOM   373   C  CG    . MET A 1 1579 ? 115.392 188.831 170.573 1.00 134.31 ? 1579 MET A CG    1 
ATOM   374   S  SD    . MET A 1 1579 ? 116.620 188.873 171.899 1.00 131.63 ? 1579 MET A SD    1 
ATOM   375   C  CE    . MET A 1 1579 ? 117.868 187.745 171.296 1.00 119.81 ? 1579 MET A CE    1 
ATOM   376   N  N     . LYS A 1 1580 ? 111.185 189.781 172.394 1.00 130.31 ? 1580 LYS A N     1 
ATOM   377   C  CA    . LYS A 1 1580 ? 110.131 190.598 172.984 1.00 126.04 ? 1580 LYS A CA    1 
ATOM   378   C  C     . LYS A 1 1580 ? 109.668 190.078 174.339 1.00 129.67 ? 1580 LYS A C     1 
ATOM   379   O  O     . LYS A 1 1580 ? 109.098 190.852 175.115 1.00 127.29 ? 1580 LYS A O     1 
ATOM   380   C  CB    . LYS A 1 1580 ? 108.941 190.693 172.028 1.00 118.64 ? 1580 LYS A CB    1 
ATOM   381   C  CG    . LYS A 1 1580 ? 108.121 191.968 172.184 1.00 110.59 ? 1580 LYS A CG    1 
ATOM   382   C  CD    . LYS A 1 1580 ? 108.981 193.217 172.033 1.00 105.59 ? 1580 LYS A CD    1 
ATOM   383   C  CE    . LYS A 1 1580 ? 109.643 193.289 170.665 1.00 100.09 ? 1580 LYS A CE    1 
ATOM   384   N  NZ    . LYS A 1 1580 ? 110.485 194.509 170.521 1.00 75.20  ? 1580 LYS A NZ    1 
ATOM   385   N  N     . LYS A 1 1581 ? 109.896 188.801 174.643 1.00 133.86 ? 1581 LYS A N     1 
ATOM   386   C  CA    . LYS A 1 1581 ? 109.457 188.232 175.914 1.00 131.81 ? 1581 LYS A CA    1 
ATOM   387   C  C     . LYS A 1 1581 ? 110.516 188.306 177.010 1.00 134.49 ? 1581 LYS A C     1 
ATOM   388   O  O     . LYS A 1 1581 ? 110.203 188.689 178.141 1.00 132.18 ? 1581 LYS A O     1 
ATOM   389   C  CB    . LYS A 1 1581 ? 109.016 186.777 175.714 1.00 126.15 ? 1581 LYS A CB    1 
ATOM   390   C  CG    . LYS A 1 1581 ? 107.724 186.626 174.924 1.00 124.66 ? 1581 LYS A CG    1 
ATOM   391   C  CD    . LYS A 1 1581 ? 106.665 187.607 175.404 1.00 121.49 ? 1581 LYS A CD    1 
ATOM   392   C  CE    . LYS A 1 1581 ? 105.428 187.562 174.524 1.00 111.98 ? 1581 LYS A CE    1 
ATOM   393   N  NZ    . LYS A 1 1581 ? 104.719 186.257 174.630 1.00 107.89 ? 1581 LYS A NZ    1 
ATOM   394   N  N     . VAL A 1 1582 ? 111.766 187.950 176.707 1.00 137.25 ? 1582 VAL A N     1 
ATOM   395   C  CA    . VAL A 1 1582 ? 112.776 187.871 177.760 1.00 138.63 ? 1582 VAL A CA    1 
ATOM   396   C  C     . VAL A 1 1582 ? 113.331 189.251 178.105 1.00 138.99 ? 1582 VAL A C     1 
ATOM   397   O  O     . VAL A 1 1582 ? 113.712 189.498 179.255 1.00 136.19 ? 1582 VAL A O     1 
ATOM   398   C  CB    . VAL A 1 1582 ? 113.902 186.895 177.364 1.00 134.82 ? 1582 VAL A CB    1 
ATOM   399   C  CG1   . VAL A 1 1582 ? 114.694 187.417 176.174 1.00 131.61 ? 1582 VAL A CG1   1 
ATOM   400   C  CG2   . VAL A 1 1582 ? 114.822 186.623 178.546 1.00 126.52 ? 1582 VAL A CG2   1 
ATOM   401   N  N     . SER A 1 1583 ? 113.381 190.171 177.139 1.00 137.74 ? 1583 SER A N     1 
ATOM   402   C  CA    . SER A 1 1583 ? 113.932 191.496 177.394 1.00 134.06 ? 1583 SER A CA    1 
ATOM   403   C  C     . SER A 1 1583 ? 113.047 192.339 178.300 1.00 137.04 ? 1583 SER A C     1 
ATOM   404   O  O     . SER A 1 1583 ? 113.538 193.302 178.900 1.00 134.62 ? 1583 SER A O     1 
ATOM   405   C  CB    . SER A 1 1583 ? 114.168 192.236 176.076 1.00 124.59 ? 1583 SER A CB    1 
ATOM   406   O  OG    . SER A 1 1583 ? 112.971 192.826 175.600 1.00 122.97 ? 1583 SER A OG    1 
ATOM   407   N  N     . LYS A 1 1584 ? 111.758 192.008 178.407 1.00 137.34 ? 1584 LYS A N     1 
ATOM   408   C  CA    . LYS A 1 1584 ? 110.877 192.745 179.306 1.00 133.63 ? 1584 LYS A CA    1 
ATOM   409   C  C     . LYS A 1 1584 ? 111.286 192.551 180.761 1.00 137.01 ? 1584 LYS A C     1 
ATOM   410   O  O     . LYS A 1 1584 ? 111.240 193.495 181.559 1.00 133.09 ? 1584 LYS A O     1 
ATOM   411   C  CB    . LYS A 1 1584 ? 109.427 192.312 179.089 1.00 130.78 ? 1584 LYS A CB    1 
ATOM   412   C  CG    . LYS A 1 1584 ? 108.794 192.885 177.830 1.00 125.90 ? 1584 LYS A CG    1 
ATOM   413   C  CD    . LYS A 1 1584 ? 107.285 192.708 177.836 1.00 121.22 ? 1584 LYS A CD    1 
ATOM   414   C  CE    . LYS A 1 1584 ? 106.903 191.238 177.864 1.00 122.82 ? 1584 LYS A CE    1 
ATOM   415   N  NZ    . LYS A 1 1584 ? 105.429 191.047 177.782 1.00 119.69 ? 1584 LYS A NZ    1 
ATOM   416   N  N     . SER A 1 1585 ? 111.689 191.334 181.125 1.00 139.57 ? 1585 SER A N     1 
ATOM   417   C  CA    . SER A 1 1585 ? 112.129 191.028 182.483 1.00 138.91 ? 1585 SER A CA    1 
ATOM   418   C  C     . SER A 1 1585 ? 113.614 190.691 182.472 1.00 139.85 ? 1585 SER A C     1 
ATOM   419   O  O     . SER A 1 1585 ? 113.993 189.567 182.107 1.00 135.44 ? 1585 SER A O     1 
ATOM   420   C  CB    . SER A 1 1585 ? 111.319 189.865 183.064 1.00 131.40 ? 1585 SER A CB    1 
ATOM   421   O  OG    . SER A 1 1585 ? 109.932 190.149 183.043 1.00 123.07 ? 1585 SER A OG    1 
ATOM   422   N  N     . PRO A 1 1586 ? 114.499 191.620 182.863 1.00 141.41 ? 1586 PRO A N     1 
ATOM   423   C  CA    . PRO A 1 1586 ? 115.947 191.377 182.839 1.00 140.24 ? 1586 PRO A CA    1 
ATOM   424   C  C     . PRO A 1 1586 ? 116.464 190.628 184.067 1.00 140.62 ? 1586 PRO A C     1 
ATOM   425   O  O     . PRO A 1 1586 ? 117.444 191.031 184.697 1.00 139.31 ? 1586 PRO A O     1 
ATOM   426   C  CB    . PRO A 1 1586 ? 116.522 192.794 182.758 1.00 131.15 ? 1586 PRO A CB    1 
ATOM   427   C  CG    . PRO A 1 1586 ? 115.533 193.627 183.505 1.00 127.54 ? 1586 PRO A CG    1 
ATOM   428   C  CD    . PRO A 1 1586 ? 114.176 192.990 183.301 1.00 134.09 ? 1586 PRO A CD    1 
ATOM   429   N  N     . LEU A 1 1587 ? 115.800 189.527 184.409 1.00 140.49 ? 1587 LEU A N     1 
ATOM   430   C  CA    . LEU A 1 1587 ? 116.179 188.707 185.550 1.00 141.43 ? 1587 LEU A CA    1 
ATOM   431   C  C     . LEU A 1 1587 ? 116.199 187.241 185.146 1.00 142.17 ? 1587 LEU A C     1 
ATOM   432   O  O     . LEU A 1 1587 ? 115.302 186.769 184.441 1.00 140.88 ? 1587 LEU A O     1 
ATOM   433   C  CB    . LEU A 1 1587 ? 115.220 188.914 186.729 1.00 138.10 ? 1587 LEU A CB    1 
ATOM   434   C  CG    . LEU A 1 1587 ? 115.774 188.578 188.115 1.00 132.64 ? 1587 LEU A CG    1 
ATOM   435   C  CD1   . LEU A 1 1587 ? 117.135 189.226 188.322 1.00 128.32 ? 1587 LEU A CD1   1 
ATOM   436   C  CD2   . LEU A 1 1587 ? 114.801 189.007 189.200 1.00 121.06 ? 1587 LEU A CD2   1 
ATOM   437   N  N     . VAL A 1 1588 ? 117.232 186.527 185.596 1.00 143.60 ? 1588 VAL A N     1 
ATOM   438   C  CA    . VAL A 1 1588 ? 117.344 185.103 185.294 1.00 144.06 ? 1588 VAL A CA    1 
ATOM   439   C  C     . VAL A 1 1588 ? 116.240 184.315 185.994 1.00 145.20 ? 1588 VAL A C     1 
ATOM   440   O  O     . VAL A 1 1588 ? 115.645 183.398 185.412 1.00 143.57 ? 1588 VAL A O     1 
ATOM   441   C  CB    . VAL A 1 1588 ? 118.751 184.594 185.666 1.00 135.20 ? 1588 VAL A CB    1 
ATOM   442   C  CG1   . VAL A 1 1588 ? 119.081 184.909 187.119 1.00 131.20 ? 1588 VAL A CG1   1 
ATOM   443   C  CG2   . VAL A 1 1588 ? 118.874 183.103 185.401 1.00 126.12 ? 1588 VAL A CG2   1 
ATOM   444   N  N     . MET A 1 1589 ? 115.940 184.662 187.249 1.00 145.66 ? 1589 MET A N     1 
ATOM   445   C  CA    . MET A 1 1589 ? 114.884 183.967 187.977 1.00 142.90 ? 1589 MET A CA    1 
ATOM   446   C  C     . MET A 1 1589 ? 113.516 184.255 187.373 1.00 142.73 ? 1589 MET A C     1 
ATOM   447   O  O     . MET A 1 1589 ? 112.630 183.392 187.388 1.00 136.84 ? 1589 MET A O     1 
ATOM   448   C  CB    . MET A 1 1589 ? 114.916 184.364 189.453 1.00 138.96 ? 1589 MET A CB    1 
ATOM   449   C  CG    . MET A 1 1589 ? 116.176 183.930 190.186 1.00 139.29 ? 1589 MET A CG    1 
ATOM   450   S  SD    . MET A 1 1589 ? 116.354 182.138 190.266 1.00 150.63 ? 1589 MET A SD    1 
ATOM   451   C  CE    . MET A 1 1589 ? 118.002 181.994 190.954 1.00 122.45 ? 1589 MET A CE    1 
ATOM   452   N  N     . ASP A 1 1590 ? 113.325 185.463 186.839 1.00 145.48 ? 1590 ASP A N     1 
ATOM   453   C  CA    . ASP A 1 1590 ? 112.047 185.823 186.237 1.00 144.26 ? 1590 ASP A CA    1 
ATOM   454   C  C     . ASP A 1 1590 ? 111.782 185.078 184.936 1.00 142.78 ? 1590 ASP A C     1 
ATOM   455   O  O     . ASP A 1 1590 ? 110.627 185.009 184.503 1.00 139.43 ? 1590 ASP A O     1 
ATOM   456   C  CB    . ASP A 1 1590 ? 111.990 187.331 185.988 1.00 138.75 ? 1590 ASP A CB    1 
ATOM   457   C  CG    . ASP A 1 1590 ? 111.675 188.119 187.244 1.00 133.96 ? 1590 ASP A CG    1 
ATOM   458   O  OD1   . ASP A 1 1590 ? 111.712 187.527 188.344 1.00 134.02 ? 1590 ASP A OD1   1 
ATOM   459   O  OD2   . ASP A 1 1590 ? 111.391 189.330 187.133 1.00 128.01 ? 1590 ASP A OD2   1 
ATOM   460   N  N     . VAL A 1 1591 ? 112.814 184.522 184.304 1.00 146.24 ? 1591 VAL A N     1 
ATOM   461   C  CA    . VAL A 1 1591 ? 112.649 183.836 183.031 1.00 143.13 ? 1591 VAL A CA    1 
ATOM   462   C  C     . VAL A 1 1591 ? 112.798 182.323 183.143 1.00 142.52 ? 1591 VAL A C     1 
ATOM   463   O  O     . VAL A 1 1591 ? 112.238 181.602 182.302 1.00 140.08 ? 1591 VAL A O     1 
ATOM   464   C  CB    . VAL A 1 1591 ? 113.616 184.392 181.964 1.00 138.03 ? 1591 VAL A CB    1 
ATOM   465   C  CG1   . VAL A 1 1591 ? 113.439 185.895 181.827 1.00 132.21 ? 1591 VAL A CG1   1 
ATOM   466   C  CG2   . VAL A 1 1591 ? 115.056 184.050 182.309 1.00 133.88 ? 1591 VAL A CG2   1 
ATOM   467   N  N     . LEU A 1 1592 ? 113.526 181.813 184.141 1.00 144.53 ? 1592 LEU A N     1 
ATOM   468   C  CA    . LEU A 1 1592 ? 113.570 180.366 184.338 1.00 141.51 ? 1592 LEU A CA    1 
ATOM   469   C  C     . LEU A 1 1592 ? 112.290 179.824 184.962 1.00 141.03 ? 1592 LEU A C     1 
ATOM   470   O  O     . LEU A 1 1592 ? 112.095 178.604 184.980 1.00 138.36 ? 1592 LEU A O     1 
ATOM   471   C  CB    . LEU A 1 1592 ? 114.779 179.968 185.190 1.00 136.10 ? 1592 LEU A CB    1 
ATOM   472   C  CG    . LEU A 1 1592 ? 116.115 179.730 184.474 1.00 132.56 ? 1592 LEU A CG    1 
ATOM   473   C  CD1   . LEU A 1 1592 ? 115.996 178.529 183.549 1.00 125.58 ? 1592 LEU A CD1   1 
ATOM   474   C  CD2   . LEU A 1 1592 ? 116.584 180.942 183.691 1.00 132.96 ? 1592 LEU A CD2   1 
ATOM   475   N  N     . ASN A 1 1593 ? 111.419 180.693 185.471 1.00 141.59 ? 1593 ASN A N     1 
ATOM   476   C  CA    . ASN A 1 1593 ? 110.124 180.268 185.986 1.00 142.99 ? 1593 ASN A CA    1 
ATOM   477   C  C     . ASN A 1 1593 ? 109.064 180.155 184.898 1.00 143.00 ? 1593 ASN A C     1 
ATOM   478   O  O     . ASN A 1 1593 ? 107.994 179.593 185.152 1.00 141.58 ? 1593 ASN A O     1 
ATOM   479   C  CB    . ASN A 1 1593 ? 109.644 181.239 187.071 1.00 140.14 ? 1593 ASN A CB    1 
ATOM   480   C  CG    . ASN A 1 1593 ? 108.530 180.658 187.923 1.00 137.54 ? 1593 ASN A CG    1 
ATOM   481   O  OD1   . ASN A 1 1593 ? 108.359 179.441 187.996 1.00 139.04 ? 1593 ASN A OD1   1 
ATOM   482   N  ND2   . ASN A 1 1593 ? 107.766 181.529 188.573 1.00 127.77 ? 1593 ASN A ND2   1 
ATOM   483   N  N     . ILE A 1 1594 ? 109.335 180.664 183.700 1.00 142.16 ? 1594 ILE A N     1 
ATOM   484   C  CA    . ILE A 1 1594 ? 108.365 180.627 182.611 1.00 141.40 ? 1594 ILE A CA    1 
ATOM   485   C  C     . ILE A 1 1594 ? 108.436 179.270 181.924 1.00 142.42 ? 1594 ILE A C     1 
ATOM   486   O  O     . ILE A 1 1594 ? 109.512 178.823 181.511 1.00 142.44 ? 1594 ILE A O     1 
ATOM   487   C  CB    . ILE A 1 1594 ? 108.623 181.768 181.615 1.00 136.80 ? 1594 ILE A CB    1 
ATOM   488   C  CG1   . ILE A 1 1594 ? 108.598 183.119 182.334 1.00 130.06 ? 1594 ILE A CG1   1 
ATOM   489   C  CG2   . ILE A 1 1594 ? 107.597 181.737 180.491 1.00 130.98 ? 1594 ILE A CG2   1 
ATOM   490   C  CD1   . ILE A 1 1594 ? 108.803 184.305 181.417 1.00 116.01 ? 1594 ILE A CD1   1 
ATOM   491   N  N     . GLN A 1 1595 ? 107.287 178.611 181.802 1.00 140.78 ? 1595 GLN A N     1 
ATOM   492   C  CA    . GLN A 1 1595 ? 107.223 177.316 181.145 1.00 141.18 ? 1595 GLN A CA    1 
ATOM   493   C  C     . GLN A 1 1595 ? 107.249 177.482 179.628 1.00 142.13 ? 1595 GLN A C     1 
ATOM   494   O  O     . GLN A 1 1595 ? 106.986 178.560 179.087 1.00 141.23 ? 1595 GLN A O     1 
ATOM   495   C  CB    . GLN A 1 1595 ? 105.965 176.557 181.569 1.00 135.94 ? 1595 GLN A CB    1 
ATOM   496   C  CG    . GLN A 1 1595 ? 104.690 177.046 180.902 1.00 132.52 ? 1595 GLN A CG    1 
ATOM   497   C  CD    . GLN A 1 1595 ? 104.028 178.172 181.669 1.00 128.36 ? 1595 GLN A CD    1 
ATOM   498   O  OE1   . GLN A 1 1595 ? 104.235 178.326 182.872 1.00 126.62 ? 1595 GLN A OE1   1 
ATOM   499   N  NE2   . GLN A 1 1595 ? 103.225 178.970 180.973 1.00 123.14 ? 1595 GLN A NE2   1 
ATOM   500   N  N     . GLY A 1 1596 ? 107.576 176.390 178.941 1.00 140.42 ? 1596 GLY A N     1 
ATOM   501   C  CA    . GLY A 1 1596 ? 107.649 176.403 177.496 1.00 134.25 ? 1596 GLY A CA    1 
ATOM   502   C  C     . GLY A 1 1596 ? 108.904 177.017 176.923 1.00 136.48 ? 1596 GLY A C     1 
ATOM   503   O  O     . GLY A 1 1596 ? 108.981 177.204 175.703 1.00 134.11 ? 1596 GLY A O     1 
ATOM   504   N  N     . VAL A 1 1597 ? 109.888 177.340 177.757 1.00 139.52 ? 1597 VAL A N     1 
ATOM   505   C  CA    . VAL A 1 1597 ? 111.120 177.963 177.284 1.00 136.30 ? 1597 VAL A CA    1 
ATOM   506   C  C     . VAL A 1 1597 ? 112.143 176.919 176.857 1.00 136.77 ? 1597 VAL A C     1 
ATOM   507   O  O     . VAL A 1 1597 ? 112.725 177.015 175.774 1.00 135.30 ? 1597 VAL A O     1 
ATOM   508   C  CB    . VAL A 1 1597 ? 111.691 178.898 178.372 1.00 134.43 ? 1597 VAL A CB    1 
ATOM   509   C  CG1   . VAL A 1 1597 ? 113.040 179.453 177.941 1.00 125.46 ? 1597 VAL A CG1   1 
ATOM   510   C  CG2   . VAL A 1 1597 ? 110.714 180.026 178.666 1.00 131.49 ? 1597 VAL A CG2   1 
ATOM   511   N  N     . GLN A 1 1598 ? 112.379 175.905 177.694 1.00 137.60 ? 1598 GLN A N     1 
ATOM   512   C  CA    . GLN A 1 1598 ? 113.411 174.919 177.385 1.00 138.55 ? 1598 GLN A CA    1 
ATOM   513   C  C     . GLN A 1 1598 ? 112.994 174.013 176.231 1.00 138.00 ? 1598 GLN A C     1 
ATOM   514   O  O     . GLN A 1 1598 ? 113.821 173.665 175.379 1.00 137.18 ? 1598 GLN A O     1 
ATOM   515   C  CB    . GLN A 1 1598 ? 113.738 174.093 178.628 1.00 130.66 ? 1598 GLN A CB    1 
ATOM   516   C  CG    . GLN A 1 1598 ? 114.844 173.070 178.417 1.00 132.16 ? 1598 GLN A CG    1 
ATOM   517   C  CD    . GLN A 1 1598 ? 116.206 173.712 178.238 1.00 137.47 ? 1598 GLN A CD    1 
ATOM   518   O  OE1   . GLN A 1 1598 ? 116.764 173.715 177.141 1.00 135.82 ? 1598 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A 1 1598 ? 116.748 174.262 179.318 1.00 136.10 ? 1598 GLN A NE2   1 
ATOM   520   N  N     . ARG A 1 1599 ? 111.721 173.613 176.188 1.00 135.90 ? 1599 ARG A N     1 
ATOM   521   C  CA    . ARG A 1 1599 ? 111.243 172.792 175.080 1.00 134.55 ? 1599 ARG A CA    1 
ATOM   522   C  C     . ARG A 1 1599 ? 111.333 173.546 173.758 1.00 136.39 ? 1599 ARG A C     1 
ATOM   523   O  O     . ARG A 1 1599 ? 111.791 172.997 172.746 1.00 133.78 ? 1599 ARG A O     1 
ATOM   524   C  CB    . ARG A 1 1599 ? 109.809 172.338 175.351 1.00 135.70 ? 1599 ARG A CB    1 
ATOM   525   C  CG    . ARG A 1 1599 ? 109.236 171.397 174.305 1.00 132.49 ? 1599 ARG A CG    1 
ATOM   526   C  CD    . ARG A 1 1599 ? 107.763 171.685 174.045 1.00 129.80 ? 1599 ARG A CD    1 
ATOM   527   N  NE    . ARG A 1 1599 ? 107.439 173.102 174.167 1.00 133.69 ? 1599 ARG A NE    1 
ATOM   528   C  CZ    . ARG A 1 1599 ? 107.711 174.017 173.246 1.00 132.15 ? 1599 ARG A CZ    1 
ATOM   529   N  NH1   . ARG A 1 1599 ? 108.308 173.697 172.109 1.00 132.78 ? 1599 ARG A NH1   1 
ATOM   530   N  NH2   . ARG A 1 1599 ? 107.374 175.283 173.470 1.00 127.02 ? 1599 ARG A NH2   1 
ATOM   531   N  N     . SER A 1 1600 ? 110.914 174.814 173.752 1.00 139.17 ? 1600 SER A N     1 
ATOM   532   C  CA    . SER A 1 1600 ? 111.036 175.629 172.549 1.00 136.62 ? 1600 SER A CA    1 
ATOM   533   C  C     . SER A 1 1600 ? 112.494 175.854 172.174 1.00 136.63 ? 1600 SER A C     1 
ATOM   534   O  O     . SER A 1 1600 ? 112.824 175.896 170.987 1.00 134.50 ? 1600 SER A O     1 
ATOM   535   C  CB    . SER A 1 1600 ? 110.325 176.968 172.743 1.00 133.36 ? 1600 SER A CB    1 
ATOM   536   O  OG    . SER A 1 1600 ? 110.861 177.677 173.846 1.00 133.95 ? 1600 SER A OG    1 
ATOM   537   N  N     . LEU A 1 1601 ? 113.376 175.997 173.165 1.00 137.52 ? 1601 LEU A N     1 
ATOM   538   C  CA    . LEU A 1 1601 ? 114.796 176.166 172.876 1.00 135.91 ? 1601 LEU A CA    1 
ATOM   539   C  C     . LEU A 1 1601 ? 115.386 174.913 172.240 1.00 138.27 ? 1601 LEU A C     1 
ATOM   540   O  O     . LEU A 1 1601 ? 116.184 175.005 171.303 1.00 138.49 ? 1601 LEU A O     1 
ATOM   541   C  CB    . LEU A 1 1601 ? 115.550 176.529 174.154 1.00 133.85 ? 1601 LEU A CB    1 
ATOM   542   C  CG    . LEU A 1 1601 ? 116.990 177.012 173.976 1.00 131.63 ? 1601 LEU A CG    1 
ATOM   543   C  CD1   . LEU A 1 1601 ? 117.034 178.237 173.078 1.00 125.43 ? 1601 LEU A CD1   1 
ATOM   544   C  CD2   . LEU A 1 1601 ? 117.629 177.306 175.326 1.00 130.72 ? 1601 LEU A CD2   1 
ATOM   545   N  N     . GLU A 1 1602 ? 115.008 173.733 172.738 1.00 138.49 ? 1602 GLU A N     1 
ATOM   546   C  CA    . GLU A 1 1602 ? 115.477 172.490 172.128 1.00 136.02 ? 1602 GLU A CA    1 
ATOM   547   C  C     . GLU A 1 1602 ? 114.945 172.339 170.708 1.00 134.95 ? 1602 GLU A C     1 
ATOM   548   O  O     . GLU A 1 1602 ? 115.675 171.915 169.800 1.00 132.08 ? 1602 GLU A O     1 
ATOM   549   C  CB    . GLU A 1 1602 ? 115.065 171.294 172.986 1.00 131.50 ? 1602 GLU A CB    1 
ATOM   550   C  CG    . GLU A 1 1602 ? 115.748 171.231 174.341 1.00 131.97 ? 1602 GLU A CG    1 
ATOM   551   C  CD    . GLU A 1 1602 ? 115.260 170.069 175.185 1.00 131.65 ? 1602 GLU A CD    1 
ATOM   552   O  OE1   . GLU A 1 1602 ? 114.262 169.428 174.795 1.00 132.17 ? 1602 GLU A OE1   1 
ATOM   553   O  OE2   . GLU A 1 1602 ? 115.873 169.798 176.238 1.00 127.22 ? 1602 GLU A OE2   1 
ATOM   554   N  N     . ARG A 1 1603 ? 113.669 172.678 170.497 1.00 135.47 ? 1603 ARG A N     1 
ATOM   555   C  CA    . ARG A 1 1603 ? 113.108 172.627 169.150 1.00 136.16 ? 1603 ARG A CA    1 
ATOM   556   C  C     . ARG A 1 1603 ? 113.834 173.589 168.217 1.00 138.61 ? 1603 ARG A C     1 
ATOM   557   O  O     . ARG A 1 1603 ? 114.124 173.250 167.063 1.00 135.03 ? 1603 ARG A O     1 
ATOM   558   C  CB    . ARG A 1 1603 ? 111.613 172.940 169.195 1.00 133.27 ? 1603 ARG A CB    1 
ATOM   559   C  CG    . ARG A 1 1603 ? 110.979 173.166 167.833 1.00 128.71 ? 1603 ARG A CG    1 
ATOM   560   C  CD    . ARG A 1 1603 ? 109.535 173.618 167.968 1.00 128.57 ? 1603 ARG A CD    1 
ATOM   561   N  NE    . ARG A 1 1603 ? 109.432 174.934 168.587 1.00 128.10 ? 1603 ARG A NE    1 
ATOM   562   C  CZ    . ARG A 1 1603 ? 108.323 175.424 169.123 1.00 125.10 ? 1603 ARG A CZ    1 
ATOM   563   N  NH1   . ARG A 1 1603 ? 107.195 174.734 169.131 1.00 118.79 ? 1603 ARG A NH1   1 
ATOM   564   N  NH2   . ARG A 1 1603 ? 108.346 176.639 169.665 1.00 124.28 ? 1603 ARG A NH2   1 
ATOM   565   N  N     . LEU A 1 1604 ? 114.143 174.794 168.704 1.00 141.30 ? 1604 LEU A N     1 
ATOM   566   C  CA    . LEU A 1 1604 ? 114.873 175.766 167.899 1.00 135.35 ? 1604 LEU A CA    1 
ATOM   567   C  C     . LEU A 1 1604 ? 116.284 175.283 167.593 1.00 134.55 ? 1604 LEU A C     1 
ATOM   568   O  O     . LEU A 1 1604 ? 116.797 175.510 166.495 1.00 133.74 ? 1604 LEU A O     1 
ATOM   569   C  CB    . LEU A 1 1604 ? 114.910 177.116 168.615 1.00 131.01 ? 1604 LEU A CB    1 
ATOM   570   C  CG    . LEU A 1 1604 ? 113.681 178.009 168.435 1.00 129.01 ? 1604 LEU A CG    1 
ATOM   571   C  CD1   . LEU A 1 1604 ? 113.779 179.244 169.318 1.00 116.13 ? 1604 LEU A CD1   1 
ATOM   572   C  CD2   . LEU A 1 1604 ? 113.513 178.401 166.976 1.00 123.00 ? 1604 LEU A CD2   1 
ATOM   573   N  N     . ALA A 1 1605 ? 116.934 174.631 168.560 1.00 136.20 ? 1605 ALA A N     1 
ATOM   574   C  CA    . ALA A 1 1605 ? 118.264 174.082 168.316 1.00 132.20 ? 1605 ALA A CA    1 
ATOM   575   C  C     . ALA A 1 1605 ? 118.225 173.011 167.235 1.00 130.60 ? 1605 ALA A C     1 
ATOM   576   O  O     . ALA A 1 1605 ? 119.079 172.989 166.338 1.00 128.22 ? 1605 ALA A O     1 
ATOM   577   C  CB    . ALA A 1 1605 ? 118.844 173.513 169.611 1.00 128.87 ? 1605 ALA A CB    1 
ATOM   578   N  N     . ASP A 1 1606 ? 117.236 172.116 167.301 1.00 131.59 ? 1606 ASP A N     1 
ATOM   579   C  CA    . ASP A 1 1606 ? 117.098 171.097 166.265 1.00 131.33 ? 1606 ASP A CA    1 
ATOM   580   C  C     . ASP A 1 1606 ? 116.817 171.727 164.906 1.00 132.41 ? 1606 ASP A C     1 
ATOM   581   O  O     . ASP A 1 1606 ? 117.374 171.300 163.887 1.00 129.83 ? 1606 ASP A O     1 
ATOM   582   C  CB    . ASP A 1 1606 ? 115.994 170.109 166.641 1.00 129.25 ? 1606 ASP A CB    1 
ATOM   583   C  CG    . ASP A 1 1606 ? 116.368 169.241 167.827 1.00 124.64 ? 1606 ASP A CG    1 
ATOM   584   O  OD1   . ASP A 1 1606 ? 117.569 168.941 167.991 1.00 117.31 ? 1606 ASP A OD1   1 
ATOM   585   O  OD2   . ASP A 1 1606 ? 115.461 168.859 168.596 1.00 125.81 ? 1606 ASP A OD2   1 
ATOM   586   N  N     . LEU A 1 1607 ? 115.954 172.747 164.871 1.00 133.88 ? 1607 LEU A N     1 
ATOM   587   C  CA    . LEU A 1 1607 ? 115.651 173.423 163.613 1.00 133.19 ? 1607 LEU A CA    1 
ATOM   588   C  C     . LEU A 1 1607 ? 116.886 174.102 163.036 1.00 134.92 ? 1607 LEU A C     1 
ATOM   589   O  O     . LEU A 1 1607 ? 117.129 174.042 161.825 1.00 133.10 ? 1607 LEU A O     1 
ATOM   590   C  CB    . LEU A 1 1607 ? 114.529 174.440 163.825 1.00 131.36 ? 1607 LEU A CB    1 
ATOM   591   C  CG    . LEU A 1 1607 ? 113.107 173.886 163.916 1.00 125.25 ? 1607 LEU A CG    1 
ATOM   592   C  CD1   . LEU A 1 1607 ? 112.126 174.986 164.291 1.00 118.10 ? 1607 LEU A CD1   1 
ATOM   593   C  CD2   . LEU A 1 1607 ? 112.703 173.228 162.606 1.00 111.14 ? 1607 LEU A CD2   1 
ATOM   594   N  N     . LEU A 1 1608 ? 117.672 174.764 163.889 1.00 137.07 ? 1608 LEU A N     1 
ATOM   595   C  CA    . LEU A 1 1608 ? 118.894 175.415 163.430 1.00 135.11 ? 1608 LEU A CA    1 
ATOM   596   C  C     . LEU A 1 1608 ? 119.889 174.397 162.892 1.00 132.73 ? 1608 LEU A C     1 
ATOM   597   O  O     . LEU A 1 1608 ? 120.507 174.617 161.844 1.00 130.35 ? 1608 LEU A O     1 
ATOM   598   C  CB    . LEU A 1 1608 ? 119.515 176.227 164.568 1.00 133.64 ? 1608 LEU A CB    1 
ATOM   599   C  CG    . LEU A 1 1608 ? 119.189 177.723 164.640 1.00 131.53 ? 1608 LEU A CG    1 
ATOM   600   C  CD1   . LEU A 1 1608 ? 119.779 178.451 163.449 1.00 123.77 ? 1608 LEU A CD1   1 
ATOM   601   C  CD2   . LEU A 1 1608 ? 117.691 177.974 164.723 1.00 131.16 ? 1608 LEU A CD2   1 
ATOM   602   N  N     . GLY A 1 1609 ? 120.052 173.271 163.589 1.00 131.10 ? 1609 GLY A N     1 
ATOM   603   C  CA    . GLY A 1 1609 ? 120.933 172.231 163.084 1.00 128.38 ? 1609 GLY A CA    1 
ATOM   604   C  C     . GLY A 1 1609 ? 120.479 171.688 161.743 1.00 127.42 ? 1609 GLY A C     1 
ATOM   605   O  O     . GLY A 1 1609 ? 121.288 171.506 160.829 1.00 127.52 ? 1609 GLY A O     1 
ATOM   606   N  N     . LYS A 1 1610 ? 119.174 171.439 161.601 1.00 126.57 ? 1610 LYS A N     1 
ATOM   607   C  CA    . LYS A 1 1610 ? 118.653 170.910 160.345 1.00 125.62 ? 1610 LYS A CA    1 
ATOM   608   C  C     . LYS A 1 1610 ? 118.830 171.904 159.203 1.00 127.99 ? 1610 LYS A C     1 
ATOM   609   O  O     . LYS A 1 1610 ? 119.226 171.518 158.097 1.00 125.70 ? 1610 LYS A O     1 
ATOM   610   C  CB    . LYS A 1 1610 ? 117.180 170.533 160.506 1.00 121.36 ? 1610 LYS A CB    1 
ATOM   611   C  CG    . LYS A 1 1610 ? 116.516 170.048 159.226 1.00 116.61 ? 1610 LYS A CG    1 
ATOM   612   C  CD    . LYS A 1 1610 ? 115.504 171.059 158.709 1.00 117.29 ? 1610 LYS A CD    1 
ATOM   613   C  CE    . LYS A 1 1610 ? 114.300 171.158 159.632 1.00 117.01 ? 1610 LYS A CE    1 
ATOM   614   N  NZ    . LYS A 1 1610 ? 113.322 172.177 159.163 1.00 105.27 ? 1610 LYS A NZ    1 
ATOM   615   N  N     . ILE A 1 1611 ? 118.546 173.186 159.447 1.00 129.49 ? 1611 ILE A N     1 
ATOM   616   C  CA    . ILE A 1 1611 ? 118.668 174.176 158.381 1.00 127.00 ? 1611 ILE A CA    1 
ATOM   617   C  C     . ILE A 1 1611 ? 120.133 174.398 158.018 1.00 124.91 ? 1611 ILE A C     1 
ATOM   618   O  O     . ILE A 1 1611 ? 120.467 174.610 156.846 1.00 121.70 ? 1611 ILE A O     1 
ATOM   619   C  CB    . ILE A 1 1611 ? 117.953 175.487 158.767 1.00 128.43 ? 1611 ILE A CB    1 
ATOM   620   C  CG1   . ILE A 1 1611 ? 117.824 176.403 157.548 1.00 130.67 ? 1611 ILE A CG1   1 
ATOM   621   C  CG2   . ILE A 1 1611 ? 118.665 176.204 159.894 1.00 127.06 ? 1611 ILE A CG2   1 
ATOM   622   C  CD1   . ILE A 1 1611 ? 116.815 177.518 157.726 1.00 123.46 ? 1611 ILE A CD1   1 
ATOM   623   N  N     . GLN A 1 1612 ? 121.035 174.339 159.004 1.00 125.96 ? 1612 GLN A N     1 
ATOM   624   C  CA    . GLN A 1 1612 ? 122.459 174.444 158.701 1.00 122.22 ? 1612 GLN A CA    1 
ATOM   625   C  C     . GLN A 1 1612 ? 122.932 173.259 157.869 1.00 117.58 ? 1612 GLN A C     1 
ATOM   626   O  O     . GLN A 1 1612 ? 123.704 173.427 156.917 1.00 111.51 ? 1612 GLN A O     1 
ATOM   627   C  CB    . GLN A 1 1612 ? 123.267 174.548 159.995 1.00 121.93 ? 1612 GLN A CB    1 
ATOM   628   C  CG    . GLN A 1 1612 ? 124.762 174.724 159.777 1.00 123.08 ? 1612 GLN A CG    1 
ATOM   629   C  CD    . GLN A 1 1612 ? 125.528 174.871 161.077 1.00 126.04 ? 1612 GLN A CD    1 
ATOM   630   O  OE1   . GLN A 1 1612 ? 126.211 175.871 161.299 1.00 131.63 ? 1612 GLN A OE1   1 
ATOM   631   N  NE2   . GLN A 1 1612 ? 125.421 173.870 161.943 1.00 119.51 ? 1612 GLN A NE2   1 
ATOM   632   N  N     . LYS A 1 1613 ? 122.478 172.050 158.213 1.00 117.01 ? 1613 LYS A N     1 
ATOM   633   C  CA    . LYS A 1 1613 ? 122.833 170.878 157.420 1.00 115.54 ? 1613 LYS A CA    1 
ATOM   634   C  C     . LYS A 1 1613 ? 122.290 170.992 156.001 1.00 116.65 ? 1613 LYS A C     1 
ATOM   635   O  O     . LYS A 1 1613 ? 122.976 170.640 155.034 1.00 115.27 ? 1613 LYS A O     1 
ATOM   636   C  CB    . LYS A 1 1613 ? 122.313 169.611 158.099 1.00 109.88 ? 1613 LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 1613 ? 122.401 168.361 157.239 1.00 105.64 ? 1613 LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 1613 ? 122.809 167.153 158.065 1.00 90.06  ? 1613 LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 1613 ? 123.397 166.059 157.188 1.00 81.51  ? 1613 LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 1613 ? 123.325 164.724 157.844 1.00 69.94  ? 1613 LYS A NZ    1 
ATOM   641   N  N     . ALA A 1 1614 ? 121.057 171.484 155.858 1.00 118.61 ? 1614 ALA A N     1 
ATOM   642   C  CA    . ALA A 1 1614 ? 120.481 171.669 154.529 1.00 115.38 ? 1614 ALA A CA    1 
ATOM   643   C  C     . ALA A 1 1614 ? 121.273 172.689 153.721 1.00 113.05 ? 1614 ALA A C     1 
ATOM   644   O  O     . ALA A 1 1614 ? 121.509 172.493 152.523 1.00 109.13 ? 1614 ALA A O     1 
ATOM   645   C  CB    . ALA A 1 1614 ? 119.018 172.093 154.645 1.00 109.80 ? 1614 ALA A CB    1 
ATOM   646   N  N     . LEU A 1 1615 ? 121.692 173.785 154.359 1.00 115.33 ? 1615 LEU A N     1 
ATOM   647   C  CA    . LEU A 1 1615 ? 122.492 174.787 153.662 1.00 113.26 ? 1615 LEU A CA    1 
ATOM   648   C  C     . LEU A 1 1615 ? 123.842 174.217 153.244 1.00 111.40 ? 1615 LEU A C     1 
ATOM   649   O  O     . LEU A 1 1615 ? 124.340 174.514 152.151 1.00 102.17 ? 1615 LEU A O     1 
ATOM   650   C  CB    . LEU A 1 1615 ? 122.670 176.022 154.547 1.00 106.72 ? 1615 LEU A CB    1 
ATOM   651   C  CG    . LEU A 1 1615 ? 123.204 177.302 153.895 1.00 98.77  ? 1615 LEU A CG    1 
ATOM   652   C  CD1   . LEU A 1 1615 ? 122.569 178.522 154.541 1.00 106.25 ? 1615 LEU A CD1   1 
ATOM   653   C  CD2   . LEU A 1 1615 ? 124.718 177.385 153.994 1.00 99.82  ? 1615 LEU A CD2   1 
ATOM   654   N  N     . GLY A 1 1616 ? 124.452 173.398 154.103 1.00 111.20 ? 1616 GLY A N     1 
ATOM   655   C  CA    . GLY A 1 1616 ? 125.704 172.754 153.733 1.00 105.54 ? 1616 GLY A CA    1 
ATOM   656   C  C     . GLY A 1 1616 ? 125.549 171.807 152.558 1.00 102.64 ? 1616 GLY A C     1 
ATOM   657   O  O     . GLY A 1 1616 ? 126.385 171.784 151.650 1.00 96.60  ? 1616 GLY A O     1 
ATOM   658   N  N     . GLU A 1 1617 ? 124.477 171.011 152.559 1.00 107.24 ? 1617 GLU A N     1 
ATOM   659   C  CA    . GLU A 1 1617 ? 124.222 170.120 151.431 1.00 107.02 ? 1617 GLU A CA    1 
ATOM   660   C  C     . GLU A 1 1617 ? 123.959 170.910 150.154 1.00 99.27  ? 1617 GLU A C     1 
ATOM   661   O  O     . GLU A 1 1617 ? 124.380 170.503 149.066 1.00 90.95  ? 1617 GLU A O     1 
ATOM   662   C  CB    . GLU A 1 1617 ? 123.048 169.191 151.741 1.00 101.47 ? 1617 GLU A CB    1 
ATOM   663   C  CG    . GLU A 1 1617 ? 123.240 168.331 152.978 1.00 105.56 ? 1617 GLU A CG    1 
ATOM   664   C  CD    . GLU A 1 1617 ? 124.664 167.835 153.132 1.00 109.49 ? 1617 GLU A CD    1 
ATOM   665   O  OE1   . GLU A 1 1617 ? 125.095 166.995 152.314 1.00 105.91 ? 1617 GLU A OE1   1 
ATOM   666   O  OE2   . GLU A 1 1617 ? 125.353 168.285 154.072 1.00 112.00 ? 1617 GLU A OE2   1 
ATOM   667   N  N     . TYR A 1 1618 ? 123.258 172.039 150.268 1.00 97.61  ? 1618 TYR A N     1 
ATOM   668   C  CA    . TYR A 1 1618 ? 123.031 172.891 149.105 1.00 99.44  ? 1618 TYR A CA    1 
ATOM   669   C  C     . TYR A 1 1618 ? 124.339 173.460 148.569 1.00 93.80  ? 1618 TYR A C     1 
ATOM   670   O  O     . TYR A 1 1618 ? 124.545 173.521 147.351 1.00 86.81  ? 1618 TYR A O     1 
ATOM   671   C  CB    . TYR A 1 1618 ? 122.064 174.017 149.465 1.00 101.10 ? 1618 TYR A CB    1 
ATOM   672   C  CG    . TYR A 1 1618 ? 122.252 175.269 148.643 1.00 98.54  ? 1618 TYR A CG    1 
ATOM   673   C  CD1   . TYR A 1 1618 ? 121.852 175.318 147.315 1.00 94.58  ? 1618 TYR A CD1   1 
ATOM   674   C  CD2   . TYR A 1 1618 ? 122.825 176.405 149.198 1.00 97.14  ? 1618 TYR A CD2   1 
ATOM   675   C  CE1   . TYR A 1 1618 ? 122.022 176.463 146.561 1.00 98.03  ? 1618 TYR A CE1   1 
ATOM   676   C  CE2   . TYR A 1 1618 ? 122.998 177.553 148.454 1.00 97.93  ? 1618 TYR A CE2   1 
ATOM   677   C  CZ    . TYR A 1 1618 ? 122.593 177.577 147.137 1.00 101.17 ? 1618 TYR A CZ    1 
ATOM   678   O  OH    . TYR A 1 1618 ? 122.764 178.720 146.391 1.00 99.57  ? 1618 TYR A OH    1 
ATOM   679   N  N     . LEU A 1 1619 ? 125.229 173.895 149.463 1.00 90.83  ? 1619 LEU A N     1 
ATOM   680   C  CA    . LEU A 1 1619 ? 126.528 174.394 149.021 1.00 88.70  ? 1619 LEU A CA    1 
ATOM   681   C  C     . LEU A 1 1619 ? 127.329 173.294 148.337 1.00 77.90  ? 1619 LEU A C     1 
ATOM   682   O  O     . LEU A 1 1619 ? 127.970 173.531 147.307 1.00 74.87  ? 1619 LEU A O     1 
ATOM   683   C  CB    . LEU A 1 1619 ? 127.304 174.974 150.203 1.00 87.95  ? 1619 LEU A CB    1 
ATOM   684   C  CG    . LEU A 1 1619 ? 126.849 176.346 150.705 1.00 83.23  ? 1619 LEU A CG    1 
ATOM   685   C  CD1   . LEU A 1 1619 ? 127.677 176.785 151.902 1.00 81.87  ? 1619 LEU A CD1   1 
ATOM   686   C  CD2   . LEU A 1 1619 ? 126.919 177.377 149.592 1.00 78.14  ? 1619 LEU A CD2   1 
ATOM   687   N  N     . GLU A 1 1620 ? 127.289 172.079 148.886 1.00 82.33  ? 1620 GLU A N     1 
ATOM   688   C  CA    . GLU A 1 1620 ? 127.960 170.953 148.244 1.00 79.71  ? 1620 GLU A CA    1 
ATOM   689   C  C     . GLU A 1 1620 ? 127.391 170.682 146.856 1.00 74.63  ? 1620 GLU A C     1 
ATOM   690   O  O     . GLU A 1 1620 ? 128.141 170.465 145.896 1.00 68.79  ? 1620 GLU A O     1 
ATOM   691   C  CB    . GLU A 1 1620 ? 127.831 169.708 149.120 1.00 83.35  ? 1620 GLU A CB    1 
ATOM   692   C  CG    . GLU A 1 1620 ? 128.558 168.491 148.583 1.00 80.25  ? 1620 GLU A CG    1 
ATOM   693   C  CD    . GLU A 1 1620 ? 128.445 167.294 149.501 1.00 86.94  ? 1620 GLU A CD    1 
ATOM   694   O  OE1   . GLU A 1 1620 ? 127.781 167.409 150.552 1.00 91.87  ? 1620 GLU A OE1   1 
ATOM   695   O  OE2   . GLU A 1 1620 ? 129.001 166.230 149.159 1.00 81.06  ? 1620 GLU A OE2   1 
ATOM   696   N  N     . ARG A 1 1621 ? 126.062 170.690 146.735 1.00 80.71  ? 1621 ARG A N     1 
ATOM   697   C  CA    . ARG A 1 1621 ? 125.424 170.406 145.454 1.00 75.55  ? 1621 ARG A CA    1 
ATOM   698   C  C     . ARG A 1 1621 ? 125.751 171.479 144.424 1.00 68.72  ? 1621 ARG A C     1 
ATOM   699   O  O     . ARG A 1 1621 ? 125.967 171.175 143.246 1.00 65.29  ? 1621 ARG A O     1 
ATOM   700   C  CB    . ARG A 1 1621 ? 123.913 170.280 145.645 1.00 81.91  ? 1621 ARG A CB    1 
ATOM   701   C  CG    . ARG A 1 1621 ? 123.456 168.891 146.067 1.00 86.72  ? 1621 ARG A CG    1 
ATOM   702   C  CD    . ARG A 1 1621 ? 121.964 168.705 145.842 1.00 87.72  ? 1621 ARG A CD    1 
ATOM   703   N  NE    . ARG A 1 1621 ? 121.200 169.872 146.267 1.00 97.23  ? 1621 ARG A NE    1 
ATOM   704   C  CZ    . ARG A 1 1621 ? 120.907 170.159 147.528 1.00 98.28  ? 1621 ARG A CZ    1 
ATOM   705   N  NH1   . ARG A 1 1621 ? 121.287 169.373 148.522 1.00 102.09 ? 1621 ARG A NH1   1 
ATOM   706   N  NH2   . ARG A 1 1621 ? 120.211 171.259 147.799 1.00 90.50  ? 1621 ARG A NH2   1 
ATOM   707   N  N     . GLU A 1 1622 ? 125.780 172.744 144.847 1.00 71.84  ? 1622 GLU A N     1 
ATOM   708   C  CA    . GLU A 1 1622 ? 126.113 173.817 143.917 1.00 69.26  ? 1622 GLU A CA    1 
ATOM   709   C  C     . GLU A 1 1622 ? 127.599 173.826 143.586 1.00 61.63  ? 1622 GLU A C     1 
ATOM   710   O  O     . GLU A 1 1622 ? 127.995 174.352 142.541 1.00 62.92  ? 1622 GLU A O     1 
ATOM   711   C  CB    . GLU A 1 1622 ? 125.673 175.165 144.489 1.00 79.34  ? 1622 GLU A CB    1 
ATOM   712   C  CG    . GLU A 1 1622 ? 125.894 176.342 143.553 1.00 84.28  ? 1622 GLU A CG    1 
ATOM   713   C  CD    . GLU A 1 1622 ? 125.386 177.641 144.130 1.00 89.76  ? 1622 GLU A CD    1 
ATOM   714   O  OE1   . GLU A 1 1622 ? 124.876 177.618 145.266 1.00 90.88  ? 1622 GLU A OE1   1 
ATOM   715   O  OE2   . GLU A 1 1622 ? 125.494 178.683 143.450 1.00 87.53  ? 1622 GLU A OE2   1 
ATOM   716   N  N     . ARG A 1 1623 ? 128.436 173.259 144.457 1.00 64.46  ? 1623 ARG A N     1 
ATOM   717   C  CA    . ARG A 1 1623 ? 129.834 173.055 144.095 1.00 52.58  ? 1623 ARG A CA    1 
ATOM   718   C  C     . ARG A 1 1623 ? 129.993 171.889 143.129 1.00 54.39  ? 1623 ARG A C     1 
ATOM   719   O  O     . ARG A 1 1623 ? 130.952 171.859 142.349 1.00 50.78  ? 1623 ARG A O     1 
ATOM   720   C  CB    . ARG A 1 1623 ? 130.679 172.827 145.347 1.00 45.26  ? 1623 ARG A CB    1 
ATOM   721   C  CG    . ARG A 1 1623 ? 130.914 174.077 146.175 1.00 47.67  ? 1623 ARG A CG    1 
ATOM   722   C  CD    . ARG A 1 1623 ? 132.380 174.239 146.530 1.00 38.06  ? 1623 ARG A CD    1 
ATOM   723   N  NE    . ARG A 1 1623 ? 132.629 175.455 147.295 1.00 40.15  ? 1623 ARG A NE    1 
ATOM   724   C  CZ    . ARG A 1 1623 ? 132.467 175.558 148.607 1.00 52.07  ? 1623 ARG A CZ    1 
ATOM   725   N  NH1   . ARG A 1 1623 ? 132.060 174.532 149.336 1.00 56.37  ? 1623 ARG A NH1   1 
ATOM   726   N  NH2   . ARG A 1 1623 ? 132.719 176.720 149.202 1.00 53.61  ? 1623 ARG A NH2   1 
ATOM   727   N  N     . SER A 1 1624 ? 129.073 170.921 143.171 1.00 61.17  ? 1624 SER A N     1 
ATOM   728   C  CA    . SER A 1 1624 ? 129.137 169.796 142.242 1.00 56.56  ? 1624 SER A CA    1 
ATOM   729   C  C     . SER A 1 1624 ? 129.013 170.267 140.798 1.00 56.06  ? 1624 SER A C     1 
ATOM   730   O  O     . SER A 1 1624 ? 129.720 169.774 139.912 1.00 56.43  ? 1624 SER A O     1 
ATOM   731   C  CB    . SER A 1 1624 ? 128.045 168.780 142.573 1.00 59.53  ? 1624 SER A CB    1 
ATOM   732   O  OG    . SER A 1 1624 ? 128.264 168.193 143.844 1.00 55.46  ? 1624 SER A OG    1 
ATOM   733   N  N     . SER A 1 1625 ? 128.114 171.212 140.541 1.00 53.33  ? 1625 SER A N     1 
ATOM   734   C  CA    . SER A 1 1625 ? 128.041 171.880 139.250 1.00 53.81  ? 1625 SER A CA    1 
ATOM   735   C  C     . SER A 1 1625 ? 128.992 173.069 139.246 1.00 51.76  ? 1625 SER A C     1 
ATOM   736   O  O     . SER A 1 1625 ? 129.118 173.774 140.249 1.00 48.16  ? 1625 SER A O     1 
ATOM   737   C  CB    . SER A 1 1625 ? 126.613 172.343 138.958 1.00 49.73  ? 1625 SER A CB    1 
ATOM   738   O  OG    . SER A 1 1625 ? 126.313 173.536 139.659 1.00 51.21  ? 1625 SER A OG    1 
ATOM   739   N  N     . PHE A 1 1626 ? 129.658 173.286 138.111 1.00 51.69  ? 1626 PHE A N     1 
ATOM   740   C  CA    . PHE A 1 1626 ? 130.688 174.315 137.997 1.00 45.34  ? 1626 PHE A CA    1 
ATOM   741   C  C     . PHE A 1 1626 ? 131.712 174.140 139.113 1.00 45.06  ? 1626 PHE A C     1 
ATOM   742   O  O     . PHE A 1 1626 ? 131.716 174.911 140.081 1.00 37.63  ? 1626 PHE A O     1 
ATOM   743   C  CB    . PHE A 1 1626 ? 130.080 175.718 138.043 1.00 42.32  ? 1626 PHE A CB    1 
ATOM   744   C  CG    . PHE A 1 1626 ? 131.055 176.808 137.707 1.00 38.89  ? 1626 PHE A CG    1 
ATOM   745   C  CD1   . PHE A 1 1626 ? 131.563 176.926 136.425 1.00 34.43  ? 1626 PHE A CD1   1 
ATOM   746   C  CD2   . PHE A 1 1626 ? 131.475 177.704 138.674 1.00 34.68  ? 1626 PHE A CD2   1 
ATOM   747   C  CE1   . PHE A 1 1626 ? 132.463 177.925 136.112 1.00 32.15  ? 1626 PHE A CE1   1 
ATOM   748   C  CE2   . PHE A 1 1626 ? 132.375 178.703 138.368 1.00 27.37  ? 1626 PHE A CE2   1 
ATOM   749   C  CZ    . PHE A 1 1626 ? 132.870 178.814 137.086 1.00 28.78  ? 1626 PHE A CZ    1 
ATOM   750   N  N     . PRO A 1 1627 ? 132.583 173.131 139.020 1.00 42.08  ? 1627 PRO A N     1 
ATOM   751   C  CA    . PRO A 1 1627 ? 133.462 172.798 140.155 1.00 38.10  ? 1627 PRO A CA    1 
ATOM   752   C  C     . PRO A 1 1627 ? 134.441 173.896 140.547 1.00 34.90  ? 1627 PRO A C     1 
ATOM   753   O  O     . PRO A 1 1627 ? 135.086 173.764 141.595 1.00 38.68  ? 1627 PRO A O     1 
ATOM   754   C  CB    . PRO A 1 1627 ? 134.206 171.548 139.666 1.00 31.76  ? 1627 PRO A CB    1 
ATOM   755   C  CG    . PRO A 1 1627 ? 133.365 171.006 138.551 1.00 32.14  ? 1627 PRO A CG    1 
ATOM   756   C  CD    . PRO A 1 1627 ? 132.763 172.203 137.893 1.00 33.83  ? 1627 PRO A CD    1 
ATOM   757   N  N     . ARG A 1 1628 ? 134.571 174.966 139.757 1.00 29.44  ? 1628 ARG A N     1 
ATOM   758   C  CA    . ARG A 1 1628 ? 135.510 176.031 140.097 1.00 31.54  ? 1628 ARG A CA    1 
ATOM   759   C  C     . ARG A 1 1628 ? 135.201 176.660 141.449 1.00 36.39  ? 1628 ARG A C     1 
ATOM   760   O  O     . ARG A 1 1628 ? 136.105 177.212 142.087 1.00 39.31  ? 1628 ARG A O     1 
ATOM   761   C  CB    . ARG A 1 1628 ? 135.499 177.108 139.012 1.00 33.52  ? 1628 ARG A CB    1 
ATOM   762   C  CG    . ARG A 1 1628 ? 135.698 176.573 137.607 1.00 32.73  ? 1628 ARG A CG    1 
ATOM   763   C  CD    . ARG A 1 1628 ? 137.163 176.515 137.229 1.00 29.82  ? 1628 ARG A CD    1 
ATOM   764   N  NE    . ARG A 1 1628 ? 137.340 176.248 135.807 1.00 32.40  ? 1628 ARG A NE    1 
ATOM   765   C  CZ    . ARG A 1 1628 ? 138.274 176.805 135.051 1.00 25.50  ? 1628 ARG A CZ    1 
ATOM   766   N  NH1   . ARG A 1 1628 ? 139.150 177.660 135.552 1.00 23.71  ? 1628 ARG A NH1   1 
ATOM   767   N  NH2   . ARG A 1 1628 ? 138.335 176.493 133.760 1.00 24.83  ? 1628 ARG A NH2   1 
ATOM   768   N  N     . PHE A 1 1629 ? 133.952 176.560 141.912 1.00 35.60  ? 1629 PHE A N     1 
ATOM   769   C  CA    . PHE A 1 1629 ? 133.569 177.081 143.217 1.00 37.92  ? 1629 PHE A CA    1 
ATOM   770   C  C     . PHE A 1 1629 ? 134.299 176.389 144.359 1.00 39.91  ? 1629 PHE A C     1 
ATOM   771   O  O     . PHE A 1 1629 ? 134.282 176.901 145.482 1.00 40.38  ? 1629 PHE A O     1 
ATOM   772   C  CB    . PHE A 1 1629 ? 132.059 176.943 143.415 1.00 42.82  ? 1629 PHE A CB    1 
ATOM   773   C  CG    . PHE A 1 1629 ? 131.258 178.016 142.739 1.00 47.06  ? 1629 PHE A CG    1 
ATOM   774   C  CD1   . PHE A 1 1629 ? 131.740 179.310 142.653 1.00 48.96  ? 1629 PHE A CD1   1 
ATOM   775   C  CD2   . PHE A 1 1629 ? 130.021 177.729 142.189 1.00 48.97  ? 1629 PHE A CD2   1 
ATOM   776   C  CE1   . PHE A 1 1629 ? 131.003 180.297 142.031 1.00 51.30  ? 1629 PHE A CE1   1 
ATOM   777   C  CE2   . PHE A 1 1629 ? 129.280 178.710 141.566 1.00 51.79  ? 1629 PHE A CE2   1 
ATOM   778   C  CZ    . PHE A 1 1629 ? 129.771 179.996 141.487 1.00 52.44  ? 1629 PHE A CZ    1 
ATOM   779   N  N     . TYR A 1 1630 ? 134.922 175.237 144.108 1.00 35.99  ? 1630 TYR A N     1 
ATOM   780   C  CA    . TYR A 1 1630 ? 135.757 174.609 145.121 1.00 32.60  ? 1630 TYR A CA    1 
ATOM   781   C  C     . TYR A 1 1630 ? 137.003 175.423 145.443 1.00 28.67  ? 1630 TYR A C     1 
ATOM   782   O  O     . TYR A 1 1630 ? 137.655 175.146 146.455 1.00 28.66  ? 1630 TYR A O     1 
ATOM   783   C  CB    . TYR A 1 1630 ? 136.146 173.202 144.669 1.00 26.72  ? 1630 TYR A CB    1 
ATOM   784   C  CG    . TYR A 1 1630 ? 135.075 172.171 144.935 1.00 32.13  ? 1630 TYR A CG    1 
ATOM   785   C  CD1   . TYR A 1 1630 ? 134.350 171.610 143.894 1.00 35.30  ? 1630 TYR A CD1   1 
ATOM   786   C  CD2   . TYR A 1 1630 ? 134.805 171.742 146.227 1.00 32.72  ? 1630 TYR A CD2   1 
ATOM   787   C  CE1   . TYR A 1 1630 ? 133.368 170.671 144.134 1.00 37.76  ? 1630 TYR A CE1   1 
ATOM   788   C  CE2   . TYR A 1 1630 ? 133.829 170.797 146.475 1.00 36.03  ? 1630 TYR A CE2   1 
ATOM   789   C  CZ    . TYR A 1 1630 ? 133.117 170.263 145.423 1.00 38.41  ? 1630 TYR A CZ    1 
ATOM   790   O  OH    . TYR A 1 1630 ? 132.143 169.321 145.661 1.00 43.97  ? 1630 TYR A OH    1 
ATOM   791   N  N     . PHE A 1 1631 ? 137.344 176.417 144.624 1.00 30.26  ? 1631 PHE A N     1 
ATOM   792   C  CA    . PHE A 1 1631 ? 138.483 177.283 144.898 1.00 34.73  ? 1631 PHE A CA    1 
ATOM   793   C  C     . PHE A 1 1631 ? 138.106 178.551 145.655 1.00 39.92  ? 1631 PHE A C     1 
ATOM   794   O  O     . PHE A 1 1631 ? 138.977 179.396 145.882 1.00 36.47  ? 1631 PHE A O     1 
ATOM   795   C  CB    . PHE A 1 1631 ? 139.197 177.656 143.595 1.00 32.55  ? 1631 PHE A CB    1 
ATOM   796   C  CG    . PHE A 1 1631 ? 139.907 176.505 142.943 1.00 26.06  ? 1631 PHE A CG    1 
ATOM   797   C  CD1   . PHE A 1 1631 ? 140.512 175.525 143.712 1.00 21.27  ? 1631 PHE A CD1   1 
ATOM   798   C  CD2   . PHE A 1 1631 ? 139.982 176.410 141.566 1.00 23.07  ? 1631 PHE A CD2   1 
ATOM   799   C  CE1   . PHE A 1 1631 ? 141.169 174.468 143.119 1.00 16.07  ? 1631 PHE A CE1   1 
ATOM   800   C  CE2   . PHE A 1 1631 ? 140.640 175.355 140.969 1.00 18.45  ? 1631 PHE A CE2   1 
ATOM   801   C  CZ    . PHE A 1 1631 ? 141.233 174.383 141.746 1.00 15.56  ? 1631 PHE A CZ    1 
ATOM   802   N  N     . VAL A 1 1632 ? 136.844 178.708 146.047 1.00 42.84  ? 1632 VAL A N     1 
ATOM   803   C  CA    . VAL A 1 1632 ? 136.417 179.850 146.844 1.00 38.37  ? 1632 VAL A CA    1 
ATOM   804   C  C     . VAL A 1 1632 ? 135.822 179.333 148.146 1.00 43.14  ? 1632 VAL A C     1 
ATOM   805   O  O     . VAL A 1 1632 ? 135.322 178.206 148.220 1.00 43.22  ? 1632 VAL A O     1 
ATOM   806   C  CB    . VAL A 1 1632 ? 135.402 180.747 146.097 1.00 41.79  ? 1632 VAL A CB    1 
ATOM   807   C  CG1   . VAL A 1 1632 ? 136.025 181.327 144.840 1.00 44.03  ? 1632 VAL A CG1   1 
ATOM   808   C  CG2   . VAL A 1 1632 ? 134.138 179.979 145.766 1.00 44.50  ? 1632 VAL A CG2   1 
ATOM   809   N  N     . GLY A 1 1633 ? 135.888 180.166 149.179 1.00 52.89  ? 1633 GLY A N     1 
ATOM   810   C  CA    . GLY A 1 1633 ? 135.375 179.786 150.477 1.00 56.24  ? 1633 GLY A CA    1 
ATOM   811   C  C     . GLY A 1 1633 ? 133.859 179.785 150.523 1.00 62.67  ? 1633 GLY A C     1 
ATOM   812   O  O     . GLY A 1 1633 ? 133.169 180.260 149.621 1.00 66.86  ? 1633 GLY A O     1 
ATOM   813   N  N     . ASP A 1 1634 ? 133.333 179.223 151.615 1.00 67.86  ? 1634 ASP A N     1 
ATOM   814   C  CA    . ASP A 1 1634 ? 131.885 179.144 151.780 1.00 69.52  ? 1634 ASP A CA    1 
ATOM   815   C  C     . ASP A 1 1634 ? 131.260 180.530 151.874 1.00 70.47  ? 1634 ASP A C     1 
ATOM   816   O  O     . ASP A 1 1634 ? 130.214 180.787 151.268 1.00 73.28  ? 1634 ASP A O     1 
ATOM   817   C  CB    . ASP A 1 1634 ? 131.542 178.312 153.015 1.00 71.07  ? 1634 ASP A CB    1 
ATOM   818   C  CG    . ASP A 1 1634 ? 131.943 176.859 152.867 1.00 74.42  ? 1634 ASP A CG    1 
ATOM   819   O  OD1   . ASP A 1 1634 ? 132.380 176.473 151.762 1.00 68.82  ? 1634 ASP A OD1   1 
ATOM   820   O  OD2   . ASP A 1 1634 ? 131.821 176.103 153.853 1.00 73.97  ? 1634 ASP A OD2   1 
ATOM   821   N  N     . GLU A 1 1635 ? 131.883 181.436 152.633 1.00 67.82  ? 1635 GLU A N     1 
ATOM   822   C  CA    . GLU A 1 1635 ? 131.373 182.802 152.707 1.00 71.74  ? 1635 GLU A CA    1 
ATOM   823   C  C     . GLU A 1 1635 ? 131.482 183.502 151.356 1.00 72.27  ? 1635 GLU A C     1 
ATOM   824   O  O     . GLU A 1 1635 ? 130.552 184.202 150.935 1.00 72.85  ? 1635 GLU A O     1 
ATOM   825   C  CB    . GLU A 1 1635 ? 132.107 183.581 153.804 1.00 78.21  ? 1635 GLU A CB    1 
ATOM   826   C  CG    . GLU A 1 1635 ? 133.518 184.057 153.464 1.00 81.53  ? 1635 GLU A CG    1 
ATOM   827   C  CD    . GLU A 1 1635 ? 134.571 182.977 153.641 1.00 81.04  ? 1635 GLU A CD    1 
ATOM   828   O  OE1   . GLU A 1 1635 ? 134.337 181.829 153.208 1.00 78.59  ? 1635 GLU A OE1   1 
ATOM   829   O  OE2   . GLU A 1 1635 ? 135.638 183.279 154.216 1.00 86.00  ? 1635 GLU A OE2   1 
ATOM   830   N  N     . ASP A 1 1636 ? 132.594 183.302 150.647 1.00 70.34  ? 1636 ASP A N     1 
ATOM   831   C  CA    . ASP A 1 1636 ? 132.724 183.866 149.309 1.00 64.38  ? 1636 ASP A CA    1 
ATOM   832   C  C     . ASP A 1 1636 ? 131.705 183.254 148.357 1.00 66.35  ? 1636 ASP A C     1 
ATOM   833   O  O     . ASP A 1 1636 ? 131.076 183.970 147.569 1.00 73.62  ? 1636 ASP A O     1 
ATOM   834   C  CB    . ASP A 1 1636 ? 134.144 183.655 148.787 1.00 64.85  ? 1636 ASP A CB    1 
ATOM   835   C  CG    . ASP A 1 1636 ? 135.094 184.749 149.230 1.00 78.02  ? 1636 ASP A CG    1 
ATOM   836   O  OD1   . ASP A 1 1636 ? 134.925 185.902 148.780 1.00 74.54  ? 1636 ASP A OD1   1 
ATOM   837   O  OD2   . ASP A 1 1636 ? 136.007 184.456 150.030 1.00 82.75  ? 1636 ASP A OD2   1 
ATOM   838   N  N     . LEU A 1 1637 ? 131.527 181.932 148.420 1.00 63.93  ? 1637 LEU A N     1 
ATOM   839   C  CA    . LEU A 1 1637 ? 130.548 181.281 147.558 1.00 67.64  ? 1637 LEU A CA    1 
ATOM   840   C  C     . LEU A 1 1637 ? 129.153 181.833 147.811 1.00 73.99  ? 1637 LEU A C     1 
ATOM   841   O  O     . LEU A 1 1637 ? 128.395 182.082 146.868 1.00 71.54  ? 1637 LEU A O     1 
ATOM   842   C  CB    . LEU A 1 1637 ? 130.581 179.768 147.774 1.00 57.21  ? 1637 LEU A CB    1 
ATOM   843   C  CG    . LEU A 1 1637 ? 129.550 178.940 147.008 1.00 52.67  ? 1637 LEU A CG    1 
ATOM   844   C  CD1   . LEU A 1 1637 ? 129.581 179.279 145.529 1.00 55.81  ? 1637 LEU A CD1   1 
ATOM   845   C  CD2   . LEU A 1 1637 ? 129.792 177.456 147.221 1.00 56.00  ? 1637 LEU A CD2   1 
ATOM   846   N  N     . LEU A 1 1638 ? 128.805 182.053 149.081 1.00 73.74  ? 1638 LEU A N     1 
ATOM   847   C  CA    . LEU A 1 1638 ? 127.521 182.664 149.403 1.00 70.51  ? 1638 LEU A CA    1 
ATOM   848   C  C     . LEU A 1 1638 ? 127.447 184.092 148.879 1.00 69.09  ? 1638 LEU A C     1 
ATOM   849   O  O     . LEU A 1 1638 ? 126.373 184.565 148.491 1.00 72.81  ? 1638 LEU A O     1 
ATOM   850   C  CB    . LEU A 1 1638 ? 127.297 182.625 150.913 1.00 73.34  ? 1638 LEU A CB    1 
ATOM   851   C  CG    . LEU A 1 1638 ? 126.796 181.289 151.466 1.00 73.60  ? 1638 LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1 1638 ? 126.556 181.383 152.960 1.00 83.86  ? 1638 LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1 1638 ? 125.532 180.844 150.748 1.00 79.17  ? 1638 LEU A CD2   1 
ATOM   854   N  N     . GLU A 1 1639 ? 128.581 184.800 148.872 1.00 75.15  ? 1639 GLU A N     1 
ATOM   855   C  CA    . GLU A 1 1639 ? 128.602 186.155 148.329 1.00 72.85  ? 1639 GLU A CA    1 
ATOM   856   C  C     . GLU A 1 1639 ? 128.274 186.163 146.839 1.00 71.21  ? 1639 GLU A C     1 
ATOM   857   O  O     . GLU A 1 1639 ? 127.480 186.989 146.378 1.00 73.98  ? 1639 GLU A O     1 
ATOM   858   C  CB    . GLU A 1 1639 ? 129.963 186.802 148.586 1.00 65.23  ? 1639 GLU A CB    1 
ATOM   859   C  CG    . GLU A 1 1639 ? 130.057 188.248 148.129 1.00 73.49  ? 1639 GLU A CG    1 
ATOM   860   C  CD    . GLU A 1 1639 ? 131.401 188.874 148.444 1.00 77.72  ? 1639 GLU A CD    1 
ATOM   861   O  OE1   . GLU A 1 1639 ? 132.270 188.173 149.002 1.00 75.39  ? 1639 GLU A OE1   1 
ATOM   862   O  OE2   . GLU A 1 1639 ? 131.587 190.070 148.134 1.00 79.42  ? 1639 GLU A OE2   1 
ATOM   863   N  N     . ILE A 1 1640 ? 128.877 185.253 146.067 1.00 72.21  ? 1640 ILE A N     1 
ATOM   864   C  CA    . ILE A 1 1640 ? 128.479 185.137 144.660 1.00 71.12  ? 1640 ILE A CA    1 
ATOM   865   C  C     . ILE A 1 1640 ? 127.031 184.672 144.540 1.00 74.96  ? 1640 ILE A C     1 
ATOM   866   O  O     . ILE A 1 1640 ? 126.298 185.128 143.652 1.00 77.94  ? 1640 ILE A O     1 
ATOM   867   C  CB    . ILE A 1 1640 ? 129.424 184.226 143.834 1.00 69.74  ? 1640 ILE A CB    1 
ATOM   868   C  CG1   . ILE A 1 1640 ? 130.854 184.774 143.741 1.00 63.60  ? 1640 ILE A CG1   1 
ATOM   869   C  CG2   . ILE A 1 1640 ? 128.878 183.996 142.435 1.00 66.31  ? 1640 ILE A CG2   1 
ATOM   870   C  CD1   . ILE A 1 1640 ? 131.785 184.359 144.811 1.00 61.53  ? 1640 ILE A CD1   1 
ATOM   871   N  N     . ILE A 1 1641 ? 126.590 183.781 145.430 1.00 78.41  ? 1641 ILE A N     1 
ATOM   872   C  CA    . ILE A 1 1641 ? 125.235 183.240 145.350 1.00 77.90  ? 1641 ILE A CA    1 
ATOM   873   C  C     . ILE A 1 1641 ? 124.204 184.354 145.490 1.00 80.82  ? 1641 ILE A C     1 
ATOM   874   O  O     . ILE A 1 1641 ? 123.245 184.441 144.713 1.00 79.55  ? 1641 ILE A O     1 
ATOM   875   C  CB    . ILE A 1 1641 ? 125.034 182.155 146.422 1.00 78.87  ? 1641 ILE A CB    1 
ATOM   876   C  CG1   . ILE A 1 1641 ? 125.605 180.819 145.952 1.00 77.50  ? 1641 ILE A CG1   1 
ATOM   877   C  CG2   . ILE A 1 1641 ? 123.561 182.003 146.769 1.00 87.41  ? 1641 ILE A CG2   1 
ATOM   878   C  CD1   . ILE A 1 1641 ? 125.972 179.898 147.091 1.00 79.34  ? 1641 ILE A CD1   1 
ATOM   879   N  N     . GLY A 1 1642 ? 124.388 185.228 146.483 1.00 81.02  ? 1642 GLY A N     1 
ATOM   880   C  CA    . GLY A 1 1642 ? 123.412 186.270 146.744 1.00 84.52  ? 1642 GLY A CA    1 
ATOM   881   C  C     . GLY A 1 1642 ? 123.551 187.505 145.882 1.00 85.85  ? 1642 GLY A C     1 
ATOM   882   O  O     . GLY A 1 1642 ? 122.619 188.313 145.826 1.00 94.51  ? 1642 GLY A O     1 
ATOM   883   N  N     . ASN A 1 1643 ? 124.685 187.670 145.208 1.00 79.40  ? 1643 ASN A N     1 
ATOM   884   C  CA    . ASN A 1 1643 ? 124.943 188.831 144.365 1.00 79.62  ? 1643 ASN A CA    1 
ATOM   885   C  C     . ASN A 1 1643 ? 124.958 188.452 142.887 1.00 77.73  ? 1643 ASN A C     1 
ATOM   886   O  O     . ASN A 1 1643 ? 125.764 188.959 142.107 1.00 83.14  ? 1643 ASN A O     1 
ATOM   887   C  CB    . ASN A 1 1643 ? 126.255 189.507 144.757 1.00 81.73  ? 1643 ASN A CB    1 
ATOM   888   C  CG    . ASN A 1 1643 ? 126.222 190.070 146.166 1.00 82.87  ? 1643 ASN A CG    1 
ATOM   889   O  OD1   . ASN A 1 1643 ? 125.468 190.996 146.461 1.00 86.30  ? 1643 ASN A OD1   1 
ATOM   890   N  ND2   . ASN A 1 1643 ? 127.046 189.510 147.044 1.00 72.88  ? 1643 ASN A ND2   1 
ATOM   891   N  N     . SER A 1 1644 ? 124.065 187.544 142.489 1.00 79.59  ? 1644 SER A N     1 
ATOM   892   C  CA    . SER A 1 1644 ? 123.982 187.165 141.083 1.00 87.81  ? 1644 SER A CA    1 
ATOM   893   C  C     . SER A 1 1644 ? 123.400 188.288 140.232 1.00 90.95  ? 1644 SER A C     1 
ATOM   894   O  O     . SER A 1 1644 ? 123.739 188.405 139.049 1.00 88.04  ? 1644 SER A O     1 
ATOM   895   C  CB    . SER A 1 1644 ? 123.148 185.893 140.930 1.00 80.10  ? 1644 SER A CB    1 
ATOM   896   O  OG    . SER A 1 1644 ? 122.997 185.544 139.565 1.00 77.18  ? 1644 SER A OG    1 
ATOM   897   N  N     . LYS A 1 1645 ? 122.521 189.112 140.810 1.00 86.53  ? 1645 LYS A N     1 
ATOM   898   C  CA    . LYS A 1 1645 ? 121.896 190.187 140.045 1.00 85.53  ? 1645 LYS A CA    1 
ATOM   899   C  C     . LYS A 1 1645 ? 122.920 191.219 139.588 1.00 81.95  ? 1645 LYS A C     1 
ATOM   900   O  O     . LYS A 1 1645 ? 122.901 191.652 138.430 1.00 77.77  ? 1645 LYS A O     1 
ATOM   901   C  CB    . LYS A 1 1645 ? 120.799 190.853 140.875 1.00 92.52  ? 1645 LYS A CB    1 
ATOM   902   C  CG    . LYS A 1 1645 ? 119.430 190.208 140.727 1.00 95.10  ? 1645 LYS A CG    1 
ATOM   903   C  CD    . LYS A 1 1645 ? 118.405 190.871 141.632 1.00 94.39  ? 1645 LYS A CD    1 
ATOM   904   C  CE    . LYS A 1 1645 ? 118.380 192.378 141.431 1.00 92.46  ? 1645 LYS A CE    1 
ATOM   905   N  NZ    . LYS A 1 1645 ? 118.204 192.745 139.999 1.00 92.62  ? 1645 LYS A NZ    1 
ATOM   906   N  N     . ASN A 1 1646 ? 123.822 191.626 140.479 1.00 83.17  ? 1646 ASN A N     1 
ATOM   907   C  CA    . ASN A 1 1646 ? 124.852 192.606 140.158 1.00 80.59  ? 1646 ASN A CA    1 
ATOM   908   C  C     . ASN A 1 1646 ? 126.169 191.884 139.898 1.00 80.11  ? 1646 ASN A C     1 
ATOM   909   O  O     . ASN A 1 1646 ? 126.661 191.144 140.756 1.00 78.96  ? 1646 ASN A O     1 
ATOM   910   C  CB    . ASN A 1 1646 ? 124.999 193.641 141.275 1.00 73.61  ? 1646 ASN A CB    1 
ATOM   911   C  CG    . ASN A 1 1646 ? 125.412 193.027 142.598 1.00 77.07  ? 1646 ASN A CG    1 
ATOM   912   O  OD1   . ASN A 1 1646 ? 125.085 191.879 142.893 1.00 85.16  ? 1646 ASN A OD1   1 
ATOM   913   N  ND2   . ASN A 1 1646 ? 126.138 193.793 143.403 1.00 73.58  ? 1646 ASN A ND2   1 
ATOM   914   N  N     . VAL A 1 1647 ? 126.736 192.098 138.706 1.00 80.74  ? 1647 VAL A N     1 
ATOM   915   C  CA    . VAL A 1 1647 ? 127.954 191.405 138.304 1.00 77.19  ? 1647 VAL A CA    1 
ATOM   916   C  C     . VAL A 1 1647 ? 129.215 192.170 138.672 1.00 74.72  ? 1647 VAL A C     1 
ATOM   917   O  O     . VAL A 1 1647 ? 130.322 191.643 138.490 1.00 70.96  ? 1647 VAL A O     1 
ATOM   918   C  CB    . VAL A 1 1647 ? 127.939 191.132 136.788 1.00 74.44  ? 1647 VAL A CB    1 
ATOM   919   C  CG1   . VAL A 1 1647 ? 126.823 190.162 136.439 1.00 72.19  ? 1647 VAL A CG1   1 
ATOM   920   C  CG2   . VAL A 1 1647 ? 127.769 192.435 136.034 1.00 72.14  ? 1647 VAL A CG2   1 
ATOM   921   N  N     . ALA A 1 1648 ? 129.088 193.400 139.174 1.00 73.73  ? 1648 ALA A N     1 
ATOM   922   C  CA    . ALA A 1 1648 ? 130.268 194.177 139.538 1.00 71.06  ? 1648 ALA A CA    1 
ATOM   923   C  C     . ALA A 1 1648 ? 130.998 193.559 140.724 1.00 66.79  ? 1648 ALA A C     1 
ATOM   924   O  O     . ALA A 1 1648 ? 132.234 193.552 140.764 1.00 63.93  ? 1648 ALA A O     1 
ATOM   925   C  CB    . ALA A 1 1648 ? 129.873 195.621 139.844 1.00 69.01  ? 1648 ALA A CB    1 
ATOM   926   N  N     . LYS A 1 1649 ? 130.253 193.041 141.703 1.00 66.76  ? 1649 LYS A N     1 
ATOM   927   C  CA    . LYS A 1 1649 ? 130.881 192.469 142.890 1.00 69.03  ? 1649 LYS A CA    1 
ATOM   928   C  C     . LYS A 1 1649 ? 131.588 191.156 142.582 1.00 67.51  ? 1649 LYS A C     1 
ATOM   929   O  O     . LYS A 1 1649 ? 132.507 190.763 143.310 1.00 62.99  ? 1649 LYS A O     1 
ATOM   930   C  CB    . LYS A 1 1649 ? 129.839 192.259 143.988 1.00 68.97  ? 1649 LYS A CB    1 
ATOM   931   C  CG    . LYS A 1 1649 ? 129.608 193.474 144.868 1.00 68.74  ? 1649 LYS A CG    1 
ATOM   932   C  CD    . LYS A 1 1649 ? 129.019 193.074 146.210 1.00 75.35  ? 1649 LYS A CD    1 
ATOM   933   C  CE    . LYS A 1 1649 ? 128.319 194.245 146.879 1.00 77.54  ? 1649 LYS A CE    1 
ATOM   934   N  NZ    . LYS A 1 1649 ? 129.193 194.916 147.879 1.00 71.92  ? 1649 LYS A NZ    1 
ATOM   935   N  N     . LEU A 1 1650 ? 131.179 190.467 141.518 1.00 67.08  ? 1650 LEU A N     1 
ATOM   936   C  CA    . LEU A 1 1650 ? 131.752 189.172 141.178 1.00 63.88  ? 1650 LEU A CA    1 
ATOM   937   C  C     . LEU A 1 1650 ? 133.099 189.277 140.477 1.00 59.25  ? 1650 LEU A C     1 
ATOM   938   O  O     . LEU A 1 1650 ? 133.774 188.254 140.319 1.00 59.89  ? 1650 LEU A O     1 
ATOM   939   C  CB    . LEU A 1 1650 ? 130.783 188.387 140.292 1.00 58.99  ? 1650 LEU A CB    1 
ATOM   940   C  CG    . LEU A 1 1650 ? 129.872 187.372 140.981 1.00 62.20  ? 1650 LEU A CG    1 
ATOM   941   C  CD1   . LEU A 1 1650 ? 129.057 188.025 142.086 1.00 65.71  ? 1650 LEU A CD1   1 
ATOM   942   C  CD2   . LEU A 1 1650 ? 128.963 186.725 139.957 1.00 62.14  ? 1650 LEU A CD2   1 
ATOM   943   N  N     . GLN A 1 1651 ? 133.506 190.476 140.060 1.00 56.44  ? 1651 GLN A N     1 
ATOM   944   C  CA    . GLN A 1 1651 ? 134.713 190.623 139.256 1.00 56.20  ? 1651 GLN A CA    1 
ATOM   945   C  C     . GLN A 1 1651 ? 135.993 190.377 140.043 1.00 55.29  ? 1651 GLN A C     1 
ATOM   946   O  O     . GLN A 1 1651 ? 137.060 190.270 139.429 1.00 62.66  ? 1651 GLN A O     1 
ATOM   947   C  CB    . GLN A 1 1651 ? 134.751 192.016 138.625 1.00 49.04  ? 1651 GLN A CB    1 
ATOM   948   C  CG    . GLN A 1 1651 ? 133.591 192.296 137.682 1.00 52.65  ? 1651 GLN A CG    1 
ATOM   949   C  CD    . GLN A 1 1651 ? 133.946 192.051 136.229 1.00 44.70  ? 1651 GLN A CD    1 
ATOM   950   O  OE1   . GLN A 1 1651 ? 134.844 191.270 135.923 1.00 47.62  ? 1651 GLN A OE1   1 
ATOM   951   N  NE2   . GLN A 1 1651 ? 133.238 192.717 135.325 1.00 42.78  ? 1651 GLN A NE2   1 
ATOM   952   N  N     . LYS A 1 1652 ? 135.923 190.290 141.369 1.00 52.92  ? 1652 LYS A N     1 
ATOM   953   C  CA    . LYS A 1 1652 ? 137.102 190.032 142.186 1.00 53.83  ? 1652 LYS A CA    1 
ATOM   954   C  C     . LYS A 1 1652 ? 137.310 188.554 142.482 1.00 53.72  ? 1652 LYS A C     1 
ATOM   955   O  O     . LYS A 1 1652 ? 138.305 188.201 143.122 1.00 53.97  ? 1652 LYS A O     1 
ATOM   956   C  CB    . LYS A 1 1652 ? 137.015 190.809 143.503 1.00 52.69  ? 1652 LYS A CB    1 
ATOM   957   C  CG    . LYS A 1 1652 ? 135.877 190.375 144.409 1.00 50.21  ? 1652 LYS A CG    1 
ATOM   958   C  CD    . LYS A 1 1652 ? 135.871 191.172 145.700 1.00 47.33  ? 1652 LYS A CD    1 
ATOM   959   C  CE    . LYS A 1 1652 ? 135.392 192.595 145.468 1.00 59.12  ? 1652 LYS A CE    1 
ATOM   960   N  NZ    . LYS A 1 1652 ? 135.255 193.350 146.744 1.00 62.18  ? 1652 LYS A NZ    1 
ATOM   961   N  N     . HIS A 1 1653 ? 136.408 187.685 142.033 1.00 53.09  ? 1653 HIS A N     1 
ATOM   962   C  CA    . HIS A 1 1653 ? 136.488 186.260 142.318 1.00 49.26  ? 1653 HIS A CA    1 
ATOM   963   C  C     . HIS A 1 1653 ? 137.010 185.443 141.144 1.00 39.60  ? 1653 HIS A C     1 
ATOM   964   O  O     . HIS A 1 1653 ? 137.321 184.262 141.321 1.00 40.01  ? 1653 HIS A O     1 
ATOM   965   C  CB    . HIS A 1 1653 ? 135.115 185.734 142.742 1.00 50.38  ? 1653 HIS A CB    1 
ATOM   966   C  CG    . HIS A 1 1653 ? 134.525 186.463 143.908 1.00 57.34  ? 1653 HIS A CG    1 
ATOM   967   N  ND1   . HIS A 1 1653 ? 135.099 186.450 145.161 1.00 52.02  ? 1653 HIS A ND1   1 
ATOM   968   C  CD2   . HIS A 1 1653 ? 133.419 187.237 144.009 1.00 63.14  ? 1653 HIS A CD2   1 
ATOM   969   C  CE1   . HIS A 1 1653 ? 134.367 187.177 145.986 1.00 58.82  ? 1653 HIS A CE1   1 
ATOM   970   N  NE2   . HIS A 1 1653 ? 133.341 187.665 145.312 1.00 60.94  ? 1653 HIS A NE2   1 
ATOM   971   N  N     . PHE A 1 1654 ? 137.116 186.037 139.956 1.00 41.91  ? 1654 PHE A N     1 
ATOM   972   C  CA    . PHE A 1 1654 ? 137.595 185.300 138.795 1.00 39.82  ? 1654 PHE A CA    1 
ATOM   973   C  C     . PHE A 1 1654 ? 139.092 185.029 138.838 1.00 38.45  ? 1654 PHE A C     1 
ATOM   974   O  O     . PHE A 1 1654 ? 139.553 184.085 138.188 1.00 37.97  ? 1654 PHE A O     1 
ATOM   975   C  CB    . PHE A 1 1654 ? 137.236 186.053 137.514 1.00 38.40  ? 1654 PHE A CB    1 
ATOM   976   C  CG    . PHE A 1 1654 ? 135.762 186.109 137.246 1.00 39.46  ? 1654 PHE A CG    1 
ATOM   977   C  CD1   . PHE A 1 1654 ? 135.098 185.003 136.745 1.00 37.80  ? 1654 PHE A CD1   1 
ATOM   978   C  CD2   . PHE A 1 1654 ? 135.037 187.256 137.514 1.00 38.91  ? 1654 PHE A CD2   1 
ATOM   979   C  CE1   . PHE A 1 1654 ? 133.742 185.044 136.501 1.00 31.86  ? 1654 PHE A CE1   1 
ATOM   980   C  CE2   . PHE A 1 1654 ? 133.680 187.301 137.274 1.00 40.45  ? 1654 PHE A CE2   1 
ATOM   981   C  CZ    . PHE A 1 1654 ? 133.032 186.193 136.768 1.00 34.47  ? 1654 PHE A CZ    1 
ATOM   982   N  N     . LYS A 1 1655 ? 139.859 185.828 139.583 1.00 43.30  ? 1655 LYS A N     1 
ATOM   983   C  CA    . LYS A 1 1655 ? 141.293 185.581 139.678 1.00 35.62  ? 1655 LYS A CA    1 
ATOM   984   C  C     . LYS A 1 1655 ? 141.593 184.285 140.420 1.00 37.68  ? 1655 LYS A C     1 
ATOM   985   O  O     . LYS A 1 1655 ? 142.617 183.646 140.155 1.00 46.91  ? 1655 LYS A O     1 
ATOM   986   C  CB    . LYS A 1 1655 ? 141.991 186.760 140.357 1.00 29.44  ? 1655 LYS A CB    1 
ATOM   987   C  CG    . LYS A 1 1655 ? 141.475 187.078 141.749 1.00 43.15  ? 1655 LYS A CG    1 
ATOM   988   C  CD    . LYS A 1 1655 ? 142.232 188.245 142.365 1.00 45.67  ? 1655 LYS A CD    1 
ATOM   989   C  CE    . LYS A 1 1655 ? 141.629 188.650 143.700 1.00 46.93  ? 1655 LYS A CE    1 
ATOM   990   N  NZ    . LYS A 1 1655 ? 141.738 187.568 144.717 1.00 49.85  ? 1655 LYS A NZ    1 
ATOM   991   N  N     . LYS A 1 1656 ? 140.725 183.883 141.346 1.00 32.87  ? 1656 LYS A N     1 
ATOM   992   C  CA    . LYS A 1 1656 ? 140.921 182.659 142.109 1.00 34.05  ? 1656 LYS A CA    1 
ATOM   993   C  C     . LYS A 1 1656 ? 140.138 181.475 141.556 1.00 34.98  ? 1656 LYS A C     1 
ATOM   994   O  O     . LYS A 1 1656 ? 140.271 180.367 142.082 1.00 40.23  ? 1656 LYS A O     1 
ATOM   995   C  CB    . LYS A 1 1656 ? 140.553 182.887 143.578 1.00 45.31  ? 1656 LYS A CB    1 
ATOM   996   C  CG    . LYS A 1 1656 ? 139.123 183.333 143.811 1.00 44.10  ? 1656 LYS A CG    1 
ATOM   997   C  CD    . LYS A 1 1656 ? 138.844 183.508 145.293 1.00 42.90  ? 1656 LYS A CD    1 
ATOM   998   C  CE    . LYS A 1 1656 ? 137.858 184.634 145.543 1.00 49.25  ? 1656 LYS A CE    1 
ATOM   999   N  NZ    . LYS A 1 1656 ? 138.501 185.972 145.436 1.00 48.65  ? 1656 LYS A NZ    1 
ATOM   1000  N  N     . MET A 1 1657 ? 139.331 181.675 140.513 1.00 35.82  ? 1657 MET A N     1 
ATOM   1001  C  CA    . MET A 1 1657 ? 138.644 180.575 139.852 1.00 28.73  ? 1657 MET A CA    1 
ATOM   1002  C  C     . MET A 1 1657 ? 139.182 180.271 138.463 1.00 28.79  ? 1657 MET A C     1 
ATOM   1003  O  O     . MET A 1 1657 ? 138.790 179.255 137.878 1.00 33.41  ? 1657 MET A O     1 
ATOM   1004  C  CB    . MET A 1 1657 ? 137.136 180.854 139.743 1.00 31.74  ? 1657 MET A CB    1 
ATOM   1005  C  CG    . MET A 1 1657 ? 136.398 180.898 141.067 1.00 39.00  ? 1657 MET A CG    1 
ATOM   1006  S  SD    . MET A 1 1657 ? 134.628 181.162 140.843 1.00 48.82  ? 1657 MET A SD    1 
ATOM   1007  C  CE    . MET A 1 1657 ? 134.582 182.893 140.397 1.00 52.33  ? 1657 MET A CE    1 
ATOM   1008  N  N     . PHE A 1 1658 ? 140.054 181.115 137.917 1.00 29.68  ? 1658 PHE A N     1 
ATOM   1009  C  CA    . PHE A 1 1658 ? 140.589 180.918 136.579 1.00 22.25  ? 1658 PHE A CA    1 
ATOM   1010  C  C     . PHE A 1 1658 ? 142.074 181.245 136.568 1.00 23.85  ? 1658 PHE A C     1 
ATOM   1011  O  O     . PHE A 1 1658 ? 142.560 182.027 137.389 1.00 23.19  ? 1658 PHE A O     1 
ATOM   1012  C  CB    . PHE A 1 1658 ? 139.851 181.777 135.545 1.00 24.33  ? 1658 PHE A CB    1 
ATOM   1013  C  CG    . PHE A 1 1658 ? 138.417 181.379 135.335 1.00 24.12  ? 1658 PHE A CG    1 
ATOM   1014  C  CD1   . PHE A 1 1658 ? 137.411 181.924 136.114 1.00 26.53  ? 1658 PHE A CD1   1 
ATOM   1015  C  CD2   . PHE A 1 1658 ? 138.076 180.464 134.355 1.00 24.93  ? 1658 PHE A CD2   1 
ATOM   1016  C  CE1   . PHE A 1 1658 ? 136.093 181.560 135.921 1.00 27.71  ? 1658 PHE A CE1   1 
ATOM   1017  C  CE2   . PHE A 1 1658 ? 136.760 180.096 134.158 1.00 25.62  ? 1658 PHE A CE2   1 
ATOM   1018  C  CZ    . PHE A 1 1658 ? 135.767 180.645 134.942 1.00 27.82  ? 1658 PHE A CZ    1 
ATOM   1019  N  N     . ALA A 1 1659 ? 142.790 180.635 135.619 1.00 29.28  ? 1659 ALA A N     1 
ATOM   1020  C  CA    . ALA A 1 1659 ? 144.236 180.814 135.541 1.00 19.72  ? 1659 ALA A CA    1 
ATOM   1021  C  C     . ALA A 1 1659 ? 144.605 182.245 135.174 1.00 25.35  ? 1659 ALA A C     1 
ATOM   1022  O  O     . ALA A 1 1659 ? 145.437 182.872 135.839 1.00 37.15  ? 1659 ALA A O     1 
ATOM   1023  C  CB    . ALA A 1 1659 ? 144.830 179.835 134.529 1.00 16.27  ? 1659 ALA A CB    1 
ATOM   1024  N  N     . GLY A 1 1660 ? 143.998 182.779 134.118 1.00 20.26  ? 1660 GLY A N     1 
ATOM   1025  C  CA    . GLY A 1 1660 ? 144.380 184.088 133.631 1.00 18.96  ? 1660 GLY A CA    1 
ATOM   1026  C  C     . GLY A 1 1660 ? 143.225 185.044 133.431 1.00 28.58  ? 1660 GLY A C     1 
ATOM   1027  O  O     . GLY A 1 1660 ? 143.423 186.168 132.960 1.00 34.52  ? 1660 GLY A O     1 
ATOM   1028  N  N     . VAL A 1 1661 ? 142.014 184.618 133.777 1.00 28.45  ? 1661 VAL A N     1 
ATOM   1029  C  CA    . VAL A 1 1661 ? 140.843 185.482 133.668 1.00 29.18  ? 1661 VAL A CA    1 
ATOM   1030  C  C     . VAL A 1 1661 ? 140.788 186.357 134.915 1.00 33.64  ? 1661 VAL A C     1 
ATOM   1031  O  O     . VAL A 1 1661 ? 140.506 185.874 136.013 1.00 37.29  ? 1661 VAL A O     1 
ATOM   1032  C  CB    . VAL A 1 1661 ? 139.553 184.673 133.500 1.00 30.08  ? 1661 VAL A CB    1 
ATOM   1033  C  CG1   . VAL A 1 1661 ? 138.343 185.592 133.544 1.00 27.97  ? 1661 VAL A CG1   1 
ATOM   1034  C  CG2   . VAL A 1 1661 ? 139.585 183.893 132.199 1.00 24.96  ? 1661 VAL A CG2   1 
ATOM   1035  N  N     . SER A 1 1662 ? 141.071 187.647 134.747 1.00 32.75  ? 1662 SER A N     1 
ATOM   1036  C  CA    . SER A 1 1662 ? 141.006 188.590 135.854 1.00 31.98  ? 1662 SER A CA    1 
ATOM   1037  C  C     . SER A 1 1662 ? 139.656 189.284 135.946 1.00 39.66  ? 1662 SER A C     1 
ATOM   1038  O  O     . SER A 1 1662 ? 139.197 189.586 137.054 1.00 47.66  ? 1662 SER A O     1 
ATOM   1039  C  CB    . SER A 1 1662 ? 142.115 189.637 135.721 1.00 33.55  ? 1662 SER A CB    1 
ATOM   1040  O  OG    . SER A 1 1662 ? 142.142 190.499 136.845 1.00 40.60  ? 1662 SER A OG    1 
ATOM   1041  N  N     . SER A 1 1663 ? 139.011 189.537 134.810 1.00 37.23  ? 1663 SER A N     1 
ATOM   1042  C  CA    . SER A 1 1663 ? 137.707 190.180 134.790 1.00 33.34  ? 1663 SER A CA    1 
ATOM   1043  C  C     . SER A 1 1663 ? 136.940 189.699 133.569 1.00 32.09  ? 1663 SER A C     1 
ATOM   1044  O  O     . SER A 1 1663 ? 137.522 189.217 132.595 1.00 34.91  ? 1663 SER A O     1 
ATOM   1045  C  CB    . SER A 1 1663 ? 137.833 191.707 134.779 1.00 35.46  ? 1663 SER A CB    1 
ATOM   1046  O  OG    . SER A 1 1663 ? 138.501 192.154 133.612 1.00 32.41  ? 1663 SER A OG    1 
ATOM   1047  N  N     . ILE A 1 1664 ? 135.619 189.837 133.632 1.00 36.82  ? 1664 ILE A N     1 
ATOM   1048  C  CA    . ILE A 1 1664 ? 134.729 189.450 132.545 1.00 36.86  ? 1664 ILE A CA    1 
ATOM   1049  C  C     . ILE A 1 1664 ? 134.175 190.716 131.906 1.00 36.45  ? 1664 ILE A C     1 
ATOM   1050  O  O     . ILE A 1 1664 ? 133.679 191.609 132.603 1.00 44.75  ? 1664 ILE A O     1 
ATOM   1051  C  CB    . ILE A 1 1664 ? 133.600 188.526 133.035 1.00 30.58  ? 1664 ILE A CB    1 
ATOM   1052  C  CG1   . ILE A 1 1664 ? 132.931 189.095 134.287 1.00 30.26  ? 1664 ILE A CG1   1 
ATOM   1053  C  CG2   . ILE A 1 1664 ? 134.136 187.131 133.306 1.00 24.87  ? 1664 ILE A CG2   1 
ATOM   1054  C  CD1   . ILE A 1 1664 ? 131.584 188.477 134.590 1.00 36.13  ? 1664 ILE A CD1   1 
ATOM   1055  N  N     . ILE A 1 1665 ? 134.279 190.799 130.585 1.00 31.62  ? 1665 ILE A N     1 
ATOM   1056  C  CA    . ILE A 1 1665 ? 133.817 191.971 129.851 1.00 39.49  ? 1665 ILE A CA    1 
ATOM   1057  C  C     . ILE A 1 1665 ? 132.317 191.853 129.625 1.00 45.96  ? 1665 ILE A C     1 
ATOM   1058  O  O     . ILE A 1 1665 ? 131.828 190.819 129.160 1.00 41.55  ? 1665 ILE A O     1 
ATOM   1059  C  CB    . ILE A 1 1665 ? 134.570 192.109 128.518 1.00 35.47  ? 1665 ILE A CB    1 
ATOM   1060  C  CG1   . ILE A 1 1665 ? 136.078 192.220 128.758 1.00 32.27  ? 1665 ILE A CG1   1 
ATOM   1061  C  CG2   . ILE A 1 1665 ? 134.063 193.312 127.741 1.00 36.64  ? 1665 ILE A CG2   1 
ATOM   1062  C  CD1   . ILE A 1 1665 ? 136.460 193.219 129.827 1.00 34.52  ? 1665 ILE A CD1   1 
ATOM   1063  N  N     . LEU A 1 1666 ? 131.580 192.907 129.968 1.00 52.64  ? 1666 LEU A N     1 
ATOM   1064  C  CA    . LEU A 1 1666 ? 130.142 192.953 129.751 1.00 49.84  ? 1666 LEU A CA    1 
ATOM   1065  C  C     . LEU A 1 1666 ? 129.764 194.262 129.075 1.00 59.11  ? 1666 LEU A C     1 
ATOM   1066  O  O     . LEU A 1 1666 ? 130.498 195.252 129.128 1.00 61.58  ? 1666 LEU A O     1 
ATOM   1067  C  CB    . LEU A 1 1666 ? 129.346 192.803 131.058 1.00 51.36  ? 1666 LEU A CB    1 
ATOM   1068  C  CG    . LEU A 1 1666 ? 129.189 191.401 131.655 1.00 53.99  ? 1666 LEU A CG    1 
ATOM   1069  C  CD1   . LEU A 1 1666 ? 130.481 190.905 132.269 1.00 47.64  ? 1666 LEU A CD1   1 
ATOM   1070  C  CD2   . LEU A 1 1666 ? 128.058 191.359 132.665 1.00 58.43  ? 1666 LEU A CD2   1 
ATOM   1071  N  N     . ASN A 1 1667 ? 128.597 194.251 128.437 1.00 59.14  ? 1667 ASN A N     1 
ATOM   1072  C  CA    . ASN A 1 1667 ? 128.086 195.432 127.762 1.00 59.51  ? 1667 ASN A CA    1 
ATOM   1073  C  C     . ASN A 1 1667 ? 127.543 196.431 128.785 1.00 70.10  ? 1667 ASN A C     1 
ATOM   1074  O  O     . ASN A 1 1667 ? 127.664 196.255 130.001 1.00 67.66  ? 1667 ASN A O     1 
ATOM   1075  C  CB    . ASN A 1 1667 ? 127.011 195.038 126.754 1.00 57.30  ? 1667 ASN A CB    1 
ATOM   1076  C  CG    . ASN A 1 1667 ? 125.877 194.258 127.389 1.00 60.08  ? 1667 ASN A CG    1 
ATOM   1077  O  OD1   . ASN A 1 1667 ? 126.046 193.642 128.440 1.00 56.17  ? 1667 ASN A OD1   1 
ATOM   1078  N  ND2   . ASN A 1 1667 ? 124.715 194.277 126.749 1.00 64.19  ? 1667 ASN A ND2   1 
ATOM   1079  N  N     . GLU A 1 1668 ? 126.934 197.505 128.275 1.00 73.52  ? 1668 GLU A N     1 
ATOM   1080  C  CA    . GLU A 1 1668 ? 126.419 198.550 129.152 1.00 72.49  ? 1668 GLU A CA    1 
ATOM   1081  C  C     . GLU A 1 1668 ? 125.241 198.062 129.987 1.00 71.49  ? 1668 GLU A C     1 
ATOM   1082  O  O     . GLU A 1 1668 ? 124.988 198.595 131.073 1.00 73.08  ? 1668 GLU A O     1 
ATOM   1083  C  CB    . GLU A 1 1668 ? 126.017 199.772 128.328 1.00 67.64  ? 1668 GLU A CB    1 
ATOM   1084  C  CG    . GLU A 1 1668 ? 125.301 199.435 127.032 1.00 76.27  ? 1668 GLU A CG    1 
ATOM   1085  C  CD    . GLU A 1 1668 ? 124.824 200.668 126.292 1.00 84.76  ? 1668 GLU A CD    1 
ATOM   1086  O  OE1   . GLU A 1 1668 ? 124.881 201.772 126.874 1.00 89.17  ? 1668 GLU A OE1   1 
ATOM   1087  O  OE2   . GLU A 1 1668 ? 124.392 200.534 125.128 1.00 82.67  ? 1668 GLU A OE2   1 
ATOM   1088  N  N     . ASP A 1 1669 ? 124.513 197.057 129.503 1.00 66.03  ? 1669 ASP A N     1 
ATOM   1089  C  CA    . ASP A 1 1669 ? 123.367 196.528 130.229 1.00 70.22  ? 1669 ASP A CA    1 
ATOM   1090  C  C     . ASP A 1 1669 ? 123.758 195.559 131.337 1.00 70.70  ? 1669 ASP A C     1 
ATOM   1091  O  O     . ASP A 1 1669 ? 122.918 195.255 132.191 1.00 70.14  ? 1669 ASP A O     1 
ATOM   1092  C  CB    . ASP A 1 1669 ? 122.411 195.829 129.258 1.00 74.47  ? 1669 ASP A CB    1 
ATOM   1093  C  CG    . ASP A 1 1669 ? 120.956 195.996 129.647 1.00 80.27  ? 1669 ASP A CG    1 
ATOM   1094  O  OD1   . ASP A 1 1669 ? 120.676 196.220 130.843 1.00 80.96  ? 1669 ASP A OD1   1 
ATOM   1095  O  OD2   . ASP A 1 1669 ? 120.088 195.898 128.755 1.00 86.56  ? 1669 ASP A OD2   1 
ATOM   1096  N  N     . ASN A 1 1670 ? 125.001 195.074 131.342 1.00 72.07  ? 1670 ASN A N     1 
ATOM   1097  C  CA    . ASN A 1 1670 ? 125.455 194.062 132.298 1.00 64.88  ? 1670 ASN A CA    1 
ATOM   1098  C  C     . ASN A 1 1670 ? 124.556 192.830 132.255 1.00 62.94  ? 1670 ASN A C     1 
ATOM   1099  O  O     . ASN A 1 1670 ? 124.274 192.200 133.276 1.00 64.25  ? 1670 ASN A O     1 
ATOM   1100  C  CB    . ASN A 1 1670 ? 125.535 194.634 133.715 1.00 61.94  ? 1670 ASN A CB    1 
ATOM   1101  C  CG    . ASN A 1 1670 ? 126.640 195.658 133.866 1.00 67.25  ? 1670 ASN A CG    1 
ATOM   1102  O  OD1   . ASN A 1 1670 ? 126.888 196.457 132.964 1.00 69.62  ? 1670 ASN A OD1   1 
ATOM   1103  N  ND2   . ASN A 1 1670 ? 127.314 195.638 135.010 1.00 65.11  ? 1670 ASN A ND2   1 
ATOM   1104  N  N     . SER A 1 1671 ? 124.102 192.483 131.049 1.00 60.76  ? 1671 SER A N     1 
ATOM   1105  C  CA    . SER A 1 1671 ? 123.203 191.359 130.846 1.00 56.68  ? 1671 SER A CA    1 
ATOM   1106  C  C     . SER A 1 1671 ? 123.792 190.240 130.003 1.00 55.73  ? 1671 SER A C     1 
ATOM   1107  O  O     . SER A 1 1671 ? 123.296 189.112 130.080 1.00 57.00  ? 1671 SER A O     1 
ATOM   1108  C  CB    . SER A 1 1671 ? 121.896 191.829 130.186 1.00 65.93  ? 1671 SER A CB    1 
ATOM   1109  O  OG    . SER A 1 1671 ? 122.137 192.332 128.884 1.00 64.31  ? 1671 SER A OG    1 
ATOM   1110  N  N     . VAL A 1 1672 ? 124.819 190.513 129.203 1.00 56.60  ? 1672 VAL A N     1 
ATOM   1111  C  CA    . VAL A 1 1672 ? 125.494 189.497 128.406 1.00 48.32  ? 1672 VAL A CA    1 
ATOM   1112  C  C     . VAL A 1 1672 ? 126.988 189.583 128.680 1.00 48.17  ? 1672 VAL A C     1 
ATOM   1113  O  O     . VAL A 1 1672 ? 127.516 190.663 128.969 1.00 49.63  ? 1672 VAL A O     1 
ATOM   1114  C  CB    . VAL A 1 1672 ? 125.200 189.651 126.897 1.00 45.46  ? 1672 VAL A CB    1 
ATOM   1115  C  CG1   . VAL A 1 1672 ? 123.702 189.695 126.644 1.00 49.48  ? 1672 VAL A CG1   1 
ATOM   1116  C  CG2   . VAL A 1 1672 ? 125.864 190.898 126.342 1.00 47.22  ? 1672 VAL A CG2   1 
ATOM   1117  N  N     . VAL A 1 1673 ? 127.664 188.441 128.614 1.00 49.72  ? 1673 VAL A N     1 
ATOM   1118  C  CA    . VAL A 1 1673 ? 129.104 188.373 128.835 1.00 41.25  ? 1673 VAL A CA    1 
ATOM   1119  C  C     . VAL A 1 1673 ? 129.783 188.344 127.471 1.00 38.96  ? 1673 VAL A C     1 
ATOM   1120  O  O     . VAL A 1 1673 ? 129.779 187.319 126.785 1.00 40.95  ? 1673 VAL A O     1 
ATOM   1121  C  CB    . VAL A 1 1673 ? 129.489 187.151 129.678 1.00 33.82  ? 1673 VAL A CB    1 
ATOM   1122  C  CG1   . VAL A 1 1673 ? 130.986 187.133 129.928 1.00 34.60  ? 1673 VAL A CG1   1 
ATOM   1123  C  CG2   . VAL A 1 1673 ? 128.726 187.154 130.992 1.00 39.34  ? 1673 VAL A CG2   1 
ATOM   1124  N  N     . LEU A 1 1674 ? 130.370 189.475 127.078 1.00 38.57  ? 1674 LEU A N     1 
ATOM   1125  C  CA    . LEU A 1 1674 ? 130.976 189.589 125.758 1.00 38.73  ? 1674 LEU A CA    1 
ATOM   1126  C  C     . LEU A 1 1674 ? 132.306 188.848 125.676 1.00 32.20  ? 1674 LEU A C     1 
ATOM   1127  O  O     . LEU A 1 1674 ? 132.655 188.317 124.617 1.00 33.62  ? 1674 LEU A O     1 
ATOM   1128  C  CB    . LEU A 1 1674 ? 131.166 191.063 125.399 1.00 39.11  ? 1674 LEU A CB    1 
ATOM   1129  C  CG    . LEU A 1 1674 ? 129.893 191.901 125.294 1.00 31.82  ? 1674 LEU A CG    1 
ATOM   1130  C  CD1   . LEU A 1 1674 ? 130.229 193.326 124.891 1.00 39.73  ? 1674 LEU A CD1   1 
ATOM   1131  C  CD2   . LEU A 1 1674 ? 128.929 191.275 124.303 1.00 29.80  ? 1674 LEU A CD2   1 
ATOM   1132  N  N     . GLY A 1 1675 ? 133.058 188.809 126.765 1.00 31.05  ? 1675 GLY A N     1 
ATOM   1133  C  CA    . GLY A 1 1675 ? 134.339 188.139 126.742 1.00 27.17  ? 1675 GLY A CA    1 
ATOM   1134  C  C     . GLY A 1 1675 ? 134.996 188.118 128.102 1.00 29.79  ? 1675 GLY A C     1 
ATOM   1135  O  O     . GLY A 1 1675 ? 134.338 188.270 129.133 1.00 27.65  ? 1675 GLY A O     1 
ATOM   1136  N  N     . ILE A 1 1676 ? 136.314 187.922 128.087 1.00 25.31  ? 1676 ILE A N     1 
ATOM   1137  C  CA    . ILE A 1 1676 ? 137.119 187.855 129.298 1.00 26.31  ? 1676 ILE A CA    1 
ATOM   1138  C  C     . ILE A 1 1676 ? 138.326 188.767 129.139 1.00 26.64  ? 1676 ILE A C     1 
ATOM   1139  O  O     . ILE A 1 1676 ? 138.721 189.126 128.029 1.00 28.18  ? 1676 ILE A O     1 
ATOM   1140  C  CB    . ILE A 1 1676 ? 137.587 186.421 129.617 1.00 24.71  ? 1676 ILE A CB    1 
ATOM   1141  C  CG1   . ILE A 1 1676 ? 138.191 185.783 128.366 1.00 25.82  ? 1676 ILE A CG1   1 
ATOM   1142  C  CG2   . ILE A 1 1676 ? 136.439 185.590 130.163 1.00 19.46  ? 1676 ILE A CG2   1 
ATOM   1143  C  CD1   . ILE A 1 1676 ? 138.785 184.429 128.600 1.00 19.24  ? 1676 ILE A CD1   1 
ATOM   1144  N  N     . SER A 1 1677 ? 138.923 189.127 130.273 1.00 27.04  ? 1677 SER A N     1 
ATOM   1145  C  CA    . SER A 1 1677 ? 140.106 189.973 130.293 1.00 27.79  ? 1677 SER A CA    1 
ATOM   1146  C  C     . SER A 1 1677 ? 141.097 189.429 131.312 1.00 30.81  ? 1677 SER A C     1 
ATOM   1147  O  O     . SER A 1 1677 ? 140.724 188.753 132.273 1.00 34.43  ? 1677 SER A O     1 
ATOM   1148  C  CB    . SER A 1 1677 ? 139.753 191.430 130.617 1.00 29.34  ? 1677 SER A CB    1 
ATOM   1149  O  OG    . SER A 1 1677 ? 140.919 192.228 130.717 1.00 32.03  ? 1677 SER A OG    1 
ATOM   1150  N  N     . SER A 1 1678 ? 142.371 189.734 131.090 1.00 27.66  ? 1678 SER A N     1 
ATOM   1151  C  CA    . SER A 1 1678 ? 143.457 189.292 131.950 1.00 28.28  ? 1678 SER A CA    1 
ATOM   1152  C  C     . SER A 1 1678 ? 143.982 190.463 132.776 1.00 35.99  ? 1678 SER A C     1 
ATOM   1153  O  O     . SER A 1 1678 ? 143.541 191.606 132.635 1.00 43.93  ? 1678 SER A O     1 
ATOM   1154  C  CB    . SER A 1 1678 ? 144.577 188.660 131.121 1.00 31.29  ? 1678 SER A CB    1 
ATOM   1155  O  OG    . SER A 1 1678 ? 145.269 189.640 130.369 1.00 30.19  ? 1678 SER A OG    1 
ATOM   1156  N  N     . ARG A 1 1679 ? 144.940 190.159 133.655 1.00 35.44  ? 1679 ARG A N     1 
ATOM   1157  C  CA    . ARG A 1 1679 ? 145.551 191.197 134.480 1.00 34.97  ? 1679 ARG A CA    1 
ATOM   1158  C  C     . ARG A 1 1679 ? 146.327 192.195 133.630 1.00 36.66  ? 1679 ARG A C     1 
ATOM   1159  O  O     . ARG A 1 1679 ? 146.287 193.404 133.889 1.00 43.49  ? 1679 ARG A O     1 
ATOM   1160  C  CB    . ARG A 1 1679 ? 146.462 190.567 135.534 1.00 30.12  ? 1679 ARG A CB    1 
ATOM   1161  C  CG    . ARG A 1 1679 ? 145.769 189.569 136.449 1.00 38.11  ? 1679 ARG A CG    1 
ATOM   1162  C  CD    . ARG A 1 1679 ? 145.958 188.137 135.963 1.00 47.73  ? 1679 ARG A CD    1 
ATOM   1163  N  NE    . ARG A 1 1679 ? 145.236 187.177 136.791 1.00 54.52  ? 1679 ARG A NE    1 
ATOM   1164  C  CZ    . ARG A 1 1679 ? 145.741 186.584 137.864 1.00 58.12  ? 1679 ARG A CZ    1 
ATOM   1165  N  NH1   . ARG A 1 1679 ? 146.976 186.827 138.272 1.00 59.33  ? 1679 ARG A NH1   1 
ATOM   1166  N  NH2   . ARG A 1 1679 ? 144.989 185.723 138.543 1.00 47.11  ? 1679 ARG A NH2   1 
ATOM   1167  N  N     . GLU A 1 1680 ? 147.035 191.711 132.609 1.00 33.86  ? 1680 GLU A N     1 
ATOM   1168  C  CA    . GLU A 1 1680 ? 147.794 192.587 131.725 1.00 32.35  ? 1680 GLU A CA    1 
ATOM   1169  C  C     . GLU A 1 1680 ? 146.905 193.421 130.815 1.00 28.27  ? 1680 GLU A C     1 
ATOM   1170  O  O     . GLU A 1 1680 ? 147.415 194.316 130.132 1.00 32.28  ? 1680 GLU A O     1 
ATOM   1171  C  CB    . GLU A 1 1680 ? 148.765 191.762 130.878 1.00 32.74  ? 1680 GLU A CB    1 
ATOM   1172  C  CG    . GLU A 1 1680 ? 149.926 191.183 131.664 1.00 34.42  ? 1680 GLU A CG    1 
ATOM   1173  C  CD    . GLU A 1 1680 ? 149.756 189.706 131.948 1.00 34.04  ? 1680 GLU A CD    1 
ATOM   1174  O  OE1   . GLU A 1 1680 ? 148.774 189.114 131.454 1.00 29.01  ? 1680 GLU A OE1   1 
ATOM   1175  O  OE2   . GLU A 1 1680 ? 150.603 189.138 132.669 1.00 33.36  ? 1680 GLU A OE2   1 
ATOM   1176  N  N     . GLY A 1 1681 ? 145.603 193.150 130.782 1.00 26.02  ? 1681 GLY A N     1 
ATOM   1177  C  CA    . GLY A 1 1681 ? 144.682 193.868 129.931 1.00 31.09  ? 1681 GLY A CA    1 
ATOM   1178  C  C     . GLY A 1 1681 ? 144.328 193.156 128.645 1.00 33.69  ? 1681 GLY A C     1 
ATOM   1179  O  O     . GLY A 1 1681 ? 143.372 193.566 127.974 1.00 38.82  ? 1681 GLY A O     1 
ATOM   1180  N  N     . GLU A 1 1682 ? 145.070 192.113 128.280 1.00 31.45  ? 1682 GLU A N     1 
ATOM   1181  C  CA    . GLU A 1 1682 ? 144.725 191.328 127.105 1.00 26.92  ? 1682 GLU A CA    1 
ATOM   1182  C  C     . GLU A 1 1682 ? 143.361 190.679 127.295 1.00 25.37  ? 1682 GLU A C     1 
ATOM   1183  O  O     . GLU A 1 1682 ? 143.067 190.109 128.348 1.00 26.93  ? 1682 GLU A O     1 
ATOM   1184  C  CB    . GLU A 1 1682 ? 145.790 190.263 126.848 1.00 25.94  ? 1682 GLU A CB    1 
ATOM   1185  C  CG    . GLU A 1 1682 ? 145.651 189.551 125.516 1.00 23.81  ? 1682 GLU A CG    1 
ATOM   1186  C  CD    . GLU A 1 1682 ? 146.494 188.296 125.441 1.00 20.95  ? 1682 GLU A CD    1 
ATOM   1187  O  OE1   . GLU A 1 1682 ? 146.135 187.296 126.094 1.00 24.83  ? 1682 GLU A OE1   1 
ATOM   1188  O  OE2   . GLU A 1 1682 ? 147.519 188.309 124.728 1.00 22.81  ? 1682 GLU A OE2   1 
ATOM   1189  N  N     . GLU A 1 1683 ? 142.526 190.767 126.265 1.00 25.24  ? 1683 GLU A N     1 
ATOM   1190  C  CA    . GLU A 1 1683 ? 141.150 190.309 126.351 1.00 29.91  ? 1683 GLU A CA    1 
ATOM   1191  C  C     . GLU A 1 1683 ? 140.852 189.329 125.228 1.00 26.66  ? 1683 GLU A C     1 
ATOM   1192  O  O     . GLU A 1 1683 ? 141.440 189.393 124.146 1.00 29.96  ? 1683 GLU A O     1 
ATOM   1193  C  CB    . GLU A 1 1683 ? 140.163 191.483 126.294 1.00 32.73  ? 1683 GLU A CB    1 
ATOM   1194  C  CG    . GLU A 1 1683 ? 140.157 192.228 124.973 1.00 38.79  ? 1683 GLU A CG    1 
ATOM   1195  C  CD    . GLU A 1 1683 ? 139.218 193.414 124.985 1.00 52.72  ? 1683 GLU A CD    1 
ATOM   1196  O  OE1   . GLU A 1 1683 ? 138.591 193.665 126.035 1.00 58.53  ? 1683 GLU A OE1   1 
ATOM   1197  O  OE2   . GLU A 1 1683 ? 139.108 194.097 123.944 1.00 59.27  ? 1683 GLU A OE2   1 
ATOM   1198  N  N     . VAL A 1 1684 ? 139.932 188.413 125.510 1.00 23.43  ? 1684 VAL A N     1 
ATOM   1199  C  CA    . VAL A 1 1684 ? 139.438 187.445 124.540 1.00 23.00  ? 1684 VAL A CA    1 
ATOM   1200  C  C     . VAL A 1 1684 ? 137.953 187.706 124.353 1.00 26.75  ? 1684 VAL A C     1 
ATOM   1201  O  O     . VAL A 1 1684 ? 137.180 187.641 125.317 1.00 33.02  ? 1684 VAL A O     1 
ATOM   1202  C  CB    . VAL A 1 1684 ? 139.687 185.997 124.992 1.00 24.56  ? 1684 VAL A CB    1 
ATOM   1203  C  CG1   . VAL A 1 1684 ? 139.415 185.034 123.851 1.00 21.40  ? 1684 VAL A CG1   1 
ATOM   1204  C  CG2   . VAL A 1 1684 ? 141.107 185.835 125.507 1.00 24.25  ? 1684 VAL A CG2   1 
ATOM   1205  N  N     . MET A 1 1685 ? 137.557 187.997 123.118 1.00 25.80  ? 1685 MET A N     1 
ATOM   1206  C  CA    . MET A 1 1685 ? 136.170 188.306 122.799 1.00 23.28  ? 1685 MET A CA    1 
ATOM   1207  C  C     . MET A 1 1685 ? 135.453 187.027 122.387 1.00 29.78  ? 1685 MET A C     1 
ATOM   1208  O  O     . MET A 1 1685 ? 135.844 186.376 121.412 1.00 35.60  ? 1685 MET A O     1 
ATOM   1209  C  CB    . MET A 1 1685 ? 136.097 189.353 121.688 1.00 26.88  ? 1685 MET A CB    1 
ATOM   1210  C  CG    . MET A 1 1685 ? 136.552 190.742 122.112 1.00 29.34  ? 1685 MET A CG    1 
ATOM   1211  S  SD    . MET A 1 1685 ? 135.648 191.417 123.521 1.00 53.54  ? 1685 MET A SD    1 
ATOM   1212  C  CE    . MET A 1 1685 ? 133.955 191.036 123.070 1.00 31.62  ? 1685 MET A CE    1 
ATOM   1213  N  N     . PHE A 1 1686 ? 134.404 186.675 123.127 1.00 29.00  ? 1686 PHE A N     1 
ATOM   1214  C  CA    . PHE A 1 1686 ? 133.683 185.436 122.874 1.00 24.23  ? 1686 PHE A CA    1 
ATOM   1215  C  C     . PHE A 1 1686 ? 133.048 185.450 121.490 1.00 29.63  ? 1686 PHE A C     1 
ATOM   1216  O  O     . PHE A 1 1686 ? 132.495 186.462 121.051 1.00 35.94  ? 1686 PHE A O     1 
ATOM   1217  C  CB    . PHE A 1 1686 ? 132.605 185.226 123.937 1.00 27.36  ? 1686 PHE A CB    1 
ATOM   1218  C  CG    . PHE A 1 1686 ? 133.145 184.918 125.302 1.00 28.84  ? 1686 PHE A CG    1 
ATOM   1219  C  CD1   . PHE A 1 1686 ? 134.459 184.522 125.470 1.00 28.84  ? 1686 PHE A CD1   1 
ATOM   1220  C  CD2   . PHE A 1 1686 ? 132.333 185.016 126.419 1.00 27.78  ? 1686 PHE A CD2   1 
ATOM   1221  C  CE1   . PHE A 1 1686 ? 134.955 184.236 126.724 1.00 27.19  ? 1686 PHE A CE1   1 
ATOM   1222  C  CE2   . PHE A 1 1686 ? 132.824 184.731 127.675 1.00 24.86  ? 1686 PHE A CE2   1 
ATOM   1223  C  CZ    . PHE A 1 1686 ? 134.137 184.340 127.827 1.00 24.92  ? 1686 PHE A CZ    1 
ATOM   1224  N  N     . LYS A 1 1687 ? 133.135 184.312 120.799 1.00 33.23  ? 1687 LYS A N     1 
ATOM   1225  C  CA    . LYS A 1 1687 ? 132.478 184.185 119.503 1.00 37.55  ? 1687 LYS A CA    1 
ATOM   1226  C  C     . LYS A 1 1687 ? 130.966 184.301 119.647 1.00 37.22  ? 1687 LYS A C     1 
ATOM   1227  O  O     . LYS A 1 1687 ? 130.307 184.979 118.850 1.00 36.37  ? 1687 LYS A O     1 
ATOM   1228  C  CB    . LYS A 1 1687 ? 132.857 182.856 118.852 1.00 34.91  ? 1687 LYS A CB    1 
ATOM   1229  C  CG    . LYS A 1 1687 ? 134.327 182.741 118.490 1.00 31.34  ? 1687 LYS A CG    1 
ATOM   1230  C  CD    . LYS A 1 1687 ? 134.772 183.887 117.604 1.00 32.48  ? 1687 LYS A CD    1 
ATOM   1231  C  CE    . LYS A 1 1687 ? 135.903 183.459 116.682 1.00 39.83  ? 1687 LYS A CE    1 
ATOM   1232  N  NZ    . LYS A 1 1687 ? 136.877 184.560 116.453 1.00 38.78  ? 1687 LYS A NZ    1 
ATOM   1233  N  N     . THR A 1 1688 ? 130.403 183.646 120.654 1.00 35.77  ? 1688 THR A N     1 
ATOM   1234  C  CA    . THR A 1 1688 ? 128.984 183.765 120.985 1.00 35.36  ? 1688 THR A CA    1 
ATOM   1235  C  C     . THR A 1 1688 ? 128.862 184.224 122.430 1.00 34.54  ? 1688 THR A C     1 
ATOM   1236  O  O     . THR A 1 1688 ? 129.136 183.432 123.351 1.00 36.10  ? 1688 THR A O     1 
ATOM   1237  C  CB    . THR A 1 1688 ? 128.256 182.437 120.780 1.00 34.30  ? 1688 THR A CB    1 
ATOM   1238  O  OG1   . THR A 1 1688 ? 129.023 181.375 121.359 1.00 38.17  ? 1688 THR A OG1   1 
ATOM   1239  C  CG2   . THR A 1 1688 ? 128.063 182.162 119.297 1.00 30.21  ? 1688 THR A CG2   1 
ATOM   1240  N  N     . PRO A 1 1689 ? 128.477 185.474 122.684 1.00 34.07  ? 1689 PRO A N     1 
ATOM   1241  C  CA    . PRO A 1 1689 ? 128.423 185.963 124.067 1.00 39.56  ? 1689 PRO A CA    1 
ATOM   1242  C  C     . PRO A 1 1689 ? 127.401 185.206 124.902 1.00 36.30  ? 1689 PRO A C     1 
ATOM   1243  O  O     . PRO A 1 1689 ? 126.378 184.734 124.400 1.00 33.96  ? 1689 PRO A O     1 
ATOM   1244  C  CB    . PRO A 1 1689 ? 128.036 187.439 123.910 1.00 38.76  ? 1689 PRO A CB    1 
ATOM   1245  C  CG    . PRO A 1 1689 ? 127.426 187.541 122.554 1.00 34.64  ? 1689 PRO A CG    1 
ATOM   1246  C  CD    . PRO A 1 1689 ? 128.102 186.510 121.708 1.00 28.22  ? 1689 PRO A CD    1 
ATOM   1247  N  N     . VAL A 1 1690 ? 127.696 185.091 126.192 1.00 38.29  ? 1690 VAL A N     1 
ATOM   1248  C  CA    . VAL A 1 1690 ? 126.829 184.400 127.139 1.00 43.24  ? 1690 VAL A CA    1 
ATOM   1249  C  C     . VAL A 1 1690 ? 125.823 185.399 127.695 1.00 43.79  ? 1690 VAL A C     1 
ATOM   1250  O  O     . VAL A 1 1690 ? 126.205 186.413 128.287 1.00 43.33  ? 1690 VAL A O     1 
ATOM   1251  C  CB    . VAL A 1 1690 ? 127.644 183.754 128.270 1.00 45.89  ? 1690 VAL A CB    1 
ATOM   1252  C  CG1   . VAL A 1 1690 ? 126.718 183.131 129.301 1.00 39.99  ? 1690 VAL A CG1   1 
ATOM   1253  C  CG2   . VAL A 1 1690 ? 128.602 182.716 127.707 1.00 41.72  ? 1690 VAL A CG2   1 
ATOM   1254  N  N     . SER A 1 1691 ? 124.538 185.106 127.518 1.00 51.19  ? 1691 SER A N     1 
ATOM   1255  C  CA    . SER A 1 1691 ? 123.468 185.984 127.973 1.00 53.85  ? 1691 SER A CA    1 
ATOM   1256  C  C     . SER A 1 1691 ? 123.027 185.570 129.372 1.00 54.06  ? 1691 SER A C     1 
ATOM   1257  O  O     . SER A 1 1691 ? 122.526 184.457 129.567 1.00 51.84  ? 1691 SER A O     1 
ATOM   1258  C  CB    . SER A 1 1691 ? 122.290 185.938 127.001 1.00 51.61  ? 1691 SER A CB    1 
ATOM   1259  O  OG    . SER A 1 1691 ? 121.902 184.601 126.744 1.00 57.23  ? 1691 SER A OG    1 
ATOM   1260  N  N     . ILE A 1 1692 ? 123.215 186.467 130.342 1.00 53.95  ? 1692 ILE A N     1 
ATOM   1261  C  CA    . ILE A 1 1692 ? 122.808 186.178 131.713 1.00 52.37  ? 1692 ILE A CA    1 
ATOM   1262  C  C     . ILE A 1 1692 ? 121.289 186.169 131.838 1.00 59.72  ? 1692 ILE A C     1 
ATOM   1263  O  O     . ILE A 1 1692 ? 120.734 185.456 132.683 1.00 60.28  ? 1692 ILE A O     1 
ATOM   1264  C  CB    . ILE A 1 1692 ? 123.453 187.186 132.682 1.00 47.72  ? 1692 ILE A CB    1 
ATOM   1265  C  CG1   . ILE A 1 1692 ? 124.959 187.268 132.433 1.00 46.41  ? 1692 ILE A CG1   1 
ATOM   1266  C  CG2   . ILE A 1 1692 ? 123.183 186.794 134.126 1.00 46.97  ? 1692 ILE A CG2   1 
ATOM   1267  C  CD1   . ILE A 1 1692 ? 125.680 188.215 133.362 1.00 45.99  ? 1692 ILE A CD1   1 
ATOM   1268  N  N     . THR A 1 1693 ? 120.592 186.958 131.017 1.00 60.66  ? 1693 THR A N     1 
ATOM   1269  C  CA    . THR A 1 1693 ? 119.134 186.983 131.079 1.00 58.26  ? 1693 THR A CA    1 
ATOM   1270  C  C     . THR A 1 1693 ? 118.538 185.628 130.715 1.00 62.58  ? 1693 THR A C     1 
ATOM   1271  O  O     . THR A 1 1693 ? 117.597 185.160 131.368 1.00 67.87  ? 1693 THR A O     1 
ATOM   1272  C  CB    . THR A 1 1693 ? 118.584 188.071 130.159 1.00 61.55  ? 1693 THR A CB    1 
ATOM   1273  O  OG1   . THR A 1 1693 ? 118.967 187.794 128.806 1.00 69.33  ? 1693 THR A OG1   1 
ATOM   1274  C  CG2   . THR A 1 1693 ? 119.122 189.432 130.565 1.00 62.15  ? 1693 THR A CG2   1 
ATOM   1275  N  N     . GLU A 1 1694 ? 119.071 184.981 129.677 1.00 58.97  ? 1694 GLU A N     1 
ATOM   1276  C  CA    . GLU A 1 1694 ? 118.553 183.679 129.273 1.00 58.95  ? 1694 GLU A CA    1 
ATOM   1277  C  C     . GLU A 1 1694 ? 118.939 182.571 130.244 1.00 58.68  ? 1694 GLU A C     1 
ATOM   1278  O  O     . GLU A 1 1694 ? 118.281 181.526 130.261 1.00 62.03  ? 1694 GLU A O     1 
ATOM   1279  C  CB    . GLU A 1 1694 ? 119.037 183.328 127.866 1.00 60.10  ? 1694 GLU A CB    1 
ATOM   1280  C  CG    . GLU A 1 1694 ? 118.662 184.346 126.805 1.00 61.84  ? 1694 GLU A CG    1 
ATOM   1281  C  CD    . GLU A 1 1694 ? 118.831 183.806 125.399 1.00 75.64  ? 1694 GLU A CD    1 
ATOM   1282  O  OE1   . GLU A 1 1694 ? 118.987 182.576 125.251 1.00 79.17  ? 1694 GLU A OE1   1 
ATOM   1283  O  OE2   . GLU A 1 1694 ? 118.808 184.609 124.443 1.00 73.91  ? 1694 GLU A OE2   1 
ATOM   1284  N  N     . HIS A 1 1695 ? 119.986 182.769 131.043 1.00 54.99  ? 1695 HIS A N     1 
ATOM   1285  C  CA    . HIS A 1 1695 ? 120.407 181.807 132.062 1.00 58.96  ? 1695 HIS A CA    1 
ATOM   1286  C  C     . HIS A 1 1695 ? 120.601 182.553 133.375 1.00 63.85  ? 1695 HIS A C     1 
ATOM   1287  O  O     . HIS A 1 1695 ? 121.734 182.864 133.767 1.00 62.22  ? 1695 HIS A O     1 
ATOM   1288  C  CB    . HIS A 1 1695 ? 121.678 181.071 131.638 1.00 53.65  ? 1695 HIS A CB    1 
ATOM   1289  C  CG    . HIS A 1 1695 ? 121.482 180.157 130.469 1.00 62.34  ? 1695 HIS A CG    1 
ATOM   1290  N  ND1   . HIS A 1 1695 ? 121.189 178.818 130.612 1.00 64.69  ? 1695 HIS A ND1   1 
ATOM   1291  C  CD2   . HIS A 1 1695 ? 121.531 180.391 129.136 1.00 62.55  ? 1695 HIS A CD2   1 
ATOM   1292  C  CE1   . HIS A 1 1695 ? 121.069 178.265 129.418 1.00 62.32  ? 1695 HIS A CE1   1 
ATOM   1293  N  NE2   . HIS A 1 1695 ? 121.271 179.198 128.505 1.00 66.60  ? 1695 HIS A NE2   1 
ATOM   1294  N  N     . PRO A 1 1696 ? 119.509 182.876 134.073 1.00 63.75  ? 1696 PRO A N     1 
ATOM   1295  C  CA    . PRO A 1 1696 ? 119.634 183.665 135.311 1.00 59.86  ? 1696 PRO A CA    1 
ATOM   1296  C  C     . PRO A 1 1696 ? 120.467 182.997 136.390 1.00 62.10  ? 1696 PRO A C     1 
ATOM   1297  O  O     . PRO A 1 1696 ? 121.128 183.700 137.165 1.00 63.90  ? 1696 PRO A O     1 
ATOM   1298  C  CB    . PRO A 1 1696 ? 118.177 183.838 135.760 1.00 62.84  ? 1696 PRO A CB    1 
ATOM   1299  C  CG    . PRO A 1 1696 ? 117.376 183.692 134.512 1.00 70.14  ? 1696 PRO A CG    1 
ATOM   1300  C  CD    . PRO A 1 1696 ? 118.103 182.674 133.685 1.00 59.44  ? 1696 PRO A CD    1 
ATOM   1301  N  N     . LYS A 1 1697 ? 120.449 181.669 136.476 1.00 64.17  ? 1697 LYS A N     1 
ATOM   1302  C  CA    . LYS A 1 1697 ? 121.159 180.979 137.545 1.00 61.79  ? 1697 LYS A CA    1 
ATOM   1303  C  C     . LYS A 1 1697 ? 122.663 181.180 137.418 1.00 60.41  ? 1697 LYS A C     1 
ATOM   1304  O  O     . LYS A 1 1697 ? 123.225 181.116 136.321 1.00 58.18  ? 1697 LYS A O     1 
ATOM   1305  C  CB    . LYS A 1 1697 ? 120.819 179.489 137.538 1.00 63.65  ? 1697 LYS A CB    1 
ATOM   1306  C  CG    . LYS A 1 1697 ? 119.442 179.173 138.114 1.00 64.87  ? 1697 LYS A CG    1 
ATOM   1307  C  CD    . LYS A 1 1697 ? 119.245 177.681 138.379 1.00 67.12  ? 1697 LYS A CD    1 
ATOM   1308  C  CE    . LYS A 1 1697 ? 119.818 176.792 137.281 1.00 70.38  ? 1697 LYS A CE    1 
ATOM   1309  N  NZ    . LYS A 1 1697 ? 119.406 177.220 135.914 1.00 73.20  ? 1697 LYS A NZ    1 
ATOM   1310  N  N     . ILE A 1 1698 ? 123.314 181.409 138.562 1.00 60.31  ? 1698 ILE A N     1 
ATOM   1311  C  CA    . ILE A 1 1698 ? 124.732 181.765 138.575 1.00 57.78  ? 1698 ILE A CA    1 
ATOM   1312  C  C     . ILE A 1 1698 ? 125.581 180.637 137.993 1.00 55.97  ? 1698 ILE A C     1 
ATOM   1313  O  O     . ILE A 1 1698 ? 126.453 180.865 137.141 1.00 52.24  ? 1698 ILE A O     1 
ATOM   1314  C  CB    . ILE A 1 1698 ? 125.167 182.144 140.007 1.00 57.35  ? 1698 ILE A CB    1 
ATOM   1315  C  CG1   . ILE A 1 1698 ? 126.544 182.805 140.011 1.00 52.00  ? 1698 ILE A CG1   1 
ATOM   1316  C  CG2   . ILE A 1 1698 ? 125.081 180.967 140.983 1.00 61.97  ? 1698 ILE A CG2   1 
ATOM   1317  C  CD1   . ILE A 1 1698 ? 126.569 184.126 139.326 1.00 56.44  ? 1698 ILE A CD1   1 
ATOM   1318  N  N     . ASN A 1 1699 ? 125.320 179.400 138.423 1.00 55.71  ? 1699 ASN A N     1 
ATOM   1319  C  CA    . ASN A 1 1699 ? 126.147 178.277 138.000 1.00 54.18  ? 1699 ASN A CA    1 
ATOM   1320  C  C     . ASN A 1 1699 ? 126.029 178.035 136.502 1.00 58.19  ? 1699 ASN A C     1 
ATOM   1321  O  O     . ASN A 1 1699 ? 127.029 177.754 135.831 1.00 58.45  ? 1699 ASN A O     1 
ATOM   1322  C  CB    . ASN A 1 1699 ? 125.776 177.024 138.798 1.00 59.10  ? 1699 ASN A CB    1 
ATOM   1323  C  CG    . ASN A 1 1699 ? 124.337 176.579 138.577 1.00 68.02  ? 1699 ASN A CG    1 
ATOM   1324  O  OD1   . ASN A 1 1699 ? 123.616 177.129 137.744 1.00 64.89  ? 1699 ASN A OD1   1 
ATOM   1325  N  ND2   . ASN A 1 1699 ? 123.913 175.571 139.330 1.00 70.77  ? 1699 ASN A ND2   1 
ATOM   1326  N  N     . GLU A 1 1700 ? 124.817 178.157 135.957 1.00 58.05  ? 1700 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1700 ? 124.618 177.872 134.542 1.00 56.05  ? 1700 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1700 ? 125.388 178.848 133.663 1.00 53.97  ? 1700 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1700 ? 126.112 178.432 132.751 1.00 55.56  ? 1700 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1700 ? 123.128 177.892 134.199 1.00 62.78  ? 1700 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1700 ? 122.438 176.552 134.402 1.00 71.53  ? 1700 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1700 ? 121.202 176.393 133.538 1.00 77.51  ? 1700 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1700 ? 120.806 177.374 132.875 1.00 74.07  ? 1700 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1700 ? 120.628 175.284 133.520 1.00 80.63  ? 1700 GLU A OE2   1 
ATOM   1335  N  N     . TRP A 1 1701 ? 125.263 180.155 133.921 1.00 48.84  ? 1701 TRP A N     1 
ATOM   1336  C  CA    . TRP A 1 1701 ? 125.929 181.083 133.015 1.00 44.78  ? 1701 TRP A CA    1 
ATOM   1337  C  C     . TRP A 1 1701 ? 127.424 181.142 133.294 1.00 42.64  ? 1701 TRP A C     1 
ATOM   1338  O  O     . TRP A 1 1701 ? 128.200 181.441 132.385 1.00 44.62  ? 1701 TRP A O     1 
ATOM   1339  C  CB    . TRP A 1 1701 ? 125.312 182.486 133.069 1.00 44.69  ? 1701 TRP A CB    1 
ATOM   1340  C  CG    . TRP A 1 1701 ? 125.530 183.296 134.309 1.00 41.11  ? 1701 TRP A CG    1 
ATOM   1341  C  CD1   . TRP A 1 1701 ? 124.676 183.447 135.357 1.00 49.46  ? 1701 TRP A CD1   1 
ATOM   1342  C  CD2   . TRP A 1 1701 ? 126.654 184.142 134.584 1.00 38.68  ? 1701 TRP A CD2   1 
ATOM   1343  N  NE1   . TRP A 1 1701 ? 125.214 184.302 136.288 1.00 44.06  ? 1701 TRP A NE1   1 
ATOM   1344  C  CE2   . TRP A 1 1701 ? 126.429 184.744 135.834 1.00 40.49  ? 1701 TRP A CE2   1 
ATOM   1345  C  CE3   . TRP A 1 1701 ? 127.838 184.433 133.901 1.00 42.17  ? 1701 TRP A CE3   1 
ATOM   1346  C  CZ2   . TRP A 1 1701 ? 127.342 185.620 136.415 1.00 43.53  ? 1701 TRP A CZ2   1 
ATOM   1347  C  CZ3   . TRP A 1 1701 ? 128.743 185.300 134.480 1.00 35.60  ? 1701 TRP A CZ3   1 
ATOM   1348  C  CH2   . TRP A 1 1701 ? 128.492 185.882 135.725 1.00 43.34  ? 1701 TRP A CH2   1 
ATOM   1349  N  N     . LEU A 1 1702 ? 127.858 180.831 134.520 1.00 45.50  ? 1702 LEU A N     1 
ATOM   1350  C  CA    . LEU A 1 1702 ? 129.295 180.700 134.753 1.00 40.02  ? 1702 LEU A CA    1 
ATOM   1351  C  C     . LEU A 1 1702 ? 129.878 179.520 133.978 1.00 39.06  ? 1702 LEU A C     1 
ATOM   1352  O  O     . LEU A 1 1702 ? 130.955 179.632 133.374 1.00 42.93  ? 1702 LEU A O     1 
ATOM   1353  C  CB    . LEU A 1 1702 ? 129.578 180.559 136.247 1.00 37.49  ? 1702 LEU A CB    1 
ATOM   1354  C  CG    . LEU A 1 1702 ? 129.931 181.867 136.957 1.00 39.39  ? 1702 LEU A CG    1 
ATOM   1355  C  CD1   . LEU A 1 1702 ? 130.314 181.611 138.402 1.00 43.22  ? 1702 LEU A CD1   1 
ATOM   1356  C  CD2   . LEU A 1 1702 ? 131.049 182.585 136.224 1.00 38.84  ? 1702 LEU A CD2   1 
ATOM   1357  N  N     . THR A 1 1703 ? 129.177 178.382 133.978 1.00 36.37  ? 1703 THR A N     1 
ATOM   1358  C  CA    . THR A 1 1703 ? 129.621 177.239 133.187 1.00 38.95  ? 1703 THR A CA    1 
ATOM   1359  C  C     . THR A 1 1703 ? 129.624 177.574 131.702 1.00 37.61  ? 1703 THR A C     1 
ATOM   1360  O  O     . THR A 1 1703 ? 130.540 177.181 130.968 1.00 41.65  ? 1703 THR A O     1 
ATOM   1361  C  CB    . THR A 1 1703 ? 128.725 176.031 133.467 1.00 39.71  ? 1703 THR A CB    1 
ATOM   1362  O  OG1   . THR A 1 1703 ? 128.852 175.648 134.842 1.00 49.93  ? 1703 THR A OG1   1 
ATOM   1363  C  CG2   . THR A 1 1703 ? 129.111 174.855 132.584 1.00 30.89  ? 1703 THR A CG2   1 
ATOM   1364  N  N     . LEU A 1 1704 ? 128.602 178.299 131.241 1.00 38.10  ? 1704 LEU A N     1 
ATOM   1365  C  CA    . LEU A 1 1704 ? 128.565 178.717 129.845 1.00 36.31  ? 1704 LEU A CA    1 
ATOM   1366  C  C     . LEU A 1 1704 ? 129.724 179.650 129.517 1.00 34.80  ? 1704 LEU A C     1 
ATOM   1367  O  O     . LEU A 1 1704 ? 130.298 179.572 128.428 1.00 35.72  ? 1704 LEU A O     1 
ATOM   1368  C  CB    . LEU A 1 1704 ? 127.229 179.386 129.531 1.00 41.86  ? 1704 LEU A CB    1 
ATOM   1369  C  CG    . LEU A 1 1704 ? 126.034 178.438 129.440 1.00 45.92  ? 1704 LEU A CG    1 
ATOM   1370  C  CD1   . LEU A 1 1704 ? 124.762 179.136 129.884 1.00 50.92  ? 1704 LEU A CD1   1 
ATOM   1371  C  CD2   . LEU A 1 1704 ? 125.892 177.892 128.027 1.00 41.07  ? 1704 LEU A CD2   1 
ATOM   1372  N  N     . VAL A 1 1705 ? 130.079 180.540 130.446 1.00 35.29  ? 1705 VAL A N     1 
ATOM   1373  C  CA    . VAL A 1 1705 ? 131.213 181.436 130.233 1.00 34.49  ? 1705 VAL A CA    1 
ATOM   1374  C  C     . VAL A 1 1705 ? 132.504 180.640 130.102 1.00 26.57  ? 1705 VAL A C     1 
ATOM   1375  O  O     . VAL A 1 1705 ? 133.330 180.914 129.226 1.00 27.11  ? 1705 VAL A O     1 
ATOM   1376  C  CB    . VAL A 1 1705 ? 131.295 182.472 131.370 1.00 30.89  ? 1705 VAL A CB    1 
ATOM   1377  C  CG1   . VAL A 1 1705 ? 132.686 183.082 131.441 1.00 25.49  ? 1705 VAL A CG1   1 
ATOM   1378  C  CG2   . VAL A 1 1705 ? 130.256 183.561 131.169 1.00 26.16  ? 1705 VAL A CG2   1 
ATOM   1379  N  N     . GLU A 1 1706 ? 132.700 179.644 130.968 1.00 27.99  ? 1706 GLU A N     1 
ATOM   1380  C  CA    . GLU A 1 1706 ? 133.911 178.827 130.892 1.00 26.16  ? 1706 GLU A CA    1 
ATOM   1381  C  C     . GLU A 1 1706 ? 133.969 178.036 129.586 1.00 26.12  ? 1706 GLU A C     1 
ATOM   1382  O  O     . GLU A 1 1706 ? 135.013 177.976 128.916 1.00 28.32  ? 1706 GLU A O     1 
ATOM   1383  C  CB    . GLU A 1 1706 ? 133.976 177.894 132.101 1.00 25.20  ? 1706 GLU A CB    1 
ATOM   1384  C  CG    . GLU A 1 1706 ? 135.173 176.968 132.117 1.00 31.41  ? 1706 GLU A CG    1 
ATOM   1385  C  CD    . GLU A 1 1706 ? 134.891 175.678 132.857 1.00 38.60  ? 1706 GLU A CD    1 
ATOM   1386  O  OE1   . GLU A 1 1706 ? 134.366 174.735 132.229 1.00 36.20  ? 1706 GLU A OE1   1 
ATOM   1387  O  OE2   . GLU A 1 1706 ? 135.193 175.606 134.066 1.00 35.98  ? 1706 GLU A OE2   1 
ATOM   1388  N  N     . LYS A 1 1707 ? 132.844 177.428 129.200 1.00 21.68  ? 1707 LYS A N     1 
ATOM   1389  C  CA    . LYS A 1 1707 ? 132.799 176.666 127.957 1.00 24.83  ? 1707 LYS A CA    1 
ATOM   1390  C  C     . LYS A 1 1707 ? 133.042 177.563 126.751 1.00 26.03  ? 1707 LYS A C     1 
ATOM   1391  O  O     . LYS A 1 1707 ? 133.739 177.174 125.805 1.00 29.59  ? 1707 LYS A O     1 
ATOM   1392  C  CB    . LYS A 1 1707 ? 131.454 175.953 127.831 1.00 34.26  ? 1707 LYS A CB    1 
ATOM   1393  C  CG    . LYS A 1 1707 ? 131.336 175.062 126.610 1.00 32.37  ? 1707 LYS A CG    1 
ATOM   1394  C  CD    . LYS A 1 1707 ? 130.000 174.348 126.579 1.00 36.58  ? 1707 LYS A CD    1 
ATOM   1395  C  CE    . LYS A 1 1707 ? 129.919 173.387 125.405 1.00 46.79  ? 1707 LYS A CE    1 
ATOM   1396  N  NZ    . LYS A 1 1707 ? 129.900 174.105 124.103 1.00 42.52  ? 1707 LYS A NZ    1 
ATOM   1397  N  N     . GLU A 1 1708 ? 132.463 178.765 126.761 1.00 27.83  ? 1708 GLU A N     1 
ATOM   1398  C  CA    . GLU A 1 1708 ? 132.677 179.697 125.666 1.00 29.36  ? 1708 GLU A CA    1 
ATOM   1399  C  C     . GLU A 1 1708 ? 134.116 180.188 125.632 1.00 24.53  ? 1708 GLU A C     1 
ATOM   1400  O  O     . GLU A 1 1708 ? 134.666 180.393 124.549 1.00 29.33  ? 1708 GLU A O     1 
ATOM   1401  C  CB    . GLU A 1 1708 ? 131.704 180.869 125.771 1.00 31.58  ? 1708 GLU A CB    1 
ATOM   1402  C  CG    . GLU A 1 1708 ? 131.828 181.866 124.638 1.00 31.05  ? 1708 GLU A CG    1 
ATOM   1403  C  CD    . GLU A 1 1708 ? 131.451 181.275 123.291 1.00 38.11  ? 1708 GLU A CD    1 
ATOM   1404  O  OE1   . GLU A 1 1708 ? 130.658 180.310 123.256 1.00 35.33  ? 1708 GLU A OE1   1 
ATOM   1405  O  OE2   . GLU A 1 1708 ? 131.950 181.776 122.263 1.00 42.11  ? 1708 GLU A OE2   1 
ATOM   1406  N  N     . MET A 1 1709 ? 134.736 180.379 126.798 1.00 20.84  ? 1709 MET A N     1 
ATOM   1407  C  CA    . MET A 1 1709 ? 136.170 180.641 126.848 1.00 19.27  ? 1709 MET A CA    1 
ATOM   1408  C  C     . MET A 1 1709 ? 136.942 179.573 126.094 1.00 24.28  ? 1709 MET A C     1 
ATOM   1409  O  O     . MET A 1 1709 ? 137.760 179.879 125.216 1.00 28.94  ? 1709 MET A O     1 
ATOM   1410  C  CB    . MET A 1 1709 ? 136.644 180.689 128.300 1.00 22.05  ? 1709 MET A CB    1 
ATOM   1411  C  CG    . MET A 1 1709 ? 138.121 181.002 128.450 1.00 25.35  ? 1709 MET A CG    1 
ATOM   1412  S  SD    . MET A 1 1709 ? 138.665 181.076 130.167 1.00 39.99  ? 1709 MET A SD    1 
ATOM   1413  C  CE    . MET A 1 1709 ? 138.609 179.343 130.616 1.00 19.85  ? 1709 MET A CE    1 
ATOM   1414  N  N     . ARG A 1 1710 ? 136.685 178.306 126.422 1.00 26.63  ? 1710 ARG A N     1 
ATOM   1415  C  CA    . ARG A 1 1710 ? 137.433 177.226 125.785 1.00 20.82  ? 1710 ARG A CA    1 
ATOM   1416  C  C     . ARG A 1 1710 ? 137.187 177.183 124.279 1.00 20.86  ? 1710 ARG A C     1 
ATOM   1417  O  O     . ARG A 1 1710 ? 138.136 177.070 123.492 1.00 22.12  ? 1710 ARG A O     1 
ATOM   1418  C  CB    . ARG A 1 1710 ? 137.084 175.887 126.430 1.00 21.63  ? 1710 ARG A CB    1 
ATOM   1419  C  CG    . ARG A 1 1710 ? 137.987 175.525 127.595 1.00 18.21  ? 1710 ARG A CG    1 
ATOM   1420  C  CD    . ARG A 1 1710 ? 137.830 174.071 127.987 1.00 23.63  ? 1710 ARG A CD    1 
ATOM   1421  N  NE    . ARG A 1 1710 ? 136.937 173.897 129.124 1.00 28.26  ? 1710 ARG A NE    1 
ATOM   1422  C  CZ    . ARG A 1 1710 ? 137.347 173.720 130.372 1.00 30.88  ? 1710 ARG A CZ    1 
ATOM   1423  N  NH1   . ARG A 1 1710 ? 138.633 173.705 130.681 1.00 27.03  ? 1710 ARG A NH1   1 
ATOM   1424  N  NH2   . ARG A 1 1710 ? 136.445 173.548 131.334 1.00 29.86  ? 1710 ARG A NH2   1 
ATOM   1425  N  N     . VAL A 1 1711 ? 135.924 177.288 123.856 1.00 20.82  ? 1711 VAL A N     1 
ATOM   1426  C  CA    . VAL A 1 1711 ? 135.623 177.149 122.432 1.00 23.91  ? 1711 VAL A CA    1 
ATOM   1427  C  C     . VAL A 1 1711 ? 136.152 178.346 121.645 1.00 22.82  ? 1711 VAL A C     1 
ATOM   1428  O  O     . VAL A 1 1711 ? 136.639 178.194 120.518 1.00 28.90  ? 1711 VAL A O     1 
ATOM   1429  C  CB    . VAL A 1 1711 ? 134.114 176.925 122.206 1.00 23.97  ? 1711 VAL A CB    1 
ATOM   1430  C  CG1   . VAL A 1 1711 ? 133.307 178.132 122.622 1.00 24.39  ? 1711 VAL A CG1   1 
ATOM   1431  C  CG2   . VAL A 1 1711 ? 133.841 176.580 120.749 1.00 31.03  ? 1711 VAL A CG2   1 
ATOM   1432  N  N     . THR A 1 1712 ? 136.072 179.551 122.218 1.00 19.66  ? 1712 THR A N     1 
ATOM   1433  C  CA    . THR A 1 1712 ? 136.612 180.728 121.552 1.00 23.84  ? 1712 THR A CA    1 
ATOM   1434  C  C     . THR A 1 1712 ? 138.126 180.655 121.436 1.00 23.96  ? 1712 THR A C     1 
ATOM   1435  O  O     . THR A 1 1712 ? 138.683 181.023 120.396 1.00 26.25  ? 1712 THR A O     1 
ATOM   1436  C  CB    . THR A 1 1712 ? 136.200 181.994 122.303 1.00 23.87  ? 1712 THR A CB    1 
ATOM   1437  O  OG1   . THR A 1 1712 ? 134.792 181.960 122.564 1.00 28.84  ? 1712 THR A OG1   1 
ATOM   1438  C  CG2   . THR A 1 1712 ? 136.528 183.229 121.482 1.00 24.12  ? 1712 THR A CG2   1 
ATOM   1439  N  N     . LEU A 1 1713 ? 138.806 180.181 122.484 1.00 20.62  ? 1713 LEU A N     1 
ATOM   1440  C  CA    . LEU A 1 1713 ? 140.248 179.995 122.390 1.00 17.35  ? 1713 LEU A CA    1 
ATOM   1441  C  C     . LEU A 1 1713 ? 140.595 178.975 121.315 1.00 17.96  ? 1713 LEU A C     1 
ATOM   1442  O  O     . LEU A 1 1713 ? 141.547 179.169 120.553 1.00 19.09  ? 1713 LEU A O     1 
ATOM   1443  C  CB    . LEU A 1 1713 ? 140.814 179.570 123.744 1.00 19.76  ? 1713 LEU A CB    1 
ATOM   1444  C  CG    . LEU A 1 1713 ? 141.124 180.706 124.720 1.00 18.99  ? 1713 LEU A CG    1 
ATOM   1445  C  CD1   . LEU A 1 1713 ? 141.658 180.157 126.032 1.00 13.63  ? 1713 LEU A CD1   1 
ATOM   1446  C  CD2   . LEU A 1 1713 ? 142.109 181.684 124.104 1.00 20.41  ? 1713 LEU A CD2   1 
ATOM   1447  N  N     . ALA A 1 1714 ? 139.821 177.889 121.226 1.00 20.26  ? 1714 ALA A N     1 
ATOM   1448  C  CA    . ALA A 1 1714 ? 140.076 176.885 120.197 1.00 17.45  ? 1714 ALA A CA    1 
ATOM   1449  C  C     . ALA A 1 1714 ? 139.888 177.456 118.795 1.00 19.37  ? 1714 ALA A C     1 
ATOM   1450  O  O     . ALA A 1 1714 ? 140.711 177.216 117.902 1.00 22.84  ? 1714 ALA A O     1 
ATOM   1451  C  CB    . ALA A 1 1714 ? 139.169 175.675 120.412 1.00 20.18  ? 1714 ALA A CB    1 
ATOM   1452  N  N     . LYS A 1 1715 ? 138.811 178.214 118.580 1.00 19.71  ? 1715 LYS A N     1 
ATOM   1453  C  CA    . LYS A 1 1715 ? 138.559 178.787 117.260 1.00 22.17  ? 1715 LYS A CA    1 
ATOM   1454  C  C     . LYS A 1 1715 ? 139.628 179.806 116.881 1.00 25.75  ? 1715 LYS A C     1 
ATOM   1455  O  O     . LYS A 1 1715 ? 140.108 179.822 115.737 1.00 30.08  ? 1715 LYS A O     1 
ATOM   1456  C  CB    . LYS A 1 1715 ? 137.172 179.426 117.226 1.00 29.52  ? 1715 LYS A CB    1 
ATOM   1457  C  CG    . LYS A 1 1715 ? 136.029 178.428 117.290 1.00 34.67  ? 1715 LYS A CG    1 
ATOM   1458  C  CD    . LYS A 1 1715 ? 134.689 179.135 117.394 1.00 42.19  ? 1715 LYS A CD    1 
ATOM   1459  C  CE    . LYS A 1 1715 ? 134.334 179.829 116.088 1.00 49.85  ? 1715 LYS A CE    1 
ATOM   1460  N  NZ    . LYS A 1 1715 ? 132.974 180.432 116.128 1.00 60.44  ? 1715 LYS A NZ    1 
ATOM   1461  N  N     . LEU A 1 1716 ? 140.011 180.666 117.828 1.00 21.23  ? 1716 LEU A N     1 
ATOM   1462  C  CA    . LEU A 1 1716 ? 141.064 181.637 117.561 1.00 18.02  ? 1716 LEU A CA    1 
ATOM   1463  C  C     . LEU A 1 1716 ? 142.386 180.940 117.273 1.00 20.27  ? 1716 LEU A C     1 
ATOM   1464  O  O     . LEU A 1 1716 ? 143.153 181.381 116.409 1.00 26.44  ? 1716 LEU A O     1 
ATOM   1465  C  CB    . LEU A 1 1716 ? 141.201 182.597 118.740 1.00 20.68  ? 1716 LEU A CB    1 
ATOM   1466  C  CG    . LEU A 1 1716 ? 140.102 183.643 118.921 1.00 18.15  ? 1716 LEU A CG    1 
ATOM   1467  C  CD1   . LEU A 1 1716 ? 140.361 184.470 120.166 1.00 14.26  ? 1716 LEU A CD1   1 
ATOM   1468  C  CD2   . LEU A 1 1716 ? 140.009 184.533 117.697 1.00 19.97  ? 1716 LEU A CD2   1 
ATOM   1469  N  N     . LEU A 1 1717 ? 142.671 179.848 117.987 1.00 19.50  ? 1717 LEU A N     1 
ATOM   1470  C  CA    . LEU A 1 1717 ? 143.877 179.079 117.711 1.00 21.86  ? 1717 LEU A CA    1 
ATOM   1471  C  C     . LEU A 1 1717 ? 143.837 178.494 116.308 1.00 21.95  ? 1717 LEU A C     1 
ATOM   1472  O  O     . LEU A 1 1717 ? 144.854 178.472 115.610 1.00 24.91  ? 1717 LEU A O     1 
ATOM   1473  C  CB    . LEU A 1 1717 ? 144.041 177.969 118.751 1.00 15.88  ? 1717 LEU A CB    1 
ATOM   1474  C  CG    . LEU A 1 1717 ? 144.923 176.776 118.372 1.00 17.93  ? 1717 LEU A CG    1 
ATOM   1475  C  CD1   . LEU A 1 1717 ? 146.368 177.216 118.174 1.00 14.01  ? 1717 LEU A CD1   1 
ATOM   1476  C  CD2   . LEU A 1 1717 ? 144.833 175.668 119.403 1.00 19.88  ? 1717 LEU A CD2   1 
ATOM   1477  N  N     . ALA A 1 1718 ? 142.671 178.005 115.881 1.00 22.36  ? 1718 ALA A N     1 
ATOM   1478  C  CA    . ALA A 1 1718 ? 142.548 177.460 114.532 1.00 23.70  ? 1718 ALA A CA    1 
ATOM   1479  C  C     . ALA A 1 1718 ? 142.827 178.527 113.480 1.00 28.81  ? 1718 ALA A C     1 
ATOM   1480  O  O     . ALA A 1 1718 ? 143.555 178.286 112.507 1.00 30.60  ? 1718 ALA A O     1 
ATOM   1481  C  CB    . ALA A 1 1718 ? 141.157 176.858 114.336 1.00 24.71  ? 1718 ALA A CB    1 
ATOM   1482  N  N     . GLU A 1 1719 ? 142.259 179.722 113.663 1.00 27.28  ? 1719 GLU A N     1 
ATOM   1483  C  CA    . GLU A 1 1719 ? 142.513 180.806 112.714 1.00 23.69  ? 1719 GLU A CA    1 
ATOM   1484  C  C     . GLU A 1 1719 ? 143.986 181.211 112.709 1.00 23.80  ? 1719 GLU A C     1 
ATOM   1485  O  O     . GLU A 1 1719 ? 144.579 181.438 111.642 1.00 27.82  ? 1719 GLU A O     1 
ATOM   1486  C  CB    . GLU A 1 1719 ? 141.626 182.008 113.037 1.00 26.25  ? 1719 GLU A CB    1 
ATOM   1487  C  CG    . GLU A 1 1719 ? 140.147 181.681 113.130 1.00 32.67  ? 1719 GLU A CG    1 
ATOM   1488  C  CD    . GLU A 1 1719 ? 139.333 182.820 113.710 1.00 44.72  ? 1719 GLU A CD    1 
ATOM   1489  O  OE1   . GLU A 1 1719 ? 139.900 183.914 113.913 1.00 42.96  ? 1719 GLU A OE1   1 
ATOM   1490  O  OE2   . GLU A 1 1719 ? 138.126 182.623 113.961 1.00 44.51  ? 1719 GLU A OE2   1 
ATOM   1491  N  N     . SER A 1 1720 ? 144.594 181.304 113.894 1.00 25.03  ? 1720 SER A N     1 
ATOM   1492  C  CA    . SER A 1 1720 ? 146.001 181.677 113.978 1.00 22.99  ? 1720 SER A CA    1 
ATOM   1493  C  C     . SER A 1 1720 ? 146.889 180.625 113.328 1.00 27.64  ? 1720 SER A C     1 
ATOM   1494  O  O     . SER A 1 1720 ? 147.897 180.959 112.697 1.00 32.36  ? 1720 SER A O     1 
ATOM   1495  C  CB    . SER A 1 1720 ? 146.396 181.892 115.438 1.00 21.74  ? 1720 SER A CB    1 
ATOM   1496  O  OG    . SER A 1 1720 ? 147.783 182.150 115.557 1.00 24.72  ? 1720 SER A OG    1 
ATOM   1497  N  N     . VAL A 1 1721 ? 146.535 179.347 113.479 1.00 26.93  ? 1721 VAL A N     1 
ATOM   1498  C  CA    . VAL A 1 1721 ? 147.272 178.279 112.812 1.00 22.76  ? 1721 VAL A CA    1 
ATOM   1499  C  C     . VAL A 1 1721 ? 147.137 178.406 111.303 1.00 29.01  ? 1721 VAL A C     1 
ATOM   1500  O  O     . VAL A 1 1721 ? 148.113 178.244 110.561 1.00 34.56  ? 1721 VAL A O     1 
ATOM   1501  C  CB    . VAL A 1 1721 ? 146.793 176.903 113.311 1.00 24.92  ? 1721 VAL A CB    1 
ATOM   1502  C  CG1   . VAL A 1 1721 ? 147.264 175.801 112.376 1.00 30.49  ? 1721 VAL A CG1   1 
ATOM   1503  C  CG2   . VAL A 1 1721 ? 147.307 176.648 114.712 1.00 20.85  ? 1721 VAL A CG2   1 
ATOM   1504  N  N     . THR A 1 1722 ? 145.926 178.700 110.825 1.00 30.14  ? 1722 THR A N     1 
ATOM   1505  C  CA    . THR A 1 1722 ? 145.725 178.877 109.390 1.00 28.98  ? 1722 THR A CA    1 
ATOM   1506  C  C     . THR A 1 1722 ? 146.606 179.995 108.848 1.00 31.44  ? 1722 THR A C     1 
ATOM   1507  O  O     . THR A 1 1722 ? 147.176 179.875 107.757 1.00 39.57  ? 1722 THR A O     1 
ATOM   1508  C  CB    . THR A 1 1722 ? 144.252 179.161 109.097 1.00 29.69  ? 1722 THR A CB    1 
ATOM   1509  O  OG1   . THR A 1 1722 ? 143.453 178.062 109.550 1.00 34.11  ? 1722 THR A OG1   1 
ATOM   1510  C  CG2   . THR A 1 1722 ? 144.031 179.356 107.607 1.00 26.32  ? 1722 THR A CG2   1 
ATOM   1511  N  N     . GLU A 1 1723 ? 146.737 181.089 109.600 1.00 32.77  ? 1723 GLU A N     1 
ATOM   1512  C  CA    . GLU A 1 1723 ? 147.579 182.192 109.135 1.00 33.20  ? 1723 GLU A CA    1 
ATOM   1513  C  C     . GLU A 1 1723 ? 149.067 181.850 109.220 1.00 37.19  ? 1723 GLU A C     1 
ATOM   1514  O  O     . GLU A 1 1723 ? 149.835 182.140 108.290 1.00 43.21  ? 1723 GLU A O     1 
ATOM   1515  C  CB    . GLU A 1 1723 ? 147.267 183.459 109.931 1.00 34.49  ? 1723 GLU A CB    1 
ATOM   1516  C  CG    . GLU A 1 1723 ? 145.934 184.092 109.569 1.00 36.37  ? 1723 GLU A CG    1 
ATOM   1517  C  CD    . GLU A 1 1723 ? 145.637 185.336 110.380 1.00 45.59  ? 1723 GLU A CD    1 
ATOM   1518  O  OE1   . GLU A 1 1723 ? 146.521 186.215 110.464 1.00 41.02  ? 1723 GLU A OE1   1 
ATOM   1519  O  OE2   . GLU A 1 1723 ? 144.520 185.438 110.928 1.00 42.01  ? 1723 GLU A OE2   1 
ATOM   1520  N  N     . VAL A 1 1724 ? 149.500 181.237 110.326 1.00 36.86  ? 1724 VAL A N     1 
ATOM   1521  C  CA    . VAL A 1 1724 ? 150.919 180.948 110.500 1.00 34.25  ? 1724 VAL A CA    1 
ATOM   1522  C  C     . VAL A 1 1724 ? 151.390 179.866 109.536 1.00 42.67  ? 1724 VAL A C     1 
ATOM   1523  O  O     . VAL A 1 1724 ? 152.580 179.817 109.203 1.00 49.27  ? 1724 VAL A O     1 
ATOM   1524  C  CB    . VAL A 1 1724 ? 151.222 180.565 111.963 1.00 31.35  ? 1724 VAL A CB    1 
ATOM   1525  C  CG1   . VAL A 1 1724 ? 150.678 179.187 112.292 1.00 31.56  ? 1724 VAL A CG1   1 
ATOM   1526  C  CG2   . VAL A 1 1724 ? 152.716 180.648 112.250 1.00 27.94  ? 1724 VAL A CG2   1 
ATOM   1527  N  N     . GLU A 1 1725 ? 150.487 178.997 109.070 1.00 41.36  ? 1725 GLU A N     1 
ATOM   1528  C  CA    . GLU A 1 1725 ? 150.848 178.065 108.007 1.00 39.99  ? 1725 GLU A CA    1 
ATOM   1529  C  C     . GLU A 1 1725 ? 151.224 178.812 106.736 1.00 43.22  ? 1725 GLU A C     1 
ATOM   1530  O  O     . GLU A 1 1725 ? 152.183 178.442 106.048 1.00 46.79  ? 1725 GLU A O     1 
ATOM   1531  C  CB    . GLU A 1 1725 ? 149.697 177.097 107.737 1.00 41.84  ? 1725 GLU A CB    1 
ATOM   1532  C  CG    . GLU A 1 1725 ? 149.489 176.043 108.811 1.00 39.25  ? 1725 GLU A CG    1 
ATOM   1533  C  CD    . GLU A 1 1725 ? 148.630 174.892 108.329 1.00 50.60  ? 1725 GLU A CD    1 
ATOM   1534  O  OE1   . GLU A 1 1725 ? 147.518 175.152 107.823 1.00 46.98  ? 1725 GLU A OE1   1 
ATOM   1535  O  OE2   . GLU A 1 1725 ? 149.066 173.728 108.451 1.00 52.96  ? 1725 GLU A OE2   1 
ATOM   1536  N  N     . ILE A 1 1726 ? 150.474 179.865 106.405 1.00 47.07  ? 1726 ILE A N     1 
ATOM   1537  C  CA    . ILE A 1 1726 ? 150.843 180.717 105.279 1.00 49.54  ? 1726 ILE A CA    1 
ATOM   1538  C  C     . ILE A 1 1726 ? 152.181 181.392 105.547 1.00 47.41  ? 1726 ILE A C     1 
ATOM   1539  O  O     . ILE A 1 1726 ? 153.032 181.494 104.654 1.00 44.53  ? 1726 ILE A O     1 
ATOM   1540  C  CB    . ILE A 1 1726 ? 149.733 181.744 104.995 1.00 38.13  ? 1726 ILE A CB    1 
ATOM   1541  C  CG1   . ILE A 1 1726 ? 148.417 181.031 104.682 1.00 38.20  ? 1726 ILE A CG1   1 
ATOM   1542  C  CG2   . ILE A 1 1726 ? 150.128 182.651 103.844 1.00 42.57  ? 1726 ILE A CG2   1 
ATOM   1543  C  CD1   . ILE A 1 1726 ? 148.480 180.141 103.462 1.00 43.89  ? 1726 ILE A CD1   1 
ATOM   1544  N  N     . PHE A 1 1727 ? 152.391 181.866 106.779 1.00 48.27  ? 1727 PHE A N     1 
ATOM   1545  C  CA    . PHE A 1 1727 ? 153.708 182.391 107.134 1.00 48.64  ? 1727 PHE A CA    1 
ATOM   1546  C  C     . PHE A 1 1727 ? 154.776 181.308 107.058 1.00 48.86  ? 1727 PHE A C     1 
ATOM   1547  O  O     . PHE A 1 1727 ? 155.938 181.591 106.741 1.00 48.86  ? 1727 PHE A O     1 
ATOM   1548  C  CB    . PHE A 1 1727 ? 153.684 183.020 108.526 1.00 44.67  ? 1727 PHE A CB    1 
ATOM   1549  C  CG    . PHE A 1 1727 ? 152.900 184.292 108.597 1.00 41.77  ? 1727 PHE A CG    1 
ATOM   1550  C  CD1   . PHE A 1 1727 ? 152.535 184.962 107.440 1.00 48.15  ? 1727 PHE A CD1   1 
ATOM   1551  C  CD2   . PHE A 1 1727 ? 152.540 184.828 109.816 1.00 33.14  ? 1727 PHE A CD2   1 
ATOM   1552  C  CE1   . PHE A 1 1727 ? 151.818 186.136 107.502 1.00 51.66  ? 1727 PHE A CE1   1 
ATOM   1553  C  CE2   . PHE A 1 1727 ? 151.827 186.000 109.881 1.00 43.35  ? 1727 PHE A CE2   1 
ATOM   1554  C  CZ    . PHE A 1 1727 ? 151.463 186.656 108.724 1.00 51.67  ? 1727 PHE A CZ    1 
ATOM   1555  N  N     . GLY A 1 1728 ? 154.409 180.065 107.347 1.00 53.64  ? 1728 GLY A N     1 
ATOM   1556  C  CA    . GLY A 1 1728 ? 155.307 178.952 107.144 1.00 53.77  ? 1728 GLY A CA    1 
ATOM   1557  C  C     . GLY A 1 1728 ? 155.486 178.663 105.665 1.00 58.08  ? 1728 GLY A C     1 
ATOM   1558  O  O     . GLY A 1 1728 ? 154.877 179.286 104.795 1.00 61.74  ? 1728 GLY A O     1 
ATOM   1559  N  N     . LYS A 1 1729 ? 156.354 177.685 105.387 1.00 52.09  ? 1729 LYS A N     1 
ATOM   1560  C  CA    . LYS A 1 1729 ? 156.721 177.256 104.036 1.00 60.36  ? 1729 LYS A CA    1 
ATOM   1561  C  C     . LYS A 1 1729 ? 156.887 178.435 103.081 1.00 60.72  ? 1729 LYS A C     1 
ATOM   1562  O  O     . LYS A 1 1729 ? 156.444 178.382 101.929 1.00 64.91  ? 1729 LYS A O     1 
ATOM   1563  C  CB    . LYS A 1 1729 ? 155.705 176.242 103.482 1.00 66.09  ? 1729 LYS A CB    1 
ATOM   1564  C  CG    . LYS A 1 1729 ? 154.259 176.713 103.355 1.00 62.42  ? 1729 LYS A CG    1 
ATOM   1565  C  CD    . LYS A 1 1729 ? 153.412 175.726 102.570 1.00 73.40  ? 1729 LYS A CD    1 
ATOM   1566  C  CE    . LYS A 1 1729 ? 151.956 176.163 102.535 1.00 84.34  ? 1729 LYS A CE    1 
ATOM   1567  N  NZ    . LYS A 1 1729 ? 151.617 176.878 101.273 1.00 78.99  ? 1729 LYS A NZ    1 
ATOM   1568  N  N     . ALA A 1 1730 ? 157.538 179.498 103.549 1.00 58.11  ? 1730 ALA A N     1 
ATOM   1569  C  CA    . ALA A 1 1730 ? 157.778 180.692 102.753 1.00 56.08  ? 1730 ALA A CA    1 
ATOM   1570  C  C     . ALA A 1 1730 ? 159.257 181.040 102.796 1.00 57.80  ? 1730 ALA A C     1 
ATOM   1571  O  O     . ALA A 1 1730 ? 159.898 180.937 103.847 1.00 50.68  ? 1730 ALA A O     1 
ATOM   1572  C  CB    . ALA A 1 1730 ? 156.945 181.876 103.256 1.00 44.03  ? 1730 ALA A CB    1 
ATOM   1573  N  N     . THR A 1 1731 ? 159.798 181.442 101.644 1.00 62.11  ? 1731 THR A N     1 
ATOM   1574  C  CA    . THR A 1 1731 ? 161.211 181.803 101.577 1.00 58.44  ? 1731 THR A CA    1 
ATOM   1575  C  C     . THR A 1 1731 ? 161.502 183.065 102.380 1.00 51.89  ? 1731 THR A C     1 
ATOM   1576  O  O     . THR A 1 1731 ? 162.528 183.149 103.064 1.00 57.82  ? 1731 THR A O     1 
ATOM   1577  C  CB    . THR A 1 1731 ? 161.640 181.985 100.122 1.00 60.64  ? 1731 THR A CB    1 
ATOM   1578  O  OG1   . THR A 1 1731 ? 160.940 183.096 99.549  1.00 63.95  ? 1731 THR A OG1   1 
ATOM   1579  C  CG2   . THR A 1 1731 ? 161.337 180.731 99.318  1.00 50.64  ? 1731 THR A CG2   1 
ATOM   1580  N  N     . SER A 1 1732 ? 160.616 184.055 102.311 1.00 44.78  ? 1732 SER A N     1 
ATOM   1581  C  CA    . SER A 1 1732 ? 160.790 185.309 103.025 1.00 48.21  ? 1732 SER A CA    1 
ATOM   1582  C  C     . SER A 1 1732 ? 159.496 185.680 103.733 1.00 49.83  ? 1732 SER A C     1 
ATOM   1583  O  O     . SER A 1 1732 ? 158.403 185.295 103.308 1.00 50.46  ? 1732 SER A O     1 
ATOM   1584  C  CB    . SER A 1 1732 ? 161.214 186.442 102.080 1.00 53.48  ? 1732 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 1732 ? 161.461 187.638 102.797 1.00 56.70  ? 1732 SER A OG    1 
ATOM   1586  N  N     . ILE A 1 1733 ? 159.630 186.434 104.820 1.00 47.32  ? 1733 ILE A N     1 
ATOM   1587  C  CA    . ILE A 1 1733 ? 158.506 186.831 105.658 1.00 43.61  ? 1733 ILE A CA    1 
ATOM   1588  C  C     . ILE A 1 1733 ? 158.447 188.350 105.694 1.00 44.12  ? 1733 ILE A C     1 
ATOM   1589  O  O     . ILE A 1 1733 ? 159.448 189.008 106.001 1.00 44.99  ? 1733 ILE A O     1 
ATOM   1590  C  CB    . ILE A 1 1733 ? 158.629 186.255 107.080 1.00 42.92  ? 1733 ILE A CB    1 
ATOM   1591  C  CG1   . ILE A 1 1733 ? 158.449 184.736 107.057 1.00 36.53  ? 1733 ILE A CG1   1 
ATOM   1592  C  CG2   . ILE A 1 1733 ? 157.619 186.909 108.014 1.00 36.03  ? 1733 ILE A CG2   1 
ATOM   1593  C  CD1   . ILE A 1 1733 ? 158.219 184.124 108.418 1.00 33.73  ? 1733 ILE A CD1   1 
ATOM   1594  N  N     . ASP A 1 1734 ? 157.281 188.902 105.380 1.00 44.46  ? 1734 ASP A N     1 
ATOM   1595  C  CA    . ASP A 1 1734 ? 157.078 190.340 105.480 1.00 44.82  ? 1734 ASP A CA    1 
ATOM   1596  C  C     . ASP A 1 1734 ? 156.932 190.728 106.945 1.00 46.82  ? 1734 ASP A C     1 
ATOM   1597  O  O     . ASP A 1 1734 ? 156.044 190.202 107.626 1.00 43.05  ? 1734 ASP A O     1 
ATOM   1598  C  CB    . ASP A 1 1734 ? 155.841 190.761 104.698 1.00 45.35  ? 1734 ASP A CB    1 
ATOM   1599  C  CG    . ASP A 1 1734 ? 155.731 192.266 104.543 1.00 55.95  ? 1734 ASP A CG    1 
ATOM   1600  O  OD1   . ASP A 1 1734 ? 156.764 192.956 104.666 1.00 54.21  ? 1734 ASP A OD1   1 
ATOM   1601  O  OD2   . ASP A 1 1734 ? 154.610 192.759 104.301 1.00 57.72  ? 1734 ASP A OD2   1 
ATOM   1602  N  N     . PRO A 1 1735 ? 157.775 191.619 107.472 1.00 44.89  ? 1735 PRO A N     1 
ATOM   1603  C  CA    . PRO A 1 1735 ? 157.641 192.001 108.886 1.00 42.86  ? 1735 PRO A CA    1 
ATOM   1604  C  C     . PRO A 1 1735 ? 156.290 192.601 109.232 1.00 43.12  ? 1735 PRO A C     1 
ATOM   1605  O  O     . PRO A 1 1735 ? 155.782 192.355 110.332 1.00 43.99  ? 1735 PRO A O     1 
ATOM   1606  C  CB    . PRO A 1 1735 ? 158.775 193.017 109.081 1.00 40.96  ? 1735 PRO A CB    1 
ATOM   1607  C  CG    . PRO A 1 1735 ? 159.765 192.685 108.021 1.00 37.77  ? 1735 PRO A CG    1 
ATOM   1608  C  CD    . PRO A 1 1735 ? 158.963 192.221 106.845 1.00 39.02  ? 1735 PRO A CD    1 
ATOM   1609  N  N     . ASN A 1 1736 ? 155.687 193.373 108.325 1.00 46.29  ? 1736 ASN A N     1 
ATOM   1610  C  CA    . ASN A 1 1736 ? 154.419 194.028 108.635 1.00 48.99  ? 1736 ASN A CA    1 
ATOM   1611  C  C     . ASN A 1 1736 ? 153.313 193.007 108.870 1.00 39.38  ? 1736 ASN A C     1 
ATOM   1612  O  O     . ASN A 1 1736 ? 152.559 193.104 109.845 1.00 37.06  ? 1736 ASN A O     1 
ATOM   1613  C  CB    . ASN A 1 1736 ? 154.038 194.989 107.509 1.00 53.31  ? 1736 ASN A CB    1 
ATOM   1614  C  CG    . ASN A 1 1736 ? 155.187 195.885 107.096 1.00 50.45  ? 1736 ASN A CG    1 
ATOM   1615  O  OD1   . ASN A 1 1736 ? 155.967 196.340 107.932 1.00 42.10  ? 1736 ASN A OD1   1 
ATOM   1616  N  ND2   . ASN A 1 1736 ? 155.297 196.145 105.798 1.00 57.62  ? 1736 ASN A ND2   1 
ATOM   1617  N  N     . THR A 1 1737 ? 153.205 192.013 107.985 1.00 38.41  ? 1737 THR A N     1 
ATOM   1618  C  CA    . THR A 1 1737 ? 152.175 190.991 108.142 1.00 41.62  ? 1737 THR A CA    1 
ATOM   1619  C  C     . THR A 1 1737 ? 152.411 190.153 109.392 1.00 38.07  ? 1737 THR A C     1 
ATOM   1620  O  O     . THR A 1 1737 ? 151.457 189.785 110.089 1.00 36.14  ? 1737 THR A O     1 
ATOM   1621  C  CB    . THR A 1 1737 ? 152.124 190.101 106.901 1.00 43.25  ? 1737 THR A CB    1 
ATOM   1622  O  OG1   . THR A 1 1737 ? 153.382 189.438 106.734 1.00 53.77  ? 1737 THR A OG1   1 
ATOM   1623  C  CG2   . THR A 1 1737 ? 151.829 190.933 105.665 1.00 41.62  ? 1737 THR A CG2   1 
ATOM   1624  N  N     . TYR A 1 1738 ? 153.673 189.836 109.688 1.00 35.59  ? 1738 TYR A N     1 
ATOM   1625  C  CA    . TYR A 1 1738 ? 153.981 189.067 110.889 1.00 28.94  ? 1738 TYR A CA    1 
ATOM   1626  C  C     . TYR A 1 1738 ? 153.605 189.834 112.152 1.00 29.34  ? 1738 TYR A C     1 
ATOM   1627  O  O     . TYR A 1 1738 ? 153.026 189.263 113.084 1.00 32.57  ? 1738 TYR A O     1 
ATOM   1628  C  CB    . TYR A 1 1738 ? 155.463 188.694 110.905 1.00 28.15  ? 1738 TYR A CB    1 
ATOM   1629  C  CG    . TYR A 1 1738 ? 155.770 187.470 111.732 1.00 26.93  ? 1738 TYR A CG    1 
ATOM   1630  C  CD1   . TYR A 1 1738 ? 155.372 186.208 111.313 1.00 32.42  ? 1738 TYR A CD1   1 
ATOM   1631  C  CD2   . TYR A 1 1738 ? 156.450 187.574 112.935 1.00 21.76  ? 1738 TYR A CD2   1 
ATOM   1632  C  CE1   . TYR A 1 1738 ? 155.647 185.086 112.067 1.00 27.92  ? 1738 TYR A CE1   1 
ATOM   1633  C  CE2   . TYR A 1 1738 ? 156.729 186.459 113.695 1.00 18.87  ? 1738 TYR A CE2   1 
ATOM   1634  C  CZ    . TYR A 1 1738 ? 156.326 185.218 113.258 1.00 20.53  ? 1738 TYR A CZ    1 
ATOM   1635  O  OH    . TYR A 1 1738 ? 156.603 184.105 114.016 1.00 22.92  ? 1738 TYR A OH    1 
ATOM   1636  N  N     . ILE A 1 1739 ? 153.919 191.131 112.201 1.00 22.41  ? 1739 ILE A N     1 
ATOM   1637  C  CA    . ILE A 1 1739 ? 153.553 191.932 113.366 1.00 23.90  ? 1739 ILE A CA    1 
ATOM   1638  C  C     . ILE A 1 1739 ? 152.039 192.072 113.466 1.00 27.99  ? 1739 ILE A C     1 
ATOM   1639  O  O     . ILE A 1 1739 ? 151.474 192.068 114.566 1.00 32.11  ? 1739 ILE A O     1 
ATOM   1640  C  CB    . ILE A 1 1739 ? 154.255 193.302 113.321 1.00 28.59  ? 1739 ILE A CB    1 
ATOM   1641  C  CG1   . ILE A 1 1739 ? 155.774 193.125 113.309 1.00 29.84  ? 1739 ILE A CG1   1 
ATOM   1642  C  CG2   . ILE A 1 1739 ? 153.840 194.160 114.503 1.00 30.58  ? 1739 ILE A CG2   1 
ATOM   1643  C  CD1   . ILE A 1 1739 ? 156.318 192.428 114.532 1.00 27.70  ? 1739 ILE A CD1   1 
ATOM   1644  N  N     . THR A 1 1740 ? 151.357 192.193 112.325 1.00 26.49  ? 1740 THR A N     1 
ATOM   1645  C  CA    . THR A 1 1740 ? 149.899 192.252 112.340 1.00 27.66  ? 1740 THR A CA    1 
ATOM   1646  C  C     . THR A 1 1740 ? 149.304 190.973 112.916 1.00 26.83  ? 1740 THR A C     1 
ATOM   1647  O  O     . THR A 1 1740 ? 148.379 191.022 113.736 1.00 31.30  ? 1740 THR A O     1 
ATOM   1648  C  CB    . THR A 1 1740 ? 149.373 192.502 110.926 1.00 32.97  ? 1740 THR A CB    1 
ATOM   1649  O  OG1   . THR A 1 1740 ? 149.743 193.821 110.504 1.00 27.30  ? 1740 THR A OG1   1 
ATOM   1650  C  CG2   . THR A 1 1740 ? 147.859 192.366 110.881 1.00 31.63  ? 1740 THR A CG2   1 
ATOM   1651  N  N     . TRP A 1 1741 ? 149.833 189.818 112.508 1.00 24.03  ? 1741 TRP A N     1 
ATOM   1652  C  CA    . TRP A 1 1741 ? 149.352 188.548 113.040 1.00 19.93  ? 1741 TRP A CA    1 
ATOM   1653  C  C     . TRP A 1 1741 ? 149.654 188.417 114.528 1.00 22.90  ? 1741 TRP A C     1 
ATOM   1654  O  O     . TRP A 1 1741 ? 148.832 187.893 115.289 1.00 23.98  ? 1741 TRP A O     1 
ATOM   1655  C  CB    . TRP A 1 1741 ? 149.969 187.389 112.263 1.00 21.18  ? 1741 TRP A CB    1 
ATOM   1656  C  CG    . TRP A 1 1741 ? 149.828 186.057 112.932 1.00 25.88  ? 1741 TRP A CG    1 
ATOM   1657  C  CD1   . TRP A 1 1741 ? 148.725 185.256 112.937 1.00 28.43  ? 1741 TRP A CD1   1 
ATOM   1658  C  CD2   . TRP A 1 1741 ? 150.829 185.365 113.688 1.00 22.96  ? 1741 TRP A CD2   1 
ATOM   1659  N  NE1   . TRP A 1 1741 ? 148.974 184.112 113.653 1.00 28.26  ? 1741 TRP A NE1   1 
ATOM   1660  C  CE2   . TRP A 1 1741 ? 150.260 184.154 114.125 1.00 21.18  ? 1741 TRP A CE2   1 
ATOM   1661  C  CE3   . TRP A 1 1741 ? 152.151 185.654 114.040 1.00 23.55  ? 1741 TRP A CE3   1 
ATOM   1662  C  CZ2   . TRP A 1 1741 ? 150.965 183.233 114.894 1.00 23.71  ? 1741 TRP A CZ2   1 
ATOM   1663  C  CZ3   . TRP A 1 1741 ? 152.848 184.739 114.805 1.00 21.81  ? 1741 TRP A CZ3   1 
ATOM   1664  C  CH2   . TRP A 1 1741 ? 152.255 183.543 115.223 1.00 21.58  ? 1741 TRP A CH2   1 
ATOM   1665  N  N     . ILE A 1 1742 ? 150.830 188.878 114.959 1.00 22.69  ? 1742 ILE A N     1 
ATOM   1666  C  CA    . ILE A 1 1742 ? 151.171 188.829 116.378 1.00 21.69  ? 1742 ILE A CA    1 
ATOM   1667  C  C     . ILE A 1 1742 ? 150.205 189.683 117.187 1.00 25.78  ? 1742 ILE A C     1 
ATOM   1668  O  O     . ILE A 1 1742 ? 149.722 189.269 118.248 1.00 27.30  ? 1742 ILE A O     1 
ATOM   1669  C  CB    . ILE A 1 1742 ? 152.631 189.270 116.590 1.00 24.94  ? 1742 ILE A CB    1 
ATOM   1670  C  CG1   . ILE A 1 1742 ? 153.592 188.202 116.070 1.00 28.46  ? 1742 ILE A CG1   1 
ATOM   1671  C  CG2   . ILE A 1 1742 ? 152.900 189.547 118.060 1.00 19.75  ? 1742 ILE A CG2   1 
ATOM   1672  C  CD1   . ILE A 1 1742 ? 155.037 188.641 116.065 1.00 28.78  ? 1742 ILE A CD1   1 
ATOM   1673  N  N     . ASP A 1 1743 ? 149.901 190.886 116.696 1.00 25.16  ? 1743 ASP A N     1 
ATOM   1674  C  CA    . ASP A 1 1743 ? 148.970 191.762 117.398 1.00 25.99  ? 1743 ASP A CA    1 
ATOM   1675  C  C     . ASP A 1 1743 ? 147.554 191.204 117.395 1.00 23.37  ? 1743 ASP A C     1 
ATOM   1676  O  O     . ASP A 1 1743 ? 146.802 191.421 118.353 1.00 22.92  ? 1743 ASP A O     1 
ATOM   1677  C  CB    . ASP A 1 1743 ? 148.987 193.155 116.771 1.00 22.77  ? 1743 ASP A CB    1 
ATOM   1678  C  CG    . ASP A 1 1743 ? 150.123 194.010 117.284 1.00 27.76  ? 1743 ASP A CG    1 
ATOM   1679  O  OD1   . ASP A 1 1743 ? 150.681 193.680 118.351 1.00 35.47  ? 1743 ASP A OD1   1 
ATOM   1680  O  OD2   . ASP A 1 1743 ? 150.460 195.013 116.621 1.00 31.29  ? 1743 ASP A OD2   1 
ATOM   1681  N  N     . LYS A 1 1744 ? 147.171 190.495 116.332 1.00 22.71  ? 1744 LYS A N     1 
ATOM   1682  C  CA    . LYS A 1 1744 ? 145.796 190.019 116.211 1.00 19.85  ? 1744 LYS A CA    1 
ATOM   1683  C  C     . LYS A 1 1744 ? 145.452 189.001 117.292 1.00 22.59  ? 1744 LYS A C     1 
ATOM   1684  O  O     . LYS A 1 1744 ? 144.354 189.040 117.858 1.00 22.11  ? 1744 LYS A O     1 
ATOM   1685  C  CB    . LYS A 1 1744 ? 145.574 189.423 114.822 1.00 17.27  ? 1744 LYS A CB    1 
ATOM   1686  C  CG    . LYS A 1 1744 ? 144.172 188.888 114.589 1.00 19.37  ? 1744 LYS A CG    1 
ATOM   1687  C  CD    . LYS A 1 1744 ? 143.914 188.654 113.111 1.00 28.28  ? 1744 LYS A CD    1 
ATOM   1688  C  CE    . LYS A 1 1744 ? 142.550 188.031 112.880 1.00 28.78  ? 1744 LYS A CE    1 
ATOM   1689  N  NZ    . LYS A 1 1744 ? 141.475 188.773 113.594 1.00 26.05  ? 1744 LYS A NZ    1 
ATOM   1690  N  N     . TYR A 1 1745 ? 146.370 188.092 117.596 1.00 23.02  ? 1745 TYR A N     1 
ATOM   1691  C  CA    . TYR A 1 1745 ? 146.077 186.950 118.447 1.00 15.04  ? 1745 TYR A CA    1 
ATOM   1692  C  C     . TYR A 1 1745 ? 146.768 187.079 119.798 1.00 16.93  ? 1745 TYR A C     1 
ATOM   1693  O  O     . TYR A 1 1745 ? 147.696 187.870 119.979 1.00 23.25  ? 1745 TYR A O     1 
ATOM   1694  C  CB    . TYR A 1 1745 ? 146.495 185.647 117.760 1.00 15.32  ? 1745 TYR A CB    1 
ATOM   1695  C  CG    . TYR A 1 1745 ? 145.707 185.370 116.504 1.00 17.65  ? 1745 TYR A CG    1 
ATOM   1696  C  CD1   . TYR A 1 1745 ? 144.398 184.913 116.568 1.00 18.90  ? 1745 TYR A CD1   1 
ATOM   1697  C  CD2   . TYR A 1 1745 ? 146.266 185.584 115.253 1.00 15.83  ? 1745 TYR A CD2   1 
ATOM   1698  C  CE1   . TYR A 1 1745 ? 143.673 184.668 115.421 1.00 21.00  ? 1745 TYR A CE1   1 
ATOM   1699  C  CE2   . TYR A 1 1745 ? 145.549 185.342 114.101 1.00 22.46  ? 1745 TYR A CE2   1 
ATOM   1700  C  CZ    . TYR A 1 1745 ? 144.253 184.884 114.191 1.00 26.29  ? 1745 TYR A CZ    1 
ATOM   1701  O  OH    . TYR A 1 1745 ? 143.536 184.641 113.043 1.00 30.06  ? 1745 TYR A OH    1 
ATOM   1702  N  N     . GLN A 1 1746 ? 146.295 186.276 120.747 1.00 17.74  ? 1746 GLN A N     1 
ATOM   1703  C  CA    . GLN A 1 1746 ? 146.788 186.312 122.113 1.00 14.65  ? 1746 GLN A CA    1 
ATOM   1704  C  C     . GLN A 1 1746 ? 148.199 185.736 122.199 1.00 14.55  ? 1746 GLN A C     1 
ATOM   1705  O  O     . GLN A 1 1746 ? 148.660 185.009 121.314 1.00 17.50  ? 1746 GLN A O     1 
ATOM   1706  C  CB    . GLN A 1 1746 ? 145.845 185.536 123.034 1.00 13.84  ? 1746 GLN A CB    1 
ATOM   1707  C  CG    . GLN A 1 1746 ? 144.570 186.285 123.396 1.00 21.56  ? 1746 GLN A CG    1 
ATOM   1708  C  CD    . GLN A 1 1746 ? 143.551 186.289 122.272 1.00 20.66  ? 1746 GLN A CD    1 
ATOM   1709  O  OE1   . GLN A 1 1746 ? 143.707 185.588 121.274 1.00 20.05  ? 1746 GLN A OE1   1 
ATOM   1710  N  NE2   . GLN A 1 1746 ? 142.499 187.084 122.430 1.00 16.94  ? 1746 GLN A NE2   1 
ATOM   1711  N  N     . ALA A 1 1747 ? 148.889 186.075 123.292 1.00 15.87  ? 1747 ALA A N     1 
ATOM   1712  C  CA    . ALA A 1 1747 ? 150.266 185.625 123.478 1.00 12.62  ? 1747 ALA A CA    1 
ATOM   1713  C  C     . ALA A 1 1747 ? 150.346 184.107 123.578 1.00 15.03  ? 1747 ALA A C     1 
ATOM   1714  O  O     . ALA A 1 1747 ? 151.298 183.493 123.084 1.00 17.87  ? 1747 ALA A O     1 
ATOM   1715  C  CB    . ALA A 1 1747 ? 150.866 186.278 124.723 1.00 11.63  ? 1747 ALA A CB    1 
ATOM   1716  N  N     . GLN A 1 1748 ? 149.365 183.488 124.235 1.00 14.52  ? 1748 GLN A N     1 
ATOM   1717  C  CA    . GLN A 1 1748 ? 149.287 182.032 124.270 1.00 12.84  ? 1748 GLN A CA    1 
ATOM   1718  C  C     . GLN A 1 1748 ? 149.142 181.456 122.867 1.00 14.69  ? 1748 GLN A C     1 
ATOM   1719  O  O     . GLN A 1 1748 ? 149.862 180.520 122.484 1.00 16.97  ? 1748 GLN A O     1 
ATOM   1720  C  CB    . GLN A 1 1748 ? 148.104 181.618 125.143 1.00 10.32  ? 1748 GLN A CB    1 
ATOM   1721  C  CG    . GLN A 1 1748 ? 147.917 180.132 125.345 1.00 13.46  ? 1748 GLN A CG    1 
ATOM   1722  C  CD    . GLN A 1 1748 ? 146.743 179.831 126.256 1.00 16.42  ? 1748 GLN A CD    1 
ATOM   1723  O  OE1   . GLN A 1 1748 ? 146.047 180.740 126.707 1.00 11.71  ? 1748 GLN A OE1   1 
ATOM   1724  N  NE2   . GLN A 1 1748 ? 146.512 178.554 126.528 1.00 15.57  ? 1748 GLN A NE2   1 
ATOM   1725  N  N     . LEU A 1 1749 ? 148.237 182.031 122.076 1.00 14.54  ? 1749 LEU A N     1 
ATOM   1726  C  CA    . LEU A 1 1749 ? 147.854 181.421 120.812 1.00 13.28  ? 1749 LEU A CA    1 
ATOM   1727  C  C     . LEU A 1 1749 ? 148.928 181.580 119.747 1.00 13.29  ? 1749 LEU A C     1 
ATOM   1728  O  O     . LEU A 1 1749 ? 149.087 180.691 118.909 1.00 18.49  ? 1749 LEU A O     1 
ATOM   1729  C  CB    . LEU A 1 1749 ? 146.532 182.015 120.333 1.00 16.56  ? 1749 LEU A CB    1 
ATOM   1730  C  CG    . LEU A 1 1749 ? 145.358 181.710 121.263 1.00 14.67  ? 1749 LEU A CG    1 
ATOM   1731  C  CD1   . LEU A 1 1749 ? 144.088 182.344 120.742 1.00 17.52  ? 1749 LEU A CD1   1 
ATOM   1732  C  CD2   . LEU A 1 1749 ? 145.185 180.212 121.438 1.00 15.48  ? 1749 LEU A CD2   1 
ATOM   1733  N  N     . VAL A 1 1750 ? 149.670 182.690 119.751 1.00 10.85  ? 1750 VAL A N     1 
ATOM   1734  C  CA    . VAL A 1 1750 ? 150.721 182.856 118.751 1.00 13.65  ? 1750 VAL A CA    1 
ATOM   1735  C  C     . VAL A 1 1750 ? 151.820 181.819 118.953 1.00 11.91  ? 1750 VAL A C     1 
ATOM   1736  O  O     . VAL A 1 1750 ? 152.290 181.197 117.991 1.00 16.67  ? 1750 VAL A O     1 
ATOM   1737  C  CB    . VAL A 1 1750 ? 151.274 184.295 118.769 1.00 14.31  ? 1750 VAL A CB    1 
ATOM   1738  C  CG1   . VAL A 1 1750 ? 150.250 185.261 118.200 1.00 17.20  ? 1750 VAL A CG1   1 
ATOM   1739  C  CG2   . VAL A 1 1750 ? 151.675 184.714 120.169 1.00 13.66  ? 1750 VAL A CG2   1 
ATOM   1740  N  N     . VAL A 1 1751 ? 152.234 181.601 120.203 1.00 8.22   ? 1751 VAL A N     1 
ATOM   1741  C  CA    . VAL A 1 1751 ? 153.244 180.588 120.487 1.00 9.67   ? 1751 VAL A CA    1 
ATOM   1742  C  C     . VAL A 1 1751 ? 152.713 179.198 120.163 1.00 8.72   ? 1751 VAL A C     1 
ATOM   1743  O  O     . VAL A 1 1751 ? 153.423 178.369 119.578 1.00 9.53   ? 1751 VAL A O     1 
ATOM   1744  C  CB    . VAL A 1 1751 ? 153.709 180.693 121.950 1.00 9.91   ? 1751 VAL A CB    1 
ATOM   1745  C  CG1   . VAL A 1 1751 ? 154.831 179.706 122.223 1.00 6.44   ? 1751 VAL A CG1   1 
ATOM   1746  C  CG2   . VAL A 1 1751 ? 154.159 182.110 122.256 1.00 10.58  ? 1751 VAL A CG2   1 
ATOM   1747  N  N     . LEU A 1 1752 ? 151.458 178.919 120.531 1.00 8.76   ? 1752 LEU A N     1 
ATOM   1748  C  CA    . LEU A 1 1752 ? 150.882 177.614 120.224 1.00 8.21   ? 1752 LEU A CA    1 
ATOM   1749  C  C     . LEU A 1 1752 ? 150.835 177.370 118.719 1.00 11.39  ? 1752 LEU A C     1 
ATOM   1750  O  O     . LEU A 1 1752 ? 151.162 176.275 118.248 1.00 12.71  ? 1752 LEU A O     1 
ATOM   1751  C  CB    . LEU A 1 1752 ? 149.485 177.507 120.834 1.00 7.68   ? 1752 LEU A CB    1 
ATOM   1752  C  CG    . LEU A 1 1752 ? 148.947 176.104 121.118 1.00 8.20   ? 1752 LEU A CG    1 
ATOM   1753  C  CD1   . LEU A 1 1752 ? 149.912 175.326 121.993 1.00 6.81   ? 1752 LEU A CD1   1 
ATOM   1754  C  CD2   . LEU A 1 1752 ? 147.585 176.192 121.773 1.00 9.55   ? 1752 LEU A CD2   1 
ATOM   1755  N  N     . SER A 1 1753 ? 150.442 178.386 117.949 1.00 10.07  ? 1753 SER A N     1 
ATOM   1756  C  CA    . SER A 1 1753 ? 150.357 178.247 116.500 1.00 9.90   ? 1753 SER A CA    1 
ATOM   1757  C  C     . SER A 1 1753 ? 151.733 178.069 115.878 1.00 10.94  ? 1753 SER A C     1 
ATOM   1758  O  O     . SER A 1 1753 ? 151.893 177.288 114.934 1.00 10.16  ? 1753 SER A O     1 
ATOM   1759  C  CB    . SER A 1 1753 ? 149.654 179.464 115.904 1.00 14.60  ? 1753 SER A CB    1 
ATOM   1760  O  OG    . SER A 1 1753 ? 148.357 179.610 116.449 1.00 22.79  ? 1753 SER A OG    1 
ATOM   1761  N  N     . ALA A 1 1754 ? 152.735 178.796 116.378 1.00 10.04  ? 1754 ALA A N     1 
ATOM   1762  C  CA    . ALA A 1 1754 ? 154.092 178.609 115.877 1.00 6.14   ? 1754 ALA A CA    1 
ATOM   1763  C  C     . ALA A 1 1754 ? 154.579 177.192 116.140 1.00 9.20   ? 1754 ALA A C     1 
ATOM   1764  O  O     . ALA A 1 1754 ? 155.185 176.560 115.264 1.00 15.99  ? 1754 ALA A O     1 
ATOM   1765  C  CB    . ALA A 1 1754 ? 155.033 179.630 116.513 1.00 6.81   ? 1754 ALA A CB    1 
ATOM   1766  N  N     . GLN A 1 1755 ? 154.312 176.670 117.341 1.00 9.10   ? 1755 GLN A N     1 
ATOM   1767  C  CA    . GLN A 1 1755 ? 154.692 175.294 117.648 1.00 7.96   ? 1755 GLN A CA    1 
ATOM   1768  C  C     . GLN A 1 1755 ? 153.982 174.306 116.732 1.00 8.54   ? 1755 GLN A C     1 
ATOM   1769  O  O     . GLN A 1 1755 ? 154.600 173.360 116.230 1.00 10.62  ? 1755 GLN A O     1 
ATOM   1770  C  CB    . GLN A 1 1755 ? 154.391 174.979 119.112 1.00 5.57   ? 1755 GLN A CB    1 
ATOM   1771  C  CG    . GLN A 1 1755 ? 155.216 175.779 120.096 1.00 5.04   ? 1755 GLN A CG    1 
ATOM   1772  C  CD    . GLN A 1 1755 ? 154.792 175.560 121.530 1.00 5.81   ? 1755 GLN A CD    1 
ATOM   1773  O  OE1   . GLN A 1 1755 ? 153.613 175.668 121.864 1.00 7.18   ? 1755 GLN A OE1   1 
ATOM   1774  N  NE2   . GLN A 1 1755 ? 155.755 175.258 122.391 1.00 5.41   ? 1755 GLN A NE2   1 
ATOM   1775  N  N     . ILE A 1 1756 ? 152.683 174.510 116.500 1.00 7.38   ? 1756 ILE A N     1 
ATOM   1776  C  CA    . ILE A 1 1756 ? 151.927 173.602 115.640 1.00 7.90   ? 1756 ILE A CA    1 
ATOM   1777  C  C     . ILE A 1 1756 ? 152.475 173.627 114.220 1.00 12.39  ? 1756 ILE A C     1 
ATOM   1778  O  O     . ILE A 1 1756 ? 152.662 172.578 113.591 1.00 16.55  ? 1756 ILE A O     1 
ATOM   1779  C  CB    . ILE A 1 1756 ? 150.428 173.957 115.671 1.00 9.23   ? 1756 ILE A CB    1 
ATOM   1780  C  CG1   . ILE A 1 1756 ? 149.834 173.667 117.048 1.00 12.26  ? 1756 ILE A CG1   1 
ATOM   1781  C  CG2   . ILE A 1 1756 ? 149.674 173.187 114.599 1.00 13.43  ? 1756 ILE A CG2   1 
ATOM   1782  C  CD1   . ILE A 1 1756 ? 148.452 174.240 117.243 1.00 13.65  ? 1756 ILE A CD1   1 
ATOM   1783  N  N     . ALA A 1 1757 ? 152.740 174.824 113.692 1.00 9.93   ? 1757 ALA A N     1 
ATOM   1784  C  CA    . ALA A 1 1757 ? 153.244 174.939 112.328 1.00 10.16  ? 1757 ALA A CA    1 
ATOM   1785  C  C     . ALA A 1 1757 ? 154.619 174.301 112.190 1.00 11.99  ? 1757 ALA A C     1 
ATOM   1786  O  O     . ALA A 1 1757 ? 154.888 173.597 111.209 1.00 16.98  ? 1757 ALA A O     1 
ATOM   1787  C  CB    . ALA A 1 1757 ? 153.287 176.407 111.907 1.00 17.03  ? 1757 ALA A CB    1 
ATOM   1788  N  N     . TRP A 1 1758 ? 155.504 174.531 113.163 1.00 10.20  ? 1758 TRP A N     1 
ATOM   1789  C  CA    . TRP A 1 1758 ? 156.829 173.927 113.098 1.00 9.79   ? 1758 TRP A CA    1 
ATOM   1790  C  C     . TRP A 1 1758 ? 156.749 172.409 113.193 1.00 12.36  ? 1758 TRP A C     1 
ATOM   1791  O  O     . TRP A 1 1758 ? 157.460 171.697 112.473 1.00 18.57  ? 1758 TRP A O     1 
ATOM   1792  C  CB    . TRP A 1 1758 ? 157.718 174.492 114.203 1.00 8.06   ? 1758 TRP A CB    1 
ATOM   1793  C  CG    . TRP A 1 1758 ? 159.022 173.780 114.339 1.00 7.19   ? 1758 TRP A CG    1 
ATOM   1794  C  CD1   . TRP A 1 1758 ? 160.120 173.924 113.546 1.00 7.89   ? 1758 TRP A CD1   1 
ATOM   1795  C  CD2   . TRP A 1 1758 ? 159.367 172.810 115.331 1.00 6.19   ? 1758 TRP A CD2   1 
ATOM   1796  N  NE1   . TRP A 1 1758 ? 161.129 173.102 113.982 1.00 7.26   ? 1758 TRP A NE1   1 
ATOM   1797  C  CE2   . TRP A 1 1758 ? 160.691 172.407 115.078 1.00 6.69   ? 1758 TRP A CE2   1 
ATOM   1798  C  CE3   . TRP A 1 1758 ? 158.685 172.242 116.411 1.00 6.90   ? 1758 TRP A CE3   1 
ATOM   1799  C  CZ2   . TRP A 1 1758 ? 161.346 171.464 115.862 1.00 7.05   ? 1758 TRP A CZ2   1 
ATOM   1800  C  CZ3   . TRP A 1 1758 ? 159.336 171.307 117.187 1.00 9.47   ? 1758 TRP A CZ3   1 
ATOM   1801  C  CH2   . TRP A 1 1758 ? 160.652 170.927 116.910 1.00 8.54   ? 1758 TRP A CH2   1 
ATOM   1802  N  N     . SER A 1 1759 ? 155.889 171.894 114.077 1.00 10.04  ? 1759 SER A N     1 
ATOM   1803  C  CA    . SER A 1 1759 ? 155.733 170.448 114.193 1.00 11.63  ? 1759 SER A CA    1 
ATOM   1804  C  C     . SER A 1 1759 ? 155.212 169.848 112.896 1.00 16.07  ? 1759 SER A C     1 
ATOM   1805  O  O     . SER A 1 1759 ? 155.699 168.804 112.447 1.00 18.09  ? 1759 SER A O     1 
ATOM   1806  C  CB    . SER A 1 1759 ? 154.795 170.113 115.352 1.00 10.28  ? 1759 SER A CB    1 
ATOM   1807  O  OG    . SER A 1 1759 ? 155.306 170.597 116.581 1.00 12.37  ? 1759 SER A OG    1 
ATOM   1808  N  N     . GLU A 1 1760 ? 154.226 170.500 112.274 1.00 16.99  ? 1760 GLU A N     1 
ATOM   1809  C  CA    . GLU A 1 1760 ? 153.696 170.004 111.009 1.00 15.34  ? 1760 GLU A CA    1 
ATOM   1810  C  C     . GLU A 1 1760 ? 154.757 170.030 109.915 1.00 18.25  ? 1760 GLU A C     1 
ATOM   1811  O  O     . GLU A 1 1760 ? 154.858 169.090 109.118 1.00 25.67  ? 1760 GLU A O     1 
ATOM   1812  C  CB    . GLU A 1 1760 ? 152.475 170.823 110.597 1.00 18.57  ? 1760 GLU A CB    1 
ATOM   1813  C  CG    . GLU A 1 1760 ? 151.241 170.561 111.446 1.00 29.96  ? 1760 GLU A CG    1 
ATOM   1814  C  CD    . GLU A 1 1760 ? 150.026 171.328 110.963 1.00 54.90  ? 1760 GLU A CD    1 
ATOM   1815  O  OE1   . GLU A 1 1760 ? 150.125 172.563 110.809 1.00 43.15  ? 1760 GLU A OE1   1 
ATOM   1816  O  OE2   . GLU A 1 1760 ? 148.972 170.697 110.739 1.00 60.06  ? 1760 GLU A OE2   1 
ATOM   1817  N  N     . ASN A 1 1761 ? 155.558 171.097 109.861 1.00 19.42  ? 1761 ASN A N     1 
ATOM   1818  C  CA    . ASN A 1 1761 ? 156.606 171.186 108.848 1.00 19.04  ? 1761 ASN A CA    1 
ATOM   1819  C  C     . ASN A 1 1761 ? 157.644 170.085 109.031 1.00 20.13  ? 1761 ASN A C     1 
ATOM   1820  O  O     . ASN A 1 1761 ? 158.059 169.437 108.062 1.00 25.23  ? 1761 ASN A O     1 
ATOM   1821  C  CB    . ASN A 1 1761 ? 157.268 172.563 108.900 1.00 17.70  ? 1761 ASN A CB    1 
ATOM   1822  C  CG    . ASN A 1 1761 ? 156.365 173.662 108.386 1.00 18.75  ? 1761 ASN A CG    1 
ATOM   1823  O  OD1   . ASN A 1 1761 ? 155.197 173.428 108.076 1.00 18.70  ? 1761 ASN A OD1   1 
ATOM   1824  N  ND2   . ASN A 1 1761 ? 156.901 174.872 108.293 1.00 26.39  ? 1761 ASN A ND2   1 
ATOM   1825  N  N     . VAL A 1 1762 ? 158.076 169.858 110.274 1.00 20.05  ? 1762 VAL A N     1 
ATOM   1826  C  CA    . VAL A 1 1762 ? 159.067 168.817 110.530 1.00 20.65  ? 1762 VAL A CA    1 
ATOM   1827  C  C     . VAL A 1 1762 ? 158.493 167.443 110.211 1.00 21.40  ? 1762 VAL A C     1 
ATOM   1828  O  O     . VAL A 1 1762 ? 159.178 166.587 109.638 1.00 26.90  ? 1762 VAL A O     1 
ATOM   1829  C  CB    . VAL A 1 1762 ? 159.574 168.898 111.982 1.00 16.15  ? 1762 VAL A CB    1 
ATOM   1830  C  CG1   . VAL A 1 1762 ? 160.513 167.741 112.278 1.00 13.46  ? 1762 VAL A CG1   1 
ATOM   1831  C  CG2   . VAL A 1 1762 ? 160.274 170.221 112.225 1.00 16.09  ? 1762 VAL A CG2   1 
ATOM   1832  N  N     . GLU A 1 1763 ? 157.229 167.208 110.575 1.00 23.65  ? 1763 GLU A N     1 
ATOM   1833  C  CA    . GLU A 1 1763 ? 156.600 165.925 110.284 1.00 24.78  ? 1763 GLU A CA    1 
ATOM   1834  C  C     . GLU A 1 1763 ? 156.500 165.689 108.782 1.00 32.59  ? 1763 GLU A C     1 
ATOM   1835  O  O     . GLU A 1 1763 ? 156.761 164.580 108.302 1.00 36.07  ? 1763 GLU A O     1 
ATOM   1836  C  CB    . GLU A 1 1763 ? 155.217 165.869 110.934 1.00 20.65  ? 1763 GLU A CB    1 
ATOM   1837  C  CG    . GLU A 1 1763 ? 154.473 164.559 110.744 1.00 36.62  ? 1763 GLU A CG    1 
ATOM   1838  C  CD    . GLU A 1 1763 ? 155.156 163.390 111.426 1.00 46.86  ? 1763 GLU A CD    1 
ATOM   1839  O  OE1   . GLU A 1 1763 ? 155.886 163.617 112.414 1.00 40.37  ? 1763 GLU A OE1   1 
ATOM   1840  O  OE2   . GLU A 1 1763 ? 154.958 162.241 110.978 1.00 55.69  ? 1763 GLU A OE2   1 
ATOM   1841  N  N     . THR A 1 1764 ? 156.130 166.723 108.022 1.00 27.32  ? 1764 THR A N     1 
ATOM   1842  C  CA    . THR A 1 1764 ? 156.053 166.589 106.570 1.00 26.48  ? 1764 THR A CA    1 
ATOM   1843  C  C     . THR A 1 1764 ? 157.425 166.318 105.966 1.00 33.05  ? 1764 THR A C     1 
ATOM   1844  O  O     . THR A 1 1764 ? 157.564 165.471 105.073 1.00 41.03  ? 1764 THR A O     1 
ATOM   1845  C  CB    . THR A 1 1764 ? 155.440 167.848 105.959 1.00 30.78  ? 1764 THR A CB    1 
ATOM   1846  O  OG1   . THR A 1 1764 ? 154.134 168.062 106.509 1.00 30.35  ? 1764 THR A OG1   1 
ATOM   1847  C  CG2   . THR A 1 1764 ? 155.332 167.712 104.448 1.00 38.37  ? 1764 THR A CG2   1 
ATOM   1848  N  N     . ALA A 1 1765 ? 158.452 167.026 106.440 1.00 33.42  ? 1765 ALA A N     1 
ATOM   1849  C  CA    . ALA A 1 1765 ? 159.799 166.800 105.927 1.00 28.43  ? 1765 ALA A CA    1 
ATOM   1850  C  C     . ALA A 1 1765 ? 160.270 165.382 106.221 1.00 33.62  ? 1765 ALA A C     1 
ATOM   1851  O  O     . ALA A 1 1765 ? 160.867 164.726 105.359 1.00 39.99  ? 1765 ALA A O     1 
ATOM   1852  C  CB    . ALA A 1 1765 ? 160.766 167.823 106.522 1.00 28.17  ? 1765 ALA A CB    1 
ATOM   1853  N  N     . LEU A 1 1766 ? 160.005 164.888 107.432 1.00 34.31  ? 1766 LEU A N     1 
ATOM   1854  C  CA    . LEU A 1 1766 ? 160.412 163.531 107.780 1.00 32.03  ? 1766 LEU A CA    1 
ATOM   1855  C  C     . LEU A 1 1766 ? 159.634 162.496 106.974 1.00 35.91  ? 1766 LEU A C     1 
ATOM   1856  O  O     . LEU A 1 1766 ? 160.195 161.473 106.564 1.00 35.66  ? 1766 LEU A O     1 
ATOM   1857  C  CB    . LEU A 1 1766 ? 160.233 163.302 109.280 1.00 26.48  ? 1766 LEU A CB    1 
ATOM   1858  C  CG    . LEU A 1 1766 ? 161.214 164.060 110.176 1.00 23.46  ? 1766 LEU A CG    1 
ATOM   1859  C  CD1   . LEU A 1 1766 ? 161.024 163.682 111.634 1.00 19.30  ? 1766 LEU A CD1   1 
ATOM   1860  C  CD2   . LEU A 1 1766 ? 162.647 163.813 109.740 1.00 27.76  ? 1766 LEU A CD2   1 
ATOM   1861  N  N     . SER A 1 1767 ? 158.344 162.742 106.735 1.00 39.00  ? 1767 SER A N     1 
ATOM   1862  C  CA    . SER A 1 1767 ? 157.562 161.830 105.907 1.00 38.26  ? 1767 SER A CA    1 
ATOM   1863  C  C     . SER A 1 1767 ? 158.102 161.784 104.485 1.00 48.23  ? 1767 SER A C     1 
ATOM   1864  O  O     . SER A 1 1767 ? 158.148 160.716 103.864 1.00 61.79  ? 1767 SER A O     1 
ATOM   1865  C  CB    . SER A 1 1767 ? 156.092 162.246 105.912 1.00 36.09  ? 1767 SER A CB    1 
ATOM   1866  O  OG    . SER A 1 1767 ? 155.570 162.254 107.229 1.00 53.74  ? 1767 SER A OG    1 
ATOM   1867  N  N     . SER A 1 1768 ? 158.507 162.937 103.948 1.00 41.85  ? 1768 SER A N     1 
ATOM   1868  C  CA    . SER A 1 1768 ? 159.125 162.954 102.626 1.00 35.69  ? 1768 SER A CA    1 
ATOM   1869  C  C     . SER A 1 1768 ? 160.453 162.206 102.626 1.00 44.91  ? 1768 SER A C     1 
ATOM   1870  O  O     . SER A 1 1768 ? 160.748 161.451 101.693 1.00 51.00  ? 1768 SER A O     1 
ATOM   1871  C  CB    . SER A 1 1768 ? 159.324 164.395 102.159 1.00 37.55  ? 1768 SER A CB    1 
ATOM   1872  O  OG    . SER A 1 1768 ? 160.267 165.067 102.975 1.00 53.97  ? 1768 SER A OG    1 
ATOM   1873  N  N     . MET A 1 1769 ? 161.264 162.397 103.668 1.00 44.19  ? 1769 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1769 ? 162.596 161.805 103.724 1.00 44.79  ? 1769 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1769 ? 162.586 160.336 104.123 1.00 52.44  ? 1769 MET A C     1 
ATOM   1876  O  O     . MET A 1 1769 ? 163.636 159.687 104.052 1.00 57.75  ? 1769 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1769 ? 163.475 162.590 104.700 1.00 41.15  ? 1769 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1769 ? 163.899 163.948 104.180 1.00 48.19  ? 1769 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1769 ? 164.717 164.985 105.408 1.00 57.93  ? 1769 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1769 ? 165.548 163.756 106.404 1.00 38.81  ? 1769 MET A CE    1 
ATOM   1881  N  N     . GLY A 1 1770 ? 161.442 159.803 104.548 1.00 60.41  ? 1770 GLY A N     1 
ATOM   1882  C  CA    . GLY A 1 1770 ? 161.338 158.411 104.949 1.00 63.19  ? 1770 GLY A CA    1 
ATOM   1883  C  C     . GLY A 1 1770 ? 161.807 157.384 103.936 1.00 74.73  ? 1770 GLY A C     1 
ATOM   1884  O  O     . GLY A 1 1770 ? 161.935 156.201 104.267 1.00 76.65  ? 1770 GLY A O     1 
ATOM   1885  N  N     . GLY A 1 1771 ? 162.064 157.813 102.699 1.00 73.68  ? 1771 GLY A N     1 
ATOM   1886  C  CA    . GLY A 1 1771 ? 162.595 156.904 101.699 1.00 76.85  ? 1771 GLY A CA    1 
ATOM   1887  C  C     . GLY A 1 1771 ? 164.022 156.471 101.958 1.00 83.32  ? 1771 GLY A C     1 
ATOM   1888  O  O     . GLY A 1 1771 ? 164.435 155.413 101.471 1.00 83.88  ? 1771 GLY A O     1 
ATOM   1889  N  N     . GLY A 1 1772 ? 164.782 157.261 102.711 1.00 85.28  ? 1772 GLY A N     1 
ATOM   1890  C  CA    . GLY A 1 1772 ? 166.149 156.912 103.044 1.00 81.31  ? 1772 GLY A CA    1 
ATOM   1891  C  C     . GLY A 1 1772 ? 167.154 157.330 101.990 1.00 86.79  ? 1772 GLY A C     1 
ATOM   1892  O  O     . GLY A 1 1772 ? 166.975 157.038 100.804 1.00 89.84  ? 1772 GLY A O     1 
ATOM   1893  N  N     . GLY A 1 1773 ? 168.218 158.007 102.412 1.00 83.69  ? 1773 GLY A N     1 
ATOM   1894  C  CA    . GLY A 1 1773 ? 169.245 158.443 101.477 1.00 91.15  ? 1773 GLY A CA    1 
ATOM   1895  C  C     . GLY A 1 1773 ? 168.746 159.422 100.437 1.00 96.36  ? 1773 GLY A C     1 
ATOM   1896  O  O     . GLY A 1 1773 ? 169.054 159.272 99.248  1.00 100.17 ? 1773 GLY A O     1 
ATOM   1897  N  N     . ASP A 1 1774 ? 167.980 160.423 100.858 1.00 95.21  ? 1774 ASP A N     1 
ATOM   1898  C  CA    . ASP A 1 1774 ? 167.357 161.375 99.953  1.00 96.34  ? 1774 ASP A CA    1 
ATOM   1899  C  C     . ASP A 1 1774 ? 167.718 162.796 100.365 1.00 94.67  ? 1774 ASP A C     1 
ATOM   1900  O  O     . ASP A 1 1774 ? 168.053 163.056 101.525 1.00 85.51  ? 1774 ASP A O     1 
ATOM   1901  C  CB    . ASP A 1 1774 ? 165.830 161.197 99.940  1.00 93.24  ? 1774 ASP A CB    1 
ATOM   1902  C  CG    . ASP A 1 1774 ? 165.138 162.141 98.978  1.00 100.89 ? 1774 ASP A CG    1 
ATOM   1903  O  OD1   . ASP A 1 1774 ? 165.402 162.052 97.761  1.00 101.03 ? 1774 ASP A OD1   1 
ATOM   1904  O  OD2   . ASP A 1 1774 ? 164.328 162.973 99.439  1.00 95.18  ? 1774 ASP A OD2   1 
ATOM   1905  N  N     . ALA A 1 1775 ? 167.662 163.710 99.397  1.00 95.35  ? 1775 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 1775 ? 167.889 165.119 99.683  1.00 89.29  ? 1775 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 1775 ? 166.908 165.605 100.741 1.00 85.12  ? 1775 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 1775 ? 165.717 165.286 100.702 1.00 79.06  ? 1775 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 1775 ? 167.750 165.950 98.408  1.00 87.15  ? 1775 ALA A CB    1 
ATOM   1910  N  N     . ALA A 1 1776 ? 167.420 166.381 101.693 1.00 76.70  ? 1776 ALA A N     1 
ATOM   1911  C  CA    . ALA A 1 1776 ? 166.661 166.725 102.886 1.00 52.96  ? 1776 ALA A CA    1 
ATOM   1912  C  C     . ALA A 1 1776 ? 165.968 168.068 102.710 1.00 50.83  ? 1776 ALA A C     1 
ATOM   1913  O  O     . ALA A 1 1776 ? 166.651 169.088 102.548 1.00 39.86  ? 1776 ALA A O     1 
ATOM   1914  C  CB    . ALA A 1 1776 ? 167.572 166.770 104.100 1.00 39.21  ? 1776 ALA A CB    1 
ATOM   1915  N  N     . PRO A 1 1777 ? 164.633 168.120 102.723 1.00 49.46  ? 1777 PRO A N     1 
ATOM   1916  C  CA    . PRO A 1 1777 ? 163.938 169.403 102.872 1.00 38.94  ? 1777 PRO A CA    1 
ATOM   1917  C  C     . PRO A 1 1777 ? 163.840 169.878 104.312 1.00 37.29  ? 1777 PRO A C     1 
ATOM   1918  O  O     . PRO A 1 1777 ? 163.195 170.901 104.566 1.00 36.67  ? 1777 PRO A O     1 
ATOM   1919  C  CB    . PRO A 1 1777 ? 162.548 169.103 102.297 1.00 41.89  ? 1777 PRO A CB    1 
ATOM   1920  C  CG    . PRO A 1 1777 ? 162.345 167.662 102.577 1.00 35.06  ? 1777 PRO A CG    1 
ATOM   1921  C  CD    . PRO A 1 1777 ? 163.698 167.013 102.461 1.00 45.82  ? 1777 PRO A CD    1 
ATOM   1922  N  N     . LEU A 1 1778 ? 164.440 169.153 105.259 1.00 34.68  ? 1778 LEU A N     1 
ATOM   1923  C  CA    . LEU A 1 1778 ? 164.485 169.624 106.638 1.00 30.88  ? 1778 LEU A CA    1 
ATOM   1924  C  C     . LEU A 1 1778 ? 165.317 170.896 106.746 1.00 29.49  ? 1778 LEU A C     1 
ATOM   1925  O  O     . LEU A 1 1778 ? 165.076 171.739 107.621 1.00 28.10  ? 1778 LEU A O     1 
ATOM   1926  C  CB    . LEU A 1 1778 ? 165.046 168.523 107.540 1.00 33.85  ? 1778 LEU A CB    1 
ATOM   1927  C  CG    . LEU A 1 1778 ? 164.734 168.578 109.035 1.00 33.21  ? 1778 LEU A CG    1 
ATOM   1928  C  CD1   . LEU A 1 1778 ? 163.239 168.463 109.275 1.00 25.41  ? 1778 LEU A CD1   1 
ATOM   1929  C  CD2   . LEU A 1 1778 ? 165.477 167.473 109.764 1.00 23.60  ? 1778 LEU A CD2   1 
ATOM   1930  N  N     . HIS A 1 1779 ? 166.301 171.050 105.856 1.00 32.40  ? 1779 HIS A N     1 
ATOM   1931  C  CA    . HIS A 1 1779 ? 167.054 172.296 105.783 1.00 29.64  ? 1779 HIS A CA    1 
ATOM   1932  C  C     . HIS A 1 1779 ? 166.142 173.467 105.445 1.00 26.07  ? 1779 HIS A C     1 
ATOM   1933  O  O     . HIS A 1 1779 ? 166.372 174.593 105.896 1.00 25.16  ? 1779 HIS A O     1 
ATOM   1934  C  CB    . HIS A 1 1779 ? 168.174 172.172 104.749 1.00 30.06  ? 1779 HIS A CB    1 
ATOM   1935  C  CG    . HIS A 1 1779 ? 169.185 171.118 105.076 1.00 37.38  ? 1779 HIS A CG    1 
ATOM   1936  N  ND1   . HIS A 1 1779 ? 170.149 171.287 106.047 1.00 40.78  ? 1779 HIS A ND1   1 
ATOM   1937  C  CD2   . HIS A 1 1779 ? 169.383 169.882 104.561 1.00 40.41  ? 1779 HIS A CD2   1 
ATOM   1938  C  CE1   . HIS A 1 1779 ? 170.898 170.201 106.115 1.00 33.20  ? 1779 HIS A CE1   1 
ATOM   1939  N  NE2   . HIS A 1 1779 ? 170.454 169.332 105.225 1.00 33.74  ? 1779 HIS A NE2   1 
ATOM   1940  N  N     . SER A 1 1780 ? 165.099 173.220 104.650 1.00 27.75  ? 1780 SER A N     1 
ATOM   1941  C  CA    . SER A 1 1780 ? 164.128 174.268 104.352 1.00 23.82  ? 1780 SER A CA    1 
ATOM   1942  C  C     . SER A 1 1780 ? 163.386 174.700 105.611 1.00 24.97  ? 1780 SER A C     1 
ATOM   1943  O  O     . SER A 1 1780 ? 163.140 175.892 105.825 1.00 28.69  ? 1780 SER A O     1 
ATOM   1944  C  CB    . SER A 1 1780 ? 163.145 173.787 103.284 1.00 25.64  ? 1780 SER A CB    1 
ATOM   1945  O  OG    . SER A 1 1780 ? 162.147 172.960 103.853 1.00 36.75  ? 1780 SER A OG    1 
ATOM   1946  N  N     . VAL A 1 1781 ? 163.022 173.736 106.458 1.00 28.22  ? 1781 VAL A N     1 
ATOM   1947  C  CA    . VAL A 1 1781 ? 162.376 174.061 107.729 1.00 24.33  ? 1781 VAL A CA    1 
ATOM   1948  C  C     . VAL A 1 1781 ? 163.322 174.866 108.610 1.00 22.27  ? 1781 VAL A C     1 
ATOM   1949  O  O     . VAL A 1 1781 ? 162.925 175.851 109.249 1.00 26.08  ? 1781 VAL A O     1 
ATOM   1950  C  CB    . VAL A 1 1781 ? 161.906 172.776 108.434 1.00 18.22  ? 1781 VAL A CB    1 
ATOM   1951  C  CG1   . VAL A 1 1781 ? 161.103 173.116 109.676 1.00 22.73  ? 1781 VAL A CG1   1 
ATOM   1952  C  CG2   . VAL A 1 1781 ? 161.088 171.922 107.483 1.00 22.45  ? 1781 VAL A CG2   1 
ATOM   1953  N  N     . LEU A 1 1782 ? 164.592 174.457 108.658 1.00 21.32  ? 1782 LEU A N     1 
ATOM   1954  C  CA    . LEU A 1 1782 ? 165.572 175.190 109.454 1.00 19.98  ? 1782 LEU A CA    1 
ATOM   1955  C  C     . LEU A 1 1782 ? 165.723 176.622 108.953 1.00 23.98  ? 1782 LEU A C     1 
ATOM   1956  O  O     . LEU A 1 1782 ? 165.784 177.566 109.747 1.00 24.94  ? 1782 LEU A O     1 
ATOM   1957  C  CB    . LEU A 1 1782 ? 166.917 174.464 109.429 1.00 19.47  ? 1782 LEU A CB    1 
ATOM   1958  C  CG    . LEU A 1 1782 ? 168.073 175.153 110.156 1.00 21.01  ? 1782 LEU A CG    1 
ATOM   1959  C  CD1   . LEU A 1 1782 ? 167.710 175.422 111.607 1.00 23.54  ? 1782 LEU A CD1   1 
ATOM   1960  C  CD2   . LEU A 1 1782 ? 169.337 174.319 110.065 1.00 22.26  ? 1782 LEU A CD2   1 
ATOM   1961  N  N     . SER A 1 1783 ? 165.776 176.801 107.631 1.00 24.52  ? 1783 SER A N     1 
ATOM   1962  C  CA    . SER A 1 1783 ? 165.912 178.140 107.065 1.00 21.95  ? 1783 SER A CA    1 
ATOM   1963  C  C     . SER A 1 1783 ? 164.670 178.983 107.328 1.00 23.17  ? 1783 SER A C     1 
ATOM   1964  O  O     . SER A 1 1783 ? 164.771 180.192 107.568 1.00 27.07  ? 1783 SER A O     1 
ATOM   1965  C  CB    . SER A 1 1783 ? 166.191 178.046 105.565 1.00 25.55  ? 1783 SER A CB    1 
ATOM   1966  O  OG    . SER A 1 1783 ? 167.364 177.290 105.316 1.00 33.12  ? 1783 SER A OG    1 
ATOM   1967  N  N     . ASN A 1 1784 ? 163.487 178.367 107.271 1.00 23.08  ? 1784 ASN A N     1 
ATOM   1968  C  CA    . ASN A 1 1784 ? 162.268 179.084 107.623 1.00 24.84  ? 1784 ASN A CA    1 
ATOM   1969  C  C     . ASN A 1 1784 ? 162.301 179.547 109.072 1.00 24.47  ? 1784 ASN A C     1 
ATOM   1970  O  O     . ASN A 1 1784 ? 161.859 180.660 109.378 1.00 27.99  ? 1784 ASN A O     1 
ATOM   1971  C  CB    . ASN A 1 1784 ? 161.044 178.203 107.377 1.00 24.17  ? 1784 ASN A CB    1 
ATOM   1972  C  CG    . ASN A 1 1784 ? 159.743 178.968 107.503 1.00 30.81  ? 1784 ASN A CG    1 
ATOM   1973  O  OD1   . ASN A 1 1784 ? 158.985 178.774 108.453 1.00 38.79  ? 1784 ASN A OD1   1 
ATOM   1974  N  ND2   . ASN A 1 1784 ? 159.475 179.844 106.543 1.00 33.53  ? 1784 ASN A ND2   1 
ATOM   1975  N  N     . VAL A 1 1785 ? 162.812 178.708 109.973 1.00 21.39  ? 1785 VAL A N     1 
ATOM   1976  C  CA    . VAL A 1 1785 ? 162.977 179.125 111.363 1.00 21.88  ? 1785 VAL A CA    1 
ATOM   1977  C  C     . VAL A 1 1785 ? 163.966 180.283 111.457 1.00 22.31  ? 1785 VAL A C     1 
ATOM   1978  O  O     . VAL A 1 1785 ? 163.748 181.248 112.199 1.00 24.97  ? 1785 VAL A O     1 
ATOM   1979  C  CB    . VAL A 1 1785 ? 163.413 177.934 112.235 1.00 23.02  ? 1785 VAL A CB    1 
ATOM   1980  C  CG1   . VAL A 1 1785 ? 163.688 178.389 113.657 1.00 18.10  ? 1785 VAL A CG1   1 
ATOM   1981  C  CG2   . VAL A 1 1785 ? 162.342 176.858 112.232 1.00 20.69  ? 1785 VAL A CG2   1 
ATOM   1982  N  N     . GLU A 1 1786 ? 165.068 180.201 110.706 1.00 24.21  ? 1786 GLU A N     1 
ATOM   1983  C  CA    . GLU A 1 1786 ? 166.107 181.228 110.777 1.00 21.94  ? 1786 GLU A CA    1 
ATOM   1984  C  C     . GLU A 1 1786 ? 165.592 182.587 110.314 1.00 22.95  ? 1786 GLU A C     1 
ATOM   1985  O  O     . GLU A 1 1786 ? 165.868 183.614 110.944 1.00 25.16  ? 1786 GLU A O     1 
ATOM   1986  C  CB    . GLU A 1 1786 ? 167.323 180.810 109.947 1.00 24.39  ? 1786 GLU A CB    1 
ATOM   1987  C  CG    . GLU A 1 1786 ? 168.027 179.538 110.404 1.00 25.24  ? 1786 GLU A CG    1 
ATOM   1988  C  CD    . GLU A 1 1786 ? 168.861 179.715 111.664 1.00 36.09  ? 1786 GLU A CD    1 
ATOM   1989  O  OE1   . GLU A 1 1786 ? 169.822 178.938 111.844 1.00 31.26  ? 1786 GLU A OE1   1 
ATOM   1990  O  OE2   . GLU A 1 1786 ? 168.574 180.626 112.470 1.00 37.29  ? 1786 GLU A OE2   1 
ATOM   1991  N  N     . VAL A 1 1787 ? 164.856 182.621 109.200 1.00 21.64  ? 1787 VAL A N     1 
ATOM   1992  C  CA    . VAL A 1 1787 ? 164.383 183.906 108.684 1.00 22.60  ? 1787 VAL A CA    1 
ATOM   1993  C  C     . VAL A 1 1787 ? 163.333 184.508 109.613 1.00 28.12  ? 1787 VAL A C     1 
ATOM   1994  O  O     . VAL A 1 1787 ? 163.295 185.728 109.824 1.00 30.73  ? 1787 VAL A O     1 
ATOM   1995  C  CB    . VAL A 1 1787 ? 163.875 183.766 107.234 1.00 22.05  ? 1787 VAL A CB    1 
ATOM   1996  C  CG1   . VAL A 1 1787 ? 164.899 183.034 106.387 1.00 30.67  ? 1787 VAL A CG1   1 
ATOM   1997  C  CG2   . VAL A 1 1787 ? 162.539 183.042 107.176 1.00 21.21  ? 1787 VAL A CG2   1 
ATOM   1998  N  N     . THR A 1 1788 ? 162.479 183.667 110.199 1.00 27.89  ? 1788 THR A N     1 
ATOM   1999  C  CA    . THR A 1 1788 ? 161.501 184.168 111.157 1.00 26.01  ? 1788 THR A CA    1 
ATOM   2000  C  C     . THR A 1 1788 ? 162.195 184.705 112.403 1.00 23.76  ? 1788 THR A C     1 
ATOM   2001  O  O     . THR A 1 1788 ? 161.784 185.725 112.969 1.00 26.85  ? 1788 THR A O     1 
ATOM   2002  C  CB    . THR A 1 1788 ? 160.506 183.066 111.521 1.00 24.71  ? 1788 THR A CB    1 
ATOM   2003  O  OG1   . THR A 1 1788 ? 160.139 182.348 110.338 1.00 29.72  ? 1788 THR A OG1   1 
ATOM   2004  C  CG2   . THR A 1 1788 ? 159.254 183.676 112.123 1.00 20.28  ? 1788 THR A CG2   1 
ATOM   2005  N  N     . LEU A 1 1789 ? 163.260 184.030 112.840 1.00 23.60  ? 1789 LEU A N     1 
ATOM   2006  C  CA    . LEU A 1 1789 ? 164.046 184.532 113.961 1.00 20.75  ? 1789 LEU A CA    1 
ATOM   2007  C  C     . LEU A 1 1789 ? 164.698 185.864 113.622 1.00 22.59  ? 1789 LEU A C     1 
ATOM   2008  O  O     . LEU A 1 1789 ? 164.796 186.748 114.477 1.00 26.67  ? 1789 LEU A O     1 
ATOM   2009  C  CB    . LEU A 1 1789 ? 165.104 183.507 114.366 1.00 13.29  ? 1789 LEU A CB    1 
ATOM   2010  C  CG    . LEU A 1 1789 ? 164.693 182.512 115.450 1.00 13.53  ? 1789 LEU A CG    1 
ATOM   2011  C  CD1   . LEU A 1 1789 ? 165.714 181.396 115.572 1.00 16.88  ? 1789 LEU A CD1   1 
ATOM   2012  C  CD2   . LEU A 1 1789 ? 164.517 183.225 116.778 1.00 14.88  ? 1789 LEU A CD2   1 
ATOM   2013  N  N     . ASN A 1 1790 ? 165.163 186.021 112.382 1.00 26.19  ? 1790 ASN A N     1 
ATOM   2014  C  CA    . ASN A 1 1790 ? 165.738 187.297 111.964 1.00 26.07  ? 1790 ASN A CA    1 
ATOM   2015  C  C     . ASN A 1 1790 ? 164.697 188.407 112.017 1.00 28.48  ? 1790 ASN A C     1 
ATOM   2016  O  O     . ASN A 1 1790 ? 164.974 189.516 112.489 1.00 30.02  ? 1790 ASN A O     1 
ATOM   2017  C  CB    . ASN A 1 1790 ? 166.322 187.174 110.557 1.00 23.81  ? 1790 ASN A CB    1 
ATOM   2018  C  CG    . ASN A 1 1790 ? 167.572 186.324 110.518 1.00 34.50  ? 1790 ASN A CG    1 
ATOM   2019  O  OD1   . ASN A 1 1790 ? 168.346 186.296 111.474 1.00 36.11  ? 1790 ASN A OD1   1 
ATOM   2020  N  ND2   . ASN A 1 1790 ? 167.777 185.625 109.408 1.00 38.48  ? 1790 ASN A ND2   1 
ATOM   2021  N  N     . VAL A 1 1791 ? 163.486 188.122 111.533 1.00 27.94  ? 1791 VAL A N     1 
ATOM   2022  C  CA    . VAL A 1 1791 ? 162.414 189.116 111.580 1.00 23.03  ? 1791 VAL A CA    1 
ATOM   2023  C  C     . VAL A 1 1791 ? 162.093 189.485 113.023 1.00 22.82  ? 1791 VAL A C     1 
ATOM   2024  O  O     . VAL A 1 1791 ? 161.940 190.665 113.363 1.00 28.59  ? 1791 VAL A O     1 
ATOM   2025  C  CB    . VAL A 1 1791 ? 161.167 188.603 110.838 1.00 26.80  ? 1791 VAL A CB    1 
ATOM   2026  C  CG1   . VAL A 1 1791 ? 160.059 189.638 110.898 1.00 23.52  ? 1791 VAL A CG1   1 
ATOM   2027  C  CG2   . VAL A 1 1791 ? 161.507 188.284 109.395 1.00 33.03  ? 1791 VAL A CG2   1 
ATOM   2028  N  N     . LEU A 1 1792 ? 161.990 188.480 113.896 1.00 20.16  ? 1792 LEU A N     1 
ATOM   2029  C  CA    . LEU A 1 1792 ? 161.682 188.747 115.299 1.00 18.10  ? 1792 LEU A CA    1 
ATOM   2030  C  C     . LEU A 1 1792 ? 162.791 189.547 115.974 1.00 20.31  ? 1792 LEU A C     1 
ATOM   2031  O  O     . LEU A 1 1792 ? 162.516 190.457 116.764 1.00 20.79  ? 1792 LEU A O     1 
ATOM   2032  C  CB    . LEU A 1 1792 ? 161.437 187.435 116.043 1.00 21.47  ? 1792 LEU A CB    1 
ATOM   2033  C  CG    . LEU A 1 1792 ? 160.207 186.618 115.648 1.00 19.10  ? 1792 LEU A CG    1 
ATOM   2034  C  CD1   . LEU A 1 1792 ? 160.351 185.179 116.106 1.00 15.27  ? 1792 LEU A CD1   1 
ATOM   2035  C  CD2   . LEU A 1 1792 ? 158.962 187.236 116.245 1.00 11.51  ? 1792 LEU A CD2   1 
ATOM   2036  N  N     . ALA A 1 1793 ? 164.051 189.218 115.681 1.00 21.24  ? 1793 ALA A N     1 
ATOM   2037  C  CA    . ALA A 1 1793 ? 165.170 189.944 116.269 1.00 23.08  ? 1793 ALA A CA    1 
ATOM   2038  C  C     . ALA A 1 1793 ? 165.216 191.385 115.787 1.00 26.60  ? 1793 ALA A C     1 
ATOM   2039  O  O     . ALA A 1 1793 ? 165.565 192.285 116.557 1.00 34.39  ? 1793 ALA A O     1 
ATOM   2040  C  CB    . ALA A 1 1793 ? 166.484 189.233 115.950 1.00 26.15  ? 1793 ALA A CB    1 
ATOM   2041  N  N     . ASP A 1 1794 ? 164.884 191.623 114.518 1.00 25.11  ? 1794 ASP A N     1 
ATOM   2042  C  CA    . ASP A 1 1794 ? 164.750 192.996 114.046 1.00 30.45  ? 1794 ASP A CA    1 
ATOM   2043  C  C     . ASP A 1 1794 ? 163.605 193.712 114.751 1.00 29.11  ? 1794 ASP A C     1 
ATOM   2044  O  O     . ASP A 1 1794 ? 163.705 194.908 115.047 1.00 31.04  ? 1794 ASP A O     1 
ATOM   2045  C  CB    . ASP A 1 1794 ? 164.540 193.018 112.533 1.00 36.30  ? 1794 ASP A CB    1 
ATOM   2046  C  CG    . ASP A 1 1794 ? 165.770 192.578 111.768 1.00 42.16  ? 1794 ASP A CG    1 
ATOM   2047  O  OD1   . ASP A 1 1794 ? 166.811 192.325 112.409 1.00 41.91  ? 1794 ASP A OD1   1 
ATOM   2048  O  OD2   . ASP A 1 1794 ? 165.695 192.485 110.525 1.00 40.44  ? 1794 ASP A OD2   1 
ATOM   2049  N  N     . SER A 1 1795 ? 162.511 192.995 115.021 1.00 26.45  ? 1795 SER A N     1 
ATOM   2050  C  CA    . SER A 1 1795 ? 161.348 193.616 115.646 1.00 23.93  ? 1795 SER A CA    1 
ATOM   2051  C  C     . SER A 1 1795 ? 161.656 194.098 117.059 1.00 25.80  ? 1795 SER A C     1 
ATOM   2052  O  O     . SER A 1 1795 ? 161.231 195.190 117.453 1.00 34.07  ? 1795 SER A O     1 
ATOM   2053  C  CB    . SER A 1 1795 ? 160.179 192.633 115.660 1.00 24.46  ? 1795 SER A CB    1 
ATOM   2054  O  OG    . SER A 1 1795 ? 159.877 192.183 114.352 1.00 24.74  ? 1795 SER A OG    1 
ATOM   2055  N  N     . VAL A 1 1796 ? 162.386 193.300 117.841 1.00 24.50  ? 1796 VAL A N     1 
ATOM   2056  C  CA    . VAL A 1 1796 ? 162.618 193.656 119.236 1.00 23.83  ? 1796 VAL A CA    1 
ATOM   2057  C  C     . VAL A 1 1796 ? 163.634 194.781 119.382 1.00 26.11  ? 1796 VAL A C     1 
ATOM   2058  O  O     . VAL A 1 1796 ? 163.714 195.399 120.449 1.00 28.67  ? 1796 VAL A O     1 
ATOM   2059  C  CB    . VAL A 1 1796 ? 163.059 192.424 120.048 1.00 17.69  ? 1796 VAL A CB    1 
ATOM   2060  C  CG1   . VAL A 1 1796 ? 161.927 191.420 120.137 1.00 17.11  ? 1796 VAL A CG1   1 
ATOM   2061  C  CG2   . VAL A 1 1796 ? 164.292 191.791 119.433 1.00 21.48  ? 1796 VAL A CG2   1 
ATOM   2062  N  N     . LEU A 1 1797 ? 164.424 195.059 118.343 1.00 26.24  ? 1797 LEU A N     1 
ATOM   2063  C  CA    . LEU A 1 1797 ? 165.351 196.185 118.406 1.00 31.47  ? 1797 LEU A CA    1 
ATOM   2064  C  C     . LEU A 1 1797 ? 164.607 197.509 118.512 1.00 33.12  ? 1797 LEU A C     1 
ATOM   2065  O  O     . LEU A 1 1797 ? 164.995 198.386 119.293 1.00 32.08  ? 1797 LEU A O     1 
ATOM   2066  C  CB    . LEU A 1 1797 ? 166.260 196.190 117.181 1.00 33.18  ? 1797 LEU A CB    1 
ATOM   2067  C  CG    . LEU A 1 1797 ? 167.241 195.031 117.031 1.00 33.16  ? 1797 LEU A CG    1 
ATOM   2068  C  CD1   . LEU A 1 1797 ? 167.944 195.141 115.699 1.00 34.34  ? 1797 LEU A CD1   1 
ATOM   2069  C  CD2   . LEU A 1 1797 ? 168.245 195.031 118.168 1.00 29.13  ? 1797 LEU A CD2   1 
ATOM   2070  N  N     . MET A 1 1798 ? 163.540 197.671 117.737 1.00 35.08  ? 1798 MET A N     1 
ATOM   2071  C  CA    . MET A 1 1798 ? 162.778 198.906 117.716 1.00 37.17  ? 1798 MET A CA    1 
ATOM   2072  C  C     . MET A 1 1798 ? 161.758 198.917 118.854 1.00 38.05  ? 1798 MET A C     1 
ATOM   2073  O  O     . MET A 1 1798 ? 161.446 197.886 119.455 1.00 39.93  ? 1798 MET A O     1 
ATOM   2074  C  CB    . MET A 1 1798 ? 162.109 199.084 116.353 1.00 42.65  ? 1798 MET A CB    1 
ATOM   2075  C  CG    . MET A 1 1798 ? 161.071 198.034 116.023 1.00 43.71  ? 1798 MET A CG    1 
ATOM   2076  S  SD    . MET A 1 1798 ? 160.382 198.219 114.367 1.00 71.43  ? 1798 MET A SD    1 
ATOM   2077  C  CE    . MET A 1 1798 ? 161.754 197.658 113.363 1.00 39.59  ? 1798 MET A CE    1 
ATOM   2078  N  N     . GLU A 1 1799 ? 161.239 200.102 119.163 1.00 42.47  ? 1799 GLU A N     1 
ATOM   2079  C  CA    . GLU A 1 1799 ? 160.271 200.250 120.241 1.00 44.84  ? 1799 GLU A CA    1 
ATOM   2080  C  C     . GLU A 1 1799 ? 158.955 199.572 119.879 1.00 46.19  ? 1799 GLU A C     1 
ATOM   2081  O  O     . GLU A 1 1799 ? 158.471 199.677 118.748 1.00 43.80  ? 1799 GLU A O     1 
ATOM   2082  C  CB    . GLU A 1 1799 ? 160.040 201.730 120.554 1.00 57.32  ? 1799 GLU A CB    1 
ATOM   2083  C  CG    . GLU A 1 1799 ? 159.393 202.528 119.431 1.00 68.39  ? 1799 GLU A CG    1 
ATOM   2084  C  CD    . GLU A 1 1799 ? 159.245 203.998 119.768 1.00 75.78  ? 1799 GLU A CD    1 
ATOM   2085  O  OE1   . GLU A 1 1799 ? 159.668 204.401 120.872 1.00 81.71  ? 1799 GLU A OE1   1 
ATOM   2086  O  OE2   . GLU A 1 1799 ? 158.706 204.750 118.930 1.00 75.62  ? 1799 GLU A OE2   1 
ATOM   2087  N  N     . GLN A 1 1800 ? 158.389 198.857 120.846 1.00 39.66  ? 1800 GLN A N     1 
ATOM   2088  C  CA    . GLN A 1 1800 ? 157.176 198.080 120.649 1.00 39.31  ? 1800 GLN A CA    1 
ATOM   2089  C  C     . GLN A 1 1800 ? 156.238 198.290 121.827 1.00 35.35  ? 1800 GLN A C     1 
ATOM   2090  O  O     . GLN A 1 1800 ? 156.685 198.643 122.925 1.00 40.00  ? 1800 GLN A O     1 
ATOM   2091  C  CB    . GLN A 1 1800 ? 157.480 196.579 120.506 1.00 36.44  ? 1800 GLN A CB    1 
ATOM   2092  C  CG    . GLN A 1 1800 ? 158.554 196.237 119.489 1.00 27.33  ? 1800 GLN A CG    1 
ATOM   2093  C  CD    . GLN A 1 1800 ? 158.030 196.238 118.070 1.00 31.94  ? 1800 GLN A CD    1 
ATOM   2094  O  OE1   . GLN A 1 1800 ? 156.851 196.494 117.832 1.00 35.31  ? 1800 GLN A OE1   1 
ATOM   2095  N  NE2   . GLN A 1 1800 ? 158.902 195.934 117.119 1.00 35.59  ? 1800 GLN A NE2   1 
ATOM   2096  N  N     . PRO A 1 1801 ? 154.936 198.090 121.628 1.00 28.99  ? 1801 PRO A N     1 
ATOM   2097  C  CA    . PRO A 1 1801 ? 154.026 198.062 122.767 1.00 29.45  ? 1801 PRO A CA    1 
ATOM   2098  C  C     . PRO A 1 1801 ? 154.396 196.937 123.709 1.00 26.79  ? 1801 PRO A C     1 
ATOM   2099  O  O     . PRO A 1 1801 ? 154.892 195.879 123.276 1.00 30.52  ? 1801 PRO A O     1 
ATOM   2100  C  CB    . PRO A 1 1801 ? 152.655 197.829 122.117 1.00 32.54  ? 1801 PRO A CB    1 
ATOM   2101  C  CG    . PRO A 1 1801 ? 152.810 198.325 120.721 1.00 31.55  ? 1801 PRO A CG    1 
ATOM   2102  C  CD    . PRO A 1 1801 ? 154.223 198.016 120.342 1.00 25.53  ? 1801 PRO A CD    1 
ATOM   2103  N  N     . PRO A 1 1802 ? 154.190 197.123 125.017 1.00 28.26  ? 1802 PRO A N     1 
ATOM   2104  C  CA    . PRO A 1 1802 ? 154.642 196.101 125.979 1.00 29.87  ? 1802 PRO A CA    1 
ATOM   2105  C  C     . PRO A 1 1802 ? 154.062 194.720 125.727 1.00 24.90  ? 1802 PRO A C     1 
ATOM   2106  O  O     . PRO A 1 1802 ? 154.787 193.721 125.832 1.00 24.53  ? 1802 PRO A O     1 
ATOM   2107  C  CB    . PRO A 1 1802 ? 154.186 196.672 127.330 1.00 29.45  ? 1802 PRO A CB    1 
ATOM   2108  C  CG    . PRO A 1 1802 ? 154.029 198.138 127.096 1.00 29.45  ? 1802 PRO A CG    1 
ATOM   2109  C  CD    . PRO A 1 1802 ? 153.564 198.277 125.682 1.00 28.22  ? 1802 PRO A CD    1 
ATOM   2110  N  N     . LEU A 1 1803 ? 152.776 194.633 125.381 1.00 22.81  ? 1803 LEU A N     1 
ATOM   2111  C  CA    . LEU A 1 1803 ? 152.182 193.336 125.073 1.00 21.16  ? 1803 LEU A CA    1 
ATOM   2112  C  C     . LEU A 1 1803 ? 152.819 192.723 123.834 1.00 19.85  ? 1803 LEU A C     1 
ATOM   2113  O  O     . LEU A 1 1803 ? 153.152 191.530 123.821 1.00 21.98  ? 1803 LEU A O     1 
ATOM   2114  C  CB    . LEU A 1 1803 ? 150.674 193.483 124.883 1.00 27.10  ? 1803 LEU A CB    1 
ATOM   2115  C  CG    . LEU A 1 1803 ? 149.857 192.191 124.887 1.00 25.90  ? 1803 LEU A CG    1 
ATOM   2116  C  CD1   . LEU A 1 1803 ? 149.737 191.652 126.300 1.00 19.65  ? 1803 LEU A CD1   1 
ATOM   2117  C  CD2   . LEU A 1 1803 ? 148.484 192.418 124.278 1.00 19.62  ? 1803 LEU A CD2   1 
ATOM   2118  N  N     . ARG A 1 1804 ? 153.000 193.527 122.786 1.00 20.83  ? 1804 ARG A N     1 
ATOM   2119  C  CA    . ARG A 1 1804 ? 153.659 193.035 121.583 1.00 18.67  ? 1804 ARG A CA    1 
ATOM   2120  C  C     . ARG A 1 1804 ? 155.101 192.644 121.870 1.00 18.68  ? 1804 ARG A C     1 
ATOM   2121  O  O     . ARG A 1 1804 ? 155.603 191.663 121.314 1.00 19.10  ? 1804 ARG A O     1 
ATOM   2122  C  CB    . ARG A 1 1804 ? 153.596 194.087 120.477 1.00 21.84  ? 1804 ARG A CB    1 
ATOM   2123  C  CG    . ARG A 1 1804 ? 153.907 193.538 119.098 1.00 24.90  ? 1804 ARG A CG    1 
ATOM   2124  C  CD    . ARG A 1 1804 ? 154.224 194.649 118.117 1.00 29.43  ? 1804 ARG A CD    1 
ATOM   2125  N  NE    . ARG A 1 1804 ? 153.109 195.574 117.962 1.00 32.27  ? 1804 ARG A NE    1 
ATOM   2126  C  CZ    . ARG A 1 1804 ? 153.137 196.658 117.200 1.00 28.91  ? 1804 ARG A CZ    1 
ATOM   2127  N  NH1   . ARG A 1 1804 ? 154.213 196.987 116.506 1.00 31.98  ? 1804 ARG A NH1   1 
ATOM   2128  N  NH2   . ARG A 1 1804 ? 152.057 197.431 117.131 1.00 33.94  ? 1804 ARG A NH2   1 
ATOM   2129  N  N     . ARG A 1 1805 ? 155.785 193.399 122.733 1.00 20.59  ? 1805 ARG A N     1 
ATOM   2130  C  CA    . ARG A 1 1805 ? 157.155 193.046 123.087 1.00 20.37  ? 1805 ARG A CA    1 
ATOM   2131  C  C     . ARG A 1 1805 ? 157.214 191.702 123.802 1.00 19.56  ? 1805 ARG A C     1 
ATOM   2132  O  O     . ARG A 1 1805 ? 158.090 190.879 123.517 1.00 23.46  ? 1805 ARG A O     1 
ATOM   2133  C  CB    . ARG A 1 1805 ? 157.779 194.140 123.951 1.00 23.70  ? 1805 ARG A CB    1 
ATOM   2134  C  CG    . ARG A 1 1805 ? 159.250 193.911 124.244 1.00 25.13  ? 1805 ARG A CG    1 
ATOM   2135  C  CD    . ARG A 1 1805 ? 159.830 195.027 125.086 1.00 32.14  ? 1805 ARG A CD    1 
ATOM   2136  N  NE    . ARG A 1 1805 ? 159.814 196.296 124.368 1.00 50.03  ? 1805 ARG A NE    1 
ATOM   2137  C  CZ    . ARG A 1 1805 ? 160.751 196.686 123.516 1.00 44.11  ? 1805 ARG A CZ    1 
ATOM   2138  N  NH1   . ARG A 1 1805 ? 161.795 195.923 123.238 1.00 26.40  ? 1805 ARG A NH1   1 
ATOM   2139  N  NH2   . ARG A 1 1805 ? 160.636 197.871 122.923 1.00 46.59  ? 1805 ARG A NH2   1 
ATOM   2140  N  N     . ARG A 1 1806 ? 156.291 191.462 124.737 1.00 21.14  ? 1806 ARG A N     1 
ATOM   2141  C  CA    . ARG A 1 1806 ? 156.268 190.175 125.426 1.00 16.63  ? 1806 ARG A CA    1 
ATOM   2142  C  C     . ARG A 1 1806 ? 155.946 189.038 124.464 1.00 12.64  ? 1806 ARG A C     1 
ATOM   2143  O  O     . ARG A 1 1806 ? 156.540 187.954 124.552 1.00 15.67  ? 1806 ARG A O     1 
ATOM   2144  C  CB    . ARG A 1 1806 ? 155.266 190.214 126.577 1.00 16.53  ? 1806 ARG A CB    1 
ATOM   2145  C  CG    . ARG A 1 1806 ? 155.611 191.232 127.645 1.00 17.62  ? 1806 ARG A CG    1 
ATOM   2146  C  CD    . ARG A 1 1806 ? 154.634 191.174 128.797 1.00 19.26  ? 1806 ARG A CD    1 
ATOM   2147  N  NE    . ARG A 1 1806 ? 154.884 190.026 129.658 1.00 23.49  ? 1806 ARG A NE    1 
ATOM   2148  C  CZ    . ARG A 1 1806 ? 154.185 189.742 130.747 1.00 26.15  ? 1806 ARG A CZ    1 
ATOM   2149  N  NH1   . ARG A 1 1806 ? 153.176 190.504 131.138 1.00 23.21  ? 1806 ARG A NH1   1 
ATOM   2150  N  NH2   . ARG A 1 1806 ? 154.505 188.668 131.463 1.00 23.59  ? 1806 ARG A NH2   1 
ATOM   2151  N  N     . LYS A 1 1807 ? 155.011 189.265 123.538 1.00 15.36  ? 1807 LYS A N     1 
ATOM   2152  C  CA    . LYS A 1 1807 ? 154.719 188.256 122.524 1.00 11.97  ? 1807 LYS A CA    1 
ATOM   2153  C  C     . LYS A 1 1807 ? 155.949 187.962 121.673 1.00 12.38  ? 1807 LYS A C     1 
ATOM   2154  O  O     . LYS A 1 1807 ? 156.238 186.799 121.365 1.00 17.05  ? 1807 LYS A O     1 
ATOM   2155  C  CB    . LYS A 1 1807 ? 153.558 188.714 121.644 1.00 11.92  ? 1807 LYS A CB    1 
ATOM   2156  C  CG    . LYS A 1 1807 ? 152.228 188.814 122.362 1.00 13.42  ? 1807 LYS A CG    1 
ATOM   2157  C  CD    . LYS A 1 1807 ? 151.119 189.202 121.400 1.00 12.43  ? 1807 LYS A CD    1 
ATOM   2158  C  CE    . LYS A 1 1807 ? 149.792 189.350 122.118 1.00 16.92  ? 1807 LYS A CE    1 
ATOM   2159  N  NZ    . LYS A 1 1807 ? 148.693 189.679 121.173 1.00 22.34  ? 1807 LYS A NZ    1 
ATOM   2160  N  N     . LEU A 1 1808 ? 156.683 189.007 121.284 1.00 13.10  ? 1808 LEU A N     1 
ATOM   2161  C  CA    . LEU A 1 1808 ? 157.898 188.817 120.499 1.00 13.44  ? 1808 LEU A CA    1 
ATOM   2162  C  C     . LEU A 1 1808 ? 158.942 188.033 121.281 1.00 12.16  ? 1808 LEU A C     1 
ATOM   2163  O  O     . LEU A 1 1808 ? 159.634 187.182 120.716 1.00 15.72  ? 1808 LEU A O     1 
ATOM   2164  C  CB    . LEU A 1 1808 ? 158.464 190.169 120.062 1.00 17.63  ? 1808 LEU A CB    1 
ATOM   2165  C  CG    . LEU A 1 1808 ? 157.687 190.986 119.028 1.00 15.14  ? 1808 LEU A CG    1 
ATOM   2166  C  CD1   . LEU A 1 1808 ? 158.138 192.435 119.051 1.00 15.36  ? 1808 LEU A CD1   1 
ATOM   2167  C  CD2   . LEU A 1 1808 ? 157.856 190.402 117.639 1.00 17.70  ? 1808 LEU A CD2   1 
ATOM   2168  N  N     . GLU A 1 1809 ? 159.083 188.316 122.577 1.00 10.37  ? 1809 GLU A N     1 
ATOM   2169  C  CA    . GLU A 1 1809 ? 160.039 187.571 123.394 1.00 9.49   ? 1809 GLU A CA    1 
ATOM   2170  C  C     . GLU A 1 1809 ? 159.664 186.096 123.484 1.00 11.73  ? 1809 GLU A C     1 
ATOM   2171  O  O     . GLU A 1 1809 ? 160.528 185.217 123.353 1.00 11.94  ? 1809 GLU A O     1 
ATOM   2172  C  CB    . GLU A 1 1809 ? 160.130 188.183 124.791 1.00 11.85  ? 1809 GLU A CB    1 
ATOM   2173  C  CG    . GLU A 1 1809 ? 160.625 189.614 124.813 1.00 17.72  ? 1809 GLU A CG    1 
ATOM   2174  C  CD    . GLU A 1 1809 ? 160.716 190.173 126.217 1.00 34.00  ? 1809 GLU A CD    1 
ATOM   2175  O  OE1   . GLU A 1 1809 ? 159.657 190.406 126.836 1.00 35.15  ? 1809 GLU A OE1   1 
ATOM   2176  O  OE2   . GLU A 1 1809 ? 161.847 190.375 126.703 1.00 38.34  ? 1809 GLU A OE2   1 
ATOM   2177  N  N     . HIS A 1 1810 ? 158.378 185.805 123.708 1.00 10.53  ? 1810 HIS A N     1 
ATOM   2178  C  CA    . HIS A 1 1810 ? 157.946 184.411 123.763 1.00 8.55   ? 1810 HIS A CA    1 
ATOM   2179  C  C     . HIS A 1 1810 ? 158.191 183.708 122.434 1.00 10.03  ? 1810 HIS A C     1 
ATOM   2180  O  O     . HIS A 1 1810 ? 158.661 182.562 122.403 1.00 11.56  ? 1810 HIS A O     1 
ATOM   2181  C  CB    . HIS A 1 1810 ? 156.468 184.319 124.144 1.00 9.06   ? 1810 HIS A CB    1 
ATOM   2182  C  CG    . HIS A 1 1810 ? 156.138 184.946 125.461 1.00 11.09  ? 1810 HIS A CG    1 
ATOM   2183  N  ND1   . HIS A 1 1810 ? 156.950 184.825 126.568 1.00 16.58  ? 1810 HIS A ND1   1 
ATOM   2184  C  CD2   . HIS A 1 1810 ? 155.065 185.669 125.860 1.00 12.51  ? 1810 HIS A CD2   1 
ATOM   2185  C  CE1   . HIS A 1 1810 ? 156.404 185.466 127.585 1.00 14.61  ? 1810 HIS A CE1   1 
ATOM   2186  N  NE2   . HIS A 1 1810 ? 155.259 185.986 127.183 1.00 14.89  ? 1810 HIS A NE2   1 
ATOM   2187  N  N     . LEU A 1 1811 ? 157.882 184.384 121.325 1.00 9.86   ? 1811 LEU A N     1 
ATOM   2188  C  CA    . LEU A 1 1811 ? 158.101 183.788 120.013 1.00 8.77   ? 1811 LEU A CA    1 
ATOM   2189  C  C     . LEU A 1 1811 ? 159.584 183.561 119.751 1.00 9.15   ? 1811 LEU A C     1 
ATOM   2190  O  O     . LEU A 1 1811 ? 159.969 182.536 119.178 1.00 10.63  ? 1811 LEU A O     1 
ATOM   2191  C  CB    . LEU A 1 1811 ? 157.489 184.673 118.930 1.00 8.13   ? 1811 LEU A CB    1 
ATOM   2192  C  CG    . LEU A 1 1811 ? 156.050 184.325 118.546 1.00 8.36   ? 1811 LEU A CG    1 
ATOM   2193  C  CD1   . LEU A 1 1811 ? 155.541 185.256 117.462 1.00 14.18  ? 1811 LEU A CD1   1 
ATOM   2194  C  CD2   . LEU A 1 1811 ? 155.954 182.877 118.104 1.00 8.40   ? 1811 LEU A CD2   1 
ATOM   2195  N  N     . ILE A 1 1812 ? 160.432 184.505 120.165 1.00 8.34   ? 1812 ILE A N     1 
ATOM   2196  C  CA    . ILE A 1 1812 ? 161.872 184.348 119.988 1.00 9.27   ? 1812 ILE A CA    1 
ATOM   2197  C  C     . ILE A 1 1812 ? 162.368 183.135 120.756 1.00 7.59   ? 1812 ILE A C     1 
ATOM   2198  O  O     . ILE A 1 1812 ? 163.136 182.322 120.230 1.00 8.60   ? 1812 ILE A O     1 
ATOM   2199  C  CB    . ILE A 1 1812 ? 162.609 185.630 120.420 1.00 10.61  ? 1812 ILE A CB    1 
ATOM   2200  C  CG1   . ILE A 1 1812 ? 162.482 186.708 119.346 1.00 7.40   ? 1812 ILE A CG1   1 
ATOM   2201  C  CG2   . ILE A 1 1812 ? 164.074 185.341 120.701 1.00 10.11  ? 1812 ILE A CG2   1 
ATOM   2202  C  CD1   . ILE A 1 1812 ? 163.148 188.009 119.709 1.00 9.82   ? 1812 ILE A CD1   1 
ATOM   2203  N  N     . THR A 1 1813 ? 161.929 182.985 122.007 1.00 9.84   ? 1813 THR A N     1 
ATOM   2204  C  CA    . THR A 1 1813 ? 162.346 181.834 122.803 1.00 6.07   ? 1813 THR A CA    1 
ATOM   2205  C  C     . THR A 1 1813 ? 161.905 180.527 122.151 1.00 6.13   ? 1813 THR A C     1 
ATOM   2206  O  O     . THR A 1 1813 ? 162.704 179.589 121.993 1.00 8.07   ? 1813 THR A O     1 
ATOM   2207  C  CB    . THR A 1 1813 ? 161.779 181.949 124.219 1.00 6.12   ? 1813 THR A CB    1 
ATOM   2208  O  OG1   . THR A 1 1813 ? 162.113 183.230 124.764 1.00 9.14   ? 1813 THR A OG1   1 
ATOM   2209  C  CG2   . THR A 1 1813 ? 162.351 180.865 125.113 1.00 7.22   ? 1813 THR A CG2   1 
ATOM   2210  N  N     . GLU A 1 1814 ? 160.635 180.458 121.743 1.00 6.13   ? 1814 GLU A N     1 
ATOM   2211  C  CA    . GLU A 1 1814 ? 160.118 179.223 121.163 1.00 8.16   ? 1814 GLU A CA    1 
ATOM   2212  C  C     . GLU A 1 1814 ? 160.830 178.872 119.863 1.00 8.81   ? 1814 GLU A C     1 
ATOM   2213  O  O     . GLU A 1 1814 ? 161.179 177.710 119.634 1.00 9.69   ? 1814 GLU A O     1 
ATOM   2214  C  CB    . GLU A 1 1814 ? 158.612 179.334 120.934 1.00 10.37  ? 1814 GLU A CB    1 
ATOM   2215  C  CG    . GLU A 1 1814 ? 157.939 178.016 120.563 1.00 10.65  ? 1814 GLU A CG    1 
ATOM   2216  C  CD    . GLU A 1 1814 ? 158.500 176.808 121.306 1.00 20.09  ? 1814 GLU A CD    1 
ATOM   2217  O  OE1   . GLU A 1 1814 ? 158.721 176.892 122.533 1.00 18.76  ? 1814 GLU A OE1   1 
ATOM   2218  O  OE2   . GLU A 1 1814 ? 158.731 175.767 120.654 1.00 16.16  ? 1814 GLU A OE2   1 
ATOM   2219  N  N     . LEU A 1 1815 ? 161.063 179.860 118.998 1.00 7.19   ? 1815 LEU A N     1 
ATOM   2220  C  CA    . LEU A 1 1815 ? 161.708 179.561 117.726 1.00 6.73   ? 1815 LEU A CA    1 
ATOM   2221  C  C     . LEU A 1 1815 ? 163.201 179.308 117.883 1.00 7.74   ? 1815 LEU A C     1 
ATOM   2222  O  O     . LEU A 1 1815 ? 163.786 178.597 117.064 1.00 11.57  ? 1815 LEU A O     1 
ATOM   2223  C  CB    . LEU A 1 1815 ? 161.446 180.673 116.713 1.00 7.58   ? 1815 LEU A CB    1 
ATOM   2224  C  CG    . LEU A 1 1815 ? 160.120 180.576 115.950 1.00 6.56   ? 1815 LEU A CG    1 
ATOM   2225  C  CD1   . LEU A 1 1815 ? 158.895 180.681 116.845 1.00 10.35  ? 1815 LEU A CD1   1 
ATOM   2226  C  CD2   . LEU A 1 1815 ? 160.076 181.629 114.871 1.00 14.35  ? 1815 LEU A CD2   1 
ATOM   2227  N  N     . VAL A 1 1816 ? 163.835 179.850 118.925 1.00 5.82   ? 1816 VAL A N     1 
ATOM   2228  C  CA    . VAL A 1 1816 ? 165.209 179.455 119.221 1.00 6.43   ? 1816 VAL A CA    1 
ATOM   2229  C  C     . VAL A 1 1816 ? 165.256 177.985 119.615 1.00 7.80   ? 1816 VAL A C     1 
ATOM   2230  O  O     . VAL A 1 1816 ? 166.131 177.228 119.166 1.00 10.56  ? 1816 VAL A O     1 
ATOM   2231  C  CB    . VAL A 1 1816 ? 165.806 180.361 120.315 1.00 6.14   ? 1816 VAL A CB    1 
ATOM   2232  C  CG1   . VAL A 1 1816 ? 166.978 179.680 120.997 1.00 6.49   ? 1816 VAL A CG1   1 
ATOM   2233  C  CG2   . VAL A 1 1816 ? 166.243 181.687 119.717 1.00 8.50   ? 1816 VAL A CG2   1 
ATOM   2234  N  N     . HIS A 1 1817 ? 164.304 177.551 120.446 1.00 7.62   ? 1817 HIS A N     1 
ATOM   2235  C  CA    . HIS A 1 1817 ? 164.224 176.131 120.780 1.00 6.61   ? 1817 HIS A CA    1 
ATOM   2236  C  C     . HIS A 1 1817 ? 163.966 175.287 119.535 1.00 9.23   ? 1817 HIS A C     1 
ATOM   2237  O  O     . HIS A 1 1817 ? 164.560 174.214 119.366 1.00 11.83  ? 1817 HIS A O     1 
ATOM   2238  C  CB    . HIS A 1 1817 ? 163.137 175.894 121.826 1.00 7.73   ? 1817 HIS A CB    1 
ATOM   2239  C  CG    . HIS A 1 1817 ? 162.899 174.448 122.129 1.00 7.17   ? 1817 HIS A CG    1 
ATOM   2240  N  ND1   . HIS A 1 1817 ? 163.894 173.609 122.581 1.00 7.20   ? 1817 HIS A ND1   1 
ATOM   2241  C  CD2   . HIS A 1 1817 ? 161.781 173.690 122.041 1.00 6.18   ? 1817 HIS A CD2   1 
ATOM   2242  C  CE1   . HIS A 1 1817 ? 163.400 172.398 122.760 1.00 6.53   ? 1817 HIS A CE1   1 
ATOM   2243  N  NE2   . HIS A 1 1817 ? 162.119 172.420 122.440 1.00 5.49   ? 1817 HIS A NE2   1 
ATOM   2244  N  N     . GLN A 1 1818 ? 163.080 175.758 118.655 1.00 8.80   ? 1818 GLN A N     1 
ATOM   2245  C  CA    . GLN A 1 1818 ? 162.794 175.035 117.418 1.00 6.86   ? 1818 GLN A CA    1 
ATOM   2246  C  C     . GLN A 1 1818 ? 164.032 174.933 116.537 1.00 9.15   ? 1818 GLN A C     1 
ATOM   2247  O  O     . GLN A 1 1818 ? 164.285 173.888 115.928 1.00 10.89  ? 1818 GLN A O     1 
ATOM   2248  C  CB    . GLN A 1 1818 ? 161.660 175.720 116.658 1.00 5.99   ? 1818 GLN A CB    1 
ATOM   2249  C  CG    . GLN A 1 1818 ? 160.307 175.627 117.331 1.00 6.86   ? 1818 GLN A CG    1 
ATOM   2250  C  CD    . GLN A 1 1818 ? 159.249 176.440 116.615 1.00 6.91   ? 1818 GLN A CD    1 
ATOM   2251  O  OE1   . GLN A 1 1818 ? 159.524 177.080 115.601 1.00 6.33   ? 1818 GLN A OE1   1 
ATOM   2252  N  NE2   . GLN A 1 1818 ? 158.031 176.418 117.139 1.00 8.71   ? 1818 GLN A NE2   1 
ATOM   2253  N  N     . ARG A 1 1819 ? 164.805 176.016 116.443 1.00 11.31  ? 1819 ARG A N     1 
ATOM   2254  C  CA    . ARG A 1 1819 ? 166.036 175.997 115.663 1.00 13.77  ? 1819 ARG A CA    1 
ATOM   2255  C  C     . ARG A 1 1819 ? 167.033 175.000 116.235 1.00 13.49  ? 1819 ARG A C     1 
ATOM   2256  O  O     . ARG A 1 1819 ? 167.677 174.256 115.486 1.00 16.49  ? 1819 ARG A O     1 
ATOM   2257  C  CB    . ARG A 1 1819 ? 166.644 177.398 115.620 1.00 12.71  ? 1819 ARG A CB    1 
ATOM   2258  C  CG    . ARG A 1 1819 ? 167.909 177.512 114.792 1.00 15.67  ? 1819 ARG A CG    1 
ATOM   2259  C  CD    . ARG A 1 1819 ? 168.673 178.770 115.156 1.00 18.03  ? 1819 ARG A CD    1 
ATOM   2260  N  NE    . ARG A 1 1819 ? 169.086 178.763 116.554 1.00 17.87  ? 1819 ARG A NE    1 
ATOM   2261  C  CZ    . ARG A 1 1819 ? 169.421 179.846 117.242 1.00 20.74  ? 1819 ARG A CZ    1 
ATOM   2262  N  NH1   . ARG A 1 1819 ? 169.403 181.048 116.690 1.00 20.68  ? 1819 ARG A NH1   1 
ATOM   2263  N  NH2   . ARG A 1 1819 ? 169.781 179.719 118.516 1.00 24.15  ? 1819 ARG A NH2   1 
ATOM   2264  N  N     . ASP A 1 1820 ? 167.174 174.971 117.562 1.00 12.93  ? 1820 ASP A N     1 
ATOM   2265  C  CA    . ASP A 1 1820 ? 168.079 174.006 118.181 1.00 13.30  ? 1820 ASP A CA    1 
ATOM   2266  C  C     . ASP A 1 1820 ? 167.634 172.573 117.905 1.00 13.11  ? 1820 ASP A C     1 
ATOM   2267  O  O     . ASP A 1 1820 ? 168.458 171.709 117.577 1.00 13.78  ? 1820 ASP A O     1 
ATOM   2268  C  CB    . ASP A 1 1820 ? 168.168 174.263 119.686 1.00 14.95  ? 1820 ASP A CB    1 
ATOM   2269  C  CG    . ASP A 1 1820 ? 168.907 175.547 120.015 1.00 28.14  ? 1820 ASP A CG    1 
ATOM   2270  O  OD1   . ASP A 1 1820 ? 169.416 176.199 119.079 1.00 26.85  ? 1820 ASP A OD1   1 
ATOM   2271  O  OD2   . ASP A 1 1820 ? 168.975 175.908 121.209 1.00 24.36  ? 1820 ASP A OD2   1 
ATOM   2272  N  N     . VAL A 1 1821 ? 166.331 172.306 118.018 1.00 15.20  ? 1821 VAL A N     1 
ATOM   2273  C  CA    . VAL A 1 1821 ? 165.827 170.956 117.774 1.00 12.21  ? 1821 VAL A CA    1 
ATOM   2274  C  C     . VAL A 1 1821 ? 166.031 170.560 116.316 1.00 12.37  ? 1821 VAL A C     1 
ATOM   2275  O  O     . VAL A 1 1821 ? 166.415 169.423 116.016 1.00 18.96  ? 1821 VAL A O     1 
ATOM   2276  C  CB    . VAL A 1 1821 ? 164.349 170.852 118.190 1.00 7.74   ? 1821 VAL A CB    1 
ATOM   2277  C  CG1   . VAL A 1 1821 ? 163.763 169.528 117.735 1.00 9.53   ? 1821 VAL A CG1   1 
ATOM   2278  C  CG2   . VAL A 1 1821 ? 164.213 170.999 119.691 1.00 6.89   ? 1821 VAL A CG2   1 
ATOM   2279  N  N     . THR A 1 1822 ? 165.768 171.481 115.388 1.00 10.79  ? 1822 THR A N     1 
ATOM   2280  C  CA    . THR A 1 1822 ? 165.950 171.180 113.973 1.00 12.88  ? 1822 THR A CA    1 
ATOM   2281  C  C     . THR A 1 1822 ? 167.417 170.936 113.646 1.00 18.18  ? 1822 THR A C     1 
ATOM   2282  O  O     . THR A 1 1822 ? 167.743 170.044 112.853 1.00 19.38  ? 1822 THR A O     1 
ATOM   2283  C  CB    . THR A 1 1822 ? 165.388 172.316 113.120 1.00 14.26  ? 1822 THR A CB    1 
ATOM   2284  O  OG1   . THR A 1 1822 ? 163.991 172.470 113.395 1.00 18.59  ? 1822 THR A OG1   1 
ATOM   2285  C  CG2   . THR A 1 1822 ? 165.560 172.005 111.646 1.00 16.69  ? 1822 THR A CG2   1 
ATOM   2286  N  N     . ARG A 1 1823 ? 168.319 171.717 114.246 1.00 17.03  ? 1823 ARG A N     1 
ATOM   2287  C  CA    . ARG A 1 1823 ? 169.745 171.486 114.044 1.00 16.61  ? 1823 ARG A CA    1 
ATOM   2288  C  C     . ARG A 1 1823 ? 170.163 170.125 114.583 1.00 20.03  ? 1823 ARG A C     1 
ATOM   2289  O  O     . ARG A 1 1823 ? 170.965 169.422 113.958 1.00 20.80  ? 1823 ARG A O     1 
ATOM   2290  C  CB    . ARG A 1 1823 ? 170.556 172.599 114.706 1.00 16.22  ? 1823 ARG A CB    1 
ATOM   2291  C  CG    . ARG A 1 1823 ? 170.653 173.869 113.881 1.00 15.83  ? 1823 ARG A CG    1 
ATOM   2292  C  CD    . ARG A 1 1823 ? 171.337 174.979 114.659 1.00 13.72  ? 1823 ARG A CD    1 
ATOM   2293  N  NE    . ARG A 1 1823 ? 171.436 176.209 113.882 1.00 17.00  ? 1823 ARG A NE    1 
ATOM   2294  C  CZ    . ARG A 1 1823 ? 171.743 177.393 114.393 1.00 24.05  ? 1823 ARG A CZ    1 
ATOM   2295  N  NH1   . ARG A 1 1823 ? 171.990 177.546 115.683 1.00 26.64  ? 1823 ARG A NH1   1 
ATOM   2296  N  NH2   . ARG A 1 1823 ? 171.802 178.451 113.589 1.00 21.50  ? 1823 ARG A NH2   1 
ATOM   2297  N  N     . SER A 1 1824 ? 169.638 169.739 115.749 1.00 19.72  ? 1824 SER A N     1 
ATOM   2298  C  CA    . SER A 1 1824 ? 169.944 168.418 116.291 1.00 17.64  ? 1824 SER A CA    1 
ATOM   2299  C  C     . SER A 1 1824 ? 169.426 167.312 115.380 1.00 20.79  ? 1824 SER A C     1 
ATOM   2300  O  O     . SER A 1 1824 ? 170.104 166.300 115.171 1.00 26.03  ? 1824 SER A O     1 
ATOM   2301  C  CB    . SER A 1 1824 ? 169.360 168.274 117.696 1.00 20.21  ? 1824 SER A CB    1 
ATOM   2302  O  OG    . SER A 1 1824 ? 169.962 169.188 118.595 1.00 36.05  ? 1824 SER A OG    1 
ATOM   2303  N  N     . LEU A 1 1825 ? 168.219 167.484 114.837 1.00 18.30  ? 1825 LEU A N     1 
ATOM   2304  C  CA    . LEU A 1 1825 ? 167.674 166.491 113.916 1.00 21.01  ? 1825 LEU A CA    1 
ATOM   2305  C  C     . LEU A 1 1825 ? 168.518 166.384 112.652 1.00 21.13  ? 1825 LEU A C     1 
ATOM   2306  O  O     . LEU A 1 1825 ? 168.775 165.280 112.159 1.00 26.21  ? 1825 LEU A O     1 
ATOM   2307  C  CB    . LEU A 1 1825 ? 166.227 166.836 113.564 1.00 18.27  ? 1825 LEU A CB    1 
ATOM   2308  C  CG    . LEU A 1 1825 ? 165.153 166.542 114.613 1.00 17.10  ? 1825 LEU A CG    1 
ATOM   2309  C  CD1   . LEU A 1 1825 ? 163.782 166.517 113.966 1.00 13.42  ? 1825 LEU A CD1   1 
ATOM   2310  C  CD2   . LEU A 1 1825 ? 165.430 165.229 115.322 1.00 18.61  ? 1825 LEU A CD2   1 
ATOM   2311  N  N     . ILE A 1 1826 ? 168.949 167.524 112.108 1.00 21.95  ? 1826 ILE A N     1 
ATOM   2312  C  CA    . ILE A 1 1826 ? 169.747 167.514 110.886 1.00 19.81  ? 1826 ILE A CA    1 
ATOM   2313  C  C     . ILE A 1 1826 ? 171.105 166.870 111.134 1.00 22.40  ? 1826 ILE A C     1 
ATOM   2314  O  O     . ILE A 1 1826 ? 171.578 166.057 110.330 1.00 26.53  ? 1826 ILE A O     1 
ATOM   2315  C  CB    . ILE A 1 1826 ? 169.888 168.944 110.333 1.00 15.96  ? 1826 ILE A CB    1 
ATOM   2316  C  CG1   . ILE A 1 1826 ? 168.585 169.385 109.666 1.00 19.35  ? 1826 ILE A CG1   1 
ATOM   2317  C  CG2   . ILE A 1 1826 ? 171.049 169.031 109.360 1.00 20.12  ? 1826 ILE A CG2   1 
ATOM   2318  C  CD1   . ILE A 1 1826 ? 168.599 170.812 109.177 1.00 19.65  ? 1826 ILE A CD1   1 
ATOM   2319  N  N     . LYS A 1 1827 ? 171.750 167.215 112.251 1.00 22.50  ? 1827 LYS A N     1 
ATOM   2320  C  CA    . LYS A 1 1827 ? 173.061 166.651 112.556 1.00 21.63  ? 1827 LYS A CA    1 
ATOM   2321  C  C     . LYS A 1 1827 ? 172.983 165.142 112.741 1.00 33.50  ? 1827 LYS A C     1 
ATOM   2322  O  O     . LYS A 1 1827 ? 173.879 164.407 112.309 1.00 40.17  ? 1827 LYS A O     1 
ATOM   2323  C  CB    . LYS A 1 1827 ? 173.636 167.319 113.804 1.00 25.67  ? 1827 LYS A CB    1 
ATOM   2324  C  CG    . LYS A 1 1827 ? 175.015 166.825 114.196 1.00 33.69  ? 1827 LYS A CG    1 
ATOM   2325  C  CD    . LYS A 1 1827 ? 175.511 167.517 115.452 1.00 29.15  ? 1827 LYS A CD    1 
ATOM   2326  C  CE    . LYS A 1 1827 ? 176.988 167.248 115.676 1.00 31.47  ? 1827 LYS A CE    1 
ATOM   2327  N  NZ    . LYS A 1 1827 ? 177.810 167.702 114.520 1.00 27.47  ? 1827 LYS A NZ    1 
ATOM   2328  N  N     . SER A 1 1828 ? 171.916 164.660 113.374 1.00 33.79  ? 1828 SER A N     1 
ATOM   2329  C  CA    . SER A 1 1828 ? 171.728 163.236 113.615 1.00 28.97  ? 1828 SER A CA    1 
ATOM   2330  C  C     . SER A 1 1828 ? 171.290 162.474 112.371 1.00 30.39  ? 1828 SER A C     1 
ATOM   2331  O  O     . SER A 1 1828 ? 171.188 161.244 112.429 1.00 40.13  ? 1828 SER A O     1 
ATOM   2332  C  CB    . SER A 1 1828 ? 170.703 163.028 114.733 1.00 36.76  ? 1828 SER A CB    1 
ATOM   2333  O  OG    . SER A 1 1828 ? 170.476 161.650 114.967 1.00 51.52  ? 1828 SER A OG    1 
ATOM   2334  N  N     . LYS A 1 1829 ? 171.027 163.169 111.262 1.00 30.29  ? 1829 LYS A N     1 
ATOM   2335  C  CA    . LYS A 1 1829 ? 170.594 162.543 110.012 1.00 35.02  ? 1829 LYS A CA    1 
ATOM   2336  C  C     . LYS A 1 1829 ? 169.325 161.718 110.213 1.00 44.14  ? 1829 LYS A C     1 
ATOM   2337  O  O     . LYS A 1 1829 ? 169.211 160.587 109.737 1.00 47.97  ? 1829 LYS A O     1 
ATOM   2338  C  CB    . LYS A 1 1829 ? 171.709 161.690 109.403 1.00 38.37  ? 1829 LYS A CB    1 
ATOM   2339  C  CG    . LYS A 1 1829 ? 172.955 162.475 109.032 1.00 38.38  ? 1829 LYS A CG    1 
ATOM   2340  C  CD    . LYS A 1 1829 ? 174.186 161.587 109.042 1.00 45.38  ? 1829 LYS A CD    1 
ATOM   2341  C  CE    . LYS A 1 1829 ? 174.712 161.397 110.456 1.00 41.89  ? 1829 LYS A CE    1 
ATOM   2342  N  NZ    . LYS A 1 1829 ? 175.459 162.591 110.938 1.00 38.17  ? 1829 LYS A NZ    1 
ATOM   2343  N  N     . ILE A 1 1830 ? 168.361 162.292 110.927 1.00 41.42  ? 1830 ILE A N     1 
ATOM   2344  C  CA    . ILE A 1 1830 ? 167.084 161.631 111.169 1.00 40.78  ? 1830 ILE A CA    1 
ATOM   2345  C  C     . ILE A 1 1830 ? 166.220 161.769 109.923 1.00 42.91  ? 1830 ILE A C     1 
ATOM   2346  O  O     . ILE A 1 1830 ? 165.881 162.883 109.510 1.00 49.60  ? 1830 ILE A O     1 
ATOM   2347  C  CB    . ILE A 1 1830 ? 166.381 162.222 112.398 1.00 31.87  ? 1830 ILE A CB    1 
ATOM   2348  C  CG1   . ILE A 1 1830 ? 167.263 162.064 113.636 1.00 33.62  ? 1830 ILE A CG1   1 
ATOM   2349  C  CG2   . ILE A 1 1830 ? 165.030 161.563 112.608 1.00 34.87  ? 1830 ILE A CG2   1 
ATOM   2350  C  CD1   . ILE A 1 1830 ? 167.571 160.625 113.975 1.00 35.22  ? 1830 ILE A CD1   1 
ATOM   2351  N  N     . ASP A 1 1831 ? 165.857 160.636 109.325 1.00 36.30  ? 1831 ASP A N     1 
ATOM   2352  C  CA    . ASP A 1 1831 ? 165.034 160.625 108.126 1.00 42.83  ? 1831 ASP A CA    1 
ATOM   2353  C  C     . ASP A 1 1831 ? 163.693 159.938 108.328 1.00 44.07  ? 1831 ASP A C     1 
ATOM   2354  O  O     . ASP A 1 1831 ? 162.894 159.885 107.386 1.00 50.17  ? 1831 ASP A O     1 
ATOM   2355  C  CB    . ASP A 1 1831 ? 165.786 159.950 106.971 1.00 51.13  ? 1831 ASP A CB    1 
ATOM   2356  C  CG    . ASP A 1 1831 ? 166.295 158.572 107.334 1.00 53.77  ? 1831 ASP A CG    1 
ATOM   2357  O  OD1   . ASP A 1 1831 ? 166.449 158.295 108.541 1.00 57.10  ? 1831 ASP A OD1   1 
ATOM   2358  O  OD2   . ASP A 1 1831 ? 166.540 157.767 106.412 1.00 57.60  ? 1831 ASP A OD2   1 
ATOM   2359  N  N     . ASN A 1 1832 ? 163.419 159.418 109.519 1.00 38.31  ? 1832 ASN A N     1 
ATOM   2360  C  CA    . ASN A 1 1832 ? 162.174 158.725 109.814 1.00 32.87  ? 1832 ASN A CA    1 
ATOM   2361  C  C     . ASN A 1 1832 ? 161.394 159.516 110.854 1.00 27.78  ? 1832 ASN A C     1 
ATOM   2362  O  O     . ASN A 1 1832 ? 161.957 159.938 111.869 1.00 30.02  ? 1832 ASN A O     1 
ATOM   2363  C  CB    . ASN A 1 1832 ? 162.447 157.305 110.317 1.00 29.96  ? 1832 ASN A CB    1 
ATOM   2364  C  CG    . ASN A 1 1832 ? 161.176 156.546 110.642 1.00 27.66  ? 1832 ASN A CG    1 
ATOM   2365  O  OD1   . ASN A 1 1832 ? 160.098 156.876 110.149 1.00 28.01  ? 1832 ASN A OD1   1 
ATOM   2366  N  ND2   . ASN A 1 1832 ? 161.299 155.522 111.477 1.00 27.68  ? 1832 ASN A ND2   1 
ATOM   2367  N  N     . ALA A 1 1833 ? 160.101 159.718 110.595 1.00 22.99  ? 1833 ALA A N     1 
ATOM   2368  C  CA    . ALA A 1 1833 ? 159.251 160.408 111.556 1.00 18.20  ? 1833 ALA A CA    1 
ATOM   2369  C  C     . ALA A 1 1833 ? 159.003 159.578 112.807 1.00 22.29  ? 1833 ALA A C     1 
ATOM   2370  O  O     . ALA A 1 1833 ? 158.567 160.127 113.823 1.00 26.91  ? 1833 ALA A O     1 
ATOM   2371  C  CB    . ALA A 1 1833 ? 157.919 160.785 110.909 1.00 24.63  ? 1833 ALA A CB    1 
ATOM   2372  N  N     . LYS A 1 1834 ? 159.265 158.274 112.756 1.00 24.72  ? 1834 LYS A N     1 
ATOM   2373  C  CA    . LYS A 1 1834 ? 159.107 157.397 113.907 1.00 19.70  ? 1834 LYS A CA    1 
ATOM   2374  C  C     . LYS A 1 1834 ? 160.399 157.205 114.690 1.00 21.48  ? 1834 LYS A C     1 
ATOM   2375  O  O     . LYS A 1 1834 ? 160.416 156.418 115.641 1.00 22.53  ? 1834 LYS A O     1 
ATOM   2376  C  CB    . LYS A 1 1834 ? 158.566 156.035 113.464 1.00 24.35  ? 1834 LYS A CB    1 
ATOM   2377  C  CG    . LYS A 1 1834 ? 157.186 156.094 112.833 1.00 26.86  ? 1834 LYS A CG    1 
ATOM   2378  C  CD    . LYS A 1 1834 ? 156.145 156.570 113.832 1.00 28.99  ? 1834 LYS A CD    1 
ATOM   2379  C  CE    . LYS A 1 1834 ? 155.877 155.519 114.895 1.00 35.79  ? 1834 LYS A CE    1 
ATOM   2380  N  NZ    . LYS A 1 1834 ? 154.805 155.945 115.836 1.00 30.06  ? 1834 LYS A NZ    1 
ATOM   2381  N  N     . SER A 1 1835 ? 161.473 157.894 114.315 1.00 19.67  ? 1835 SER A N     1 
ATOM   2382  C  CA    . SER A 1 1835 ? 162.712 157.818 115.075 1.00 19.02  ? 1835 SER A CA    1 
ATOM   2383  C  C     . SER A 1 1835 ? 162.551 158.515 116.420 1.00 19.36  ? 1835 SER A C     1 
ATOM   2384  O  O     . SER A 1 1835 ? 161.924 159.573 116.515 1.00 27.04  ? 1835 SER A O     1 
ATOM   2385  C  CB    . SER A 1 1835 ? 163.859 158.450 114.290 1.00 25.01  ? 1835 SER A CB    1 
ATOM   2386  O  OG    . SER A 1 1835 ? 165.009 158.602 115.102 1.00 31.05  ? 1835 SER A OG    1 
ATOM   2387  N  N     . PHE A 1 1836 ? 163.132 157.920 117.464 1.00 19.91  ? 1836 PHE A N     1 
ATOM   2388  C  CA    . PHE A 1 1836 ? 162.960 158.456 118.810 1.00 14.88  ? 1836 PHE A CA    1 
ATOM   2389  C  C     . PHE A 1 1836 ? 163.574 159.837 118.981 1.00 12.10  ? 1836 PHE A C     1 
ATOM   2390  O  O     . PHE A 1 1836 ? 163.187 160.558 119.907 1.00 12.61  ? 1836 PHE A O     1 
ATOM   2391  C  CB    . PHE A 1 1836 ? 163.547 157.502 119.849 1.00 10.55  ? 1836 PHE A CB    1 
ATOM   2392  C  CG    . PHE A 1 1836 ? 163.096 157.794 121.250 1.00 7.23   ? 1836 PHE A CG    1 
ATOM   2393  C  CD1   . PHE A 1 1836 ? 161.783 157.574 121.628 1.00 7.24   ? 1836 PHE A CD1   1 
ATOM   2394  C  CD2   . PHE A 1 1836 ? 163.981 158.296 122.185 1.00 6.48   ? 1836 PHE A CD2   1 
ATOM   2395  C  CE1   . PHE A 1 1836 ? 161.365 157.845 122.914 1.00 7.16   ? 1836 PHE A CE1   1 
ATOM   2396  C  CE2   . PHE A 1 1836 ? 163.566 158.569 123.471 1.00 7.66   ? 1836 PHE A CE2   1 
ATOM   2397  C  CZ    . PHE A 1 1836 ? 162.257 158.342 123.837 1.00 8.44   ? 1836 PHE A CZ    1 
ATOM   2398  N  N     . GLU A 1 1837 ? 164.515 160.226 118.120 1.00 14.77  ? 1837 GLU A N     1 
ATOM   2399  C  CA    . GLU A 1 1837 ? 165.057 161.578 118.199 1.00 18.65  ? 1837 GLU A CA    1 
ATOM   2400  C  C     . GLU A 1 1837 ? 163.991 162.621 117.888 1.00 16.14  ? 1837 GLU A C     1 
ATOM   2401  O  O     . GLU A 1 1837 ? 164.148 163.795 118.242 1.00 14.25  ? 1837 GLU A O     1 
ATOM   2402  C  CB    . GLU A 1 1837 ? 166.245 161.720 117.251 1.00 21.91  ? 1837 GLU A CB    1 
ATOM   2403  C  CG    . GLU A 1 1837 ? 167.506 161.033 117.744 1.00 27.48  ? 1837 GLU A CG    1 
ATOM   2404  C  CD    . GLU A 1 1837 ? 167.581 159.578 117.322 1.00 39.20  ? 1837 GLU A CD    1 
ATOM   2405  O  OE1   . GLU A 1 1837 ? 166.612 159.082 116.709 1.00 30.66  ? 1837 GLU A OE1   1 
ATOM   2406  O  OE2   . GLU A 1 1837 ? 168.611 158.929 117.601 1.00 45.30  ? 1837 GLU A OE2   1 
ATOM   2407  N  N     . TRP A 1 1838 ? 162.906 162.214 117.232 1.00 11.99  ? 1838 TRP A N     1 
ATOM   2408  C  CA    . TRP A 1 1838 ? 161.773 163.091 116.975 1.00 10.39  ? 1838 TRP A CA    1 
ATOM   2409  C  C     . TRP A 1 1838 ? 160.615 162.866 117.935 1.00 12.42  ? 1838 TRP A C     1 
ATOM   2410  O  O     . TRP A 1 1838 ? 159.909 163.823 118.268 1.00 13.45  ? 1838 TRP A O     1 
ATOM   2411  C  CB    . TRP A 1 1838 ? 161.285 162.911 115.533 1.00 10.16  ? 1838 TRP A CB    1 
ATOM   2412  C  CG    . TRP A 1 1838 ? 160.037 163.674 115.205 1.00 10.42  ? 1838 TRP A CG    1 
ATOM   2413  C  CD1   . TRP A 1 1838 ? 158.870 163.161 114.723 1.00 11.49  ? 1838 TRP A CD1   1 
ATOM   2414  C  CD2   . TRP A 1 1838 ? 159.830 165.086 115.336 1.00 9.91   ? 1838 TRP A CD2   1 
ATOM   2415  N  NE1   . TRP A 1 1838 ? 157.950 164.163 114.543 1.00 12.20  ? 1838 TRP A NE1   1 
ATOM   2416  C  CE2   . TRP A 1 1838 ? 158.514 165.355 114.912 1.00 11.67  ? 1838 TRP A CE2   1 
ATOM   2417  C  CE3   . TRP A 1 1838 ? 160.629 166.149 115.769 1.00 8.12   ? 1838 TRP A CE3   1 
ATOM   2418  C  CZ2   . TRP A 1 1838 ? 157.980 166.640 114.910 1.00 14.25  ? 1838 TRP A CZ2   1 
ATOM   2419  C  CZ3   . TRP A 1 1838 ? 160.096 167.422 115.767 1.00 10.12  ? 1838 TRP A CZ3   1 
ATOM   2420  C  CH2   . TRP A 1 1838 ? 158.784 167.657 115.342 1.00 13.04  ? 1838 TRP A CH2   1 
ATOM   2421  N  N     . LEU A 1 1839 ? 160.401 161.629 118.390 1.00 11.42  ? 1839 LEU A N     1 
ATOM   2422  C  CA    . LEU A 1 1839 ? 159.341 161.381 119.362 1.00 10.40  ? 1839 LEU A CA    1 
ATOM   2423  C  C     . LEU A 1 1839 ? 159.720 161.858 120.757 1.00 10.77  ? 1839 LEU A C     1 
ATOM   2424  O  O     . LEU A 1 1839 ? 158.835 162.195 121.551 1.00 15.73  ? 1839 LEU A O     1 
ATOM   2425  C  CB    . LEU A 1 1839 ? 158.964 159.898 119.391 1.00 10.85  ? 1839 LEU A CB    1 
ATOM   2426  C  CG    . LEU A 1 1839 ? 158.070 159.375 118.261 1.00 13.07  ? 1839 LEU A CG    1 
ATOM   2427  C  CD1   . LEU A 1 1839 ? 158.800 159.297 116.943 1.00 17.42  ? 1839 LEU A CD1   1 
ATOM   2428  C  CD2   . LEU A 1 1839 ? 157.488 158.019 118.627 1.00 13.43  ? 1839 LEU A CD2   1 
ATOM   2429  N  N     . SER A 1 1840 ? 161.014 161.902 121.076 1.00 7.53   ? 1840 SER A N     1 
ATOM   2430  C  CA    . SER A 1 1840 ? 161.432 162.439 122.365 1.00 8.06   ? 1840 SER A CA    1 
ATOM   2431  C  C     . SER A 1 1840 ? 161.164 163.932 122.492 1.00 9.66   ? 1840 SER A C     1 
ATOM   2432  O  O     . SER A 1 1840 ? 161.246 164.467 123.602 1.00 9.37   ? 1840 SER A O     1 
ATOM   2433  C  CB    . SER A 1 1840 ? 162.915 162.157 122.603 1.00 9.39   ? 1840 SER A CB    1 
ATOM   2434  O  OG    . SER A 1 1840 ? 163.690 162.505 121.470 1.00 15.45  ? 1840 SER A OG    1 
ATOM   2435  N  N     . GLN A 1 1841 ? 160.853 164.612 121.392 1.00 11.35  ? 1841 GLN A N     1 
ATOM   2436  C  CA    . GLN A 1 1841 ? 160.503 166.020 121.431 1.00 9.85   ? 1841 GLN A CA    1 
ATOM   2437  C  C     . GLN A 1 1841 ? 159.003 166.194 121.649 1.00 8.14   ? 1841 GLN A C     1 
ATOM   2438  O  O     . GLN A 1 1841 ? 158.208 165.267 121.472 1.00 7.75   ? 1841 GLN A O     1 
ATOM   2439  C  CB    . GLN A 1 1841 ? 160.921 166.717 120.136 1.00 7.67   ? 1841 GLN A CB    1 
ATOM   2440  C  CG    . GLN A 1 1841 ? 162.332 166.397 119.679 1.00 7.33   ? 1841 GLN A CG    1 
ATOM   2441  C  CD    . GLN A 1 1841 ? 163.384 166.902 120.640 1.00 10.56  ? 1841 GLN A CD    1 
ATOM   2442  O  OE1   . GLN A 1 1841 ? 163.323 168.039 121.103 1.00 14.56  ? 1841 GLN A OE1   1 
ATOM   2443  N  NE2   . GLN A 1 1841 ? 164.358 166.057 120.947 1.00 12.40  ? 1841 GLN A NE2   1 
ATOM   2444  N  N     . MET A 1 1842 ? 158.623 167.406 122.043 1.00 7.15   ? 1842 MET A N     1 
ATOM   2445  C  CA    . MET A 1 1842 ? 157.216 167.767 122.163 1.00 5.71   ? 1842 MET A CA    1 
ATOM   2446  C  C     . MET A 1 1842 ? 156.677 168.139 120.787 1.00 6.89   ? 1842 MET A C     1 
ATOM   2447  O  O     . MET A 1 1842 ? 157.161 169.088 120.162 1.00 11.54  ? 1842 MET A O     1 
ATOM   2448  C  CB    . MET A 1 1842 ? 157.047 168.924 123.143 1.00 4.75   ? 1842 MET A CB    1 
ATOM   2449  C  CG    . MET A 1 1842 ? 155.631 169.113 123.648 1.00 6.07   ? 1842 MET A CG    1 
ATOM   2450  S  SD    . MET A 1 1842 ? 155.560 169.812 125.306 1.00 16.13  ? 1842 MET A SD    1 
ATOM   2451  C  CE    . MET A 1 1842 ? 155.464 168.329 126.302 1.00 9.19   ? 1842 MET A CE    1 
ATOM   2452  N  N     . ARG A 1 1843 ? 155.680 167.397 120.315 1.00 7.02   ? 1843 ARG A N     1 
ATOM   2453  C  CA    . ARG A 1 1843 ? 155.125 167.579 118.983 1.00 6.18   ? 1843 ARG A CA    1 
ATOM   2454  C  C     . ARG A 1 1843 ? 153.654 167.948 119.093 1.00 8.67   ? 1843 ARG A C     1 
ATOM   2455  O  O     . ARG A 1 1843 ? 152.947 167.466 119.985 1.00 9.88   ? 1843 ARG A O     1 
ATOM   2456  C  CB    . ARG A 1 1843 ? 155.295 166.312 118.140 1.00 8.52   ? 1843 ARG A CB    1 
ATOM   2457  C  CG    . ARG A 1 1843 ? 156.561 165.541 118.464 1.00 7.74   ? 1843 ARG A CG    1 
ATOM   2458  C  CD    . ARG A 1 1843 ? 156.644 164.226 117.712 1.00 8.79   ? 1843 ARG A CD    1 
ATOM   2459  N  NE    . ARG A 1 1843 ? 155.619 163.269 118.114 1.00 11.77  ? 1843 ARG A NE    1 
ATOM   2460  C  CZ    . ARG A 1 1843 ? 155.634 162.574 119.243 1.00 10.44  ? 1843 ARG A CZ    1 
ATOM   2461  N  NH1   . ARG A 1 1843 ? 156.571 162.759 120.158 1.00 8.04   ? 1843 ARG A NH1   1 
ATOM   2462  N  NH2   . ARG A 1 1843 ? 154.681 161.674 119.463 1.00 13.88  ? 1843 ARG A NH2   1 
ATOM   2463  N  N     . PHE A 1 1844 ? 153.199 168.805 118.185 1.00 10.71  ? 1844 PHE A N     1 
ATOM   2464  C  CA    . PHE A 1 1844 ? 151.844 169.337 118.208 1.00 9.57   ? 1844 PHE A CA    1 
ATOM   2465  C  C     . PHE A 1 1844 ? 151.122 168.927 116.935 1.00 13.33  ? 1844 PHE A C     1 
ATOM   2466  O  O     . PHE A 1 1844 ? 151.605 169.191 115.830 1.00 15.91  ? 1844 PHE A O     1 
ATOM   2467  C  CB    . PHE A 1 1844 ? 151.858 170.862 118.353 1.00 7.83   ? 1844 PHE A CB    1 
ATOM   2468  C  CG    . PHE A 1 1844 ? 152.565 171.345 119.588 1.00 7.43   ? 1844 PHE A CG    1 
ATOM   2469  C  CD1   . PHE A 1 1844 ? 153.948 171.406 119.635 1.00 8.11   ? 1844 PHE A CD1   1 
ATOM   2470  C  CD2   . PHE A 1 1844 ? 151.847 171.730 120.704 1.00 6.70   ? 1844 PHE A CD2   1 
ATOM   2471  C  CE1   . PHE A 1 1844 ? 154.597 171.842 120.770 1.00 6.40   ? 1844 PHE A CE1   1 
ATOM   2472  C  CE2   . PHE A 1 1844 ? 152.493 172.168 121.839 1.00 7.17   ? 1844 PHE A CE2   1 
ATOM   2473  C  CZ    . PHE A 1 1844 ? 153.869 172.224 121.872 1.00 6.29   ? 1844 PHE A CZ    1 
ATOM   2474  N  N     . TYR A 1 1845 ? 149.967 168.288 117.094 1.00 18.35  ? 1845 TYR A N     1 
ATOM   2475  C  CA    . TYR A 1 1845 ? 149.174 167.791 115.981 1.00 17.76  ? 1845 TYR A CA    1 
ATOM   2476  C  C     . TYR A 1 1845 ? 147.819 168.478 115.984 1.00 21.55  ? 1845 TYR A C     1 
ATOM   2477  O  O     . TYR A 1 1845 ? 147.114 168.472 116.999 1.00 19.94  ? 1845 TYR A O     1 
ATOM   2478  C  CB    . TYR A 1 1845 ? 149.017 166.273 116.066 1.00 14.60  ? 1845 TYR A CB    1 
ATOM   2479  C  CG    . TYR A 1 1845 ? 150.339 165.547 116.019 1.00 16.05  ? 1845 TYR A CG    1 
ATOM   2480  C  CD1   . TYR A 1 1845 ? 151.069 165.479 114.841 1.00 18.63  ? 1845 TYR A CD1   1 
ATOM   2481  C  CD2   . TYR A 1 1845 ? 150.873 164.959 117.155 1.00 19.74  ? 1845 TYR A CD2   1 
ATOM   2482  C  CE1   . TYR A 1 1845 ? 152.281 164.826 114.791 1.00 21.92  ? 1845 TYR A CE1   1 
ATOM   2483  C  CE2   . TYR A 1 1845 ? 152.089 164.305 117.113 1.00 19.41  ? 1845 TYR A CE2   1 
ATOM   2484  C  CZ    . TYR A 1 1845 ? 152.787 164.242 115.929 1.00 16.55  ? 1845 TYR A CZ    1 
ATOM   2485  O  OH    . TYR A 1 1845 ? 153.998 163.593 115.879 1.00 19.14  ? 1845 TYR A OH    1 
ATOM   2486  N  N     . PHE A 1 1846 ? 147.461 169.068 114.849 1.00 26.92  ? 1846 PHE A N     1 
ATOM   2487  C  CA    . PHE A 1 1846 ? 146.227 169.822 114.701 1.00 30.71  ? 1846 PHE A CA    1 
ATOM   2488  C  C     . PHE A 1 1846 ? 145.360 169.140 113.653 1.00 42.26  ? 1846 PHE A C     1 
ATOM   2489  O  O     . PHE A 1 1846 ? 145.796 168.945 112.514 1.00 48.71  ? 1846 PHE A O     1 
ATOM   2490  C  CB    . PHE A 1 1846 ? 146.526 171.267 114.299 1.00 32.60  ? 1846 PHE A CB    1 
ATOM   2491  C  CG    . PHE A 1 1846 ? 145.412 172.226 114.598 1.00 30.67  ? 1846 PHE A CG    1 
ATOM   2492  C  CD1   . PHE A 1 1846 ? 144.928 173.074 113.618 1.00 30.92  ? 1846 PHE A CD1   1 
ATOM   2493  C  CD2   . PHE A 1 1846 ? 144.863 172.291 115.867 1.00 27.84  ? 1846 PHE A CD2   1 
ATOM   2494  C  CE1   . PHE A 1 1846 ? 143.909 173.960 113.895 1.00 34.92  ? 1846 PHE A CE1   1 
ATOM   2495  C  CE2   . PHE A 1 1846 ? 143.845 173.177 116.150 1.00 29.49  ? 1846 PHE A CE2   1 
ATOM   2496  C  CZ    . PHE A 1 1846 ? 143.367 174.012 115.163 1.00 34.34  ? 1846 PHE A CZ    1 
ATOM   2497  N  N     . ASP A 1 1847 ? 144.136 168.779 114.038 1.00 46.68  ? 1847 ASP A N     1 
ATOM   2498  C  CA    . ASP A 1 1847 ? 143.217 168.036 113.177 1.00 57.29  ? 1847 ASP A CA    1 
ATOM   2499  C  C     . ASP A 1 1847 ? 141.952 168.860 112.985 1.00 63.52  ? 1847 ASP A C     1 
ATOM   2500  O  O     . ASP A 1 1847 ? 141.010 168.763 113.787 1.00 62.32  ? 1847 ASP A O     1 
ATOM   2501  C  CB    . ASP A 1 1847 ? 142.895 166.666 113.771 1.00 63.53  ? 1847 ASP A CB    1 
ATOM   2502  C  CG    . ASP A 1 1847 ? 142.338 165.700 112.744 1.00 68.45  ? 1847 ASP A CG    1 
ATOM   2503  O  OD1   . ASP A 1 1847 ? 141.485 164.866 113.112 1.00 64.18  ? 1847 ASP A OD1   1 
ATOM   2504  O  OD2   . ASP A 1 1847 ? 142.754 165.773 111.568 1.00 72.56  ? 1847 ASP A OD2   1 
ATOM   2505  N  N     . PRO A 1 1848 ? 141.881 169.677 111.931 1.00 69.74  ? 1848 PRO A N     1 
ATOM   2506  C  CA    . PRO A 1 1848 ? 140.670 170.484 111.707 1.00 74.14  ? 1848 PRO A CA    1 
ATOM   2507  C  C     . PRO A 1 1848 ? 139.425 169.655 111.443 1.00 73.72  ? 1848 PRO A C     1 
ATOM   2508  O  O     . PRO A 1 1848 ? 138.312 170.177 111.583 1.00 63.96  ? 1848 PRO A O     1 
ATOM   2509  C  CB    . PRO A 1 1848 ? 141.041 171.343 110.491 1.00 69.73  ? 1848 PRO A CB    1 
ATOM   2510  C  CG    . PRO A 1 1848 ? 142.120 170.577 109.800 1.00 69.20  ? 1848 PRO A CG    1 
ATOM   2511  C  CD    . PRO A 1 1848 ? 142.898 169.901 110.891 1.00 64.85  ? 1848 PRO A CD    1 
ATOM   2512  N  N     . LYS A 1 1849 ? 139.573 168.386 111.062 1.00 69.55  ? 1849 LYS A N     1 
ATOM   2513  C  CA    . LYS A 1 1849 ? 138.426 167.533 110.784 1.00 66.19  ? 1849 LYS A CA    1 
ATOM   2514  C  C     . LYS A 1 1849 ? 137.696 167.082 112.043 1.00 71.26  ? 1849 LYS A C     1 
ATOM   2515  O  O     . LYS A 1 1849 ? 136.595 166.531 111.933 1.00 73.02  ? 1849 LYS A O     1 
ATOM   2516  C  CB    . LYS A 1 1849 ? 138.867 166.307 109.981 1.00 71.80  ? 1849 LYS A CB    1 
ATOM   2517  C  CG    . LYS A 1 1849 ? 139.702 166.641 108.754 1.00 74.49  ? 1849 LYS A CG    1 
ATOM   2518  C  CD    . LYS A 1 1849 ? 138.838 167.175 107.625 1.00 75.50  ? 1849 LYS A CD    1 
ATOM   2519  C  CE    . LYS A 1 1849 ? 139.645 168.057 106.685 1.00 79.46  ? 1849 LYS A CE    1 
ATOM   2520  N  NZ    . LYS A 1 1849 ? 140.732 167.298 106.006 1.00 85.30  ? 1849 LYS A NZ    1 
ATOM   2521  N  N     . GLN A 1 1850 ? 138.273 167.293 113.224 1.00 71.61  ? 1850 GLN A N     1 
ATOM   2522  C  CA    . GLN A 1 1850 ? 137.596 166.930 114.462 1.00 63.50  ? 1850 GLN A CA    1 
ATOM   2523  C  C     . GLN A 1 1850 ? 136.404 167.846 114.706 1.00 62.34  ? 1850 GLN A C     1 
ATOM   2524  O  O     . GLN A 1 1850 ? 136.512 169.071 114.590 1.00 56.79  ? 1850 GLN A O     1 
ATOM   2525  C  CB    . GLN A 1 1850 ? 138.565 167.000 115.641 1.00 54.96  ? 1850 GLN A CB    1 
ATOM   2526  C  CG    . GLN A 1 1850 ? 139.693 165.990 115.579 1.00 63.97  ? 1850 GLN A CG    1 
ATOM   2527  C  CD    . GLN A 1 1850 ? 139.191 164.559 115.620 1.00 68.53  ? 1850 GLN A CD    1 
ATOM   2528  O  OE1   . GLN A 1 1850 ? 139.248 163.839 114.623 1.00 71.12  ? 1850 GLN A OE1   1 
ATOM   2529  N  NE2   . GLN A 1 1850 ? 138.694 164.140 116.777 1.00 50.85  ? 1850 GLN A NE2   1 
ATOM   2530  N  N     . THR A 1 1851 ? 135.260 167.245 115.040 1.00 67.55  ? 1851 THR A N     1 
ATOM   2531  C  CA    . THR A 1 1851 ? 134.079 168.035 115.370 1.00 64.89  ? 1851 THR A CA    1 
ATOM   2532  C  C     . THR A 1 1851 ? 134.279 168.807 116.668 1.00 54.73  ? 1851 THR A C     1 
ATOM   2533  O  O     . THR A 1 1851 ? 133.868 169.968 116.776 1.00 49.27  ? 1851 THR A O     1 
ATOM   2534  C  CB    . THR A 1 1851 ? 132.850 167.131 115.469 1.00 64.51  ? 1851 THR A CB    1 
ATOM   2535  O  OG1   . THR A 1 1851 ? 133.024 166.200 116.545 1.00 60.54  ? 1851 THR A OG1   1 
ATOM   2536  C  CG2   . THR A 1 1851 ? 132.647 166.365 114.171 1.00 58.81  ? 1851 THR A CG2   1 
ATOM   2537  N  N     . ASP A 1 1852 ? 134.903 168.180 117.662 1.00 52.21  ? 1852 ASP A N     1 
ATOM   2538  C  CA    . ASP A 1 1852 ? 135.159 168.825 118.945 1.00 51.17  ? 1852 ASP A CA    1 
ATOM   2539  C  C     . ASP A 1 1852 ? 136.407 169.690 118.823 1.00 52.24  ? 1852 ASP A C     1 
ATOM   2540  O  O     . ASP A 1 1852 ? 137.513 169.174 118.634 1.00 51.83  ? 1852 ASP A O     1 
ATOM   2541  C  CB    . ASP A 1 1852 ? 135.319 167.780 120.045 1.00 43.64  ? 1852 ASP A CB    1 
ATOM   2542  C  CG    . ASP A 1 1852 ? 135.087 168.352 121.428 1.00 52.06  ? 1852 ASP A CG    1 
ATOM   2543  O  OD1   . ASP A 1 1852 ? 134.713 169.540 121.526 1.00 49.49  ? 1852 ASP A OD1   1 
ATOM   2544  O  OD2   . ASP A 1 1852 ? 135.280 167.615 122.418 1.00 51.56  ? 1852 ASP A OD2   1 
ATOM   2545  N  N     . VAL A 1 1853 ? 136.230 171.009 118.929 1.00 53.94  ? 1853 VAL A N     1 
ATOM   2546  C  CA    . VAL A 1 1853 ? 137.366 171.919 118.843 1.00 46.70  ? 1853 VAL A CA    1 
ATOM   2547  C  C     . VAL A 1 1853 ? 138.269 171.780 120.062 1.00 45.88  ? 1853 VAL A C     1 
ATOM   2548  O  O     . VAL A 1 1853 ? 139.451 172.142 120.011 1.00 44.90  ? 1853 VAL A O     1 
ATOM   2549  C  CB    . VAL A 1 1853 ? 136.878 173.368 118.665 1.00 46.89  ? 1853 VAL A CB    1 
ATOM   2550  C  CG1   . VAL A 1 1853 ? 136.101 173.510 117.367 1.00 45.36  ? 1853 VAL A CG1   1 
ATOM   2551  C  CG2   . VAL A 1 1853 ? 136.020 173.784 119.847 1.00 44.17  ? 1853 VAL A CG2   1 
ATOM   2552  N  N     . LEU A 1 1854 ? 137.738 171.270 121.175 1.00 36.21  ? 1854 LEU A N     1 
ATOM   2553  C  CA    . LEU A 1 1854 ? 138.565 171.080 122.361 1.00 34.10  ? 1854 LEU A CA    1 
ATOM   2554  C  C     . LEU A 1 1854 ? 139.573 169.955 122.158 1.00 40.62  ? 1854 LEU A C     1 
ATOM   2555  O  O     . LEU A 1 1854 ? 140.748 170.095 122.515 1.00 49.52  ? 1854 LEU A O     1 
ATOM   2556  C  CB    . LEU A 1 1854 ? 137.683 170.801 123.578 1.00 39.51  ? 1854 LEU A CB    1 
ATOM   2557  C  CG    . LEU A 1 1854 ? 136.662 171.879 123.951 1.00 36.66  ? 1854 LEU A CG    1 
ATOM   2558  C  CD1   . LEU A 1 1854 ? 136.220 171.710 125.395 1.00 29.26  ? 1854 LEU A CD1   1 
ATOM   2559  C  CD2   . LEU A 1 1854 ? 137.228 173.272 123.725 1.00 28.71  ? 1854 LEU A CD2   1 
ATOM   2560  N  N     . GLN A 1 1855 ? 139.137 168.840 121.578 1.00 40.74  ? 1855 GLN A N     1 
ATOM   2561  C  CA    . GLN A 1 1855 ? 140.017 167.723 121.263 1.00 35.13  ? 1855 GLN A CA    1 
ATOM   2562  C  C     . GLN A 1 1855 ? 140.723 167.898 119.926 1.00 32.07  ? 1855 GLN A C     1 
ATOM   2563  O  O     . GLN A 1 1855 ? 141.285 166.932 119.403 1.00 37.86  ? 1855 GLN A O     1 
ATOM   2564  C  CB    . GLN A 1 1855 ? 139.228 166.413 121.260 1.00 34.25  ? 1855 GLN A CB    1 
ATOM   2565  C  CG    . GLN A 1 1855 ? 139.010 165.809 122.632 1.00 36.13  ? 1855 GLN A CG    1 
ATOM   2566  C  CD    . GLN A 1 1855 ? 138.193 164.535 122.576 1.00 51.83  ? 1855 GLN A CD    1 
ATOM   2567  O  OE1   . GLN A 1 1855 ? 137.529 164.254 121.579 1.00 54.33  ? 1855 GLN A OE1   1 
ATOM   2568  N  NE2   . GLN A 1 1855 ? 138.238 163.755 123.650 1.00 55.24  ? 1855 GLN A NE2   1 
ATOM   2569  N  N     . GLN A 1 1856 ? 140.702 169.107 119.364 1.00 33.02  ? 1856 GLN A N     1 
ATOM   2570  C  CA    . GLN A 1 1856 ? 141.242 169.318 118.025 1.00 38.90  ? 1856 GLN A CA    1 
ATOM   2571  C  C     . GLN A 1 1856 ? 142.767 169.323 118.033 1.00 31.73  ? 1856 GLN A C     1 
ATOM   2572  O  O     . GLN A 1 1856 ? 143.401 168.960 117.035 1.00 32.10  ? 1856 GLN A O     1 
ATOM   2573  C  CB    . GLN A 1 1856 ? 140.686 170.624 117.456 1.00 41.93  ? 1856 GLN A CB    1 
ATOM   2574  C  CG    . GLN A 1 1856 ? 141.087 170.934 116.029 1.00 51.47  ? 1856 GLN A CG    1 
ATOM   2575  C  CD    . GLN A 1 1856 ? 140.447 172.212 115.521 1.00 57.09  ? 1856 GLN A CD    1 
ATOM   2576  O  OE1   . GLN A 1 1856 ? 139.728 172.890 116.253 1.00 57.24  ? 1856 GLN A OE1   1 
ATOM   2577  N  NE2   . GLN A 1 1856 ? 140.697 172.541 114.260 1.00 47.38  ? 1856 GLN A NE2   1 
ATOM   2578  N  N     . LEU A 1 1857 ? 143.372 169.719 119.149 1.00 27.06  ? 1857 LEU A N     1 
ATOM   2579  C  CA    . LEU A 1 1857 ? 144.821 169.806 119.274 1.00 16.14  ? 1857 LEU A CA    1 
ATOM   2580  C  C     . LEU A 1 1857 ? 145.331 168.712 120.202 1.00 16.17  ? 1857 LEU A C     1 
ATOM   2581  O  O     . LEU A 1 1857 ? 144.773 168.497 121.283 1.00 17.26  ? 1857 LEU A O     1 
ATOM   2582  C  CB    . LEU A 1 1857 ? 145.237 171.179 119.805 1.00 13.00  ? 1857 LEU A CB    1 
ATOM   2583  C  CG    . LEU A 1 1857 ? 146.708 171.346 120.187 1.00 13.27  ? 1857 LEU A CG    1 
ATOM   2584  C  CD1   . LEU A 1 1857 ? 147.610 171.128 118.984 1.00 14.92  ? 1857 LEU A CD1   1 
ATOM   2585  C  CD2   . LEU A 1 1857 ? 146.951 172.710 120.802 1.00 11.16  ? 1857 LEU A CD2   1 
ATOM   2586  N  N     . SER A 1 1858 ? 146.392 168.028 119.781 1.00 16.23  ? 1858 SER A N     1 
ATOM   2587  C  CA    . SER A 1 1858 ? 147.036 166.995 120.579 1.00 12.21  ? 1858 SER A CA    1 
ATOM   2588  C  C     . SER A 1 1858 ? 148.507 167.338 120.765 1.00 12.71  ? 1858 SER A C     1 
ATOM   2589  O  O     . SER A 1 1858 ? 149.170 167.798 119.832 1.00 15.78  ? 1858 SER A O     1 
ATOM   2590  C  CB    . SER A 1 1858 ? 146.897 165.621 119.919 1.00 10.98  ? 1858 SER A CB    1 
ATOM   2591  O  OG    . SER A 1 1858 ? 147.597 164.632 120.652 1.00 17.93  ? 1858 SER A OG    1 
ATOM   2592  N  N     . ILE A 1 1859 ? 149.013 167.124 121.976 1.00 8.66   ? 1859 ILE A N     1 
ATOM   2593  C  CA    . ILE A 1 1859 ? 150.415 167.360 122.299 1.00 8.20   ? 1859 ILE A CA    1 
ATOM   2594  C  C     . ILE A 1 1859 ? 151.019 166.036 122.738 1.00 9.36   ? 1859 ILE A C     1 
ATOM   2595  O  O     . ILE A 1 1859 ? 150.548 165.423 123.703 1.00 11.90  ? 1859 ILE A O     1 
ATOM   2596  C  CB    . ILE A 1 1859 ? 150.580 168.432 123.387 1.00 11.19  ? 1859 ILE A CB    1 
ATOM   2597  C  CG1   . ILE A 1 1859 ? 149.757 169.673 123.038 1.00 8.95   ? 1859 ILE A CG1   1 
ATOM   2598  C  CG2   . ILE A 1 1859 ? 152.041 168.795 123.557 1.00 9.04   ? 1859 ILE A CG2   1 
ATOM   2599  C  CD1   . ILE A 1 1859 ? 149.748 170.722 124.118 1.00 7.62   ? 1859 ILE A CD1   1 
ATOM   2600  N  N     . GLN A 1 1860 ? 152.060 165.595 122.039 1.00 11.34  ? 1860 GLN A N     1 
ATOM   2601  C  CA    . GLN A 1 1860 ? 152.631 164.273 122.249 1.00 7.40   ? 1860 GLN A CA    1 
ATOM   2602  C  C     . GLN A 1 1860 ? 154.118 164.378 122.552 1.00 9.03   ? 1860 GLN A C     1 
ATOM   2603  O  O     . GLN A 1 1860 ? 154.851 165.092 121.861 1.00 8.26   ? 1860 GLN A O     1 
ATOM   2604  C  CB    . GLN A 1 1860 ? 152.396 163.381 121.029 1.00 9.17   ? 1860 GLN A CB    1 
ATOM   2605  C  CG    . GLN A 1 1860 ? 150.986 163.465 120.471 1.00 11.82  ? 1860 GLN A CG    1 
ATOM   2606  C  CD    . GLN A 1 1860 ? 150.668 162.336 119.517 1.00 19.76  ? 1860 GLN A CD    1 
ATOM   2607  O  OE1   . GLN A 1 1860 ? 151.470 161.424 119.325 1.00 23.60  ? 1860 GLN A OE1   1 
ATOM   2608  N  NE2   . GLN A 1 1860 ? 149.488 162.390 118.912 1.00 20.06  ? 1860 GLN A NE2   1 
ATOM   2609  N  N     . MET A 1 1861 ? 154.552 163.668 123.590 1.00 8.26   ? 1861 MET A N     1 
ATOM   2610  C  CA    . MET A 1 1861 ? 155.964 163.552 123.934 1.00 6.75   ? 1861 MET A CA    1 
ATOM   2611  C  C     . MET A 1 1861 ? 156.252 162.093 124.241 1.00 12.81  ? 1861 MET A C     1 
ATOM   2612  O  O     . MET A 1 1861 ? 155.664 161.532 125.171 1.00 19.81  ? 1861 MET A O     1 
ATOM   2613  C  CB    . MET A 1 1861 ? 156.328 164.439 125.128 1.00 6.73   ? 1861 MET A CB    1 
ATOM   2614  C  CG    . MET A 1 1861 ? 157.813 164.734 125.240 1.00 10.16  ? 1861 MET A CG    1 
ATOM   2615  S  SD    . MET A 1 1861 ? 158.196 165.996 126.465 1.00 14.19  ? 1861 MET A SD    1 
ATOM   2616  C  CE    . MET A 1 1861 ? 159.879 166.400 126.012 1.00 4.51   ? 1861 MET A CE    1 
ATOM   2617  N  N     . ALA A 1 1862 ? 157.155 161.489 123.466 1.00 12.17  ? 1862 ALA A N     1 
ATOM   2618  C  CA    . ALA A 1 1862 ? 157.457 160.056 123.538 1.00 10.64  ? 1862 ALA A CA    1 
ATOM   2619  C  C     . ALA A 1 1862 ? 156.147 159.307 123.323 1.00 13.59  ? 1862 ALA A C     1 
ATOM   2620  O  O     . ALA A 1 1862 ? 155.510 159.509 122.274 1.00 17.20  ? 1862 ALA A O     1 
ATOM   2621  C  CB    . ALA A 1 1862 ? 158.197 159.749 124.841 1.00 8.45   ? 1862 ALA A CB    1 
ATOM   2622  N  N     . ASN A 1 1863 ? 155.706 158.459 124.247 1.00 10.76  ? 1863 ASN A N     1 
ATOM   2623  C  CA    . ASN A 1 1863 ? 154.444 157.748 124.109 1.00 11.76  ? 1863 ASN A CA    1 
ATOM   2624  C  C     . ASN A 1 1863 ? 153.297 158.425 124.845 1.00 13.91  ? 1863 ASN A C     1 
ATOM   2625  O  O     . ASN A 1 1863 ? 152.183 157.895 124.846 1.00 18.96  ? 1863 ASN A O     1 
ATOM   2626  C  CB    . ASN A 1 1863 ? 154.596 156.307 124.604 1.00 14.48  ? 1863 ASN A CB    1 
ATOM   2627  C  CG    . ASN A 1 1863 ? 154.751 156.222 126.107 1.00 14.74  ? 1863 ASN A CG    1 
ATOM   2628  O  OD1   . ASN A 1 1863 ? 155.677 156.791 126.680 1.00 15.53  ? 1863 ASN A OD1   1 
ATOM   2629  N  ND2   . ASN A 1 1863 ? 153.843 155.504 126.753 1.00 20.12  ? 1863 ASN A ND2   1 
ATOM   2630  N  N     . ALA A 1 1864 ? 153.536 159.579 125.461 1.00 11.98  ? 1864 ALA A N     1 
ATOM   2631  C  CA    . ALA A 1 1864 ? 152.516 160.274 126.232 1.00 10.00  ? 1864 ALA A CA    1 
ATOM   2632  C  C     . ALA A 1 1864 ? 151.768 161.258 125.343 1.00 10.73  ? 1864 ALA A C     1 
ATOM   2633  O  O     . ALA A 1 1864 ? 152.384 162.041 124.615 1.00 14.88  ? 1864 ALA A O     1 
ATOM   2634  C  CB    . ALA A 1 1864 ? 153.142 161.006 127.419 1.00 12.45  ? 1864 ALA A CB    1 
ATOM   2635  N  N     . LYS A 1 1865 ? 150.441 161.215 125.407 1.00 12.43  ? 1865 LYS A N     1 
ATOM   2636  C  CA    . LYS A 1 1865 ? 149.585 162.100 124.633 1.00 10.19  ? 1865 LYS A CA    1 
ATOM   2637  C  C     . LYS A 1 1865 ? 148.679 162.885 125.569 1.00 8.51   ? 1865 LYS A C     1 
ATOM   2638  O  O     . LYS A 1 1865 ? 148.188 162.351 126.568 1.00 9.92   ? 1865 LYS A O     1 
ATOM   2639  C  CB    . LYS A 1 1865 ? 148.741 161.317 123.623 1.00 10.27  ? 1865 LYS A CB    1 
ATOM   2640  C  CG    . LYS A 1 1865 ? 149.558 160.532 122.615 1.00 13.53  ? 1865 LYS A CG    1 
ATOM   2641  C  CD    . LYS A 1 1865 ? 148.667 159.698 121.712 1.00 19.61  ? 1865 LYS A CD    1 
ATOM   2642  C  CE    . LYS A 1 1865 ? 149.489 158.759 120.847 1.00 23.50  ? 1865 LYS A CE    1 
ATOM   2643  N  NZ    . LYS A 1 1865 ? 150.462 157.973 121.656 1.00 24.86  ? 1865 LYS A NZ    1 
ATOM   2644  N  N     . PHE A 1 1866 ? 148.468 164.157 125.241 1.00 8.52   ? 1866 PHE A N     1 
ATOM   2645  C  CA    . PHE A 1 1866 ? 147.621 165.036 126.028 1.00 10.25  ? 1866 PHE A CA    1 
ATOM   2646  C  C     . PHE A 1 1866 ? 146.759 165.863 125.088 1.00 10.63  ? 1866 PHE A C     1 
ATOM   2647  O  O     . PHE A 1 1866 ? 147.117 166.106 123.934 1.00 14.57  ? 1866 PHE A O     1 
ATOM   2648  C  CB    . PHE A 1 1866 ? 148.448 165.962 126.931 1.00 8.33   ? 1866 PHE A CB    1 
ATOM   2649  C  CG    . PHE A 1 1866 ? 149.454 165.243 127.779 1.00 7.63   ? 1866 PHE A CG    1 
ATOM   2650  C  CD1   . PHE A 1 1866 ? 149.106 164.755 129.025 1.00 7.65   ? 1866 PHE A CD1   1 
ATOM   2651  C  CD2   . PHE A 1 1866 ? 150.749 165.050 127.327 1.00 8.14   ? 1866 PHE A CD2   1 
ATOM   2652  C  CE1   . PHE A 1 1866 ? 150.029 164.092 129.806 1.00 8.02   ? 1866 PHE A CE1   1 
ATOM   2653  C  CE2   . PHE A 1 1866 ? 151.674 164.387 128.103 1.00 8.36   ? 1866 PHE A CE2   1 
ATOM   2654  C  CZ    . PHE A 1 1866 ? 151.315 163.907 129.343 1.00 7.10   ? 1866 PHE A CZ    1 
ATOM   2655  N  N     . ASN A 1 1867 ? 145.615 166.297 125.602 1.00 10.94  ? 1867 ASN A N     1 
ATOM   2656  C  CA    . ASN A 1 1867 ? 144.738 167.222 124.904 1.00 11.18  ? 1867 ASN A CA    1 
ATOM   2657  C  C     . ASN A 1 1867 ? 144.857 168.593 125.549 1.00 14.38  ? 1867 ASN A C     1 
ATOM   2658  O  O     . ASN A 1 1867 ? 144.869 168.710 126.779 1.00 12.94  ? 1867 ASN A O     1 
ATOM   2659  C  CB    . ASN A 1 1867 ? 143.284 166.745 124.937 1.00 13.83  ? 1867 ASN A CB    1 
ATOM   2660  C  CG    . ASN A 1 1867 ? 143.022 165.611 123.967 1.00 26.43  ? 1867 ASN A CG    1 
ATOM   2661  O  OD1   . ASN A 1 1867 ? 143.494 165.629 122.831 1.00 25.13  ? 1867 ASN A OD1   1 
ATOM   2662  N  ND2   . ASN A 1 1867 ? 142.266 164.615 124.412 1.00 27.52  ? 1867 ASN A ND2   1 
ATOM   2663  N  N     . TYR A 1 1868 ? 144.965 169.625 124.716 1.00 14.53  ? 1868 TYR A N     1 
ATOM   2664  C  CA    . TYR A 1 1868 ? 145.113 170.981 125.224 1.00 8.43   ? 1868 TYR A CA    1 
ATOM   2665  C  C     . TYR A 1 1868 ? 143.897 171.369 126.054 1.00 8.96   ? 1868 TYR A C     1 
ATOM   2666  O  O     . TYR A 1 1868 ? 142.754 171.214 125.615 1.00 12.34  ? 1868 TYR A O     1 
ATOM   2667  C  CB    . TYR A 1 1868 ? 145.302 171.959 124.065 1.00 11.62  ? 1868 TYR A CB    1 
ATOM   2668  C  CG    . TYR A 1 1868 ? 145.946 173.264 124.465 1.00 10.37  ? 1868 TYR A CG    1 
ATOM   2669  C  CD1   . TYR A 1 1868 ? 147.296 173.324 124.776 1.00 6.76   ? 1868 TYR A CD1   1 
ATOM   2670  C  CD2   . TYR A 1 1868 ? 145.207 174.436 124.530 1.00 7.67   ? 1868 TYR A CD2   1 
ATOM   2671  C  CE1   . TYR A 1 1868 ? 147.890 174.510 125.141 1.00 6.44   ? 1868 TYR A CE1   1 
ATOM   2672  C  CE2   . TYR A 1 1868 ? 145.795 175.628 124.895 1.00 6.16   ? 1868 TYR A CE2   1 
ATOM   2673  C  CZ    . TYR A 1 1868 ? 147.138 175.658 125.200 1.00 6.60   ? 1868 TYR A CZ    1 
ATOM   2674  O  OH    . TYR A 1 1868 ? 147.736 176.841 125.564 1.00 9.82   ? 1868 TYR A OH    1 
ATOM   2675  N  N     . GLY A 1 1869 ? 144.149 171.873 127.263 1.00 8.18   ? 1869 GLY A N     1 
ATOM   2676  C  CA    . GLY A 1 1869 ? 143.063 172.221 128.160 1.00 10.61  ? 1869 GLY A CA    1 
ATOM   2677  C  C     . GLY A 1 1869 ? 142.313 173.472 127.763 1.00 12.11  ? 1869 GLY A C     1 
ATOM   2678  O  O     . GLY A 1 1869 ? 141.169 173.656 128.192 1.00 16.97  ? 1869 GLY A O     1 
ATOM   2679  N  N     . PHE A 1 1870 ? 142.931 174.331 126.951 1.00 11.66  ? 1870 PHE A N     1 
ATOM   2680  C  CA    . PHE A 1 1870 ? 142.325 175.580 126.491 1.00 11.60  ? 1870 PHE A CA    1 
ATOM   2681  C  C     . PHE A 1 1870 ? 141.909 176.469 127.656 1.00 10.54  ? 1870 PHE A C     1 
ATOM   2682  O  O     . PHE A 1 1870 ? 140.890 177.160 127.597 1.00 14.06  ? 1870 PHE A O     1 
ATOM   2683  C  CB    . PHE A 1 1870 ? 141.141 175.312 125.560 1.00 13.03  ? 1870 PHE A CB    1 
ATOM   2684  C  CG    . PHE A 1 1870 ? 141.551 174.896 124.182 1.00 12.14  ? 1870 PHE A CG    1 
ATOM   2685  C  CD1   . PHE A 1 1870 ? 142.226 175.775 123.356 1.00 12.18  ? 1870 PHE A CD1   1 
ATOM   2686  C  CD2   . PHE A 1 1870 ? 141.284 173.620 123.721 1.00 16.41  ? 1870 PHE A CD2   1 
ATOM   2687  C  CE1   . PHE A 1 1870 ? 142.614 175.394 122.092 1.00 14.30  ? 1870 PHE A CE1   1 
ATOM   2688  C  CE2   . PHE A 1 1870 ? 141.669 173.235 122.455 1.00 23.65  ? 1870 PHE A CE2   1 
ATOM   2689  C  CZ    . PHE A 1 1870 ? 142.335 174.124 121.639 1.00 15.81  ? 1870 PHE A CZ    1 
ATOM   2690  N  N     . GLU A 1 1871 ? 142.699 176.449 128.724 1.00 13.70  ? 1871 GLU A N     1 
ATOM   2691  C  CA    . GLU A 1 1871 ? 142.514 177.366 129.836 1.00 13.45  ? 1871 GLU A CA    1 
ATOM   2692  C  C     . GLU A 1 1871 ? 143.220 178.676 129.520 1.00 14.47  ? 1871 GLU A C     1 
ATOM   2693  O  O     . GLU A 1 1871 ? 144.395 178.677 129.142 1.00 22.85  ? 1871 GLU A O     1 
ATOM   2694  C  CB    . GLU A 1 1871 ? 143.071 176.754 131.121 1.00 9.90   ? 1871 GLU A CB    1 
ATOM   2695  C  CG    . GLU A 1 1871 ? 142.894 177.602 132.366 1.00 17.59  ? 1871 GLU A CG    1 
ATOM   2696  C  CD    . GLU A 1 1871 ? 141.442 177.780 132.756 1.00 29.81  ? 1871 GLU A CD    1 
ATOM   2697  O  OE1   . GLU A 1 1871 ? 140.620 176.906 132.410 1.00 31.18  ? 1871 GLU A OE1   1 
ATOM   2698  O  OE2   . GLU A 1 1871 ? 141.124 178.794 133.412 1.00 29.38  ? 1871 GLU A OE2   1 
ATOM   2699  N  N     . TYR A 1 1872 ? 142.506 179.789 129.659 1.00 14.57  ? 1872 TYR A N     1 
ATOM   2700  C  CA    . TYR A 1 1872 ? 143.099 181.093 129.385 1.00 14.05  ? 1872 TYR A CA    1 
ATOM   2701  C  C     . TYR A 1 1872 ? 144.155 181.392 130.439 1.00 17.40  ? 1872 TYR A C     1 
ATOM   2702  O  O     . TYR A 1 1872 ? 143.840 181.526 131.626 1.00 21.48  ? 1872 TYR A O     1 
ATOM   2703  C  CB    . TYR A 1 1872 ? 142.031 182.181 129.363 1.00 13.84  ? 1872 TYR A CB    1 
ATOM   2704  C  CG    . TYR A 1 1872 ? 142.573 183.524 128.940 1.00 15.25  ? 1872 TYR A CG    1 
ATOM   2705  C  CD1   . TYR A 1 1872 ? 143.434 183.634 127.857 1.00 18.04  ? 1872 TYR A CD1   1 
ATOM   2706  C  CD2   . TYR A 1 1872 ? 142.245 184.679 129.634 1.00 16.47  ? 1872 TYR A CD2   1 
ATOM   2707  C  CE1   . TYR A 1 1872 ? 143.942 184.854 127.469 1.00 16.47  ? 1872 TYR A CE1   1 
ATOM   2708  C  CE2   . TYR A 1 1872 ? 142.748 185.906 129.253 1.00 20.95  ? 1872 TYR A CE2   1 
ATOM   2709  C  CZ    . TYR A 1 1872 ? 143.596 185.987 128.170 1.00 21.63  ? 1872 TYR A CZ    1 
ATOM   2710  O  OH    . TYR A 1 1872 ? 144.101 187.207 127.785 1.00 25.69  ? 1872 TYR A OH    1 
ATOM   2711  N  N     . LEU A 1 1873 ? 145.409 181.490 130.010 1.00 13.77  ? 1873 LEU A N     1 
ATOM   2712  C  CA    . LEU A 1 1873 ? 146.524 181.724 130.915 1.00 17.07  ? 1873 LEU A CA    1 
ATOM   2713  C  C     . LEU A 1 1873 ? 146.994 183.171 130.918 1.00 16.84  ? 1873 LEU A C     1 
ATOM   2714  O  O     . LEU A 1 1873 ? 147.944 183.495 131.637 1.00 23.34  ? 1873 LEU A O     1 
ATOM   2715  C  CB    . LEU A 1 1873 ? 147.691 180.803 130.554 1.00 17.94  ? 1873 LEU A CB    1 
ATOM   2716  C  CG    . LEU A 1 1873 ? 147.335 179.324 130.410 1.00 11.55  ? 1873 LEU A CG    1 
ATOM   2717  C  CD1   . LEU A 1 1873 ? 148.331 178.621 129.505 1.00 9.84   ? 1873 LEU A CD1   1 
ATOM   2718  C  CD2   . LEU A 1 1873 ? 147.265 178.652 131.767 1.00 12.48  ? 1873 LEU A CD2   1 
ATOM   2719  N  N     . GLY A 1 1874 ? 146.353 184.046 130.148 1.00 15.42  ? 1874 GLY A N     1 
ATOM   2720  C  CA    . GLY A 1 1874 ? 146.812 185.422 130.082 1.00 16.03  ? 1874 GLY A CA    1 
ATOM   2721  C  C     . GLY A 1 1874 ? 148.170 185.513 129.413 1.00 19.77  ? 1874 GLY A C     1 
ATOM   2722  O  O     . GLY A 1 1874 ? 148.454 184.825 128.426 1.00 20.45  ? 1874 GLY A O     1 
ATOM   2723  N  N     . VAL A 1 1875 ? 149.025 186.378 129.953 1.00 17.41  ? 1875 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1875 ? 150.382 186.528 129.444 1.00 13.95  ? 1875 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1875 ? 151.368 186.101 130.521 1.00 16.16  ? 1875 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1875 ? 151.758 186.902 131.378 1.00 18.16  ? 1875 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1875 ? 150.653 187.972 128.984 1.00 16.45  ? 1875 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1875 ? 152.030 188.077 128.350 1.00 14.31  ? 1875 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1875 ? 149.578 188.426 128.014 1.00 16.53  ? 1875 VAL A CG2   1 
ATOM   2730  N  N     . GLN A 1 1876 ? 151.773 184.838 130.488 1.00 23.15  ? 1876 GLN A N     1 
ATOM   2731  C  CA    . GLN A 1 1876 ? 152.754 184.315 131.424 1.00 20.65  ? 1876 GLN A CA    1 
ATOM   2732  C  C     . GLN A 1 1876 ? 154.164 184.547 130.895 1.00 20.98  ? 1876 GLN A C     1 
ATOM   2733  O  O     . GLN A 1 1876 ? 154.374 184.819 129.712 1.00 22.80  ? 1876 GLN A O     1 
ATOM   2734  C  CB    . GLN A 1 1876 ? 152.526 182.823 131.670 1.00 16.46  ? 1876 GLN A CB    1 
ATOM   2735  C  CG    . GLN A 1 1876 ? 151.067 182.426 131.816 1.00 16.89  ? 1876 GLN A CG    1 
ATOM   2736  C  CD    . GLN A 1 1876 ? 150.604 182.431 133.259 1.00 24.38  ? 1876 GLN A CD    1 
ATOM   2737  O  OE1   . GLN A 1 1876 ? 151.363 182.772 134.165 1.00 25.79  ? 1876 GLN A OE1   1 
ATOM   2738  N  NE2   . GLN A 1 1876 ? 149.354 182.044 133.479 1.00 28.73  ? 1876 GLN A NE2   1 
ATOM   2739  N  N     . ASP A 1 1877 ? 155.137 184.436 131.794 1.00 20.64  ? 1877 ASP A N     1 
ATOM   2740  C  CA    . ASP A 1 1877 ? 156.542 184.555 131.430 1.00 18.88  ? 1877 ASP A CA    1 
ATOM   2741  C  C     . ASP A 1 1877 ? 157.055 183.194 130.975 1.00 15.49  ? 1877 ASP A C     1 
ATOM   2742  O  O     . ASP A 1 1877 ? 157.178 182.269 131.785 1.00 15.03  ? 1877 ASP A O     1 
ATOM   2743  C  CB    . ASP A 1 1877 ? 157.367 185.081 132.604 1.00 22.26  ? 1877 ASP A CB    1 
ATOM   2744  C  CG    . ASP A 1 1877 ? 157.570 186.582 132.547 1.00 31.32  ? 1877 ASP A CG    1 
ATOM   2745  O  OD1   . ASP A 1 1877 ? 157.238 187.189 131.507 1.00 26.35  ? 1877 ASP A OD1   1 
ATOM   2746  O  OD2   . ASP A 1 1877 ? 158.062 187.156 133.540 1.00 38.14  ? 1877 ASP A OD2   1 
ATOM   2747  N  N     . LYS A 1 1878 ? 157.361 183.083 129.679 1.00 11.53  ? 1878 LYS A N     1 
ATOM   2748  C  CA    . LYS A 1 1878 ? 157.834 181.796 129.108 1.00 10.41  ? 1878 LYS A CA    1 
ATOM   2749  C  C     . LYS A 1 1878 ? 159.275 181.524 129.556 1.00 12.19  ? 1878 LYS A C     1 
ATOM   2750  O  O     . LYS A 1 1878 ? 160.092 182.467 129.524 1.00 14.13  ? 1878 LYS A O     1 
ATOM   2751  C  CB    . LYS A 1 1878 ? 157.743 181.855 127.580 1.00 9.03   ? 1878 LYS A CB    1 
ATOM   2752  C  CG    . LYS A 1 1878 ? 158.215 180.618 126.832 1.00 14.14  ? 1878 LYS A CG    1 
ATOM   2753  C  CD    . LYS A 1 1878 ? 158.209 180.809 125.320 1.00 12.09  ? 1878 LYS A CD    1 
ATOM   2754  C  CE    . LYS A 1 1878 ? 158.576 179.564 124.576 1.00 12.58  ? 1878 LYS A CE    1 
ATOM   2755  N  NZ    . LYS A 1 1878 ? 157.598 178.496 124.790 1.00 12.36  ? 1878 LYS A NZ    1 
ATOM   2756  N  N     . LEU A 1 1879 ? 159.571 180.284 129.953 1.00 9.67   ? 1879 LEU A N     1 
ATOM   2757  C  CA    . LEU A 1 1879 ? 160.955 179.914 130.343 1.00 4.25   ? 1879 LEU A CA    1 
ATOM   2758  C  C     . LEU A 1 1879 ? 161.745 179.555 129.078 1.00 6.29   ? 1879 LEU A C     1 
ATOM   2759  O  O     . LEU A 1 1879 ? 161.106 179.348 128.024 1.00 8.94   ? 1879 LEU A O     1 
ATOM   2760  C  CB    . LEU A 1 1879 ? 160.936 178.745 131.326 1.00 5.02   ? 1879 LEU A CB    1 
ATOM   2761  C  CG    . LEU A 1 1879 ? 160.259 178.992 132.676 1.00 4.06   ? 1879 LEU A CG    1 
ATOM   2762  C  CD1   . LEU A 1 1879 ? 160.406 177.752 133.538 1.00 3.06   ? 1879 LEU A CD1   1 
ATOM   2763  C  CD2   . LEU A 1 1879 ? 160.857 180.201 133.373 1.00 7.35   ? 1879 LEU A CD2   1 
ATOM   2764  N  N     . VAL A 1 1880 ? 163.074 179.490 129.178 1.00 5.66   ? 1880 VAL A N     1 
ATOM   2765  C  CA    . VAL A 1 1880 ? 163.909 179.051 128.020 1.00 3.11   ? 1880 VAL A CA    1 
ATOM   2766  C  C     . VAL A 1 1880 ? 163.936 177.515 128.030 1.00 4.09   ? 1880 VAL A C     1 
ATOM   2767  O  O     . VAL A 1 1880 ? 164.199 176.940 129.106 1.00 5.01   ? 1880 VAL A O     1 
ATOM   2768  C  CB    . VAL A 1 1880 ? 165.331 179.640 128.082 1.00 3.93   ? 1880 VAL A CB    1 
ATOM   2769  C  CG1   . VAL A 1 1880 ? 166.238 179.059 127.004 1.00 3.94   ? 1880 VAL A CG1   1 
ATOM   2770  C  CG2   . VAL A 1 1880 ? 165.320 181.163 128.026 1.00 4.54   ? 1880 VAL A CG2   1 
ATOM   2771  N  N     . GLN A 1 1881 ? 163.664 176.881 126.887 1.00 5.39   ? 1881 GLN A N     1 
ATOM   2772  C  CA    . GLN A 1 1881 ? 163.601 175.397 126.838 1.00 4.74   ? 1881 GLN A CA    1 
ATOM   2773  C  C     . GLN A 1 1881 ? 165.034 174.850 126.803 1.00 6.35   ? 1881 GLN A C     1 
ATOM   2774  O  O     . GLN A 1 1881 ? 165.539 174.579 125.694 1.00 10.86  ? 1881 GLN A O     1 
ATOM   2775  C  CB    . GLN A 1 1881 ? 162.775 174.913 125.647 1.00 5.41   ? 1881 GLN A CB    1 
ATOM   2776  C  CG    . GLN A 1 1881 ? 162.416 173.433 125.715 1.00 7.38   ? 1881 GLN A CG    1 
ATOM   2777  C  CD    . GLN A 1 1881 ? 161.392 173.111 126.781 1.00 7.73   ? 1881 GLN A CD    1 
ATOM   2778  O  OE1   . GLN A 1 1881 ? 160.845 174.001 127.442 1.00 13.79  ? 1881 GLN A OE1   1 
ATOM   2779  N  NE2   . GLN A 1 1881 ? 161.108 171.827 126.948 1.00 7.89   ? 1881 GLN A NE2   1 
ATOM   2780  N  N     . THR A 1 1882 ? 165.655 174.708 127.975 1.00 5.88   ? 1882 THR A N     1 
ATOM   2781  C  CA    . THR A 1 1882 ? 167.042 174.209 128.060 1.00 5.02   ? 1882 THR A CA    1 
ATOM   2782  C  C     . THR A 1 1882 ? 167.026 172.698 128.071 1.00 6.53   ? 1882 THR A C     1 
ATOM   2783  O  O     . THR A 1 1882 ? 165.937 172.117 128.258 1.00 9.08   ? 1882 THR A O     1 
ATOM   2784  C  CB    . THR A 1 1882 ? 167.681 174.779 129.323 1.00 6.87   ? 1882 THR A CB    1 
ATOM   2785  O  OG1   . THR A 1 1882 ? 166.969 174.179 130.401 1.00 6.79   ? 1882 THR A OG1   1 
ATOM   2786  C  CG2   . THR A 1 1882 ? 167.569 176.290 129.395 1.00 6.42   ? 1882 THR A CG2   1 
ATOM   2787  N  N     . PRO A 1 1883 ? 168.179 172.022 127.878 1.00 6.93   ? 1883 PRO A N     1 
ATOM   2788  C  CA    . PRO A 1 1883 ? 168.229 170.569 127.959 1.00 5.57   ? 1883 PRO A CA    1 
ATOM   2789  C  C     . PRO A 1 1883 ? 167.570 170.030 129.221 1.00 6.65   ? 1883 PRO A C     1 
ATOM   2790  O  O     . PRO A 1 1883 ? 166.862 169.008 129.140 1.00 7.95   ? 1883 PRO A O     1 
ATOM   2791  C  CB    . PRO A 1 1883 ? 169.741 170.315 127.942 1.00 5.34   ? 1883 PRO A CB    1 
ATOM   2792  C  CG    . PRO A 1 1883 ? 170.289 171.441 127.102 1.00 5.51   ? 1883 PRO A CG    1 
ATOM   2793  C  CD    . PRO A 1 1883 ? 169.452 172.631 127.526 1.00 7.90   ? 1883 PRO A CD    1 
ATOM   2794  N  N     . LEU A 1 1884 ? 167.796 170.691 130.360 1.00 5.67   ? 1884 LEU A N     1 
ATOM   2795  C  CA    . LEU A 1 1884 ? 167.190 170.254 131.645 1.00 4.50   ? 1884 LEU A CA    1 
ATOM   2796  C  C     . LEU A 1 1884 ? 165.662 170.383 131.560 1.00 4.82   ? 1884 LEU A C     1 
ATOM   2797  O  O     . LEU A 1 1884 ? 164.965 169.446 131.999 1.00 6.19   ? 1884 LEU A O     1 
ATOM   2798  C  CB    . LEU A 1 1884 ? 167.760 171.087 132.791 1.00 7.17   ? 1884 LEU A CB    1 
ATOM   2799  C  CG    . LEU A 1 1884 ? 167.230 170.758 134.190 1.00 6.30   ? 1884 LEU A CG    1 
ATOM   2800  C  CD1   . LEU A 1 1884 ? 167.438 169.289 134.513 1.00 4.22   ? 1884 LEU A CD1   1 
ATOM   2801  C  CD2   . LEU A 1 1884 ? 167.902 171.632 135.235 1.00 5.31   ? 1884 LEU A CD2   1 
ATOM   2802  N  N     . THR A 1 1885 ? 165.169 171.496 131.015 1.00 6.13   ? 1885 THR A N     1 
ATOM   2803  C  CA    . THR A 1 1885 ? 163.713 171.707 130.880 1.00 4.87   ? 1885 THR A CA    1 
ATOM   2804  C  C     . THR A 1 1885 ? 163.146 170.609 130.010 1.00 5.88   ? 1885 THR A C     1 
ATOM   2805  O  O     . THR A 1 1885 ? 162.063 170.087 130.347 1.00 5.82   ? 1885 THR A O     1 
ATOM   2806  C  CB    . THR A 1 1885 ? 163.457 173.090 130.285 1.00 4.80   ? 1885 THR A CB    1 
ATOM   2807  O  OG1   . THR A 1 1885 ? 164.242 173.988 131.064 1.00 5.23   ? 1885 THR A OG1   1 
ATOM   2808  C  CG2   . THR A 1 1885 ? 161.993 173.488 130.346 1.00 7.24   ? 1885 THR A CG2   1 
ATOM   2809  N  N     . ASP A 1 1886 ? 163.849 170.264 128.928 1.00 5.78   ? 1886 ASP A N     1 
ATOM   2810  C  CA    . ASP A 1 1886 ? 163.397 169.175 128.021 1.00 4.68   ? 1886 ASP A CA    1 
ATOM   2811  C  C     . ASP A 1 1886 ? 163.379 167.861 128.802 1.00 4.21   ? 1886 ASP A C     1 
ATOM   2812  O  O     . ASP A 1 1886 ? 162.369 167.133 128.714 1.00 4.60   ? 1886 ASP A O     1 
ATOM   2813  C  CB    . ASP A 1 1886 ? 164.260 169.107 126.773 1.00 5.97   ? 1886 ASP A CB    1 
ATOM   2814  C  CG    . ASP A 1 1886 ? 164.109 170.281 125.817 1.00 15.52  ? 1886 ASP A CG    1 
ATOM   2815  O  OD1   . ASP A 1 1886 ? 165.112 170.992 125.598 1.00 15.49  ? 1886 ASP A OD1   1 
ATOM   2816  O  OD2   . ASP A 1 1886 ? 162.991 170.468 125.296 1.00 22.17  ? 1886 ASP A OD2   1 
ATOM   2817  N  N     . ARG A 1 1887 ? 164.453 167.572 129.539 1.00 4.18   ? 1887 ARG A N     1 
ATOM   2818  C  CA    . ARG A 1 1887 ? 164.475 166.368 130.362 1.00 4.33   ? 1887 ARG A CA    1 
ATOM   2819  C  C     . ARG A 1 1887 ? 163.341 166.383 131.379 1.00 5.76   ? 1887 ARG A C     1 
ATOM   2820  O  O     . ARG A 1 1887 ? 162.703 165.353 131.627 1.00 5.61   ? 1887 ARG A O     1 
ATOM   2821  C  CB    . ARG A 1 1887 ? 165.832 166.245 131.055 1.00 4.17   ? 1887 ARG A CB    1 
ATOM   2822  C  CG    . ARG A 1 1887 ? 166.073 164.927 131.762 1.00 5.24   ? 1887 ARG A CG    1 
ATOM   2823  C  CD    . ARG A 1 1887 ? 167.366 164.979 132.553 1.00 5.55   ? 1887 ARG A CD    1 
ATOM   2824  N  NE    . ARG A 1 1887 ? 167.628 163.740 133.273 1.00 7.31   ? 1887 ARG A NE    1 
ATOM   2825  C  CZ    . ARG A 1 1887 ? 168.773 163.074 133.225 1.00 6.93   ? 1887 ARG A CZ    1 
ATOM   2826  N  NH1   . ARG A 1 1887 ? 169.791 163.504 132.499 1.00 6.59   ? 1887 ARG A NH1   1 
ATOM   2827  N  NH2   . ARG A 1 1887 ? 168.901 161.952 133.925 1.00 7.40   ? 1887 ARG A NH2   1 
ATOM   2828  N  N     . CYS A 1 1888 ? 163.075 167.549 131.974 1.00 4.59   ? 1888 CYS A N     1 
ATOM   2829  C  CA    . CYS A 1 1888 ? 161.961 167.674 132.906 1.00 3.42   ? 1888 CYS A CA    1 
ATOM   2830  C  C     . CYS A 1 1888 ? 160.631 167.417 132.215 1.00 3.99   ? 1888 CYS A C     1 
ATOM   2831  O  O     . CYS A 1 1888 ? 159.775 166.706 132.751 1.00 4.45   ? 1888 CYS A O     1 
ATOM   2832  C  CB    . CYS A 1 1888 ? 161.971 169.057 133.556 1.00 5.15   ? 1888 CYS A CB    1 
ATOM   2833  S  SG    . CYS A 1 1888 ? 160.667 169.322 134.781 1.00 12.18  ? 1888 CYS A SG    1 
ATOM   2834  N  N     . TYR A 1 1889 ? 160.441 167.988 131.024 1.00 4.55   ? 1889 TYR A N     1 
ATOM   2835  C  CA    . TYR A 1 1889 ? 159.212 167.749 130.276 1.00 3.84   ? 1889 TYR A CA    1 
ATOM   2836  C  C     . TYR A 1 1889 ? 159.030 166.264 130.001 1.00 4.17   ? 1889 TYR A C     1 
ATOM   2837  O  O     . TYR A 1 1889 ? 157.947 165.710 130.215 1.00 4.99   ? 1889 TYR A O     1 
ATOM   2838  C  CB    . TYR A 1 1889 ? 159.227 168.534 128.964 1.00 3.46   ? 1889 TYR A CB    1 
ATOM   2839  C  CG    . TYR A 1 1889 ? 158.737 169.960 129.068 1.00 4.77   ? 1889 TYR A CG    1 
ATOM   2840  C  CD1   . TYR A 1 1889 ? 158.925 170.701 130.226 1.00 4.27   ? 1889 TYR A CD1   1 
ATOM   2841  C  CD2   . TYR A 1 1889 ? 158.082 170.564 128.003 1.00 5.14   ? 1889 TYR A CD2   1 
ATOM   2842  C  CE1   . TYR A 1 1889 ? 158.478 172.004 130.319 1.00 3.51   ? 1889 TYR A CE1   1 
ATOM   2843  C  CE2   . TYR A 1 1889 ? 157.631 171.865 128.088 1.00 6.59   ? 1889 TYR A CE2   1 
ATOM   2844  C  CZ    . TYR A 1 1889 ? 157.832 172.580 129.248 1.00 5.65   ? 1889 TYR A CZ    1 
ATOM   2845  O  OH    . TYR A 1 1889 ? 157.385 173.876 129.335 1.00 6.38   ? 1889 TYR A OH    1 
ATOM   2846  N  N     . LEU A 1 1890 ? 160.094 165.599 129.547 1.00 4.01   ? 1890 LEU A N     1 
ATOM   2847  C  CA    . LEU A 1 1890 ? 160.005 164.176 129.238 1.00 3.13   ? 1890 LEU A CA    1 
ATOM   2848  C  C     . LEU A 1 1890 ? 159.654 163.363 130.479 1.00 4.29   ? 1890 LEU A C     1 
ATOM   2849  O  O     . LEU A 1 1890 ? 158.754 162.515 130.446 1.00 4.70   ? 1890 LEU A O     1 
ATOM   2850  C  CB    . LEU A 1 1890 ? 161.320 163.693 128.628 1.00 2.78   ? 1890 LEU A CB    1 
ATOM   2851  C  CG    . LEU A 1 1890 ? 161.360 162.249 128.128 1.00 3.27   ? 1890 LEU A CG    1 
ATOM   2852  C  CD1   . LEU A 1 1890 ? 160.516 162.088 126.875 1.00 3.74   ? 1890 LEU A CD1   1 
ATOM   2853  C  CD2   . LEU A 1 1890 ? 162.792 161.819 127.870 1.00 4.52   ? 1890 LEU A CD2   1 
ATOM   2854  N  N     . THR A 1 1891 ? 160.346 163.619 131.592 1.00 4.72   ? 1891 THR A N     1 
ATOM   2855  C  CA    . THR A 1 1891 ? 160.112 162.839 132.804 1.00 3.88   ? 1891 THR A CA    1 
ATOM   2856  C  C     . THR A 1 1891 ? 158.709 163.065 133.358 1.00 3.48   ? 1891 THR A C     1 
ATOM   2857  O  O     . THR A 1 1891 ? 158.024 162.109 133.741 1.00 5.16   ? 1891 THR A O     1 
ATOM   2858  C  CB    . THR A 1 1891 ? 161.169 163.176 133.854 1.00 6.09   ? 1891 THR A CB    1 
ATOM   2859  O  OG1   . THR A 1 1891 ? 162.472 163.074 133.268 1.00 6.64   ? 1891 THR A OG1   1 
ATOM   2860  C  CG2   . THR A 1 1891 ? 161.075 162.222 135.035 1.00 3.91   ? 1891 THR A CG2   1 
ATOM   2861  N  N     . MET A 1 1892 ? 158.255 164.320 133.401 1.00 2.88   ? 1892 MET A N     1 
ATOM   2862  C  CA    . MET A 1 1892 ? 156.929 164.590 133.947 1.00 3.60   ? 1892 MET A CA    1 
ATOM   2863  C  C     . MET A 1 1892 ? 155.828 164.077 133.029 1.00 4.37   ? 1892 MET A C     1 
ATOM   2864  O  O     . MET A 1 1892 ? 154.784 163.626 133.508 1.00 4.87   ? 1892 MET A O     1 
ATOM   2865  C  CB    . MET A 1 1892 ? 156.754 166.083 134.226 1.00 3.59   ? 1892 MET A CB    1 
ATOM   2866  C  CG    . MET A 1 1892 ? 157.846 166.743 135.070 1.00 2.95   ? 1892 MET A CG    1 
ATOM   2867  S  SD    . MET A 1 1892 ? 157.874 166.320 136.829 1.00 22.89  ? 1892 MET A SD    1 
ATOM   2868  C  CE    . MET A 1 1892 ? 158.799 164.786 136.853 1.00 4.63   ? 1892 MET A CE    1 
ATOM   2869  N  N     . THR A 1 1893 ? 156.034 164.122 131.711 1.00 4.34   ? 1893 THR A N     1 
ATOM   2870  C  CA    . THR A 1 1893 ? 155.041 163.553 130.806 1.00 3.91   ? 1893 THR A CA    1 
ATOM   2871  C  C     . THR A 1 1893 ? 154.994 162.034 130.926 1.00 4.10   ? 1893 THR A C     1 
ATOM   2872  O  O     . THR A 1 1893 ? 153.916 161.434 130.840 1.00 4.95   ? 1893 THR A O     1 
ATOM   2873  C  CB    . THR A 1 1893 ? 155.332 163.975 129.367 1.00 4.91   ? 1893 THR A CB    1 
ATOM   2874  O  OG1   . THR A 1 1893 ? 156.727 163.802 129.088 1.00 6.74   ? 1893 THR A OG1   1 
ATOM   2875  C  CG2   . THR A 1 1893 ? 154.951 165.431 129.155 1.00 3.25   ? 1893 THR A CG2   1 
ATOM   2876  N  N     . GLN A 1 1894 ? 156.150 161.396 131.128 1.00 4.37   ? 1894 GLN A N     1 
ATOM   2877  C  CA    . GLN A 1 1894 ? 156.161 159.960 131.385 1.00 4.05   ? 1894 GLN A CA    1 
ATOM   2878  C  C     . GLN A 1 1894 ? 155.422 159.630 132.674 1.00 5.20   ? 1894 GLN A C     1 
ATOM   2879  O  O     . GLN A 1 1894 ? 154.690 158.636 132.742 1.00 7.62   ? 1894 GLN A O     1 
ATOM   2880  C  CB    . GLN A 1 1894 ? 157.599 159.446 131.444 1.00 4.23   ? 1894 GLN A CB    1 
ATOM   2881  C  CG    . GLN A 1 1894 ? 158.270 159.314 130.090 1.00 4.01   ? 1894 GLN A CG    1 
ATOM   2882  C  CD    . GLN A 1 1894 ? 157.472 158.458 129.131 1.00 5.95   ? 1894 GLN A CD    1 
ATOM   2883  O  OE1   . GLN A 1 1894 ? 157.308 157.258 129.343 1.00 8.20   ? 1894 GLN A OE1   1 
ATOM   2884  N  NE2   . GLN A 1 1894 ? 156.967 159.072 128.069 1.00 9.70   ? 1894 GLN A NE2   1 
ATOM   2885  N  N     . ALA A 1 1895 ? 155.611 160.450 133.711 1.00 4.98   ? 1895 ALA A N     1 
ATOM   2886  C  CA    . ALA A 1 1895 ? 154.873 160.252 134.954 1.00 4.47   ? 1895 ALA A CA    1 
ATOM   2887  C  C     . ALA A 1 1895 ? 153.374 160.432 134.745 1.00 4.62   ? 1895 ALA A C     1 
ATOM   2888  O  O     . ALA A 1 1895 ? 152.567 159.672 135.292 1.00 7.96   ? 1895 ALA A O     1 
ATOM   2889  C  CB    . ALA A 1 1895 ? 155.382 161.214 136.025 1.00 4.33   ? 1895 ALA A CB    1 
ATOM   2890  N  N     . LEU A 1 1896 ? 152.985 161.439 133.962 1.00 4.90   ? 1896 LEU A N     1 
ATOM   2891  C  CA    . LEU A 1 1896 ? 151.570 161.686 133.706 1.00 4.56   ? 1896 LEU A CA    1 
ATOM   2892  C  C     . LEU A 1 1896 ? 150.935 160.532 132.944 1.00 7.96   ? 1896 LEU A C     1 
ATOM   2893  O  O     . LEU A 1 1896 ? 149.799 160.139 133.233 1.00 12.17  ? 1896 LEU A O     1 
ATOM   2894  C  CB    . LEU A 1 1896 ? 151.398 162.992 132.932 1.00 3.67   ? 1896 LEU A CB    1 
ATOM   2895  C  CG    . LEU A 1 1896 ? 151.664 164.291 133.691 1.00 3.56   ? 1896 LEU A CG    1 
ATOM   2896  C  CD1   . LEU A 1 1896 ? 151.758 165.452 132.721 1.00 5.36   ? 1896 LEU A CD1   1 
ATOM   2897  C  CD2   . LEU A 1 1896 ? 150.583 164.537 134.719 1.00 2.70   ? 1896 LEU A CD2   1 
ATOM   2898  N  N     . GLU A 1 1897 ? 151.648 159.984 131.957 1.00 7.28   ? 1897 GLU A N     1 
ATOM   2899  C  CA    . GLU A 1 1897 ? 151.127 158.836 131.222 1.00 7.58   ? 1897 GLU A CA    1 
ATOM   2900  C  C     . GLU A 1 1897 ? 150.950 157.633 132.140 1.00 10.47  ? 1897 GLU A C     1 
ATOM   2901  O  O     . GLU A 1 1897 ? 150.007 156.850 131.978 1.00 15.79  ? 1897 GLU A O     1 
ATOM   2902  C  CB    . GLU A 1 1897 ? 152.051 158.497 130.052 1.00 10.13  ? 1897 GLU A CB    1 
ATOM   2903  C  CG    . GLU A 1 1897 ? 151.574 157.333 129.199 1.00 12.39  ? 1897 GLU A CG    1 
ATOM   2904  C  CD    . GLU A 1 1897 ? 150.657 157.764 128.071 1.00 26.20  ? 1897 GLU A CD    1 
ATOM   2905  O  OE1   . GLU A 1 1897 ? 149.967 158.795 128.217 1.00 29.33  ? 1897 GLU A OE1   1 
ATOM   2906  O  OE2   . GLU A 1 1897 ? 150.619 157.065 127.038 1.00 29.54  ? 1897 GLU A OE2   1 
ATOM   2907  N  N     . ALA A 1 1898 ? 151.843 157.475 133.114 1.00 9.04   ? 1898 ALA A N     1 
ATOM   2908  C  CA    . ALA A 1 1898 ? 151.719 156.430 134.119 1.00 8.32   ? 1898 ALA A CA    1 
ATOM   2909  C  C     . ALA A 1 1898 ? 150.671 156.750 135.176 1.00 12.51  ? 1898 ALA A C     1 
ATOM   2910  O  O     . ALA A 1 1898 ? 150.481 155.948 136.097 1.00 19.97  ? 1898 ALA A O     1 
ATOM   2911  C  CB    . ALA A 1 1898 ? 153.071 156.185 134.791 1.00 8.00   ? 1898 ALA A CB    1 
ATOM   2912  N  N     . ARG A 1 1899 ? 149.998 157.899 135.064 1.00 10.52  ? 1899 ARG A N     1 
ATOM   2913  C  CA    . ARG A 1 1899 ? 148.962 158.320 136.009 1.00 13.88  ? 1899 ARG A CA    1 
ATOM   2914  C  C     . ARG A 1 1899 ? 149.509 158.405 137.431 1.00 12.20  ? 1899 ARG A C     1 
ATOM   2915  O  O     . ARG A 1 1899 ? 148.841 158.038 138.399 1.00 16.52  ? 1899 ARG A O     1 
ATOM   2916  C  CB    . ARG A 1 1899 ? 147.740 157.400 135.941 1.00 12.97  ? 1899 ARG A CB    1 
ATOM   2917  C  CG    . ARG A 1 1899 ? 146.700 157.839 134.924 1.00 11.74  ? 1899 ARG A CG    1 
ATOM   2918  C  CD    . ARG A 1 1899 ? 147.128 157.462 133.518 1.00 16.96  ? 1899 ARG A CD    1 
ATOM   2919  N  NE    . ARG A 1 1899 ? 146.467 158.268 132.499 1.00 24.66  ? 1899 ARG A NE    1 
ATOM   2920  C  CZ    . ARG A 1 1899 ? 146.668 158.136 131.195 1.00 21.23  ? 1899 ARG A CZ    1 
ATOM   2921  N  NH1   . ARG A 1 1899 ? 147.520 157.246 130.715 1.00 20.09  ? 1899 ARG A NH1   1 
ATOM   2922  N  NH2   . ARG A 1 1899 ? 146.001 158.919 130.353 1.00 17.76  ? 1899 ARG A NH2   1 
ATOM   2923  N  N     . LEU A 1 1900 ? 150.739 158.897 137.555 1.00 6.99   ? 1900 LEU A N     1 
ATOM   2924  C  CA    . LEU A 1 1900 ? 151.368 159.122 138.846 1.00 7.48   ? 1900 LEU A CA    1 
ATOM   2925  C  C     . LEU A 1 1900 ? 152.061 160.477 138.823 1.00 6.51   ? 1900 LEU A C     1 
ATOM   2926  O  O     . LEU A 1 1900 ? 152.393 161.010 137.762 1.00 9.82   ? 1900 LEU A O     1 
ATOM   2927  C  CB    . LEU A 1 1900 ? 152.334 157.978 139.202 1.00 7.99   ? 1900 LEU A CB    1 
ATOM   2928  C  CG    . LEU A 1 1900 ? 153.554 157.651 138.336 1.00 8.03   ? 1900 LEU A CG    1 
ATOM   2929  C  CD1   . LEU A 1 1900 ? 154.745 158.532 138.654 1.00 9.45   ? 1900 LEU A CD1   1 
ATOM   2930  C  CD2   . LEU A 1 1900 ? 153.923 156.187 138.496 1.00 8.66   ? 1900 LEU A CD2   1 
ATOM   2931  N  N     . GLY A 1 1901 ? 152.263 161.037 140.009 1.00 6.10   ? 1901 GLY A N     1 
ATOM   2932  C  CA    . GLY A 1 1901 ? 152.757 162.393 140.121 1.00 4.75   ? 1901 GLY A CA    1 
ATOM   2933  C  C     . GLY A 1 1901 ? 154.225 162.525 139.769 1.00 4.80   ? 1901 GLY A C     1 
ATOM   2934  O  O     . GLY A 1 1901 ? 154.950 161.552 139.573 1.00 6.39   ? 1901 GLY A O     1 
ATOM   2935  N  N     . GLY A 1 1902 ? 154.670 163.773 139.688 1.00 3.37   ? 1902 GLY A N     1 
ATOM   2936  C  CA    . GLY A 1 1902 ? 156.059 164.097 139.390 1.00 2.49   ? 1902 GLY A CA    1 
ATOM   2937  C  C     . GLY A 1 1902 ? 156.711 164.778 140.579 1.00 2.78   ? 1902 GLY A C     1 
ATOM   2938  O  O     . GLY A 1 1902 ? 156.072 165.570 141.276 1.00 4.27   ? 1902 GLY A O     1 
ATOM   2939  N  N     . SER A 1 1903 ? 157.985 164.466 140.806 1.00 3.42   ? 1903 SER A N     1 
ATOM   2940  C  CA    . SER A 1 1903 ? 158.741 164.981 141.946 1.00 2.98   ? 1903 SER A CA    1 
ATOM   2941  C  C     . SER A 1 1903 ? 160.088 165.505 141.465 1.00 3.61   ? 1903 SER A C     1 
ATOM   2942  O  O     . SER A 1 1903 ? 161.095 164.785 141.491 1.00 4.70   ? 1903 SER A O     1 
ATOM   2943  C  CB    . SER A 1 1903 ? 158.923 163.903 143.014 1.00 3.12   ? 1903 SER A CB    1 
ATOM   2944  O  OG    . SER A 1 1903 ? 159.886 164.295 143.974 1.00 8.39   ? 1903 SER A OG    1 
ATOM   2945  N  N     . PRO A 1 1904 ? 160.139 166.749 140.984 1.00 3.83   ? 1904 PRO A N     1 
ATOM   2946  C  CA    . PRO A 1 1904 ? 161.440 167.379 140.718 1.00 3.61   ? 1904 PRO A CA    1 
ATOM   2947  C  C     . PRO A 1 1904 ? 162.078 167.832 142.023 1.00 4.49   ? 1904 PRO A C     1 
ATOM   2948  O  O     . PRO A 1 1904 ? 161.484 168.596 142.787 1.00 6.07   ? 1904 PRO A O     1 
ATOM   2949  C  CB    . PRO A 1 1904 ? 161.083 168.566 139.817 1.00 3.28   ? 1904 PRO A CB    1 
ATOM   2950  C  CG    . PRO A 1 1904 ? 159.664 168.853 140.108 1.00 3.59   ? 1904 PRO A CG    1 
ATOM   2951  C  CD    . PRO A 1 1904 ? 159.017 167.556 140.479 1.00 4.08   ? 1904 PRO A CD    1 
ATOM   2952  N  N     . PHE A 1 1905 ? 163.292 167.337 142.275 1.00 4.51   ? 1905 PHE A N     1 
ATOM   2953  C  CA    . PHE A 1 1905 ? 164.016 167.687 143.525 1.00 4.19   ? 1905 PHE A CA    1 
ATOM   2954  C  C     . PHE A 1 1905 ? 165.370 168.275 143.158 1.00 4.05   ? 1905 PHE A C     1 
ATOM   2955  O  O     . PHE A 1 1905 ? 165.823 168.096 142.008 1.00 3.74   ? 1905 PHE A O     1 
ATOM   2956  C  CB    . PHE A 1 1905 ? 164.168 166.424 144.375 1.00 4.27   ? 1905 PHE A CB    1 
ATOM   2957  C  CG    . PHE A 1 1905 ? 164.920 165.293 143.686 1.00 3.75   ? 1905 PHE A CG    1 
ATOM   2958  C  CD1   . PHE A 1 1905 ? 164.245 164.346 142.925 1.00 3.42   ? 1905 PHE A CD1   1 
ATOM   2959  C  CD2   . PHE A 1 1905 ? 166.301 165.180 143.800 1.00 2.84   ? 1905 PHE A CD2   1 
ATOM   2960  C  CE1   . PHE A 1 1905 ? 164.932 163.318 142.299 1.00 3.75   ? 1905 PHE A CE1   1 
ATOM   2961  C  CE2   . PHE A 1 1905 ? 166.983 164.150 143.172 1.00 3.25   ? 1905 PHE A CE2   1 
ATOM   2962  C  CZ    . PHE A 1 1905 ? 166.298 163.222 142.423 1.00 3.46   ? 1905 PHE A CZ    1 
ATOM   2963  N  N     . GLY A 1 1906 ? 166.007 168.959 144.110 1.00 6.61   ? 1906 GLY A N     1 
ATOM   2964  C  CA    . GLY A 1 1906 ? 167.331 169.556 143.859 1.00 6.45   ? 1906 GLY A CA    1 
ATOM   2965  C  C     . GLY A 1 1906 ? 167.553 170.781 144.719 1.00 5.40   ? 1906 GLY A C     1 
ATOM   2966  O  O     . GLY A 1 1906 ? 166.706 171.052 145.595 1.00 7.49   ? 1906 GLY A O     1 
ATOM   2967  N  N     . PRO A 1 1907 ? 168.650 171.542 144.516 1.00 4.91   ? 1907 PRO A N     1 
ATOM   2968  C  CA    . PRO A 1 1907 ? 168.871 172.770 145.266 1.00 5.91   ? 1907 PRO A CA    1 
ATOM   2969  C  C     . PRO A 1 1907 ? 167.917 173.867 144.817 1.00 8.62   ? 1907 PRO A C     1 
ATOM   2970  O  O     . PRO A 1 1907 ? 167.199 173.679 143.815 1.00 9.98   ? 1907 PRO A O     1 
ATOM   2971  C  CB    . PRO A 1 1907 ? 170.336 173.101 144.953 1.00 5.56   ? 1907 PRO A CB    1 
ATOM   2972  C  CG    . PRO A 1 1907 ? 170.565 172.492 143.589 1.00 6.09   ? 1907 PRO A CG    1 
ATOM   2973  C  CD    . PRO A 1 1907 ? 169.704 171.242 143.563 1.00 4.00   ? 1907 PRO A CD    1 
ATOM   2974  N  N     . ALA A 1 1908 ? 167.896 174.987 145.545 1.00 10.76  ? 1908 ALA A N     1 
ATOM   2975  C  CA    . ALA A 1 1908 ? 166.981 176.103 145.208 1.00 10.57  ? 1908 ALA A CA    1 
ATOM   2976  C  C     . ALA A 1 1908 ? 167.451 176.802 143.932 1.00 7.56   ? 1908 ALA A C     1 
ATOM   2977  O  O     . ALA A 1 1908 ? 168.667 176.777 143.648 1.00 11.60  ? 1908 ALA A O     1 
ATOM   2978  C  CB    . ALA A 1 1908 ? 166.907 177.070 146.368 1.00 11.24  ? 1908 ALA A CB    1 
ATOM   2979  N  N     . GLY A 1 1909 ? 166.520 177.404 143.185 1.00 6.28   ? 1909 GLY A N     1 
ATOM   2980  C  CA    . GLY A 1 1909 ? 166.884 178.151 141.965 1.00 5.61   ? 1909 GLY A CA    1 
ATOM   2981  C  C     . GLY A 1 1909 ? 167.395 177.234 140.873 1.00 6.93   ? 1909 GLY A C     1 
ATOM   2982  O  O     . GLY A 1 1909 ? 168.380 177.610 140.205 1.00 11.54  ? 1909 GLY A O     1 
ATOM   2983  N  N     . THR A 1 1910 ? 166.758 176.074 140.691 1.00 7.13   ? 1910 THR A N     1 
ATOM   2984  C  CA    . THR A 1 1910 ? 167.153 175.144 139.611 1.00 5.61   ? 1910 THR A CA    1 
ATOM   2985  C  C     . THR A 1 1910 ? 166.058 175.115 138.569 1.00 6.21   ? 1910 THR A C     1 
ATOM   2986  O  O     . THR A 1 1910 ? 166.289 174.533 137.489 1.00 11.85  ? 1910 THR A O     1 
ATOM   2987  C  CB    . THR A 1 1910 ? 167.434 173.764 140.198 1.00 5.50   ? 1910 THR A CB    1 
ATOM   2988  O  OG1   . THR A 1 1910 ? 166.304 173.465 141.011 1.00 6.79   ? 1910 THR A OG1   1 
ATOM   2989  C  CG2   . THR A 1 1910 ? 168.697 173.742 141.040 1.00 4.64   ? 1910 THR A CG2   1 
ATOM   2990  N  N     . GLY A 1 1911 ? 164.905 175.719 138.874 1.00 5.71   ? 1911 GLY A N     1 
ATOM   2991  C  CA    . GLY A 1 1911 ? 163.793 175.798 137.906 1.00 5.10   ? 1911 GLY A CA    1 
ATOM   2992  C  C     . GLY A 1 1911 ? 162.770 174.701 138.125 1.00 4.88   ? 1911 GLY A C     1 
ATOM   2993  O  O     . GLY A 1 1911 ? 161.983 174.448 137.195 1.00 7.34   ? 1911 GLY A O     1 
ATOM   2994  N  N     . LYS A 1 1912 ? 162.757 174.084 139.310 1.00 4.07   ? 1912 LYS A N     1 
ATOM   2995  C  CA    . LYS A 1 1912 ? 161.848 172.935 139.565 1.00 3.79   ? 1912 LYS A CA    1 
ATOM   2996  C  C     . LYS A 1 1912 ? 160.378 173.382 139.498 1.00 5.47   ? 1912 LYS A C     1 
ATOM   2997  O  O     . LYS A 1 1912 ? 159.598 172.724 138.779 1.00 8.42   ? 1912 LYS A O     1 
ATOM   2998  C  CB    . LYS A 1 1912 ? 162.168 172.306 140.925 1.00 4.21   ? 1912 LYS A CB    1 
ATOM   2999  C  CG    . LYS A 1 1912 ? 163.595 171.801 141.071 1.00 3.61   ? 1912 LYS A CG    1 
ATOM   3000  C  CD    . LYS A 1 1912 ? 163.853 171.141 142.418 1.00 4.97   ? 1912 LYS A CD    1 
ATOM   3001  C  CE    . LYS A 1 1912 ? 163.564 172.054 143.565 1.00 4.71   ? 1912 LYS A CE    1 
ATOM   3002  N  NZ    . LYS A 1 1912 ? 164.475 173.201 143.590 1.00 4.62   ? 1912 LYS A NZ    1 
ATOM   3003  N  N     . THR A 1 1913 ? 160.018 174.453 140.209 1.00 4.36   ? 1913 THR A N     1 
ATOM   3004  C  CA    . THR A 1 1913 ? 158.606 174.897 140.250 1.00 4.94   ? 1913 THR A CA    1 
ATOM   3005  C  C     . THR A 1 1913 ? 158.235 175.516 138.922 1.00 6.06   ? 1913 THR A C     1 
ATOM   3006  O  O     . THR A 1 1913 ? 157.179 175.138 138.370 1.00 6.97   ? 1913 THR A O     1 
ATOM   3007  C  CB    . THR A 1 1913 ? 158.404 175.885 141.396 1.00 7.11   ? 1913 THR A CB    1 
ATOM   3008  O  OG1   . THR A 1 1913 ? 158.595 175.128 142.587 1.00 18.27  ? 1913 THR A OG1   1 
ATOM   3009  C  CG2   . THR A 1 1913 ? 157.016 176.499 141.392 1.00 10.58  ? 1913 THR A CG2   1 
ATOM   3010  N  N     . GLU A 1 1914 ? 159.063 176.435 138.421 1.00 6.65   ? 1914 GLU A N     1 
ATOM   3011  C  CA    . GLU A 1 1914 ? 158.743 177.149 137.156 1.00 3.90   ? 1914 GLU A CA    1 
ATOM   3012  C  C     . GLU A 1 1914 ? 158.609 176.138 136.005 1.00 3.80   ? 1914 GLU A C     1 
ATOM   3013  O  O     . GLU A 1 1914 ? 157.708 176.327 135.164 1.00 4.96   ? 1914 GLU A O     1 
ATOM   3014  C  CB    . GLU A 1 1914 ? 159.803 178.211 136.861 1.00 9.57   ? 1914 GLU A CB    1 
ATOM   3015  C  CG    . GLU A 1 1914 ? 159.791 179.372 137.851 1.00 14.21  ? 1914 GLU A CG    1 
ATOM   3016  C  CD    . GLU A 1 1914 ? 158.464 180.101 137.955 1.00 17.15  ? 1914 GLU A CD    1 
ATOM   3017  O  OE1   . GLU A 1 1914 ? 158.006 180.646 136.928 1.00 18.17  ? 1914 GLU A OE1   1 
ATOM   3018  O  OE2   . GLU A 1 1914 ? 157.889 180.124 139.063 1.00 14.85  ? 1914 GLU A OE2   1 
ATOM   3019  N  N     . SER A 1 1915 ? 159.469 175.115 135.973 1.00 4.09   ? 1915 SER A N     1 
ATOM   3020  C  CA    . SER A 1 1915 ? 159.407 174.084 134.905 1.00 2.56   ? 1915 SER A CA    1 
ATOM   3021  C  C     . SER A 1 1915 ? 158.060 173.355 134.974 1.00 2.62   ? 1915 SER A C     1 
ATOM   3022  O  O     . SER A 1 1915 ? 157.479 173.083 133.903 1.00 2.93   ? 1915 SER A O     1 
ATOM   3023  C  CB    . SER A 1 1915 ? 160.557 173.118 134.998 1.00 3.21   ? 1915 SER A CB    1 
ATOM   3024  O  OG    . SER A 1 1915 ? 161.788 173.764 134.706 1.00 6.76   ? 1915 SER A OG    1 
ATOM   3025  N  N     . VAL A 1 1916 ? 157.586 173.055 136.186 1.00 3.65   ? 1916 VAL A N     1 
ATOM   3026  C  CA    . VAL A 1 1916 ? 156.278 172.416 136.320 1.00 3.37   ? 1916 VAL A CA    1 
ATOM   3027  C  C     . VAL A 1 1916 ? 155.179 173.343 135.813 1.00 3.69   ? 1916 VAL A C     1 
ATOM   3028  O  O     . VAL A 1 1916 ? 154.278 172.920 135.075 1.00 5.42   ? 1916 VAL A O     1 
ATOM   3029  C  CB    . VAL A 1 1916 ? 156.038 171.987 137.779 1.00 2.93   ? 1916 VAL A CB    1 
ATOM   3030  C  CG1   . VAL A 1 1916 ? 154.592 171.570 137.981 1.00 3.00   ? 1916 VAL A CG1   1 
ATOM   3031  C  CG2   . VAL A 1 1916 ? 156.973 170.854 138.152 1.00 4.20   ? 1916 VAL A CG2   1 
ATOM   3032  N  N     . LYS A 1 1917 ? 155.243 174.623 136.187 1.00 3.26   ? 1917 LYS A N     1 
ATOM   3033  C  CA    . LYS A 1 1917 ? 154.248 175.581 135.715 1.00 3.04   ? 1917 LYS A CA    1 
ATOM   3034  C  C     . LYS A 1 1917 ? 154.318 175.756 134.203 1.00 3.29   ? 1917 LYS A C     1 
ATOM   3035  O  O     . LYS A 1 1917 ? 153.285 175.895 133.540 1.00 6.36   ? 1917 LYS A O     1 
ATOM   3036  C  CB    . LYS A 1 1917 ? 154.433 176.925 136.416 1.00 4.34   ? 1917 LYS A CB    1 
ATOM   3037  C  CG    . LYS A 1 1917 ? 153.983 176.936 137.862 1.00 5.83   ? 1917 LYS A CG    1 
ATOM   3038  C  CD    . LYS A 1 1917 ? 153.689 178.348 138.335 1.00 8.01   ? 1917 LYS A CD    1 
ATOM   3039  C  CE    . LYS A 1 1917 ? 154.863 179.273 138.088 1.00 7.54   ? 1917 LYS A CE    1 
ATOM   3040  N  NZ    . LYS A 1 1917 ? 154.585 180.656 138.567 1.00 11.22  ? 1917 LYS A NZ    1 
ATOM   3041  N  N     . ALA A 1 1918 ? 155.528 175.765 133.642 1.00 2.56   ? 1918 ALA A N     1 
ATOM   3042  C  CA    . ALA A 1 1918 ? 155.688 175.911 132.201 1.00 2.29   ? 1918 ALA A CA    1 
ATOM   3043  C  C     . ALA A 1 1918 ? 155.114 174.716 131.456 1.00 3.09   ? 1918 ALA A C     1 
ATOM   3044  O  O     . ALA A 1 1918 ? 154.481 174.878 130.408 1.00 5.75   ? 1918 ALA A O     1 
ATOM   3045  C  CB    . ALA A 1 1918 ? 157.164 176.100 131.856 1.00 1.56   ? 1918 ALA A CB    1 
ATOM   3046  N  N     . LEU A 1 1919 ? 155.332 173.506 131.974 1.00 2.60   ? 1919 LEU A N     1 
ATOM   3047  C  CA    . LEU A 1 1919 ? 154.733 172.331 131.352 1.00 2.76   ? 1919 LEU A CA    1 
ATOM   3048  C  C     . LEU A 1 1919 ? 153.214 172.367 131.462 1.00 3.51   ? 1919 LEU A C     1 
ATOM   3049  O  O     . LEU A 1 1919 ? 152.509 171.986 130.521 1.00 3.89   ? 1919 LEU A O     1 
ATOM   3050  C  CB    . LEU A 1 1919 ? 155.290 171.054 131.978 1.00 3.32   ? 1919 LEU A CB    1 
ATOM   3051  C  CG    . LEU A 1 1919 ? 154.690 169.763 131.419 1.00 2.73   ? 1919 LEU A CG    1 
ATOM   3052  C  CD1   . LEU A 1 1919 ? 154.954 169.660 129.928 1.00 3.07   ? 1919 LEU A CD1   1 
ATOM   3053  C  CD2   . LEU A 1 1919 ? 155.235 168.553 132.145 1.00 1.91   ? 1919 LEU A CD2   1 
ATOM   3054  N  N     . GLY A 1 1920 ? 152.693 172.819 132.604 1.00 3.95   ? 1920 GLY A N     1 
ATOM   3055  C  CA    . GLY A 1 1920 ? 151.251 172.947 132.742 1.00 3.90   ? 1920 GLY A CA    1 
ATOM   3056  C  C     . GLY A 1 1920 ? 150.657 173.953 131.774 1.00 4.92   ? 1920 GLY A C     1 
ATOM   3057  O  O     . GLY A 1 1920 ? 149.590 173.723 131.200 1.00 6.80   ? 1920 GLY A O     1 
ATOM   3058  N  N     . HIS A 1 1921 ? 151.339 175.084 131.581 1.00 4.75   ? 1921 HIS A N     1 
ATOM   3059  C  CA    . HIS A 1 1921 ? 150.868 176.086 130.633 1.00 4.31   ? 1921 HIS A CA    1 
ATOM   3060  C  C     . HIS A 1 1921 ? 151.023 175.613 129.194 1.00 5.16   ? 1921 HIS A C     1 
ATOM   3061  O  O     . HIS A 1 1921 ? 150.259 176.034 128.319 1.00 7.76   ? 1921 HIS A O     1 
ATOM   3062  C  CB    . HIS A 1 1921 ? 151.615 177.402 130.843 1.00 5.30   ? 1921 HIS A CB    1 
ATOM   3063  C  CG    . HIS A 1 1921 ? 151.427 177.992 132.205 1.00 13.68  ? 1921 HIS A CG    1 
ATOM   3064  N  ND1   . HIS A 1 1921 ? 150.397 177.620 133.042 1.00 14.90  ? 1921 HIS A ND1   1 
ATOM   3065  C  CD2   . HIS A 1 1921 ? 152.143 178.921 132.881 1.00 15.92  ? 1921 HIS A CD2   1 
ATOM   3066  C  CE1   . HIS A 1 1921 ? 150.484 178.298 134.172 1.00 13.61  ? 1921 HIS A CE1   1 
ATOM   3067  N  NE2   . HIS A 1 1921 ? 151.535 179.094 134.100 1.00 19.35  ? 1921 HIS A NE2   1 
ATOM   3068  N  N     . GLN A 1 1922 ? 152.005 174.749 128.931 1.00 4.33   ? 1922 GLN A N     1 
ATOM   3069  C  CA    . GLN A 1 1922 ? 152.172 174.198 127.591 1.00 3.25   ? 1922 GLN A CA    1 
ATOM   3070  C  C     . GLN A 1 1922 ? 150.987 173.331 127.192 1.00 5.05   ? 1922 GLN A C     1 
ATOM   3071  O  O     . GLN A 1 1922 ? 150.595 173.315 126.020 1.00 6.26   ? 1922 GLN A O     1 
ATOM   3072  C  CB    . GLN A 1 1922 ? 153.471 173.398 127.515 1.00 3.47   ? 1922 GLN A CB    1 
ATOM   3073  C  CG    . GLN A 1 1922 ? 153.710 172.718 126.179 1.00 6.41   ? 1922 GLN A CG    1 
ATOM   3074  C  CD    . GLN A 1 1922 ? 154.008 173.699 125.066 1.00 6.46   ? 1922 GLN A CD    1 
ATOM   3075  O  OE1   . GLN A 1 1922 ? 155.156 174.087 124.857 1.00 7.82   ? 1922 GLN A OE1   1 
ATOM   3076  N  NE2   . GLN A 1 1922 ? 152.973 174.104 124.342 1.00 7.57   ? 1922 GLN A NE2   1 
ATOM   3077  N  N     . LEU A 1 1923 ? 150.405 172.608 128.144 1.00 4.76   ? 1923 LEU A N     1 
ATOM   3078  C  CA    . LEU A 1 1923 ? 149.247 171.765 127.893 1.00 4.02   ? 1923 LEU A CA    1 
ATOM   3079  C  C     . LEU A 1 1923 ? 147.929 172.492 128.128 1.00 6.48   ? 1923 LEU A C     1 
ATOM   3080  O  O     . LEU A 1 1923 ? 146.870 171.860 128.087 1.00 8.86   ? 1923 LEU A O     1 
ATOM   3081  C  CB    . LEU A 1 1923 ? 149.313 170.507 128.763 1.00 4.18   ? 1923 LEU A CB    1 
ATOM   3082  C  CG    . LEU A 1 1923 ? 150.632 169.732 128.721 1.00 3.33   ? 1923 LEU A CG    1 
ATOM   3083  C  CD1   . LEU A 1 1923 ? 150.617 168.583 129.711 1.00 3.72   ? 1923 LEU A CD1   1 
ATOM   3084  C  CD2   . LEU A 1 1923 ? 150.915 169.225 127.319 1.00 3.82   ? 1923 LEU A CD2   1 
ATOM   3085  N  N     . GLY A 1 1924 ? 147.972 173.797 128.375 1.00 5.78   ? 1924 GLY A N     1 
ATOM   3086  C  CA    . GLY A 1 1924 ? 146.763 174.560 128.628 1.00 6.12   ? 1924 GLY A CA    1 
ATOM   3087  C  C     . GLY A 1 1924 ? 146.063 174.180 129.913 1.00 8.31   ? 1924 GLY A C     1 
ATOM   3088  O  O     . GLY A 1 1924 ? 144.828 174.208 129.975 1.00 10.24  ? 1924 GLY A O     1 
ATOM   3089  N  N     . ARG A 1 1925 ? 146.821 173.833 130.945 1.00 8.42   ? 1925 ARG A N     1 
ATOM   3090  C  CA    . ARG A 1 1925 ? 146.265 173.407 132.217 1.00 5.63   ? 1925 ARG A CA    1 
ATOM   3091  C  C     . ARG A 1 1925 ? 146.259 174.561 133.211 1.00 7.71   ? 1925 ARG A C     1 
ATOM   3092  O  O     . ARG A 1 1925 ? 147.052 175.500 133.120 1.00 6.31   ? 1925 ARG A O     1 
ATOM   3093  C  CB    . ARG A 1 1925 ? 147.058 172.229 132.788 1.00 4.78   ? 1925 ARG A CB    1 
ATOM   3094  C  CG    . ARG A 1 1925 ? 147.003 170.976 131.936 1.00 4.80   ? 1925 ARG A CG    1 
ATOM   3095  C  CD    . ARG A 1 1925 ? 145.586 170.448 131.825 1.00 7.63   ? 1925 ARG A CD    1 
ATOM   3096  N  NE    . ARG A 1 1925 ? 145.553 169.064 131.371 1.00 9.32   ? 1925 ARG A NE    1 
ATOM   3097  C  CZ    . ARG A 1 1925 ? 145.682 168.685 130.107 1.00 11.90  ? 1925 ARG A CZ    1 
ATOM   3098  N  NH1   . ARG A 1 1925 ? 145.849 169.566 129.136 1.00 10.52  ? 1925 ARG A NH1   1 
ATOM   3099  N  NH2   . ARG A 1 1925 ? 145.642 167.390 129.811 1.00 18.64  ? 1925 ARG A NH2   1 
ATOM   3100  N  N     . PHE A 1 1926 ? 145.340 174.476 134.167 1.00 7.35   ? 1926 PHE A N     1 
ATOM   3101  C  CA    . PHE A 1 1926 ? 145.220 175.452 135.244 1.00 7.24   ? 1926 PHE A CA    1 
ATOM   3102  C  C     . PHE A 1 1926 ? 146.086 174.956 136.397 1.00 8.17   ? 1926 PHE A C     1 
ATOM   3103  O  O     . PHE A 1 1926 ? 145.750 173.977 137.067 1.00 7.72   ? 1926 PHE A O     1 
ATOM   3104  C  CB    . PHE A 1 1926 ? 143.755 175.631 135.633 1.00 8.08   ? 1926 PHE A CB    1 
ATOM   3105  C  CG    . PHE A 1 1926 ? 143.531 176.542 136.807 1.00 10.14  ? 1926 PHE A CG    1 
ATOM   3106  C  CD1   . PHE A 1 1926 ? 144.396 177.587 137.077 1.00 11.31  ? 1926 PHE A CD1   1 
ATOM   3107  C  CD2   . PHE A 1 1926 ? 142.414 176.387 137.608 1.00 11.08  ? 1926 PHE A CD2   1 
ATOM   3108  C  CE1   . PHE A 1 1926 ? 144.176 178.428 138.148 1.00 12.95  ? 1926 PHE A CE1   1 
ATOM   3109  C  CE2   . PHE A 1 1926 ? 142.185 177.231 138.673 1.00 13.56  ? 1926 PHE A CE2   1 
ATOM   3110  C  CZ    . PHE A 1 1926 ? 143.067 178.251 138.944 1.00 14.72  ? 1926 PHE A CZ    1 
ATOM   3111  N  N     . VAL A 1 1927 ? 147.211 175.631 136.616 1.00 7.13   ? 1927 VAL A N     1 
ATOM   3112  C  CA    . VAL A 1 1927 ? 148.197 175.231 137.612 1.00 4.97   ? 1927 VAL A CA    1 
ATOM   3113  C  C     . VAL A 1 1927 ? 148.064 176.139 138.825 1.00 8.19   ? 1927 VAL A C     1 
ATOM   3114  O  O     . VAL A 1 1927 ? 148.096 177.369 138.697 1.00 17.41  ? 1927 VAL A O     1 
ATOM   3115  C  CB    . VAL A 1 1927 ? 149.623 175.290 137.039 1.00 4.56   ? 1927 VAL A CB    1 
ATOM   3116  C  CG1   . VAL A 1 1927 ? 150.619 174.729 138.038 1.00 6.10   ? 1927 VAL A CG1   1 
ATOM   3117  C  CG2   . VAL A 1 1927 ? 149.699 174.536 135.725 1.00 5.15   ? 1927 VAL A CG2   1 
ATOM   3118  N  N     . LEU A 1 1928 ? 147.913 175.535 140.001 1.00 5.82   ? 1928 LEU A N     1 
ATOM   3119  C  CA    . LEU A 1 1928 ? 147.879 176.258 141.266 1.00 6.28   ? 1928 LEU A CA    1 
ATOM   3120  C  C     . LEU A 1 1928 ? 149.078 175.824 142.094 1.00 6.67   ? 1928 LEU A C     1 
ATOM   3121  O  O     . LEU A 1 1928 ? 149.305 174.624 142.281 1.00 8.92   ? 1928 LEU A O     1 
ATOM   3122  C  CB    . LEU A 1 1928 ? 146.578 176.004 142.035 1.00 7.33   ? 1928 LEU A CB    1 
ATOM   3123  C  CG    . LEU A 1 1928 ? 145.236 176.416 141.424 1.00 7.18   ? 1928 LEU A CG    1 
ATOM   3124  C  CD1   . LEU A 1 1928 ? 144.758 175.421 140.378 1.00 7.02   ? 1928 LEU A CD1   1 
ATOM   3125  C  CD2   . LEU A 1 1928 ? 144.190 176.599 142.509 1.00 7.33   ? 1928 LEU A CD2   1 
ATOM   3126  N  N     . VAL A 1 1929 ? 149.839 176.792 142.581 1.00 7.48   ? 1929 VAL A N     1 
ATOM   3127  C  CA    . VAL A 1 1929 ? 151.012 176.521 143.401 1.00 7.38   ? 1929 VAL A CA    1 
ATOM   3128  C  C     . VAL A 1 1929 ? 150.633 176.694 144.865 1.00 8.44   ? 1929 VAL A C     1 
ATOM   3129  O  O     . VAL A 1 1929 ? 150.076 177.726 145.256 1.00 8.92   ? 1929 VAL A O     1 
ATOM   3130  C  CB    . VAL A 1 1929 ? 152.179 177.446 143.018 1.00 9.42   ? 1929 VAL A CB    1 
ATOM   3131  C  CG1   . VAL A 1 1929 ? 153.310 177.315 144.017 1.00 11.93  ? 1929 VAL A CG1   1 
ATOM   3132  C  CG2   . VAL A 1 1929 ? 152.669 177.124 141.619 1.00 6.74   ? 1929 VAL A CG2   1 
ATOM   3133  N  N     . PHE A 1 1930 ? 150.924 175.678 145.671 1.00 8.03   ? 1930 PHE A N     1 
ATOM   3134  C  CA    . PHE A 1 1930 ? 150.639 175.690 147.103 1.00 7.14   ? 1930 PHE A CA    1 
ATOM   3135  C  C     . PHE A 1 1930 ? 151.971 175.631 147.841 1.00 9.17   ? 1930 PHE A C     1 
ATOM   3136  O  O     . PHE A 1 1930 ? 152.653 174.603 147.820 1.00 13.03  ? 1930 PHE A O     1 
ATOM   3137  C  CB    . PHE A 1 1930 ? 149.741 174.522 147.497 1.00 7.77   ? 1930 PHE A CB    1 
ATOM   3138  C  CG    . PHE A 1 1930 ? 148.355 174.604 146.934 1.00 6.56   ? 1930 PHE A CG    1 
ATOM   3139  C  CD1   . PHE A 1 1930 ? 147.394 175.395 147.537 1.00 7.27   ? 1930 PHE A CD1   1 
ATOM   3140  C  CD2   . PHE A 1 1930 ? 148.012 173.888 145.801 1.00 6.28   ? 1930 PHE A CD2   1 
ATOM   3141  C  CE1   . PHE A 1 1930 ? 146.118 175.470 147.020 1.00 8.17   ? 1930 PHE A CE1   1 
ATOM   3142  C  CE2   . PHE A 1 1930 ? 146.739 173.960 145.280 1.00 7.26   ? 1930 PHE A CE2   1 
ATOM   3143  C  CZ    . PHE A 1 1930 ? 145.790 174.751 145.890 1.00 7.49   ? 1930 PHE A CZ    1 
ATOM   3144  N  N     . ASN A 1 1931 ? 152.345 176.734 148.487 1.00 11.05  ? 1931 ASN A N     1 
ATOM   3145  C  CA    . ASN A 1 1931 ? 153.524 176.725 149.339 1.00 7.98   ? 1931 ASN A CA    1 
ATOM   3146  C  C     . ASN A 1 1931 ? 153.195 175.966 150.615 1.00 9.02   ? 1931 ASN A C     1 
ATOM   3147  O  O     . ASN A 1 1931 ? 152.441 176.456 151.461 1.00 11.09  ? 1931 ASN A O     1 
ATOM   3148  C  CB    . ASN A 1 1931 ? 153.986 178.147 149.652 1.00 8.82   ? 1931 ASN A CB    1 
ATOM   3149  C  CG    . ASN A 1 1931 ? 155.338 178.183 150.329 1.00 9.24   ? 1931 ASN A CG    1 
ATOM   3150  O  OD1   . ASN A 1 1931 ? 156.338 177.746 149.764 1.00 13.28  ? 1931 ASN A OD1   1 
ATOM   3151  N  ND2   . ASN A 1 1931 ? 155.375 178.697 151.547 1.00 10.64  ? 1931 ASN A ND2   1 
ATOM   3152  N  N     . CYS A 1 1932 ? 153.755 174.771 150.762 1.00 9.34   ? 1932 CYS A N     1 
ATOM   3153  C  CA    . CYS A 1 1932 ? 153.330 173.862 151.814 1.00 8.95   ? 1932 CYS A CA    1 
ATOM   3154  C  C     . CYS A 1 1932 ? 154.209 173.996 153.050 1.00 8.92   ? 1932 CYS A C     1 
ATOM   3155  O  O     . CYS A 1 1932 ? 155.422 174.199 152.953 1.00 10.85  ? 1932 CYS A O     1 
ATOM   3156  C  CB    . CYS A 1 1932 ? 153.361 172.422 151.305 1.00 12.97  ? 1932 CYS A CB    1 
ATOM   3157  S  SG    . CYS A 1 1932 ? 152.192 172.067 149.978 1.00 24.27  ? 1932 CYS A SG    1 
ATOM   3158  N  N     . ASP A 1 1933 ? 153.581 173.884 154.219 1.00 11.56  ? 1933 ASP A N     1 
ATOM   3159  C  CA    . ASP A 1 1933 ? 154.281 173.846 155.493 1.00 11.42  ? 1933 ASP A CA    1 
ATOM   3160  C  C     . ASP A 1 1933 ? 153.651 172.757 156.353 1.00 18.36  ? 1933 ASP A C     1 
ATOM   3161  O  O     . ASP A 1 1933 ? 152.823 171.970 155.884 1.00 15.86  ? 1933 ASP A O     1 
ATOM   3162  C  CB    . ASP A 1 1933 ? 154.261 175.218 156.182 1.00 12.94  ? 1933 ASP A CB    1 
ATOM   3163  C  CG    . ASP A 1 1933 ? 152.944 175.517 156.867 1.00 18.85  ? 1933 ASP A CG    1 
ATOM   3164  O  OD1   . ASP A 1 1933 ? 152.957 176.243 157.882 1.00 23.73  ? 1933 ASP A OD1   1 
ATOM   3165  O  OD2   . ASP A 1 1933 ? 151.891 175.056 156.379 1.00 20.59  ? 1933 ASP A OD2   1 
ATOM   3166  N  N     . GLU A 1 1934 ? 154.047 172.708 157.627 1.00 20.94  ? 1934 GLU A N     1 
ATOM   3167  C  CA    . GLU A 1 1934 ? 153.553 171.655 158.506 1.00 18.64  ? 1934 GLU A CA    1 
ATOM   3168  C  C     . GLU A 1 1934 ? 152.099 171.862 158.912 1.00 18.43  ? 1934 GLU A C     1 
ATOM   3169  O  O     . GLU A 1 1934 ? 151.492 170.943 159.469 1.00 29.52  ? 1934 GLU A O     1 
ATOM   3170  C  CB    . GLU A 1 1934 ? 154.434 171.542 159.752 1.00 21.77  ? 1934 GLU A CB    1 
ATOM   3171  C  CG    . GLU A 1 1934 ? 154.343 172.710 160.715 1.00 21.79  ? 1934 GLU A CG    1 
ATOM   3172  C  CD    . GLU A 1 1934 ? 155.268 173.851 160.346 1.00 37.41  ? 1934 GLU A CD    1 
ATOM   3173  O  OE1   . GLU A 1 1934 ? 155.760 173.883 159.198 1.00 40.52  ? 1934 GLU A OE1   1 
ATOM   3174  O  OE2   . GLU A 1 1934 ? 155.517 174.711 161.214 1.00 48.80  ? 1934 GLU A OE2   1 
ATOM   3175  N  N     . THR A 1 1935 ? 151.526 173.037 158.651 1.00 15.88  ? 1935 THR A N     1 
ATOM   3176  C  CA    . THR A 1 1935 ? 150.110 173.250 158.918 1.00 15.97  ? 1935 THR A CA    1 
ATOM   3177  C  C     . THR A 1 1935 ? 149.214 172.658 157.839 1.00 18.01  ? 1935 THR A C     1 
ATOM   3178  O  O     . THR A 1 1935 ? 147.992 172.625 158.020 1.00 18.18  ? 1935 THR A O     1 
ATOM   3179  C  CB    . THR A 1 1935 ? 149.809 174.743 159.066 1.00 13.83  ? 1935 THR A CB    1 
ATOM   3180  O  OG1   . THR A 1 1935 ? 150.076 175.414 157.830 1.00 16.83  ? 1935 THR A OG1   1 
ATOM   3181  C  CG2   . THR A 1 1935 ? 150.668 175.349 160.161 1.00 16.74  ? 1935 THR A CG2   1 
ATOM   3182  N  N     . PHE A 1 1936 ? 149.786 172.199 156.726 1.00 18.94  ? 1936 PHE A N     1 
ATOM   3183  C  CA    . PHE A 1 1936 ? 149.033 171.502 155.686 1.00 15.98  ? 1936 PHE A CA    1 
ATOM   3184  C  C     . PHE A 1 1936 ? 148.789 170.076 156.169 1.00 21.83  ? 1936 PHE A C     1 
ATOM   3185  O  O     . PHE A 1 1936 ? 149.493 169.127 155.815 1.00 23.59  ? 1936 PHE A O     1 
ATOM   3186  C  CB    . PHE A 1 1936 ? 149.786 171.531 154.362 1.00 17.11  ? 1936 PHE A CB    1 
ATOM   3187  C  CG    . PHE A 1 1936 ? 149.570 172.787 153.567 1.00 17.41  ? 1936 PHE A CG    1 
ATOM   3188  C  CD1   . PHE A 1 1936 ? 149.971 174.015 154.063 1.00 12.08  ? 1936 PHE A CD1   1 
ATOM   3189  C  CD2   . PHE A 1 1936 ? 148.971 172.738 152.320 1.00 22.49  ? 1936 PHE A CD2   1 
ATOM   3190  C  CE1   . PHE A 1 1936 ? 149.776 175.171 153.333 1.00 10.86  ? 1936 PHE A CE1   1 
ATOM   3191  C  CE2   . PHE A 1 1936 ? 148.774 173.890 151.585 1.00 21.58  ? 1936 PHE A CE2   1 
ATOM   3192  C  CZ    . PHE A 1 1936 ? 149.177 175.108 152.093 1.00 13.11  ? 1936 PHE A CZ    1 
ATOM   3193  N  N     . ASP A 1 1937 ? 147.766 169.930 157.005 1.00 25.17  ? 1937 ASP A N     1 
ATOM   3194  C  CA    . ASP A 1 1937 ? 147.466 168.655 157.639 1.00 13.84  ? 1937 ASP A CA    1 
ATOM   3195  C  C     . ASP A 1 1937 ? 146.660 167.775 156.685 1.00 16.12  ? 1937 ASP A C     1 
ATOM   3196  O  O     . ASP A 1 1937 ? 146.518 168.066 155.495 1.00 18.58  ? 1937 ASP A O     1 
ATOM   3197  C  CB    . ASP A 1 1937 ? 146.739 168.883 158.961 1.00 14.97  ? 1937 ASP A CB    1 
ATOM   3198  C  CG    . ASP A 1 1937 ? 145.373 169.509 158.774 1.00 20.50  ? 1937 ASP A CG    1 
ATOM   3199  O  OD1   . ASP A 1 1937 ? 145.293 170.593 158.162 1.00 24.32  ? 1937 ASP A OD1   1 
ATOM   3200  O  OD2   . ASP A 1 1937 ? 144.379 168.915 159.240 1.00 20.67  ? 1937 ASP A OD2   1 
ATOM   3201  N  N     . PHE A 1 1938 ? 146.125 166.672 157.213 1.00 19.01  ? 1938 PHE A N     1 
ATOM   3202  C  CA    . PHE A 1 1938 ? 145.384 165.724 156.386 1.00 14.95  ? 1938 PHE A CA    1 
ATOM   3203  C  C     . PHE A 1 1938 ? 144.133 166.360 155.792 1.00 15.12  ? 1938 PHE A C     1 
ATOM   3204  O  O     . PHE A 1 1938 ? 143.818 166.148 154.616 1.00 17.34  ? 1938 PHE A O     1 
ATOM   3205  C  CB    . PHE A 1 1938 ? 145.026 164.492 157.218 1.00 18.47  ? 1938 PHE A CB    1 
ATOM   3206  C  CG    . PHE A 1 1938 ? 144.284 163.432 156.455 1.00 20.95  ? 1938 PHE A CG    1 
ATOM   3207  C  CD1   . PHE A 1 1938 ? 144.953 162.592 155.584 1.00 18.47  ? 1938 PHE A CD1   1 
ATOM   3208  C  CD2   . PHE A 1 1938 ? 142.921 163.265 156.624 1.00 21.68  ? 1938 PHE A CD2   1 
ATOM   3209  C  CE1   . PHE A 1 1938 ? 144.276 161.613 154.889 1.00 17.63  ? 1938 PHE A CE1   1 
ATOM   3210  C  CE2   . PHE A 1 1938 ? 142.239 162.289 155.929 1.00 20.34  ? 1938 PHE A CE2   1 
ATOM   3211  C  CZ    . PHE A 1 1938 ? 142.916 161.462 155.061 1.00 20.88  ? 1938 PHE A CZ    1 
ATOM   3212  N  N     . GLN A 1 1939 ? 143.414 167.154 156.587 1.00 16.01  ? 1939 GLN A N     1 
ATOM   3213  C  CA    . GLN A 1 1939 ? 142.150 167.721 156.126 1.00 17.11  ? 1939 GLN A CA    1 
ATOM   3214  C  C     . GLN A 1 1939 ? 142.363 168.793 155.062 1.00 17.96  ? 1939 GLN A C     1 
ATOM   3215  O  O     . GLN A 1 1939 ? 141.638 168.834 154.058 1.00 23.58  ? 1939 GLN A O     1 
ATOM   3216  C  CB    . GLN A 1 1939 ? 141.381 168.288 157.317 1.00 24.77  ? 1939 GLN A CB    1 
ATOM   3217  C  CG    . GLN A 1 1939 ? 141.106 167.274 158.409 1.00 22.32  ? 1939 GLN A CG    1 
ATOM   3218  C  CD    . GLN A 1 1939 ? 139.799 166.543 158.200 1.00 36.39  ? 1939 GLN A CD    1 
ATOM   3219  O  OE1   . GLN A 1 1939 ? 138.742 167.161 158.082 1.00 35.65  ? 1939 GLN A OE1   1 
ATOM   3220  N  NE2   . GLN A 1 1939 ? 139.863 165.218 158.150 1.00 39.15  ? 1939 GLN A NE2   1 
ATOM   3221  N  N     . ALA A 1 1940 ? 143.342 169.676 155.268 1.00 13.41  ? 1940 ALA A N     1 
ATOM   3222  C  CA    . ALA A 1 1940 ? 143.610 170.728 154.292 1.00 14.06  ? 1940 ALA A CA    1 
ATOM   3223  C  C     . ALA A 1 1940 ? 144.065 170.140 152.962 1.00 14.26  ? 1940 ALA A C     1 
ATOM   3224  O  O     . ALA A 1 1940 ? 143.589 170.543 151.892 1.00 13.22  ? 1940 ALA A O     1 
ATOM   3225  C  CB    . ALA A 1 1940 ? 144.658 171.695 154.843 1.00 17.97  ? 1940 ALA A CB    1 
ATOM   3226  N  N     . MET A 1 1941 ? 144.989 169.177 153.013 1.00 13.69  ? 1941 MET A N     1 
ATOM   3227  C  CA    . MET A 1 1941 ? 145.435 168.517 151.792 1.00 10.95  ? 1941 MET A CA    1 
ATOM   3228  C  C     . MET A 1 1941 ? 144.289 167.766 151.131 1.00 11.41  ? 1941 MET A C     1 
ATOM   3229  O  O     . MET A 1 1941 ? 144.185 167.740 149.900 1.00 13.64  ? 1941 MET A O     1 
ATOM   3230  C  CB    . MET A 1 1941 ? 146.597 167.571 152.094 1.00 9.98   ? 1941 MET A CB    1 
ATOM   3231  C  CG    . MET A 1 1941 ? 147.859 168.266 152.578 1.00 13.70  ? 1941 MET A CG    1 
ATOM   3232  S  SD    . MET A 1 1941 ? 148.655 169.257 151.300 1.00 22.35  ? 1941 MET A SD    1 
ATOM   3233  C  CE    . MET A 1 1941 ? 148.941 168.020 150.040 1.00 6.95   ? 1941 MET A CE    1 
ATOM   3234  N  N     . GLY A 1 1942 ? 143.416 167.154 151.932 1.00 11.12  ? 1942 GLY A N     1 
ATOM   3235  C  CA    . GLY A 1 1942 ? 142.275 166.455 151.368 1.00 11.04  ? 1942 GLY A CA    1 
ATOM   3236  C  C     . GLY A 1 1942 ? 141.335 167.377 150.618 1.00 12.75  ? 1942 GLY A C     1 
ATOM   3237  O  O     . GLY A 1 1942 ? 140.868 167.047 149.528 1.00 15.43  ? 1942 GLY A O     1 
ATOM   3238  N  N     . ARG A 1 1943 ? 141.048 168.550 151.187 1.00 12.76  ? 1943 ARG A N     1 
ATOM   3239  C  CA    . ARG A 1 1943 ? 140.159 169.487 150.501 1.00 11.65  ? 1943 ARG A CA    1 
ATOM   3240  C  C     . ARG A 1 1943 ? 140.824 170.102 149.274 1.00 13.41  ? 1943 ARG A C     1 
ATOM   3241  O  O     . ARG A 1 1943 ? 140.157 170.347 148.260 1.00 20.27  ? 1943 ARG A O     1 
ATOM   3242  C  CB    . ARG A 1 1943 ? 139.672 170.561 151.468 1.00 14.75  ? 1943 ARG A CB    1 
ATOM   3243  C  CG    . ARG A 1 1943 ? 138.747 169.995 152.522 1.00 28.12  ? 1943 ARG A CG    1 
ATOM   3244  C  CD    . ARG A 1 1943 ? 138.249 171.034 153.497 1.00 31.54  ? 1943 ARG A CD    1 
ATOM   3245  N  NE    . ARG A 1 1943 ? 137.342 170.425 154.462 1.00 38.99  ? 1943 ARG A NE    1 
ATOM   3246  C  CZ    . ARG A 1 1943 ? 137.724 169.906 155.619 1.00 43.80  ? 1943 ARG A CZ    1 
ATOM   3247  N  NH1   . ARG A 1 1943 ? 138.995 169.890 155.981 1.00 38.53  ? 1943 ARG A NH1   1 
ATOM   3248  N  NH2   . ARG A 1 1943 ? 136.810 169.379 156.428 1.00 47.95  ? 1943 ARG A NH2   1 
ATOM   3249  N  N     . ILE A 1 1944 ? 142.135 170.346 149.334 1.00 11.60  ? 1944 ILE A N     1 
ATOM   3250  C  CA    . ILE A 1 1944 ? 142.843 170.800 148.141 1.00 9.09   ? 1944 ILE A CA    1 
ATOM   3251  C  C     . ILE A 1 1944 ? 142.756 169.746 147.043 1.00 12.83  ? 1944 ILE A C     1 
ATOM   3252  O  O     . ILE A 1 1944 ? 142.510 170.062 145.871 1.00 14.18  ? 1944 ILE A O     1 
ATOM   3253  C  CB    . ILE A 1 1944 ? 144.303 171.149 148.484 1.00 10.14  ? 1944 ILE A CB    1 
ATOM   3254  C  CG1   . ILE A 1 1944 ? 144.360 172.425 149.325 1.00 7.60   ? 1944 ILE A CG1   1 
ATOM   3255  C  CG2   . ILE A 1 1944 ? 145.131 171.311 147.219 1.00 6.38   ? 1944 ILE A CG2   1 
ATOM   3256  C  CD1   . ILE A 1 1944 ? 145.731 172.726 149.881 1.00 6.77   ? 1944 ILE A CD1   1 
ATOM   3257  N  N     . PHE A 1 1945 ? 142.944 168.475 147.408 1.00 10.47  ? 1945 PHE A N     1 
ATOM   3258  C  CA    . PHE A 1 1945 ? 142.832 167.392 146.439 1.00 9.12   ? 1945 PHE A CA    1 
ATOM   3259  C  C     . PHE A 1 1945 ? 141.418 167.287 145.887 1.00 11.17  ? 1945 PHE A C     1 
ATOM   3260  O  O     . PHE A 1 1945 ? 141.229 166.980 144.708 1.00 14.72  ? 1945 PHE A O     1 
ATOM   3261  C  CB    . PHE A 1 1945 ? 143.252 166.071 147.081 1.00 8.68   ? 1945 PHE A CB    1 
ATOM   3262  C  CG    . PHE A 1 1945 ? 144.733 165.931 147.266 1.00 10.84  ? 1945 PHE A CG    1 
ATOM   3263  C  CD1   . PHE A 1 1945 ? 145.615 166.564 146.408 1.00 8.92   ? 1945 PHE A CD1   1 
ATOM   3264  C  CD2   . PHE A 1 1945 ? 145.244 165.170 148.301 1.00 9.07   ? 1945 PHE A CD2   1 
ATOM   3265  C  CE1   . PHE A 1 1945 ? 146.977 166.437 146.578 1.00 7.03   ? 1945 PHE A CE1   1 
ATOM   3266  C  CE2   . PHE A 1 1945 ? 146.605 165.041 148.476 1.00 9.15   ? 1945 PHE A CE2   1 
ATOM   3267  C  CZ    . PHE A 1 1945 ? 147.473 165.675 147.613 1.00 7.29   ? 1945 PHE A CZ    1 
ATOM   3268  N  N     . VAL A 1 1946 ? 140.411 167.519 146.731 1.00 12.45  ? 1946 VAL A N     1 
ATOM   3269  C  CA    . VAL A 1 1946 ? 139.025 167.488 146.270 1.00 10.02  ? 1946 VAL A CA    1 
ATOM   3270  C  C     . VAL A 1 1946 ? 138.794 168.573 145.226 1.00 14.54  ? 1946 VAL A C     1 
ATOM   3271  O  O     . VAL A 1 1946 ? 138.184 168.334 144.175 1.00 17.82  ? 1946 VAL A O     1 
ATOM   3272  C  CB    . VAL A 1 1946 ? 138.062 167.640 147.461 1.00 7.60   ? 1946 VAL A CB    1 
ATOM   3273  C  CG1   . VAL A 1 1946 ? 136.674 168.036 146.981 1.00 15.25  ? 1946 VAL A CG1   1 
ATOM   3274  C  CG2   . VAL A 1 1946 ? 138.003 166.353 148.263 1.00 10.29  ? 1946 VAL A CG2   1 
ATOM   3275  N  N     . GLY A 1 1947 ? 139.282 169.782 145.505 1.00 16.26  ? 1947 GLY A N     1 
ATOM   3276  C  CA    . GLY A 1 1947 ? 139.152 170.861 144.538 1.00 12.65  ? 1947 GLY A CA    1 
ATOM   3277  C  C     . GLY A 1 1947 ? 139.863 170.557 143.234 1.00 13.69  ? 1947 GLY A C     1 
ATOM   3278  O  O     . GLY A 1 1947 ? 139.336 170.813 142.148 1.00 15.52  ? 1947 GLY A O     1 
ATOM   3279  N  N     . LEU A 1 1948 ? 141.073 170.000 143.324 1.00 14.44  ? 1948 LEU A N     1 
ATOM   3280  C  CA    . LEU A 1 1948 ? 141.820 169.656 142.117 1.00 9.66   ? 1948 LEU A CA    1 
ATOM   3281  C  C     . LEU A 1 1948 ? 141.121 168.559 141.322 1.00 11.36  ? 1948 LEU A C     1 
ATOM   3282  O  O     . LEU A 1 1948 ? 141.103 168.595 140.087 1.00 14.37  ? 1948 LEU A O     1 
ATOM   3283  C  CB    . LEU A 1 1948 ? 143.242 169.233 142.480 1.00 11.71  ? 1948 LEU A CB    1 
ATOM   3284  C  CG    . LEU A 1 1948 ? 144.130 170.304 143.115 1.00 7.69   ? 1948 LEU A CG    1 
ATOM   3285  C  CD1   . LEU A 1 1948 ? 145.484 169.726 143.481 1.00 4.96   ? 1948 LEU A CD1   1 
ATOM   3286  C  CD2   . LEU A 1 1948 ? 144.285 171.497 142.190 1.00 6.24   ? 1948 LEU A CD2   1 
ATOM   3287  N  N     . CYS A 1 1949 ? 140.552 167.568 142.013 1.00 14.37  ? 1949 CYS A N     1 
ATOM   3288  C  CA    . CYS A 1 1949 ? 139.812 166.506 141.341 1.00 11.52  ? 1949 CYS A CA    1 
ATOM   3289  C  C     . CYS A 1 1949 ? 138.602 167.065 140.608 1.00 14.61  ? 1949 CYS A C     1 
ATOM   3290  O  O     . CYS A 1 1949 ? 138.376 166.758 139.432 1.00 15.11  ? 1949 CYS A O     1 
ATOM   3291  C  CB    . CYS A 1 1949 ? 139.363 165.453 142.357 1.00 17.25  ? 1949 CYS A CB    1 
ATOM   3292  S  SG    . CYS A 1 1949 ? 140.621 164.308 142.948 1.00 23.98  ? 1949 CYS A SG    1 
ATOM   3293  N  N     . GLN A 1 1950 ? 137.809 167.888 141.295 1.00 15.55  ? 1950 GLN A N     1 
ATOM   3294  C  CA    . GLN A 1 1950 ? 136.587 168.410 140.694 1.00 15.97  ? 1950 GLN A CA    1 
ATOM   3295  C  C     . GLN A 1 1950 ? 136.890 169.347 139.532 1.00 15.00  ? 1950 GLN A C     1 
ATOM   3296  O  O     . GLN A 1 1950 ? 136.308 169.210 138.450 1.00 18.11  ? 1950 GLN A O     1 
ATOM   3297  C  CB    . GLN A 1 1950 ? 135.750 169.116 141.758 1.00 21.16  ? 1950 GLN A CB    1 
ATOM   3298  C  CG    . GLN A 1 1950 ? 135.225 168.195 142.842 1.00 22.70  ? 1950 GLN A CG    1 
ATOM   3299  C  CD    . GLN A 1 1950 ? 134.285 167.140 142.301 1.00 30.58  ? 1950 GLN A CD    1 
ATOM   3300  O  OE1   . GLN A 1 1950 ? 134.621 165.960 142.250 1.00 36.19  ? 1950 GLN A OE1   1 
ATOM   3301  N  NE2   . GLN A 1 1950 ? 133.097 167.564 141.890 1.00 35.27  ? 1950 GLN A NE2   1 
ATOM   3302  N  N     . VAL A 1 1951 ? 137.797 170.305 139.733 1.00 13.84  ? 1951 VAL A N     1 
ATOM   3303  C  CA    . VAL A 1 1951 ? 138.116 171.253 138.671 1.00 13.58  ? 1951 VAL A CA    1 
ATOM   3304  C  C     . VAL A 1 1951 ? 138.891 170.569 137.552 1.00 11.55  ? 1951 VAL A C     1 
ATOM   3305  O  O     . VAL A 1 1951 ? 138.643 170.814 136.366 1.00 9.43   ? 1951 VAL A O     1 
ATOM   3306  C  CB    . VAL A 1 1951 ? 138.888 172.453 139.249 1.00 13.04  ? 1951 VAL A CB    1 
ATOM   3307  C  CG1   . VAL A 1 1951 ? 139.302 173.405 138.142 1.00 13.87  ? 1951 VAL A CG1   1 
ATOM   3308  C  CG2   . VAL A 1 1951 ? 138.039 173.169 140.281 1.00 21.83  ? 1951 VAL A CG2   1 
ATOM   3309  N  N     . GLY A 1 1952 ? 139.829 169.697 137.905 1.00 14.64  ? 1952 GLY A N     1 
ATOM   3310  C  CA    . GLY A 1 1952 ? 140.687 169.078 136.916 1.00 9.89   ? 1952 GLY A CA    1 
ATOM   3311  C  C     . GLY A 1 1952 ? 141.937 169.900 136.696 1.00 9.87   ? 1952 GLY A C     1 
ATOM   3312  O  O     . GLY A 1 1952 ? 142.381 170.092 135.561 1.00 16.56  ? 1952 GLY A O     1 
ATOM   3313  N  N     . ALA A 1 1953 ? 142.510 170.390 137.788 1.00 8.22   ? 1953 ALA A N     1 
ATOM   3314  C  CA    . ALA A 1 1953 ? 143.641 171.301 137.757 1.00 5.99   ? 1953 ALA A CA    1 
ATOM   3315  C  C     . ALA A 1 1953 ? 144.906 170.598 138.228 1.00 8.49   ? 1953 ALA A C     1 
ATOM   3316  O  O     . ALA A 1 1953 ? 144.873 169.489 138.768 1.00 9.12   ? 1953 ALA A O     1 
ATOM   3317  C  CB    . ALA A 1 1953 ? 143.359 172.534 138.621 1.00 7.36   ? 1953 ALA A CB    1 
ATOM   3318  N  N     . TRP A 1 1954 ? 146.033 171.267 138.014 1.00 8.54   ? 1954 TRP A N     1 
ATOM   3319  C  CA    . TRP A 1 1954 ? 147.339 170.767 138.415 1.00 4.96   ? 1954 TRP A CA    1 
ATOM   3320  C  C     . TRP A 1 1954 ? 147.741 171.405 139.735 1.00 5.12   ? 1954 TRP A C     1 
ATOM   3321  O  O     . TRP A 1 1954 ? 147.692 172.631 139.878 1.00 7.14   ? 1954 TRP A O     1 
ATOM   3322  C  CB    . TRP A 1 1954 ? 148.391 171.070 137.348 1.00 4.04   ? 1954 TRP A CB    1 
ATOM   3323  C  CG    . TRP A 1 1954 ? 148.352 170.153 136.170 1.00 4.34   ? 1954 TRP A CG    1 
ATOM   3324  C  CD1   . TRP A 1 1954 ? 147.280 169.450 135.712 1.00 5.62   ? 1954 TRP A CD1   1 
ATOM   3325  C  CD2   . TRP A 1 1954 ? 149.438 169.849 135.289 1.00 4.06   ? 1954 TRP A CD2   1 
ATOM   3326  N  NE1   . TRP A 1 1954 ? 147.631 168.720 134.604 1.00 6.35   ? 1954 TRP A NE1   1 
ATOM   3327  C  CE2   . TRP A 1 1954 ? 148.952 168.949 134.323 1.00 4.76   ? 1954 TRP A CE2   1 
ATOM   3328  C  CE3   . TRP A 1 1954 ? 150.775 170.249 135.225 1.00 3.67   ? 1954 TRP A CE3   1 
ATOM   3329  C  CZ2   . TRP A 1 1954 ? 149.755 168.445 133.306 1.00 4.41   ? 1954 TRP A CZ2   1 
ATOM   3330  C  CZ3   . TRP A 1 1954 ? 151.569 169.745 134.216 1.00 2.72   ? 1954 TRP A CZ3   1 
ATOM   3331  C  CH2   . TRP A 1 1954 ? 151.058 168.855 133.270 1.00 3.11   ? 1954 TRP A CH2   1 
ATOM   3332  N  N     . GLY A 1 1955 ? 148.137 170.575 140.694 1.00 5.23   ? 1955 GLY A N     1 
ATOM   3333  C  CA    . GLY A 1 1955 ? 148.590 171.078 141.973 1.00 4.15   ? 1955 GLY A CA    1 
ATOM   3334  C  C     . GLY A 1 1955 ? 150.084 170.943 142.158 1.00 4.04   ? 1955 GLY A C     1 
ATOM   3335  O  O     . GLY A 1 1955 ? 150.594 169.837 142.353 1.00 5.23   ? 1955 GLY A O     1 
ATOM   3336  N  N     . CYS A 1 1956 ? 150.799 172.062 142.097 1.00 4.48   ? 1956 CYS A N     1 
ATOM   3337  C  CA    . CYS A 1 1956 ? 152.244 172.077 142.308 1.00 4.24   ? 1956 CYS A CA    1 
ATOM   3338  C  C     . CYS A 1 1956 ? 152.492 172.378 143.779 1.00 7.02   ? 1956 CYS A C     1 
ATOM   3339  O  O     . CYS A 1 1956 ? 152.402 173.528 144.214 1.00 10.56  ? 1956 CYS A O     1 
ATOM   3340  C  CB    . CYS A 1 1956 ? 152.915 173.101 141.401 1.00 6.18   ? 1956 CYS A CB    1 
ATOM   3341  S  SG    . CYS A 1 1956 ? 154.718 173.025 141.399 1.00 18.24  ? 1956 CYS A SG    1 
ATOM   3342  N  N     . PHE A 1 1957 ? 152.801 171.338 144.550 1.00 5.59   ? 1957 PHE A N     1 
ATOM   3343  C  CA    . PHE A 1 1957 ? 153.009 171.470 145.991 1.00 5.99   ? 1957 PHE A CA    1 
ATOM   3344  C  C     . PHE A 1 1957 ? 154.491 171.701 146.251 1.00 8.66   ? 1957 PHE A C     1 
ATOM   3345  O  O     . PHE A 1 1957 ? 155.285 170.766 146.344 1.00 10.49  ? 1957 PHE A O     1 
ATOM   3346  C  CB    . PHE A 1 1957 ? 152.483 170.242 146.721 1.00 4.96   ? 1957 PHE A CB    1 
ATOM   3347  C  CG    . PHE A 1 1957 ? 151.007 170.030 146.555 1.00 4.99   ? 1957 PHE A CG    1 
ATOM   3348  C  CD1   . PHE A 1 1957 ? 150.111 170.597 147.442 1.00 4.77   ? 1957 PHE A CD1   1 
ATOM   3349  C  CD2   . PHE A 1 1957 ? 150.513 169.271 145.509 1.00 5.43   ? 1957 PHE A CD2   1 
ATOM   3350  C  CE1   . PHE A 1 1957 ? 148.755 170.410 147.292 1.00 4.66   ? 1957 PHE A CE1   1 
ATOM   3351  C  CE2   . PHE A 1 1957 ? 149.156 169.081 145.355 1.00 4.32   ? 1957 PHE A CE2   1 
ATOM   3352  C  CZ    . PHE A 1 1957 ? 148.278 169.651 146.247 1.00 4.40   ? 1957 PHE A CZ    1 
ATOM   3353  N  N     . ASP A 1 1958 ? 154.866 172.971 146.368 1.00 8.82   ? 1958 ASP A N     1 
ATOM   3354  C  CA    . ASP A 1 1958 ? 156.237 173.342 146.675 1.00 8.99   ? 1958 ASP A CA    1 
ATOM   3355  C  C     . ASP A 1 1958 ? 156.530 173.139 148.155 1.00 12.97  ? 1958 ASP A C     1 
ATOM   3356  O  O     . ASP A 1 1958 ? 155.656 173.306 149.011 1.00 15.42  ? 1958 ASP A O     1 
ATOM   3357  C  CB    . ASP A 1 1958 ? 156.501 174.795 146.288 1.00 15.00  ? 1958 ASP A CB    1 
ATOM   3358  C  CG    . ASP A 1 1958 ? 156.176 175.082 144.842 1.00 22.51  ? 1958 ASP A CG    1 
ATOM   3359  O  OD1   . ASP A 1 1958 ? 155.770 174.146 144.124 1.00 21.58  ? 1958 ASP A OD1   1 
ATOM   3360  O  OD2   . ASP A 1 1958 ? 156.328 176.247 144.423 1.00 27.87  ? 1958 ASP A OD2   1 
ATOM   3361  N  N     . GLU A 1 1959 ? 157.788 172.804 148.451 1.00 13.09  ? 1959 GLU A N     1 
ATOM   3362  C  CA    . GLU A 1 1959 ? 158.213 172.420 149.800 1.00 9.85   ? 1959 GLU A CA    1 
ATOM   3363  C  C     . GLU A 1 1959 ? 157.269 171.386 150.409 1.00 8.57   ? 1959 GLU A C     1 
ATOM   3364  O  O     . GLU A 1 1959 ? 156.703 171.591 151.483 1.00 12.72  ? 1959 GLU A O     1 
ATOM   3365  C  CB    . GLU A 1 1959 ? 158.364 173.631 150.726 1.00 13.06  ? 1959 GLU A CB    1 
ATOM   3366  C  CG    . GLU A 1 1959 ? 159.502 174.582 150.366 1.00 15.97  ? 1959 GLU A CG    1 
ATOM   3367  C  CD    . GLU A 1 1959 ? 159.144 175.580 149.289 1.00 23.54  ? 1959 GLU A CD    1 
ATOM   3368  O  OE1   . GLU A 1 1959 ? 157.980 175.593 148.851 1.00 31.16  ? 1959 GLU A OE1   1 
ATOM   3369  O  OE2   . GLU A 1 1959 ? 160.036 176.348 148.870 1.00 25.02  ? 1959 GLU A OE2   1 
ATOM   3370  N  N     . PHE A 1 1960 ? 157.070 170.275 149.697 1.00 10.18  ? 1960 PHE A N     1 
ATOM   3371  C  CA    . PHE A 1 1960 ? 156.146 169.219 150.193 1.00 8.88   ? 1960 PHE A CA    1 
ATOM   3372  C  C     . PHE A 1 1960 ? 156.770 168.559 151.418 1.00 7.15   ? 1960 PHE A C     1 
ATOM   3373  O  O     . PHE A 1 1960 ? 156.035 167.957 152.229 1.00 10.44  ? 1960 PHE A O     1 
ATOM   3374  C  CB    . PHE A 1 1960 ? 155.872 168.186 149.097 1.00 7.27   ? 1960 PHE A CB    1 
ATOM   3375  C  CG    . PHE A 1 1960 ? 154.768 167.191 149.429 1.00 6.93   ? 1960 PHE A CG    1 
ATOM   3376  C  CD1   . PHE A 1 1960 ? 153.641 167.587 150.141 1.00 8.45   ? 1960 PHE A CD1   1 
ATOM   3377  C  CD2   . PHE A 1 1960 ? 154.871 165.858 149.049 1.00 6.86   ? 1960 PHE A CD2   1 
ATOM   3378  C  CE1   . PHE A 1 1960 ? 152.640 166.679 150.444 1.00 9.39   ? 1960 PHE A CE1   1 
ATOM   3379  C  CE2   . PHE A 1 1960 ? 153.866 164.954 149.356 1.00 5.59   ? 1960 PHE A CE2   1 
ATOM   3380  C  CZ    . PHE A 1 1960 ? 152.755 165.366 150.053 1.00 7.65   ? 1960 PHE A CZ    1 
ATOM   3381  N  N     . ASN A 1 1961 ? 158.093 168.674 151.558 1.00 5.85   ? 1961 ASN A N     1 
ATOM   3382  C  CA    . ASN A 1 1961 ? 158.807 168.019 152.688 1.00 6.97   ? 1961 ASN A CA    1 
ATOM   3383  C  C     . ASN A 1 1961 ? 158.716 168.894 153.944 1.00 8.54   ? 1961 ASN A C     1 
ATOM   3384  O  O     . ASN A 1 1961 ? 159.212 168.457 155.001 1.00 12.58  ? 1961 ASN A O     1 
ATOM   3385  C  CB    . ASN A 1 1961 ? 160.246 167.683 152.311 1.00 8.57   ? 1961 ASN A CB    1 
ATOM   3386  C  CG    . ASN A 1 1961 ? 160.939 168.820 151.598 1.00 9.77   ? 1961 ASN A CG    1 
ATOM   3387  O  OD1   . ASN A 1 1961 ? 160.356 169.895 151.420 1.00 12.82  ? 1961 ASN A OD1   1 
ATOM   3388  N  ND2   . ASN A 1 1961 ? 162.180 168.606 151.187 1.00 8.77   ? 1961 ASN A ND2   1 
ATOM   3389  N  N     . ARG A 1 1962 ? 158.101 170.076 153.836 1.00 8.27   ? 1962 ARG A N     1 
ATOM   3390  C  CA    . ARG A 1 1962 ? 157.925 170.957 155.022 1.00 11.30  ? 1962 ARG A CA    1 
ATOM   3391  C  C     . ARG A 1 1962 ? 156.774 170.414 155.884 1.00 15.34  ? 1962 ARG A C     1 
ATOM   3392  O  O     . ARG A 1 1962 ? 156.586 170.931 157.006 1.00 18.76  ? 1962 ARG A O     1 
ATOM   3393  C  CB    . ARG A 1 1962 ? 157.716 172.414 154.595 1.00 7.89   ? 1962 ARG A CB    1 
ATOM   3394  C  CG    . ARG A 1 1962 ? 158.994 173.040 154.057 1.00 8.37   ? 1962 ARG A CG    1 
ATOM   3395  C  CD    . ARG A 1 1962 ? 158.910 174.552 153.920 1.00 8.24   ? 1962 ARG A CD    1 
ATOM   3396  N  NE    . ARG A 1 1962 ? 158.699 175.225 155.206 1.00 6.36   ? 1962 ARG A NE    1 
ATOM   3397  C  CZ    . ARG A 1 1962 ? 157.681 176.032 155.475 1.00 6.42   ? 1962 ARG A CZ    1 
ATOM   3398  N  NH1   . ARG A 1 1962 ? 156.837 176.372 154.519 1.00 7.48   ? 1962 ARG A NH1   1 
ATOM   3399  N  NH2   . ARG A 1 1962 ? 157.517 176.501 156.699 1.00 6.97   ? 1962 ARG A NH2   1 
ATOM   3400  N  N     . LEU A 1 1963 ? 156.038 169.416 155.385 1.00 11.27  ? 1963 LEU A N     1 
ATOM   3401  C  CA    . LEU A 1 1963 ? 154.983 168.798 156.168 1.00 11.21  ? 1963 LEU A CA    1 
ATOM   3402  C  C     . LEU A 1 1963 ? 155.584 167.870 157.217 1.00 18.28  ? 1963 LEU A C     1 
ATOM   3403  O  O     . LEU A 1 1963 ? 156.758 167.497 157.155 1.00 20.09  ? 1963 LEU A O     1 
ATOM   3404  C  CB    . LEU A 1 1963 ? 154.030 168.002 155.274 1.00 11.26  ? 1963 LEU A CB    1 
ATOM   3405  C  CG    . LEU A 1 1963 ? 152.897 168.701 154.521 1.00 13.73  ? 1963 LEU A CG    1 
ATOM   3406  C  CD1   . LEU A 1 1963 ? 153.433 169.707 153.528 1.00 13.50  ? 1963 LEU A CD1   1 
ATOM   3407  C  CD2   . LEU A 1 1963 ? 152.018 167.676 153.821 1.00 9.71   ? 1963 LEU A CD2   1 
ATOM   3408  N  N     . GLU A 1 1964 ? 154.762 167.499 158.192 1.00 20.34  ? 1964 GLU A N     1 
ATOM   3409  C  CA    . GLU A 1 1964 ? 155.159 166.465 159.133 1.00 15.04  ? 1964 GLU A CA    1 
ATOM   3410  C  C     . GLU A 1 1964 ? 155.219 165.116 158.427 1.00 13.29  ? 1964 GLU A C     1 
ATOM   3411  O  O     . GLU A 1 1964 ? 154.502 164.868 157.454 1.00 14.05  ? 1964 GLU A O     1 
ATOM   3412  C  CB    . GLU A 1 1964 ? 154.185 166.403 160.312 1.00 22.66  ? 1964 GLU A CB    1 
ATOM   3413  C  CG    . GLU A 1 1964 ? 153.865 167.741 160.999 1.00 35.40  ? 1964 GLU A CG    1 
ATOM   3414  C  CD    . GLU A 1 1964 ? 155.074 168.482 161.575 1.00 46.37  ? 1964 GLU A CD    1 
ATOM   3415  O  OE1   . GLU A 1 1964 ? 156.234 168.075 161.354 1.00 34.06  ? 1964 GLU A OE1   1 
ATOM   3416  O  OE2   . GLU A 1 1964 ? 154.850 169.496 162.270 1.00 52.11  ? 1964 GLU A OE2   1 
ATOM   3417  N  N     . GLU A 1 1965 ? 156.095 164.239 158.923 1.00 13.79  ? 1965 GLU A N     1 
ATOM   3418  C  CA    . GLU A 1 1965 ? 156.226 162.917 158.320 1.00 15.46  ? 1965 GLU A CA    1 
ATOM   3419  C  C     . GLU A 1 1965 ? 154.931 162.126 158.439 1.00 13.95  ? 1965 GLU A C     1 
ATOM   3420  O  O     . GLU A 1 1965 ? 154.548 161.401 157.514 1.00 15.75  ? 1965 GLU A O     1 
ATOM   3421  C  CB    . GLU A 1 1965 ? 157.383 162.154 158.963 1.00 14.25  ? 1965 GLU A CB    1 
ATOM   3422  C  CG    . GLU A 1 1965 ? 158.695 162.913 158.968 1.00 22.77  ? 1965 GLU A CG    1 
ATOM   3423  C  CD    . GLU A 1 1965 ? 159.898 161.995 159.006 1.00 37.42  ? 1965 GLU A CD    1 
ATOM   3424  O  OE1   . GLU A 1 1965 ? 161.035 162.504 159.098 1.00 34.03  ? 1965 GLU A OE1   1 
ATOM   3425  O  OE2   . GLU A 1 1965 ? 159.706 160.763 158.941 1.00 40.63  ? 1965 GLU A OE2   1 
ATOM   3426  N  N     . ARG A 1 1966 ? 154.246 162.249 159.576 1.00 10.35  ? 1966 ARG A N     1 
ATOM   3427  C  CA    . ARG A 1 1966 ? 152.974 161.558 159.751 1.00 10.85  ? 1966 ARG A CA    1 
ATOM   3428  C  C     . ARG A 1 1966 ? 151.898 162.140 158.837 1.00 10.43  ? 1966 ARG A C     1 
ATOM   3429  O  O     . ARG A 1 1966 ? 151.070 161.399 158.295 1.00 11.34  ? 1966 ARG A O     1 
ATOM   3430  C  CB    . ARG A 1 1966 ? 152.578 161.596 161.230 1.00 14.15  ? 1966 ARG A CB    1 
ATOM   3431  C  CG    . ARG A 1 1966 ? 152.302 162.964 161.827 1.00 14.38  ? 1966 ARG A CG    1 
ATOM   3432  C  CD    . ARG A 1 1966 ? 151.969 162.813 163.309 1.00 20.20  ? 1966 ARG A CD    1 
ATOM   3433  N  NE    . ARG A 1 1966 ? 151.778 164.091 163.983 1.00 33.46  ? 1966 ARG A NE    1 
ATOM   3434  C  CZ    . ARG A 1 1966 ? 150.619 164.724 164.087 1.00 29.99  ? 1966 ARG A CZ    1 
ATOM   3435  N  NH1   . ARG A 1 1966 ? 149.490 164.168 163.683 1.00 19.34  ? 1966 ARG A NH1   1 
ATOM   3436  N  NH2   . ARG A 1 1966 ? 150.586 165.931 164.644 1.00 20.27  ? 1966 ARG A NH2   1 
ATOM   3437  N  N     . MET A 1 1967 ? 151.920 163.458 158.617 1.00 12.09  ? 1967 MET A N     1 
ATOM   3438  C  CA    . MET A 1 1967 ? 151.072 164.045 157.582 1.00 9.96   ? 1967 MET A CA    1 
ATOM   3439  C  C     . MET A 1 1967 ? 151.443 163.563 156.188 1.00 7.79   ? 1967 MET A C     1 
ATOM   3440  O  O     . MET A 1 1967 ? 150.553 163.346 155.363 1.00 8.43   ? 1967 MET A O     1 
ATOM   3441  C  CB    . MET A 1 1967 ? 151.123 165.571 157.646 1.00 11.20  ? 1967 MET A CB    1 
ATOM   3442  C  CG    . MET A 1 1967 ? 150.616 166.130 158.949 1.00 21.13  ? 1967 MET A CG    1 
ATOM   3443  S  SD    . MET A 1 1967 ? 148.900 165.611 159.137 1.00 21.34  ? 1967 MET A SD    1 
ATOM   3444  C  CE    . MET A 1 1967 ? 148.963 164.744 160.687 1.00 13.62  ? 1967 MET A CE    1 
ATOM   3445  N  N     . LEU A 1 1968 ? 152.735 163.408 155.894 1.00 8.46   ? 1968 LEU A N     1 
ATOM   3446  C  CA    . LEU A 1 1968 ? 153.121 162.875 154.592 1.00 7.33   ? 1968 LEU A CA    1 
ATOM   3447  C  C     . LEU A 1 1968 ? 152.572 161.468 154.397 1.00 7.82   ? 1968 LEU A C     1 
ATOM   3448  O  O     . LEU A 1 1968 ? 152.024 161.143 153.335 1.00 9.59   ? 1968 LEU A O     1 
ATOM   3449  C  CB    . LEU A 1 1968 ? 154.642 162.886 154.450 1.00 8.91   ? 1968 LEU A CB    1 
ATOM   3450  C  CG    . LEU A 1 1968 ? 155.296 164.254 154.248 1.00 9.57   ? 1968 LEU A CG    1 
ATOM   3451  C  CD1   . LEU A 1 1968 ? 156.790 164.178 154.510 1.00 13.47  ? 1968 LEU A CD1   1 
ATOM   3452  C  CD2   . LEU A 1 1968 ? 155.018 164.783 152.852 1.00 6.65   ? 1968 LEU A CD2   1 
ATOM   3453  N  N     . SER A 1 1969 ? 152.688 160.627 155.427 1.00 10.69  ? 1969 SER A N     1 
ATOM   3454  C  CA    . SER A 1 1969 ? 152.139 159.278 155.355 1.00 7.38   ? 1969 SER A CA    1 
ATOM   3455  C  C     . SER A 1 1969 ? 150.627 159.305 155.168 1.00 7.15   ? 1969 SER A C     1 
ATOM   3456  O  O     . SER A 1 1969 ? 150.083 158.547 154.358 1.00 8.31   ? 1969 SER A O     1 
ATOM   3457  C  CB    . SER A 1 1969 ? 152.511 158.497 156.615 1.00 6.49   ? 1969 SER A CB    1 
ATOM   3458  O  OG    . SER A 1 1969 ? 151.983 157.183 156.579 1.00 15.08  ? 1969 SER A OG    1 
ATOM   3459  N  N     . ALA A 1 1970 ? 149.934 160.180 155.901 1.00 7.14   ? 1970 ALA A N     1 
ATOM   3460  C  CA    . ALA A 1 1970 ? 148.482 160.260 155.779 1.00 7.89   ? 1970 ALA A CA    1 
ATOM   3461  C  C     . ALA A 1 1970 ? 148.060 160.721 154.388 1.00 11.60  ? 1970 ALA A C     1 
ATOM   3462  O  O     . ALA A 1 1970 ? 147.095 160.200 153.818 1.00 13.93  ? 1970 ALA A O     1 
ATOM   3463  C  CB    . ALA A 1 1970 ? 147.922 161.195 156.850 1.00 8.51   ? 1970 ALA A CB    1 
ATOM   3464  N  N     . VAL A 1 1971 ? 148.769 161.703 153.828 1.00 9.34   ? 1971 VAL A N     1 
ATOM   3465  C  CA    . VAL A 1 1971 ? 148.430 162.227 152.508 1.00 9.29   ? 1971 VAL A CA    1 
ATOM   3466  C  C     . VAL A 1 1971 ? 148.766 161.212 151.422 1.00 7.88   ? 1971 VAL A C     1 
ATOM   3467  O  O     . VAL A 1 1971 ? 148.167 161.228 150.335 1.00 12.05  ? 1971 VAL A O     1 
ATOM   3468  C  CB    . VAL A 1 1971 ? 149.147 163.577 152.298 1.00 8.50   ? 1971 VAL A CB    1 
ATOM   3469  C  CG1   . VAL A 1 1971 ? 149.080 164.034 150.849 1.00 7.04   ? 1971 VAL A CG1   1 
ATOM   3470  C  CG2   . VAL A 1 1971 ? 148.553 164.634 153.214 1.00 6.52   ? 1971 VAL A CG2   1 
ATOM   3471  N  N     . SER A 1 1972 ? 149.722 160.318 151.692 1.00 8.55   ? 1972 SER A N     1 
ATOM   3472  C  CA    . SER A 1 1972 ? 150.051 159.274 150.726 1.00 9.21   ? 1972 SER A CA    1 
ATOM   3473  C  C     . SER A 1 1972 ? 148.831 158.429 150.380 1.00 10.30  ? 1972 SER A C     1 
ATOM   3474  O  O     . SER A 1 1972 ? 148.678 157.993 149.235 1.00 10.63  ? 1972 SER A O     1 
ATOM   3475  C  CB    . SER A 1 1972 ? 151.173 158.392 151.270 1.00 6.62   ? 1972 SER A CB    1 
ATOM   3476  O  OG    . SER A 1 1972 ? 150.651 157.335 152.054 1.00 9.11   ? 1972 SER A OG    1 
ATOM   3477  N  N     . GLN A 1 1973 ? 147.952 158.187 151.355 1.00 12.19  ? 1973 GLN A N     1 
ATOM   3478  C  CA    . GLN A 1 1973 ? 146.763 157.382 151.092 1.00 11.23  ? 1973 GLN A CA    1 
ATOM   3479  C  C     . GLN A 1 1973 ? 145.822 158.081 150.115 1.00 9.91   ? 1973 GLN A C     1 
ATOM   3480  O  O     . GLN A 1 1973 ? 145.297 157.448 149.190 1.00 10.42  ? 1973 GLN A O     1 
ATOM   3481  C  CB    . GLN A 1 1973 ? 146.051 157.062 152.406 1.00 12.83  ? 1973 GLN A CB    1 
ATOM   3482  C  CG    . GLN A 1 1973 ? 144.960 156.009 152.284 1.00 21.51  ? 1973 GLN A CG    1 
ATOM   3483  C  CD    . GLN A 1 1973 ? 144.351 155.643 153.621 1.00 24.85  ? 1973 GLN A CD    1 
ATOM   3484  O  OE1   . GLN A 1 1973 ? 144.704 156.211 154.653 1.00 30.43  ? 1973 GLN A OE1   1 
ATOM   3485  N  NE2   . GLN A 1 1973 ? 143.428 154.690 153.609 1.00 22.71  ? 1973 GLN A NE2   1 
ATOM   3486  N  N     . GLN A 1 1974 ? 145.607 159.385 150.297 1.00 11.92  ? 1974 GLN A N     1 
ATOM   3487  C  CA    . GLN A 1 1974 ? 144.771 160.136 149.366 1.00 11.36  ? 1974 GLN A CA    1 
ATOM   3488  C  C     . GLN A 1 1974 ? 145.396 160.181 147.978 1.00 10.07  ? 1974 GLN A C     1 
ATOM   3489  O  O     . GLN A 1 1974 ? 144.693 160.053 146.967 1.00 13.79  ? 1974 GLN A O     1 
ATOM   3490  C  CB    . GLN A 1 1974 ? 144.537 161.552 149.890 1.00 10.66  ? 1974 GLN A CB    1 
ATOM   3491  C  CG    . GLN A 1 1974 ? 144.145 161.620 151.352 1.00 11.45  ? 1974 GLN A CG    1 
ATOM   3492  C  CD    . GLN A 1 1974 ? 143.994 163.043 151.848 1.00 18.58  ? 1974 GLN A CD    1 
ATOM   3493  O  OE1   . GLN A 1 1974 ? 142.940 163.428 152.351 1.00 21.59  ? 1974 GLN A OE1   1 
ATOM   3494  N  NE2   . GLN A 1 1974 ? 145.050 163.833 151.709 1.00 16.85  ? 1974 GLN A NE2   1 
ATOM   3495  N  N     . VAL A 1 1975 ? 146.716 160.365 147.910 1.00 8.55   ? 1975 VAL A N     1 
ATOM   3496  C  CA    . VAL A 1 1975 ? 147.393 160.386 146.616 1.00 7.86   ? 1975 VAL A CA    1 
ATOM   3497  C  C     . VAL A 1 1975 ? 147.241 159.042 145.915 1.00 9.27   ? 1975 VAL A C     1 
ATOM   3498  O  O     . VAL A 1 1975 ? 146.984 158.979 144.706 1.00 11.26  ? 1975 VAL A O     1 
ATOM   3499  C  CB    . VAL A 1 1975 ? 148.874 160.773 146.788 1.00 5.73   ? 1975 VAL A CB    1 
ATOM   3500  C  CG1   . VAL A 1 1975 ? 149.600 160.696 145.459 1.00 5.49   ? 1975 VAL A CG1   1 
ATOM   3501  C  CG2   . VAL A 1 1975 ? 148.987 162.170 147.368 1.00 6.46   ? 1975 VAL A CG2   1 
ATOM   3502  N  N     . GLN A 1 1976 ? 147.392 157.947 146.664 1.00 8.49   ? 1976 GLN A N     1 
ATOM   3503  C  CA    . GLN A 1 1976 ? 147.229 156.617 146.090 1.00 9.97   ? 1976 GLN A CA    1 
ATOM   3504  C  C     . GLN A 1 1976 ? 145.807 156.400 145.592 1.00 12.66  ? 1976 GLN A C     1 
ATOM   3505  O  O     . GLN A 1 1976 ? 145.600 155.828 144.515 1.00 16.36  ? 1976 GLN A O     1 
ATOM   3506  C  CB    . GLN A 1 1976 ? 147.607 155.558 147.125 1.00 12.70  ? 1976 GLN A CB    1 
ATOM   3507  C  CG    . GLN A 1 1976 ? 147.149 154.151 146.789 1.00 15.21  ? 1976 GLN A CG    1 
ATOM   3508  C  CD    . GLN A 1 1976 ? 148.115 153.097 147.282 1.00 23.22  ? 1976 GLN A CD    1 
ATOM   3509  O  OE1   . GLN A 1 1976 ? 148.986 153.375 148.104 1.00 25.46  ? 1976 GLN A OE1   1 
ATOM   3510  N  NE2   . GLN A 1 1976 ? 147.965 151.877 146.783 1.00 37.92  ? 1976 GLN A NE2   1 
ATOM   3511  N  N     . CYS A 1 1977 ? 144.811 156.850 146.360 1.00 13.40  ? 1977 CYS A N     1 
ATOM   3512  C  CA    . CYS A 1 1977 ? 143.425 156.707 145.922 1.00 13.21  ? 1977 CYS A CA    1 
ATOM   3513  C  C     . CYS A 1 1977 ? 143.166 157.487 144.638 1.00 13.84  ? 1977 CYS A C     1 
ATOM   3514  O  O     . CYS A 1 1977 ? 142.523 156.978 143.709 1.00 16.32  ? 1977 CYS A O     1 
ATOM   3515  C  CB    . CYS A 1 1977 ? 142.475 157.166 147.028 1.00 13.00  ? 1977 CYS A CB    1 
ATOM   3516  S  SG    . CYS A 1 1977 ? 142.280 155.987 148.381 1.00 52.37  ? 1977 CYS A SG    1 
ATOM   3517  N  N     . ILE A 1 1978 ? 143.669 158.721 144.562 1.00 12.30  ? 1978 ILE A N     1 
ATOM   3518  C  CA    . ILE A 1 1978 ? 143.460 159.533 143.365 1.00 14.61  ? 1978 ILE A CA    1 
ATOM   3519  C  C     . ILE A 1 1978 ? 144.146 158.899 142.162 1.00 13.13  ? 1978 ILE A C     1 
ATOM   3520  O  O     . ILE A 1 1978 ? 143.584 158.853 141.061 1.00 14.88  ? 1978 ILE A O     1 
ATOM   3521  C  CB    . ILE A 1 1978 ? 143.944 160.975 143.600 1.00 12.99  ? 1978 ILE A CB    1 
ATOM   3522  C  CG1   . ILE A 1 1978 ? 143.100 161.654 144.678 1.00 12.00  ? 1978 ILE A CG1   1 
ATOM   3523  C  CG2   . ILE A 1 1978 ? 143.884 161.772 142.310 1.00 11.82  ? 1978 ILE A CG2   1 
ATOM   3524  C  CD1   . ILE A 1 1978 ? 143.675 162.960 145.164 1.00 10.12  ? 1978 ILE A CD1   1 
ATOM   3525  N  N     . GLN A 1 1979 ? 145.371 158.404 142.349 1.00 14.77  ? 1979 GLN A N     1 
ATOM   3526  C  CA    . GLN A 1 1979 ? 146.090 157.784 141.241 1.00 12.36  ? 1979 GLN A CA    1 
ATOM   3527  C  C     . GLN A 1 1979 ? 145.411 156.497 140.786 1.00 18.03  ? 1979 GLN A C     1 
ATOM   3528  O  O     . GLN A 1 1979 ? 145.386 156.196 139.588 1.00 19.18  ? 1979 GLN A O     1 
ATOM   3529  C  CB    . GLN A 1 1979 ? 147.541 157.522 141.637 1.00 14.25  ? 1979 GLN A CB    1 
ATOM   3530  C  CG    . GLN A 1 1979 ? 148.387 158.779 141.709 1.00 9.60   ? 1979 GLN A CG    1 
ATOM   3531  C  CD    . GLN A 1 1979 ? 149.823 158.493 142.081 1.00 9.56   ? 1979 GLN A CD    1 
ATOM   3532  O  OE1   . GLN A 1 1979 ? 150.229 157.337 142.187 1.00 15.00  ? 1979 GLN A OE1   1 
ATOM   3533  N  NE2   . GLN A 1 1979 ? 150.605 159.547 142.277 1.00 9.87   ? 1979 GLN A NE2   1 
ATOM   3534  N  N     . GLU A 1 1980 ? 144.860 155.722 141.723 1.00 21.82  ? 1980 GLU A N     1 
ATOM   3535  C  CA    . GLU A 1 1980 ? 144.117 154.524 141.346 1.00 18.72  ? 1980 GLU A CA    1 
ATOM   3536  C  C     . GLU A 1 1980 ? 142.867 154.884 140.553 1.00 19.90  ? 1980 GLU A C     1 
ATOM   3537  O  O     . GLU A 1 1980 ? 142.527 154.213 139.570 1.00 25.20  ? 1980 GLU A O     1 
ATOM   3538  C  CB    . GLU A 1 1980 ? 143.753 153.720 142.592 1.00 19.62  ? 1980 GLU A CB    1 
ATOM   3539  C  CG    . GLU A 1 1980 ? 143.012 152.424 142.308 1.00 45.13  ? 1980 GLU A CG    1 
ATOM   3540  C  CD    . GLU A 1 1980 ? 143.858 151.419 141.545 1.00 60.34  ? 1980 GLU A CD    1 
ATOM   3541  O  OE1   . GLU A 1 1980 ? 145.101 151.480 141.649 1.00 48.60  ? 1980 GLU A OE1   1 
ATOM   3542  O  OE2   . GLU A 1 1980 ? 143.277 150.567 140.840 1.00 62.60  ? 1980 GLU A OE2   1 
ATOM   3543  N  N     . ALA A 1 1981 ? 142.170 155.946 140.966 1.00 21.77  ? 1981 ALA A N     1 
ATOM   3544  C  CA    . ALA A 1 1981 ? 141.017 156.411 140.201 1.00 24.79  ? 1981 ALA A CA    1 
ATOM   3545  C  C     . ALA A 1 1981 ? 141.425 156.845 138.797 1.00 22.55  ? 1981 ALA A C     1 
ATOM   3546  O  O     . ALA A 1 1981 ? 140.722 156.561 137.821 1.00 33.02  ? 1981 ALA A O     1 
ATOM   3547  C  CB    . ALA A 1 1981 ? 140.325 157.556 140.938 1.00 26.16  ? 1981 ALA A CB    1 
ATOM   3548  N  N     . LEU A 1 1982 ? 142.559 157.538 138.677 1.00 19.73  ? 1982 LEU A N     1 
ATOM   3549  C  CA    . LEU A 1 1982 ? 143.039 157.953 137.361 1.00 18.06  ? 1982 LEU A CA    1 
ATOM   3550  C  C     . LEU A 1 1982 ? 143.387 156.748 136.494 1.00 24.58  ? 1982 LEU A C     1 
ATOM   3551  O  O     . LEU A 1 1982 ? 143.084 156.725 135.294 1.00 28.55  ? 1982 LEU A O     1 
ATOM   3552  C  CB    . LEU A 1 1982 ? 144.251 158.870 137.510 1.00 13.98  ? 1982 LEU A CB    1 
ATOM   3553  C  CG    . LEU A 1 1982 ? 143.981 160.284 138.023 1.00 10.94  ? 1982 LEU A CG    1 
ATOM   3554  C  CD1   . LEU A 1 1982 ? 145.283 161.049 138.159 1.00 12.33  ? 1982 LEU A CD1   1 
ATOM   3555  C  CD2   . LEU A 1 1982 ? 143.025 161.009 137.098 1.00 12.24  ? 1982 LEU A CD2   1 
ATOM   3556  N  N     . ARG A 1 1983 ? 144.032 155.741 137.086 1.00 27.37  ? 1983 ARG A N     1 
ATOM   3557  C  CA    . ARG A 1 1983 ? 144.361 154.528 136.347 1.00 25.31  ? 1983 ARG A CA    1 
ATOM   3558  C  C     . ARG A 1 1983 ? 143.101 153.827 135.859 1.00 36.36  ? 1983 ARG A C     1 
ATOM   3559  O  O     . ARG A 1 1983 ? 143.048 153.350 134.720 1.00 45.45  ? 1983 ARG A O     1 
ATOM   3560  C  CB    . ARG A 1 1983 ? 145.191 153.591 137.223 1.00 19.32  ? 1983 ARG A CB    1 
ATOM   3561  C  CG    . ARG A 1 1983 ? 146.683 153.847 137.164 1.00 21.48  ? 1983 ARG A CG    1 
ATOM   3562  C  CD    . ARG A 1 1983 ? 147.327 153.616 138.517 1.00 26.22  ? 1983 ARG A CD    1 
ATOM   3563  N  NE    . ARG A 1 1983 ? 148.657 154.207 138.594 1.00 28.93  ? 1983 ARG A NE    1 
ATOM   3564  C  CZ    . ARG A 1 1983 ? 149.360 154.323 139.712 1.00 31.80  ? 1983 ARG A CZ    1 
ATOM   3565  N  NH1   . ARG A 1 1983 ? 148.885 153.903 140.873 1.00 27.92  ? 1983 ARG A NH1   1 
ATOM   3566  N  NH2   . ARG A 1 1983 ? 150.568 154.878 139.664 1.00 28.90  ? 1983 ARG A NH2   1 
ATOM   3567  N  N     . GLU A 1 1984 ? 142.075 153.752 136.710 1.00 38.68  ? 1984 GLU A N     1 
ATOM   3568  C  CA    . GLU A 1 1984 ? 140.807 153.175 136.282 1.00 44.93  ? 1984 GLU A CA    1 
ATOM   3569  C  C     . GLU A 1 1984 ? 140.148 153.998 135.181 1.00 46.19  ? 1984 GLU A C     1 
ATOM   3570  O  O     . GLU A 1 1984 ? 139.526 153.424 134.282 1.00 55.31  ? 1984 GLU A O     1 
ATOM   3571  C  CB    . GLU A 1 1984 ? 139.861 153.034 137.476 1.00 48.19  ? 1984 GLU A CB    1 
ATOM   3572  C  CG    . GLU A 1 1984 ? 138.538 152.365 137.143 1.00 64.63  ? 1984 GLU A CG    1 
ATOM   3573  C  CD    . GLU A 1 1984 ? 137.648 152.194 138.357 1.00 75.75  ? 1984 GLU A CD    1 
ATOM   3574  O  OE1   . GLU A 1 1984 ? 138.055 152.618 139.459 1.00 78.75  ? 1984 GLU A OE1   1 
ATOM   3575  O  OE2   . GLU A 1 1984 ? 136.542 151.632 138.210 1.00 68.33  ? 1984 GLU A OE2   1 
ATOM   3576  N  N     . HIS A 1 1985 ? 140.273 155.326 135.235 1.00 47.42  ? 1985 HIS A N     1 
ATOM   3577  C  CA    . HIS A 1 1985 ? 139.763 156.164 134.154 1.00 48.14  ? 1985 HIS A CA    1 
ATOM   3578  C  C     . HIS A 1 1985 ? 140.470 155.864 132.839 1.00 51.92  ? 1985 HIS A C     1 
ATOM   3579  O  O     . HIS A 1 1985 ? 139.828 155.786 131.786 1.00 58.71  ? 1985 HIS A O     1 
ATOM   3580  C  CB    . HIS A 1 1985 ? 139.925 157.642 134.509 1.00 48.60  ? 1985 HIS A CB    1 
ATOM   3581  C  CG    . HIS A 1 1985 ? 139.304 158.572 133.514 1.00 54.53  ? 1985 HIS A CG    1 
ATOM   3582  N  ND1   . HIS A 1 1985 ? 139.962 158.992 132.378 1.00 57.52  ? 1985 HIS A ND1   1 
ATOM   3583  C  CD2   . HIS A 1 1985 ? 138.095 159.182 133.495 1.00 51.75  ? 1985 HIS A CD2   1 
ATOM   3584  C  CE1   . HIS A 1 1985 ? 139.177 159.804 131.693 1.00 56.57  ? 1985 HIS A CE1   1 
ATOM   3585  N  NE2   . HIS A 1 1985 ? 138.039 159.938 132.350 1.00 50.33  ? 1985 HIS A NE2   1 
ATOM   3586  N  N     . SER A 1 1986 ? 141.793 155.693 132.881 1.00 60.29  ? 1986 SER A N     1 
ATOM   3587  C  CA    . SER A 1 1986 ? 142.577 155.495 131.667 1.00 51.87  ? 1986 SER A CA    1 
ATOM   3588  C  C     . SER A 1 1986 ? 142.293 154.167 130.977 1.00 60.15  ? 1986 SER A C     1 
ATOM   3589  O  O     . SER A 1 1986 ? 142.706 153.991 129.826 1.00 66.64  ? 1986 SER A O     1 
ATOM   3590  C  CB    . SER A 1 1986 ? 144.069 155.596 131.988 1.00 37.67  ? 1986 SER A CB    1 
ATOM   3591  O  OG    . SER A 1 1986 ? 144.580 154.352 132.434 1.00 41.58  ? 1986 SER A OG    1 
ATOM   3592  N  N     . ASN A 1 1987 ? 141.614 153.239 131.638 1.00 66.78  ? 1987 ASN A N     1 
ATOM   3593  C  CA    . ASN A 1 1987 ? 141.329 151.946 131.027 1.00 76.28  ? 1987 ASN A CA    1 
ATOM   3594  C  C     . ASN A 1 1987 ? 140.362 152.118 129.860 1.00 88.39  ? 1987 ASN A C     1 
ATOM   3595  O  O     . ASN A 1 1987 ? 139.361 152.832 129.991 1.00 90.42  ? 1987 ASN A O     1 
ATOM   3596  C  CB    . ASN A 1 1987 ? 140.745 150.986 132.059 1.00 71.51  ? 1987 ASN A CB    1 
ATOM   3597  C  CG    . ASN A 1 1987 ? 141.736 150.630 133.147 1.00 67.24  ? 1987 ASN A CG    1 
ATOM   3598  O  OD1   . ASN A 1 1987 ? 141.395 150.601 134.329 1.00 64.51  ? 1987 ASN A OD1   1 
ATOM   3599  N  ND2   . ASN A 1 1987 ? 142.975 150.359 132.754 1.00 70.10  ? 1987 ASN A ND2   1 
ATOM   3600  N  N     . PRO A 1 1988 ? 140.625 151.494 128.707 1.00 91.73  ? 1988 PRO A N     1 
ATOM   3601  C  CA    . PRO A 1 1988 ? 139.705 151.640 127.567 1.00 95.49  ? 1988 PRO A CA    1 
ATOM   3602  C  C     . PRO A 1 1988 ? 138.333 151.034 127.803 1.00 98.68  ? 1988 PRO A C     1 
ATOM   3603  O  O     . PRO A 1 1988 ? 137.383 151.411 127.106 1.00 95.25  ? 1988 PRO A O     1 
ATOM   3604  C  CB    . PRO A 1 1988 ? 140.442 150.923 126.428 1.00 92.17  ? 1988 PRO A CB    1 
ATOM   3605  C  CG    . PRO A 1 1988 ? 141.335 149.947 127.117 1.00 87.49  ? 1988 PRO A CG    1 
ATOM   3606  C  CD    . PRO A 1 1988 ? 141.758 150.605 128.399 1.00 83.94  ? 1988 PRO A CD    1 
ATOM   3607  N  N     . ASN A 1 1989 ? 138.199 150.107 128.755 1.00 98.67  ? 1989 ASN A N     1 
ATOM   3608  C  CA    . ASN A 1 1989 ? 136.907 149.471 128.993 1.00 94.95  ? 1989 ASN A CA    1 
ATOM   3609  C  C     . ASN A 1 1989 ? 135.876 150.475 129.494 1.00 97.52  ? 1989 ASN A C     1 
ATOM   3610  O  O     . ASN A 1 1989 ? 134.677 150.328 129.230 1.00 95.53  ? 1989 ASN A O     1 
ATOM   3611  C  CB    . ASN A 1 1989 ? 137.067 148.320 129.986 1.00 89.42  ? 1989 ASN A CB    1 
ATOM   3612  C  CG    . ASN A 1 1989 ? 138.009 148.659 131.123 1.00 91.39  ? 1989 ASN A CG    1 
ATOM   3613  O  OD1   . ASN A 1 1989 ? 137.757 149.581 131.899 1.00 93.62  ? 1989 ASN A OD1   1 
ATOM   3614  N  ND2   . ASN A 1 1989 ? 139.104 147.914 131.227 1.00 83.69  ? 1989 ASN A ND2   1 
ATOM   3615  N  N     . TYR A 1 1990 ? 136.321 151.496 130.221 1.00 99.04  ? 1990 TYR A N     1 
ATOM   3616  C  CA    . TYR A 1 1990 ? 135.412 152.531 130.692 1.00 98.99  ? 1990 TYR A CA    1 
ATOM   3617  C  C     . TYR A 1 1990 ? 134.877 153.356 129.527 1.00 99.88  ? 1990 TYR A C     1 
ATOM   3618  O  O     . TYR A 1 1990 ? 135.590 153.635 128.559 1.00 98.84  ? 1990 TYR A O     1 
ATOM   3619  C  CB    . TYR A 1 1990 ? 136.115 153.445 131.696 1.00 95.24  ? 1990 TYR A CB    1 
ATOM   3620  C  CG    . TYR A 1 1990 ? 135.331 154.697 132.023 1.00 92.64  ? 1990 TYR A CG    1 
ATOM   3621  C  CD1   . TYR A 1 1990 ? 134.241 154.654 132.881 1.00 94.34  ? 1990 TYR A CD1   1 
ATOM   3622  C  CD2   . TYR A 1 1990 ? 135.674 155.920 131.460 1.00 86.99  ? 1990 TYR A CD2   1 
ATOM   3623  C  CE1   . TYR A 1 1990 ? 133.518 155.796 133.175 1.00 91.94  ? 1990 TYR A CE1   1 
ATOM   3624  C  CE2   . TYR A 1 1990 ? 134.957 157.065 131.746 1.00 92.04  ? 1990 TYR A CE2   1 
ATOM   3625  C  CZ    . TYR A 1 1990 ? 133.879 156.998 132.603 1.00 93.73  ? 1990 TYR A CZ    1 
ATOM   3626  O  OH    . TYR A 1 1990 ? 133.166 158.138 132.893 1.00 87.62  ? 1990 TYR A OH    1 
ATOM   3627  N  N     . ASP A 1 1991 ? 133.609 153.746 129.628 1.00 103.83 ? 1991 ASP A N     1 
ATOM   3628  C  CA    . ASP A 1 1991 ? 132.987 154.668 128.692 1.00 104.12 ? 1991 ASP A CA    1 
ATOM   3629  C  C     . ASP A 1 1991 ? 132.415 155.851 129.461 1.00 101.80 ? 1991 ASP A C     1 
ATOM   3630  O  O     . ASP A 1 1991 ? 131.882 155.693 130.564 1.00 101.07 ? 1991 ASP A O     1 
ATOM   3631  C  CB    . ASP A 1 1991 ? 131.879 153.987 127.878 1.00 106.60 ? 1991 ASP A CB    1 
ATOM   3632  C  CG    . ASP A 1 1991 ? 130.831 153.330 128.753 1.00 107.71 ? 1991 ASP A CG    1 
ATOM   3633  O  OD1   . ASP A 1 1991 ? 131.204 152.502 129.611 1.00 110.42 ? 1991 ASP A OD1   1 
ATOM   3634  O  OD2   . ASP A 1 1991 ? 129.634 153.645 128.586 1.00 99.95  ? 1991 ASP A OD2   1 
ATOM   3635  N  N     . LYS A 1 1992 ? 132.527 157.042 128.867 1.00 101.63 ? 1992 LYS A N     1 
ATOM   3636  C  CA    . LYS A 1 1992 ? 132.093 158.258 129.547 1.00 104.09 ? 1992 LYS A CA    1 
ATOM   3637  C  C     . LYS A 1 1992 ? 130.603 158.253 129.863 1.00 106.31 ? 1992 LYS A C     1 
ATOM   3638  O  O     . LYS A 1 1992 ? 130.166 159.006 130.741 1.00 106.48 ? 1992 LYS A O     1 
ATOM   3639  C  CB    . LYS A 1 1992 ? 132.441 159.487 128.705 1.00 100.28 ? 1992 LYS A CB    1 
ATOM   3640  C  CG    . LYS A 1 1992 ? 133.932 159.684 128.478 1.00 98.14  ? 1992 LYS A CG    1 
ATOM   3641  C  CD    . LYS A 1 1992 ? 134.215 161.007 127.785 1.00 98.07  ? 1992 LYS A CD    1 
ATOM   3642  C  CE    . LYS A 1 1992 ? 133.432 161.134 126.489 1.00 90.80  ? 1992 LYS A CE    1 
ATOM   3643  N  NZ    . LYS A 1 1992 ? 133.646 162.457 125.838 1.00 79.09  ? 1992 LYS A NZ    1 
ATOM   3644  N  N     . THR A 1 1993 ? 129.815 157.429 129.173 1.00 106.22 ? 1993 THR A N     1 
ATOM   3645  C  CA    . THR A 1 1993 ? 128.386 157.340 129.442 1.00 105.17 ? 1993 THR A CA    1 
ATOM   3646  C  C     . THR A 1 1993 ? 128.061 156.494 130.666 1.00 106.70 ? 1993 THR A C     1 
ATOM   3647  O  O     . THR A 1 1993 ? 126.922 156.541 131.144 1.00 102.32 ? 1993 THR A O     1 
ATOM   3648  C  CB    . THR A 1 1993 ? 127.656 156.771 128.224 1.00 103.87 ? 1993 THR A CB    1 
ATOM   3649  O  OG1   . THR A 1 1993 ? 128.182 155.475 127.911 1.00 105.36 ? 1993 THR A OG1   1 
ATOM   3650  C  CG2   . THR A 1 1993 ? 127.834 157.687 127.023 1.00 88.66  ? 1993 THR A CG2   1 
ATOM   3651  N  N     . SER A 1 1994 ? 129.020 155.729 131.182 1.00 106.43 ? 1994 SER A N     1 
ATOM   3652  C  CA    . SER A 1 1994 ? 128.792 154.891 132.351 1.00 99.82  ? 1994 SER A CA    1 
ATOM   3653  C  C     . SER A 1 1994 ? 128.969 155.725 133.620 1.00 100.48 ? 1994 SER A C     1 
ATOM   3654  O  O     . SER A 1 1994 ? 129.030 156.958 133.581 1.00 96.62  ? 1994 SER A O     1 
ATOM   3655  C  CB    . SER A 1 1994 ? 129.717 153.677 132.322 1.00 95.55  ? 1994 SER A CB    1 
ATOM   3656  O  OG    . SER A 1 1994 ? 131.079 154.064 132.345 1.00 95.93  ? 1994 SER A OG    1 
ATOM   3657  N  N     . ALA A 1 1995 ? 129.042 155.054 134.765 1.00 99.91  ? 1995 ALA A N     1 
ATOM   3658  C  CA    . ALA A 1 1995 ? 129.179 155.758 136.031 1.00 92.75  ? 1995 ALA A CA    1 
ATOM   3659  C  C     . ALA A 1 1995 ? 130.508 156.510 136.076 1.00 89.50  ? 1995 ALA A C     1 
ATOM   3660  O  O     . ALA A 1 1995 ? 131.556 155.939 135.751 1.00 88.55  ? 1995 ALA A O     1 
ATOM   3661  C  CB    . ALA A 1 1995 ? 129.092 154.778 137.202 1.00 79.51  ? 1995 ALA A CB    1 
ATOM   3662  N  N     . PRO A 1 1996 ? 130.501 157.785 136.460 1.00 84.84  ? 1996 PRO A N     1 
ATOM   3663  C  CA    . PRO A 1 1996 ? 131.757 158.537 136.542 1.00 78.58  ? 1996 PRO A CA    1 
ATOM   3664  C  C     . PRO A 1 1996 ? 132.684 157.962 137.600 1.00 70.86  ? 1996 PRO A C     1 
ATOM   3665  O  O     . PRO A 1 1996 ? 132.247 157.388 138.600 1.00 68.32  ? 1996 PRO A O     1 
ATOM   3666  C  CB    . PRO A 1 1996 ? 131.299 159.951 136.919 1.00 71.40  ? 1996 PRO A CB    1 
ATOM   3667  C  CG    . PRO A 1 1996 ? 129.888 160.029 136.435 1.00 78.33  ? 1996 PRO A CG    1 
ATOM   3668  C  CD    . PRO A 1 1996 ? 129.325 158.652 136.648 1.00 80.94  ? 1996 PRO A CD    1 
ATOM   3669  N  N     . ILE A 1 1997 ? 133.983 158.121 137.365 1.00 60.65  ? 1997 ILE A N     1 
ATOM   3670  C  CA    . ILE A 1 1997 ? 134.991 157.640 138.303 1.00 53.82  ? 1997 ILE A CA    1 
ATOM   3671  C  C     . ILE A 1 1997 ? 134.999 158.550 139.522 1.00 49.50  ? 1997 ILE A C     1 
ATOM   3672  O  O     . ILE A 1 1997 ? 135.119 159.773 139.398 1.00 42.32  ? 1997 ILE A O     1 
ATOM   3673  C  CB    . ILE A 1 1997 ? 136.382 157.576 137.656 1.00 49.03  ? 1997 ILE A CB    1 
ATOM   3674  C  CG1   . ILE A 1 1997 ? 136.406 156.581 136.495 1.00 55.17  ? 1997 ILE A CG1   1 
ATOM   3675  C  CG2   . ILE A 1 1997 ? 137.432 157.205 138.690 1.00 48.48  ? 1997 ILE A CG2   1 
ATOM   3676  C  CD1   . ILE A 1 1997 ? 136.035 157.173 135.172 1.00 56.03  ? 1997 ILE A CD1   1 
ATOM   3677  N  N     . THR A 1 1998 ? 134.868 157.953 140.703 1.00 45.38  ? 1998 THR A N     1 
ATOM   3678  C  CA    . THR A 1 1998 ? 134.921 158.678 141.961 1.00 40.97  ? 1998 THR A CA    1 
ATOM   3679  C  C     . THR A 1 1998 ? 135.966 158.033 142.858 1.00 37.26  ? 1998 THR A C     1 
ATOM   3680  O  O     . THR A 1 1998 ? 136.273 156.845 142.739 1.00 42.23  ? 1998 THR A O     1 
ATOM   3681  C  CB    . THR A 1 1998 ? 133.560 158.700 142.678 1.00 44.42  ? 1998 THR A CB    1 
ATOM   3682  O  OG1   . THR A 1 1998 ? 133.359 157.461 143.369 1.00 48.07  ? 1998 THR A OG1   1 
ATOM   3683  C  CG2   . THR A 1 1998 ? 132.425 158.914 141.687 1.00 41.87  ? 1998 THR A CG2   1 
ATOM   3684  N  N     . CYS A 1 1999 ? 136.519 158.841 143.755 1.00 33.30  ? 1999 CYS A N     1 
ATOM   3685  C  CA    . CYS A 1 1999 ? 137.487 158.373 144.733 1.00 37.04  ? 1999 CYS A CA    1 
ATOM   3686  C  C     . CYS A 1 1999 ? 137.028 158.773 146.126 1.00 38.60  ? 1999 CYS A C     1 
ATOM   3687  O  O     . CYS A 1 1999 ? 136.295 159.751 146.301 1.00 35.99  ? 1999 CYS A O     1 
ATOM   3688  C  CB    . CYS A 1 1999 ? 138.891 158.933 144.457 1.00 35.55  ? 1999 CYS A CB    1 
ATOM   3689  S  SG    . CYS A 1 1999 ? 139.129 160.653 144.951 1.00 51.49  ? 1999 CYS A SG    1 
ATOM   3690  N  N     . GLU A 1 2000 ? 137.454 157.995 147.116 1.00 34.66  ? 2000 GLU A N     1 
ATOM   3691  C  CA    . GLU A 1 2000 ? 137.116 158.251 148.513 1.00 31.92  ? 2000 GLU A CA    1 
ATOM   3692  C  C     . GLU A 1 2000 ? 138.079 159.305 149.043 1.00 34.76  ? 2000 GLU A C     1 
ATOM   3693  O  O     . GLU A 1 2000 ? 139.234 159.011 149.357 1.00 38.91  ? 2000 GLU A O     1 
ATOM   3694  C  CB    . GLU A 1 2000 ? 137.172 156.959 149.322 1.00 39.73  ? 2000 GLU A CB    1 
ATOM   3695  C  CG    . GLU A 1 2000 ? 136.624 157.063 150.739 1.00 48.24  ? 2000 GLU A CG    1 
ATOM   3696  C  CD    . GLU A 1 2000 ? 137.654 157.565 151.733 1.00 53.81  ? 2000 GLU A CD    1 
ATOM   3697  O  OE1   . GLU A 1 2000 ? 138.859 157.321 151.518 1.00 55.47  ? 2000 GLU A OE1   1 
ATOM   3698  O  OE2   . GLU A 1 2000 ? 137.260 158.199 152.734 1.00 49.94  ? 2000 GLU A OE2   1 
ATOM   3699  N  N     . LEU A 1 2001 ? 137.603 160.545 149.128 1.00 32.60  ? 2001 LEU A N     1 
ATOM   3700  C  CA    . LEU A 1 2001 ? 138.378 161.660 149.656 1.00 27.51  ? 2001 LEU A CA    1 
ATOM   3701  C  C     . LEU A 1 2001 ? 137.610 162.278 150.813 1.00 27.78  ? 2001 LEU A C     1 
ATOM   3702  O  O     . LEU A 1 2001 ? 136.506 162.798 150.618 1.00 25.44  ? 2001 LEU A O     1 
ATOM   3703  C  CB    . LEU A 1 2001 ? 138.651 162.704 148.573 1.00 23.74  ? 2001 LEU A CB    1 
ATOM   3704  C  CG    . LEU A 1 2001 ? 140.017 162.645 147.889 1.00 20.29  ? 2001 LEU A CG    1 
ATOM   3705  C  CD1   . LEU A 1 2001 ? 140.090 163.665 146.766 1.00 13.05  ? 2001 LEU A CD1   1 
ATOM   3706  C  CD2   . LEU A 1 2001 ? 141.129 162.872 148.897 1.00 18.31  ? 2001 LEU A CD2   1 
ATOM   3707  N  N     . LEU A 1 2002 ? 138.199 162.226 152.008 1.00 29.06  ? 2002 LEU A N     1 
ATOM   3708  C  CA    . LEU A 1 2002 ? 137.596 162.786 153.218 1.00 32.11  ? 2002 LEU A CA    1 
ATOM   3709  C  C     . LEU A 1 2002 ? 136.205 162.201 153.464 1.00 34.66  ? 2002 LEU A C     1 
ATOM   3710  O  O     . LEU A 1 2002 ? 135.240 162.921 153.729 1.00 38.66  ? 2002 LEU A O     1 
ATOM   3711  C  CB    . LEU A 1 2002 ? 137.548 164.314 153.148 1.00 34.23  ? 2002 LEU A CB    1 
ATOM   3712  C  CG    . LEU A 1 2002 ? 138.898 165.032 153.196 1.00 23.04  ? 2002 LEU A CG    1 
ATOM   3713  C  CD1   . LEU A 1 2002 ? 138.705 166.507 153.480 1.00 26.30  ? 2002 LEU A CD1   1 
ATOM   3714  C  CD2   . LEU A 1 2002 ? 139.806 164.403 154.237 1.00 24.94  ? 2002 LEU A CD2   1 
ATOM   3715  N  N     . ASN A 1 2003 ? 136.113 160.872 153.364 1.00 34.85  ? 2003 ASN A N     1 
ATOM   3716  C  CA    . ASN A 1 2003 ? 134.873 160.130 153.604 1.00 36.99  ? 2003 ASN A CA    1 
ATOM   3717  C  C     . ASN A 1 2003 ? 133.757 160.560 152.657 1.00 35.82  ? 2003 ASN A C     1 
ATOM   3718  O  O     . ASN A 1 2003 ? 132.579 160.539 153.017 1.00 38.49  ? 2003 ASN A O     1 
ATOM   3719  C  CB    . ASN A 1 2003 ? 134.418 160.257 155.061 1.00 32.01  ? 2003 ASN A CB    1 
ATOM   3720  C  CG    . ASN A 1 2003 ? 135.451 159.739 156.039 1.00 36.96  ? 2003 ASN A CG    1 
ATOM   3721  O  OD1   . ASN A 1 2003 ? 136.285 158.904 155.693 1.00 35.96  ? 2003 ASN A OD1   1 
ATOM   3722  N  ND2   . ASN A 1 2003 ? 135.399 160.231 157.271 1.00 47.78  ? 2003 ASN A ND2   1 
ATOM   3723  N  N     . LYS A 1 2004 ? 134.119 160.955 151.441 1.00 35.41  ? 2004 LYS A N     1 
ATOM   3724  C  CA    . LYS A 1 2004 ? 133.151 161.384 150.445 1.00 32.83  ? 2004 LYS A CA    1 
ATOM   3725  C  C     . LYS A 1 2004 ? 133.588 160.875 149.080 1.00 34.00  ? 2004 LYS A C     1 
ATOM   3726  O  O     . LYS A 1 2004 ? 134.778 160.691 148.817 1.00 36.04  ? 2004 LYS A O     1 
ATOM   3727  C  CB    . LYS A 1 2004 ? 133.009 162.913 150.441 1.00 34.93  ? 2004 LYS A CB    1 
ATOM   3728  C  CG    . LYS A 1 2004 ? 131.991 163.462 149.464 1.00 42.13  ? 2004 LYS A CG    1 
ATOM   3729  C  CD    . LYS A 1 2004 ? 131.835 164.962 149.631 1.00 49.27  ? 2004 LYS A CD    1 
ATOM   3730  C  CE    . LYS A 1 2004 ? 133.043 165.707 149.085 1.00 50.83  ? 2004 LYS A CE    1 
ATOM   3731  N  NZ    . LYS A 1 2004 ? 132.850 167.185 149.136 1.00 59.03  ? 2004 LYS A NZ    1 
ATOM   3732  N  N     . GLN A 1 2005 ? 132.609 160.646 148.207 1.00 35.02  ? 2005 GLN A N     1 
ATOM   3733  C  CA    . GLN A 1 2005 ? 132.872 160.258 146.825 1.00 33.89  ? 2005 GLN A CA    1 
ATOM   3734  C  C     . GLN A 1 2005 ? 133.089 161.526 146.008 1.00 36.05  ? 2005 GLN A C     1 
ATOM   3735  O  O     . GLN A 1 2005 ? 132.178 162.349 145.872 1.00 37.74  ? 2005 GLN A O     1 
ATOM   3736  C  CB    . GLN A 1 2005 ? 131.721 159.430 146.263 1.00 32.25  ? 2005 GLN A CB    1 
ATOM   3737  C  CG    . GLN A 1 2005 ? 131.567 158.064 146.904 1.00 33.20  ? 2005 GLN A CG    1 
ATOM   3738  C  CD    . GLN A 1 2005 ? 132.826 157.226 146.799 1.00 37.14  ? 2005 GLN A CD    1 
ATOM   3739  O  OE1   . GLN A 1 2005 ? 133.317 156.957 145.704 1.00 43.91  ? 2005 GLN A OE1   1 
ATOM   3740  N  NE2   . GLN A 1 2005 ? 133.353 156.808 147.942 1.00 33.79  ? 2005 GLN A NE2   1 
ATOM   3741  N  N     . VAL A 1 2006 ? 134.294 161.684 145.467 1.00 33.43  ? 2006 VAL A N     1 
ATOM   3742  C  CA    . VAL A 1 2006 ? 134.692 162.885 144.745 1.00 26.29  ? 2006 VAL A CA    1 
ATOM   3743  C  C     . VAL A 1 2006 ? 135.040 162.492 143.317 1.00 28.32  ? 2006 VAL A C     1 
ATOM   3744  O  O     . VAL A 1 2006 ? 135.838 161.573 143.100 1.00 35.99  ? 2006 VAL A O     1 
ATOM   3745  C  CB    . VAL A 1 2006 ? 135.880 163.579 145.432 1.00 25.27  ? 2006 VAL A CB    1 
ATOM   3746  C  CG1   . VAL A 1 2006 ? 136.489 164.632 144.522 1.00 22.06  ? 2006 VAL A CG1   1 
ATOM   3747  C  CG2   . VAL A 1 2006 ? 135.446 164.186 146.754 1.00 25.46  ? 2006 VAL A CG2   1 
ATOM   3748  N  N     . LYS A 1 2007 ? 134.434 163.176 142.350 1.00 27.25  ? 2007 LYS A N     1 
ATOM   3749  C  CA    . LYS A 1 2007 ? 134.722 162.905 140.948 1.00 29.09  ? 2007 LYS A CA    1 
ATOM   3750  C  C     . LYS A 1 2007 ? 136.138 163.351 140.607 1.00 25.90  ? 2007 LYS A C     1 
ATOM   3751  O  O     . LYS A 1 2007 ? 136.564 164.446 140.986 1.00 21.41  ? 2007 LYS A O     1 
ATOM   3752  C  CB    . LYS A 1 2007 ? 133.710 163.615 140.051 1.00 24.23  ? 2007 LYS A CB    1 
ATOM   3753  C  CG    . LYS A 1 2007 ? 132.307 163.042 140.140 1.00 31.61  ? 2007 LYS A CG    1 
ATOM   3754  C  CD    . LYS A 1 2007 ? 131.315 163.864 139.338 1.00 34.24  ? 2007 LYS A CD    1 
ATOM   3755  C  CE    . LYS A 1 2007 ? 131.540 163.695 137.847 1.00 36.80  ? 2007 LYS A CE    1 
ATOM   3756  N  NZ    . LYS A 1 2007 ? 130.506 164.400 137.042 1.00 40.71  ? 2007 LYS A NZ    1 
ATOM   3757  N  N     . VAL A 1 2008 ? 136.867 162.505 139.886 1.00 24.23  ? 2008 VAL A N     1 
ATOM   3758  C  CA    . VAL A 1 2008 ? 138.257 162.766 139.528 1.00 17.81  ? 2008 VAL A CA    1 
ATOM   3759  C  C     . VAL A 1 2008 ? 138.322 163.022 138.031 1.00 17.47  ? 2008 VAL A C     1 
ATOM   3760  O  O     . VAL A 1 2008 ? 138.005 162.137 137.226 1.00 24.97  ? 2008 VAL A O     1 
ATOM   3761  C  CB    . VAL A 1 2008 ? 139.173 161.601 139.930 1.00 19.85  ? 2008 VAL A CB    1 
ATOM   3762  C  CG1   . VAL A 1 2008 ? 140.629 161.997 139.772 1.00 18.28  ? 2008 VAL A CG1   1 
ATOM   3763  C  CG2   . VAL A 1 2008 ? 138.883 161.170 141.355 1.00 22.12  ? 2008 VAL A CG2   1 
ATOM   3764  N  N     . SER A 1 2009 ? 138.730 164.229 137.659 1.00 17.45  ? 2009 SER A N     1 
ATOM   3765  C  CA    . SER A 1 2009 ? 138.887 164.558 136.251 1.00 16.06  ? 2009 SER A CA    1 
ATOM   3766  C  C     . SER A 1 2009 ? 140.174 163.940 135.710 1.00 16.98  ? 2009 SER A C     1 
ATOM   3767  O  O     . SER A 1 2009 ? 141.165 163.830 136.439 1.00 20.28  ? 2009 SER A O     1 
ATOM   3768  C  CB    . SER A 1 2009 ? 138.907 166.073 136.059 1.00 14.95  ? 2009 SER A CB    1 
ATOM   3769  O  OG    . SER A 1 2009 ? 139.184 166.421 134.715 1.00 17.94  ? 2009 SER A OG    1 
ATOM   3770  N  N     . PRO A 1 2010 ? 140.191 163.520 134.443 1.00 17.86  ? 2010 PRO A N     1 
ATOM   3771  C  CA    . PRO A 1 2010 ? 141.433 162.979 133.868 1.00 20.78  ? 2010 PRO A CA    1 
ATOM   3772  C  C     . PRO A 1 2010 ? 142.561 163.991 133.785 1.00 19.37  ? 2010 PRO A C     1 
ATOM   3773  O  O     . PRO A 1 2010 ? 143.730 163.590 133.734 1.00 17.63  ? 2010 PRO A O     1 
ATOM   3774  C  CB    . PRO A 1 2010 ? 141.000 162.512 132.473 1.00 21.98  ? 2010 PRO A CB    1 
ATOM   3775  C  CG    . PRO A 1 2010 ? 139.776 163.313 132.168 1.00 25.15  ? 2010 PRO A CG    1 
ATOM   3776  C  CD    . PRO A 1 2010 ? 139.079 163.499 133.479 1.00 21.46  ? 2010 PRO A CD    1 
ATOM   3777  N  N     . ASP A 1 2011 ? 142.255 165.286 133.771 1.00 16.30  ? 2011 ASP A N     1 
ATOM   3778  C  CA    . ASP A 1 2011 ? 143.272 166.316 133.613 1.00 11.42  ? 2011 ASP A CA    1 
ATOM   3779  C  C     . ASP A 1 2011 ? 143.973 166.667 134.917 1.00 12.84  ? 2011 ASP A C     1 
ATOM   3780  O  O     . ASP A 1 2011 ? 144.871 167.516 134.906 1.00 14.65  ? 2011 ASP A O     1 
ATOM   3781  C  CB    . ASP A 1 2011 ? 142.655 167.576 133.004 1.00 11.61  ? 2011 ASP A CB    1 
ATOM   3782  C  CG    . ASP A 1 2011 ? 142.313 167.406 131.537 1.00 26.03  ? 2011 ASP A CG    1 
ATOM   3783  O  OD1   . ASP A 1 2011 ? 142.208 166.249 131.080 1.00 27.91  ? 2011 ASP A OD1   1 
ATOM   3784  O  OD2   . ASP A 1 2011 ? 142.155 168.428 130.838 1.00 35.89  ? 2011 ASP A OD2   1 
ATOM   3785  N  N     . MET A 1 2012 ? 143.588 166.049 136.031 1.00 9.87   ? 2012 MET A N     1 
ATOM   3786  C  CA    . MET A 1 2012 ? 144.259 166.308 137.295 1.00 8.56   ? 2012 MET A CA    1 
ATOM   3787  C  C     . MET A 1 2012 ? 145.703 165.829 137.256 1.00 9.19   ? 2012 MET A C     1 
ATOM   3788  O  O     . MET A 1 2012 ? 146.027 164.815 136.632 1.00 7.85   ? 2012 MET A O     1 
ATOM   3789  C  CB    . MET A 1 2012 ? 143.529 165.616 138.445 1.00 10.24  ? 2012 MET A CB    1 
ATOM   3790  C  CG    . MET A 1 2012 ? 144.148 165.919 139.797 1.00 12.81  ? 2012 MET A CG    1 
ATOM   3791  S  SD    . MET A 1 2012 ? 143.281 165.202 141.188 1.00 49.26  ? 2012 MET A SD    1 
ATOM   3792  C  CE    . MET A 1 2012 ? 144.352 165.685 142.538 1.00 15.77  ? 2012 MET A CE    1 
ATOM   3793  N  N     . ALA A 1 2013 ? 146.573 166.570 137.936 1.00 6.79   ? 2013 ALA A N     1 
ATOM   3794  C  CA    . ALA A 1 2013 ? 147.947 166.153 138.152 1.00 4.25   ? 2013 ALA A CA    1 
ATOM   3795  C  C     . ALA A 1 2013 ? 148.400 166.669 139.507 1.00 4.65   ? 2013 ALA A C     1 
ATOM   3796  O  O     . ALA A 1 2013 ? 147.963 167.729 139.960 1.00 7.58   ? 2013 ALA A O     1 
ATOM   3797  C  CB    . ALA A 1 2013 ? 148.875 166.665 137.048 1.00 4.84   ? 2013 ALA A CB    1 
ATOM   3798  N  N     . ILE A 1 2014 ? 149.274 165.905 140.153 1.00 3.32   ? 2014 ILE A N     1 
ATOM   3799  C  CA    . ILE A 1 2014 ? 149.887 166.298 141.414 1.00 3.17   ? 2014 ILE A CA    1 
ATOM   3800  C  C     . ILE A 1 2014 ? 151.392 166.352 141.208 1.00 3.21   ? 2014 ILE A C     1 
ATOM   3801  O  O     . ILE A 1 2014 ? 151.999 165.372 140.763 1.00 2.93   ? 2014 ILE A O     1 
ATOM   3802  C  CB    . ILE A 1 2014 ? 149.524 165.331 142.557 1.00 3.31   ? 2014 ILE A CB    1 
ATOM   3803  C  CG1   . ILE A 1 2014 ? 148.007 165.190 142.676 1.00 4.13   ? 2014 ILE A CG1   1 
ATOM   3804  C  CG2   . ILE A 1 2014 ? 150.117 165.810 143.871 1.00 3.81   ? 2014 ILE A CG2   1 
ATOM   3805  C  CD1   . ILE A 1 2014 ? 147.570 164.057 143.572 1.00 6.93   ? 2014 ILE A CD1   1 
ATOM   3806  N  N     . PHE A 1 2015 ? 151.988 167.497 141.519 1.00 3.60   ? 2015 PHE A N     1 
ATOM   3807  C  CA    . PHE A 1 2015 ? 153.426 167.686 141.426 1.00 2.56   ? 2015 PHE A CA    1 
ATOM   3808  C  C     . PHE A 1 2015 ? 153.943 168.210 142.754 1.00 2.89   ? 2015 PHE A C     1 
ATOM   3809  O  O     . PHE A 1 2015 ? 153.307 169.058 143.385 1.00 4.72   ? 2015 PHE A O     1 
ATOM   3810  C  CB    . PHE A 1 2015 ? 153.795 168.657 140.301 1.00 3.52   ? 2015 PHE A CB    1 
ATOM   3811  C  CG    . PHE A 1 2015 ? 153.602 168.094 138.926 1.00 2.72   ? 2015 PHE A CG    1 
ATOM   3812  C  CD1   . PHE A 1 2015 ? 152.377 168.178 138.294 1.00 2.95   ? 2015 PHE A CD1   1 
ATOM   3813  C  CD2   . PHE A 1 2015 ? 154.649 167.484 138.262 1.00 2.13   ? 2015 PHE A CD2   1 
ATOM   3814  C  CE1   . PHE A 1 2015 ? 152.200 167.664 137.029 1.00 3.03   ? 2015 PHE A CE1   1 
ATOM   3815  C  CE2   . PHE A 1 2015 ? 154.476 166.969 136.998 1.00 3.22   ? 2015 PHE A CE2   1 
ATOM   3816  C  CZ    . PHE A 1 2015 ? 153.251 167.059 136.381 1.00 3.29   ? 2015 PHE A CZ    1 
ATOM   3817  N  N     . ILE A 1 2016 ? 155.095 167.699 143.179 1.00 3.22   ? 2016 ILE A N     1 
ATOM   3818  C  CA    . ILE A 1 2016 ? 155.721 168.104 144.430 1.00 4.56   ? 2016 ILE A CA    1 
ATOM   3819  C  C     . ILE A 1 2016 ? 157.161 168.505 144.131 1.00 5.64   ? 2016 ILE A C     1 
ATOM   3820  O  O     . ILE A 1 2016 ? 157.908 167.742 143.506 1.00 5.56   ? 2016 ILE A O     1 
ATOM   3821  C  CB    . ILE A 1 2016 ? 155.658 166.999 145.496 1.00 4.15   ? 2016 ILE A CB    1 
ATOM   3822  C  CG1   . ILE A 1 2016 ? 156.267 165.694 144.980 1.00 3.61   ? 2016 ILE A CG1   1 
ATOM   3823  C  CG2   . ILE A 1 2016 ? 154.217 166.755 145.909 1.00 3.37   ? 2016 ILE A CG2   1 
ATOM   3824  C  CD1   . ILE A 1 2016 ? 156.339 164.604 146.018 1.00 4.06   ? 2016 ILE A CD1   1 
ATOM   3825  N  N     . THR A 1 2017 ? 157.531 169.725 144.529 1.00 7.31   ? 2017 THR A N     1 
ATOM   3826  C  CA    . THR A 1 2017 ? 158.914 170.204 144.323 1.00 6.41   ? 2017 THR A CA    1 
ATOM   3827  C  C     . THR A 1 2017 ? 159.543 170.388 145.684 1.00 7.93   ? 2017 THR A C     1 
ATOM   3828  O  O     . THR A 1 2017 ? 159.021 171.214 146.464 1.00 13.02  ? 2017 THR A O     1 
ATOM   3829  C  CB    . THR A 1 2017 ? 158.903 171.499 143.512 1.00 9.15   ? 2017 THR A CB    1 
ATOM   3830  O  OG1   . THR A 1 2017 ? 158.203 172.448 144.310 1.00 13.62  ? 2017 THR A OG1   1 
ATOM   3831  C  CG2   . THR A 1 2017 ? 158.204 171.343 142.174 1.00 8.94   ? 2017 THR A CG2   1 
ATOM   3832  N  N     . MET A 1 2018 ? 160.613 169.646 145.980 1.00 7.42   ? 2018 MET A N     1 
ATOM   3833  C  CA    . MET A 1 2018 ? 161.209 169.706 147.340 1.00 8.86   ? 2018 MET A CA    1 
ATOM   3834  C  C     . MET A 1 2018 ? 162.733 169.873 147.246 1.00 9.05   ? 2018 MET A C     1 
ATOM   3835  O  O     . MET A 1 2018 ? 163.335 169.298 146.316 1.00 7.08   ? 2018 MET A O     1 
ATOM   3836  C  CB    . MET A 1 2018 ? 160.876 168.430 148.121 1.00 10.08  ? 2018 MET A CB    1 
ATOM   3837  C  CG    . MET A 1 2018 ? 161.159 167.152 147.357 1.00 13.38  ? 2018 MET A CG    1 
ATOM   3838  S  SD    . MET A 1 2018 ? 160.451 165.708 148.172 1.00 8.43   ? 2018 MET A SD    1 
ATOM   3839  C  CE    . MET A 1 2018 ? 158.734 166.228 148.284 1.00 5.84   ? 2018 MET A CE    1 
ATOM   3840  N  N     . ASN A 1 2019 ? 163.322 170.641 148.168 1.00 11.76  ? 2019 ASN A N     1 
ATOM   3841  C  CA    . ASN A 1 2019 ? 164.802 170.801 148.204 1.00 10.06  ? 2019 ASN A CA    1 
ATOM   3842  C  C     . ASN A 1 2019 ? 165.362 169.836 149.251 1.00 11.69  ? 2019 ASN A C     1 
ATOM   3843  O  O     . ASN A 1 2019 ? 165.391 170.207 150.444 1.00 14.35  ? 2019 ASN A O     1 
ATOM   3844  C  CB    . ASN A 1 2019 ? 165.216 172.240 148.494 1.00 10.94  ? 2019 ASN A CB    1 
ATOM   3845  C  CG    . ASN A 1 2019 ? 164.810 173.191 147.395 1.00 12.68  ? 2019 ASN A CG    1 
ATOM   3846  O  OD1   . ASN A 1 2019 ? 164.200 172.775 146.405 1.00 22.12  ? 2019 ASN A OD1   1 
ATOM   3847  N  ND2   . ASN A 1 2019 ? 165.134 174.467 147.548 1.00 12.12  ? 2019 ASN A ND2   1 
ATOM   3848  N  N     . PRO A 1 2020 ? 165.798 168.617 148.868 1.00 13.69  ? 2020 PRO A N     1 
ATOM   3849  C  CA    . PRO A 1 2020 ? 166.271 167.643 149.841 1.00 15.49  ? 2020 PRO A CA    1 
ATOM   3850  C  C     . PRO A 1 2020 ? 167.514 168.151 150.555 1.00 20.50  ? 2020 PRO A C     1 
ATOM   3851  O  O     . PRO A 1 2020 ? 168.419 168.685 149.883 1.00 19.65  ? 2020 PRO A O     1 
ATOM   3852  C  CB    . PRO A 1 2020 ? 166.555 166.399 148.985 1.00 13.55  ? 2020 PRO A CB    1 
ATOM   3853  C  CG    . PRO A 1 2020 ? 165.777 166.638 147.709 1.00 13.65  ? 2020 PRO A CG    1 
ATOM   3854  C  CD    . PRO A 1 2020 ? 165.851 168.138 147.500 1.00 12.18  ? 2020 PRO A CD    1 
ATOM   3855  N  N     . GLY A 1 2021 ? 167.561 167.995 151.881 1.00 14.38  ? 2021 GLY A N     1 
ATOM   3856  C  CA    . GLY A 1 2021 ? 168.745 168.412 152.657 1.00 17.21  ? 2021 GLY A CA    1 
ATOM   3857  C  C     . GLY A 1 2021 ? 168.531 169.739 153.359 1.00 16.75  ? 2021 GLY A C     1 
ATOM   3858  O  O     . GLY A 1 2021 ? 169.263 170.010 154.333 1.00 20.64  ? 2021 GLY A O     1 
ATOM   3859  N  N     . TYR A 1 2022 ? 167.567 170.540 152.895 1.00 16.92  ? 2022 TYR A N     1 
ATOM   3860  C  CA    . TYR A 1 2022 ? 167.334 171.886 153.490 1.00 16.94  ? 2022 TYR A CA    1 
ATOM   3861  C  C     . TYR A 1 2022 ? 166.772 171.717 154.903 1.00 22.49  ? 2022 TYR A C     1 
ATOM   3862  O  O     . TYR A 1 2022 ? 166.076 170.713 155.164 1.00 23.29  ? 2022 TYR A O     1 
ATOM   3863  C  CB    . TYR A 1 2022 ? 166.413 172.732 152.605 1.00 13.59  ? 2022 TYR A CB    1 
ATOM   3864  C  CG    . TYR A 1 2022 ? 167.092 173.377 151.404 1.00 18.24  ? 2022 TYR A CG    1 
ATOM   3865  C  CD1   . TYR A 1 2022 ? 166.680 174.616 150.928 1.00 18.33  ? 2022 TYR A CD1   1 
ATOM   3866  C  CD2   . TYR A 1 2022 ? 168.139 172.746 150.744 1.00 15.44  ? 2022 TYR A CD2   1 
ATOM   3867  C  CE1   . TYR A 1 2022 ? 167.293 175.210 149.837 1.00 13.80  ? 2022 TYR A CE1   1 
ATOM   3868  C  CE2   . TYR A 1 2022 ? 168.758 173.328 149.651 1.00 17.03  ? 2022 TYR A CE2   1 
ATOM   3869  C  CZ    . TYR A 1 2022 ? 168.334 174.564 149.196 1.00 16.15  ? 2022 TYR A CZ    1 
ATOM   3870  O  OH    . TYR A 1 2022 ? 168.941 175.142 148.119 1.00 21.65  ? 2022 TYR A OH    1 
ATOM   3871  N  N     . ALA A 1 2023 ? 167.072 172.669 155.792 1.00 23.71  ? 2023 ALA A N     1 
ATOM   3872  C  CA    . ALA A 1 2023 ? 166.577 172.602 157.189 1.00 15.98  ? 2023 ALA A CA    1 
ATOM   3873  C  C     . ALA A 1 2023 ? 165.071 172.864 157.217 1.00 18.06  ? 2023 ALA A C     1 
ATOM   3874  O  O     . ALA A 1 2023 ? 164.574 173.611 156.346 1.00 19.63  ? 2023 ALA A O     1 
ATOM   3875  C  CB    . ALA A 1 2023 ? 167.324 173.597 158.048 1.00 14.10  ? 2023 ALA A CB    1 
ATOM   3876  N  N     . GLY A 1 2024 ? 164.368 172.276 158.190 1.00 23.44  ? 2024 GLY A N     1 
ATOM   3877  C  CA    . GLY A 1 2024 ? 162.904 172.441 158.282 1.00 16.81  ? 2024 GLY A CA    1 
ATOM   3878  C  C     . GLY A 1 2024 ? 162.196 171.478 157.351 1.00 15.84  ? 2024 GLY A C     1 
ATOM   3879  O  O     . GLY A 1 2024 ? 160.958 171.582 157.225 1.00 20.27  ? 2024 GLY A O     1 
ATOM   3880  N  N     . ARG A 1 2025 ? 162.949 170.572 156.721 1.00 15.27  ? 2025 ARG A N     1 
ATOM   3881  C  CA    . ARG A 1 2025 ? 162.359 169.597 155.768 1.00 12.88  ? 2025 ARG A CA    1 
ATOM   3882  C  C     . ARG A 1 2025 ? 162.253 168.223 156.447 1.00 15.08  ? 2025 ARG A C     1 
ATOM   3883  O  O     . ARG A 1 2025 ? 163.136 167.901 157.271 1.00 17.92  ? 2025 ARG A O     1 
ATOM   3884  C  CB    . ARG A 1 2025 ? 163.206 169.520 154.494 1.00 12.58  ? 2025 ARG A CB    1 
ATOM   3885  C  CG    . ARG A 1 2025 ? 162.935 170.608 153.466 1.00 11.28  ? 2025 ARG A CG    1 
ATOM   3886  C  CD    . ARG A 1 2025 ? 163.261 172.011 153.945 1.00 13.23  ? 2025 ARG A CD    1 
ATOM   3887  N  NE    . ARG A 1 2025 ? 163.157 172.972 152.841 1.00 19.36  ? 2025 ARG A NE    1 
ATOM   3888  C  CZ    . ARG A 1 2025 ? 163.420 174.268 152.934 1.00 21.69  ? 2025 ARG A CZ    1 
ATOM   3889  N  NH1   . ARG A 1 2025 ? 163.639 174.816 154.116 1.00 17.51  ? 2025 ARG A NH1   1 
ATOM   3890  N  NH2   . ARG A 1 2025 ? 163.467 175.009 151.842 1.00 15.97  ? 2025 ARG A NH2   1 
ATOM   3891  N  N     . SER A 1 2026 ? 161.216 167.451 156.111 1.00 15.10  ? 2026 SER A N     1 
ATOM   3892  C  CA    . SER A 1 2026 ? 161.011 166.115 156.727 1.00 14.55  ? 2026 SER A CA    1 
ATOM   3893  C  C     . SER A 1 2026 ? 161.425 165.013 155.744 1.00 16.10  ? 2026 SER A C     1 
ATOM   3894  O  O     . SER A 1 2026 ? 161.841 165.353 154.616 1.00 21.75  ? 2026 SER A O     1 
ATOM   3895  C  CB    . SER A 1 2026 ? 159.581 165.936 157.166 1.00 14.85  ? 2026 SER A CB    1 
ATOM   3896  O  OG    . SER A 1 2026 ? 159.197 166.955 158.078 1.00 19.98  ? 2026 SER A OG    1 
ATOM   3897  N  N     . ASN A 1 2027 ? 161.311 163.749 156.158 1.00 19.33  ? 2027 ASN A N     1 
ATOM   3898  C  CA    . ASN A 1 2027 ? 161.669 162.632 155.297 1.00 15.71  ? 2027 ASN A CA    1 
ATOM   3899  C  C     . ASN A 1 2027 ? 160.399 161.997 154.751 1.00 16.93  ? 2027 ASN A C     1 
ATOM   3900  O  O     . ASN A 1 2027 ? 159.479 161.682 155.513 1.00 23.45  ? 2027 ASN A O     1 
ATOM   3901  C  CB    . ASN A 1 2027 ? 162.499 161.595 156.057 1.00 19.18  ? 2027 ASN A CB    1 
ATOM   3902  C  CG    . ASN A 1 2027 ? 163.988 161.799 155.877 1.00 24.76  ? 2027 ASN A CG    1 
ATOM   3903  O  OD1   . ASN A 1 2027 ? 164.444 162.228 154.818 1.00 28.13  ? 2027 ASN A OD1   1 
ATOM   3904  N  ND2   . ASN A 1 2027 ? 164.757 161.489 156.913 1.00 26.93  ? 2027 ASN A ND2   1 
ATOM   3905  N  N     . LEU A 1 2028 ? 160.349 161.821 153.437 1.00 14.03  ? 2028 LEU A N     1 
ATOM   3906  C  CA    . LEU A 1 2028 ? 159.174 161.238 152.812 1.00 9.21   ? 2028 LEU A CA    1 
ATOM   3907  C  C     . LEU A 1 2028 ? 159.136 159.732 153.058 1.00 11.87  ? 2028 LEU A C     1 
ATOM   3908  O  O     . LEU A 1 2028 ? 160.168 159.061 152.964 1.00 14.65  ? 2028 LEU A O     1 
ATOM   3909  C  CB    . LEU A 1 2028 ? 159.171 161.520 151.312 1.00 9.25   ? 2028 LEU A CB    1 
ATOM   3910  C  CG    . LEU A 1 2028 ? 158.339 162.708 150.831 1.00 9.46   ? 2028 LEU A CG    1 
ATOM   3911  C  CD1   . LEU A 1 2028 ? 158.979 164.018 151.252 1.00 6.51   ? 2028 LEU A CD1   1 
ATOM   3912  C  CD2   . LEU A 1 2028 ? 158.170 162.652 149.324 1.00 10.57  ? 2028 LEU A CD2   1 
ATOM   3913  N  N     . PRO A 1 2029 ? 157.972 159.175 153.384 1.00 15.70  ? 2029 PRO A N     1 
ATOM   3914  C  CA    . PRO A 1 2029 ? 157.859 157.716 153.479 1.00 10.34  ? 2029 PRO A CA    1 
ATOM   3915  C  C     . PRO A 1 2029 ? 158.028 157.058 152.119 1.00 11.78  ? 2029 PRO A C     1 
ATOM   3916  O  O     . PRO A 1 2029 ? 157.777 157.661 151.073 1.00 11.61  ? 2029 PRO A O     1 
ATOM   3917  C  CB    . PRO A 1 2029 ? 156.446 157.501 154.034 1.00 8.13   ? 2029 PRO A CB    1 
ATOM   3918  C  CG    . PRO A 1 2029 ? 155.715 158.759 153.728 1.00 9.42   ? 2029 PRO A CG    1 
ATOM   3919  C  CD    . PRO A 1 2029 ? 156.729 159.857 153.777 1.00 11.65  ? 2029 PRO A CD    1 
ATOM   3920  N  N     . ASP A 1 2030 ? 158.470 155.799 152.148 1.00 11.49  ? 2030 ASP A N     1 
ATOM   3921  C  CA    . ASP A 1 2030 ? 158.763 155.080 150.912 1.00 12.33  ? 2030 ASP A CA    1 
ATOM   3922  C  C     . ASP A 1 2030 ? 157.509 154.863 150.073 1.00 13.24  ? 2030 ASP A C     1 
ATOM   3923  O  O     . ASP A 1 2030 ? 157.561 154.941 148.839 1.00 16.47  ? 2030 ASP A O     1 
ATOM   3924  C  CB    . ASP A 1 2030 ? 159.432 153.744 151.233 1.00 19.57  ? 2030 ASP A CB    1 
ATOM   3925  C  CG    . ASP A 1 2030 ? 160.821 153.915 151.812 1.00 27.65  ? 2030 ASP A CG    1 
ATOM   3926  O  OD1   . ASP A 1 2030 ? 161.409 152.907 152.256 1.00 25.58  ? 2030 ASP A OD1   1 
ATOM   3927  O  OD2   . ASP A 1 2030 ? 161.326 155.057 151.823 1.00 29.62  ? 2030 ASP A OD2   1 
ATOM   3928  N  N     . ASN A 1 2031 ? 156.376 154.577 150.719 1.00 10.13  ? 2031 ASN A N     1 
ATOM   3929  C  CA    . ASN A 1 2031 ? 155.137 154.375 149.975 1.00 12.81  ? 2031 ASN A CA    1 
ATOM   3930  C  C     . ASN A 1 2031 ? 154.704 155.643 149.251 1.00 12.48  ? 2031 ASN A C     1 
ATOM   3931  O  O     . ASN A 1 2031 ? 154.199 155.569 148.125 1.00 12.72  ? 2031 ASN A O     1 
ATOM   3932  C  CB    . ASN A 1 2031 ? 154.030 153.892 150.911 1.00 12.20  ? 2031 ASN A CB    1 
ATOM   3933  C  CG    . ASN A 1 2031 ? 153.918 154.735 152.161 1.00 14.72  ? 2031 ASN A CG    1 
ATOM   3934  O  OD1   . ASN A 1 2031 ? 154.828 154.760 152.989 1.00 19.32  ? 2031 ASN A OD1   1 
ATOM   3935  N  ND2   . ASN A 1 2031 ? 152.798 155.430 152.307 1.00 10.85  ? 2031 ASN A ND2   1 
ATOM   3936  N  N     . LEU A 1 2032 ? 154.878 156.806 149.880 1.00 8.53   ? 2032 LEU A N     1 
ATOM   3937  C  CA    . LEU A 1 2032 ? 154.585 158.063 149.202 1.00 6.83   ? 2032 LEU A CA    1 
ATOM   3938  C  C     . LEU A 1 2032 ? 155.570 158.321 148.070 1.00 7.55   ? 2032 LEU A C     1 
ATOM   3939  O  O     . LEU A 1 2032 ? 155.185 158.814 147.004 1.00 7.31   ? 2032 LEU A O     1 
ATOM   3940  C  CB    . LEU A 1 2032 ? 154.604 159.215 150.206 1.00 8.53   ? 2032 LEU A CB    1 
ATOM   3941  C  CG    . LEU A 1 2032 ? 154.429 160.626 149.643 1.00 5.56   ? 2032 LEU A CG    1 
ATOM   3942  C  CD1   . LEU A 1 2032 ? 153.020 160.816 149.110 1.00 4.04   ? 2032 LEU A CD1   1 
ATOM   3943  C  CD2   . LEU A 1 2032 ? 154.752 161.666 150.698 1.00 6.44   ? 2032 LEU A CD2   1 
ATOM   3944  N  N     . LYS A 1 2033 ? 156.848 157.992 148.283 1.00 8.67   ? 2033 LYS A N     1 
ATOM   3945  C  CA    . LYS A 1 2033 ? 157.854 158.216 147.252 1.00 6.32   ? 2033 LYS A CA    1 
ATOM   3946  C  C     . LYS A 1 2033 ? 157.610 157.349 146.024 1.00 7.92   ? 2033 LYS A C     1 
ATOM   3947  O  O     . LYS A 1 2033 ? 157.870 157.788 144.898 1.00 13.16  ? 2033 LYS A O     1 
ATOM   3948  C  CB    . LYS A 1 2033 ? 159.253 157.963 147.815 1.00 5.44   ? 2033 LYS A CB    1 
ATOM   3949  C  CG    . LYS A 1 2033 ? 159.825 159.147 148.574 1.00 8.76   ? 2033 LYS A CG    1 
ATOM   3950  C  CD    . LYS A 1 2033 ? 161.324 159.019 148.785 1.00 8.51   ? 2033 LYS A CD    1 
ATOM   3951  C  CE    . LYS A 1 2033 ? 161.652 157.995 149.853 1.00 14.76  ? 2033 LYS A CE    1 
ATOM   3952  N  NZ    . LYS A 1 2033 ? 163.075 158.083 150.278 1.00 17.14  ? 2033 LYS A NZ    1 
ATOM   3953  N  N     . LYS A 1 2034 ? 157.114 156.126 146.212 1.00 7.57   ? 2034 LYS A N     1 
ATOM   3954  C  CA    . LYS A 1 2034 ? 156.820 155.266 145.072 1.00 8.25   ? 2034 LYS A CA    1 
ATOM   3955  C  C     . LYS A 1 2034 ? 155.655 155.776 144.234 1.00 9.77   ? 2034 LYS A C     1 
ATOM   3956  O  O     . LYS A 1 2034 ? 155.466 155.296 143.111 1.00 17.90  ? 2034 LYS A O     1 
ATOM   3957  C  CB    . LYS A 1 2034 ? 156.533 153.840 145.547 1.00 12.30  ? 2034 LYS A CB    1 
ATOM   3958  C  CG    . LYS A 1 2034 ? 155.061 153.530 145.748 1.00 13.26  ? 2034 LYS A CG    1 
ATOM   3959  C  CD    . LYS A 1 2034 ? 154.867 152.182 146.415 1.00 20.69  ? 2034 LYS A CD    1 
ATOM   3960  C  CE    . LYS A 1 2034 ? 153.393 151.843 146.541 1.00 33.28  ? 2034 LYS A CE    1 
ATOM   3961  N  NZ    . LYS A 1 2034 ? 152.769 151.581 145.215 1.00 40.64  ? 2034 LYS A NZ    1 
ATOM   3962  N  N     . LEU A 1 2035 ? 154.879 156.730 144.743 1.00 6.22   ? 2035 LEU A N     1 
ATOM   3963  C  CA    . LEU A 1 2035 ? 153.758 157.304 144.013 1.00 5.52   ? 2035 LEU A CA    1 
ATOM   3964  C  C     . LEU A 1 2035 ? 154.168 158.438 143.086 1.00 5.98   ? 2035 LEU A C     1 
ATOM   3965  O  O     . LEU A 1 2035 ? 153.318 158.961 142.359 1.00 4.67   ? 2035 LEU A O     1 
ATOM   3966  C  CB    . LEU A 1 2035 ? 152.695 157.810 144.994 1.00 7.68   ? 2035 LEU A CB    1 
ATOM   3967  C  CG    . LEU A 1 2035 ? 151.953 156.765 145.828 1.00 7.88   ? 2035 LEU A CG    1 
ATOM   3968  C  CD1   . LEU A 1 2035 ? 151.000 157.446 146.790 1.00 7.18   ? 2035 LEU A CD1   1 
ATOM   3969  C  CD2   . LEU A 1 2035 ? 151.207 155.794 144.933 1.00 8.06   ? 2035 LEU A CD2   1 
ATOM   3970  N  N     . PHE A 1 2036 ? 155.439 158.833 143.094 1.00 7.73   ? 2036 PHE A N     1 
ATOM   3971  C  CA    . PHE A 1 2036 ? 155.926 159.929 142.272 1.00 3.80   ? 2036 PHE A CA    1 
ATOM   3972  C  C     . PHE A 1 2036 ? 157.154 159.489 141.490 1.00 4.73   ? 2036 PHE A C     1 
ATOM   3973  O  O     . PHE A 1 2036 ? 157.972 158.701 141.972 1.00 7.95   ? 2036 PHE A O     1 
ATOM   3974  C  CB    . PHE A 1 2036 ? 156.274 161.162 143.120 1.00 2.98   ? 2036 PHE A CB    1 
ATOM   3975  C  CG    . PHE A 1 2036 ? 155.095 161.768 143.826 1.00 4.23   ? 2036 PHE A CG    1 
ATOM   3976  C  CD1   . PHE A 1 2036 ? 154.705 161.307 145.071 1.00 4.23   ? 2036 PHE A CD1   1 
ATOM   3977  C  CD2   . PHE A 1 2036 ? 154.381 162.801 143.247 1.00 3.92   ? 2036 PHE A CD2   1 
ATOM   3978  C  CE1   . PHE A 1 2036 ? 153.623 161.861 145.721 1.00 3.12   ? 2036 PHE A CE1   1 
ATOM   3979  C  CE2   . PHE A 1 2036 ? 153.297 163.359 143.894 1.00 4.09   ? 2036 PHE A CE2   1 
ATOM   3980  C  CZ    . PHE A 1 2036 ? 152.919 162.888 145.133 1.00 3.83   ? 2036 PHE A CZ    1 
ATOM   3981  N  N     . ARG A 1 2037 ? 157.269 160.008 140.271 1.00 4.37   ? 2037 ARG A N     1 
ATOM   3982  C  CA    . ARG A 1 2037 ? 158.458 159.835 139.444 1.00 4.65   ? 2037 ARG A CA    1 
ATOM   3983  C  C     . ARG A 1 2037 ? 159.415 160.972 139.776 1.00 3.51   ? 2037 ARG A C     1 
ATOM   3984  O  O     . ARG A 1 2037 ? 159.107 162.140 139.524 1.00 3.10   ? 2037 ARG A O     1 
ATOM   3985  C  CB    . ARG A 1 2037 ? 158.091 159.845 137.963 1.00 5.18   ? 2037 ARG A CB    1 
ATOM   3986  C  CG    . ARG A 1 2037 ? 159.254 159.606 137.022 1.00 8.40   ? 2037 ARG A CG    1 
ATOM   3987  C  CD    . ARG A 1 2037 ? 159.794 158.201 137.168 1.00 8.17   ? 2037 ARG A CD    1 
ATOM   3988  N  NE    . ARG A 1 2037 ? 158.763 157.218 136.861 1.00 13.14  ? 2037 ARG A NE    1 
ATOM   3989  C  CZ    . ARG A 1 2037 ? 158.463 156.807 135.637 1.00 14.88  ? 2037 ARG A CZ    1 
ATOM   3990  N  NH1   . ARG A 1 2037 ? 159.114 157.257 134.577 1.00 10.06  ? 2037 ARG A NH1   1 
ATOM   3991  N  NH2   . ARG A 1 2037 ? 157.482 155.924 135.470 1.00 12.83  ? 2037 ARG A NH2   1 
ATOM   3992  N  N     . SER A 1 2038 ? 160.560 160.640 140.361 1.00 4.91   ? 2038 SER A N     1 
ATOM   3993  C  CA    . SER A 1 2038 ? 161.488 161.669 140.797 1.00 4.31   ? 2038 SER A CA    1 
ATOM   3994  C  C     . SER A 1 2038 ? 162.402 162.097 139.653 1.00 5.48   ? 2038 SER A C     1 
ATOM   3995  O  O     . SER A 1 2038 ? 162.643 161.354 138.698 1.00 9.76   ? 2038 SER A O     1 
ATOM   3996  C  CB    . SER A 1 2038 ? 162.322 161.182 141.981 1.00 3.64   ? 2038 SER A CB    1 
ATOM   3997  O  OG    . SER A 1 2038 ? 163.190 160.130 141.600 1.00 11.63  ? 2038 SER A OG    1 
ATOM   3998  N  N     . LEU A 1 2039 ? 162.909 163.322 139.762 1.00 4.19   ? 2039 LEU A N     1 
ATOM   3999  C  CA    . LEU A 1 2039 ? 163.813 163.869 138.756 1.00 4.30   ? 2039 LEU A CA    1 
ATOM   4000  C  C     . LEU A 1 2039 ? 164.760 164.857 139.414 1.00 4.89   ? 2039 LEU A C     1 
ATOM   4001  O  O     . LEU A 1 2039 ? 164.314 165.796 140.077 1.00 5.29   ? 2039 LEU A O     1 
ATOM   4002  C  CB    . LEU A 1 2039 ? 163.043 164.553 137.634 1.00 6.61   ? 2039 LEU A CB    1 
ATOM   4003  C  CG    . LEU A 1 2039 ? 163.949 165.094 136.530 1.00 5.13   ? 2039 LEU A CG    1 
ATOM   4004  C  CD1   . LEU A 1 2039 ? 164.714 163.980 135.831 1.00 6.01   ? 2039 LEU A CD1   1 
ATOM   4005  C  CD2   . LEU A 1 2039 ? 163.131 165.876 135.555 1.00 4.16   ? 2039 LEU A CD2   1 
ATOM   4006  N  N     . ALA A 1 2040 ? 166.058 164.667 139.199 1.00 4.48   ? 2040 ALA A N     1 
ATOM   4007  C  CA    . ALA A 1 2040 ? 167.080 165.518 139.800 1.00 3.42   ? 2040 ALA A CA    1 
ATOM   4008  C  C     . ALA A 1 2040 ? 167.293 166.733 138.907 1.00 6.31   ? 2040 ALA A C     1 
ATOM   4009  O  O     . ALA A 1 2040 ? 167.782 166.615 137.781 1.00 15.42  ? 2040 ALA A O     1 
ATOM   4010  C  CB    . ALA A 1 2040 ? 168.376 164.743 140.002 1.00 5.94   ? 2040 ALA A CB    1 
ATOM   4011  N  N     . MET A 1 2041 ? 166.915 167.904 139.409 1.00 6.31   ? 2041 MET A N     1 
ATOM   4012  C  CA    . MET A 1 2041 ? 167.194 169.178 138.750 1.00 4.91   ? 2041 MET A CA    1 
ATOM   4013  C  C     . MET A 1 2041 ? 168.209 169.909 139.621 1.00 5.95   ? 2041 MET A C     1 
ATOM   4014  O  O     . MET A 1 2041 ? 167.854 170.589 140.583 1.00 7.37   ? 2041 MET A O     1 
ATOM   4015  C  CB    . MET A 1 2041 ? 165.918 169.988 138.557 1.00 4.98   ? 2041 MET A CB    1 
ATOM   4016  C  CG    . MET A 1 2041 ? 164.996 169.449 137.479 1.00 7.24   ? 2041 MET A CG    1 
ATOM   4017  S  SD    . MET A 1 2041 ? 163.507 170.442 137.280 1.00 22.38  ? 2041 MET A SD    1 
ATOM   4018  C  CE    . MET A 1 2041 ? 164.166 171.866 136.420 1.00 4.51   ? 2041 MET A CE    1 
ATOM   4019  N  N     . THR A 1 2042 ? 169.488 169.761 139.282 1.00 5.93   ? 2042 THR A N     1 
ATOM   4020  C  CA    . THR A 1 2042 ? 170.574 170.301 140.090 1.00 6.40   ? 2042 THR A CA    1 
ATOM   4021  C  C     . THR A 1 2042 ? 171.402 171.349 139.362 1.00 9.69   ? 2042 THR A C     1 
ATOM   4022  O  O     . THR A 1 2042 ? 171.781 172.359 139.962 1.00 16.91  ? 2042 THR A O     1 
ATOM   4023  C  CB    . THR A 1 2042 ? 171.488 169.164 140.569 1.00 7.42   ? 2042 THR A CB    1 
ATOM   4024  O  OG1   . THR A 1 2042 ? 172.006 168.454 139.439 1.00 14.58  ? 2042 THR A OG1   1 
ATOM   4025  C  CG2   . THR A 1 2042 ? 170.716 168.205 141.454 1.00 7.00   ? 2042 THR A CG2   1 
ATOM   4026  N  N     . LYS A 1 2043 ? 171.699 171.136 138.082 1.00 8.28   ? 2043 LYS A N     1 
ATOM   4027  C  CA    . LYS A 1 2043 ? 172.531 172.066 137.324 1.00 9.85   ? 2043 LYS A CA    1 
ATOM   4028  C  C     . LYS A 1 2043 ? 171.738 172.638 136.160 1.00 11.54  ? 2043 LYS A C     1 
ATOM   4029  O  O     . LYS A 1 2043 ? 171.683 172.021 135.084 1.00 14.72  ? 2043 LYS A O     1 
ATOM   4030  C  CB    . LYS A 1 2043 ? 173.796 171.368 136.818 1.00 11.73  ? 2043 LYS A CB    1 
ATOM   4031  C  CG    . LYS A 1 2043 ? 174.947 171.376 137.806 1.00 17.71  ? 2043 LYS A CG    1 
ATOM   4032  C  CD    . LYS A 1 2043 ? 176.286 171.337 137.088 1.00 29.53  ? 2043 LYS A CD    1 
ATOM   4033  C  CE    . LYS A 1 2043 ? 177.442 171.369 138.073 1.00 37.57  ? 2043 LYS A CE    1 
ATOM   4034  N  NZ    . LYS A 1 2043 ? 178.760 171.354 137.380 1.00 35.70  ? 2043 LYS A NZ    1 
ATOM   4035  N  N     . PRO A 1 2044 ? 171.110 173.801 136.314 1.00 11.94  ? 2044 PRO A N     1 
ATOM   4036  C  CA    . PRO A 1 2044 ? 170.425 174.418 135.175 1.00 9.41   ? 2044 PRO A CA    1 
ATOM   4037  C  C     . PRO A 1 2044 ? 171.413 174.886 134.119 1.00 9.12   ? 2044 PRO A C     1 
ATOM   4038  O  O     . PRO A 1 2044 ? 172.552 175.249 134.421 1.00 11.49  ? 2044 PRO A O     1 
ATOM   4039  C  CB    . PRO A 1 2044 ? 169.674 175.591 135.812 1.00 7.37   ? 2044 PRO A CB    1 
ATOM   4040  C  CG    . PRO A 1 2044 ? 170.504 175.955 136.983 1.00 9.55   ? 2044 PRO A CG    1 
ATOM   4041  C  CD    . PRO A 1 2044 ? 171.089 174.667 137.505 1.00 7.81   ? 2044 PRO A CD    1 
ATOM   4042  N  N     . ASP A 1 2045 ? 170.964 174.870 132.864 1.00 10.80  ? 2045 ASP A N     1 
ATOM   4043  C  CA    . ASP A 1 2045 ? 171.797 175.274 131.731 1.00 10.52  ? 2045 ASP A CA    1 
ATOM   4044  C  C     . ASP A 1 2045 ? 171.820 176.796 131.673 1.00 9.37   ? 2045 ASP A C     1 
ATOM   4045  O  O     . ASP A 1 2045 ? 171.109 177.445 130.902 1.00 9.36   ? 2045 ASP A O     1 
ATOM   4046  C  CB    . ASP A 1 2045 ? 171.282 174.658 130.440 1.00 10.26  ? 2045 ASP A CB    1 
ATOM   4047  C  CG    . ASP A 1 2045 ? 171.069 173.168 130.560 1.00 14.06  ? 2045 ASP A CG    1 
ATOM   4048  O  OD1   . ASP A 1 2045 ? 172.061 172.436 130.760 1.00 16.90  ? 2045 ASP A OD1   1 
ATOM   4049  O  OD2   . ASP A 1 2045 ? 169.909 172.723 130.478 1.00 16.44  ? 2045 ASP A OD2   1 
ATOM   4050  N  N     . ARG A 1 2046 ? 172.677 177.367 132.516 1.00 9.28   ? 2046 ARG A N     1 
ATOM   4051  C  CA    . ARG A 1 2046 ? 172.688 178.808 132.726 1.00 10.37  ? 2046 ARG A CA    1 
ATOM   4052  C  C     . ARG A 1 2046 ? 173.123 179.569 131.476 1.00 9.19   ? 2046 ARG A C     1 
ATOM   4053  O  O     . ARG A 1 2046 ? 172.585 180.646 131.189 1.00 9.64   ? 2046 ARG A O     1 
ATOM   4054  C  CB    . ARG A 1 2046 ? 173.590 179.130 133.921 1.00 11.59  ? 2046 ARG A CB    1 
ATOM   4055  C  CG    . ARG A 1 2046 ? 173.587 180.592 134.304 1.00 24.80  ? 2046 ARG A CG    1 
ATOM   4056  C  CD    . ARG A 1 2046 ? 174.449 180.916 135.512 1.00 37.19  ? 2046 ARG A CD    1 
ATOM   4057  N  NE    . ARG A 1 2046 ? 173.974 180.293 136.742 1.00 35.91  ? 2046 ARG A NE    1 
ATOM   4058  C  CZ    . ARG A 1 2046 ? 174.626 179.341 137.393 1.00 29.56  ? 2046 ARG A CZ    1 
ATOM   4059  N  NH1   . ARG A 1 2046 ? 175.769 178.859 136.941 1.00 31.14  ? 2046 ARG A NH1   1 
ATOM   4060  N  NH2   . ARG A 1 2046 ? 174.114 178.855 138.521 1.00 22.14  ? 2046 ARG A NH2   1 
ATOM   4061  N  N     . GLN A 1 2047 ? 174.079 179.026 130.720 1.00 9.20   ? 2047 GLN A N     1 
ATOM   4062  C  CA    . GLN A 1 2047 ? 174.565 179.710 129.528 1.00 7.99   ? 2047 GLN A CA    1 
ATOM   4063  C  C     . GLN A 1 2047 ? 173.460 179.868 128.493 1.00 9.12   ? 2047 GLN A C     1 
ATOM   4064  O  O     . GLN A 1 2047 ? 173.294 180.943 127.906 1.00 10.45  ? 2047 GLN A O     1 
ATOM   4065  C  CB    . GLN A 1 2047 ? 175.749 178.947 128.938 1.00 10.96  ? 2047 GLN A CB    1 
ATOM   4066  C  CG    . GLN A 1 2047 ? 176.664 179.788 128.067 1.00 9.63   ? 2047 GLN A CG    1 
ATOM   4067  C  CD    . GLN A 1 2047 ? 176.316 179.685 126.596 1.00 18.24  ? 2047 GLN A CD    1 
ATOM   4068  O  OE1   . GLN A 1 2047 ? 175.725 178.701 126.154 1.00 19.14  ? 2047 GLN A OE1   1 
ATOM   4069  N  NE2   . GLN A 1 2047 ? 176.690 180.699 125.827 1.00 17.57  ? 2047 GLN A NE2   1 
ATOM   4070  N  N     . LEU A 1 2048 ? 172.695 178.799 128.262 1.00 9.41   ? 2048 LEU A N     1 
ATOM   4071  C  CA    . LEU A 1 2048 ? 171.612 178.848 127.245 1.00 7.92   ? 2048 LEU A CA    1 
ATOM   4072  C  C     . LEU A 1 2048 ? 170.567 179.894 127.667 1.00 8.04   ? 2048 LEU A C     1 
ATOM   4073  O  O     . LEU A 1 2048 ? 170.182 180.722 126.817 1.00 9.44   ? 2048 LEU A O     1 
ATOM   4074  C  CB    . LEU A 1 2048 ? 170.987 177.467 127.056 1.00 7.74   ? 2048 LEU A CB    1 
ATOM   4075  C  CG    . LEU A 1 2048 ? 169.846 177.380 126.037 1.00 6.65   ? 2048 LEU A CG    1 
ATOM   4076  C  CD1   . LEU A 1 2048 ? 170.307 177.871 124.676 1.00 7.44   ? 2048 LEU A CD1   1 
ATOM   4077  C  CD2   . LEU A 1 2048 ? 169.317 175.961 125.941 1.00 6.03   ? 2048 LEU A CD2   1 
ATOM   4078  N  N     . ILE A 1 2049 ? 170.136 179.858 128.930 1.00 6.39   ? 2049 ILE A N     1 
ATOM   4079  C  CA    . ILE A 1 2049 ? 169.094 180.810 129.419 1.00 6.21   ? 2049 ILE A CA    1 
ATOM   4080  C  C     . ILE A 1 2049 ? 169.605 182.241 129.200 1.00 8.81   ? 2049 ILE A C     1 
ATOM   4081  O  O     . ILE A 1 2049 ? 168.864 183.047 128.600 1.00 11.90  ? 2049 ILE A O     1 
ATOM   4082  C  CB    . ILE A 1 2049 ? 168.763 180.549 130.899 1.00 5.91   ? 2049 ILE A CB    1 
ATOM   4083  C  CG1   . ILE A 1 2049 ? 168.347 179.097 131.137 1.00 4.81   ? 2049 ILE A CG1   1 
ATOM   4084  C  CG2   . ILE A 1 2049 ? 167.704 181.531 131.402 1.00 5.47   ? 2049 ILE A CG2   1 
ATOM   4085  C  CD1   . ILE A 1 2049 ? 168.168 178.732 132.599 1.00 3.78   ? 2049 ILE A CD1   1 
ATOM   4086  N  N     . ALA A 1 2050 ? 170.828 182.529 129.652 1.00 8.15   ? 2050 ALA A N     1 
ATOM   4087  C  CA    . ALA A 1 2050 ? 171.414 183.877 129.478 1.00 5.74   ? 2050 ALA A CA    1 
ATOM   4088  C  C     . ALA A 1 2050 ? 171.397 184.253 127.997 1.00 8.85   ? 2050 ALA A C     1 
ATOM   4089  O  O     . ALA A 1 2050 ? 170.939 185.367 127.669 1.00 13.36  ? 2050 ALA A O     1 
ATOM   4090  C  CB    . ALA A 1 2050 ? 172.816 183.901 130.035 1.00 6.51   ? 2050 ALA A CB    1 
ATOM   4091  N  N     . GLN A 1 2051 ? 171.870 183.353 127.130 1.00 8.01   ? 2051 GLN A N     1 
ATOM   4092  C  CA    . GLN A 1 2051 ? 171.938 183.664 125.706 1.00 6.50   ? 2051 GLN A CA    1 
ATOM   4093  C  C     . GLN A 1 2051 ? 170.555 183.963 125.143 1.00 9.65   ? 2051 GLN A C     1 
ATOM   4094  O  O     . GLN A 1 2051 ? 170.355 184.980 124.468 1.00 12.80  ? 2051 GLN A O     1 
ATOM   4095  C  CB    . GLN A 1 2051 ? 172.595 182.505 124.952 1.00 10.53  ? 2051 GLN A CB    1 
ATOM   4096  C  CG    . GLN A 1 2051 ? 172.904 182.779 123.484 1.00 14.66  ? 2051 GLN A CG    1 
ATOM   4097  C  CD    . GLN A 1 2051 ? 171.727 182.499 122.569 1.00 26.78  ? 2051 GLN A CD    1 
ATOM   4098  O  OE1   . GLN A 1 2051 ? 170.892 181.642 122.856 1.00 37.58  ? 2051 GLN A OE1   1 
ATOM   4099  N  NE2   . GLN A 1 2051 ? 171.653 183.227 121.461 1.00 24.91  ? 2051 GLN A NE2   1 
ATOM   4100  N  N     . VAL A 1 2052 ? 169.581 183.095 125.424 1.00 10.20  ? 2052 VAL A N     1 
ATOM   4101  C  CA    . VAL A 1 2052 ? 168.247 183.277 124.859 1.00 7.83   ? 2052 VAL A CA    1 
ATOM   4102  C  C     . VAL A 1 2052 ? 167.585 184.526 125.426 1.00 8.43   ? 2052 VAL A C     1 
ATOM   4103  O  O     . VAL A 1 2052 ? 166.962 185.298 124.688 1.00 12.68  ? 2052 VAL A O     1 
ATOM   4104  C  CB    . VAL A 1 2052 ? 167.389 182.021 125.087 1.00 5.33   ? 2052 VAL A CB    1 
ATOM   4105  C  CG1   . VAL A 1 2052 ? 165.970 182.251 124.596 1.00 3.85   ? 2052 VAL A CG1   1 
ATOM   4106  C  CG2   . VAL A 1 2052 ? 168.002 180.836 124.370 1.00 4.66   ? 2052 VAL A CG2   1 
ATOM   4107  N  N     . MET A 1 2053 ? 167.706 184.751 126.738 1.00 7.94   ? 2053 MET A N     1 
ATOM   4108  C  CA    . MET A 1 2053 ? 167.095 185.938 127.327 1.00 8.66   ? 2053 MET A CA    1 
ATOM   4109  C  C     . MET A 1 2053 ? 167.692 187.216 126.756 1.00 10.11  ? 2053 MET A C     1 
ATOM   4110  O  O     . MET A 1 2053 ? 166.953 188.139 126.399 1.00 13.89  ? 2053 MET A O     1 
ATOM   4111  C  CB    . MET A 1 2053 ? 167.235 185.918 128.847 1.00 10.92  ? 2053 MET A CB    1 
ATOM   4112  C  CG    . MET A 1 2053 ? 166.401 184.860 129.534 1.00 10.46  ? 2053 MET A CG    1 
ATOM   4113  S  SD    . MET A 1 2053 ? 166.388 185.105 131.313 1.00 28.83  ? 2053 MET A SD    1 
ATOM   4114  C  CE    . MET A 1 2053 ? 164.994 186.217 131.461 1.00 23.02  ? 2053 MET A CE    1 
ATOM   4115  N  N     . LEU A 1 2054 ? 169.021 187.290 126.649 1.00 10.19  ? 2054 LEU A N     1 
ATOM   4116  C  CA    . LEU A 1 2054 ? 169.634 188.489 126.090 1.00 9.06   ? 2054 LEU A CA    1 
ATOM   4117  C  C     . LEU A 1 2054 ? 169.268 188.667 124.622 1.00 10.72  ? 2054 LEU A C     1 
ATOM   4118  O  O     . LEU A 1 2054 ? 169.046 189.794 124.167 1.00 11.54  ? 2054 LEU A O     1 
ATOM   4119  C  CB    . LEU A 1 2054 ? 171.149 188.439 126.278 1.00 7.52   ? 2054 LEU A CB    1 
ATOM   4120  C  CG    . LEU A 1 2054 ? 171.608 188.632 127.724 1.00 7.37   ? 2054 LEU A CG    1 
ATOM   4121  C  CD1   . LEU A 1 2054 ? 173.115 188.546 127.831 1.00 11.08  ? 2054 LEU A CD1   1 
ATOM   4122  C  CD2   . LEU A 1 2054 ? 171.108 189.960 128.269 1.00 9.11   ? 2054 LEU A CD2   1 
ATOM   4123  N  N     . TYR A 1 2055 ? 169.187 187.569 123.867 1.00 13.22  ? 2055 TYR A N     1 
ATOM   4124  C  CA    . TYR A 1 2055 ? 168.806 187.665 122.463 1.00 10.10  ? 2055 TYR A CA    1 
ATOM   4125  C  C     . TYR A 1 2055 ? 167.377 188.169 122.312 1.00 10.72  ? 2055 TYR A C     1 
ATOM   4126  O  O     . TYR A 1 2055 ? 167.070 188.919 121.377 1.00 12.47  ? 2055 TYR A O     1 
ATOM   4127  C  CB    . TYR A 1 2055 ? 168.976 186.304 121.788 1.00 9.46   ? 2055 TYR A CB    1 
ATOM   4128  C  CG    . TYR A 1 2055 ? 168.842 186.331 120.284 1.00 10.67  ? 2055 TYR A CG    1 
ATOM   4129  C  CD1   . TYR A 1 2055 ? 169.568 187.233 119.519 1.00 13.24  ? 2055 TYR A CD1   1 
ATOM   4130  C  CD2   . TYR A 1 2055 ? 167.995 185.451 119.629 1.00 8.75   ? 2055 TYR A CD2   1 
ATOM   4131  C  CE1   . TYR A 1 2055 ? 169.450 187.258 118.144 1.00 12.59  ? 2055 TYR A CE1   1 
ATOM   4132  C  CE2   . TYR A 1 2055 ? 167.870 185.469 118.256 1.00 11.61  ? 2055 TYR A CE2   1 
ATOM   4133  C  CZ    . TYR A 1 2055 ? 168.600 186.374 117.518 1.00 14.51  ? 2055 TYR A CZ    1 
ATOM   4134  O  OH    . TYR A 1 2055 ? 168.478 186.394 116.148 1.00 21.02  ? 2055 TYR A OH    1 
ATOM   4135  N  N     . SER A 1 2056 ? 166.486 187.767 123.221 1.00 10.06  ? 2056 SER A N     1 
ATOM   4136  C  CA    . SER A 1 2056 ? 165.095 188.199 123.145 1.00 9.84   ? 2056 SER A CA    1 
ATOM   4137  C  C     . SER A 1 2056 ? 164.914 189.664 123.524 1.00 16.21  ? 2056 SER A C     1 
ATOM   4138  O  O     . SER A 1 2056 ? 163.990 190.308 123.018 1.00 26.19  ? 2056 SER A O     1 
ATOM   4139  C  CB    . SER A 1 2056 ? 164.222 187.322 124.042 1.00 10.06  ? 2056 SER A CB    1 
ATOM   4140  O  OG    . SER A 1 2056 ? 164.598 187.452 125.401 1.00 15.13  ? 2056 SER A OG    1 
ATOM   4141  N  N     . GLN A 1 2057 ? 165.765 190.203 124.394 1.00 15.95  ? 2057 GLN A N     1 
ATOM   4142  C  CA    . GLN A 1 2057 ? 165.692 191.603 124.790 1.00 14.15  ? 2057 GLN A CA    1 
ATOM   4143  C  C     . GLN A 1 2057 ? 166.213 192.553 123.721 1.00 18.54  ? 2057 GLN A C     1 
ATOM   4144  O  O     . GLN A 1 2057 ? 166.069 193.770 123.872 1.00 25.94  ? 2057 GLN A O     1 
ATOM   4145  C  CB    . GLN A 1 2057 ? 166.471 191.835 126.090 1.00 16.40  ? 2057 GLN A CB    1 
ATOM   4146  C  CG    . GLN A 1 2057 ? 166.063 190.945 127.248 1.00 16.59  ? 2057 GLN A CG    1 
ATOM   4147  C  CD    . GLN A 1 2057 ? 164.976 191.558 128.103 1.00 25.00  ? 2057 GLN A CD    1 
ATOM   4148  O  OE1   . GLN A 1 2057 ? 163.926 191.958 127.602 1.00 26.60  ? 2057 GLN A OE1   1 
ATOM   4149  N  NE2   . GLN A 1 2057 ? 165.221 191.632 129.405 1.00 21.53  ? 2057 GLN A NE2   1 
ATOM   4150  N  N     . GLY A 1 2058 ? 166.807 192.035 122.652 1.00 13.93  ? 2058 GLY A N     1 
ATOM   4151  C  CA    . GLY A 1 2058 ? 167.388 192.866 121.623 1.00 16.84  ? 2058 GLY A CA    1 
ATOM   4152  C  C     . GLY A 1 2058 ? 168.878 193.084 121.733 1.00 15.63  ? 2058 GLY A C     1 
ATOM   4153  O  O     . GLY A 1 2058 ? 169.400 193.998 121.086 1.00 26.32  ? 2058 GLY A O     1 
ATOM   4154  N  N     . PHE A 1 2059 ? 169.578 192.283 122.531 1.00 13.21  ? 2059 PHE A N     1 
ATOM   4155  C  CA    . PHE A 1 2059 ? 171.021 192.418 122.687 1.00 15.97  ? 2059 PHE A CA    1 
ATOM   4156  C  C     . PHE A 1 2059 ? 171.712 191.772 121.492 1.00 19.81  ? 2059 PHE A C     1 
ATOM   4157  O  O     . PHE A 1 2059 ? 171.655 190.551 121.321 1.00 22.72  ? 2059 PHE A O     1 
ATOM   4158  C  CB    . PHE A 1 2059 ? 171.487 191.760 123.983 1.00 11.51  ? 2059 PHE A CB    1 
ATOM   4159  C  CG    . PHE A 1 2059 ? 171.289 192.603 125.209 1.00 12.79  ? 2059 PHE A CG    1 
ATOM   4160  C  CD1   . PHE A 1 2059 ? 170.062 192.638 125.850 1.00 11.42  ? 2059 PHE A CD1   1 
ATOM   4161  C  CD2   . PHE A 1 2059 ? 172.333 193.341 125.733 1.00 15.22  ? 2059 PHE A CD2   1 
ATOM   4162  C  CE1   . PHE A 1 2059 ? 169.880 193.403 126.982 1.00 10.76  ? 2059 PHE A CE1   1 
ATOM   4163  C  CE2   . PHE A 1 2059 ? 172.156 194.109 126.866 1.00 14.46  ? 2059 PHE A CE2   1 
ATOM   4164  C  CZ    . PHE A 1 2059 ? 170.928 194.139 127.491 1.00 12.20  ? 2059 PHE A CZ    1 
ATOM   4165  N  N     . ARG A 1 2060 ? 172.361 192.583 120.663 1.00 19.15  ? 2060 ARG A N     1 
ATOM   4166  C  CA    . ARG A 1 2060 ? 173.314 192.038 119.709 1.00 20.59  ? 2060 ARG A CA    1 
ATOM   4167  C  C     . ARG A 1 2060 ? 174.491 191.414 120.447 1.00 21.33  ? 2060 ARG A C     1 
ATOM   4168  O  O     . ARG A 1 2060 ? 174.845 191.825 121.555 1.00 25.57  ? 2060 ARG A O     1 
ATOM   4169  C  CB    . ARG A 1 2060 ? 173.803 193.121 118.749 1.00 25.53  ? 2060 ARG A CB    1 
ATOM   4170  C  CG    . ARG A 1 2060 ? 172.723 193.736 117.877 1.00 27.75  ? 2060 ARG A CG    1 
ATOM   4171  C  CD    . ARG A 1 2060 ? 172.239 192.693 116.880 1.00 43.68  ? 2060 ARG A CD    1 
ATOM   4172  N  NE    . ARG A 1 2060 ? 171.248 193.196 115.937 1.00 51.58  ? 2060 ARG A NE    1 
ATOM   4173  C  CZ    . ARG A 1 2060 ? 170.642 192.445 115.028 1.00 57.18  ? 2060 ARG A CZ    1 
ATOM   4174  N  NH1   . ARG A 1 2060 ? 170.890 191.149 114.927 1.00 69.30  ? 2060 ARG A NH1   1 
ATOM   4175  N  NH2   . ARG A 1 2060 ? 169.777 193.008 114.191 1.00 42.91  ? 2060 ARG A NH2   1 
ATOM   4176  N  N     . THR A 1 2061 ? 175.092 190.405 119.821 1.00 23.49  ? 2061 THR A N     1 
ATOM   4177  C  CA    . THR A 1 2061 ? 176.195 189.651 120.417 1.00 26.82  ? 2061 THR A CA    1 
ATOM   4178  C  C     . THR A 1 2061 ? 175.810 189.124 121.799 1.00 17.75  ? 2061 THR A C     1 
ATOM   4179  O  O     . THR A 1 2061 ? 176.543 189.271 122.778 1.00 16.92  ? 2061 THR A O     1 
ATOM   4180  C  CB    . THR A 1 2061 ? 177.471 190.494 120.488 1.00 35.69  ? 2061 THR A CB    1 
ATOM   4181  O  OG1   . THR A 1 2061 ? 177.282 191.584 121.400 1.00 20.81  ? 2061 THR A OG1   1 
ATOM   4182  C  CG2   . THR A 1 2061 ? 177.827 191.040 119.112 1.00 32.50  ? 2061 THR A CG2   1 
ATOM   4183  N  N     . ALA A 1 2062 ? 174.624 188.517 121.874 1.00 20.80  ? 2062 ALA A N     1 
ATOM   4184  C  CA    . ALA A 1 2062 ? 174.182 187.923 123.130 1.00 15.59  ? 2062 ALA A CA    1 
ATOM   4185  C  C     . ALA A 1 2062 ? 175.006 186.696 123.494 1.00 17.70  ? 2062 ALA A C     1 
ATOM   4186  O  O     . ALA A 1 2062 ? 175.136 186.368 124.679 1.00 21.69  ? 2062 ALA A O     1 
ATOM   4187  C  CB    . ALA A 1 2062 ? 172.700 187.561 123.047 1.00 12.11  ? 2062 ALA A CB    1 
ATOM   4188  N  N     . GLU A 1 2063 ? 175.566 186.009 122.495 1.00 16.79  ? 2063 GLU A N     1 
ATOM   4189  C  CA    . GLU A 1 2063 ? 176.350 184.808 122.767 1.00 18.12  ? 2063 GLU A CA    1 
ATOM   4190  C  C     . GLU A 1 2063 ? 177.592 185.127 123.588 1.00 22.05  ? 2063 GLU A C     1 
ATOM   4191  O  O     . GLU A 1 2063 ? 177.876 184.447 124.582 1.00 27.74  ? 2063 GLU A O     1 
ATOM   4192  C  CB    . GLU A 1 2063 ? 176.738 184.128 121.455 1.00 20.36  ? 2063 GLU A CB    1 
ATOM   4193  C  CG    . GLU A 1 2063 ? 175.556 183.686 120.615 1.00 38.09  ? 2063 GLU A CG    1 
ATOM   4194  C  CD    . GLU A 1 2063 ? 175.962 182.775 119.474 1.00 58.39  ? 2063 GLU A CD    1 
ATOM   4195  O  OE1   . GLU A 1 2063 ? 177.170 182.480 119.350 1.00 66.17  ? 2063 GLU A OE1   1 
ATOM   4196  O  OE2   . GLU A 1 2063 ? 175.075 182.354 118.703 1.00 50.98  ? 2063 GLU A OE2   1 
ATOM   4197  N  N     . VAL A 1 2064 ? 178.347 186.155 123.192 1.00 19.17  ? 2064 VAL A N     1 
ATOM   4198  C  CA    . VAL A 1 2064 ? 179.551 186.509 123.938 1.00 14.44  ? 2064 VAL A CA    1 
ATOM   4199  C  C     . VAL A 1 2064 ? 179.181 187.040 125.317 1.00 14.45  ? 2064 VAL A C     1 
ATOM   4200  O  O     . VAL A 1 2064 ? 179.877 186.778 126.306 1.00 16.55  ? 2064 VAL A O     1 
ATOM   4201  C  CB    . VAL A 1 2064 ? 180.412 187.512 123.144 1.00 16.88  ? 2064 VAL A CB    1 
ATOM   4202  C  CG1   . VAL A 1 2064 ? 180.876 186.892 121.834 1.00 19.53  ? 2064 VAL A CG1   1 
ATOM   4203  C  CG2   . VAL A 1 2064 ? 179.659 188.801 122.883 1.00 13.19  ? 2064 VAL A CG2   1 
ATOM   4204  N  N     . LEU A 1 2065 ? 178.069 187.773 125.411 1.00 13.49  ? 2065 LEU A N     1 
ATOM   4205  C  CA    . LEU A 1 2065 ? 177.621 188.265 126.708 1.00 11.35  ? 2065 LEU A CA    1 
ATOM   4206  C  C     . LEU A 1 2065 ? 177.313 187.116 127.659 1.00 11.93  ? 2065 LEU A C     1 
ATOM   4207  O  O     . LEU A 1 2065 ? 177.706 187.151 128.829 1.00 13.91  ? 2065 LEU A O     1 
ATOM   4208  C  CB    . LEU A 1 2065 ? 176.397 189.163 126.538 1.00 10.83  ? 2065 LEU A CB    1 
ATOM   4209  C  CG    . LEU A 1 2065 ? 176.638 190.543 125.928 1.00 11.92  ? 2065 LEU A CG    1 
ATOM   4210  C  CD1   . LEU A 1 2065 ? 175.363 191.365 125.959 1.00 11.75  ? 2065 LEU A CD1   1 
ATOM   4211  C  CD2   . LEU A 1 2065 ? 177.751 191.255 126.671 1.00 14.07  ? 2065 LEU A CD2   1 
ATOM   4212  N  N     . ALA A 1 2066 ? 176.616 186.086 127.173 1.00 13.48  ? 2066 ALA A N     1 
ATOM   4213  C  CA    . ALA A 1 2066 ? 176.322 184.930 128.015 1.00 11.51  ? 2066 ALA A CA    1 
ATOM   4214  C  C     . ALA A 1 2066 ? 177.595 184.175 128.376 1.00 12.95  ? 2066 ALA A C     1 
ATOM   4215  O  O     . ALA A 1 2066 ? 177.804 183.802 129.540 1.00 11.58  ? 2066 ALA A O     1 
ATOM   4216  C  CB    . ALA A 1 2066 ? 175.331 184.008 127.307 1.00 9.90   ? 2066 ALA A CB    1 
ATOM   4217  N  N     . ASN A 1 2067 ? 178.464 183.946 127.386 1.00 13.95  ? 2067 ASN A N     1 
ATOM   4218  C  CA    . ASN A 1 2067 ? 179.707 183.222 127.619 1.00 12.79  ? 2067 ASN A CA    1 
ATOM   4219  C  C     . ASN A 1 2067 ? 180.656 183.983 128.529 1.00 16.32  ? 2067 ASN A C     1 
ATOM   4220  O  O     . ASN A 1 2067 ? 181.627 183.399 129.018 1.00 20.65  ? 2067 ASN A O     1 
ATOM   4221  C  CB    . ASN A 1 2067 ? 180.396 182.920 126.289 1.00 9.19   ? 2067 ASN A CB    1 
ATOM   4222  C  CG    . ASN A 1 2067 ? 179.614 181.944 125.440 1.00 12.19  ? 2067 ASN A CG    1 
ATOM   4223  O  OD1   . ASN A 1 2067 ? 179.272 180.851 125.888 1.00 15.58  ? 2067 ASN A OD1   1 
ATOM   4224  N  ND2   . ASN A 1 2067 ? 179.326 182.333 124.206 1.00 11.90  ? 2067 ASN A ND2   1 
ATOM   4225  N  N     . LYS A 1 2068 ? 180.419 185.275 128.736 1.00 16.20  ? 2068 LYS A N     1 
ATOM   4226  C  CA    . LYS A 1 2068 ? 181.180 186.031 129.718 1.00 14.62  ? 2068 LYS A CA    1 
ATOM   4227  C  C     . LYS A 1 2068 ? 180.495 186.083 131.077 1.00 12.60  ? 2068 LYS A C     1 
ATOM   4228  O  O     . LYS A 1 2068 ? 181.175 186.025 132.107 1.00 16.36  ? 2068 LYS A O     1 
ATOM   4229  C  CB    . LYS A 1 2068 ? 181.418 187.454 129.210 1.00 14.30  ? 2068 LYS A CB    1 
ATOM   4230  C  CG    . LYS A 1 2068 ? 182.446 187.548 128.099 1.00 15.55  ? 2068 LYS A CG    1 
ATOM   4231  C  CD    . LYS A 1 2068 ? 182.639 188.982 127.645 1.00 15.62  ? 2068 LYS A CD    1 
ATOM   4232  C  CE    . LYS A 1 2068 ? 183.893 189.127 126.806 1.00 20.32  ? 2068 LYS A CE    1 
ATOM   4233  N  NZ    . LYS A 1 2068 ? 185.104 188.669 127.535 1.00 21.77  ? 2068 LYS A NZ    1 
ATOM   4234  N  N     . ILE A 1 2069 ? 179.167 186.166 131.108 1.00 10.80  ? 2069 ILE A N     1 
ATOM   4235  C  CA    . ILE A 1 2069 ? 178.469 186.414 132.363 1.00 11.22  ? 2069 ILE A CA    1 
ATOM   4236  C  C     . ILE A 1 2069 ? 178.194 185.135 133.151 1.00 10.56  ? 2069 ILE A C     1 
ATOM   4237  O  O     . ILE A 1 2069 ? 178.074 185.185 134.379 1.00 11.98  ? 2069 ILE A O     1 
ATOM   4238  C  CB    . ILE A 1 2069 ? 177.168 187.197 132.102 1.00 9.30   ? 2069 ILE A CB    1 
ATOM   4239  C  CG1   . ILE A 1 2069 ? 176.672 187.853 133.391 1.00 11.09  ? 2069 ILE A CG1   1 
ATOM   4240  C  CG2   . ILE A 1 2069 ? 176.093 186.296 131.515 1.00 6.86   ? 2069 ILE A CG2   1 
ATOM   4241  C  CD1   . ILE A 1 2069 ? 177.623 188.880 133.952 1.00 10.57  ? 2069 ILE A CD1   1 
ATOM   4242  N  N     . VAL A 1 2070 ? 178.092 183.985 132.491 1.00 10.13  ? 2070 VAL A N     1 
ATOM   4243  C  CA    . VAL A 1 2070 ? 177.845 182.745 133.227 1.00 10.90  ? 2070 VAL A CA    1 
ATOM   4244  C  C     . VAL A 1 2070 ? 179.142 182.266 133.880 1.00 11.00  ? 2070 VAL A C     1 
ATOM   4245  O  O     . VAL A 1 2070 ? 179.137 181.942 135.082 1.00 11.32  ? 2070 VAL A O     1 
ATOM   4246  C  CB    . VAL A 1 2070 ? 177.217 181.675 132.318 1.00 10.90  ? 2070 VAL A CB    1 
ATOM   4247  C  CG1   . VAL A 1 2070 ? 177.121 180.346 133.046 1.00 9.97   ? 2070 VAL A CG1   1 
ATOM   4248  C  CG2   . VAL A 1 2070 ? 175.850 182.135 131.848 1.00 9.12   ? 2070 VAL A CG2   1 
ATOM   4249  N  N     . PRO A 1 2071 ? 180.271 182.207 133.160 1.00 10.50  ? 2071 PRO A N     1 
ATOM   4250  C  CA    . PRO A 1 2071 ? 181.539 181.938 133.854 1.00 10.13  ? 2071 PRO A CA    1 
ATOM   4251  C  C     . PRO A 1 2071 ? 181.863 182.967 134.916 1.00 13.81  ? 2071 PRO A C     1 
ATOM   4252  O  O     . PRO A 1 2071 ? 182.514 182.627 135.908 1.00 14.75  ? 2071 PRO A O     1 
ATOM   4253  C  CB    . PRO A 1 2071 ? 182.568 181.952 132.718 1.00 7.46   ? 2071 PRO A CB    1 
ATOM   4254  C  CG    . PRO A 1 2071 ? 181.800 181.540 131.538 1.00 8.87   ? 2071 PRO A CG    1 
ATOM   4255  C  CD    . PRO A 1 2071 ? 180.466 182.199 131.698 1.00 10.24  ? 2071 PRO A CD    1 
ATOM   4256  N  N     . PHE A 1 2072 ? 181.434 184.219 134.740 1.00 13.42  ? 2072 PHE A N     1 
ATOM   4257  C  CA    . PHE A 1 2072 ? 181.645 185.216 135.782 1.00 10.46  ? 2072 PHE A CA    1 
ATOM   4258  C  C     . PHE A 1 2072 ? 180.934 184.824 137.070 1.00 12.48  ? 2072 PHE A C     1 
ATOM   4259  O  O     . PHE A 1 2072 ? 181.507 184.927 138.158 1.00 15.31  ? 2072 PHE A O     1 
ATOM   4260  C  CB    . PHE A 1 2072 ? 181.171 186.590 135.310 1.00 11.75  ? 2072 PHE A CB    1 
ATOM   4261  C  CG    . PHE A 1 2072 ? 181.056 187.600 136.415 1.00 12.83  ? 2072 PHE A CG    1 
ATOM   4262  C  CD1   . PHE A 1 2072 ? 182.188 188.181 136.959 1.00 11.53  ? 2072 PHE A CD1   1 
ATOM   4263  C  CD2   . PHE A 1 2072 ? 179.816 187.965 136.912 1.00 13.08  ? 2072 PHE A CD2   1 
ATOM   4264  C  CE1   . PHE A 1 2072 ? 182.086 189.106 137.978 1.00 11.63  ? 2072 PHE A CE1   1 
ATOM   4265  C  CE2   . PHE A 1 2072 ? 179.708 188.890 137.930 1.00 9.78   ? 2072 PHE A CE2   1 
ATOM   4266  C  CZ    . PHE A 1 2072 ? 180.844 189.463 138.462 1.00 11.96  ? 2072 PHE A CZ    1 
ATOM   4267  N  N     . PHE A 1 2073 ? 179.684 184.366 136.967 1.00 11.95  ? 2073 PHE A N     1 
ATOM   4268  C  CA    . PHE A 1 2073 ? 178.963 183.931 138.159 1.00 11.28  ? 2073 PHE A CA    1 
ATOM   4269  C  C     . PHE A 1 2073 ? 179.599 182.686 138.767 1.00 12.25  ? 2073 PHE A C     1 
ATOM   4270  O  O     . PHE A 1 2073 ? 179.687 182.564 139.995 1.00 17.19  ? 2073 PHE A O     1 
ATOM   4271  C  CB    . PHE A 1 2073 ? 177.493 183.681 137.827 1.00 11.66  ? 2073 PHE A CB    1 
ATOM   4272  C  CG    . PHE A 1 2073 ? 176.610 184.872 138.062 1.00 11.53  ? 2073 PHE A CG    1 
ATOM   4273  C  CD1   . PHE A 1 2073 ? 176.550 185.900 137.139 1.00 10.24  ? 2073 PHE A CD1   1 
ATOM   4274  C  CD2   . PHE A 1 2073 ? 175.846 184.967 139.212 1.00 10.47  ? 2073 PHE A CD2   1 
ATOM   4275  C  CE1   . PHE A 1 2073 ? 175.741 186.997 137.354 1.00 9.95   ? 2073 PHE A CE1   1 
ATOM   4276  C  CE2   . PHE A 1 2073 ? 175.037 186.062 139.433 1.00 7.79   ? 2073 PHE A CE2   1 
ATOM   4277  C  CZ    . PHE A 1 2073 ? 174.984 187.078 138.502 1.00 9.38   ? 2073 PHE A CZ    1 
ATOM   4278  N  N     . LYS A 1 2074 ? 180.052 181.752 137.925 1.00 15.24  ? 2074 LYS A N     1 
ATOM   4279  C  CA    . LYS A 1 2074 ? 180.727 180.568 138.453 1.00 14.73  ? 2074 LYS A CA    1 
ATOM   4280  C  C     . LYS A 1 2074 ? 181.994 180.944 139.217 1.00 16.93  ? 2074 LYS A C     1 
ATOM   4281  O  O     . LYS A 1 2074 ? 182.244 180.436 140.319 1.00 18.68  ? 2074 LYS A O     1 
ATOM   4282  C  CB    . LYS A 1 2074 ? 181.054 179.599 137.318 1.00 12.69  ? 2074 LYS A CB    1 
ATOM   4283  C  CG    . LYS A 1 2074 ? 181.848 178.383 137.760 1.00 22.86  ? 2074 LYS A CG    1 
ATOM   4284  C  CD    . LYS A 1 2074 ? 181.366 177.123 137.067 1.00 36.77  ? 2074 LYS A CD    1 
ATOM   4285  C  CE    . LYS A 1 2074 ? 181.795 175.879 137.825 1.00 41.93  ? 2074 LYS A CE    1 
ATOM   4286  N  NZ    . LYS A 1 2074 ? 183.277 175.765 137.911 1.00 49.45  ? 2074 LYS A NZ    1 
ATOM   4287  N  N     . LEU A 1 2075 ? 182.796 181.851 138.658 1.00 14.20  ? 2075 LEU A N     1 
ATOM   4288  C  CA    . LEU A 1 2075 ? 184.036 182.243 139.315 1.00 14.92  ? 2075 LEU A CA    1 
ATOM   4289  C  C     . LEU A 1 2075 ? 183.776 183.127 140.526 1.00 15.91  ? 2075 LEU A C     1 
ATOM   4290  O  O     . LEU A 1 2075 ? 184.607 183.179 141.436 1.00 19.53  ? 2075 LEU A O     1 
ATOM   4291  C  CB    . LEU A 1 2075 ? 184.961 182.949 138.325 1.00 15.58  ? 2075 LEU A CB    1 
ATOM   4292  C  CG    . LEU A 1 2075 ? 185.408 182.117 137.121 1.00 17.82  ? 2075 LEU A CG    1 
ATOM   4293  C  CD1   . LEU A 1 2075 ? 185.931 183.014 136.013 1.00 12.40  ? 2075 LEU A CD1   1 
ATOM   4294  C  CD2   . LEU A 1 2075 ? 186.447 181.079 137.518 1.00 18.62  ? 2075 LEU A CD2   1 
ATOM   4295  N  N     . CYS A 1 2076 ? 182.647 183.836 140.556 1.00 17.63  ? 2076 CYS A N     1 
ATOM   4296  C  CA    . CYS A 1 2076 ? 182.266 184.548 141.771 1.00 15.55  ? 2076 CYS A CA    1 
ATOM   4297  C  C     . CYS A 1 2076 ? 181.883 183.573 142.874 1.00 13.29  ? 2076 CYS A C     1 
ATOM   4298  O  O     . CYS A 1 2076 ? 182.215 183.787 144.045 1.00 12.24  ? 2076 CYS A O     1 
ATOM   4299  C  CB    . CYS A 1 2076 ? 181.115 185.510 141.484 1.00 11.62  ? 2076 CYS A CB    1 
ATOM   4300  S  SG    . CYS A 1 2076 ? 181.628 187.100 140.819 1.00 17.08  ? 2076 CYS A SG    1 
ATOM   4301  N  N     . ASP A 1 2077 ? 181.177 182.498 142.519 1.00 17.05  ? 2077 ASP A N     1 
ATOM   4302  C  CA    . ASP A 1 2077 ? 180.861 181.472 143.506 1.00 18.87  ? 2077 ASP A CA    1 
ATOM   4303  C  C     . ASP A 1 2077 ? 182.129 180.805 144.026 1.00 18.67  ? 2077 ASP A C     1 
ATOM   4304  O  O     . ASP A 1 2077 ? 182.236 180.498 145.218 1.00 21.62  ? 2077 ASP A O     1 
ATOM   4305  C  CB    . ASP A 1 2077 ? 179.913 180.436 142.902 1.00 17.88  ? 2077 ASP A CB    1 
ATOM   4306  C  CG    . ASP A 1 2077 ? 179.105 179.700 143.952 1.00 30.30  ? 2077 ASP A CG    1 
ATOM   4307  O  OD1   . ASP A 1 2077 ? 179.558 179.621 145.113 1.00 30.15  ? 2077 ASP A OD1   1 
ATOM   4308  O  OD2   . ASP A 1 2077 ? 178.012 179.198 143.617 1.00 33.55  ? 2077 ASP A OD2   1 
ATOM   4309  N  N     . GLU A 1 2078 ? 183.104 180.575 143.144 1.00 20.72  ? 2078 GLU A N     1 
ATOM   4310  C  CA    . GLU A 1 2078 ? 184.328 179.895 143.562 1.00 18.17  ? 2078 GLU A CA    1 
ATOM   4311  C  C     . GLU A 1 2078 ? 185.237 180.811 144.378 1.00 17.57  ? 2078 GLU A C     1 
ATOM   4312  O  O     . GLU A 1 2078 ? 185.649 180.462 145.490 1.00 24.21  ? 2078 GLU A O     1 
ATOM   4313  C  CB    . GLU A 1 2078 ? 185.071 179.356 142.338 1.00 19.64  ? 2078 GLU A CB    1 
ATOM   4314  C  CG    . GLU A 1 2078 ? 184.693 177.936 141.963 1.00 29.21  ? 2078 GLU A CG    1 
ATOM   4315  C  CD    . GLU A 1 2078 ? 184.680 177.712 140.466 1.00 44.92  ? 2078 GLU A CD    1 
ATOM   4316  O  OE1   . GLU A 1 2078 ? 185.229 178.560 139.732 1.00 41.55  ? 2078 GLU A OE1   1 
ATOM   4317  O  OE2   . GLU A 1 2078 ? 184.121 176.687 140.024 1.00 53.55  ? 2078 GLU A OE2   1 
ATOM   4318  N  N     . GLN A 1 2079 ? 185.565 181.988 143.839 1.00 17.87  ? 2079 GLN A N     1 
ATOM   4319  C  CA    . GLN A 1 2079 ? 186.621 182.817 144.415 1.00 15.91  ? 2079 GLN A CA    1 
ATOM   4320  C  C     . GLN A 1 2079 ? 186.176 183.515 145.695 1.00 16.83  ? 2079 GLN A C     1 
ATOM   4321  O  O     . GLN A 1 2079 ? 186.945 183.596 146.659 1.00 21.26  ? 2079 GLN A O     1 
ATOM   4322  C  CB    . GLN A 1 2079 ? 187.091 183.844 143.385 1.00 20.04  ? 2079 GLN A CB    1 
ATOM   4323  C  CG    . GLN A 1 2079 ? 188.245 184.718 143.850 1.00 22.19  ? 2079 GLN A CG    1 
ATOM   4324  C  CD    . GLN A 1 2079 ? 189.527 183.938 144.053 1.00 31.55  ? 2079 GLN A CD    1 
ATOM   4325  O  OE1   . GLN A 1 2079 ? 189.867 183.063 143.259 1.00 28.85  ? 2079 GLN A OE1   1 
ATOM   4326  N  NE2   . GLN A 1 2079 ? 190.247 184.251 145.124 1.00 31.44  ? 2079 GLN A NE2   1 
ATOM   4327  N  N     . LEU A 1 2080 ? 184.952 184.036 145.723 1.00 17.49  ? 2080 LEU A N     1 
ATOM   4328  C  CA    . LEU A 1 2080 ? 184.521 184.857 146.846 1.00 15.33  ? 2080 LEU A CA    1 
ATOM   4329  C  C     . LEU A 1 2080 ? 184.408 184.031 148.123 1.00 21.63  ? 2080 LEU A C     1 
ATOM   4330  O  O     . LEU A 1 2080 ? 184.205 182.815 148.091 1.00 22.81  ? 2080 LEU A O     1 
ATOM   4331  C  CB    . LEU A 1 2080 ? 183.182 185.528 146.539 1.00 12.43  ? 2080 LEU A CB    1 
ATOM   4332  C  CG    . LEU A 1 2080 ? 183.171 186.566 145.414 1.00 18.35  ? 2080 LEU A CG    1 
ATOM   4333  C  CD1   . LEU A 1 2080 ? 181.959 187.471 145.531 1.00 11.13  ? 2080 LEU A CD1   1 
ATOM   4334  C  CD2   . LEU A 1 2080 ? 184.444 187.386 145.429 1.00 17.29  ? 2080 LEU A CD2   1 
ATOM   4335  N  N     . SER A 1 2081 ? 184.551 184.712 149.257 1.00 15.31  ? 2081 SER A N     1 
ATOM   4336  C  CA    . SER A 1 2081 ? 184.469 184.055 150.550 1.00 14.26  ? 2081 SER A CA    1 
ATOM   4337  C  C     . SER A 1 2081 ? 183.052 183.554 150.808 1.00 17.22  ? 2081 SER A C     1 
ATOM   4338  O  O     . SER A 1 2081 ? 182.072 184.051 150.245 1.00 19.93  ? 2081 SER A O     1 
ATOM   4339  C  CB    . SER A 1 2081 ? 184.894 185.008 151.666 1.00 16.90  ? 2081 SER A CB    1 
ATOM   4340  O  OG    . SER A 1 2081 ? 184.030 186.130 151.733 1.00 17.35  ? 2081 SER A OG    1 
ATOM   4341  N  N     . SER A 1 2082 ? 182.952 182.553 151.676 1.00 13.70  ? 2082 SER A N     1 
ATOM   4342  C  CA    . SER A 1 2082 ? 181.670 181.935 151.992 1.00 10.78  ? 2082 SER A CA    1 
ATOM   4343  C  C     . SER A 1 2082 ? 180.935 182.800 153.008 1.00 13.88  ? 2082 SER A C     1 
ATOM   4344  O  O     . SER A 1 2082 ? 181.376 182.939 154.153 1.00 21.41  ? 2082 SER A O     1 
ATOM   4345  C  CB    . SER A 1 2082 ? 181.878 180.520 152.520 1.00 20.55  ? 2082 SER A CB    1 
ATOM   4346  O  OG    . SER A 1 2082 ? 182.189 179.626 151.465 1.00 32.51  ? 2082 SER A OG    1 
ATOM   4347  N  N     . GLN A 1 2083 ? 179.819 183.388 152.589 1.00 12.26  ? 2083 GLN A N     1 
ATOM   4348  C  CA    . GLN A 1 2083 ? 178.963 184.169 153.466 1.00 9.36   ? 2083 GLN A CA    1 
ATOM   4349  C  C     . GLN A 1 2083 ? 177.540 183.636 153.398 1.00 11.45  ? 2083 GLN A C     1 
ATOM   4350  O  O     . GLN A 1 2083 ? 177.077 183.186 152.346 1.00 16.19  ? 2083 GLN A O     1 
ATOM   4351  C  CB    . GLN A 1 2083 ? 178.987 185.657 153.097 1.00 7.77   ? 2083 GLN A CB    1 
ATOM   4352  C  CG    . GLN A 1 2083 ? 180.383 186.224 152.910 1.00 9.59   ? 2083 GLN A CG    1 
ATOM   4353  C  CD    . GLN A 1 2083 ? 181.105 186.441 154.222 1.00 8.67   ? 2083 GLN A CD    1 
ATOM   4354  O  OE1   . GLN A 1 2083 ? 180.491 186.459 155.287 1.00 13.28  ? 2083 GLN A OE1   1 
ATOM   4355  N  NE2   . GLN A 1 2083 ? 182.419 186.605 154.153 1.00 13.12  ? 2083 GLN A NE2   1 
ATOM   4356  N  N     . SER A 1 2084 ? 176.850 183.687 154.540 1.00 10.50  ? 2084 SER A N     1 
ATOM   4357  C  CA    . SER A 1 2084 ? 175.508 183.127 154.628 1.00 8.90   ? 2084 SER A CA    1 
ATOM   4358  C  C     . SER A 1 2084 ? 174.501 183.878 153.769 1.00 11.39  ? 2084 SER A C     1 
ATOM   4359  O  O     . SER A 1 2084 ? 173.450 183.319 153.440 1.00 18.68  ? 2084 SER A O     1 
ATOM   4360  C  CB    . SER A 1 2084 ? 175.042 183.114 156.083 1.00 9.92   ? 2084 SER A CB    1 
ATOM   4361  O  OG    . SER A 1 2084 ? 174.905 184.431 156.585 1.00 19.09  ? 2084 SER A OG    1 
ATOM   4362  N  N     . HIS A 1 2085 ? 174.792 185.124 153.400 1.00 9.09   ? 2085 HIS A N     1 
ATOM   4363  C  CA    . HIS A 1 2085 ? 173.900 185.924 152.574 1.00 7.30   ? 2085 HIS A CA    1 
ATOM   4364  C  C     . HIS A 1 2085 ? 174.334 185.970 151.116 1.00 9.19   ? 2085 HIS A C     1 
ATOM   4365  O  O     . HIS A 1 2085 ? 173.814 186.788 150.351 1.00 14.48  ? 2085 HIS A O     1 
ATOM   4366  C  CB    . HIS A 1 2085 ? 173.791 187.344 153.136 1.00 6.88   ? 2085 HIS A CB    1 
ATOM   4367  C  CG    . HIS A 1 2085 ? 175.074 188.114 153.099 1.00 7.18   ? 2085 HIS A CG    1 
ATOM   4368  N  ND1   . HIS A 1 2085 ? 176.129 187.844 153.942 1.00 7.75   ? 2085 HIS A ND1   1 
ATOM   4369  C  CD2   . HIS A 1 2085 ? 175.467 189.154 152.326 1.00 7.03   ? 2085 HIS A CD2   1 
ATOM   4370  C  CE1   . HIS A 1 2085 ? 177.119 188.680 153.687 1.00 7.67   ? 2085 HIS A CE1   1 
ATOM   4371  N  NE2   . HIS A 1 2085 ? 176.743 189.485 152.710 1.00 6.59   ? 2085 HIS A NE2   1 
ATOM   4372  N  N     . TYR A 1 2086 ? 175.269 185.117 150.714 1.00 8.96   ? 2086 TYR A N     1 
ATOM   4373  C  CA    . TYR A 1 2086 ? 175.747 185.087 149.341 1.00 8.69   ? 2086 TYR A CA    1 
ATOM   4374  C  C     . TYR A 1 2086 ? 174.937 184.099 148.515 1.00 11.43  ? 2086 TYR A C     1 
ATOM   4375  O  O     . TYR A 1 2086 ? 174.681 182.972 148.945 1.00 15.56  ? 2086 TYR A O     1 
ATOM   4376  C  CB    . TYR A 1 2086 ? 177.226 184.707 149.290 1.00 9.16   ? 2086 TYR A CB    1 
ATOM   4377  C  CG    . TYR A 1 2086 ? 178.165 185.871 149.480 1.00 8.94   ? 2086 TYR A CG    1 
ATOM   4378  C  CD1   . TYR A 1 2086 ? 177.692 187.113 149.878 1.00 8.62   ? 2086 TYR A CD1   1 
ATOM   4379  C  CD2   . TYR A 1 2086 ? 179.526 185.729 149.261 1.00 8.94   ? 2086 TYR A CD2   1 
ATOM   4380  C  CE1   . TYR A 1 2086 ? 178.548 188.178 150.054 1.00 8.58   ? 2086 TYR A CE1   1 
ATOM   4381  C  CE2   . TYR A 1 2086 ? 180.388 186.787 149.433 1.00 10.06  ? 2086 TYR A CE2   1 
ATOM   4382  C  CZ    . TYR A 1 2086 ? 179.895 188.009 149.831 1.00 9.45   ? 2086 TYR A CZ    1 
ATOM   4383  O  OH    . TYR A 1 2086 ? 180.754 189.067 150.004 1.00 12.19  ? 2086 TYR A OH    1 
ATOM   4384  N  N     . ASP A 1 2087 ? 174.539 184.532 147.322 1.00 12.10  ? 2087 ASP A N     1 
ATOM   4385  C  CA    . ASP A 1 2087 ? 173.828 183.666 146.389 1.00 13.47  ? 2087 ASP A CA    1 
ATOM   4386  C  C     . ASP A 1 2087 ? 174.224 184.053 144.976 1.00 12.24  ? 2087 ASP A C     1 
ATOM   4387  O  O     . ASP A 1 2087 ? 173.921 185.163 144.528 1.00 15.41  ? 2087 ASP A O     1 
ATOM   4388  C  CB    . ASP A 1 2087 ? 172.314 183.776 146.570 1.00 12.15  ? 2087 ASP A CB    1 
ATOM   4389  C  CG    . ASP A 1 2087 ? 171.548 183.031 145.497 1.00 17.60  ? 2087 ASP A CG    1 
ATOM   4390  O  OD1   . ASP A 1 2087 ? 171.607 181.784 145.484 1.00 21.44  ? 2087 ASP A OD1   1 
ATOM   4391  O  OD2   . ASP A 1 2087 ? 170.890 183.691 144.665 1.00 14.83  ? 2087 ASP A OD2   1 
ATOM   4392  N  N     . PHE A 1 2088 ? 174.899 183.145 144.282 1.00 12.98  ? 2088 PHE A N     1 
ATOM   4393  C  CA    . PHE A 1 2088 ? 175.297 183.337 142.894 1.00 11.72  ? 2088 PHE A CA    1 
ATOM   4394  C  C     . PHE A 1 2088 ? 174.713 182.238 142.019 1.00 10.04  ? 2088 PHE A C     1 
ATOM   4395  O  O     . PHE A 1 2088 ? 175.381 181.692 141.140 1.00 13.99  ? 2088 PHE A O     1 
ATOM   4396  C  CB    . PHE A 1 2088 ? 176.816 183.391 142.768 1.00 14.85  ? 2088 PHE A CB    1 
ATOM   4397  C  CG    . PHE A 1 2088 ? 177.452 184.441 143.628 1.00 14.49  ? 2088 PHE A CG    1 
ATOM   4398  C  CD1   . PHE A 1 2088 ? 177.481 185.761 143.219 1.00 13.31  ? 2088 PHE A CD1   1 
ATOM   4399  C  CD2   . PHE A 1 2088 ? 178.011 184.110 144.850 1.00 12.01  ? 2088 PHE A CD2   1 
ATOM   4400  C  CE1   . PHE A 1 2088 ? 178.059 186.731 144.009 1.00 13.26  ? 2088 PHE A CE1   1 
ATOM   4401  C  CE2   . PHE A 1 2088 ? 178.591 185.076 145.645 1.00 10.96  ? 2088 PHE A CE2   1 
ATOM   4402  C  CZ    . PHE A 1 2088 ? 178.614 186.388 145.224 1.00 9.76   ? 2088 PHE A CZ    1 
ATOM   4403  N  N     . GLY A 1 2089 ? 173.427 181.947 142.237 1.00 10.99  ? 2089 GLY A N     1 
ATOM   4404  C  CA    . GLY A 1 2089 ? 172.749 180.894 141.458 1.00 8.03   ? 2089 GLY A CA    1 
ATOM   4405  C  C     . GLY A 1 2089 ? 171.979 181.463 140.283 1.00 8.25   ? 2089 GLY A C     1 
ATOM   4406  O  O     . GLY A 1 2089 ? 172.350 182.556 139.810 1.00 12.23  ? 2089 GLY A O     1 
ATOM   4407  N  N     . LEU A 1 2090 ? 170.945 180.753 139.824 1.00 6.03   ? 2090 LEU A N     1 
ATOM   4408  C  CA    . LEU A 1 2090 ? 170.178 181.190 138.629 1.00 5.63   ? 2090 LEU A CA    1 
ATOM   4409  C  C     . LEU A 1 2090 ? 169.364 182.449 138.957 1.00 5.98   ? 2090 LEU A C     1 
ATOM   4410  O  O     . LEU A 1 2090 ? 169.297 183.344 138.096 1.00 6.56   ? 2090 LEU A O     1 
ATOM   4411  C  CB    . LEU A 1 2090 ? 169.284 180.044 138.158 1.00 6.11   ? 2090 LEU A CB    1 
ATOM   4412  C  CG    . LEU A 1 2090 ? 168.480 180.296 136.879 1.00 5.15   ? 2090 LEU A CG    1 
ATOM   4413  C  CD1   . LEU A 1 2090 ? 169.387 180.811 135.775 1.00 8.63   ? 2090 LEU A CD1   1 
ATOM   4414  C  CD2   . LEU A 1 2090 ? 167.798 179.009 136.449 1.00 5.37   ? 2090 LEU A CD2   1 
ATOM   4415  N  N     . ARG A 1 2091 ? 168.764 182.504 140.148 1.00 6.54   ? 2091 ARG A N     1 
ATOM   4416  C  CA    . ARG A 1 2091 ? 167.921 183.667 140.530 1.00 4.84   ? 2091 ARG A CA    1 
ATOM   4417  C  C     . ARG A 1 2091 ? 168.777 184.940 140.463 1.00 6.74   ? 2091 ARG A C     1 
ATOM   4418  O  O     . ARG A 1 2091 ? 168.252 185.984 140.024 1.00 9.26   ? 2091 ARG A O     1 
ATOM   4419  C  CB    . ARG A 1 2091 ? 167.311 183.458 141.920 1.00 5.28   ? 2091 ARG A CB    1 
ATOM   4420  C  CG    . ARG A 1 2091 ? 166.063 182.588 141.926 1.00 7.55   ? 2091 ARG A CG    1 
ATOM   4421  C  CD    . ARG A 1 2091 ? 165.398 182.552 143.292 1.00 6.50   ? 2091 ARG A CD    1 
ATOM   4422  N  NE    . ARG A 1 2091 ? 164.174 181.744 143.277 1.00 9.64   ? 2091 ARG A NE    1 
ATOM   4423  C  CZ    . ARG A 1 2091 ? 163.989 180.651 144.004 1.00 6.95   ? 2091 ARG A CZ    1 
ATOM   4424  N  NH1   . ARG A 1 2091 ? 164.905 180.276 144.877 1.00 7.76   ? 2091 ARG A NH1   1 
ATOM   4425  N  NH2   . ARG A 1 2091 ? 162.889 179.936 143.854 1.00 6.74   ? 2091 ARG A NH2   1 
ATOM   4426  N  N     . ALA A 1 2092 ? 170.043 184.847 140.876 1.00 7.48   ? 2092 ALA A N     1 
ATOM   4427  C  CA    . ALA A 1 2092 ? 170.959 186.008 140.817 1.00 5.11   ? 2092 ALA A CA    1 
ATOM   4428  C  C     . ALA A 1 2092 ? 171.183 186.411 139.359 1.00 7.46   ? 2092 ALA A C     1 
ATOM   4429  O  O     . ALA A 1 2092 ? 171.046 187.609 139.036 1.00 9.89   ? 2092 ALA A O     1 
ATOM   4430  C  CB    . ALA A 1 2092 ? 172.259 185.654 141.500 1.00 7.03   ? 2092 ALA A CB    1 
ATOM   4431  N  N     . LEU A 1 2093 ? 171.506 185.439 138.501 1.00 8.27   ? 2093 LEU A N     1 
ATOM   4432  C  CA    . LEU A 1 2093 ? 171.730 185.724 137.061 1.00 6.03   ? 2093 LEU A CA    1 
ATOM   4433  C  C     . LEU A 1 2093 ? 170.418 186.232 136.452 1.00 7.99   ? 2093 LEU A C     1 
ATOM   4434  O  O     . LEU A 1 2093 ? 170.463 187.207 135.673 1.00 13.25  ? 2093 LEU A O     1 
ATOM   4435  C  CB    . LEU A 1 2093 ? 172.221 184.471 136.340 1.00 6.63   ? 2093 LEU A CB    1 
ATOM   4436  C  CG    . LEU A 1 2093 ? 172.564 184.653 134.859 1.00 10.78  ? 2093 LEU A CG    1 
ATOM   4437  C  CD1   . LEU A 1 2093 ? 174.056 184.847 134.650 1.00 9.14   ? 2093 LEU A CD1   1 
ATOM   4438  C  CD2   . LEU A 1 2093 ? 172.036 183.511 134.011 1.00 11.21  ? 2093 LEU A CD2   1 
ATOM   4439  N  N     . LYS A 1 2094 ? 169.301 185.595 136.803 1.00 6.08   ? 2094 LYS A N     1 
ATOM   4440  C  CA    . LYS A 1 2094 ? 167.981 185.996 136.257 1.00 7.91   ? 2094 LYS A CA    1 
ATOM   4441  C  C     . LYS A 1 2094 ? 167.731 187.466 136.610 1.00 8.00   ? 2094 LYS A C     1 
ATOM   4442  O  O     . LYS A 1 2094 ? 167.337 188.235 135.708 1.00 13.01  ? 2094 LYS A O     1 
ATOM   4443  C  CB    . LYS A 1 2094 ? 166.888 185.099 136.845 1.00 8.09   ? 2094 LYS A CB    1 
ATOM   4444  C  CG    . LYS A 1 2094 ? 165.486 185.312 136.297 1.00 12.01  ? 2094 LYS A CG    1 
ATOM   4445  C  CD    . LYS A 1 2094 ? 165.267 184.682 134.928 1.00 10.02  ? 2094 LYS A CD    1 
ATOM   4446  C  CE    . LYS A 1 2094 ? 163.865 184.883 134.450 1.00 12.03  ? 2094 LYS A CE    1 
ATOM   4447  N  NZ    . LYS A 1 2094 ? 162.888 184.445 135.448 1.00 16.64  ? 2094 LYS A NZ    1 
ATOM   4448  N  N     . SER A 1 2095 ? 167.963 187.835 137.872 1.00 5.95   ? 2095 SER A N     1 
ATOM   4449  C  CA    . SER A 1 2095 ? 167.774 189.243 138.303 1.00 8.00   ? 2095 SER A CA    1 
ATOM   4450  C  C     . SER A 1 2095 ? 168.723 190.136 137.499 1.00 8.69   ? 2095 SER A C     1 
ATOM   4451  O  O     . SER A 1 2095 ? 168.299 191.236 137.087 1.00 10.71  ? 2095 SER A O     1 
ATOM   4452  C  CB    . SER A 1 2095 ? 167.999 189.394 139.781 1.00 8.32   ? 2095 SER A CB    1 
ATOM   4453  O  OG    . SER A 1 2095 ? 169.344 189.090 140.120 1.00 14.50  ? 2095 SER A OG    1 
ATOM   4454  N  N     . VAL A 1 2096 ? 169.952 189.667 137.281 1.00 8.50   ? 2096 VAL A N     1 
ATOM   4455  C  CA    . VAL A 1 2096 ? 170.935 190.451 136.536 1.00 7.25   ? 2096 VAL A CA    1 
ATOM   4456  C  C     . VAL A 1 2096 ? 170.474 190.657 135.099 1.00 7.81   ? 2096 VAL A C     1 
ATOM   4457  O  O     . VAL A 1 2096 ? 170.585 191.757 134.551 1.00 8.43   ? 2096 VAL A O     1 
ATOM   4458  C  CB    . VAL A 1 2096 ? 172.320 189.778 136.599 1.00 7.84   ? 2096 VAL A CB    1 
ATOM   4459  C  CG1   . VAL A 1 2096 ? 173.221 190.303 135.494 1.00 8.77   ? 2096 VAL A CG1   1 
ATOM   4460  C  CG2   . VAL A 1 2096 ? 172.960 190.009 137.954 1.00 10.48  ? 2096 VAL A CG2   1 
ATOM   4461  N  N     . LEU A 1 2097 ? 169.941 189.609 134.469 1.00 8.73   ? 2097 LEU A N     1 
ATOM   4462  C  CA    . LEU A 1 2097 ? 169.501 189.713 133.080 1.00 8.46   ? 2097 LEU A CA    1 
ATOM   4463  C  C     . LEU A 1 2097 ? 168.285 190.624 132.941 1.00 9.25   ? 2097 LEU A C     1 
ATOM   4464  O  O     . LEU A 1 2097 ? 168.210 191.432 132.005 1.00 13.25  ? 2097 LEU A O     1 
ATOM   4465  C  CB    . LEU A 1 2097 ? 169.197 188.324 132.522 1.00 9.77   ? 2097 LEU A CB    1 
ATOM   4466  C  CG    . LEU A 1 2097 ? 170.358 187.328 132.462 1.00 7.20   ? 2097 LEU A CG    1 
ATOM   4467  C  CD1   . LEU A 1 2097 ? 169.834 185.929 132.195 1.00 8.40   ? 2097 LEU A CD1   1 
ATOM   4468  C  CD2   . LEU A 1 2097 ? 171.383 187.729 131.415 1.00 6.22   ? 2097 LEU A CD2   1 
ATOM   4469  N  N     . VAL A 1 2098 ? 167.316 190.504 133.853 1.00 9.65   ? 2098 VAL A N     1 
ATOM   4470  C  CA    . VAL A 1 2098 ? 166.152 191.386 133.804 1.00 11.88  ? 2098 VAL A CA    1 
ATOM   4471  C  C     . VAL A 1 2098 ? 166.576 192.835 134.015 1.00 12.57  ? 2098 VAL A C     1 
ATOM   4472  O  O     . VAL A 1 2098 ? 166.105 193.747 133.319 1.00 16.18  ? 2098 VAL A O     1 
ATOM   4473  C  CB    . VAL A 1 2098 ? 165.097 190.944 134.836 1.00 11.46  ? 2098 VAL A CB    1 
ATOM   4474  C  CG1   . VAL A 1 2098 ? 163.936 191.924 134.862 1.00 16.66  ? 2098 VAL A CG1   1 
ATOM   4475  C  CG2   . VAL A 1 2098 ? 164.596 189.548 134.514 1.00 7.69   ? 2098 VAL A CG2   1 
ATOM   4476  N  N     . SER A 1 2099 ? 167.479 193.068 134.970 1.00 12.24  ? 2099 SER A N     1 
ATOM   4477  C  CA    . SER A 1 2099 ? 167.986 194.414 135.197 1.00 14.39  ? 2099 SER A CA    1 
ATOM   4478  C  C     . SER A 1 2099 ? 168.752 194.926 133.986 1.00 14.17  ? 2099 SER A C     1 
ATOM   4479  O  O     . SER A 1 2099 ? 168.693 196.115 133.670 1.00 19.65  ? 2099 SER A O     1 
ATOM   4480  C  CB    . SER A 1 2099 ? 168.869 194.436 136.445 1.00 11.66  ? 2099 SER A CB    1 
ATOM   4481  O  OG    . SER A 1 2099 ? 169.612 195.638 136.525 1.00 24.09  ? 2099 SER A OG    1 
ATOM   4482  N  N     . ALA A 1 2100 ? 169.481 194.046 133.297 1.00 12.76  ? 2100 ALA A N     1 
ATOM   4483  C  CA    . ALA A 1 2100 ? 170.206 194.458 132.100 1.00 12.16  ? 2100 ALA A CA    1 
ATOM   4484  C  C     . ALA A 1 2100 ? 169.248 194.879 130.995 1.00 14.39  ? 2100 ALA A C     1 
ATOM   4485  O  O     . ALA A 1 2100 ? 169.484 195.878 130.308 1.00 22.29  ? 2100 ALA A O     1 
ATOM   4486  C  CB    . ALA A 1 2100 ? 171.116 193.329 131.620 1.00 12.44  ? 2100 ALA A CB    1 
ATOM   4487  N  N     . GLY A 1 2101 ? 168.164 194.126 130.807 1.00 12.17  ? 2101 GLY A N     1 
ATOM   4488  C  CA    . GLY A 1 2101 ? 167.159 194.534 129.836 1.00 13.92  ? 2101 GLY A CA    1 
ATOM   4489  C  C     . GLY A 1 2101 ? 166.522 195.868 130.184 1.00 19.94  ? 2101 GLY A C     1 
ATOM   4490  O  O     . GLY A 1 2101 ? 166.347 196.734 129.318 1.00 18.65  ? 2101 GLY A O     1 
ATOM   4491  N  N     . ASN A 1 2102 ? 166.179 196.057 131.462 1.00 18.35  ? 2102 ASN A N     1 
ATOM   4492  C  CA    . ASN A 1 2102 ? 165.602 197.327 131.893 1.00 18.10  ? 2102 ASN A CA    1 
ATOM   4493  C  C     . ASN A 1 2102 ? 166.583 198.478 131.697 1.00 23.65  ? 2102 ASN A C     1 
ATOM   4494  O  O     . ASN A 1 2102 ? 166.195 199.568 131.260 1.00 28.37  ? 2102 ASN A O     1 
ATOM   4495  C  CB    . ASN A 1 2102 ? 165.169 197.236 133.356 1.00 21.72  ? 2102 ASN A CB    1 
ATOM   4496  C  CG    . ASN A 1 2102 ? 163.955 196.350 133.550 1.00 25.68  ? 2102 ASN A CG    1 
ATOM   4497  O  OD1   . ASN A 1 2102 ? 163.315 195.934 132.586 1.00 29.70  ? 2102 ASN A OD1   1 
ATOM   4498  N  ND2   . ASN A 1 2102 ? 163.637 196.053 134.803 1.00 22.54  ? 2102 ASN A ND2   1 
ATOM   4499  N  N     . VAL A 1 2103 ? 167.858 198.252 132.018 1.00 23.95  ? 2103 VAL A N     1 
ATOM   4500  C  CA    . VAL A 1 2103 ? 168.878 199.281 131.853 1.00 22.38  ? 2103 VAL A CA    1 
ATOM   4501  C  C     . VAL A 1 2103 ? 169.066 199.615 130.381 1.00 22.72  ? 2103 VAL A C     1 
ATOM   4502  O  O     . VAL A 1 2103 ? 169.263 200.779 130.018 1.00 30.54  ? 2103 VAL A O     1 
ATOM   4503  C  CB    . VAL A 1 2103 ? 170.196 198.829 132.510 1.00 16.42  ? 2103 VAL A CB    1 
ATOM   4504  C  CG1   . VAL A 1 2103 ? 171.363 199.665 132.012 1.00 15.83  ? 2103 VAL A CG1   1 
ATOM   4505  C  CG2   . VAL A 1 2103 ? 170.089 198.918 134.022 1.00 22.51  ? 2103 VAL A CG2   1 
ATOM   4506  N  N     . LYS A 1 2104 ? 169.018 198.605 129.510 1.00 18.66  ? 2104 LYS A N     1 
ATOM   4507  C  CA    . LYS A 1 2104 ? 169.122 198.866 128.079 1.00 21.70  ? 2104 LYS A CA    1 
ATOM   4508  C  C     . LYS A 1 2104 ? 167.953 199.711 127.593 1.00 25.22  ? 2104 LYS A C     1 
ATOM   4509  O  O     . LYS A 1 2104 ? 168.141 200.653 126.813 1.00 24.55  ? 2104 LYS A O     1 
ATOM   4510  C  CB    . LYS A 1 2104 ? 169.197 197.551 127.304 1.00 18.14  ? 2104 LYS A CB    1 
ATOM   4511  C  CG    . LYS A 1 2104 ? 169.660 197.721 125.868 1.00 18.40  ? 2104 LYS A CG    1 
ATOM   4512  C  CD    . LYS A 1 2104 ? 169.683 196.403 125.116 1.00 13.26  ? 2104 LYS A CD    1 
ATOM   4513  C  CE    . LYS A 1 2104 ? 168.289 195.964 124.717 1.00 17.52  ? 2104 LYS A CE    1 
ATOM   4514  N  NZ    . LYS A 1 2104 ? 167.666 196.911 123.754 1.00 31.35  ? 2104 LYS A NZ    1 
ATOM   4515  N  N     . ARG A 1 2105 ? 166.738 199.397 128.052 1.00 27.86  ? 2105 ARG A N     1 
ATOM   4516  C  CA    . ARG A 1 2105 ? 165.585 200.209 127.665 1.00 23.74  ? 2105 ARG A CA    1 
ATOM   4517  C  C     . ARG A 1 2105 ? 165.730 201.644 128.161 1.00 27.77  ? 2105 ARG A C     1 
ATOM   4518  O  O     . ARG A 1 2105 ? 165.441 202.597 127.426 1.00 35.53  ? 2105 ARG A O     1 
ATOM   4519  C  CB    . ARG A 1 2105 ? 164.293 199.592 128.199 1.00 24.17  ? 2105 ARG A CB    1 
ATOM   4520  C  CG    . ARG A 1 2105 ? 163.922 198.270 127.561 1.00 29.45  ? 2105 ARG A CG    1 
ATOM   4521  C  CD    . ARG A 1 2105 ? 162.631 197.729 128.146 1.00 31.31  ? 2105 ARG A CD    1 
ATOM   4522  N  NE    . ARG A 1 2105 ? 162.240 196.466 127.532 1.00 33.76  ? 2105 ARG A NE    1 
ATOM   4523  C  CZ    . ARG A 1 2105 ? 162.602 195.274 127.984 1.00 37.21  ? 2105 ARG A CZ    1 
ATOM   4524  N  NH1   . ARG A 1 2105 ? 163.350 195.145 129.067 1.00 29.22  ? 2105 ARG A NH1   1 
ATOM   4525  N  NH2   . ARG A 1 2105 ? 162.200 194.184 127.337 1.00 45.73  ? 2105 ARG A NH2   1 
ATOM   4526  N  N     . GLU A 1 2106 ? 166.181 201.816 129.406 1.00 29.50  ? 2106 GLU A N     1 
ATOM   4527  C  CA    . GLU A 1 2106 ? 166.346 203.157 129.959 1.00 31.91  ? 2106 GLU A CA    1 
ATOM   4528  C  C     . GLU A 1 2106 ? 167.424 203.939 129.218 1.00 34.60  ? 2106 GLU A C     1 
ATOM   4529  O  O     . GLU A 1 2106 ? 167.268 205.140 128.974 1.00 41.17  ? 2106 GLU A O     1 
ATOM   4530  C  CB    . GLU A 1 2106 ? 166.669 203.073 131.450 1.00 33.57  ? 2106 GLU A CB    1 
ATOM   4531  C  CG    . GLU A 1 2106 ? 165.526 202.541 132.299 1.00 48.76  ? 2106 GLU A CG    1 
ATOM   4532  C  CD    . GLU A 1 2106 ? 165.884 202.450 133.769 1.00 62.70  ? 2106 GLU A CD    1 
ATOM   4533  O  OE1   . GLU A 1 2106 ? 167.062 202.683 134.110 1.00 62.71  ? 2106 GLU A OE1   1 
ATOM   4534  O  OE2   . GLU A 1 2106 ? 164.987 202.147 134.584 1.00 64.15  ? 2106 GLU A OE2   1 
ATOM   4535  N  N     . ARG A 1 2107 ? 168.527 203.281 128.856 1.00 33.96  ? 2107 ARG A N     1 
ATOM   4536  C  CA    . ARG A 1 2107 ? 169.579 203.952 128.101 1.00 33.13  ? 2107 ARG A CA    1 
ATOM   4537  C  C     . ARG A 1 2107 ? 169.099 204.336 126.708 1.00 37.88  ? 2107 ARG A C     1 
ATOM   4538  O  O     . ARG A 1 2107 ? 169.441 205.412 126.202 1.00 46.71  ? 2107 ARG A O     1 
ATOM   4539  C  CB    . ARG A 1 2107 ? 170.816 203.059 128.015 1.00 32.55  ? 2107 ARG A CB    1 
ATOM   4540  C  CG    . ARG A 1 2107 ? 172.053 203.774 127.504 1.00 41.55  ? 2107 ARG A CG    1 
ATOM   4541  C  CD    . ARG A 1 2107 ? 173.320 203.011 127.847 1.00 33.97  ? 2107 ARG A CD    1 
ATOM   4542  N  NE    . ARG A 1 2107 ? 173.433 202.744 129.275 1.00 30.41  ? 2107 ARG A NE    1 
ATOM   4543  C  CZ    . ARG A 1 2107 ? 174.547 202.348 129.874 1.00 30.06  ? 2107 ARG A CZ    1 
ATOM   4544  N  NH1   . ARG A 1 2107 ? 175.670 202.176 129.198 1.00 30.53  ? 2107 ARG A NH1   1 
ATOM   4545  N  NH2   . ARG A 1 2107 ? 174.534 202.120 131.184 1.00 28.80  ? 2107 ARG A NH2   1 
ATOM   4546  N  N     . ILE A 1 2108 ? 168.308 203.469 126.072 1.00 34.87  ? 2108 ILE A N     1 
ATOM   4547  C  CA    . ILE A 1 2108 ? 167.740 203.805 124.770 1.00 35.66  ? 2108 ILE A CA    1 
ATOM   4548  C  C     . ILE A 1 2108 ? 166.824 205.016 124.890 1.00 42.47  ? 2108 ILE A C     1 
ATOM   4549  O  O     . ILE A 1 2108 ? 166.863 205.926 124.055 1.00 53.51  ? 2108 ILE A O     1 
ATOM   4550  C  CB    . ILE A 1 2108 ? 167.007 202.588 124.176 1.00 32.73  ? 2108 ILE A CB    1 
ATOM   4551  C  CG1   . ILE A 1 2108 ? 168.016 201.545 123.694 1.00 28.01  ? 2108 ILE A CG1   1 
ATOM   4552  C  CG2   . ILE A 1 2108 ? 166.095 203.012 123.037 1.00 34.60  ? 2108 ILE A CG2   1 
ATOM   4553  C  CD1   . ILE A 1 2108 ? 167.385 200.253 123.240 1.00 25.13  ? 2108 ILE A CD1   1 
ATOM   4554  N  N     . GLN A 1 2109 ? 165.997 205.053 125.937 1.00 39.31  ? 2109 GLN A N     1 
ATOM   4555  C  CA    . GLN A 1 2109 ? 165.119 206.202 126.144 1.00 38.88  ? 2109 GLN A CA    1 
ATOM   4556  C  C     . GLN A 1 2109 ? 165.919 207.475 126.404 1.00 52.16  ? 2109 GLN A C     1 
ATOM   4557  O  O     . GLN A 1 2109 ? 165.546 208.560 125.940 1.00 62.84  ? 2109 GLN A O     1 
ATOM   4558  C  CB    . GLN A 1 2109 ? 164.160 205.927 127.302 1.00 38.91  ? 2109 GLN A CB    1 
ATOM   4559  C  CG    . GLN A 1 2109 ? 163.095 204.890 126.992 1.00 48.55  ? 2109 GLN A CG    1 
ATOM   4560  C  CD    . GLN A 1 2109 ? 162.082 205.376 125.976 1.00 56.70  ? 2109 GLN A CD    1 
ATOM   4561  O  OE1   . GLN A 1 2109 ? 162.306 205.289 124.768 1.00 60.84  ? 2109 GLN A OE1   1 
ATOM   4562  N  NE2   . GLN A 1 2109 ? 160.959 205.892 126.461 1.00 56.69  ? 2109 GLN A NE2   1 
ATOM   4563  N  N     . LYS A 1 2110 ? 167.012 207.365 127.163 1.00 53.76  ? 2110 LYS A N     1 
ATOM   4564  C  CA    . LYS A 1 2110 ? 167.847 208.530 127.433 1.00 53.87  ? 2110 LYS A CA    1 
ATOM   4565  C  C     . LYS A 1 2110 ? 168.486 209.059 126.157 1.00 56.50  ? 2110 LYS A C     1 
ATOM   4566  O  O     . LYS A 1 2110 ? 168.504 210.272 125.919 1.00 68.42  ? 2110 LYS A O     1 
ATOM   4567  C  CB    . LYS A 1 2110 ? 168.919 208.180 128.466 1.00 54.00  ? 2110 LYS A CB    1 
ATOM   4568  C  CG    . LYS A 1 2110 ? 169.908 209.301 128.733 1.00 60.02  ? 2110 LYS A CG    1 
ATOM   4569  C  CD    . LYS A 1 2110 ? 171.122 208.795 129.489 1.00 58.09  ? 2110 LYS A CD    1 
ATOM   4570  C  CE    . LYS A 1 2110 ? 171.903 207.788 128.660 1.00 59.36  ? 2110 LYS A CE    1 
ATOM   4571  N  NZ    . LYS A 1 2110 ? 172.431 208.389 127.405 1.00 62.18  ? 2110 LYS A NZ    1 
ATOM   4572  N  N     . ILE A 1 2111 ? 169.014 208.162 125.323 1.00 51.67  ? 2111 ILE A N     1 
ATOM   4573  C  CA    . ILE A 1 2111 ? 169.569 208.586 124.042 1.00 57.44  ? 2111 ILE A CA    1 
ATOM   4574  C  C     . ILE A 1 2111 ? 168.480 209.200 123.171 1.00 61.60  ? 2111 ILE A C     1 
ATOM   4575  O  O     . ILE A 1 2111 ? 168.722 210.171 122.446 1.00 63.87  ? 2111 ILE A O     1 
ATOM   4576  C  CB    . ILE A 1 2111 ? 170.272 207.407 123.342 1.00 55.51  ? 2111 ILE A CB    1 
ATOM   4577  C  CG1   . ILE A 1 2111 ? 171.459 206.925 124.177 1.00 49.57  ? 2111 ILE A CG1   1 
ATOM   4578  C  CG2   . ILE A 1 2111 ? 170.732 207.801 121.947 1.00 53.48  ? 2111 ILE A CG2   1 
ATOM   4579  C  CD1   . ILE A 1 2111 ? 172.050 205.618 123.702 1.00 48.39  ? 2111 ILE A CD1   1 
ATOM   4580  N  N     . LYS A 1 2112 ? 167.261 208.659 123.240 1.00 60.14  ? 2112 LYS A N     1 
ATOM   4581  C  CA    . LYS A 1 2112 ? 166.162 209.208 122.453 1.00 60.86  ? 2112 LYS A CA    1 
ATOM   4582  C  C     . LYS A 1 2112 ? 165.832 210.635 122.873 1.00 65.31  ? 2112 LYS A C     1 
ATOM   4583  O  O     . LYS A 1 2112 ? 165.676 211.518 122.021 1.00 72.64  ? 2112 LYS A O     1 
ATOM   4584  C  CB    . LYS A 1 2112 ? 164.928 208.314 122.581 1.00 59.00  ? 2112 LYS A CB    1 
ATOM   4585  C  CG    . LYS A 1 2112 ? 164.911 207.148 121.611 1.00 64.77  ? 2112 LYS A CG    1 
ATOM   4586  C  CD    . LYS A 1 2112 ? 163.495 206.666 121.349 1.00 68.27  ? 2112 LYS A CD    1 
ATOM   4587  C  CE    . LYS A 1 2112 ? 163.474 205.606 120.261 1.00 68.22  ? 2112 LYS A CE    1 
ATOM   4588  N  NZ    . LYS A 1 2112 ? 162.431 204.572 120.506 1.00 75.03  ? 2112 LYS A NZ    1 
ATOM   4589  N  N     . ARG A 1 2113 ? 165.726 210.888 124.180 1.00 65.42  ? 2113 ARG A N     1 
ATOM   4590  C  CA    . ARG A 1 2113 ? 165.403 212.245 124.616 1.00 67.78  ? 2113 ARG A CA    1 
ATOM   4591  C  C     . ARG A 1 2113 ? 166.565 213.198 124.357 1.00 69.65  ? 2113 ARG A C     1 
ATOM   4592  O  O     . ARG A 1 2113 ? 166.353 214.376 124.039 1.00 74.53  ? 2113 ARG A O     1 
ATOM   4593  C  CB    . ARG A 1 2113 ? 164.989 212.280 126.091 1.00 59.73  ? 2113 ARG A CB    1 
ATOM   4594  C  CG    . ARG A 1 2113 ? 166.052 211.911 127.112 1.00 63.42  ? 2113 ARG A CG    1 
ATOM   4595  C  CD    . ARG A 1 2113 ? 165.477 212.040 128.523 1.00 66.69  ? 2113 ARG A CD    1 
ATOM   4596  N  NE    . ARG A 1 2113 ? 164.387 211.108 128.786 1.00 74.21  ? 2113 ARG A NE    1 
ATOM   4597  C  CZ    . ARG A 1 2113 ? 164.545 209.878 129.252 1.00 68.14  ? 2113 ARG A CZ    1 
ATOM   4598  N  NH1   . ARG A 1 2113 ? 165.732 209.421 129.608 1.00 64.95  ? 2113 ARG A NH1   1 
ATOM   4599  N  NH2   . ARG A 1 2113 ? 163.479 209.094 129.389 1.00 61.57  ? 2113 ARG A NH2   1 
ATOM   4600  N  N     . GLU A 1 2114 ? 167.803 212.709 124.481 1.00 68.65  ? 2114 GLU A N     1 
ATOM   4601  C  CA    . GLU A 1 2114 ? 168.960 213.536 124.153 1.00 74.05  ? 2114 GLU A CA    1 
ATOM   4602  C  C     . GLU A 1 2114 ? 168.963 213.914 122.677 1.00 77.62  ? 2114 GLU A C     1 
ATOM   4603  O  O     . GLU A 1 2114 ? 169.282 215.054 122.320 1.00 78.01  ? 2114 GLU A O     1 
ATOM   4604  C  CB    . GLU A 1 2114 ? 170.246 212.800 124.534 1.00 75.66  ? 2114 GLU A CB    1 
ATOM   4605  C  CG    . GLU A 1 2114 ? 171.513 213.638 124.461 1.00 78.33  ? 2114 GLU A CG    1 
ATOM   4606  C  CD    . GLU A 1 2114 ? 172.093 213.708 123.062 1.00 87.16  ? 2114 GLU A CD    1 
ATOM   4607  O  OE1   . GLU A 1 2114 ? 171.896 212.750 122.287 1.00 84.56  ? 2114 GLU A OE1   1 
ATOM   4608  O  OE2   . GLU A 1 2114 ? 172.749 214.719 122.739 1.00 91.37  ? 2114 GLU A OE2   1 
ATOM   4609  N  N     . LYS A 1 2115 ? 168.620 212.966 121.804 1.00 78.78  ? 2115 LYS A N     1 
ATOM   4610  C  CA    . LYS A 1 2115 ? 168.512 213.265 120.381 1.00 79.23  ? 2115 LYS A CA    1 
ATOM   4611  C  C     . LYS A 1 2115 ? 167.378 214.244 120.112 1.00 78.24  ? 2115 LYS A C     1 
ATOM   4612  O  O     . LYS A 1 2115 ? 167.492 215.116 119.244 1.00 78.73  ? 2115 LYS A O     1 
ATOM   4613  C  CB    . LYS A 1 2115 ? 168.304 211.972 119.591 1.00 75.97  ? 2115 LYS A CB    1 
ATOM   4614  C  CG    . LYS A 1 2115 ? 169.580 211.199 119.305 1.00 74.85  ? 2115 LYS A CG    1 
ATOM   4615  C  CD    . LYS A 1 2115 ? 169.348 210.136 118.243 1.00 78.53  ? 2115 LYS A CD    1 
ATOM   4616  C  CE    . LYS A 1 2115 ? 170.617 209.837 117.466 1.00 77.86  ? 2115 LYS A CE    1 
ATOM   4617  N  NZ    . LYS A 1 2115 ? 170.828 208.373 117.303 1.00 77.65  ? 2115 LYS A NZ    1 
ATOM   4618  N  N     . GLU A 1 2116 ? 166.265 214.103 120.834 1.00 76.73  ? 2116 GLU A N     1 
ATOM   4619  C  CA    . GLU A 1 2116 ? 165.147 215.022 120.649 1.00 75.08  ? 2116 GLU A CA    1 
ATOM   4620  C  C     . GLU A 1 2116 ? 165.526 216.446 121.038 1.00 81.57  ? 2116 GLU A C     1 
ATOM   4621  O  O     . GLU A 1 2116 ? 165.184 217.399 120.328 1.00 81.28  ? 2116 GLU A O     1 
ATOM   4622  C  CB    . GLU A 1 2116 ? 163.938 214.550 121.455 1.00 72.53  ? 2116 GLU A CB    1 
ATOM   4623  C  CG    . GLU A 1 2116 ? 162.699 215.408 121.258 1.00 75.70  ? 2116 GLU A CG    1 
ATOM   4624  C  CD    . GLU A 1 2116 ? 161.501 214.890 122.027 1.00 79.42  ? 2116 GLU A CD    1 
ATOM   4625  O  OE1   . GLU A 1 2116 ? 161.642 213.870 122.733 1.00 79.07  ? 2116 GLU A OE1   1 
ATOM   4626  O  OE2   . GLU A 1 2116 ? 160.419 215.504 121.926 1.00 81.53  ? 2116 GLU A OE2   1 
ATOM   4627  N  N     . GLU A 1 2117 ? 166.231 216.615 122.158 1.00 84.64  ? 2117 GLU A N     1 
ATOM   4628  C  CA    . GLU A 1 2117 ? 166.619 217.953 122.589 1.00 83.78  ? 2117 GLU A CA    1 
ATOM   4629  C  C     . GLU A 1 2117 ? 167.787 218.523 121.792 1.00 85.15  ? 2117 GLU A C     1 
ATOM   4630  O  O     . GLU A 1 2117 ? 167.935 219.748 121.737 1.00 89.82  ? 2117 GLU A O     1 
ATOM   4631  C  CB    . GLU A 1 2117 ? 166.955 217.954 124.086 1.00 89.38  ? 2117 GLU A CB    1 
ATOM   4632  C  CG    . GLU A 1 2117 ? 168.119 217.062 124.500 1.00 91.00  ? 2117 GLU A CG    1 
ATOM   4633  C  CD    . GLU A 1 2117 ? 169.469 217.749 124.384 1.00 96.76  ? 2117 GLU A CD    1 
ATOM   4634  O  OE1   . GLU A 1 2117 ? 169.503 218.998 124.352 1.00 98.19  ? 2117 GLU A OE1   1 
ATOM   4635  O  OE2   . GLU A 1 2117 ? 170.496 217.040 124.331 1.00 92.13  ? 2117 GLU A OE2   1 
ATOM   4636  N  N     . ARG A 1 2118 ? 168.609 217.677 121.173 1.00 86.47  ? 2118 ARG A N     1 
ATOM   4637  C  CA    . ARG A 1 2118 ? 169.740 218.120 120.358 1.00 83.01  ? 2118 ARG A CA    1 
ATOM   4638  C  C     . ARG A 1 2118 ? 169.553 217.536 118.961 1.00 86.69  ? 2118 ARG A C     1 
ATOM   4639  O  O     . ARG A 1 2118 ? 169.846 216.360 118.726 1.00 88.30  ? 2118 ARG A O     1 
ATOM   4640  C  CB    . ARG A 1 2118 ? 171.070 217.692 120.974 1.00 84.83  ? 2118 ARG A CB    1 
ATOM   4641  C  CG    . ARG A 1 2118 ? 172.255 217.747 120.018 1.00 86.26  ? 2118 ARG A CG    1 
ATOM   4642  C  CD    . ARG A 1 2118 ? 173.425 216.930 120.536 1.00 86.52  ? 2118 ARG A CD    1 
ATOM   4643  N  NE    . ARG A 1 2118 ? 174.365 216.589 119.476 1.00 86.52  ? 2118 ARG A NE    1 
ATOM   4644  C  CZ    . ARG A 1 2118 ? 174.560 215.361 119.014 1.00 83.86  ? 2118 ARG A CZ    1 
ATOM   4645  N  NH1   . ARG A 1 2118 ? 173.888 214.327 119.495 1.00 79.34  ? 2118 ARG A NH1   1 
ATOM   4646  N  NH2   . ARG A 1 2118 ? 175.450 215.165 118.046 1.00 78.87  ? 2118 ARG A NH2   1 
ATOM   4647  N  N     . GLY A 1 2119 ? 169.064 218.355 118.037 1.00 80.99  ? 2119 GLY A N     1 
ATOM   4648  C  CA    . GLY A 1 2119 ? 168.784 217.889 116.697 1.00 82.39  ? 2119 GLY A CA    1 
ATOM   4649  C  C     . GLY A 1 2119 ? 167.436 217.198 116.597 1.00 83.22  ? 2119 GLY A C     1 
ATOM   4650  O  O     . GLY A 1 2119 ? 166.634 217.175 117.534 1.00 82.44  ? 2119 GLY A O     1 
ATOM   4651  N  N     . GLU A 1 2120 ? 167.189 216.625 115.416 1.00 86.97  ? 2120 GLU A N     1 
ATOM   4652  C  CA    . GLU A 1 2120 ? 165.925 215.944 115.163 1.00 96.40  ? 2120 GLU A CA    1 
ATOM   4653  C  C     . GLU A 1 2120 ? 166.102 214.601 114.462 1.00 94.58  ? 2120 GLU A C     1 
ATOM   4654  O  O     . GLU A 1 2120 ? 165.099 213.995 114.064 1.00 95.41  ? 2120 GLU A O     1 
ATOM   4655  C  CB    . GLU A 1 2120 ? 164.987 216.834 114.335 1.00 97.19  ? 2120 GLU A CB    1 
ATOM   4656  C  CG    . GLU A 1 2120 ? 164.525 218.094 115.051 1.00 94.86  ? 2120 GLU A CG    1 
ATOM   4657  C  CD    . GLU A 1 2120 ? 163.625 218.958 114.191 1.00 96.69  ? 2120 GLU A CD    1 
ATOM   4658  O  OE1   . GLU A 1 2120 ? 162.510 218.507 113.854 1.00 99.77  ? 2120 GLU A OE1   1 
ATOM   4659  O  OE2   . GLU A 1 2120 ? 164.033 220.088 113.851 1.00 92.87  ? 2120 GLU A OE2   1 
ATOM   4660  N  N     . ALA A 1 2121 ? 167.329 214.117 114.299 1.00 90.95  ? 2121 ALA A N     1 
ATOM   4661  C  CA    . ALA A 1 2121 ? 167.582 212.861 113.604 1.00 85.61  ? 2121 ALA A CA    1 
ATOM   4662  C  C     . ALA A 1 2121 ? 167.617 211.720 114.613 1.00 91.50  ? 2121 ALA A C     1 
ATOM   4663  O  O     . ALA A 1 2121 ? 168.501 211.673 115.475 1.00 93.08  ? 2121 ALA A O     1 
ATOM   4664  C  CB    . ALA A 1 2121 ? 168.893 212.929 112.824 1.00 71.86  ? 2121 ALA A CB    1 
ATOM   4665  N  N     . VAL A 1 2122 ? 166.659 210.803 114.503 1.00 93.74  ? 2122 VAL A N     1 
ATOM   4666  C  CA    . VAL A 1 2122 ? 166.570 209.637 115.372 1.00 87.03  ? 2122 VAL A CA    1 
ATOM   4667  C  C     . VAL A 1 2122 ? 166.524 208.393 114.497 1.00 89.28  ? 2122 VAL A C     1 
ATOM   4668  O  O     . VAL A 1 2122 ? 165.645 208.267 113.636 1.00 90.82  ? 2122 VAL A O     1 
ATOM   4669  C  CB    . VAL A 1 2122 ? 165.338 209.705 116.293 1.00 81.98  ? 2122 VAL A CB    1 
ATOM   4670  C  CG1   . VAL A 1 2122 ? 164.988 208.322 116.822 1.00 74.85  ? 2122 VAL A CG1   1 
ATOM   4671  C  CG2   . VAL A 1 2122 ? 165.584 210.674 117.435 1.00 83.96  ? 2122 VAL A CG2   1 
ATOM   4672  N  N     . ASP A 1 2123 ? 167.468 207.480 114.715 1.00 88.30  ? 2123 ASP A N     1 
ATOM   4673  C  CA    . ASP A 1 2123 ? 167.498 206.204 114.004 1.00 84.35  ? 2123 ASP A CA    1 
ATOM   4674  C  C     . ASP A 1 2123 ? 167.690 205.103 115.036 1.00 82.21  ? 2123 ASP A C     1 
ATOM   4675  O  O     . ASP A 1 2123 ? 168.781 204.956 115.595 1.00 82.46  ? 2123 ASP A O     1 
ATOM   4676  C  CB    . ASP A 1 2123 ? 168.605 206.173 112.951 1.00 84.83  ? 2123 ASP A CB    1 
ATOM   4677  C  CG    . ASP A 1 2123 ? 168.618 204.879 112.159 1.00 87.04  ? 2123 ASP A CG    1 
ATOM   4678  O  OD1   . ASP A 1 2123 ? 167.549 204.486 111.647 1.00 86.59  ? 2123 ASP A OD1   1 
ATOM   4679  O  OD2   . ASP A 1 2123 ? 169.695 204.259 112.042 1.00 84.74  ? 2123 ASP A OD2   1 
ATOM   4680  N  N     . GLU A 1 2124 ? 166.630 204.331 115.284 1.00 77.84  ? 2124 GLU A N     1 
ATOM   4681  C  CA    . GLU A 1 2124 ? 166.675 203.314 116.329 1.00 70.63  ? 2124 GLU A CA    1 
ATOM   4682  C  C     . GLU A 1 2124 ? 167.654 202.199 115.981 1.00 74.90  ? 2124 GLU A C     1 
ATOM   4683  O  O     . GLU A 1 2124 ? 168.278 201.612 116.872 1.00 76.52  ? 2124 GLU A O     1 
ATOM   4684  C  CB    . GLU A 1 2124 ? 165.272 202.755 116.564 1.00 66.84  ? 2124 GLU A CB    1 
ATOM   4685  C  CG    . GLU A 1 2124 ? 164.310 203.769 117.160 1.00 70.00  ? 2124 GLU A CG    1 
ATOM   4686  C  CD    . GLU A 1 2124 ? 162.916 203.212 117.343 1.00 67.32  ? 2124 GLU A CD    1 
ATOM   4687  O  OE1   . GLU A 1 2124 ? 162.668 202.081 116.883 1.00 55.60  ? 2124 GLU A OE1   1 
ATOM   4688  O  OE2   . GLU A 1 2124 ? 162.066 203.904 117.941 1.00 76.67  ? 2124 GLU A OE2   1 
ATOM   4689  N  N     . GLY A 1 2125 ? 167.796 201.888 114.691 1.00 81.18  ? 2125 GLY A N     1 
ATOM   4690  C  CA    . GLY A 1 2125 ? 168.801 200.918 114.286 1.00 77.20  ? 2125 GLY A CA    1 
ATOM   4691  C  C     . GLY A 1 2125 ? 170.209 201.375 114.614 1.00 75.76  ? 2125 GLY A C     1 
ATOM   4692  O  O     . GLY A 1 2125 ? 171.034 200.590 115.091 1.00 76.74  ? 2125 GLY A O     1 
ATOM   4693  N  N     . GLU A 1 2126 ? 170.502 202.655 114.368 1.00 75.66  ? 2126 GLU A N     1 
ATOM   4694  C  CA    . GLU A 1 2126 ? 171.792 203.209 114.762 1.00 78.18  ? 2126 GLU A CA    1 
ATOM   4695  C  C     . GLU A 1 2126 ? 171.967 203.165 116.274 1.00 78.70  ? 2126 GLU A C     1 
ATOM   4696  O  O     . GLU A 1 2126 ? 173.050 202.838 116.771 1.00 80.50  ? 2126 GLU A O     1 
ATOM   4697  C  CB    . GLU A 1 2126 ? 171.929 204.642 114.249 1.00 82.29  ? 2126 GLU A CB    1 
ATOM   4698  C  CG    . GLU A 1 2126 ? 173.075 205.425 114.869 1.00 85.72  ? 2126 GLU A CG    1 
ATOM   4699  C  CD    . GLU A 1 2126 ? 172.814 206.918 114.891 1.00 92.31  ? 2126 GLU A CD    1 
ATOM   4700  O  OE1   . GLU A 1 2126 ? 171.733 207.341 114.431 1.00 92.97  ? 2126 GLU A OE1   1 
ATOM   4701  O  OE2   . GLU A 1 2126 ? 173.690 207.670 115.369 1.00 92.18  ? 2126 GLU A OE2   1 
ATOM   4702  N  N     . ILE A 1 2127 ? 170.904 203.480 117.020 1.00 72.89  ? 2127 ILE A N     1 
ATOM   4703  C  CA    . ILE A 1 2127 ? 170.973 203.451 118.479 1.00 68.94  ? 2127 ILE A CA    1 
ATOM   4704  C  C     . ILE A 1 2127 ? 171.320 202.051 118.965 1.00 68.08  ? 2127 ILE A C     1 
ATOM   4705  O  O     . ILE A 1 2127 ? 172.145 201.876 119.869 1.00 72.09  ? 2127 ILE A O     1 
ATOM   4706  C  CB    . ILE A 1 2127 ? 169.647 203.948 119.085 1.00 64.21  ? 2127 ILE A CB    1 
ATOM   4707  C  CG1   . ILE A 1 2127 ? 169.424 205.422 118.749 1.00 70.40  ? 2127 ILE A CG1   1 
ATOM   4708  C  CG2   . ILE A 1 2127 ? 169.633 203.739 120.591 1.00 52.86  ? 2127 ILE A CG2   1 
ATOM   4709  C  CD1   . ILE A 1 2127 ? 168.078 205.947 119.188 1.00 65.13  ? 2127 ILE A CD1   1 
ATOM   4710  N  N     . ALA A 1 2128 ? 170.696 201.032 118.371 1.00 69.80  ? 2128 ALA A N     1 
ATOM   4711  C  CA    . ALA A 1 2128 ? 171.016 199.657 118.734 1.00 71.04  ? 2128 ALA A CA    1 
ATOM   4712  C  C     . ALA A 1 2128 ? 172.432 199.276 118.321 1.00 67.26  ? 2128 ALA A C     1 
ATOM   4713  O  O     . ALA A 1 2128 ? 173.096 198.513 119.032 1.00 64.80  ? 2128 ALA A O     1 
ATOM   4714  C  CB    . ALA A 1 2128 ? 170.006 198.699 118.104 1.00 70.05  ? 2128 ALA A CB    1 
ATOM   4715  N  N     . GLU A 1 2129 ? 172.909 199.787 117.183 1.00 72.00  ? 2129 GLU A N     1 
ATOM   4716  C  CA    . GLU A 1 2129 ? 174.222 199.387 116.684 1.00 73.80  ? 2129 GLU A CA    1 
ATOM   4717  C  C     . GLU A 1 2129 ? 175.342 199.864 117.602 1.00 70.62  ? 2129 GLU A C     1 
ATOM   4718  O  O     . GLU A 1 2129 ? 176.210 199.077 117.997 1.00 66.21  ? 2129 GLU A O     1 
ATOM   4719  C  CB    . GLU A 1 2129 ? 174.428 199.921 115.266 1.00 81.48  ? 2129 GLU A CB    1 
ATOM   4720  C  CG    . GLU A 1 2129 ? 175.331 199.054 114.403 1.00 88.00  ? 2129 GLU A CG    1 
ATOM   4721  C  CD    . GLU A 1 2129 ? 175.476 199.589 112.992 1.00 94.93  ? 2129 GLU A CD    1 
ATOM   4722  O  OE1   . GLU A 1 2129 ? 174.851 200.624 112.680 1.00 93.79  ? 2129 GLU A OE1   1 
ATOM   4723  O  OE2   . GLU A 1 2129 ? 176.217 198.975 112.195 1.00 94.66  ? 2129 GLU A OE2   1 
ATOM   4724  N  N     . ASN A 1 2130 ? 175.345 201.147 117.948 1.00 69.07  ? 2130 ASN A N     1 
ATOM   4725  C  CA    . ASN A 1 2130 ? 176.407 201.731 118.771 1.00 67.45  ? 2130 ASN A CA    1 
ATOM   4726  C  C     . ASN A 1 2130 ? 176.032 201.743 120.248 1.00 62.18  ? 2130 ASN A C     1 
ATOM   4727  O  O     . ASN A 1 2130 ? 176.081 202.777 120.912 1.00 63.14  ? 2130 ASN A O     1 
ATOM   4728  C  CB    . ASN A 1 2130 ? 176.743 203.134 118.276 1.00 67.05  ? 2130 ASN A CB    1 
ATOM   4729  C  CG    . ASN A 1 2130 ? 175.529 204.049 118.220 1.00 75.31  ? 2130 ASN A CG    1 
ATOM   4730  O  OD1   . ASN A 1 2130 ? 174.508 203.795 118.859 1.00 71.38  ? 2130 ASN A OD1   1 
ATOM   4731  N  ND2   . ASN A 1 2130 ? 175.639 205.124 117.448 1.00 76.24  ? 2130 ASN A ND2   1 
ATOM   4732  N  N     . LEU A 1 2131 ? 175.664 200.583 120.789 1.00 55.40  ? 2131 LEU A N     1 
ATOM   4733  C  CA    . LEU A 1 2131 ? 175.174 200.499 122.156 1.00 47.36  ? 2131 LEU A CA    1 
ATOM   4734  C  C     . LEU A 1 2131 ? 176.120 199.650 122.991 1.00 44.46  ? 2131 LEU A C     1 
ATOM   4735  O  O     . LEU A 1 2131 ? 176.340 198.475 122.662 1.00 45.70  ? 2131 LEU A O     1 
ATOM   4736  C  CB    . LEU A 1 2131 ? 173.764 199.916 122.175 1.00 44.02  ? 2131 LEU A CB    1 
ATOM   4737  C  CG    . LEU A 1 2131 ? 173.035 199.818 123.513 1.00 43.78  ? 2131 LEU A CG    1 
ATOM   4738  C  CD1   . LEU A 1 2131 ? 172.820 201.199 124.104 1.00 39.65  ? 2131 LEU A CD1   1 
ATOM   4739  C  CD2   . LEU A 1 2131 ? 171.708 199.114 123.317 1.00 41.07  ? 2131 LEU A CD2   1 
ATOM   4740  N  N     . PRO A 1 2132 ? 176.700 200.188 124.069 1.00 45.61  ? 2132 PRO A N     1 
ATOM   4741  C  CA    . PRO A 1 2132 ? 177.668 199.429 124.894 1.00 37.41  ? 2132 PRO A CA    1 
ATOM   4742  C  C     . PRO A 1 2132 ? 176.994 198.381 125.779 1.00 30.61  ? 2132 PRO A C     1 
ATOM   4743  O  O     . PRO A 1 2132 ? 176.699 198.586 126.955 1.00 29.60  ? 2132 PRO A O     1 
ATOM   4744  C  CB    . PRO A 1 2132 ? 178.342 200.529 125.717 1.00 35.22  ? 2132 PRO A CB    1 
ATOM   4745  C  CG    . PRO A 1 2132 ? 177.311 201.597 125.831 1.00 30.51  ? 2132 PRO A CG    1 
ATOM   4746  C  CD    . PRO A 1 2132 ? 176.495 201.559 124.569 1.00 38.82  ? 2132 PRO A CD    1 
ATOM   4747  N  N     . GLU A 1 2133 ? 176.736 197.217 125.181 1.00 24.62  ? 2133 GLU A N     1 
ATOM   4748  C  CA    . GLU A 1 2133 ? 176.011 196.158 125.877 1.00 21.08  ? 2133 GLU A CA    1 
ATOM   4749  C  C     . GLU A 1 2133 ? 176.799 195.622 127.066 1.00 20.66  ? 2133 GLU A C     1 
ATOM   4750  O  O     . GLU A 1 2133 ? 176.218 195.324 128.118 1.00 24.17  ? 2133 GLU A O     1 
ATOM   4751  C  CB    . GLU A 1 2133 ? 175.680 195.032 124.902 1.00 25.05  ? 2133 GLU A CB    1 
ATOM   4752  C  CG    . GLU A 1 2133 ? 174.574 195.373 123.926 1.00 29.14  ? 2133 GLU A CG    1 
ATOM   4753  C  CD    . GLU A 1 2133 ? 174.765 194.696 122.590 1.00 32.50  ? 2133 GLU A CD    1 
ATOM   4754  O  OE1   . GLU A 1 2133 ? 175.885 194.210 122.332 1.00 33.51  ? 2133 GLU A OE1   1 
ATOM   4755  O  OE2   . GLU A 1 2133 ? 173.798 194.645 121.801 1.00 34.27  ? 2133 GLU A OE2   1 
ATOM   4756  N  N     . GLN A 1 2134 ? 178.117 195.475 126.916 1.00 18.00  ? 2134 GLN A N     1 
ATOM   4757  C  CA    . GLN A 1 2134 ? 178.931 195.006 128.032 1.00 17.69  ? 2134 GLN A CA    1 
ATOM   4758  C  C     . GLN A 1 2134 ? 178.883 195.990 129.192 1.00 24.48  ? 2134 GLN A C     1 
ATOM   4759  O  O     . GLN A 1 2134 ? 178.849 195.585 130.358 1.00 28.70  ? 2134 GLN A O     1 
ATOM   4760  C  CB    . GLN A 1 2134 ? 180.371 194.773 127.578 1.00 17.61  ? 2134 GLN A CB    1 
ATOM   4761  C  CG    . GLN A 1 2134 ? 180.542 193.570 126.667 1.00 13.66  ? 2134 GLN A CG    1 
ATOM   4762  C  CD    . GLN A 1 2134 ? 181.988 193.148 126.516 1.00 17.66  ? 2134 GLN A CD    1 
ATOM   4763  O  OE1   . GLN A 1 2134 ? 182.887 193.746 127.106 1.00 19.30  ? 2134 GLN A OE1   1 
ATOM   4764  N  NE2   . GLN A 1 2134 ? 182.220 192.110 125.723 1.00 23.94  ? 2134 GLN A NE2   1 
ATOM   4765  N  N     . GLU A 1 2135 ? 178.878 197.290 128.890 1.00 20.80  ? 2135 GLU A N     1 
ATOM   4766  C  CA    . GLU A 1 2135 ? 178.740 198.295 129.938 1.00 18.35  ? 2135 GLU A CA    1 
ATOM   4767  C  C     . GLU A 1 2135 ? 177.394 198.169 130.643 1.00 17.55  ? 2135 GLU A C     1 
ATOM   4768  O  O     . GLU A 1 2135 ? 177.308 198.321 131.868 1.00 21.11  ? 2135 GLU A O     1 
ATOM   4769  C  CB    . GLU A 1 2135 ? 178.917 199.690 129.340 1.00 25.08  ? 2135 GLU A CB    1 
ATOM   4770  C  CG    . GLU A 1 2135 ? 178.536 200.829 130.263 1.00 39.76  ? 2135 GLU A CG    1 
ATOM   4771  C  CD    . GLU A 1 2135 ? 178.759 202.183 129.624 1.00 43.44  ? 2135 GLU A CD    1 
ATOM   4772  O  OE1   . GLU A 1 2135 ? 179.747 202.332 128.875 1.00 41.53  ? 2135 GLU A OE1   1 
ATOM   4773  O  OE2   . GLU A 1 2135 ? 177.943 203.097 129.865 1.00 40.78  ? 2135 GLU A OE2   1 
ATOM   4774  N  N     . ILE A 1 2136 ? 176.334 197.884 129.885 1.00 17.34  ? 2136 ILE A N     1 
ATOM   4775  C  CA    . ILE A 1 2136 ? 175.017 197.673 130.480 1.00 16.12  ? 2136 ILE A CA    1 
ATOM   4776  C  C     . ILE A 1 2136 ? 175.039 196.468 131.412 1.00 18.55  ? 2136 ILE A C     1 
ATOM   4777  O  O     . ILE A 1 2136 ? 174.473 196.502 132.513 1.00 22.52  ? 2136 ILE A O     1 
ATOM   4778  C  CB    . ILE A 1 2136 ? 173.959 197.518 129.371 1.00 16.01  ? 2136 ILE A CB    1 
ATOM   4779  C  CG1   . ILE A 1 2136 ? 173.720 198.858 128.675 1.00 20.10  ? 2136 ILE A CG1   1 
ATOM   4780  C  CG2   . ILE A 1 2136 ? 172.663 196.958 129.932 1.00 17.52  ? 2136 ILE A CG2   1 
ATOM   4781  C  CD1   . ILE A 1 2136 ? 172.984 198.742 127.363 1.00 22.17  ? 2136 ILE A CD1   1 
ATOM   4782  N  N     . LEU A 1 2137 ? 175.693 195.385 130.987 1.00 14.86  ? 2137 LEU A N     1 
ATOM   4783  C  CA    . LEU A 1 2137 ? 175.789 194.198 131.831 1.00 11.88  ? 2137 LEU A CA    1 
ATOM   4784  C  C     . LEU A 1 2137 ? 176.583 194.484 133.102 1.00 13.91  ? 2137 LEU A C     1 
ATOM   4785  O  O     . LEU A 1 2137 ? 176.221 194.012 134.187 1.00 19.19  ? 2137 LEU A O     1 
ATOM   4786  C  CB    . LEU A 1 2137 ? 176.421 193.050 131.044 1.00 18.07  ? 2137 LEU A CB    1 
ATOM   4787  C  CG    . LEU A 1 2137 ? 175.920 191.640 131.358 1.00 17.00  ? 2137 LEU A CG    1 
ATOM   4788  C  CD1   . LEU A 1 2137 ? 174.463 191.496 130.961 1.00 19.50  ? 2137 LEU A CD1   1 
ATOM   4789  C  CD2   . LEU A 1 2137 ? 176.770 190.605 130.646 1.00 12.46  ? 2137 LEU A CD2   1 
ATOM   4790  N  N     . ILE A 1 2138 ? 177.672 195.248 132.987 1.00 16.30  ? 2138 ILE A N     1 
ATOM   4791  C  CA    . ILE A 1 2138 ? 178.449 195.626 134.167 1.00 17.35  ? 2138 ILE A CA    1 
ATOM   4792  C  C     . ILE A 1 2138 ? 177.601 196.454 135.121 1.00 15.47  ? 2138 ILE A C     1 
ATOM   4793  O  O     . ILE A 1 2138 ? 177.648 196.263 136.343 1.00 16.52  ? 2138 ILE A O     1 
ATOM   4794  C  CB    . ILE A 1 2138 ? 179.729 196.381 133.761 1.00 21.48  ? 2138 ILE A CB    1 
ATOM   4795  C  CG1   . ILE A 1 2138 ? 180.602 195.520 132.855 1.00 21.85  ? 2138 ILE A CG1   1 
ATOM   4796  C  CG2   . ILE A 1 2138 ? 180.517 196.802 134.990 1.00 19.29  ? 2138 ILE A CG2   1 
ATOM   4797  C  CD1   . ILE A 1 2138 ? 181.062 194.256 133.509 1.00 25.91  ? 2138 ILE A CD1   1 
ATOM   4798  N  N     . GLN A 1 2139 ? 176.827 197.398 134.583 1.00 14.53  ? 2139 GLN A N     1 
ATOM   4799  C  CA    . GLN A 1 2139 ? 175.958 198.207 135.429 1.00 17.44  ? 2139 GLN A CA    1 
ATOM   4800  C  C     . GLN A 1 2139 ? 174.930 197.343 136.144 1.00 18.65  ? 2139 GLN A C     1 
ATOM   4801  O  O     . GLN A 1 2139 ? 174.667 197.538 137.335 1.00 19.24  ? 2139 GLN A O     1 
ATOM   4802  C  CB    . GLN A 1 2139 ? 175.269 199.287 134.597 1.00 18.18  ? 2139 GLN A CB    1 
ATOM   4803  C  CG    . GLN A 1 2139 ? 174.179 200.036 135.342 1.00 19.67  ? 2139 GLN A CG    1 
ATOM   4804  C  CD    . GLN A 1 2139 ? 173.465 201.044 134.471 1.00 27.50  ? 2139 GLN A CD    1 
ATOM   4805  O  OE1   . GLN A 1 2139 ? 174.031 201.557 133.508 1.00 40.86  ? 2139 GLN A OE1   1 
ATOM   4806  N  NE2   . GLN A 1 2139 ? 172.220 201.345 134.813 1.00 24.58  ? 2139 GLN A NE2   1 
ATOM   4807  N  N     . SER A 1 2140 ? 174.340 196.380 135.432 1.00 21.58  ? 2140 SER A N     1 
ATOM   4808  C  CA    . SER A 1 2140 ? 173.384 195.473 136.059 1.00 12.17  ? 2140 SER A CA    1 
ATOM   4809  C  C     . SER A 1 2140 ? 174.033 194.667 137.178 1.00 10.20  ? 2140 SER A C     1 
ATOM   4810  O  O     . SER A 1 2140 ? 173.467 194.535 138.272 1.00 15.81  ? 2140 SER A O     1 
ATOM   4811  C  CB    . SER A 1 2140 ? 172.789 194.539 135.007 1.00 12.48  ? 2140 SER A CB    1 
ATOM   4812  O  OG    . SER A 1 2140 ? 171.784 193.715 135.565 1.00 25.99  ? 2140 SER A OG    1 
ATOM   4813  N  N     . VAL A 1 2141 ? 175.228 194.131 136.923 1.00 10.03  ? 2141 VAL A N     1 
ATOM   4814  C  CA    . VAL A 1 2141 ? 175.920 193.328 137.927 1.00 10.24  ? 2141 VAL A CA    1 
ATOM   4815  C  C     . VAL A 1 2141 ? 176.230 194.168 139.158 1.00 13.39  ? 2141 VAL A C     1 
ATOM   4816  O  O     . VAL A 1 2141 ? 176.021 193.731 140.296 1.00 12.65  ? 2141 VAL A O     1 
ATOM   4817  C  CB    . VAL A 1 2141 ? 177.196 192.710 137.326 1.00 9.33   ? 2141 VAL A CB    1 
ATOM   4818  C  CG1   . VAL A 1 2141 ? 178.117 192.205 138.425 1.00 9.23   ? 2141 VAL A CG1   1 
ATOM   4819  C  CG2   . VAL A 1 2141 ? 176.839 191.591 136.367 1.00 7.86   ? 2141 VAL A CG2   1 
ATOM   4820  N  N     . CYS A 1 2142 ? 176.723 195.390 138.952 1.00 17.73  ? 2142 CYS A N     1 
ATOM   4821  C  CA    . CYS A 1 2142 ? 177.032 196.261 140.080 1.00 14.26  ? 2142 CYS A CA    1 
ATOM   4822  C  C     . CYS A 1 2142 ? 175.772 196.643 140.847 1.00 16.10  ? 2142 CYS A C     1 
ATOM   4823  O  O     . CYS A 1 2142 ? 175.790 196.722 142.081 1.00 21.71  ? 2142 CYS A O     1 
ATOM   4824  C  CB    . CYS A 1 2142 ? 177.769 197.506 139.593 1.00 14.40  ? 2142 CYS A CB    1 
ATOM   4825  S  SG    . CYS A 1 2142 ? 179.440 197.184 138.991 1.00 30.75  ? 2142 CYS A SG    1 
ATOM   4826  N  N     . GLU A 1 2143 ? 174.669 196.885 140.139 1.00 12.53  ? 2143 GLU A N     1 
ATOM   4827  C  CA    . GLU A 1 2143 ? 173.431 197.258 140.810 1.00 12.02  ? 2143 GLU A CA    1 
ATOM   4828  C  C     . GLU A 1 2143 ? 172.848 196.102 141.608 1.00 14.08  ? 2143 GLU A C     1 
ATOM   4829  O  O     . GLU A 1 2143 ? 172.169 196.331 142.614 1.00 21.97  ? 2143 GLU A O     1 
ATOM   4830  C  CB    . GLU A 1 2143 ? 172.411 197.759 139.789 1.00 16.71  ? 2143 GLU A CB    1 
ATOM   4831  C  CG    . GLU A 1 2143 ? 172.626 199.195 139.345 1.00 27.95  ? 2143 GLU A CG    1 
ATOM   4832  C  CD    . GLU A 1 2143 ? 171.572 199.661 138.363 1.00 39.48  ? 2143 GLU A CD    1 
ATOM   4833  O  OE1   . GLU A 1 2143 ? 170.624 198.892 138.099 1.00 39.46  ? 2143 GLU A OE1   1 
ATOM   4834  O  OE2   . GLU A 1 2143 ? 171.692 200.794 137.851 1.00 38.40  ? 2143 GLU A OE2   1 
ATOM   4835  N  N     . THR A 1 2144 ? 173.094 194.861 141.187 1.00 12.18  ? 2144 THR A N     1 
ATOM   4836  C  CA    . THR A 1 2144 ? 172.456 193.717 141.830 1.00 9.59   ? 2144 THR A CA    1 
ATOM   4837  C  C     . THR A 1 2144 ? 173.405 192.924 142.727 1.00 13.74  ? 2144 THR A C     1 
ATOM   4838  O  O     . THR A 1 2144 ? 173.013 192.509 143.821 1.00 22.16  ? 2144 THR A O     1 
ATOM   4839  C  CB    . THR A 1 2144 ? 171.844 192.803 140.762 1.00 17.93  ? 2144 THR A CB    1 
ATOM   4840  O  OG1   . THR A 1 2144 ? 170.896 193.549 139.989 1.00 20.58  ? 2144 THR A OG1   1 
ATOM   4841  C  CG2   . THR A 1 2144 ? 171.104 191.656 141.412 1.00 18.29  ? 2144 THR A CG2   1 
ATOM   4842  N  N     . MET A 1 2145 ? 174.651 192.708 142.296 1.00 14.50  ? 2145 MET A N     1 
ATOM   4843  C  CA    . MET A 1 2145 ? 175.584 191.890 143.071 1.00 8.73   ? 2145 MET A CA    1 
ATOM   4844  C  C     . MET A 1 2145 ? 176.356 192.697 144.109 1.00 9.34   ? 2145 MET A C     1 
ATOM   4845  O  O     . MET A 1 2145 ? 176.541 192.234 145.239 1.00 10.22  ? 2145 MET A O     1 
ATOM   4846  C  CB    . MET A 1 2145 ? 176.565 191.177 142.138 1.00 9.53   ? 2145 MET A CB    1 
ATOM   4847  C  CG    . MET A 1 2145 ? 175.955 190.138 141.211 1.00 13.39  ? 2145 MET A CG    1 
ATOM   4848  S  SD    . MET A 1 2145 ? 175.190 188.777 142.117 1.00 46.03  ? 2145 MET A SD    1 
ATOM   4849  C  CE    . MET A 1 2145 ? 173.457 189.181 142.008 1.00 14.13  ? 2145 MET A CE    1 
ATOM   4850  N  N     . VAL A 1 2146 ? 176.828 193.892 143.741 1.00 11.65  ? 2146 VAL A N     1 
ATOM   4851  C  CA    . VAL A 1 2146 ? 177.734 194.638 144.624 1.00 8.90   ? 2146 VAL A CA    1 
ATOM   4852  C  C     . VAL A 1 2146 ? 177.145 194.911 146.002 1.00 7.42   ? 2146 VAL A C     1 
ATOM   4853  O  O     . VAL A 1 2146 ? 177.871 194.754 146.995 1.00 10.24  ? 2146 VAL A O     1 
ATOM   4854  C  CB    . VAL A 1 2146 ? 178.227 195.909 143.919 1.00 8.20   ? 2146 VAL A CB    1 
ATOM   4855  C  CG1   . VAL A 1 2146 ? 178.792 196.902 144.922 1.00 9.27   ? 2146 VAL A CG1   1 
ATOM   4856  C  CG2   . VAL A 1 2146 ? 179.272 195.556 142.876 1.00 10.39  ? 2146 VAL A CG2   1 
ATOM   4857  N  N     . PRO A 1 2147 ? 175.875 195.314 146.156 1.00 7.69   ? 2147 PRO A N     1 
ATOM   4858  C  CA    . PRO A 1 2147 ? 175.399 195.697 147.499 1.00 5.02   ? 2147 PRO A CA    1 
ATOM   4859  C  C     . PRO A 1 2147 ? 175.544 194.617 148.559 1.00 5.48   ? 2147 PRO A C     1 
ATOM   4860  O  O     . PRO A 1 2147 ? 175.682 194.950 149.743 1.00 6.63   ? 2147 PRO A O     1 
ATOM   4861  C  CB    . PRO A 1 2147 ? 173.925 196.043 147.255 1.00 3.88   ? 2147 PRO A CB    1 
ATOM   4862  C  CG    . PRO A 1 2147 ? 173.883 196.491 145.860 1.00 5.48   ? 2147 PRO A CG    1 
ATOM   4863  C  CD    . PRO A 1 2147 ? 174.867 195.635 145.128 1.00 7.53   ? 2147 PRO A CD    1 
ATOM   4864  N  N     . LYS A 1 2148 ? 175.508 193.341 148.187 1.00 5.21   ? 2148 LYS A N     1 
ATOM   4865  C  CA    . LYS A 1 2148 ? 175.607 192.266 149.166 1.00 5.08   ? 2148 LYS A CA    1 
ATOM   4866  C  C     . LYS A 1 2148 ? 177.042 191.904 149.523 1.00 7.26   ? 2148 LYS A C     1 
ATOM   4867  O  O     . LYS A 1 2148 ? 177.252 191.131 150.463 1.00 8.79   ? 2148 LYS A O     1 
ATOM   4868  C  CB    . LYS A 1 2148 ? 174.889 191.016 148.653 1.00 7.32   ? 2148 LYS A CB    1 
ATOM   4869  C  CG    . LYS A 1 2148 ? 175.623 190.285 147.546 1.00 7.23   ? 2148 LYS A CG    1 
ATOM   4870  C  CD    . LYS A 1 2148 ? 174.813 189.108 147.040 1.00 12.08  ? 2148 LYS A CD    1 
ATOM   4871  C  CE    . LYS A 1 2148 ? 175.552 188.358 145.952 1.00 9.41   ? 2148 LYS A CE    1 
ATOM   4872  N  NZ    . LYS A 1 2148 ? 174.741 187.233 145.417 1.00 15.57  ? 2148 LYS A NZ    1 
ATOM   4873  N  N     . LEU A 1 2149 ? 178.027 192.438 148.809 1.00 7.11   ? 2149 LEU A N     1 
ATOM   4874  C  CA    . LEU A 1 2149 ? 179.409 192.038 149.025 1.00 7.04   ? 2149 LEU A CA    1 
ATOM   4875  C  C     . LEU A 1 2149 ? 179.945 192.600 150.335 1.00 8.86   ? 2149 LEU A C     1 
ATOM   4876  O  O     . LEU A 1 2149 ? 179.637 193.732 150.719 1.00 16.46  ? 2149 LEU A O     1 
ATOM   4877  C  CB    . LEU A 1 2149 ? 180.282 192.510 147.865 1.00 7.84   ? 2149 LEU A CB    1 
ATOM   4878  C  CG    . LEU A 1 2149 ? 179.968 191.933 146.487 1.00 8.06   ? 2149 LEU A CG    1 
ATOM   4879  C  CD1   . LEU A 1 2149 ? 180.980 192.434 145.477 1.00 8.91   ? 2149 LEU A CD1   1 
ATOM   4880  C  CD2   . LEU A 1 2149 ? 179.947 190.416 146.531 1.00 6.13   ? 2149 LEU A CD2   1 
ATOM   4881  N  N     . VAL A 1 2150 ? 180.757 191.799 151.021 1.00 7.41   ? 2150 VAL A N     1 
ATOM   4882  C  CA    . VAL A 1 2150 ? 181.495 192.263 152.189 1.00 7.58   ? 2150 VAL A CA    1 
ATOM   4883  C  C     . VAL A 1 2150 ? 182.708 193.041 151.699 1.00 11.22  ? 2150 VAL A C     1 
ATOM   4884  O  O     . VAL A 1 2150 ? 183.029 193.019 150.506 1.00 13.99  ? 2150 VAL A O     1 
ATOM   4885  C  CB    . VAL A 1 2150 ? 181.905 191.099 153.108 1.00 7.47   ? 2150 VAL A CB    1 
ATOM   4886  C  CG1   . VAL A 1 2150 ? 180.674 190.408 153.671 1.00 5.31   ? 2150 VAL A CG1   1 
ATOM   4887  C  CG2   . VAL A 1 2150 ? 182.780 190.113 152.358 1.00 9.77   ? 2150 VAL A CG2   1 
ATOM   4888  N  N     . ALA A 1 2151 ? 183.385 193.738 152.615 1.00 13.49  ? 2151 ALA A N     1 
ATOM   4889  C  CA    . ALA A 1 2151 ? 184.482 194.616 152.219 1.00 13.72  ? 2151 ALA A CA    1 
ATOM   4890  C  C     . ALA A 1 2151 ? 185.609 193.843 151.545 1.00 13.80  ? 2151 ALA A C     1 
ATOM   4891  O  O     . ALA A 1 2151 ? 186.175 194.303 150.547 1.00 12.69  ? 2151 ALA A O     1 
ATOM   4892  C  CB    . ALA A 1 2151 ? 185.008 195.375 153.436 1.00 13.71  ? 2151 ALA A CB    1 
ATOM   4893  N  N     . GLU A 1 2152 ? 185.949 192.667 152.074 1.00 16.16  ? 2152 GLU A N     1 
ATOM   4894  C  CA    . GLU A 1 2152 ? 187.073 191.907 151.541 1.00 17.08  ? 2152 GLU A CA    1 
ATOM   4895  C  C     . GLU A 1 2152 ? 186.764 191.262 150.196 1.00 19.51  ? 2152 GLU A C     1 
ATOM   4896  O  O     . GLU A 1 2152 ? 187.690 190.810 149.515 1.00 20.47  ? 2152 GLU A O     1 
ATOM   4897  C  CB    . GLU A 1 2152 ? 187.503 190.836 152.544 1.00 17.76  ? 2152 GLU A CB    1 
ATOM   4898  C  CG    . GLU A 1 2152 ? 186.384 189.899 152.970 1.00 23.87  ? 2152 GLU A CG    1 
ATOM   4899  C  CD    . GLU A 1 2152 ? 185.850 190.216 154.354 1.00 35.07  ? 2152 GLU A CD    1 
ATOM   4900  O  OE1   . GLU A 1 2152 ? 185.699 191.413 154.678 1.00 29.13  ? 2152 GLU A OE1   1 
ATOM   4901  O  OE2   . GLU A 1 2152 ? 185.577 189.267 155.119 1.00 34.17  ? 2152 GLU A OE2   1 
ATOM   4902  N  N     . ASP A 1 2153 ? 185.493 191.205 149.798 1.00 16.32  ? 2153 ASP A N     1 
ATOM   4903  C  CA    . ASP A 1 2153 ? 185.100 190.560 148.552 1.00 13.24  ? 2153 ASP A CA    1 
ATOM   4904  C  C     . ASP A 1 2153 ? 184.830 191.541 147.419 1.00 17.59  ? 2153 ASP A C     1 
ATOM   4905  O  O     . ASP A 1 2153 ? 184.719 191.111 146.267 1.00 24.90  ? 2153 ASP A O     1 
ATOM   4906  C  CB    . ASP A 1 2153 ? 183.859 189.690 148.777 1.00 9.42   ? 2153 ASP A CB    1 
ATOM   4907  C  CG    . ASP A 1 2153 ? 184.178 188.398 149.499 1.00 17.77  ? 2153 ASP A CG    1 
ATOM   4908  O  OD1   . ASP A 1 2153 ? 185.369 188.028 149.561 1.00 25.80  ? 2153 ASP A OD1   1 
ATOM   4909  O  OD2   . ASP A 1 2153 ? 183.241 187.752 150.007 1.00 18.15  ? 2153 ASP A OD2   1 
ATOM   4910  N  N     . ILE A 1 2154 ? 184.710 192.836 147.715 1.00 12.55  ? 2154 ILE A N     1 
ATOM   4911  C  CA    . ILE A 1 2154 ? 184.502 193.823 146.653 1.00 12.74  ? 2154 ILE A CA    1 
ATOM   4912  C  C     . ILE A 1 2154 ? 185.675 193.875 145.680 1.00 17.18  ? 2154 ILE A C     1 
ATOM   4913  O  O     . ILE A 1 2154 ? 185.438 193.835 144.459 1.00 21.39  ? 2154 ILE A O     1 
ATOM   4914  C  CB    . ILE A 1 2154 ? 184.175 195.195 147.268 1.00 14.90  ? 2154 ILE A CB    1 
ATOM   4915  C  CG1   . ILE A 1 2154 ? 182.886 195.118 148.088 1.00 11.36  ? 2154 ILE A CG1   1 
ATOM   4916  C  CG2   . ILE A 1 2154 ? 184.056 196.255 146.188 1.00 17.25  ? 2154 ILE A CG2   1 
ATOM   4917  C  CD1   . ILE A 1 2154 ? 182.493 196.423 148.734 1.00 13.86  ? 2154 ILE A CD1   1 
ATOM   4918  N  N     . PRO A 1 2155 ? 186.939 193.974 146.124 1.00 17.05  ? 2155 PRO A N     1 
ATOM   4919  C  CA    . PRO A 1 2155 ? 188.038 193.976 145.145 1.00 15.89  ? 2155 PRO A CA    1 
ATOM   4920  C  C     . PRO A 1 2155 ? 188.099 192.712 144.311 1.00 18.14  ? 2155 PRO A C     1 
ATOM   4921  O  O     . PRO A 1 2155 ? 188.443 192.776 143.126 1.00 19.10  ? 2155 PRO A O     1 
ATOM   4922  C  CB    . PRO A 1 2155 ? 189.288 194.137 146.022 1.00 13.83  ? 2155 PRO A CB    1 
ATOM   4923  C  CG    . PRO A 1 2155 ? 188.798 194.762 147.268 1.00 14.52  ? 2155 PRO A CG    1 
ATOM   4924  C  CD    . PRO A 1 2155 ? 187.448 194.167 147.494 1.00 16.55  ? 2155 PRO A CD    1 
ATOM   4925  N  N     . LEU A 1 2156 ? 187.769 191.560 144.897 1.00 16.59  ? 2156 LEU A N     1 
ATOM   4926  C  CA    . LEU A 1 2156 ? 187.794 190.313 144.142 1.00 16.11  ? 2156 LEU A CA    1 
ATOM   4927  C  C     . LEU A 1 2156 ? 186.775 190.337 143.010 1.00 16.14  ? 2156 LEU A C     1 
ATOM   4928  O  O     . LEU A 1 2156 ? 187.083 189.968 141.871 1.00 21.39  ? 2156 LEU A O     1 
ATOM   4929  C  CB    . LEU A 1 2156 ? 187.535 189.132 145.075 1.00 17.78  ? 2156 LEU A CB    1 
ATOM   4930  C  CG    . LEU A 1 2156 ? 188.476 188.963 146.266 1.00 16.34  ? 2156 LEU A CG    1 
ATOM   4931  C  CD1   . LEU A 1 2156 ? 188.087 187.738 147.074 1.00 23.94  ? 2156 LEU A CD1   1 
ATOM   4932  C  CD2   . LEU A 1 2156 ? 189.916 188.863 145.795 1.00 14.25  ? 2156 LEU A CD2   1 
ATOM   4933  N  N     . LEU A 1 2157 ? 185.553 190.785 143.303 1.00 12.54  ? 2157 LEU A N     1 
ATOM   4934  C  CA    . LEU A 1 2157 ? 184.526 190.827 142.269 1.00 12.22  ? 2157 LEU A CA    1 
ATOM   4935  C  C     . LEU A 1 2157 ? 184.851 191.872 141.210 1.00 15.23  ? 2157 LEU A C     1 
ATOM   4936  O  O     . LEU A 1 2157 ? 184.588 191.658 140.022 1.00 20.13  ? 2157 LEU A O     1 
ATOM   4937  C  CB    . LEU A 1 2157 ? 183.154 191.092 142.890 1.00 11.86  ? 2157 LEU A CB    1 
ATOM   4938  C  CG    . LEU A 1 2157 ? 181.962 190.997 141.935 1.00 8.54   ? 2157 LEU A CG    1 
ATOM   4939  C  CD1   . LEU A 1 2157 ? 180.822 190.229 142.574 1.00 7.97   ? 2157 LEU A CD1   1 
ATOM   4940  C  CD2   . LEU A 1 2157 ? 181.493 192.381 141.514 1.00 9.87   ? 2157 LEU A CD2   1 
ATOM   4941  N  N     . PHE A 1 2158 ? 185.429 193.005 141.612 1.00 16.46  ? 2158 PHE A N     1 
ATOM   4942  C  CA    . PHE A 1 2158 ? 185.775 194.007 140.609 1.00 18.75  ? 2158 PHE A CA    1 
ATOM   4943  C  C     . PHE A 1 2158 ? 186.942 193.554 139.737 1.00 22.66  ? 2158 PHE A C     1 
ATOM   4944  O  O     . PHE A 1 2158 ? 186.966 193.850 138.536 1.00 30.34  ? 2158 PHE A O     1 
ATOM   4945  C  CB    . PHE A 1 2158 ? 186.068 195.346 141.280 1.00 17.75  ? 2158 PHE A CB    1 
ATOM   4946  C  CG    . PHE A 1 2158 ? 184.844 196.192 141.474 1.00 21.79  ? 2158 PHE A CG    1 
ATOM   4947  C  CD1   . PHE A 1 2158 ? 183.993 196.448 140.414 1.00 20.47  ? 2158 PHE A CD1   1 
ATOM   4948  C  CD2   . PHE A 1 2158 ? 184.534 196.715 142.716 1.00 27.69  ? 2158 PHE A CD2   1 
ATOM   4949  C  CE1   . PHE A 1 2158 ? 182.861 197.218 140.586 1.00 19.03  ? 2158 PHE A CE1   1 
ATOM   4950  C  CE2   . PHE A 1 2158 ? 183.402 197.486 142.893 1.00 32.07  ? 2158 PHE A CE2   1 
ATOM   4951  C  CZ    . PHE A 1 2158 ? 182.565 197.737 141.826 1.00 26.78  ? 2158 PHE A CZ    1 
ATOM   4952  N  N     . SER A 1 2159 ? 187.903 192.820 140.305 1.00 16.03  ? 2159 SER A N     1 
ATOM   4953  C  CA    . SER A 1 2159 ? 188.955 192.223 139.490 1.00 15.81  ? 2159 SER A CA    1 
ATOM   4954  C  C     . SER A 1 2159 ? 188.385 191.174 138.544 1.00 16.09  ? 2159 SER A C     1 
ATOM   4955  O  O     . SER A 1 2159 ? 188.821 191.063 137.392 1.00 18.81  ? 2159 SER A O     1 
ATOM   4956  C  CB    . SER A 1 2159 ? 190.031 191.610 140.385 1.00 18.67  ? 2159 SER A CB    1 
ATOM   4957  O  OG    . SER A 1 2159 ? 190.633 192.595 141.206 1.00 27.38  ? 2159 SER A OG    1 
ATOM   4958  N  N     . LEU A 1 2160 ? 187.413 190.389 139.015 1.00 14.24  ? 2160 LEU A N     1 
ATOM   4959  C  CA    . LEU A 1 2160 ? 186.752 189.424 138.142 1.00 15.07  ? 2160 LEU A CA    1 
ATOM   4960  C  C     . LEU A 1 2160 ? 186.046 190.125 136.989 1.00 19.30  ? 2160 LEU A C     1 
ATOM   4961  O  O     . LEU A 1 2160 ? 186.077 189.650 135.849 1.00 25.66  ? 2160 LEU A O     1 
ATOM   4962  C  CB    . LEU A 1 2160 ? 185.760 188.586 138.948 1.00 15.06  ? 2160 LEU A CB    1 
ATOM   4963  C  CG    . LEU A 1 2160 ? 186.267 187.298 139.600 1.00 16.23  ? 2160 LEU A CG    1 
ATOM   4964  C  CD1   . LEU A 1 2160 ? 185.102 186.440 140.053 1.00 15.05  ? 2160 LEU A CD1   1 
ATOM   4965  C  CD2   . LEU A 1 2160 ? 187.162 186.522 138.661 1.00 14.18  ? 2160 LEU A CD2   1 
ATOM   4966  N  N     . LEU A 1 2161 ? 185.390 191.253 137.273 1.00 18.24  ? 2161 LEU A N     1 
ATOM   4967  C  CA    . LEU A 1 2161 ? 184.769 192.044 136.215 1.00 18.94  ? 2161 LEU A CA    1 
ATOM   4968  C  C     . LEU A 1 2161 ? 185.807 192.560 135.227 1.00 17.93  ? 2161 LEU A C     1 
ATOM   4969  O  O     . LEU A 1 2161 ? 185.601 192.499 134.010 1.00 23.36  ? 2161 LEU A O     1 
ATOM   4970  C  CB    . LEU A 1 2161 ? 183.990 193.211 136.819 1.00 21.39  ? 2161 LEU A CB    1 
ATOM   4971  C  CG    . LEU A 1 2161 ? 182.583 192.953 137.353 1.00 16.68  ? 2161 LEU A CG    1 
ATOM   4972  C  CD1   . LEU A 1 2161 ? 181.889 194.271 137.629 1.00 22.89  ? 2161 LEU A CD1   1 
ATOM   4973  C  CD2   . LEU A 1 2161 ? 181.784 192.142 136.354 1.00 12.22  ? 2161 LEU A CD2   1 
ATOM   4974  N  N     . SER A 1 2162 ? 186.928 193.075 135.734 1.00 20.54  ? 2162 SER A N     1 
ATOM   4975  C  CA    . SER A 1 2162 ? 187.959 193.618 134.855 1.00 24.77  ? 2162 SER A CA    1 
ATOM   4976  C  C     . SER A 1 2162 ? 188.621 192.532 134.016 1.00 18.85  ? 2162 SER A C     1 
ATOM   4977  O  O     . SER A 1 2162 ? 189.128 192.818 132.926 1.00 18.36  ? 2162 SER A O     1 
ATOM   4978  C  CB    . SER A 1 2162 ? 189.006 194.367 135.678 1.00 24.00  ? 2162 SER A CB    1 
ATOM   4979  O  OG    . SER A 1 2162 ? 188.401 195.352 136.495 1.00 26.25  ? 2162 SER A OG    1 
ATOM   4980  N  N     . ASP A 1 2163 ? 188.641 191.292 134.507 1.00 21.86  ? 2163 ASP A N     1 
ATOM   4981  C  CA    . ASP A 1 2163 ? 189.242 190.208 133.737 1.00 20.01  ? 2163 ASP A CA    1 
ATOM   4982  C  C     . ASP A 1 2163 ? 188.262 189.644 132.714 1.00 19.81  ? 2163 ASP A C     1 
ATOM   4983  O  O     . ASP A 1 2163 ? 188.615 189.444 131.546 1.00 25.31  ? 2163 ASP A O     1 
ATOM   4984  C  CB    . ASP A 1 2163 ? 189.736 189.107 134.675 1.00 18.96  ? 2163 ASP A CB    1 
ATOM   4985  C  CG    . ASP A 1 2163 ? 190.817 189.589 135.619 1.00 29.57  ? 2163 ASP A CG    1 
ATOM   4986  O  OD1   . ASP A 1 2163 ? 191.126 188.868 136.590 1.00 34.00  ? 2163 ASP A OD1   1 
ATOM   4987  O  OD2   . ASP A 1 2163 ? 191.360 190.690 135.392 1.00 29.50  ? 2163 ASP A OD2   1 
ATOM   4988  N  N     . VAL A 1 2164 ? 187.024 189.375 133.135 1.00 19.02  ? 2164 VAL A N     1 
ATOM   4989  C  CA    . VAL A 1 2164 ? 186.040 188.794 132.227 1.00 18.31  ? 2164 VAL A CA    1 
ATOM   4990  C  C     . VAL A 1 2164 ? 185.602 189.815 131.184 1.00 20.80  ? 2164 VAL A C     1 
ATOM   4991  O  O     . VAL A 1 2164 ? 185.469 189.493 129.997 1.00 26.52  ? 2164 VAL A O     1 
ATOM   4992  C  CB    . VAL A 1 2164 ? 184.845 188.240 133.023 1.00 20.73  ? 2164 VAL A CB    1 
ATOM   4993  C  CG1   . VAL A 1 2164 ? 183.648 188.043 132.117 1.00 15.08  ? 2164 VAL A CG1   1 
ATOM   4994  C  CG2   . VAL A 1 2164 ? 185.220 186.934 133.703 1.00 20.33  ? 2164 VAL A CG2   1 
ATOM   4995  N  N     . PHE A 1 2165 ? 185.370 191.057 131.604 1.00 21.04  ? 2165 PHE A N     1 
ATOM   4996  C  CA    . PHE A 1 2165 ? 185.027 192.132 130.682 1.00 19.05  ? 2165 PHE A CA    1 
ATOM   4997  C  C     . PHE A 1 2165 ? 186.156 193.154 130.647 1.00 23.19  ? 2165 PHE A C     1 
ATOM   4998  O  O     . PHE A 1 2165 ? 186.066 194.198 131.305 1.00 28.50  ? 2165 PHE A O     1 
ATOM   4999  C  CB    . PHE A 1 2165 ? 183.719 192.815 131.088 1.00 18.68  ? 2165 PHE A CB    1 
ATOM   5000  C  CG    . PHE A 1 2165 ? 182.540 191.890 131.169 1.00 16.42  ? 2165 PHE A CG    1 
ATOM   5001  C  CD1   . PHE A 1 2165 ? 181.740 191.672 130.062 1.00 16.74  ? 2165 PHE A CD1   1 
ATOM   5002  C  CD2   . PHE A 1 2165 ? 182.217 191.257 132.357 1.00 18.36  ? 2165 PHE A CD2   1 
ATOM   5003  C  CE1   . PHE A 1 2165 ? 180.648 190.830 130.134 1.00 18.91  ? 2165 PHE A CE1   1 
ATOM   5004  C  CE2   . PHE A 1 2165 ? 181.125 190.417 132.435 1.00 19.39  ? 2165 PHE A CE2   1 
ATOM   5005  C  CZ    . PHE A 1 2165 ? 180.341 190.201 131.322 1.00 16.05  ? 2165 PHE A CZ    1 
ATOM   5006  N  N     . PRO A 1 2166 ? 187.228 192.900 129.898 1.00 25.29  ? 2166 PRO A N     1 
ATOM   5007  C  CA    . PRO A 1 2166 ? 188.360 193.830 129.900 1.00 25.67  ? 2166 PRO A CA    1 
ATOM   5008  C  C     . PRO A 1 2166 ? 188.098 195.042 129.020 1.00 31.33  ? 2166 PRO A C     1 
ATOM   5009  O  O     . PRO A 1 2166 ? 187.415 194.960 127.996 1.00 34.36  ? 2166 PRO A O     1 
ATOM   5010  C  CB    . PRO A 1 2166 ? 189.507 192.980 129.344 1.00 23.43  ? 2166 PRO A CB    1 
ATOM   5011  C  CG    . PRO A 1 2166 ? 188.829 192.021 128.431 1.00 27.81  ? 2166 PRO A CG    1 
ATOM   5012  C  CD    . PRO A 1 2166 ? 187.459 191.752 129.006 1.00 23.65  ? 2166 PRO A CD    1 
ATOM   5013  N  N     . GLY A 1 2167 ? 188.651 196.178 129.436 1.00 27.81  ? 2167 GLY A N     1 
ATOM   5014  C  CA    . GLY A 1 2167 ? 188.578 197.392 128.655 1.00 34.91  ? 2167 GLY A CA    1 
ATOM   5015  C  C     . GLY A 1 2167 ? 187.287 198.167 128.778 1.00 36.85  ? 2167 GLY A C     1 
ATOM   5016  O  O     . GLY A 1 2167 ? 187.161 199.226 128.151 1.00 46.43  ? 2167 GLY A O     1 
ATOM   5017  N  N     . VAL A 1 2168 ? 186.326 197.683 129.558 1.00 31.70  ? 2168 VAL A N     1 
ATOM   5018  C  CA    . VAL A 1 2168 ? 185.055 198.363 129.763 1.00 35.89  ? 2168 VAL A CA    1 
ATOM   5019  C  C     . VAL A 1 2168 ? 184.915 198.678 131.245 1.00 32.50  ? 2168 VAL A C     1 
ATOM   5020  O  O     . VAL A 1 2168 ? 185.232 197.841 132.099 1.00 24.46  ? 2168 VAL A O     1 
ATOM   5021  C  CB    . VAL A 1 2168 ? 183.867 197.530 129.241 1.00 32.24  ? 2168 VAL A CB    1 
ATOM   5022  C  CG1   . VAL A 1 2168 ? 183.706 196.241 130.025 1.00 26.13  ? 2168 VAL A CG1   1 
ATOM   5023  C  CG2   . VAL A 1 2168 ? 182.583 198.344 129.287 1.00 31.59  ? 2168 VAL A CG2   1 
ATOM   5024  N  N     . GLN A 1 2169 ? 184.485 199.898 131.547 1.00 41.84  ? 2169 GLN A N     1 
ATOM   5025  C  CA    . GLN A 1 2169 ? 184.291 200.345 132.916 1.00 40.98  ? 2169 GLN A CA    1 
ATOM   5026  C  C     . GLN A 1 2169 ? 182.928 201.008 133.047 1.00 46.21  ? 2169 GLN A C     1 
ATOM   5027  O  O     . GLN A 1 2169 ? 182.426 201.629 132.105 1.00 47.98  ? 2169 GLN A O     1 
ATOM   5028  C  CB    . GLN A 1 2169 ? 185.396 201.319 133.352 1.00 44.08  ? 2169 GLN A CB    1 
ATOM   5029  C  CG    . GLN A 1 2169 ? 185.347 202.680 132.671 1.00 54.60  ? 2169 GLN A CG    1 
ATOM   5030  C  CD    . GLN A 1 2169 ? 186.040 202.695 131.321 1.00 61.40  ? 2169 GLN A CD    1 
ATOM   5031  O  OE1   . GLN A 1 2169 ? 186.304 201.648 130.732 1.00 58.64  ? 2169 GLN A OE1   1 
ATOM   5032  N  NE2   . GLN A 1 2169 ? 186.334 203.890 130.822 1.00 63.88  ? 2169 GLN A NE2   1 
ATOM   5033  N  N     . TYR A 1 2170 ? 182.327 200.858 134.222 1.00 43.49  ? 2170 TYR A N     1 
ATOM   5034  C  CA    . TYR A 1 2170 ? 181.046 201.471 134.535 1.00 43.36  ? 2170 TYR A CA    1 
ATOM   5035  C  C     . TYR A 1 2170 ? 181.200 202.370 135.750 1.00 46.12  ? 2170 TYR A C     1 
ATOM   5036  O  O     . TYR A 1 2170 ? 181.810 201.975 136.749 1.00 47.11  ? 2170 TYR A O     1 
ATOM   5037  C  CB    . TYR A 1 2170 ? 179.969 200.417 134.803 1.00 42.97  ? 2170 TYR A CB    1 
ATOM   5038  C  CG    . TYR A 1 2170 ? 178.733 200.993 135.451 1.00 41.69  ? 2170 TYR A CG    1 
ATOM   5039  C  CD1   . TYR A 1 2170 ? 178.367 200.627 136.739 1.00 32.58  ? 2170 TYR A CD1   1 
ATOM   5040  C  CD2   . TYR A 1 2170 ? 177.943 201.918 134.782 1.00 38.21  ? 2170 TYR A CD2   1 
ATOM   5041  C  CE1   . TYR A 1 2170 ? 177.242 201.158 137.339 1.00 38.22  ? 2170 TYR A CE1   1 
ATOM   5042  C  CE2   . TYR A 1 2170 ? 176.818 202.455 135.374 1.00 37.94  ? 2170 TYR A CE2   1 
ATOM   5043  C  CZ    . TYR A 1 2170 ? 176.473 202.073 136.652 1.00 47.39  ? 2170 TYR A CZ    1 
ATOM   5044  O  OH    . TYR A 1 2170 ? 175.349 202.605 137.242 1.00 46.60  ? 2170 TYR A OH    1 
ATOM   5045  N  N     . HIS A 1 2171 ? 180.646 203.573 135.660 1.00 50.42  ? 2171 HIS A N     1 
ATOM   5046  C  CA    . HIS A 1 2171 ? 180.596 204.508 136.773 1.00 48.21  ? 2171 HIS A CA    1 
ATOM   5047  C  C     . HIS A 1 2171 ? 179.141 204.734 137.155 1.00 44.11  ? 2171 HIS A C     1 
ATOM   5048  O  O     . HIS A 1 2171 ? 178.323 205.104 136.307 1.00 44.20  ? 2171 HIS A O     1 
ATOM   5049  C  CB    . HIS A 1 2171 ? 181.272 205.830 136.408 1.00 50.12  ? 2171 HIS A CB    1 
ATOM   5050  C  CG    . HIS A 1 2171 ? 182.511 205.663 135.585 1.00 59.27  ? 2171 HIS A CG    1 
ATOM   5051  N  ND1   . HIS A 1 2171 ? 183.759 205.493 136.144 1.00 61.56  ? 2171 HIS A ND1   1 
ATOM   5052  C  CD2   . HIS A 1 2171 ? 182.693 205.635 134.243 1.00 57.38  ? 2171 HIS A CD2   1 
ATOM   5053  C  CE1   . HIS A 1 2171 ? 184.657 205.369 135.183 1.00 61.98  ? 2171 HIS A CE1   1 
ATOM   5054  N  NE2   . HIS A 1 2171 ? 184.036 205.452 134.020 1.00 58.89  ? 2171 HIS A NE2   1 
ATOM   5055  N  N     . ARG A 1 2172 ? 178.823 204.503 138.425 1.00 42.28  ? 2172 ARG A N     1 
ATOM   5056  C  CA    . ARG A 1 2172 ? 177.450 204.639 138.889 1.00 40.58  ? 2172 ARG A CA    1 
ATOM   5057  C  C     . ARG A 1 2172 ? 176.972 206.078 138.747 1.00 43.47  ? 2172 ARG A C     1 
ATOM   5058  O  O     . ARG A 1 2172 ? 177.685 207.025 139.091 1.00 52.99  ? 2172 ARG A O     1 
ATOM   5059  C  CB    . ARG A 1 2172 ? 177.333 204.187 140.343 1.00 51.76  ? 2172 ARG A CB    1 
ATOM   5060  C  CG    . ARG A 1 2172 ? 177.538 202.696 140.545 1.00 64.23  ? 2172 ARG A CG    1 
ATOM   5061  C  CD    . ARG A 1 2172 ? 177.336 202.313 141.999 1.00 69.83  ? 2172 ARG A CD    1 
ATOM   5062  N  NE    . ARG A 1 2172 ? 178.399 202.842 142.843 1.00 81.83  ? 2172 ARG A NE    1 
ATOM   5063  C  CZ    . ARG A 1 2172 ? 178.227 203.780 143.764 1.00 73.68  ? 2172 ARG A CZ    1 
ATOM   5064  N  NH1   . ARG A 1 2172 ? 177.042 204.326 143.981 1.00 66.44  ? 2172 ARG A NH1   1 
ATOM   5065  N  NH2   . ARG A 1 2172 ? 179.271 204.181 144.484 1.00 57.84  ? 2172 ARG A NH2   1 
ATOM   5066  N  N     . GLY A 1 2173 ? 175.757 206.234 138.231 1.00 45.97  ? 2173 GLY A N     1 
ATOM   5067  C  CA    . GLY A 1 2173 ? 175.185 207.560 138.094 1.00 44.04  ? 2173 GLY A CA    1 
ATOM   5068  C  C     . GLY A 1 2173 ? 174.932 208.192 139.451 1.00 42.89  ? 2173 GLY A C     1 
ATOM   5069  O  O     . GLY A 1 2173 ? 174.669 207.508 140.441 1.00 43.05  ? 2173 GLY A O     1 
ATOM   5070  N  N     . GLU A 1 2174 ? 175.035 209.516 139.496 1.00 46.58  ? 2174 GLU A N     1 
ATOM   5071  C  CA    . GLU A 1 2174 ? 174.792 210.273 140.718 1.00 52.38  ? 2174 GLU A CA    1 
ATOM   5072  C  C     . GLU A 1 2174 ? 173.306 210.601 140.796 1.00 51.04  ? 2174 GLU A C     1 
ATOM   5073  O  O     . GLU A 1 2174 ? 172.830 211.520 140.121 1.00 60.37  ? 2174 GLU A O     1 
ATOM   5074  C  CB    . GLU A 1 2174 ? 175.645 211.538 140.743 1.00 52.90  ? 2174 GLU A CB    1 
ATOM   5075  C  CG    . GLU A 1 2174 ? 177.129 211.275 140.944 1.00 68.71  ? 2174 GLU A CG    1 
ATOM   5076  C  CD    . GLU A 1 2174 ? 177.983 212.498 140.673 1.00 83.29  ? 2174 GLU A CD    1 
ATOM   5077  O  OE1   . GLU A 1 2174 ? 177.427 213.533 140.251 1.00 76.42  ? 2174 GLU A OE1   1 
ATOM   5078  O  OE2   . GLU A 1 2174 ? 179.213 212.422 140.877 1.00 84.52  ? 2174 GLU A OE2   1 
ATOM   5079  N  N     . MET A 1 2175 ? 172.571 209.849 141.616 1.00 35.68  ? 2175 MET A N     1 
ATOM   5080  C  CA    . MET A 1 2175 ? 171.141 210.089 141.811 1.00 39.02  ? 2175 MET A CA    1 
ATOM   5081  C  C     . MET A 1 2175 ? 170.961 211.328 142.689 1.00 33.97  ? 2175 MET A C     1 
ATOM   5082  O  O     . MET A 1 2175 ? 170.620 211.257 143.872 1.00 42.26  ? 2175 MET A O     1 
ATOM   5083  C  CB    . MET A 1 2175 ? 170.462 208.871 142.423 1.00 41.24  ? 2175 MET A CB    1 
ATOM   5084  C  CG    . MET A 1 2175 ? 170.207 207.728 141.454 1.00 40.61  ? 2175 MET A CG    1 
ATOM   5085  S  SD    . MET A 1 2175 ? 171.699 206.833 140.998 1.00 74.21  ? 2175 MET A SD    1 
ATOM   5086  C  CE    . MET A 1 2175 ? 172.005 205.908 142.499 1.00 35.67  ? 2175 MET A CE    1 
ATOM   5087  N  N     . THR A 1 2176 ? 171.199 212.489 142.075 1.00 30.16  ? 2176 THR A N     1 
ATOM   5088  C  CA    . THR A 1 2176 ? 171.131 213.745 142.814 1.00 24.64  ? 2176 THR A CA    1 
ATOM   5089  C  C     . THR A 1 2176 ? 169.730 213.995 143.355 1.00 23.02  ? 2176 THR A C     1 
ATOM   5090  O  O     . THR A 1 2176 ? 169.554 214.209 144.561 1.00 26.90  ? 2176 THR A O     1 
ATOM   5091  C  CB    . THR A 1 2176 ? 171.574 214.904 141.922 1.00 29.97  ? 2176 THR A CB    1 
ATOM   5092  O  OG1   . THR A 1 2176 ? 170.970 214.772 140.630 1.00 34.13  ? 2176 THR A OG1   1 
ATOM   5093  C  CG2   . THR A 1 2176 ? 173.085 214.906 141.766 1.00 31.46  ? 2176 THR A CG2   1 
ATOM   5094  N  N     . ALA A 1 2177 ? 168.715 213.906 142.487 1.00 25.18  ? 2177 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2177 ? 167.354 214.266 142.876 1.00 17.66  ? 2177 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2177 ? 166.919 213.528 144.135 1.00 21.17  ? 2177 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2177 ? 166.184 214.078 144.963 1.00 23.22  ? 2177 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2177 ? 166.389 213.979 141.727 1.00 16.81  ? 2177 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2178 ? 167.364 212.283 144.298 1.00 20.06  ? 2178 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2178 ? 167.168 211.592 145.564 1.00 16.85  ? 2178 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2178 ? 168.154 212.067 146.624 1.00 18.17  ? 2178 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2178 ? 167.860 211.976 147.820 1.00 20.73  ? 2178 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2178 ? 167.292 210.081 145.361 1.00 16.93  ? 2178 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2178 ? 166.985 209.186 146.563 1.00 10.36  ? 2178 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2178 ? 165.524 209.307 146.957 1.00 10.87  ? 2178 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2178 ? 167.341 207.743 146.265 1.00 6.58   ? 2178 LEU A CD2   1 
ATOM   5107  N  N     . ARG A 1 2179 ? 169.315 212.585 146.212 1.00 20.11  ? 2179 ARG A N     1 
ATOM   5108  C  CA    . ARG A 1 2179 ? 170.344 212.950 147.183 1.00 17.15  ? 2179 ARG A CA    1 
ATOM   5109  C  C     . ARG A 1 2179 ? 169.960 214.193 147.982 1.00 19.01  ? 2179 ARG A C     1 
ATOM   5110  O  O     . ARG A 1 2179 ? 170.217 214.251 149.189 1.00 20.13  ? 2179 ARG A O     1 
ATOM   5111  C  CB    . ARG A 1 2179 ? 171.692 213.146 146.488 1.00 22.56  ? 2179 ARG A CB    1 
ATOM   5112  C  CG    . ARG A 1 2179 ? 172.510 211.871 146.353 1.00 13.87  ? 2179 ARG A CG    1 
ATOM   5113  C  CD    . ARG A 1 2179 ? 173.915 212.173 145.866 1.00 19.32  ? 2179 ARG A CD    1 
ATOM   5114  N  NE    . ARG A 1 2179 ? 174.642 210.971 145.477 1.00 24.35  ? 2179 ARG A NE    1 
ATOM   5115  C  CZ    . ARG A 1 2179 ? 175.403 210.257 146.295 1.00 25.52  ? 2179 ARG A CZ    1 
ATOM   5116  N  NH1   . ARG A 1 2179 ? 175.551 210.588 147.568 1.00 21.84  ? 2179 ARG A NH1   1 
ATOM   5117  N  NH2   . ARG A 1 2179 ? 176.035 209.186 145.824 1.00 21.23  ? 2179 ARG A NH2   1 
ATOM   5118  N  N     . GLU A 1 2180 ? 169.353 215.202 147.345 1.00 19.52  ? 2180 GLU A N     1 
ATOM   5119  C  CA    . GLU A 1 2180 ? 168.899 216.346 148.141 1.00 24.62  ? 2180 GLU A CA    1 
ATOM   5120  C  C     . GLU A 1 2180 ? 167.785 215.944 149.102 1.00 21.47  ? 2180 GLU A C     1 
ATOM   5121  O  O     . GLU A 1 2180 ? 167.714 216.454 150.228 1.00 23.15  ? 2180 GLU A O     1 
ATOM   5122  C  CB    . GLU A 1 2180 ? 168.438 217.532 147.283 1.00 28.49  ? 2180 GLU A CB    1 
ATOM   5123  C  CG    . GLU A 1 2180 ? 169.519 218.250 146.482 1.00 25.52  ? 2180 GLU A CG    1 
ATOM   5124  C  CD    . GLU A 1 2180 ? 169.814 217.595 145.166 1.00 35.18  ? 2180 GLU A CD    1 
ATOM   5125  O  OE1   . GLU A 1 2180 ? 169.117 216.625 144.841 1.00 39.55  ? 2180 GLU A OE1   1 
ATOM   5126  O  OE2   . GLU A 1 2180 ? 170.739 218.046 144.459 1.00 45.74  ? 2180 GLU A OE2   1 
ATOM   5127  N  N     . GLU A 1 2181 ? 166.897 215.045 148.674 1.00 21.11  ? 2181 GLU A N     1 
ATOM   5128  C  CA    . GLU A 1 2181 ? 165.855 214.565 149.575 1.00 19.52  ? 2181 GLU A CA    1 
ATOM   5129  C  C     . GLU A 1 2181 ? 166.455 213.814 150.757 1.00 15.17  ? 2181 GLU A C     1 
ATOM   5130  O  O     . GLU A 1 2181 ? 166.009 213.977 151.900 1.00 17.04  ? 2181 GLU A O     1 
ATOM   5131  C  CB    . GLU A 1 2181 ? 164.870 213.680 148.814 1.00 17.02  ? 2181 GLU A CB    1 
ATOM   5132  C  CG    . GLU A 1 2181 ? 163.792 214.448 148.059 1.00 21.31  ? 2181 GLU A CG    1 
ATOM   5133  C  CD    . GLU A 1 2181 ? 163.241 215.629 148.840 1.00 35.74  ? 2181 GLU A CD    1 
ATOM   5134  O  OE1   . GLU A 1 2181 ? 163.074 216.711 148.239 1.00 36.88  ? 2181 GLU A OE1   1 
ATOM   5135  O  OE2   . GLU A 1 2181 ? 162.952 215.475 150.046 1.00 39.59  ? 2181 GLU A OE2   1 
ATOM   5136  N  N     . LEU A 1 2182 ? 167.472 212.989 150.498 1.00 16.05  ? 2182 LEU A N     1 
ATOM   5137  C  CA    . LEU A 1 2182 ? 168.175 212.310 151.580 1.00 13.84  ? 2182 LEU A CA    1 
ATOM   5138  C  C     . LEU A 1 2182 ? 168.830 213.314 152.518 1.00 14.19  ? 2182 LEU A C     1 
ATOM   5139  O  O     . LEU A 1 2182 ? 168.806 213.138 153.740 1.00 20.01  ? 2182 LEU A O     1 
ATOM   5140  C  CB    . LEU A 1 2182 ? 169.219 211.349 151.011 1.00 10.39  ? 2182 LEU A CB    1 
ATOM   5141  C  CG    . LEU A 1 2182 ? 168.714 210.098 150.288 1.00 8.84   ? 2182 LEU A CG    1 
ATOM   5142  C  CD1   . LEU A 1 2182 ? 169.876 209.254 149.794 1.00 7.04   ? 2182 LEU A CD1   1 
ATOM   5143  C  CD2   . LEU A 1 2182 ? 167.816 209.282 151.194 1.00 8.25   ? 2182 LEU A CD2   1 
ATOM   5144  N  N     . LYS A 1 2183 ? 169.419 214.375 151.961 1.00 14.37  ? 2183 LYS A N     1 
ATOM   5145  C  CA    . LYS A 1 2183 ? 170.016 215.424 152.781 1.00 13.05  ? 2183 LYS A CA    1 
ATOM   5146  C  C     . LYS A 1 2183 ? 168.981 216.055 153.703 1.00 16.08  ? 2183 LYS A C     1 
ATOM   5147  O  O     . LYS A 1 2183 ? 169.219 216.225 154.904 1.00 22.08  ? 2183 LYS A O     1 
ATOM   5148  C  CB    . LYS A 1 2183 ? 170.639 216.494 151.885 1.00 16.21  ? 2183 LYS A CB    1 
ATOM   5149  C  CG    . LYS A 1 2183 ? 172.081 216.249 151.516 1.00 19.22  ? 2183 LYS A CG    1 
ATOM   5150  C  CD    . LYS A 1 2183 ? 172.774 217.536 151.109 1.00 23.96  ? 2183 LYS A CD    1 
ATOM   5151  C  CE    . LYS A 1 2183 ? 172.984 218.449 152.304 1.00 20.83  ? 2183 LYS A CE    1 
ATOM   5152  N  NZ    . LYS A 1 2183 ? 173.885 217.830 153.312 1.00 25.20  ? 2183 LYS A NZ    1 
ATOM   5153  N  N     . LYS A 1 2184 ? 167.825 216.420 153.147 1.00 16.15  ? 2184 LYS A N     1 
ATOM   5154  C  CA    . LYS A 1 2184 ? 166.792 217.071 153.945 1.00 15.80  ? 2184 LYS A CA    1 
ATOM   5155  C  C     . LYS A 1 2184 ? 166.266 216.142 155.032 1.00 14.81  ? 2184 LYS A C     1 
ATOM   5156  O  O     . LYS A 1 2184 ? 166.063 216.566 156.177 1.00 21.65  ? 2184 LYS A O     1 
ATOM   5157  C  CB    . LYS A 1 2184 ? 165.653 217.544 153.044 1.00 20.30  ? 2184 LYS A CB    1 
ATOM   5158  C  CG    . LYS A 1 2184 ? 166.032 218.687 152.121 1.00 22.35  ? 2184 LYS A CG    1 
ATOM   5159  C  CD    . LYS A 1 2184 ? 164.880 219.060 151.208 1.00 36.66  ? 2184 LYS A CD    1 
ATOM   5160  C  CE    . LYS A 1 2184 ? 163.761 219.735 151.984 1.00 46.22  ? 2184 LYS A CE    1 
ATOM   5161  N  NZ    . LYS A 1 2184 ? 164.168 221.071 152.497 1.00 44.76  ? 2184 LYS A NZ    1 
ATOM   5162  N  N     . VAL A 1 2185 ? 166.044 214.870 154.696 1.00 13.05  ? 2185 VAL A N     1 
ATOM   5163  C  CA    . VAL A 1 2185 ? 165.548 213.922 155.688 1.00 14.07  ? 2185 VAL A CA    1 
ATOM   5164  C  C     . VAL A 1 2185 ? 166.581 213.707 156.789 1.00 14.97  ? 2185 VAL A C     1 
ATOM   5165  O  O     . VAL A 1 2185 ? 166.237 213.639 157.975 1.00 16.30  ? 2185 VAL A O     1 
ATOM   5166  C  CB    . VAL A 1 2185 ? 165.146 212.600 155.010 1.00 14.62  ? 2185 VAL A CB    1 
ATOM   5167  C  CG1   . VAL A 1 2185 ? 164.838 211.534 156.049 1.00 10.79  ? 2185 VAL A CG1   1 
ATOM   5168  C  CG2   . VAL A 1 2185 ? 163.944 212.820 154.108 1.00 15.59  ? 2185 VAL A CG2   1 
ATOM   5169  N  N     . CYS A 1 2186 ? 167.861 213.604 156.422 1.00 12.08  ? 2186 CYS A N     1 
ATOM   5170  C  CA    . CYS A 1 2186 ? 168.907 213.424 157.422 1.00 10.26  ? 2186 CYS A CA    1 
ATOM   5171  C  C     . CYS A 1 2186 ? 169.014 214.635 158.338 1.00 16.55  ? 2186 CYS A C     1 
ATOM   5172  O  O     . CYS A 1 2186 ? 169.206 214.488 159.551 1.00 19.25  ? 2186 CYS A O     1 
ATOM   5173  C  CB    . CYS A 1 2186 ? 170.246 213.146 156.739 1.00 11.27  ? 2186 CYS A CB    1 
ATOM   5174  S  SG    . CYS A 1 2186 ? 170.389 211.497 156.020 1.00 21.38  ? 2186 CYS A SG    1 
ATOM   5175  N  N     . GLN A 1 2187 ? 168.902 215.843 157.778 1.00 17.08  ? 2187 GLN A N     1 
ATOM   5176  C  CA    . GLN A 1 2187 ? 168.892 217.038 158.617 1.00 18.30  ? 2187 GLN A CA    1 
ATOM   5177  C  C     . GLN A 1 2187 ? 167.698 217.034 159.560 1.00 18.54  ? 2187 GLN A C     1 
ATOM   5178  O  O     . GLN A 1 2187 ? 167.826 217.388 160.738 1.00 24.52  ? 2187 GLN A O     1 
ATOM   5179  C  CB    . GLN A 1 2187 ? 168.885 218.300 157.753 1.00 25.40  ? 2187 GLN A CB    1 
ATOM   5180  C  CG    . GLN A 1 2187 ? 170.123 218.491 156.897 1.00 34.55  ? 2187 GLN A CG    1 
ATOM   5181  C  CD    . GLN A 1 2187 ? 171.371 218.735 157.722 1.00 45.74  ? 2187 GLN A CD    1 
ATOM   5182  O  OE1   . GLN A 1 2187 ? 171.331 219.429 158.738 1.00 40.34  ? 2187 GLN A OE1   1 
ATOM   5183  N  NE2   . GLN A 1 2187 ? 172.488 218.166 157.288 1.00 49.07  ? 2187 GLN A NE2   1 
ATOM   5184  N  N     . GLU A 1 2188 ? 166.528 216.630 159.065 1.00 15.73  ? 2188 GLU A N     1 
ATOM   5185  C  CA    . GLU A 1 2188 ? 165.341 216.596 159.908 1.00 18.05  ? 2188 GLU A CA    1 
ATOM   5186  C  C     . GLU A 1 2188 ? 165.366 215.455 160.918 1.00 15.95  ? 2188 GLU A C     1 
ATOM   5187  O  O     . GLU A 1 2188 ? 164.704 215.552 161.956 1.00 16.07  ? 2188 GLU A O     1 
ATOM   5188  C  CB    . GLU A 1 2188 ? 164.087 216.497 159.038 1.00 19.30  ? 2188 GLU A CB    1 
ATOM   5189  C  CG    . GLU A 1 2188 ? 162.856 217.133 159.658 1.00 31.90  ? 2188 GLU A CG    1 
ATOM   5190  C  CD    . GLU A 1 2188 ? 161.776 217.424 158.637 1.00 55.43  ? 2188 GLU A CD    1 
ATOM   5191  O  OE1   . GLU A 1 2188 ? 161.995 217.134 157.443 1.00 57.24  ? 2188 GLU A OE1   1 
ATOM   5192  O  OE2   . GLU A 1 2188 ? 160.710 217.947 159.026 1.00 51.72  ? 2188 GLU A OE2   1 
ATOM   5193  N  N     . MET A 1 2189 ? 166.116 214.388 160.647 1.00 17.08  ? 2189 MET A N     1 
ATOM   5194  C  CA    . MET A 1 2189 ? 166.202 213.240 161.541 1.00 10.93  ? 2189 MET A CA    1 
ATOM   5195  C  C     . MET A 1 2189 ? 167.499 213.211 162.342 1.00 10.09  ? 2189 MET A C     1 
ATOM   5196  O  O     . MET A 1 2189 ? 167.825 212.176 162.932 1.00 8.09   ? 2189 MET A O     1 
ATOM   5197  C  CB    . MET A 1 2189 ? 166.042 211.942 160.748 1.00 10.86  ? 2189 MET A CB    1 
ATOM   5198  C  CG    . MET A 1 2189 ? 164.597 211.522 160.539 1.00 11.26  ? 2189 MET A CG    1 
ATOM   5199  S  SD    . MET A 1 2189 ? 164.426 210.085 159.465 1.00 26.07  ? 2189 MET A SD    1 
ATOM   5200  C  CE    . MET A 1 2189 ? 164.824 208.759 160.598 1.00 7.73   ? 2189 MET A CE    1 
ATOM   5201  N  N     . TYR A 1 2190 ? 168.243 214.319 162.373 1.00 12.75  ? 2190 TYR A N     1 
ATOM   5202  C  CA    . TYR A 1 2190 ? 169.485 214.437 163.142 1.00 10.40  ? 2190 TYR A CA    1 
ATOM   5203  C  C     . TYR A 1 2190 ? 170.521 213.398 162.724 1.00 9.40   ? 2190 TYR A C     1 
ATOM   5204  O  O     . TYR A 1 2190 ? 171.279 212.893 163.554 1.00 9.06   ? 2190 TYR A O     1 
ATOM   5205  C  CB    . TYR A 1 2190 ? 169.218 214.344 164.648 1.00 9.73   ? 2190 TYR A CB    1 
ATOM   5206  C  CG    . TYR A 1 2190 ? 168.076 215.212 165.121 1.00 11.46  ? 2190 TYR A CG    1 
ATOM   5207  C  CD1   . TYR A 1 2190 ? 168.124 216.591 164.983 1.00 12.62  ? 2190 TYR A CD1   1 
ATOM   5208  C  CD2   . TYR A 1 2190 ? 166.944 214.650 165.692 1.00 10.00  ? 2190 TYR A CD2   1 
ATOM   5209  C  CE1   . TYR A 1 2190 ? 167.083 217.386 165.408 1.00 14.88  ? 2190 TYR A CE1   1 
ATOM   5210  C  CE2   . TYR A 1 2190 ? 165.896 215.438 166.119 1.00 14.96  ? 2190 TYR A CE2   1 
ATOM   5211  C  CZ    . TYR A 1 2190 ? 165.970 216.805 165.976 1.00 21.82  ? 2190 TYR A CZ    1 
ATOM   5212  O  OH    . TYR A 1 2190 ? 164.928 217.595 166.400 1.00 31.92  ? 2190 TYR A OH    1 
ATOM   5213  N  N     . LEU A 1 2191 ? 170.568 213.075 161.437 1.00 9.82   ? 2191 LEU A N     1 
ATOM   5214  C  CA    . LEU A 1 2191 ? 171.506 212.099 160.908 1.00 7.02   ? 2191 LEU A CA    1 
ATOM   5215  C  C     . LEU A 1 2191 ? 172.599 212.793 160.107 1.00 7.45   ? 2191 LEU A C     1 
ATOM   5216  O  O     . LEU A 1 2191 ? 172.457 213.941 159.678 1.00 11.58  ? 2191 LEU A O     1 
ATOM   5217  C  CB    . LEU A 1 2191 ? 170.789 211.062 160.038 1.00 6.67   ? 2191 LEU A CB    1 
ATOM   5218  C  CG    . LEU A 1 2191 ? 169.718 210.215 160.731 1.00 6.82   ? 2191 LEU A CG    1 
ATOM   5219  C  CD1   . LEU A 1 2191 ? 169.382 208.998 159.896 1.00 6.45   ? 2191 LEU A CD1   1 
ATOM   5220  C  CD2   . LEU A 1 2191 ? 170.165 209.796 162.121 1.00 6.01   ? 2191 LEU A CD2   1 
ATOM   5221  N  N     . THR A 1 2192 ? 173.700 212.075 159.912 1.00 7.11   ? 2192 THR A N     1 
ATOM   5222  C  CA    . THR A 1 2192 ? 174.872 212.590 159.218 1.00 7.77   ? 2192 THR A CA    1 
ATOM   5223  C  C     . THR A 1 2192 ? 174.831 212.140 157.764 1.00 9.59   ? 2192 THR A C     1 
ATOM   5224  O  O     . THR A 1 2192 ? 174.662 210.949 157.482 1.00 11.79  ? 2192 THR A O     1 
ATOM   5225  C  CB    . THR A 1 2192 ? 176.158 212.109 159.891 1.00 7.63   ? 2192 THR A CB    1 
ATOM   5226  O  OG1   . THR A 1 2192 ? 176.234 212.648 161.216 1.00 12.10  ? 2192 THR A OG1   1 
ATOM   5227  C  CG2   . THR A 1 2192 ? 177.375 212.554 159.100 1.00 8.43   ? 2192 THR A CG2   1 
ATOM   5228  N  N     . TYR A 1 2193 ? 174.980 213.091 156.847 1.00 13.81  ? 2193 TYR A N     1 
ATOM   5229  C  CA    . TYR A 1 2193 ? 174.974 212.822 155.418 1.00 10.49  ? 2193 TYR A CA    1 
ATOM   5230  C  C     . TYR A 1 2193 ? 176.348 213.116 154.830 1.00 12.62  ? 2193 TYR A C     1 
ATOM   5231  O  O     . TYR A 1 2193 ? 177.001 214.092 155.212 1.00 19.67  ? 2193 TYR A O     1 
ATOM   5232  C  CB    . TYR A 1 2193 ? 173.905 213.658 154.710 1.00 10.35  ? 2193 TYR A CB    1 
ATOM   5233  C  CG    . TYR A 1 2193 ? 173.869 213.466 153.213 1.00 15.62  ? 2193 TYR A CG    1 
ATOM   5234  C  CD1   . TYR A 1 2193 ? 174.691 214.209 152.377 1.00 17.92  ? 2193 TYR A CD1   1 
ATOM   5235  C  CD2   . TYR A 1 2193 ? 173.016 212.539 152.635 1.00 14.72  ? 2193 TYR A CD2   1 
ATOM   5236  C  CE1   . TYR A 1 2193 ? 174.665 214.034 151.015 1.00 18.11  ? 2193 TYR A CE1   1 
ATOM   5237  C  CE2   . TYR A 1 2193 ? 172.982 212.357 151.271 1.00 13.10  ? 2193 TYR A CE2   1 
ATOM   5238  C  CZ    . TYR A 1 2193 ? 173.810 213.108 150.466 1.00 17.95  ? 2193 TYR A CZ    1 
ATOM   5239  O  OH    . TYR A 1 2193 ? 173.784 212.935 149.103 1.00 32.25  ? 2193 TYR A OH    1 
ATOM   5240  N  N     . GLY A 1 2194 ? 176.775 212.277 153.899 1.00 12.72  ? 2194 GLY A N     1 
ATOM   5241  C  CA    . GLY A 1 2194 ? 178.050 212.476 153.232 1.00 15.37  ? 2194 GLY A CA    1 
ATOM   5242  C  C     . GLY A 1 2194 ? 178.004 211.940 151.821 1.00 18.02  ? 2194 GLY A C     1 
ATOM   5243  O  O     . GLY A 1 2194 ? 177.212 211.048 151.502 1.00 22.24  ? 2194 GLY A O     1 
ATOM   5244  N  N     . ASP A 1 2195 ? 178.857 212.496 150.965 1.00 26.13  ? 2195 ASP A N     1 
ATOM   5245  C  CA    . ASP A 1 2195 ? 178.982 212.063 149.579 1.00 24.18  ? 2195 ASP A CA    1 
ATOM   5246  C  C     . ASP A 1 2195 ? 180.361 211.457 149.366 1.00 25.84  ? 2195 ASP A C     1 
ATOM   5247  O  O     . ASP A 1 2195 ? 181.377 212.122 149.596 1.00 34.70  ? 2195 ASP A O     1 
ATOM   5248  C  CB    . ASP A 1 2195 ? 178.750 213.229 148.620 1.00 27.55  ? 2195 ASP A CB    1 
ATOM   5249  C  CG    . ASP A 1 2195 ? 177.310 213.693 148.607 1.00 33.54  ? 2195 ASP A CG    1 
ATOM   5250  O  OD1   . ASP A 1 2195 ? 176.421 212.853 148.847 1.00 35.71  ? 2195 ASP A OD1   1 
ATOM   5251  O  OD2   . ASP A 1 2195 ? 177.068 214.894 148.368 1.00 36.48  ? 2195 ASP A OD2   1 
ATOM   5252  N  N     . GLY A 1 2196 ? 180.392 210.207 148.910 1.00 25.70  ? 2196 GLY A N     1 
ATOM   5253  C  CA    . GLY A 1 2196 ? 181.648 209.546 148.621 1.00 26.61  ? 2196 GLY A CA    1 
ATOM   5254  C  C     . GLY A 1 2196 ? 182.487 209.239 149.843 1.00 28.29  ? 2196 GLY A C     1 
ATOM   5255  O  O     . GLY A 1 2196 ? 182.146 208.353 150.634 1.00 28.67  ? 2196 GLY A O     1 
ATOM   5256  N  N     . GLU A 1 2197 ? 183.593 209.964 150.004 1.00 30.46  ? 2197 GLU A N     1 
ATOM   5257  C  CA    . GLU A 1 2197 ? 184.571 209.689 151.046 1.00 26.74  ? 2197 GLU A CA    1 
ATOM   5258  C  C     . GLU A 1 2197 ? 184.415 210.570 152.279 1.00 26.46  ? 2197 GLU A C     1 
ATOM   5259  O  O     . GLU A 1 2197 ? 185.258 210.498 153.178 1.00 31.60  ? 2197 GLU A O     1 
ATOM   5260  C  CB    . GLU A 1 2197 ? 185.989 209.841 150.486 1.00 31.17  ? 2197 GLU A CB    1 
ATOM   5261  C  CG    . GLU A 1 2197 ? 186.347 208.810 149.431 1.00 39.37  ? 2197 GLU A CG    1 
ATOM   5262  C  CD    . GLU A 1 2197 ? 186.421 207.408 149.994 1.00 51.42  ? 2197 GLU A CD    1 
ATOM   5263  O  OE1   . GLU A 1 2197 ? 186.792 207.262 151.177 1.00 51.00  ? 2197 GLU A OE1   1 
ATOM   5264  O  OE2   . GLU A 1 2197 ? 186.105 206.450 149.257 1.00 54.40  ? 2197 GLU A OE2   1 
ATOM   5265  N  N     . GLU A 1 2198 ? 183.374 211.397 152.350 1.00 27.29  ? 2198 GLU A N     1 
ATOM   5266  C  CA    . GLU A 1 2198 ? 183.137 212.178 153.555 1.00 25.35  ? 2198 GLU A CA    1 
ATOM   5267  C  C     . GLU A 1 2198 ? 182.580 211.282 154.662 1.00 22.01  ? 2198 GLU A C     1 
ATOM   5268  O  O     . GLU A 1 2198 ? 182.365 210.080 154.485 1.00 19.35  ? 2198 GLU A O     1 
ATOM   5269  C  CB    . GLU A 1 2198 ? 182.184 213.338 153.276 1.00 21.91  ? 2198 GLU A CB    1 
ATOM   5270  C  CG    . GLU A 1 2198 ? 182.290 213.931 151.888 1.00 26.62  ? 2198 GLU A CG    1 
ATOM   5271  C  CD    . GLU A 1 2198 ? 181.366 215.117 151.693 1.00 37.32  ? 2198 GLU A CD    1 
ATOM   5272  O  OE1   . GLU A 1 2198 ? 180.237 215.087 152.227 1.00 31.32  ? 2198 GLU A OE1   1 
ATOM   5273  O  OE2   . GLU A 1 2198 ? 181.763 216.076 150.999 1.00 54.50  ? 2198 GLU A OE2   1 
ATOM   5274  N  N     . VAL A 1 2199 ? 182.345 211.886 155.826 1.00 16.85  ? 2199 VAL A N     1 
ATOM   5275  C  CA    . VAL A 1 2199 ? 181.760 211.157 156.943 1.00 13.86  ? 2199 VAL A CA    1 
ATOM   5276  C  C     . VAL A 1 2199 ? 180.304 210.847 156.628 1.00 15.09  ? 2199 VAL A C     1 
ATOM   5277  O  O     . VAL A 1 2199 ? 179.512 211.744 156.312 1.00 14.92  ? 2199 VAL A O     1 
ATOM   5278  C  CB    . VAL A 1 2199 ? 181.892 211.963 158.242 1.00 18.50  ? 2199 VAL A CB    1 
ATOM   5279  C  CG1   . VAL A 1 2199 ? 181.226 211.227 159.393 1.00 17.50  ? 2199 VAL A CG1   1 
ATOM   5280  C  CG2   . VAL A 1 2199 ? 183.356 212.231 158.552 1.00 18.73  ? 2199 VAL A CG2   1 
ATOM   5281  N  N     . GLY A 1 2200 ? 179.944 209.569 156.713 1.00 14.98  ? 2200 GLY A N     1 
ATOM   5282  C  CA    . GLY A 1 2200 ? 178.612 209.131 156.360 1.00 10.00  ? 2200 GLY A CA    1 
ATOM   5283  C  C     . GLY A 1 2200 ? 178.400 208.833 154.895 1.00 10.57  ? 2200 GLY A C     1 
ATOM   5284  O  O     . GLY A 1 2200 ? 177.269 208.528 154.501 1.00 14.05  ? 2200 GLY A O     1 
ATOM   5285  N  N     . GLY A 1 2201 ? 179.448 208.913 154.073 1.00 11.21  ? 2201 GLY A N     1 
ATOM   5286  C  CA    . GLY A 1 2201 ? 179.288 208.631 152.657 1.00 12.36  ? 2201 GLY A CA    1 
ATOM   5287  C  C     . GLY A 1 2201 ? 178.945 207.181 152.378 1.00 9.60   ? 2201 GLY A C     1 
ATOM   5288  O  O     . GLY A 1 2201 ? 178.121 206.886 151.508 1.00 9.85   ? 2201 GLY A O     1 
ATOM   5289  N  N     . MET A 1 2202 ? 179.575 206.256 153.106 1.00 10.19  ? 2202 MET A N     1 
ATOM   5290  C  CA    . MET A 1 2202 ? 179.279 204.838 152.927 1.00 6.59   ? 2202 MET A CA    1 
ATOM   5291  C  C     . MET A 1 2202 ? 177.832 204.529 153.287 1.00 7.50   ? 2202 MET A C     1 
ATOM   5292  O  O     . MET A 1 2202 ? 177.187 203.692 152.645 1.00 10.39  ? 2202 MET A O     1 
ATOM   5293  C  CB    . MET A 1 2202 ? 180.236 203.996 153.768 1.00 7.62   ? 2202 MET A CB    1 
ATOM   5294  C  CG    . MET A 1 2202 ? 181.684 204.066 153.314 1.00 11.77  ? 2202 MET A CG    1 
ATOM   5295  S  SD    . MET A 1 2202 ? 182.792 203.128 154.380 1.00 47.14  ? 2202 MET A SD    1 
ATOM   5296  C  CE    . MET A 1 2202 ? 182.315 201.451 153.974 1.00 31.85  ? 2202 MET A CE    1 
ATOM   5297  N  N     . TRP A 1 2203 ? 177.305 205.195 154.316 1.00 7.09   ? 2203 TRP A N     1 
ATOM   5298  C  CA    . TRP A 1 2203 ? 175.906 205.010 154.682 1.00 5.52   ? 2203 TRP A CA    1 
ATOM   5299  C  C     . TRP A 1 2203 ? 174.975 205.461 153.562 1.00 5.05   ? 2203 TRP A C     1 
ATOM   5300  O  O     . TRP A 1 2203 ? 173.987 204.784 153.254 1.00 6.87   ? 2203 TRP A O     1 
ATOM   5301  C  CB    . TRP A 1 2203 ? 175.608 205.766 155.975 1.00 6.30   ? 2203 TRP A CB    1 
ATOM   5302  C  CG    . TRP A 1 2203 ? 174.245 205.515 156.519 1.00 3.36   ? 2203 TRP A CG    1 
ATOM   5303  C  CD1   . TRP A 1 2203 ? 173.819 204.404 157.180 1.00 2.05   ? 2203 TRP A CD1   1 
ATOM   5304  C  CD2   . TRP A 1 2203 ? 173.124 206.400 156.453 1.00 3.53   ? 2203 TRP A CD2   1 
ATOM   5305  N  NE1   . TRP A 1 2203 ? 172.499 204.540 157.529 1.00 2.15   ? 2203 TRP A NE1   1 
ATOM   5306  C  CE2   . TRP A 1 2203 ? 172.049 205.758 157.094 1.00 3.19   ? 2203 TRP A CE2   1 
ATOM   5307  C  CE3   . TRP A 1 2203 ? 172.925 207.673 155.914 1.00 4.74   ? 2203 TRP A CE3   1 
ATOM   5308  C  CZ2   . TRP A 1 2203 ? 170.794 206.345 157.211 1.00 3.53   ? 2203 TRP A CZ2   1 
ATOM   5309  C  CZ3   . TRP A 1 2203 ? 171.679 208.252 156.030 1.00 5.49   ? 2203 TRP A CZ3   1 
ATOM   5310  C  CH2   . TRP A 1 2203 ? 170.629 207.589 156.672 1.00 3.97   ? 2203 TRP A CH2   1 
ATOM   5311  N  N     . VAL A 1 2204 ? 175.275 206.600 152.936 1.00 6.08   ? 2204 VAL A N     1 
ATOM   5312  C  CA    . VAL A 1 2204 ? 174.447 207.076 151.833 1.00 6.00   ? 2204 VAL A CA    1 
ATOM   5313  C  C     . VAL A 1 2204 ? 174.569 206.145 150.633 1.00 5.85   ? 2204 VAL A C     1 
ATOM   5314  O  O     . VAL A 1 2204 ? 173.593 205.908 149.910 1.00 7.35   ? 2204 VAL A O     1 
ATOM   5315  C  CB    . VAL A 1 2204 ? 174.818 208.526 151.474 1.00 7.86   ? 2204 VAL A CB    1 
ATOM   5316  C  CG1   . VAL A 1 2204 ? 173.949 209.032 150.336 1.00 12.30  ? 2204 VAL A CG1   1 
ATOM   5317  C  CG2   . VAL A 1 2204 ? 174.676 209.417 152.694 1.00 7.15   ? 2204 VAL A CG2   1 
ATOM   5318  N  N     . GLU A 1 2205 ? 175.767 205.602 150.400 1.00 6.93   ? 2205 GLU A N     1 
ATOM   5319  C  CA    . GLU A 1 2205 ? 175.933 204.612 149.341 1.00 7.08   ? 2205 GLU A CA    1 
ATOM   5320  C  C     . GLU A 1 2205 ? 175.069 203.387 149.603 1.00 6.82   ? 2205 GLU A C     1 
ATOM   5321  O  O     . GLU A 1 2205 ? 174.440 202.851 148.683 1.00 10.13  ? 2205 GLU A O     1 
ATOM   5322  C  CB    . GLU A 1 2205 ? 177.402 204.208 149.220 1.00 6.94   ? 2205 GLU A CB    1 
ATOM   5323  C  CG    . GLU A 1 2205 ? 178.326 205.317 148.751 1.00 18.20  ? 2205 GLU A CG    1 
ATOM   5324  C  CD    . GLU A 1 2205 ? 178.053 205.743 147.325 1.00 30.76  ? 2205 GLU A CD    1 
ATOM   5325  O  OE1   . GLU A 1 2205 ? 177.634 204.888 146.518 1.00 41.21  ? 2205 GLU A OE1   1 
ATOM   5326  O  OE2   . GLU A 1 2205 ? 178.262 206.932 147.009 1.00 34.17  ? 2205 GLU A OE2   1 
ATOM   5327  N  N     . LYS A 1 2206 ? 175.026 202.933 150.856 1.00 5.12   ? 2206 LYS A N     1 
ATOM   5328  C  CA    . LYS A 1 2206 ? 174.179 201.799 151.208 1.00 3.99   ? 2206 LYS A CA    1 
ATOM   5329  C  C     . LYS A 1 2206 ? 172.704 202.133 151.016 1.00 4.56   ? 2206 LYS A C     1 
ATOM   5330  O  O     . LYS A 1 2206 ? 171.919 201.283 150.585 1.00 5.50   ? 2206 LYS A O     1 
ATOM   5331  C  CB    . LYS A 1 2206 ? 174.453 201.371 152.648 1.00 4.23   ? 2206 LYS A CB    1 
ATOM   5332  C  CG    . LYS A 1 2206 ? 175.722 200.558 152.818 1.00 4.51   ? 2206 LYS A CG    1 
ATOM   5333  C  CD    . LYS A 1 2206 ? 175.640 199.236 152.085 1.00 4.36   ? 2206 LYS A CD    1 
ATOM   5334  C  CE    . LYS A 1 2206 ? 177.005 198.807 151.579 1.00 4.26   ? 2206 LYS A CE    1 
ATOM   5335  N  NZ    . LYS A 1 2206 ? 176.951 197.497 150.880 1.00 4.76   ? 2206 LYS A NZ    1 
ATOM   5336  N  N     . VAL A 1 2207 ? 172.308 203.365 151.343 1.00 5.11   ? 2207 VAL A N     1 
ATOM   5337  C  CA    . VAL A 1 2207 ? 170.920 203.780 151.138 1.00 5.46   ? 2207 VAL A CA    1 
ATOM   5338  C  C     . VAL A 1 2207 ? 170.565 203.753 149.655 1.00 6.45   ? 2207 VAL A C     1 
ATOM   5339  O  O     . VAL A 1 2207 ? 169.484 203.291 149.266 1.00 9.62   ? 2207 VAL A O     1 
ATOM   5340  C  CB    . VAL A 1 2207 ? 170.682 205.173 151.752 1.00 5.41   ? 2207 VAL A CB    1 
ATOM   5341  C  CG1   . VAL A 1 2207 ? 169.316 205.703 151.357 1.00 5.87   ? 2207 VAL A CG1   1 
ATOM   5342  C  CG2   . VAL A 1 2207 ? 170.810 205.117 153.263 1.00 3.65   ? 2207 VAL A CG2   1 
ATOM   5343  N  N     . LEU A 1 2208 ? 171.465 204.251 148.806 1.00 5.09   ? 2208 LEU A N     1 
ATOM   5344  C  CA    . LEU A 1 2208 ? 171.220 204.228 147.366 1.00 4.12   ? 2208 LEU A CA    1 
ATOM   5345  C  C     . LEU A 1 2208 ? 171.171 202.800 146.831 1.00 4.23   ? 2208 LEU A C     1 
ATOM   5346  O  O     . LEU A 1 2208 ? 170.356 202.485 145.954 1.00 6.24   ? 2208 LEU A O     1 
ATOM   5347  C  CB    . LEU A 1 2208 ? 172.291 205.042 146.643 1.00 5.38   ? 2208 LEU A CB    1 
ATOM   5348  C  CG    . LEU A 1 2208 ? 172.308 206.536 146.967 1.00 5.81   ? 2208 LEU A CG    1 
ATOM   5349  C  CD1   . LEU A 1 2208 ? 173.390 207.236 146.178 1.00 10.21  ? 2208 LEU A CD1   1 
ATOM   5350  C  CD2   . LEU A 1 2208 ? 170.955 207.156 146.679 1.00 5.05   ? 2208 LEU A CD2   1 
ATOM   5351  N  N     . GLN A 1 2209 ? 172.036 201.924 147.345 1.00 4.89   ? 2209 GLN A N     1 
ATOM   5352  C  CA    . GLN A 1 2209 ? 171.980 200.517 146.961 1.00 5.41   ? 2209 GLN A CA    1 
ATOM   5353  C  C     . GLN A 1 2209 ? 170.651 199.893 147.366 1.00 5.58   ? 2209 GLN A C     1 
ATOM   5354  O  O     . GLN A 1 2209 ? 170.067 199.109 146.610 1.00 7.32   ? 2209 GLN A O     1 
ATOM   5355  C  CB    . GLN A 1 2209 ? 173.141 199.753 147.593 1.00 3.01   ? 2209 GLN A CB    1 
ATOM   5356  C  CG    . GLN A 1 2209 ? 174.501 200.115 147.039 1.00 3.55   ? 2209 GLN A CG    1 
ATOM   5357  C  CD    . GLN A 1 2209 ? 175.626 199.474 147.817 1.00 3.49   ? 2209 GLN A CD    1 
ATOM   5358  O  OE1   . GLN A 1 2209 ? 175.390 198.746 148.778 1.00 6.14   ? 2209 GLN A OE1   1 
ATOM   5359  N  NE2   . GLN A 1 2209 ? 176.858 199.740 147.407 1.00 3.25   ? 2209 GLN A NE2   1 
ATOM   5360  N  N     . LEU A 1 2210 ? 170.165 200.226 148.563 1.00 4.68   ? 2210 LEU A N     1 
ATOM   5361  C  CA    . LEU A 1 2210 ? 168.870 199.726 149.009 1.00 4.81   ? 2210 LEU A CA    1 
ATOM   5362  C  C     . LEU A 1 2210 ? 167.752 200.227 148.106 1.00 5.07   ? 2210 LEU A C     1 
ATOM   5363  O  O     . LEU A 1 2210 ? 166.815 199.485 147.796 1.00 8.16   ? 2210 LEU A O     1 
ATOM   5364  C  CB    . LEU A 1 2210 ? 168.624 200.143 150.458 1.00 5.25   ? 2210 LEU A CB    1 
ATOM   5365  C  CG    . LEU A 1 2210 ? 167.303 199.726 151.102 1.00 5.67   ? 2210 LEU A CG    1 
ATOM   5366  C  CD1   . LEU A 1 2210 ? 167.254 198.223 151.286 1.00 5.67   ? 2210 LEU A CD1   1 
ATOM   5367  C  CD2   . LEU A 1 2210 ? 167.114 200.437 152.429 1.00 5.27   ? 2210 LEU A CD2   1 
ATOM   5368  N  N     . TYR A 1 2211 ? 167.834 201.489 147.678 1.00 5.09   ? 2211 TYR A N     1 
ATOM   5369  C  CA    . TYR A 1 2211 ? 166.847 202.020 146.742 1.00 5.46   ? 2211 TYR A CA    1 
ATOM   5370  C  C     . TYR A 1 2211 ? 166.865 201.255 145.424 1.00 5.74   ? 2211 TYR A C     1 
ATOM   5371  O  O     . TYR A 1 2211 ? 165.807 200.913 144.878 1.00 6.48   ? 2211 TYR A O     1 
ATOM   5372  C  CB    . TYR A 1 2211 ? 167.106 203.505 146.495 1.00 5.46   ? 2211 TYR A CB    1 
ATOM   5373  C  CG    . TYR A 1 2211 ? 166.221 204.101 145.425 1.00 7.19   ? 2211 TYR A CG    1 
ATOM   5374  C  CD1   . TYR A 1 2211 ? 164.840 204.042 145.527 1.00 7.18   ? 2211 TYR A CD1   1 
ATOM   5375  C  CD2   . TYR A 1 2211 ? 166.769 204.706 144.304 1.00 10.14  ? 2211 TYR A CD2   1 
ATOM   5376  C  CE1   . TYR A 1 2211 ? 164.030 204.578 144.550 1.00 8.86   ? 2211 TYR A CE1   1 
ATOM   5377  C  CE2   . TYR A 1 2211 ? 165.968 205.244 143.322 1.00 12.88  ? 2211 TYR A CE2   1 
ATOM   5378  C  CZ    . TYR A 1 2211 ? 164.598 205.178 143.450 1.00 14.53  ? 2211 TYR A CZ    1 
ATOM   5379  O  OH    . TYR A 1 2211 ? 163.794 205.715 142.471 1.00 38.07  ? 2211 TYR A OH    1 
ATOM   5380  N  N     . GLN A 1 2212 ? 168.059 200.979 144.896 1.00 6.02   ? 2212 GLN A N     1 
ATOM   5381  C  CA    . GLN A 1 2212 ? 168.155 200.224 143.650 1.00 6.49   ? 2212 GLN A CA    1 
ATOM   5382  C  C     . GLN A 1 2212 ? 167.587 198.817 143.808 1.00 6.59   ? 2212 GLN A C     1 
ATOM   5383  O  O     . GLN A 1 2212 ? 166.870 198.323 142.927 1.00 8.21   ? 2212 GLN A O     1 
ATOM   5384  C  CB    . GLN A 1 2212 ? 169.608 200.166 143.180 1.00 8.78   ? 2212 GLN A CB    1 
ATOM   5385  C  CG    . GLN A 1 2212 ? 170.202 201.518 142.834 1.00 12.49  ? 2212 GLN A CG    1 
ATOM   5386  C  CD    . GLN A 1 2212 ? 171.606 201.412 142.274 1.00 22.43  ? 2212 GLN A CD    1 
ATOM   5387  O  OE1   . GLN A 1 2212 ? 171.888 201.898 141.180 1.00 27.38  ? 2212 GLN A OE1   1 
ATOM   5388  N  NE2   . GLN A 1 2212 ? 172.495 200.770 143.023 1.00 20.22  ? 2212 GLN A NE2   1 
ATOM   5389  N  N     . ILE A 1 2213 ? 167.893 198.158 144.928 1.00 5.35   ? 2213 ILE A N     1 
ATOM   5390  C  CA    . ILE A 1 2213 ? 167.373 196.813 145.161 1.00 6.34   ? 2213 ILE A CA    1 
ATOM   5391  C  C     . ILE A 1 2213 ? 165.854 196.843 145.287 1.00 7.49   ? 2213 ILE A C     1 
ATOM   5392  O  O     . ILE A 1 2213 ? 165.160 195.941 144.804 1.00 9.35   ? 2213 ILE A O     1 
ATOM   5393  C  CB    . ILE A 1 2213 ? 168.040 196.182 146.398 1.00 8.03   ? 2213 ILE A CB    1 
ATOM   5394  C  CG1   . ILE A 1 2213 ? 169.549 196.059 146.186 1.00 6.99   ? 2213 ILE A CG1   1 
ATOM   5395  C  CG2   . ILE A 1 2213 ? 167.461 194.808 146.673 1.00 7.80   ? 2213 ILE A CG2   1 
ATOM   5396  C  CD1   . ILE A 1 2213 ? 169.944 195.020 145.164 1.00 6.50   ? 2213 ILE A CD1   1 
ATOM   5397  N  N     . THR A 1 2214 ? 165.313 197.881 145.931 1.00 7.64   ? 2214 THR A N     1 
ATOM   5398  C  CA    . THR A 1 2214 ? 163.863 198.048 145.980 1.00 6.28   ? 2214 THR A CA    1 
ATOM   5399  C  C     . THR A 1 2214 ? 163.289 198.182 144.578 1.00 7.92   ? 2214 THR A C     1 
ATOM   5400  O  O     . THR A 1 2214 ? 162.247 197.594 144.262 1.00 9.20   ? 2214 THR A O     1 
ATOM   5401  C  CB    . THR A 1 2214 ? 163.499 199.278 146.817 1.00 7.36   ? 2214 THR A CB    1 
ATOM   5402  O  OG1   . THR A 1 2214 ? 163.713 199.007 148.205 1.00 10.44  ? 2214 THR A OG1   1 
ATOM   5403  C  CG2   . THR A 1 2214 ? 162.042 199.659 146.612 1.00 8.12   ? 2214 THR A CG2   1 
ATOM   5404  N  N     . GLN A 1 2215 ? 163.965 198.947 143.721 1.00 13.55  ? 2215 GLN A N     1 
ATOM   5405  C  CA    . GLN A 1 2215 ? 163.487 199.128 142.354 1.00 11.19  ? 2215 GLN A CA    1 
ATOM   5406  C  C     . GLN A 1 2215 ? 163.522 197.820 141.574 1.00 12.76  ? 2215 GLN A C     1 
ATOM   5407  O  O     . GLN A 1 2215 ? 162.680 197.590 140.698 1.00 13.75  ? 2215 GLN A O     1 
ATOM   5408  C  CB    . GLN A 1 2215 ? 164.321 200.196 141.646 1.00 9.50   ? 2215 GLN A CB    1 
ATOM   5409  C  CG    . GLN A 1 2215 ? 164.055 201.615 142.120 1.00 10.83  ? 2215 GLN A CG    1 
ATOM   5410  C  CD    . GLN A 1 2215 ? 162.730 202.161 141.628 1.00 26.68  ? 2215 GLN A CD    1 
ATOM   5411  O  OE1   . GLN A 1 2215 ? 161.669 201.810 142.145 1.00 29.86  ? 2215 GLN A OE1   1 
ATOM   5412  N  NE2   . GLN A 1 2215 ? 162.783 203.026 140.623 1.00 27.01  ? 2215 GLN A NE2   1 
ATOM   5413  N  N     . ILE A 1 2216 ? 164.489 196.947 141.873 1.00 12.74  ? 2216 ILE A N     1 
ATOM   5414  C  CA    . ILE A 1 2216 ? 164.668 195.727 141.087 1.00 11.72  ? 2216 ILE A CA    1 
ATOM   5415  C  C     . ILE A 1 2216 ? 164.086 194.485 141.762 1.00 8.71   ? 2216 ILE A C     1 
ATOM   5416  O  O     . ILE A 1 2216 ? 163.783 193.504 141.064 1.00 7.06   ? 2216 ILE A O     1 
ATOM   5417  C  CB    . ILE A 1 2216 ? 166.161 195.500 140.756 1.00 10.88  ? 2216 ILE A CB    1 
ATOM   5418  C  CG1   . ILE A 1 2216 ? 166.325 194.423 139.681 1.00 14.35  ? 2216 ILE A CG1   1 
ATOM   5419  C  CG2   . ILE A 1 2216 ? 166.935 195.108 142.001 1.00 11.54  ? 2216 ILE A CG2   1 
ATOM   5420  C  CD1   . ILE A 1 2216 ? 165.760 194.819 138.334 1.00 14.73  ? 2216 ILE A CD1   1 
ATOM   5421  N  N     . ASN A 1 2217 ? 163.894 194.500 143.079 1.00 10.95  ? 2217 ASN A N     1 
ATOM   5422  C  CA    . ASN A 1 2217 ? 163.420 193.330 143.807 1.00 9.84   ? 2217 ASN A CA    1 
ATOM   5423  C  C     . ASN A 1 2217 ? 162.180 193.683 144.614 1.00 8.79   ? 2217 ASN A C     1 
ATOM   5424  O  O     . ASN A 1 2217 ? 162.075 194.788 145.153 1.00 11.61  ? 2217 ASN A O     1 
ATOM   5425  C  CB    . ASN A 1 2217 ? 164.502 192.781 144.747 1.00 7.23   ? 2217 ASN A CB    1 
ATOM   5426  C  CG    . ASN A 1 2217 ? 165.441 191.813 144.058 1.00 12.01  ? 2217 ASN A CG    1 
ATOM   5427  O  OD1   . ASN A 1 2217 ? 166.607 192.126 143.820 1.00 14.29  ? 2217 ASN A OD1   1 
ATOM   5428  N  ND2   . ASN A 1 2217 ? 164.939 190.628 143.739 1.00 10.73  ? 2217 ASN A ND2   1 
ATOM   5429  N  N     . HIS A 1 2218 ? 161.238 192.743 144.687 1.00 7.43   ? 2218 HIS A N     1 
ATOM   5430  C  CA    . HIS A 1 2218 ? 160.091 192.869 145.576 1.00 6.07   ? 2218 HIS A CA    1 
ATOM   5431  C  C     . HIS A 1 2218 ? 160.316 192.180 146.913 1.00 5.59   ? 2218 HIS A C     1 
ATOM   5432  O  O     . HIS A 1 2218 ? 159.464 192.278 147.802 1.00 4.85   ? 2218 HIS A O     1 
ATOM   5433  C  CB    . HIS A 1 2218 ? 158.829 192.308 144.912 1.00 5.51   ? 2218 HIS A CB    1 
ATOM   5434  C  CG    . HIS A 1 2218 ? 158.837 190.820 144.753 1.00 5.42   ? 2218 HIS A CG    1 
ATOM   5435  N  ND1   . HIS A 1 2218 ? 159.667 190.171 143.865 1.00 7.88   ? 2218 HIS A ND1   1 
ATOM   5436  C  CD2   . HIS A 1 2218 ? 158.113 189.855 145.365 1.00 6.28   ? 2218 HIS A CD2   1 
ATOM   5437  C  CE1   . HIS A 1 2218 ? 159.455 188.869 143.939 1.00 7.04   ? 2218 HIS A CE1   1 
ATOM   5438  N  NE2   . HIS A 1 2218 ? 158.518 188.651 144.843 1.00 7.74   ? 2218 HIS A NE2   1 
ATOM   5439  N  N     . GLY A 1 2219 ? 161.438 191.487 147.071 1.00 7.07   ? 2219 GLY A N     1 
ATOM   5440  C  CA    . GLY A 1 2219 ? 161.829 190.935 148.348 1.00 5.35   ? 2219 GLY A CA    1 
ATOM   5441  C  C     . GLY A 1 2219 ? 163.250 191.332 148.683 1.00 6.94   ? 2219 GLY A C     1 
ATOM   5442  O  O     . GLY A 1 2219 ? 164.195 190.964 147.979 1.00 8.57   ? 2219 GLY A O     1 
ATOM   5443  N  N     . LEU A 1 2220 ? 163.412 192.081 149.765 1.00 10.17  ? 2220 LEU A N     1 
ATOM   5444  C  CA    . LEU A 1 2220 ? 164.693 192.667 150.116 1.00 6.16   ? 2220 LEU A CA    1 
ATOM   5445  C  C     . LEU A 1 2220 ? 165.120 192.173 151.484 1.00 8.05   ? 2220 LEU A C     1 
ATOM   5446  O  O     . LEU A 1 2220 ? 164.300 191.701 152.274 1.00 10.11  ? 2220 LEU A O     1 
ATOM   5447  C  CB    . LEU A 1 2220 ? 164.636 194.188 150.154 1.00 4.93   ? 2220 LEU A CB    1 
ATOM   5448  C  CG    . LEU A 1 2220 ? 164.646 194.962 148.843 1.00 8.99   ? 2220 LEU A CG    1 
ATOM   5449  C  CD1   . LEU A 1 2220 ? 163.328 194.822 148.091 1.00 10.31  ? 2220 LEU A CD1   1 
ATOM   5450  C  CD2   . LEU A 1 2220 ? 164.956 196.402 149.129 1.00 11.58  ? 2220 LEU A CD2   1 
ATOM   5451  N  N     . MET A 1 2221 ? 166.417 192.284 151.756 1.00 7.18   ? 2221 MET A N     1 
ATOM   5452  C  CA    . MET A 1 2221 ? 166.937 191.970 153.076 1.00 8.31   ? 2221 MET A CA    1 
ATOM   5453  C  C     . MET A 1 2221 ? 168.173 192.812 153.370 1.00 7.64   ? 2221 MET A C     1 
ATOM   5454  O  O     . MET A 1 2221 ? 169.045 192.977 152.509 1.00 8.51   ? 2221 MET A O     1 
ATOM   5455  C  CB    . MET A 1 2221 ? 167.232 190.475 153.177 1.00 5.40   ? 2221 MET A CB    1 
ATOM   5456  C  CG    . MET A 1 2221 ? 167.665 190.006 154.542 1.00 7.20   ? 2221 MET A CG    1 
ATOM   5457  S  SD    . MET A 1 2221 ? 167.956 188.242 154.510 1.00 39.92  ? 2221 MET A SD    1 
ATOM   5458  C  CE    . MET A 1 2221 ? 166.285 187.626 154.392 1.00 6.62   ? 2221 MET A CE    1 
ATOM   5459  N  N     . MET A 1 2222 ? 168.219 193.365 154.584 1.00 5.76   ? 2222 MET A N     1 
ATOM   5460  C  CA    . MET A 1 2222 ? 169.285 194.254 155.036 1.00 4.44   ? 2222 MET A CA    1 
ATOM   5461  C  C     . MET A 1 2222 ? 170.083 193.507 156.100 1.00 4.82   ? 2222 MET A C     1 
ATOM   5462  O  O     . MET A 1 2222 ? 169.650 193.394 157.249 1.00 5.81   ? 2222 MET A O     1 
ATOM   5463  C  CB    . MET A 1 2222 ? 168.705 195.558 155.573 1.00 4.57   ? 2222 MET A CB    1 
ATOM   5464  C  CG    . MET A 1 2222 ? 168.118 196.444 154.489 1.00 6.46   ? 2222 MET A CG    1 
ATOM   5465  S  SD    . MET A 1 2222 ? 167.285 197.888 155.159 1.00 21.32  ? 2222 MET A SD    1 
ATOM   5466  C  CE    . MET A 1 2222 ? 165.652 197.208 155.433 1.00 8.58   ? 2222 MET A CE    1 
ATOM   5467  N  N     . VAL A 1 2223 ? 171.246 193.004 155.714 1.00 4.06   ? 2223 VAL A N     1 
ATOM   5468  C  CA    . VAL A 1 2223 ? 172.044 192.131 156.563 1.00 4.28   ? 2223 VAL A CA    1 
ATOM   5469  C  C     . VAL A 1 2223 ? 173.250 192.904 157.073 1.00 5.29   ? 2223 VAL A C     1 
ATOM   5470  O  O     . VAL A 1 2223 ? 173.891 193.659 156.334 1.00 6.18   ? 2223 VAL A O     1 
ATOM   5471  C  CB    . VAL A 1 2223 ? 172.474 190.859 155.800 1.00 4.35   ? 2223 VAL A CB    1 
ATOM   5472  C  CG1   . VAL A 1 2223 ? 173.374 189.986 156.662 1.00 4.77   ? 2223 VAL A CG1   1 
ATOM   5473  C  CG2   . VAL A 1 2223 ? 171.251 190.082 155.326 1.00 5.19   ? 2223 VAL A CG2   1 
ATOM   5474  N  N     . GLY A 1 2224 ? 173.551 192.731 158.356 1.00 4.00   ? 2224 GLY A N     1 
ATOM   5475  C  CA    . GLY A 1 2224 ? 174.719 193.333 158.947 1.00 3.04   ? 2224 GLY A CA    1 
ATOM   5476  C  C     . GLY A 1 2224 ? 174.686 193.276 160.458 1.00 5.42   ? 2224 GLY A C     1 
ATOM   5477  O  O     . GLY A 1 2224 ? 173.629 193.098 161.066 1.00 5.78   ? 2224 GLY A O     1 
ATOM   5478  N  N     . PRO A 1 2225 ? 175.845 193.440 161.095 1.00 6.54   ? 2225 PRO A N     1 
ATOM   5479  C  CA    . PRO A 1 2225 ? 175.899 193.381 162.559 1.00 4.27   ? 2225 PRO A CA    1 
ATOM   5480  C  C     . PRO A 1 2225 ? 175.013 194.443 163.191 1.00 4.48   ? 2225 PRO A C     1 
ATOM   5481  O  O     . PRO A 1 2225 ? 174.635 195.433 162.561 1.00 7.06   ? 2225 PRO A O     1 
ATOM   5482  C  CB    . PRO A 1 2225 ? 177.378 193.633 162.873 1.00 5.98   ? 2225 PRO A CB    1 
ATOM   5483  C  CG    . PRO A 1 2225 ? 178.097 193.273 161.622 1.00 6.02   ? 2225 PRO A CG    1 
ATOM   5484  C  CD    . PRO A 1 2225 ? 177.178 193.632 160.502 1.00 5.51   ? 2225 PRO A CD    1 
ATOM   5485  N  N     . SER A 1 2226 ? 174.672 194.215 164.458 1.00 4.47   ? 2226 SER A N     1 
ATOM   5486  C  CA    . SER A 1 2226 ? 173.758 195.110 165.154 1.00 4.85   ? 2226 SER A CA    1 
ATOM   5487  C  C     . SER A 1 2226 ? 174.311 196.528 165.180 1.00 4.12   ? 2226 SER A C     1 
ATOM   5488  O  O     . SER A 1 2226 ? 175.499 196.748 165.425 1.00 7.79   ? 2226 SER A O     1 
ATOM   5489  C  CB    . SER A 1 2226 ? 173.506 194.618 166.579 1.00 5.07   ? 2226 SER A CB    1 
ATOM   5490  O  OG    . SER A 1 2226 ? 172.437 195.329 167.178 1.00 4.51   ? 2226 SER A OG    1 
ATOM   5491  N  N     . GLY A 1 2227 ? 173.434 197.491 164.926 1.00 3.27   ? 2227 GLY A N     1 
ATOM   5492  C  CA    . GLY A 1 2227 ? 173.840 198.881 164.874 1.00 3.01   ? 2227 GLY A CA    1 
ATOM   5493  C  C     . GLY A 1 2227 ? 174.753 199.243 163.725 1.00 3.75   ? 2227 GLY A C     1 
ATOM   5494  O  O     . GLY A 1 2227 ? 175.745 199.952 163.927 1.00 7.04   ? 2227 GLY A O     1 
ATOM   5495  N  N     . SER A 1 2228 ? 174.446 198.766 162.521 1.00 4.67   ? 2228 SER A N     1 
ATOM   5496  C  CA    . SER A 1 2228 ? 175.164 199.158 161.318 1.00 4.45   ? 2228 SER A CA    1 
ATOM   5497  C  C     . SER A 1 2228 ? 174.403 200.199 160.506 1.00 3.63   ? 2228 SER A C     1 
ATOM   5498  O  O     . SER A 1 2228 ? 174.806 200.512 159.382 1.00 6.90   ? 2228 SER A O     1 
ATOM   5499  C  CB    . SER A 1 2228 ? 175.466 197.929 160.459 1.00 5.25   ? 2228 SER A CB    1 
ATOM   5500  O  OG    . SER A 1 2228 ? 174.335 197.083 160.359 1.00 5.02   ? 2228 SER A OG    1 
ATOM   5501  N  N     . GLY A 1 2229 ? 173.315 200.741 161.047 1.00 2.33   ? 2229 GLY A N     1 
ATOM   5502  C  CA    . GLY A 1 2229 ? 172.572 201.787 160.377 1.00 3.20   ? 2229 GLY A CA    1 
ATOM   5503  C  C     . GLY A 1 2229 ? 171.477 201.325 159.446 1.00 3.47   ? 2229 GLY A C     1 
ATOM   5504  O  O     . GLY A 1 2229 ? 171.039 202.109 158.598 1.00 7.10   ? 2229 GLY A O     1 
ATOM   5505  N  N     . LYS A 1 2230 ? 171.017 200.080 159.575 1.00 1.85   ? 2230 LYS A N     1 
ATOM   5506  C  CA    . LYS A 1 2230 ? 170.016 199.547 158.655 1.00 1.57   ? 2230 LYS A CA    1 
ATOM   5507  C  C     . LYS A 1 2230 ? 168.662 200.220 158.845 1.00 3.06   ? 2230 LYS A C     1 
ATOM   5508  O  O     . LYS A 1 2230 ? 168.014 200.628 157.869 1.00 5.76   ? 2230 LYS A O     1 
ATOM   5509  C  CB    . LYS A 1 2230 ? 169.892 198.038 158.851 1.00 4.07   ? 2230 LYS A CB    1 
ATOM   5510  C  CG    . LYS A 1 2230 ? 171.207 197.288 158.779 1.00 2.47   ? 2230 LYS A CG    1 
ATOM   5511  C  CD    . LYS A 1 2230 ? 171.043 195.857 159.247 1.00 3.08   ? 2230 LYS A CD    1 
ATOM   5512  C  CE    . LYS A 1 2230 ? 170.561 195.812 160.685 1.00 3.39   ? 2230 LYS A CE    1 
ATOM   5513  N  NZ    . LYS A 1 2230 ? 170.649 194.452 161.276 1.00 3.59   ? 2230 LYS A NZ    1 
ATOM   5514  N  N     . SER A 1 2231 ? 168.206 200.322 160.097 1.00 2.91   ? 2231 SER A N     1 
ATOM   5515  C  CA    . SER A 1 2231 ? 166.884 200.878 160.368 1.00 2.44   ? 2231 SER A CA    1 
ATOM   5516  C  C     . SER A 1 2231 ? 166.794 202.322 159.904 1.00 2.87   ? 2231 SER A C     1 
ATOM   5517  O  O     . SER A 1 2231 ? 165.839 202.711 159.218 1.00 3.23   ? 2231 SER A O     1 
ATOM   5518  C  CB    . SER A 1 2231 ? 166.564 200.775 161.858 1.00 2.39   ? 2231 SER A CB    1 
ATOM   5519  O  OG    . SER A 1 2231 ? 166.553 199.428 162.290 1.00 3.23   ? 2231 SER A OG    1 
ATOM   5520  N  N     . MET A 1 2232 ? 167.785 203.132 160.276 1.00 3.13   ? 2232 MET A N     1 
ATOM   5521  C  CA    . MET A 1 2232 ? 167.817 204.514 159.820 1.00 3.09   ? 2232 MET A CA    1 
ATOM   5522  C  C     . MET A 1 2232 ? 167.901 204.583 158.305 1.00 3.21   ? 2232 MET A C     1 
ATOM   5523  O  O     . MET A 1 2232 ? 167.280 205.451 157.686 1.00 4.99   ? 2232 MET A O     1 
ATOM   5524  C  CB    . MET A 1 2232 ? 168.986 205.255 160.464 1.00 2.82   ? 2232 MET A CB    1 
ATOM   5525  C  CG    . MET A 1 2232 ? 168.882 205.543 161.971 1.00 2.92   ? 2232 MET A CG    1 
ATOM   5526  S  SD    . MET A 1 2232 ? 167.417 206.408 162.605 1.00 14.44  ? 2232 MET A SD    1 
ATOM   5527  C  CE    . MET A 1 2232 ? 166.166 205.127 162.684 1.00 4.08   ? 2232 MET A CE    1 
ATOM   5528  N  N     . ALA A 1 2233 ? 168.642 203.659 157.691 1.00 3.00   ? 2233 ALA A N     1 
ATOM   5529  C  CA    . ALA A 1 2233 ? 168.757 203.650 156.238 1.00 2.40   ? 2233 ALA A CA    1 
ATOM   5530  C  C     . ALA A 1 2233 ? 167.395 203.494 155.578 1.00 3.11   ? 2233 ALA A C     1 
ATOM   5531  O  O     . ALA A 1 2233 ? 167.007 204.312 154.735 1.00 4.31   ? 2233 ALA A O     1 
ATOM   5532  C  CB    . ALA A 1 2233 ? 169.699 202.535 155.789 1.00 1.97   ? 2233 ALA A CB    1 
ATOM   5533  N  N     . TRP A 1 2234 ? 166.637 202.465 155.965 1.00 3.33   ? 2234 TRP A N     1 
ATOM   5534  C  CA    . TRP A 1 2234 ? 165.372 202.248 155.268 1.00 2.48   ? 2234 TRP A CA    1 
ATOM   5535  C  C     . TRP A 1 2234 ? 164.321 203.281 155.662 1.00 3.31   ? 2234 TRP A C     1 
ATOM   5536  O  O     . TRP A 1 2234 ? 163.498 203.664 154.823 1.00 4.71   ? 2234 TRP A O     1 
ATOM   5537  C  CB    . TRP A 1 2234 ? 164.864 200.814 155.474 1.00 2.56   ? 2234 TRP A CB    1 
ATOM   5538  C  CG    . TRP A 1 2234 ? 164.336 200.463 156.829 1.00 2.53   ? 2234 TRP A CG    1 
ATOM   5539  C  CD1   . TRP A 1 2234 ? 164.983 199.755 157.795 1.00 2.44   ? 2234 TRP A CD1   1 
ATOM   5540  C  CD2   . TRP A 1 2234 ? 163.035 200.758 157.352 1.00 2.75   ? 2234 TRP A CD2   1 
ATOM   5541  N  NE1   . TRP A 1 2234 ? 164.180 199.611 158.896 1.00 3.34   ? 2234 TRP A NE1   1 
ATOM   5542  C  CE2   . TRP A 1 2234 ? 162.978 200.219 158.650 1.00 2.78   ? 2234 TRP A CE2   1 
ATOM   5543  C  CE3   . TRP A 1 2234 ? 161.920 201.438 156.856 1.00 2.68   ? 2234 TRP A CE3   1 
ATOM   5544  C  CZ2   . TRP A 1 2234 ? 161.852 200.337 159.456 1.00 2.53   ? 2234 TRP A CZ2   1 
ATOM   5545  C  CZ3   . TRP A 1 2234 ? 160.807 201.555 157.657 1.00 2.68   ? 2234 TRP A CZ3   1 
ATOM   5546  C  CH2   . TRP A 1 2234 ? 160.779 201.007 158.942 1.00 3.44   ? 2234 TRP A CH2   1 
ATOM   5547  N  N     . ARG A 1 2235 ? 164.348 203.780 156.901 1.00 3.21   ? 2235 ARG A N     1 
ATOM   5548  C  CA    . ARG A 1 2235 ? 163.406 204.832 157.275 1.00 2.91   ? 2235 ARG A CA    1 
ATOM   5549  C  C     . ARG A 1 2235 ? 163.672 206.118 156.497 1.00 4.62   ? 2235 ARG A C     1 
ATOM   5550  O  O     . ARG A 1 2235 ? 162.738 206.765 156.000 1.00 8.76   ? 2235 ARG A O     1 
ATOM   5551  C  CB    . ARG A 1 2235 ? 163.480 205.090 158.779 1.00 3.18   ? 2235 ARG A CB    1 
ATOM   5552  C  CG    . ARG A 1 2235 ? 162.889 203.981 159.626 1.00 3.21   ? 2235 ARG A CG    1 
ATOM   5553  C  CD    . ARG A 1 2235 ? 163.095 204.279 161.094 1.00 5.62   ? 2235 ARG A CD    1 
ATOM   5554  N  NE    . ARG A 1 2235 ? 162.672 203.183 161.954 1.00 10.88  ? 2235 ARG A NE    1 
ATOM   5555  C  CZ    . ARG A 1 2235 ? 161.410 202.912 162.256 1.00 11.14  ? 2235 ARG A CZ    1 
ATOM   5556  N  NH1   . ARG A 1 2235 ? 160.411 203.625 161.761 1.00 6.73   ? 2235 ARG A NH1   1 
ATOM   5557  N  NH2   . ARG A 1 2235 ? 161.144 201.905 163.081 1.00 11.76  ? 2235 ARG A NH2   1 
ATOM   5558  N  N     . VAL A 1 2236 ? 164.944 206.506 156.384 1.00 3.68   ? 2236 VAL A N     1 
ATOM   5559  C  CA    . VAL A 1 2236 ? 165.301 207.705 155.637 1.00 3.63   ? 2236 VAL A CA    1 
ATOM   5560  C  C     . VAL A 1 2236 ? 164.969 207.527 154.165 1.00 6.22   ? 2236 VAL A C     1 
ATOM   5561  O  O     . VAL A 1 2236 ? 164.495 208.460 153.506 1.00 9.91   ? 2236 VAL A O     1 
ATOM   5562  C  CB    . VAL A 1 2236 ? 166.788 208.042 155.856 1.00 4.75   ? 2236 VAL A CB    1 
ATOM   5563  C  CG1   . VAL A 1 2236 ? 167.296 208.984 154.781 1.00 11.37  ? 2236 VAL A CG1   1 
ATOM   5564  C  CG2   . VAL A 1 2236 ? 166.987 208.653 157.227 1.00 5.31   ? 2236 VAL A CG2   1 
ATOM   5565  N  N     . LEU A 1 2237 ? 165.203 206.327 153.624 1.00 5.83   ? 2237 LEU A N     1 
ATOM   5566  C  CA    . LEU A 1 2237 ? 164.830 206.067 152.239 1.00 4.38   ? 2237 LEU A CA    1 
ATOM   5567  C  C     . LEU A 1 2237 ? 163.328 206.208 152.038 1.00 4.57   ? 2237 LEU A C     1 
ATOM   5568  O  O     . LEU A 1 2237 ? 162.883 206.784 151.041 1.00 6.92   ? 2237 LEU A O     1 
ATOM   5569  C  CB    . LEU A 1 2237 ? 165.300 204.675 151.817 1.00 4.34   ? 2237 LEU A CB    1 
ATOM   5570  C  CG    . LEU A 1 2237 ? 164.984 204.289 150.372 1.00 6.02   ? 2237 LEU A CG    1 
ATOM   5571  C  CD1   . LEU A 1 2237 ? 165.630 205.264 149.406 1.00 4.97   ? 2237 LEU A CD1   1 
ATOM   5572  C  CD2   . LEU A 1 2237 ? 165.438 202.871 150.083 1.00 5.08   ? 2237 LEU A CD2   1 
ATOM   5573  N  N     . LEU A 1 2238 ? 162.532 205.693 152.977 1.00 4.26   ? 2238 LEU A N     1 
ATOM   5574  C  CA    . LEU A 1 2238 ? 161.081 205.800 152.860 1.00 5.64   ? 2238 LEU A CA    1 
ATOM   5575  C  C     . LEU A 1 2238 ? 160.634 207.258 152.878 1.00 8.71   ? 2238 LEU A C     1 
ATOM   5576  O  O     . LEU A 1 2238 ? 159.823 207.683 152.044 1.00 11.32  ? 2238 LEU A O     1 
ATOM   5577  C  CB    . LEU A 1 2238 ? 160.414 205.014 153.989 1.00 4.03   ? 2238 LEU A CB    1 
ATOM   5578  C  CG    . LEU A 1 2238 ? 158.924 204.697 153.857 1.00 4.63   ? 2238 LEU A CG    1 
ATOM   5579  C  CD1   . LEU A 1 2238 ? 158.654 203.904 152.593 1.00 3.97   ? 2238 LEU A CD1   1 
ATOM   5580  C  CD2   . LEU A 1 2238 ? 158.432 203.944 155.078 1.00 4.79   ? 2238 LEU A CD2   1 
ATOM   5581  N  N     . LYS A 1 2239 ? 161.168 208.045 153.816 1.00 7.67   ? 2239 LYS A N     1 
ATOM   5582  C  CA    . LYS A 1 2239 ? 160.784 209.454 153.891 1.00 8.00   ? 2239 LYS A CA    1 
ATOM   5583  C  C     . LYS A 1 2239 ? 161.223 210.222 152.647 1.00 12.97  ? 2239 LYS A C     1 
ATOM   5584  O  O     . LYS A 1 2239 ? 160.469 211.054 152.122 1.00 16.38  ? 2239 LYS A O     1 
ATOM   5585  C  CB    . LYS A 1 2239 ? 161.363 210.093 155.152 1.00 13.18  ? 2239 LYS A CB    1 
ATOM   5586  C  CG    . LYS A 1 2239 ? 160.835 209.490 156.441 1.00 20.12  ? 2239 LYS A CG    1 
ATOM   5587  C  CD    . LYS A 1 2239 ? 161.057 210.416 157.623 1.00 19.65  ? 2239 LYS A CD    1 
ATOM   5588  C  CE    . LYS A 1 2239 ? 160.551 209.788 158.909 1.00 23.45  ? 2239 LYS A CE    1 
ATOM   5589  N  NZ    . LYS A 1 2239 ? 160.475 210.774 160.021 1.00 33.74  ? 2239 LYS A NZ    1 
ATOM   5590  N  N     . ALA A 1 2240 ? 162.437 209.956 152.158 1.00 11.61  ? 2240 ALA A N     1 
ATOM   5591  C  CA    . ALA A 1 2240 ? 162.924 210.640 150.966 1.00 10.87  ? 2240 ALA A CA    1 
ATOM   5592  C  C     . ALA A 1 2240 ? 162.102 210.271 149.740 1.00 11.67  ? 2240 ALA A C     1 
ATOM   5593  O  O     . ALA A 1 2240 ? 161.817 211.127 148.897 1.00 15.65  ? 2240 ALA A O     1 
ATOM   5594  C  CB    . ALA A 1 2240 ? 164.398 210.317 150.741 1.00 12.31  ? 2240 ALA A CB    1 
ATOM   5595  N  N     . LEU A 1 2241 ? 161.719 208.999 149.614 1.00 12.43  ? 2241 LEU A N     1 
ATOM   5596  C  CA    . LEU A 1 2241 ? 160.875 208.595 148.496 1.00 12.03  ? 2241 LEU A CA    1 
ATOM   5597  C  C     . LEU A 1 2241 ? 159.503 209.245 148.585 1.00 12.23  ? 2241 LEU A C     1 
ATOM   5598  O  O     . LEU A 1 2241 ? 158.924 209.627 147.562 1.00 14.25  ? 2241 LEU A O     1 
ATOM   5599  C  CB    . LEU A 1 2241 ? 160.751 207.074 148.448 1.00 8.31   ? 2241 LEU A CB    1 
ATOM   5600  C  CG    . LEU A 1 2241 ? 161.980 206.337 147.916 1.00 7.18   ? 2241 LEU A CG    1 
ATOM   5601  C  CD1   . LEU A 1 2241 ? 161.676 204.866 147.705 1.00 12.41  ? 2241 LEU A CD1   1 
ATOM   5602  C  CD2   . LEU A 1 2241 ? 162.466 206.981 146.631 1.00 8.45   ? 2241 LEU A CD2   1 
ATOM   5603  N  N     . GLU A 1 2242 ? 158.965 209.379 149.800 1.00 16.33  ? 2242 GLU A N     1 
ATOM   5604  C  CA    . GLU A 1 2242 ? 157.690 210.068 149.962 1.00 17.92  ? 2242 GLU A CA    1 
ATOM   5605  C  C     . GLU A 1 2242 ? 157.795 211.527 149.539 1.00 19.60  ? 2242 GLU A C     1 
ATOM   5606  O  O     . GLU A 1 2242 ? 156.890 212.059 148.885 1.00 24.48  ? 2242 GLU A O     1 
ATOM   5607  C  CB    . GLU A 1 2242 ? 157.211 209.962 151.408 1.00 17.42  ? 2242 GLU A CB    1 
ATOM   5608  C  CG    . GLU A 1 2242 ? 155.901 210.682 151.674 1.00 24.49  ? 2242 GLU A CG    1 
ATOM   5609  C  CD    . GLU A 1 2242 ? 155.494 210.635 153.132 1.00 40.68  ? 2242 GLU A CD    1 
ATOM   5610  O  OE1   . GLU A 1 2242 ? 155.897 209.684 153.833 1.00 42.15  ? 2242 GLU A OE1   1 
ATOM   5611  O  OE2   . GLU A 1 2242 ? 154.770 211.551 153.577 1.00 45.27  ? 2242 GLU A OE2   1 
ATOM   5612  N  N     . ARG A 1 2243 ? 158.893 212.192 149.898 1.00 22.06  ? 2243 ARG A N     1 
ATOM   5613  C  CA    . ARG A 1 2243 ? 159.045 213.600 149.550 1.00 20.35  ? 2243 ARG A CA    1 
ATOM   5614  C  C     . ARG A 1 2243 ? 159.498 213.825 148.112 1.00 20.51  ? 2243 ARG A C     1 
ATOM   5615  O  O     . ARG A 1 2243 ? 159.388 214.951 147.618 1.00 32.57  ? 2243 ARG A O     1 
ATOM   5616  C  CB    . ARG A 1 2243 ? 160.025 214.279 150.508 1.00 18.02  ? 2243 ARG A CB    1 
ATOM   5617  C  CG    . ARG A 1 2243 ? 159.435 214.582 151.871 1.00 25.92  ? 2243 ARG A CG    1 
ATOM   5618  C  CD    . ARG A 1 2243 ? 160.316 215.532 152.662 1.00 33.96  ? 2243 ARG A CD    1 
ATOM   5619  N  NE    . ARG A 1 2243 ? 160.509 215.080 154.034 1.00 35.89  ? 2243 ARG A NE    1 
ATOM   5620  C  CZ    . ARG A 1 2243 ? 161.369 215.619 154.886 1.00 40.43  ? 2243 ARG A CZ    1 
ATOM   5621  N  NH1   . ARG A 1 2243 ? 162.136 216.640 154.540 1.00 41.75  ? 2243 ARG A NH1   1 
ATOM   5622  N  NH2   . ARG A 1 2243 ? 161.461 215.124 156.116 1.00 42.88  ? 2243 ARG A NH2   1 
ATOM   5623  N  N     . LEU A 1 2244 ? 160.003 212.797 147.432 1.00 17.45  ? 2244 LEU A N     1 
ATOM   5624  C  CA    . LEU A 1 2244 ? 160.454 212.924 146.051 1.00 15.67  ? 2244 LEU A CA    1 
ATOM   5625  C  C     . LEU A 1 2244 ? 159.393 212.505 145.041 1.00 19.31  ? 2244 LEU A C     1 
ATOM   5626  O  O     . LEU A 1 2244 ? 159.100 213.252 144.104 1.00 20.85  ? 2244 LEU A O     1 
ATOM   5627  C  CB    . LEU A 1 2244 ? 161.729 212.099 145.841 1.00 17.01  ? 2244 LEU A CB    1 
ATOM   5628  C  CG    . LEU A 1 2244 ? 162.242 211.965 144.406 1.00 22.92  ? 2244 LEU A CG    1 
ATOM   5629  C  CD1   . LEU A 1 2244 ? 163.085 213.167 144.021 1.00 16.66  ? 2244 LEU A CD1   1 
ATOM   5630  C  CD2   . LEU A 1 2244 ? 163.034 210.679 144.236 1.00 19.94  ? 2244 LEU A CD2   1 
ATOM   5631  N  N     . GLU A 1 2245 ? 158.811 211.317 145.207 1.00 25.61  ? 2245 GLU A N     1 
ATOM   5632  C  CA    . GLU A 1 2245 ? 157.796 210.829 144.284 1.00 23.20  ? 2245 GLU A CA    1 
ATOM   5633  C  C     . GLU A 1 2245 ? 156.391 211.292 144.637 1.00 19.24  ? 2245 GLU A C     1 
ATOM   5634  O  O     . GLU A 1 2245 ? 155.490 211.179 143.799 1.00 27.29  ? 2245 GLU A O     1 
ATOM   5635  C  CB    . GLU A 1 2245 ? 157.816 209.299 144.237 1.00 26.84  ? 2245 GLU A CB    1 
ATOM   5636  C  CG    . GLU A 1 2245 ? 159.175 208.702 143.931 1.00 22.54  ? 2245 GLU A CG    1 
ATOM   5637  C  CD    . GLU A 1 2245 ? 159.157 207.189 143.956 1.00 27.81  ? 2245 GLU A CD    1 
ATOM   5638  O  OE1   . GLU A 1 2245 ? 158.051 206.611 143.988 1.00 30.44  ? 2245 GLU A OE1   1 
ATOM   5639  O  OE2   . GLU A 1 2245 ? 160.246 206.579 143.944 1.00 32.82  ? 2245 GLU A OE2   1 
ATOM   5640  N  N     . GLY A 1 2246 ? 156.181 211.803 145.846 1.00 19.12  ? 2246 GLY A N     1 
ATOM   5641  C  CA    . GLY A 1 2246 ? 154.862 212.206 146.279 1.00 20.30  ? 2246 GLY A CA    1 
ATOM   5642  C  C     . GLY A 1 2246 ? 153.973 211.081 146.757 1.00 24.64  ? 2246 GLY A C     1 
ATOM   5643  O  O     . GLY A 1 2246 ? 152.818 211.340 147.119 1.00 28.56  ? 2246 GLY A O     1 
ATOM   5644  N  N     . VAL A 1 2247 ? 154.465 209.848 146.771 1.00 24.81  ? 2247 VAL A N     1 
ATOM   5645  C  CA    . VAL A 1 2247 ? 153.690 208.701 147.229 1.00 22.61  ? 2247 VAL A CA    1 
ATOM   5646  C  C     . VAL A 1 2247 ? 153.993 208.479 148.704 1.00 23.39  ? 2247 VAL A C     1 
ATOM   5647  O  O     . VAL A 1 2247 ? 155.150 208.279 149.086 1.00 27.31  ? 2247 VAL A O     1 
ATOM   5648  C  CB    . VAL A 1 2247 ? 154.012 207.446 146.404 1.00 22.49  ? 2247 VAL A CB    1 
ATOM   5649  C  CG1   . VAL A 1 2247 ? 153.004 206.348 146.692 1.00 23.54  ? 2247 VAL A CG1   1 
ATOM   5650  C  CG2   . VAL A 1 2247 ? 154.031 207.781 144.923 1.00 22.81  ? 2247 VAL A CG2   1 
ATOM   5651  N  N     . GLU A 1 2248 ? 152.953 208.512 149.534 1.00 24.14  ? 2248 GLU A N     1 
ATOM   5652  C  CA    . GLU A 1 2248 ? 153.143 208.354 150.968 1.00 25.45  ? 2248 GLU A CA    1 
ATOM   5653  C  C     . GLU A 1 2248 ? 153.585 206.934 151.298 1.00 22.45  ? 2248 GLU A C     1 
ATOM   5654  O  O     . GLU A 1 2248 ? 153.026 205.956 150.795 1.00 28.80  ? 2248 GLU A O     1 
ATOM   5655  C  CB    . GLU A 1 2248 ? 151.853 208.704 151.713 1.00 26.35  ? 2248 GLU A CB    1 
ATOM   5656  C  CG    . GLU A 1 2248 ? 151.801 208.202 153.145 1.00 35.79  ? 2248 GLU A CG    1 
ATOM   5657  C  CD    . GLU A 1 2248 ? 150.385 208.001 153.644 1.00 51.03  ? 2248 GLU A CD    1 
ATOM   5658  O  OE1   . GLU A 1 2248 ? 149.439 208.384 152.926 1.00 48.78  ? 2248 GLU A OE1   1 
ATOM   5659  O  OE2   . GLU A 1 2248 ? 150.219 207.457 154.755 1.00 55.35  ? 2248 GLU A OE2   1 
ATOM   5660  N  N     . GLY A 1 2249 ? 154.600 206.826 152.151 1.00 16.74  ? 2249 GLY A N     1 
ATOM   5661  C  CA    . GLY A 1 2249 ? 155.152 205.537 152.514 1.00 13.04  ? 2249 GLY A CA    1 
ATOM   5662  C  C     . GLY A 1 2249 ? 154.714 205.055 153.881 1.00 13.27  ? 2249 GLY A C     1 
ATOM   5663  O  O     . GLY A 1 2249 ? 154.889 205.755 154.882 1.00 15.62  ? 2249 GLY A O     1 
ATOM   5664  N  N     . VAL A 1 2250 ? 154.143 203.855 153.932 1.00 14.89  ? 2250 VAL A N     1 
ATOM   5665  C  CA    . VAL A 1 2250 ? 153.676 203.247 155.171 1.00 10.65  ? 2250 VAL A CA    1 
ATOM   5666  C  C     . VAL A 1 2250 ? 154.499 201.994 155.426 1.00 12.03  ? 2250 VAL A C     1 
ATOM   5667  O  O     . VAL A 1 2250 ? 154.614 201.131 154.547 1.00 12.67  ? 2250 VAL A O     1 
ATOM   5668  C  CB    . VAL A 1 2250 ? 152.177 202.908 155.113 1.00 11.03  ? 2250 VAL A CB    1 
ATOM   5669  C  CG1   . VAL A 1 2250 ? 151.680 202.483 156.483 1.00 10.40  ? 2250 VAL A CG1   1 
ATOM   5670  C  CG2   . VAL A 1 2250 ? 151.384 204.095 154.594 1.00 23.36  ? 2250 VAL A CG2   1 
ATOM   5671  N  N     . ALA A 1 2251 ? 155.059 201.893 156.627 1.00 8.86   ? 2251 ALA A N     1 
ATOM   5672  C  CA    . ALA A 1 2251 ? 155.891 200.767 157.019 1.00 7.02   ? 2251 ALA A CA    1 
ATOM   5673  C  C     . ALA A 1 2251 ? 155.224 200.012 158.158 1.00 7.90   ? 2251 ALA A C     1 
ATOM   5674  O  O     . ALA A 1 2251 ? 154.842 200.611 159.168 1.00 10.54  ? 2251 ALA A O     1 
ATOM   5675  C  CB    . ALA A 1 2251 ? 157.286 201.234 157.440 1.00 4.92   ? 2251 ALA A CB    1 
ATOM   5676  N  N     . HIS A 1 2252 ? 155.085 198.701 157.989 1.00 6.82   ? 2252 HIS A N     1 
ATOM   5677  C  CA    . HIS A 1 2252 ? 154.586 197.808 159.028 1.00 5.38   ? 2252 HIS A CA    1 
ATOM   5678  C  C     . HIS A 1 2252 ? 155.755 196.960 159.512 1.00 6.66   ? 2252 HIS A C     1 
ATOM   5679  O  O     . HIS A 1 2252 ? 156.259 196.110 158.772 1.00 6.84   ? 2252 HIS A O     1 
ATOM   5680  C  CB    . HIS A 1 2252 ? 153.448 196.934 158.506 1.00 4.83   ? 2252 HIS A CB    1 
ATOM   5681  C  CG    . HIS A 1 2252 ? 152.389 197.695 157.774 1.00 8.70   ? 2252 HIS A CG    1 
ATOM   5682  N  ND1   . HIS A 1 2252 ? 151.278 198.215 158.402 1.00 7.31   ? 2252 HIS A ND1   1 
ATOM   5683  C  CD2   . HIS A 1 2252 ? 152.269 198.024 156.466 1.00 10.13  ? 2252 HIS A CD2   1 
ATOM   5684  C  CE1   . HIS A 1 2252 ? 150.521 198.832 157.513 1.00 6.66   ? 2252 HIS A CE1   1 
ATOM   5685  N  NE2   . HIS A 1 2252 ? 151.100 198.731 156.330 1.00 7.15   ? 2252 HIS A NE2   1 
ATOM   5686  N  N     . ILE A 1 2253 ? 156.182 197.192 160.748 1.00 5.60   ? 2253 ILE A N     1 
ATOM   5687  C  CA    . ILE A 1 2253 ? 157.320 196.494 161.335 1.00 4.77   ? 2253 ILE A CA    1 
ATOM   5688  C  C     . ILE A 1 2253 ? 156.800 195.350 162.189 1.00 6.50   ? 2253 ILE A C     1 
ATOM   5689  O  O     . ILE A 1 2253 ? 155.948 195.553 163.063 1.00 11.20  ? 2253 ILE A O     1 
ATOM   5690  C  CB    . ILE A 1 2253 ? 158.190 197.451 162.164 1.00 4.17   ? 2253 ILE A CB    1 
ATOM   5691  C  CG1   . ILE A 1 2253 ? 158.371 198.770 161.417 1.00 4.34   ? 2253 ILE A CG1   1 
ATOM   5692  C  CG2   . ILE A 1 2253 ? 159.536 196.816 162.466 1.00 5.13   ? 2253 ILE A CG2   1 
ATOM   5693  C  CD1   . ILE A 1 2253 ? 158.762 199.912 162.303 1.00 6.05   ? 2253 ILE A CD1   1 
ATOM   5694  N  N     . ILE A 1 2254 ? 157.308 194.147 161.937 1.00 4.46   ? 2254 ILE A N     1 
ATOM   5695  C  CA    . ILE A 1 2254 ? 156.877 192.944 162.635 1.00 5.49   ? 2254 ILE A CA    1 
ATOM   5696  C  C     . ILE A 1 2254 ? 158.110 192.224 163.157 1.00 7.08   ? 2254 ILE A C     1 
ATOM   5697  O  O     . ILE A 1 2254 ? 159.097 192.071 162.430 1.00 9.67   ? 2254 ILE A O     1 
ATOM   5698  C  CB    . ILE A 1 2254 ? 156.059 192.014 161.718 1.00 5.41   ? 2254 ILE A CB    1 
ATOM   5699  C  CG1   . ILE A 1 2254 ? 154.777 192.709 161.252 1.00 7.53   ? 2254 ILE A CG1   1 
ATOM   5700  C  CG2   . ILE A 1 2254 ? 155.744 190.703 162.418 1.00 5.47   ? 2254 ILE A CG2   1 
ATOM   5701  C  CD1   . ILE A 1 2254 ? 154.064 191.987 160.134 1.00 5.99   ? 2254 ILE A CD1   1 
ATOM   5702  N  N     . ASP A 1 2255 ? 158.061 191.801 164.416 1.00 8.91   ? 2255 ASP A N     1 
ATOM   5703  C  CA    . ASP A 1 2255 ? 159.068 190.890 164.940 1.00 7.96   ? 2255 ASP A CA    1 
ATOM   5704  C  C     . ASP A 1 2255 ? 158.547 189.466 164.795 1.00 7.76   ? 2255 ASP A C     1 
ATOM   5705  O  O     . ASP A 1 2255 ? 157.727 189.016 165.604 1.00 6.57   ? 2255 ASP A O     1 
ATOM   5706  C  CB    . ASP A 1 2255 ? 159.400 191.207 166.397 1.00 7.42   ? 2255 ASP A CB    1 
ATOM   5707  C  CG    . ASP A 1 2255 ? 160.806 190.787 166.777 1.00 10.39  ? 2255 ASP A CG    1 
ATOM   5708  O  OD1   . ASP A 1 2255 ? 161.185 189.637 166.473 1.00 7.86   ? 2255 ASP A OD1   1 
ATOM   5709  O  OD2   . ASP A 1 2255 ? 161.532 191.605 167.378 1.00 11.56  ? 2255 ASP A OD2   1 
ATOM   5710  N  N     . PRO A 1 2256 ? 158.985 188.738 163.766 1.00 7.31   ? 2256 PRO A N     1 
ATOM   5711  C  CA    . PRO A 1 2256 ? 158.417 187.404 163.513 1.00 6.25   ? 2256 PRO A CA    1 
ATOM   5712  C  C     . PRO A 1 2256 ? 158.643 186.413 164.638 1.00 6.75   ? 2256 PRO A C     1 
ATOM   5713  O  O     . PRO A 1 2256 ? 157.792 185.543 164.863 1.00 8.93   ? 2256 PRO A O     1 
ATOM   5714  C  CB    . PRO A 1 2256 ? 159.130 186.968 162.226 1.00 5.03   ? 2256 PRO A CB    1 
ATOM   5715  C  CG    . PRO A 1 2256 ? 160.411 187.732 162.242 1.00 5.32   ? 2256 PRO A CG    1 
ATOM   5716  C  CD    . PRO A 1 2256 ? 160.078 189.060 162.835 1.00 5.75   ? 2256 PRO A CD    1 
ATOM   5717  N  N     . LYS A 1 2257 ? 159.764 186.506 165.348 1.00 7.68   ? 2257 LYS A N     1 
ATOM   5718  C  CA    . LYS A 1 2257 ? 160.077 185.561 166.408 1.00 5.19   ? 2257 LYS A CA    1 
ATOM   5719  C  C     . LYS A 1 2257 ? 159.657 186.044 167.789 1.00 5.69   ? 2257 LYS A C     1 
ATOM   5720  O  O     . LYS A 1 2257 ? 159.866 185.320 168.767 1.00 9.14   ? 2257 LYS A O     1 
ATOM   5721  C  CB    . LYS A 1 2257 ? 161.575 185.247 166.404 1.00 5.87   ? 2257 LYS A CB    1 
ATOM   5722  C  CG    . LYS A 1 2257 ? 162.087 184.774 165.058 1.00 4.40   ? 2257 LYS A CG    1 
ATOM   5723  C  CD    . LYS A 1 2257 ? 162.014 183.264 164.948 1.00 5.93   ? 2257 LYS A CD    1 
ATOM   5724  C  CE    . LYS A 1 2257 ? 163.213 182.613 165.602 1.00 5.76   ? 2257 LYS A CE    1 
ATOM   5725  N  NZ    . LYS A 1 2257 ? 163.090 181.136 165.655 1.00 5.29   ? 2257 LYS A NZ    1 
ATOM   5726  N  N     . ALA A 1 2258 ? 159.079 187.239 167.897 1.00 5.47   ? 2258 ALA A N     1 
ATOM   5727  C  CA    . ALA A 1 2258 ? 158.496 187.680 169.156 1.00 5.17   ? 2258 ALA A CA    1 
ATOM   5728  C  C     . ALA A 1 2258 ? 157.125 187.073 169.403 1.00 6.83   ? 2258 ALA A C     1 
ATOM   5729  O  O     . ALA A 1 2258 ? 156.598 187.196 170.513 1.00 10.64  ? 2258 ALA A O     1 
ATOM   5730  C  CB    . ALA A 1 2258 ? 158.394 189.206 169.192 1.00 4.48   ? 2258 ALA A CB    1 
ATOM   5731  N  N     . ILE A 1 2259 ? 156.541 186.426 168.396 1.00 6.17   ? 2259 ILE A N     1 
ATOM   5732  C  CA    . ILE A 1 2259 ? 155.236 185.794 168.495 1.00 6.05   ? 2259 ILE A CA    1 
ATOM   5733  C  C     . ILE A 1 2259 ? 155.336 184.397 167.902 1.00 7.21   ? 2259 ILE A C     1 
ATOM   5734  O  O     . ILE A 1 2259 ? 156.284 184.066 167.186 1.00 8.70   ? 2259 ILE A O     1 
ATOM   5735  C  CB    . ILE A 1 2259 ? 154.140 186.609 167.777 1.00 6.32   ? 2259 ILE A CB    1 
ATOM   5736  C  CG1   . ILE A 1 2259 ? 154.554 186.892 166.331 1.00 5.87   ? 2259 ILE A CG1   1 
ATOM   5737  C  CG2   . ILE A 1 2259 ? 153.866 187.906 168.519 1.00 4.86   ? 2259 ILE A CG2   1 
ATOM   5738  C  CD1   . ILE A 1 2259 ? 153.597 187.790 165.583 1.00 7.29   ? 2259 ILE A CD1   1 
ATOM   5739  N  N     . SER A 1 2260 ? 154.347 183.568 168.220 1.00 7.96   ? 2260 SER A N     1 
ATOM   5740  C  CA    . SER A 1 2260 ? 154.279 182.240 167.632 1.00 5.54   ? 2260 SER A CA    1 
ATOM   5741  C  C     . SER A 1 2260 ? 153.936 182.336 166.150 1.00 9.84   ? 2260 SER A C     1 
ATOM   5742  O  O     . SER A 1 2260 ? 153.313 183.298 165.695 1.00 12.10  ? 2260 SER A O     1 
ATOM   5743  C  CB    . SER A 1 2260 ? 153.244 181.382 168.357 1.00 6.32   ? 2260 SER A CB    1 
ATOM   5744  O  OG    . SER A 1 2260 ? 151.930 181.834 168.089 1.00 9.90   ? 2260 SER A OG    1 
ATOM   5745  N  N     . LYS A 1 2261 ? 154.364 181.324 165.391 1.00 10.49  ? 2261 LYS A N     1 
ATOM   5746  C  CA    . LYS A 1 2261 ? 154.087 181.311 163.958 1.00 6.29   ? 2261 LYS A CA    1 
ATOM   5747  C  C     . LYS A 1 2261 ? 152.590 181.275 163.682 1.00 7.72   ? 2261 LYS A C     1 
ATOM   5748  O  O     . LYS A 1 2261 ? 152.134 181.785 162.652 1.00 8.84   ? 2261 LYS A O     1 
ATOM   5749  C  CB    . LYS A 1 2261 ? 154.781 180.119 163.300 1.00 5.90   ? 2261 LYS A CB    1 
ATOM   5750  C  CG    . LYS A 1 2261 ? 154.765 180.159 161.785 1.00 9.66   ? 2261 LYS A CG    1 
ATOM   5751  C  CD    . LYS A 1 2261 ? 155.583 179.030 161.190 1.00 9.03   ? 2261 LYS A CD    1 
ATOM   5752  C  CE    . LYS A 1 2261 ? 154.777 177.749 161.142 1.00 19.46  ? 2261 LYS A CE    1 
ATOM   5753  N  NZ    . LYS A 1 2261 ? 154.274 177.455 159.771 1.00 27.73  ? 2261 LYS A NZ    1 
ATOM   5754  N  N     . ASP A 1 2262 ? 151.814 180.679 164.590 1.00 9.41   ? 2262 ASP A N     1 
ATOM   5755  C  CA    . ASP A 1 2262 ? 150.362 180.704 164.455 1.00 9.73   ? 2262 ASP A CA    1 
ATOM   5756  C  C     . ASP A 1 2262 ? 149.830 182.129 164.531 1.00 9.25   ? 2262 ASP A C     1 
ATOM   5757  O  O     . ASP A 1 2262 ? 148.908 182.496 163.793 1.00 11.96  ? 2262 ASP A O     1 
ATOM   5758  C  CB    . ASP A 1 2262 ? 149.723 179.830 165.533 1.00 12.94  ? 2262 ASP A CB    1 
ATOM   5759  C  CG    . ASP A 1 2262 ? 149.994 178.356 165.323 1.00 27.85  ? 2262 ASP A CG    1 
ATOM   5760  O  OD1   . ASP A 1 2262 ? 150.160 177.943 164.156 1.00 37.37  ? 2262 ASP A OD1   1 
ATOM   5761  O  OD2   . ASP A 1 2262 ? 150.037 177.607 166.321 1.00 29.56  ? 2262 ASP A OD2   1 
ATOM   5762  N  N     . HIS A 1 2263 ? 150.395 182.945 165.420 1.00 7.25   ? 2263 HIS A N     1 
ATOM   5763  C  CA    . HIS A 1 2263 ? 150.012 184.347 165.502 1.00 6.48   ? 2263 HIS A CA    1 
ATOM   5764  C  C     . HIS A 1 2263 ? 150.580 185.177 164.360 1.00 6.37   ? 2263 HIS A C     1 
ATOM   5765  O  O     . HIS A 1 2263 ? 150.101 186.291 164.124 1.00 8.24   ? 2263 HIS A O     1 
ATOM   5766  C  CB    . HIS A 1 2263 ? 150.463 184.940 166.838 1.00 7.47   ? 2263 HIS A CB    1 
ATOM   5767  C  CG    . HIS A 1 2263 ? 149.674 184.452 168.012 1.00 6.77   ? 2263 HIS A CG    1 
ATOM   5768  N  ND1   . HIS A 1 2263 ? 148.304 184.307 167.979 1.00 6.63   ? 2263 HIS A ND1   1 
ATOM   5769  C  CD2   . HIS A 1 2263 ? 150.061 184.082 169.255 1.00 6.33   ? 2263 HIS A CD2   1 
ATOM   5770  C  CE1   . HIS A 1 2263 ? 147.882 183.865 169.149 1.00 6.12   ? 2263 HIS A CE1   1 
ATOM   5771  N  NE2   . HIS A 1 2263 ? 148.928 183.721 169.941 1.00 8.98   ? 2263 HIS A NE2   1 
ATOM   5772  N  N     . LEU A 1 2264 ? 151.583 184.664 163.649 1.00 6.98   ? 2264 LEU A N     1 
ATOM   5773  C  CA    . LEU A 1 2264 ? 152.207 185.393 162.554 1.00 5.15   ? 2264 LEU A CA    1 
ATOM   5774  C  C     . LEU A 1 2264 ? 151.505 185.155 161.223 1.00 6.73   ? 2264 LEU A C     1 
ATOM   5775  O  O     . LEU A 1 2264 ? 151.312 186.099 160.449 1.00 8.30   ? 2264 LEU A O     1 
ATOM   5776  C  CB    . LEU A 1 2264 ? 153.682 185.001 162.439 1.00 4.96   ? 2264 LEU A CB    1 
ATOM   5777  C  CG    . LEU A 1 2264 ? 154.479 185.599 161.279 1.00 3.60   ? 2264 LEU A CG    1 
ATOM   5778  C  CD1   . LEU A 1 2264 ? 154.557 187.110 161.407 1.00 4.55   ? 2264 LEU A CD1   1 
ATOM   5779  C  CD2   . LEU A 1 2264 ? 155.868 184.991 161.214 1.00 4.58   ? 2264 LEU A CD2   1 
ATOM   5780  N  N     . TYR A 1 2265 ? 151.117 183.913 160.938 1.00 8.13   ? 2265 TYR A N     1 
ATOM   5781  C  CA    . TYR A 1 2265 ? 150.487 183.578 159.667 1.00 7.30   ? 2265 TYR A CA    1 
ATOM   5782  C  C     . TYR A 1 2265 ? 149.004 183.272 159.774 1.00 8.48   ? 2265 TYR A C     1 
ATOM   5783  O  O     . TYR A 1 2265 ? 148.265 183.541 158.827 1.00 10.97  ? 2265 TYR A O     1 
ATOM   5784  C  CB    . TYR A 1 2265 ? 151.191 182.378 159.022 1.00 4.77   ? 2265 TYR A CB    1 
ATOM   5785  C  CG    . TYR A 1 2265 ? 152.571 182.698 158.507 1.00 4.68   ? 2265 TYR A CG    1 
ATOM   5786  C  CD1   . TYR A 1 2265 ? 152.749 183.563 157.439 1.00 4.53   ? 2265 TYR A CD1   1 
ATOM   5787  C  CD2   . TYR A 1 2265 ? 153.696 182.140 159.092 1.00 5.62   ? 2265 TYR A CD2   1 
ATOM   5788  C  CE1   . TYR A 1 2265 ? 154.009 183.861 156.967 1.00 4.19   ? 2265 TYR A CE1   1 
ATOM   5789  C  CE2   . TYR A 1 2265 ? 154.959 182.431 158.627 1.00 4.79   ? 2265 TYR A CE2   1 
ATOM   5790  C  CZ    . TYR A 1 2265 ? 155.110 183.292 157.565 1.00 4.71   ? 2265 TYR A CZ    1 
ATOM   5791  O  OH    . TYR A 1 2265 ? 156.369 183.584 157.097 1.00 9.16   ? 2265 TYR A OH    1 
ATOM   5792  N  N     . GLY A 1 2266 ? 148.551 182.719 160.891 1.00 6.76   ? 2266 GLY A N     1 
ATOM   5793  C  CA    . GLY A 1 2266 ? 147.152 182.397 161.082 1.00 8.53   ? 2266 GLY A CA    1 
ATOM   5794  C  C     . GLY A 1 2266 ? 146.957 180.955 161.505 1.00 11.83  ? 2266 GLY A C     1 
ATOM   5795  O  O     . GLY A 1 2266 ? 147.855 180.119 161.429 1.00 16.39  ? 2266 GLY A O     1 
ATOM   5796  N  N     . THR A 1 2267 ? 145.738 180.682 161.955 1.00 13.03  ? 2267 THR A N     1 
ATOM   5797  C  CA    . THR A 1 2267 ? 145.355 179.369 162.453 1.00 15.33  ? 2267 THR A CA    1 
ATOM   5798  C  C     . THR A 1 2267 ? 144.130 178.861 161.711 1.00 15.12  ? 2267 THR A C     1 
ATOM   5799  O  O     . THR A 1 2267 ? 143.227 179.633 161.373 1.00 16.64  ? 2267 THR A O     1 
ATOM   5800  C  CB    . THR A 1 2267 ? 145.057 179.401 163.958 1.00 19.82  ? 2267 THR A CB    1 
ATOM   5801  O  OG1   . THR A 1 2267 ? 143.960 180.288 164.213 1.00 26.67  ? 2267 THR A OG1   1 
ATOM   5802  C  CG2   . THR A 1 2267 ? 146.268 179.869 164.735 1.00 16.70  ? 2267 THR A CG2   1 
ATOM   5803  N  N     . LEU A 1 2268 ? 144.106 177.558 161.458 1.00 18.45  ? 2268 LEU A N     1 
ATOM   5804  C  CA    . LEU A 1 2268 ? 142.937 176.875 160.924 1.00 26.32  ? 2268 LEU A CA    1 
ATOM   5805  C  C     . LEU A 1 2268 ? 142.347 176.017 162.033 1.00 30.47  ? 2268 LEU A C     1 
ATOM   5806  O  O     . LEU A 1 2268 ? 143.041 175.162 162.594 1.00 26.11  ? 2268 LEU A O     1 
ATOM   5807  C  CB    . LEU A 1 2268 ? 143.299 176.026 159.707 1.00 23.04  ? 2268 LEU A CB    1 
ATOM   5808  C  CG    . LEU A 1 2268 ? 142.125 175.509 158.875 1.00 24.51  ? 2268 LEU A CG    1 
ATOM   5809  C  CD1   . LEU A 1 2268 ? 141.249 176.660 158.419 1.00 22.31  ? 2268 LEU A CD1   1 
ATOM   5810  C  CD2   . LEU A 1 2268 ? 142.627 174.716 157.682 1.00 25.19  ? 2268 LEU A CD2   1 
ATOM   5811  N  N     . ASP A 1 2269 ? 141.082 176.249 162.347 1.00 35.71  ? 2269 ASP A N     1 
ATOM   5812  C  CA    . ASP A 1 2269 ? 140.433 175.542 163.444 1.00 38.26  ? 2269 ASP A CA    1 
ATOM   5813  C  C     . ASP A 1 2269 ? 140.256 174.078 163.065 1.00 46.13  ? 2269 ASP A C     1 
ATOM   5814  O  O     . ASP A 1 2269 ? 139.572 173.782 162.076 1.00 44.42  ? 2269 ASP A O     1 
ATOM   5815  C  CB    . ASP A 1 2269 ? 139.085 176.193 163.747 1.00 38.34  ? 2269 ASP A CB    1 
ATOM   5816  C  CG    . ASP A 1 2269 ? 138.446 175.671 165.019 1.00 44.41  ? 2269 ASP A CG    1 
ATOM   5817  O  OD1   . ASP A 1 2269 ? 139.024 174.779 165.670 1.00 54.24  ? 2269 ASP A OD1   1 
ATOM   5818  O  OD2   . ASP A 1 2269 ? 137.353 176.161 165.369 1.00 52.05  ? 2269 ASP A OD2   1 
ATOM   5819  N  N     . PRO A 1 2270 ? 140.845 173.134 163.807 1.00 42.31  ? 2270 PRO A N     1 
ATOM   5820  C  CA    . PRO A 1 2270 ? 140.689 171.717 163.445 1.00 45.14  ? 2270 PRO A CA    1 
ATOM   5821  C  C     . PRO A 1 2270 ? 139.264 171.213 163.561 1.00 53.76  ? 2270 PRO A C     1 
ATOM   5822  O  O     . PRO A 1 2270 ? 138.945 170.171 162.974 1.00 53.08  ? 2270 PRO A O     1 
ATOM   5823  C  CB    . PRO A 1 2270 ? 141.620 170.997 164.429 1.00 43.25  ? 2270 PRO A CB    1 
ATOM   5824  C  CG    . PRO A 1 2270 ? 141.744 171.930 165.585 1.00 40.01  ? 2270 PRO A CG    1 
ATOM   5825  C  CD    . PRO A 1 2270 ? 141.683 173.312 165.005 1.00 36.78  ? 2270 PRO A CD    1 
ATOM   5826  N  N     . ASN A 1 2271 ? 138.398 171.912 164.293 1.00 53.01  ? 2271 ASN A N     1 
ATOM   5827  C  CA    . ASN A 1 2271 ? 137.024 171.465 164.494 1.00 49.40  ? 2271 ASN A CA    1 
ATOM   5828  C  C     . ASN A 1 2271 ? 136.067 172.105 163.491 1.00 51.83  ? 2271 ASN A C     1 
ATOM   5829  O  O     . ASN A 1 2271 ? 135.355 171.401 162.767 1.00 47.02  ? 2271 ASN A O     1 
ATOM   5830  C  CB    . ASN A 1 2271 ? 136.586 171.770 165.930 1.00 53.57  ? 2271 ASN A CB    1 
ATOM   5831  C  CG    . ASN A 1 2271 ? 137.638 171.390 166.951 1.00 59.67  ? 2271 ASN A CG    1 
ATOM   5832  O  OD1   . ASN A 1 2271 ? 137.979 172.178 167.833 1.00 57.92  ? 2271 ASN A OD1   1 
ATOM   5833  N  ND2   . ASN A 1 2271 ? 138.162 170.175 166.837 1.00 60.90  ? 2271 ASN A ND2   1 
ATOM   5834  N  N     . THR A 1 2272 ? 136.045 173.435 163.434 1.00 51.91  ? 2272 THR A N     1 
ATOM   5835  C  CA    . THR A 1 2272 ? 135.067 174.165 162.637 1.00 45.99  ? 2272 THR A CA    1 
ATOM   5836  C  C     . THR A 1 2272 ? 135.601 174.628 161.289 1.00 45.74  ? 2272 THR A C     1 
ATOM   5837  O  O     . THR A 1 2272 ? 134.855 175.263 160.536 1.00 49.19  ? 2272 THR A O     1 
ATOM   5838  C  CB    . THR A 1 2272 ? 134.553 175.377 163.418 1.00 44.82  ? 2272 THR A CB    1 
ATOM   5839  O  OG1   . THR A 1 2272 ? 135.606 176.339 163.559 1.00 39.07  ? 2272 THR A OG1   1 
ATOM   5840  C  CG2   . THR A 1 2272 ? 134.070 174.955 164.797 1.00 46.98  ? 2272 THR A CG2   1 
ATOM   5841  N  N     . ARG A 1 2273 ? 136.862 174.330 160.966 1.00 45.49  ? 2273 ARG A N     1 
ATOM   5842  C  CA    . ARG A 1 2273 ? 137.464 174.731 159.691 1.00 41.33  ? 2273 ARG A CA    1 
ATOM   5843  C  C     . ARG A 1 2273 ? 137.377 176.241 159.483 1.00 39.26  ? 2273 ARG A C     1 
ATOM   5844  O  O     . ARG A 1 2273 ? 137.152 176.727 158.373 1.00 41.51  ? 2273 ARG A O     1 
ATOM   5845  C  CB    . ARG A 1 2273 ? 136.820 173.986 158.522 1.00 39.43  ? 2273 ARG A CB    1 
ATOM   5846  C  CG    . ARG A 1 2273 ? 137.137 172.505 158.466 1.00 37.49  ? 2273 ARG A CG    1 
ATOM   5847  C  CD    . ARG A 1 2273 ? 138.580 172.261 158.064 1.00 33.35  ? 2273 ARG A CD    1 
ATOM   5848  N  NE    . ARG A 1 2273 ? 139.397 171.752 159.157 1.00 37.74  ? 2273 ARG A NE    1 
ATOM   5849  C  CZ    . ARG A 1 2273 ? 140.688 171.467 159.052 1.00 32.77  ? 2273 ARG A CZ    1 
ATOM   5850  N  NH1   . ARG A 1 2273 ? 141.336 171.614 157.908 1.00 23.22  ? 2273 ARG A NH1   1 
ATOM   5851  N  NH2   . ARG A 1 2273 ? 141.343 171.017 160.118 1.00 30.87  ? 2273 ARG A NH2   1 
ATOM   5852  N  N     . GLU A 1 2274 ? 137.557 176.992 160.565 1.00 38.18  ? 2274 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2274 ? 137.475 178.445 160.534 1.00 33.32  ? 2274 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2274 ? 138.883 179.022 160.582 1.00 34.90  ? 2274 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2274 ? 139.700 178.610 161.413 1.00 32.06  ? 2274 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2274 ? 136.632 178.962 161.702 1.00 36.46  ? 2274 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2274 ? 136.280 180.444 161.644 1.00 41.97  ? 2274 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2274 ? 137.376 181.339 162.187 1.00 51.20  ? 2274 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2274 ? 138.136 180.887 163.069 1.00 46.30  ? 2274 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2274 ? 137.473 182.500 161.737 1.00 48.14  ? 2274 GLU A OE2   1 
ATOM   5861  N  N     . TRP A 1 2275 ? 139.165 179.968 159.691 1.00 28.36  ? 2275 TRP A N     1 
ATOM   5862  C  CA    . TRP A 1 2275 ? 140.493 180.549 159.552 1.00 21.70  ? 2275 TRP A CA    1 
ATOM   5863  C  C     . TRP A 1 2275 ? 140.561 181.867 160.312 1.00 22.20  ? 2275 TRP A C     1 
ATOM   5864  O  O     . TRP A 1 2275 ? 139.752 182.770 160.073 1.00 28.21  ? 2275 TRP A O     1 
ATOM   5865  C  CB    . TRP A 1 2275 ? 140.842 180.766 158.079 1.00 18.11  ? 2275 TRP A CB    1 
ATOM   5866  C  CG    . TRP A 1 2275 ? 142.134 181.499 157.873 1.00 16.89  ? 2275 TRP A CG    1 
ATOM   5867  C  CD1   . TRP A 1 2275 ? 142.285 182.814 157.546 1.00 12.77  ? 2275 TRP A CD1   1 
ATOM   5868  C  CD2   . TRP A 1 2275 ? 143.456 180.961 157.989 1.00 16.35  ? 2275 TRP A CD2   1 
ATOM   5869  N  NE1   . TRP A 1 2275 ? 143.617 183.128 157.448 1.00 10.36  ? 2275 TRP A NE1   1 
ATOM   5870  C  CE2   . TRP A 1 2275 ? 144.358 182.007 157.717 1.00 13.44  ? 2275 TRP A CE2   1 
ATOM   5871  C  CE3   . TRP A 1 2275 ? 143.964 179.695 158.293 1.00 14.10  ? 2275 TRP A CE3   1 
ATOM   5872  C  CZ2   . TRP A 1 2275 ? 145.738 181.827 157.741 1.00 12.60  ? 2275 TRP A CZ2   1 
ATOM   5873  C  CZ3   . TRP A 1 2275 ? 145.334 179.519 158.316 1.00 11.30  ? 2275 TRP A CZ3   1 
ATOM   5874  C  CH2   . TRP A 1 2275 ? 146.205 180.578 158.042 1.00 10.30  ? 2275 TRP A CH2   1 
ATOM   5875  N  N     . THR A 1 2276 ? 141.528 181.975 161.218 1.00 17.98  ? 2276 THR A N     1 
ATOM   5876  C  CA    . THR A 1 2276 ? 141.827 183.215 161.919 1.00 17.45  ? 2276 THR A CA    1 
ATOM   5877  C  C     . THR A 1 2276 ? 143.144 183.750 161.378 1.00 16.52  ? 2276 THR A C     1 
ATOM   5878  O  O     . THR A 1 2276 ? 144.159 183.047 161.408 1.00 18.30  ? 2276 THR A O     1 
ATOM   5879  C  CB    . THR A 1 2276 ? 141.915 182.993 163.430 1.00 21.95  ? 2276 THR A CB    1 
ATOM   5880  O  OG1   . THR A 1 2276 ? 140.654 182.524 163.921 1.00 41.44  ? 2276 THR A OG1   1 
ATOM   5881  C  CG2   . THR A 1 2276 ? 142.279 184.287 164.137 1.00 13.24  ? 2276 THR A CG2   1 
ATOM   5882  N  N     . ASP A 1 2277 ? 143.124 184.983 160.880 1.00 11.97  ? 2277 ASP A N     1 
ATOM   5883  C  CA    . ASP A 1 2277 ? 144.310 185.563 160.268 1.00 9.79   ? 2277 ASP A CA    1 
ATOM   5884  C  C     . ASP A 1 2277 ? 145.393 185.830 161.307 1.00 10.15  ? 2277 ASP A C     1 
ATOM   5885  O  O     . ASP A 1 2277 ? 145.113 186.140 162.468 1.00 10.15  ? 2277 ASP A O     1 
ATOM   5886  C  CB    . ASP A 1 2277 ? 143.961 186.865 159.547 1.00 10.66  ? 2277 ASP A CB    1 
ATOM   5887  C  CG    . ASP A 1 2277 ? 143.503 186.639 158.123 1.00 10.36  ? 2277 ASP A CG    1 
ATOM   5888  O  OD1   . ASP A 1 2277 ? 143.911 185.627 157.519 1.00 15.50  ? 2277 ASP A OD1   1 
ATOM   5889  O  OD2   . ASP A 1 2277 ? 142.740 187.478 157.603 1.00 12.50  ? 2277 ASP A OD2   1 
ATOM   5890  N  N     . GLY A 1 2278 ? 146.642 185.704 160.872 1.00 8.95   ? 2278 GLY A N     1 
ATOM   5891  C  CA    . GLY A 1 2278 ? 147.781 186.082 161.679 1.00 6.59   ? 2278 GLY A CA    1 
ATOM   5892  C  C     . GLY A 1 2278 ? 148.080 187.558 161.525 1.00 7.32   ? 2278 GLY A C     1 
ATOM   5893  O  O     . GLY A 1 2278 ? 147.245 188.346 161.080 1.00 9.99   ? 2278 GLY A O     1 
ATOM   5894  N  N     . LEU A 1 2279 ? 149.302 187.935 161.896 1.00 7.31   ? 2279 LEU A N     1 
ATOM   5895  C  CA    . LEU A 1 2279 ? 149.700 189.337 161.817 1.00 5.61   ? 2279 LEU A CA    1 
ATOM   5896  C  C     . LEU A 1 2279 ? 150.054 189.732 160.387 1.00 6.47   ? 2279 LEU A C     1 
ATOM   5897  O  O     . LEU A 1 2279 ? 149.472 190.670 159.825 1.00 9.31   ? 2279 LEU A O     1 
ATOM   5898  C  CB    . LEU A 1 2279 ? 150.877 189.595 162.761 1.00 5.22   ? 2279 LEU A CB    1 
ATOM   5899  C  CG    . LEU A 1 2279 ? 151.412 191.024 162.837 1.00 6.42   ? 2279 LEU A CG    1 
ATOM   5900  C  CD1   . LEU A 1 2279 ? 150.285 192.014 163.072 1.00 6.61   ? 2279 LEU A CD1   1 
ATOM   5901  C  CD2   . LEU A 1 2279 ? 152.452 191.125 163.934 1.00 7.70   ? 2279 LEU A CD2   1 
ATOM   5902  N  N     . PHE A 1 2280 ? 151.011 189.023 159.784 1.00 5.68   ? 2280 PHE A N     1 
ATOM   5903  C  CA    . PHE A 1 2280 ? 151.396 189.318 158.408 1.00 5.91   ? 2280 PHE A CA    1 
ATOM   5904  C  C     . PHE A 1 2280 ? 150.229 189.103 157.455 1.00 6.20   ? 2280 PHE A C     1 
ATOM   5905  O  O     . PHE A 1 2280 ? 150.028 189.889 156.521 1.00 8.22   ? 2280 PHE A O     1 
ATOM   5906  C  CB    . PHE A 1 2280 ? 152.586 188.453 157.994 1.00 5.94   ? 2280 PHE A CB    1 
ATOM   5907  C  CG    . PHE A 1 2280 ? 152.915 188.539 156.532 1.00 5.73   ? 2280 PHE A CG    1 
ATOM   5908  C  CD1   . PHE A 1 2280 ? 153.510 189.673 156.008 1.00 4.34   ? 2280 PHE A CD1   1 
ATOM   5909  C  CD2   . PHE A 1 2280 ? 152.611 187.494 155.678 1.00 4.96   ? 2280 PHE A CD2   1 
ATOM   5910  C  CE1   . PHE A 1 2280 ? 153.807 189.756 154.663 1.00 4.43   ? 2280 PHE A CE1   1 
ATOM   5911  C  CE2   . PHE A 1 2280 ? 152.903 187.574 154.331 1.00 4.17   ? 2280 PHE A CE2   1 
ATOM   5912  C  CZ    . PHE A 1 2280 ? 153.503 188.706 153.824 1.00 5.02   ? 2280 PHE A CZ    1 
ATOM   5913  N  N     . THR A 1 2281 ? 149.456 188.037 157.669 1.00 5.25   ? 2281 THR A N     1 
ATOM   5914  C  CA    . THR A 1 2281 ? 148.297 187.783 156.822 1.00 5.01   ? 2281 THR A CA    1 
ATOM   5915  C  C     . THR A 1 2281 ? 147.277 188.908 156.937 1.00 6.71   ? 2281 THR A C     1 
ATOM   5916  O  O     . THR A 1 2281 ? 146.717 189.350 155.928 1.00 7.69   ? 2281 THR A O     1 
ATOM   5917  C  CB    . THR A 1 2281 ? 147.661 186.442 157.189 1.00 7.75   ? 2281 THR A CB    1 
ATOM   5918  O  OG1   . THR A 1 2281 ? 148.688 185.470 157.409 1.00 12.77  ? 2281 THR A OG1   1 
ATOM   5919  C  CG2   . THR A 1 2281 ? 146.760 185.959 156.067 1.00 6.83   ? 2281 THR A CG2   1 
ATOM   5920  N  N     . HIS A 1 2282 ? 147.030 189.389 158.158 1.00 6.35   ? 2282 HIS A N     1 
ATOM   5921  C  CA    . HIS A 1 2282 ? 146.093 190.493 158.344 1.00 8.23   ? 2282 HIS A CA    1 
ATOM   5922  C  C     . HIS A 1 2282 ? 146.581 191.755 157.646 1.00 8.07   ? 2282 HIS A C     1 
ATOM   5923  O  O     . HIS A 1 2282 ? 145.802 192.440 156.973 1.00 8.86   ? 2282 HIS A O     1 
ATOM   5924  C  CB    . HIS A 1 2282 ? 145.880 190.752 159.836 1.00 11.07  ? 2282 HIS A CB    1 
ATOM   5925  C  CG    . HIS A 1 2282 ? 145.241 192.070 160.141 1.00 14.22  ? 2282 HIS A CG    1 
ATOM   5926  N  ND1   . HIS A 1 2282 ? 143.879 192.268 160.082 1.00 13.63  ? 2282 HIS A ND1   1 
ATOM   5927  C  CD2   . HIS A 1 2282 ? 145.776 193.255 160.520 1.00 15.38  ? 2282 HIS A CD2   1 
ATOM   5928  C  CE1   . HIS A 1 2282 ? 143.603 193.518 160.406 1.00 17.79  ? 2282 HIS A CE1   1 
ATOM   5929  N  NE2   . HIS A 1 2282 ? 144.737 194.138 160.674 1.00 20.48  ? 2282 HIS A NE2   1 
ATOM   5930  N  N     . VAL A 1 2283 ? 147.870 192.074 157.785 1.00 8.02   ? 2283 VAL A N     1 
ATOM   5931  C  CA    . VAL A 1 2283 ? 148.409 193.279 157.157 1.00 8.06   ? 2283 VAL A CA    1 
ATOM   5932  C  C     . VAL A 1 2283 ? 148.308 193.179 155.639 1.00 7.98   ? 2283 VAL A C     1 
ATOM   5933  O  O     . VAL A 1 2283 ? 147.869 194.118 154.961 1.00 12.51  ? 2283 VAL A O     1 
ATOM   5934  C  CB    . VAL A 1 2283 ? 149.859 193.520 157.613 1.00 7.00   ? 2283 VAL A CB    1 
ATOM   5935  C  CG1   . VAL A 1 2283 ? 150.532 194.563 156.734 1.00 7.46   ? 2283 VAL A CG1   1 
ATOM   5936  C  CG2   . VAL A 1 2283 ? 149.893 193.945 159.070 1.00 4.86   ? 2283 VAL A CG2   1 
ATOM   5937  N  N     . LEU A 1 2284 ? 148.704 192.031 155.083 1.00 6.51   ? 2284 LEU A N     1 
ATOM   5938  C  CA    . LEU A 1 2284 ? 148.667 191.855 153.635 1.00 8.02   ? 2284 LEU A CA    1 
ATOM   5939  C  C     . LEU A 1 2284 ? 147.240 191.904 153.105 1.00 8.68   ? 2284 LEU A C     1 
ATOM   5940  O  O     . LEU A 1 2284 ? 146.982 192.510 152.060 1.00 9.58   ? 2284 LEU A O     1 
ATOM   5941  C  CB    . LEU A 1 2284 ? 149.338 190.536 153.251 1.00 6.81   ? 2284 LEU A CB    1 
ATOM   5942  C  CG    . LEU A 1 2284 ? 149.593 190.318 151.760 1.00 7.87   ? 2284 LEU A CG    1 
ATOM   5943  C  CD1   . LEU A 1 2284 ? 150.590 191.335 151.232 1.00 7.44   ? 2284 LEU A CD1   1 
ATOM   5944  C  CD2   . LEU A 1 2284 ? 150.074 188.900 151.497 1.00 6.45   ? 2284 LEU A CD2   1 
ATOM   5945  N  N     . ARG A 1 2285 ? 146.300 191.268 153.808 1.00 8.28   ? 2285 ARG A N     1 
ATOM   5946  C  CA    . ARG A 1 2285 ? 144.909 191.289 153.372 1.00 8.25   ? 2285 ARG A CA    1 
ATOM   5947  C  C     . ARG A 1 2285 ? 144.328 192.695 153.442 1.00 11.36  ? 2285 ARG A C     1 
ATOM   5948  O  O     . ARG A 1 2285 ? 143.570 193.103 152.554 1.00 14.61  ? 2285 ARG A O     1 
ATOM   5949  C  CB    . ARG A 1 2285 ? 144.084 190.316 154.214 1.00 8.44   ? 2285 ARG A CB    1 
ATOM   5950  C  CG    . ARG A 1 2285 ? 142.647 190.167 153.761 1.00 10.50  ? 2285 ARG A CG    1 
ATOM   5951  C  CD    . ARG A 1 2285 ? 141.850 189.322 154.737 1.00 11.13  ? 2285 ARG A CD    1 
ATOM   5952  N  NE    . ARG A 1 2285 ? 142.474 188.029 154.985 1.00 9.39   ? 2285 ARG A NE    1 
ATOM   5953  C  CZ    . ARG A 1 2285 ? 142.397 186.989 154.166 1.00 11.91  ? 2285 ARG A CZ    1 
ATOM   5954  N  NH1   . ARG A 1 2285 ? 141.727 187.054 153.027 1.00 12.70  ? 2285 ARG A NH1   1 
ATOM   5955  N  NH2   . ARG A 1 2285 ? 143.004 185.854 154.500 1.00 12.48  ? 2285 ARG A NH2   1 
ATOM   5956  N  N     . LYS A 1 2286 ? 144.668 193.451 154.490 1.00 13.13  ? 2286 LYS A N     1 
ATOM   5957  C  CA    . LYS A 1 2286 ? 144.207 194.831 154.582 1.00 11.53  ? 2286 LYS A CA    1 
ATOM   5958  C  C     . LYS A 1 2286 ? 144.761 195.670 153.439 1.00 13.85  ? 2286 LYS A C     1 
ATOM   5959  O  O     . LYS A 1 2286 ? 144.048 196.503 152.867 1.00 19.38  ? 2286 LYS A O     1 
ATOM   5960  C  CB    . LYS A 1 2286 ? 144.601 195.425 155.934 1.00 12.56  ? 2286 LYS A CB    1 
ATOM   5961  C  CG    . LYS A 1 2286 ? 144.745 196.936 155.937 1.00 22.48  ? 2286 LYS A CG    1 
ATOM   5962  C  CD    . LYS A 1 2286 ? 144.986 197.464 157.341 1.00 28.42  ? 2286 LYS A CD    1 
ATOM   5963  C  CE    . LYS A 1 2286 ? 143.805 197.166 158.248 1.00 31.47  ? 2286 LYS A CE    1 
ATOM   5964  N  NZ    . LYS A 1 2286 ? 142.541 197.741 157.710 1.00 32.00  ? 2286 LYS A NZ    1 
ATOM   5965  N  N     . ILE A 1 2287 ? 146.034 195.465 153.090 1.00 12.28  ? 2287 ILE A N     1 
ATOM   5966  C  CA    . ILE A 1 2287 ? 146.615 196.189 151.962 1.00 11.93  ? 2287 ILE A CA    1 
ATOM   5967  C  C     . ILE A 1 2287 ? 145.909 195.813 150.664 1.00 13.58  ? 2287 ILE A C     1 
ATOM   5968  O  O     . ILE A 1 2287 ? 145.600 196.678 149.835 1.00 17.16  ? 2287 ILE A O     1 
ATOM   5969  C  CB    . ILE A 1 2287 ? 148.130 195.927 151.879 1.00 12.61  ? 2287 ILE A CB    1 
ATOM   5970  C  CG1   . ILE A 1 2287 ? 148.848 196.557 153.074 1.00 9.10   ? 2287 ILE A CG1   1 
ATOM   5971  C  CG2   . ILE A 1 2287 ? 148.695 196.469 150.578 1.00 10.29  ? 2287 ILE A CG2   1 
ATOM   5972  C  CD1   . ILE A 1 2287 ? 150.320 196.226 153.141 1.00 5.38   ? 2287 ILE A CD1   1 
ATOM   5973  N  N     . ILE A 1 2288 ? 145.642 194.520 150.468 1.00 14.43  ? 2288 ILE A N     1 
ATOM   5974  C  CA    . ILE A 1 2288 ? 145.013 194.061 149.232 1.00 11.88  ? 2288 ILE A CA    1 
ATOM   5975  C  C     . ILE A 1 2288 ? 143.604 194.626 149.098 1.00 16.26  ? 2288 ILE A C     1 
ATOM   5976  O  O     . ILE A 1 2288 ? 143.199 195.067 148.015 1.00 20.69  ? 2288 ILE A O     1 
ATOM   5977  C  CB    . ILE A 1 2288 ? 145.017 192.522 149.173 1.00 8.74   ? 2288 ILE A CB    1 
ATOM   5978  C  CG1   . ILE A 1 2288 ? 146.436 192.003 148.943 1.00 11.35  ? 2288 ILE A CG1   1 
ATOM   5979  C  CG2   . ILE A 1 2288 ? 144.085 192.021 148.085 1.00 10.26  ? 2288 ILE A CG2   1 
ATOM   5980  C  CD1   . ILE A 1 2288 ? 146.622 190.551 149.314 1.00 10.47  ? 2288 ILE A CD1   1 
ATOM   5981  N  N     . ASP A 1 2289 ? 142.833 194.619 150.188 1.00 15.16  ? 2289 ASP A N     1 
ATOM   5982  C  CA    . ASP A 1 2289 ? 141.482 195.169 150.139 1.00 15.83  ? 2289 ASP A CA    1 
ATOM   5983  C  C     . ASP A 1 2289 ? 141.507 196.660 149.826 1.00 20.82  ? 2289 ASP A C     1 
ATOM   5984  O  O     . ASP A 1 2289 ? 140.694 197.148 149.032 1.00 24.39  ? 2289 ASP A O     1 
ATOM   5985  C  CB    . ASP A 1 2289 ? 140.760 194.905 151.459 1.00 19.56  ? 2289 ASP A CB    1 
ATOM   5986  C  CG    . ASP A 1 2289 ? 140.607 193.426 151.753 1.00 30.54  ? 2289 ASP A CG    1 
ATOM   5987  O  OD1   . ASP A 1 2289 ? 141.005 192.604 150.902 1.00 24.62  ? 2289 ASP A OD1   1 
ATOM   5988  O  OD2   . ASP A 1 2289 ? 140.087 193.085 152.836 1.00 40.41  ? 2289 ASP A OD2   1 
ATOM   5989  N  N     . SER A 1 2290 ? 142.435 197.395 150.440 1.00 22.83  ? 2290 SER A N     1 
ATOM   5990  C  CA    . SER A 1 2290 ? 142.644 198.818 150.166 1.00 26.45  ? 2290 SER A CA    1 
ATOM   5991  C  C     . SER A 1 2290 ? 141.358 199.622 150.353 1.00 30.81  ? 2290 SER A C     1 
ATOM   5992  O  O     . SER A 1 2290 ? 140.965 200.420 149.499 1.00 36.34  ? 2290 SER A O     1 
ATOM   5993  C  CB    . SER A 1 2290 ? 143.220 199.027 148.765 1.00 22.78  ? 2290 SER A CB    1 
ATOM   5994  O  OG    . SER A 1 2290 ? 143.179 200.394 148.397 1.00 30.64  ? 2290 SER A OG    1 
ATOM   5995  N  N     . VAL A 1 2291 ? 140.696 199.399 151.489 1.00 30.99  ? 2291 VAL A N     1 
ATOM   5996  C  CA    . VAL A 1 2291 ? 139.499 200.168 151.812 1.00 32.36  ? 2291 VAL A CA    1 
ATOM   5997  C  C     . VAL A 1 2291 ? 139.842 201.645 151.950 1.00 38.74  ? 2291 VAL A C     1 
ATOM   5998  O  O     . VAL A 1 2291 ? 139.118 202.518 151.456 1.00 36.30  ? 2291 VAL A O     1 
ATOM   5999  C  CB    . VAL A 1 2291 ? 138.837 199.612 153.086 1.00 29.70  ? 2291 VAL A CB    1 
ATOM   6000  C  CG1   . VAL A 1 2291 ? 137.880 200.630 153.685 1.00 31.53  ? 2291 VAL A CG1   1 
ATOM   6001  C  CG2   . VAL A 1 2291 ? 138.115 198.310 152.781 1.00 22.33  ? 2291 VAL A CG2   1 
ATOM   6002  N  N     . ARG A 1 2292 ? 140.962 201.947 152.604 1.00 39.99  ? 2292 ARG A N     1 
ATOM   6003  C  CA    . ARG A 1 2292 ? 141.407 203.319 152.838 1.00 39.94  ? 2292 ARG A CA    1 
ATOM   6004  C  C     . ARG A 1 2292 ? 142.530 203.726 151.892 1.00 36.05  ? 2292 ARG A C     1 
ATOM   6005  O  O     . ARG A 1 2292 ? 143.442 204.460 152.279 1.00 40.79  ? 2292 ARG A O     1 
ATOM   6006  C  CB    . ARG A 1 2292 ? 141.842 203.486 154.290 1.00 39.07  ? 2292 ARG A CB    1 
ATOM   6007  C  CG    . ARG A 1 2292 ? 140.708 203.375 155.293 1.00 39.05  ? 2292 ARG A CG    1 
ATOM   6008  C  CD    . ARG A 1 2292 ? 141.214 203.548 156.714 1.00 51.51  ? 2292 ARG A CD    1 
ATOM   6009  N  NE    . ARG A 1 2292 ? 140.145 203.424 157.696 1.00 70.06  ? 2292 ARG A NE    1 
ATOM   6010  C  CZ    . ARG A 1 2292 ? 140.325 203.479 159.009 1.00 67.74  ? 2292 ARG A CZ    1 
ATOM   6011  N  NH1   . ARG A 1 2292 ? 141.526 203.654 159.535 1.00 59.34  ? 2292 ARG A NH1   1 
ATOM   6012  N  NH2   . ARG A 1 2292 ? 139.273 203.354 159.814 1.00 61.78  ? 2292 ARG A NH2   1 
ATOM   6013  N  N     . GLY A 1 2293 ? 142.483 203.266 150.646 1.00 35.63  ? 2293 GLY A N     1 
ATOM   6014  C  CA    . GLY A 1 2293 ? 143.493 203.623 149.663 1.00 31.88  ? 2293 GLY A CA    1 
ATOM   6015  C  C     . GLY A 1 2293 ? 144.880 203.085 149.947 1.00 30.74  ? 2293 GLY A C     1 
ATOM   6016  O  O     . GLY A 1 2293 ? 145.866 203.815 149.790 1.00 28.44  ? 2293 GLY A O     1 
ATOM   6017  N  N     . GLU A 1 2294 ? 144.981 201.820 150.362 1.00 34.93  ? 2294 GLU A N     1 
ATOM   6018  C  CA    . GLU A 1 2294 ? 146.283 201.245 150.681 1.00 27.34  ? 2294 GLU A CA    1 
ATOM   6019  C  C     . GLU A 1 2294 ? 147.105 200.955 149.431 1.00 26.19  ? 2294 GLU A C     1 
ATOM   6020  O  O     . GLU A 1 2294 ? 148.336 201.071 149.465 1.00 25.28  ? 2294 GLU A O     1 
ATOM   6021  C  CB    . GLU A 1 2294 ? 146.102 199.970 151.504 1.00 21.30  ? 2294 GLU A CB    1 
ATOM   6022  C  CG    . GLU A 1 2294 ? 146.107 200.198 153.005 1.00 31.35  ? 2294 GLU A CG    1 
ATOM   6023  C  CD    . GLU A 1 2294 ? 144.719 200.429 153.565 1.00 41.04  ? 2294 GLU A CD    1 
ATOM   6024  O  OE1   . GLU A 1 2294 ? 143.758 200.495 152.771 1.00 37.80  ? 2294 GLU A OE1   1 
ATOM   6025  O  OE2   . GLU A 1 2294 ? 144.587 200.543 154.802 1.00 43.86  ? 2294 GLU A OE2   1 
ATOM   6026  N  N     . LEU A 1 2295 ? 146.457 200.576 148.327 1.00 23.61  ? 2295 LEU A N     1 
ATOM   6027  C  CA    . LEU A 1 2295 ? 147.180 200.257 147.101 1.00 17.72  ? 2295 LEU A CA    1 
ATOM   6028  C  C     . LEU A 1 2295 ? 147.828 201.474 146.459 1.00 19.48  ? 2295 LEU A C     1 
ATOM   6029  O  O     . LEU A 1 2295 ? 148.697 201.308 145.598 1.00 18.83  ? 2295 LEU A O     1 
ATOM   6030  C  CB    . LEU A 1 2295 ? 146.244 199.589 146.092 1.00 16.80  ? 2295 LEU A CB    1 
ATOM   6031  C  CG    . LEU A 1 2295 ? 145.766 198.176 146.425 1.00 15.90  ? 2295 LEU A CG    1 
ATOM   6032  C  CD1   . LEU A 1 2295 ? 144.562 197.803 145.578 1.00 19.61  ? 2295 LEU A CD1   1 
ATOM   6033  C  CD2   . LEU A 1 2295 ? 146.888 197.178 146.234 1.00 12.64  ? 2295 LEU A CD2   1 
ATOM   6034  N  N     . GLN A 1 2296 ? 147.432 202.680 146.851 1.00 23.30  ? 2296 GLN A N     1 
ATOM   6035  C  CA    . GLN A 1 2296 ? 148.008 203.904 146.314 1.00 20.99  ? 2296 GLN A CA    1 
ATOM   6036  C  C     . GLN A 1 2296 ? 149.205 204.384 147.120 1.00 21.80  ? 2296 GLN A C     1 
ATOM   6037  O  O     . GLN A 1 2296 ? 149.760 205.443 146.811 1.00 29.43  ? 2296 GLN A O     1 
ATOM   6038  C  CB    . GLN A 1 2296 ? 146.943 205.003 146.259 1.00 23.78  ? 2296 GLN A CB    1 
ATOM   6039  C  CG    . GLN A 1 2296 ? 145.988 204.880 145.082 1.00 23.17  ? 2296 GLN A CG    1 
ATOM   6040  C  CD    . GLN A 1 2296 ? 144.979 203.763 145.266 1.00 28.47  ? 2296 GLN A CD    1 
ATOM   6041  O  OE1   . GLN A 1 2296 ? 144.945 202.807 144.492 1.00 33.14  ? 2296 GLN A OE1   1 
ATOM   6042  N  NE2   . GLN A 1 2296 ? 144.148 203.879 146.296 1.00 25.54  ? 2296 GLN A NE2   1 
ATOM   6043  N  N     . LYS A 1 2297 ? 149.613 203.632 148.136 1.00 24.11  ? 2297 LYS A N     1 
ATOM   6044  C  CA    . LYS A 1 2297 ? 150.710 203.997 149.016 1.00 19.63  ? 2297 LYS A CA    1 
ATOM   6045  C  C     . LYS A 1 2297 ? 151.834 202.981 148.876 1.00 15.40  ? 2297 LYS A C     1 
ATOM   6046  O  O     . LYS A 1 2297 ? 151.598 201.810 148.569 1.00 16.22  ? 2297 LYS A O     1 
ATOM   6047  C  CB    . LYS A 1 2297 ? 150.243 204.052 150.476 1.00 19.44  ? 2297 LYS A CB    1 
ATOM   6048  C  CG    . LYS A 1 2297 ? 148.938 204.799 150.671 1.00 23.86  ? 2297 LYS A CG    1 
ATOM   6049  C  CD    . LYS A 1 2297 ? 148.816 205.355 152.076 1.00 32.08  ? 2297 LYS A CD    1 
ATOM   6050  C  CE    . LYS A 1 2297 ? 147.370 205.305 152.551 1.00 44.04  ? 2297 LYS A CE    1 
ATOM   6051  N  NZ    . LYS A 1 2297 ? 147.261 205.256 154.033 1.00 39.72  ? 2297 LYS A NZ    1 
ATOM   6052  N  N     . ARG A 1 2298 ? 153.062 203.438 149.104 1.00 13.89  ? 2298 ARG A N     1 
ATOM   6053  C  CA    . ARG A 1 2298 ? 154.219 202.550 149.116 1.00 9.67   ? 2298 ARG A CA    1 
ATOM   6054  C  C     . ARG A 1 2298 ? 154.226 201.789 150.436 1.00 13.36  ? 2298 ARG A C     1 
ATOM   6055  O  O     . ARG A 1 2298 ? 154.535 202.356 151.488 1.00 18.23  ? 2298 ARG A O     1 
ATOM   6056  C  CB    . ARG A 1 2298 ? 155.506 203.347 148.923 1.00 7.41   ? 2298 ARG A CB    1 
ATOM   6057  C  CG    . ARG A 1 2298 ? 156.773 202.598 149.292 1.00 5.67   ? 2298 ARG A CG    1 
ATOM   6058  C  CD    . ARG A 1 2298 ? 158.013 203.433 149.016 1.00 5.58   ? 2298 ARG A CD    1 
ATOM   6059  N  NE    . ARG A 1 2298 ? 158.322 203.512 147.594 1.00 4.60   ? 2298 ARG A NE    1 
ATOM   6060  C  CZ    . ARG A 1 2298 ? 158.044 204.552 146.820 1.00 5.88   ? 2298 ARG A CZ    1 
ATOM   6061  N  NH1   . ARG A 1 2298 ? 157.439 205.627 147.297 1.00 12.47  ? 2298 ARG A NH1   1 
ATOM   6062  N  NH2   . ARG A 1 2298 ? 158.380 204.511 145.535 1.00 5.78   ? 2298 ARG A NH2   1 
ATOM   6063  N  N     . GLN A 1 2299 ? 153.880 200.506 150.386 1.00 10.65  ? 2299 GLN A N     1 
ATOM   6064  C  CA    . GLN A 1 2299 ? 153.754 199.679 151.579 1.00 7.90   ? 2299 GLN A CA    1 
ATOM   6065  C  C     . GLN A 1 2299 ? 155.012 198.838 151.746 1.00 8.73   ? 2299 GLN A C     1 
ATOM   6066  O  O     . GLN A 1 2299 ? 155.394 198.098 150.834 1.00 7.74   ? 2299 GLN A O     1 
ATOM   6067  C  CB    . GLN A 1 2299 ? 152.518 198.785 151.490 1.00 6.77   ? 2299 GLN A CB    1 
ATOM   6068  C  CG    . GLN A 1 2299 ? 151.234 199.527 151.172 1.00 7.20   ? 2299 GLN A CG    1 
ATOM   6069  C  CD    . GLN A 1 2299 ? 150.533 200.032 152.414 1.00 9.66   ? 2299 GLN A CD    1 
ATOM   6070  O  OE1   . GLN A 1 2299 ? 151.008 199.838 153.530 1.00 13.41  ? 2299 GLN A OE1   1 
ATOM   6071  N  NE2   . GLN A 1 2299 ? 149.394 200.684 152.226 1.00 15.75  ? 2299 GLN A NE2   1 
ATOM   6072  N  N     . TRP A 1 2300 ? 155.649 198.949 152.908 1.00 11.09  ? 2300 TRP A N     1 
ATOM   6073  C  CA    . TRP A 1 2300 ? 156.857 198.194 153.222 1.00 5.77   ? 2300 TRP A CA    1 
ATOM   6074  C  C     . TRP A 1 2300 ? 156.602 197.372 154.478 1.00 6.65   ? 2300 TRP A C     1 
ATOM   6075  O  O     . TRP A 1 2300 ? 156.467 197.929 155.572 1.00 9.66   ? 2300 TRP A O     1 
ATOM   6076  C  CB    . TRP A 1 2300 ? 158.055 199.123 153.414 1.00 5.04   ? 2300 TRP A CB    1 
ATOM   6077  C  CG    . TRP A 1 2300 ? 158.632 199.652 152.139 1.00 4.32   ? 2300 TRP A CG    1 
ATOM   6078  C  CD1   . TRP A 1 2300 ? 158.146 199.467 150.880 1.00 5.02   ? 2300 TRP A CD1   1 
ATOM   6079  C  CD2   . TRP A 1 2300 ? 159.813 200.448 151.999 1.00 3.82   ? 2300 TRP A CD2   1 
ATOM   6080  N  NE1   . TRP A 1 2300 ? 158.948 200.102 149.965 1.00 5.02   ? 2300 TRP A NE1   1 
ATOM   6081  C  CE2   . TRP A 1 2300 ? 159.979 200.712 150.627 1.00 5.40   ? 2300 TRP A CE2   1 
ATOM   6082  C  CE3   . TRP A 1 2300 ? 160.746 200.966 152.902 1.00 3.38   ? 2300 TRP A CE3   1 
ATOM   6083  C  CZ2   . TRP A 1 2300 ? 161.038 201.469 150.136 1.00 5.01   ? 2300 TRP A CZ2   1 
ATOM   6084  C  CZ3   . TRP A 1 2300 ? 161.795 201.717 152.413 1.00 3.61   ? 2300 TRP A CZ3   1 
ATOM   6085  C  CH2   . TRP A 1 2300 ? 161.933 201.962 151.043 1.00 4.46   ? 2300 TRP A CH2   1 
ATOM   6086  N  N     . ILE A 1 2301 ? 156.540 196.055 154.324 1.00 4.06   ? 2301 ILE A N     1 
ATOM   6087  C  CA    . ILE A 1 2301 ? 156.407 195.138 155.448 1.00 3.73   ? 2301 ILE A CA    1 
ATOM   6088  C  C     . ILE A 1 2301 ? 157.808 194.681 155.828 1.00 5.20   ? 2301 ILE A C     1 
ATOM   6089  O  O     . ILE A 1 2301 ? 158.432 193.895 155.109 1.00 7.89   ? 2301 ILE A O     1 
ATOM   6090  C  CB    . ILE A 1 2301 ? 155.502 193.948 155.107 1.00 2.93   ? 2301 ILE A CB    1 
ATOM   6091  C  CG1   . ILE A 1 2301 ? 154.128 194.437 154.650 1.00 4.17   ? 2301 ILE A CG1   1 
ATOM   6092  C  CG2   . ILE A 1 2301 ? 155.371 193.023 156.305 1.00 3.04   ? 2301 ILE A CG2   1 
ATOM   6093  C  CD1   . ILE A 1 2301 ? 153.174 193.323 154.289 1.00 4.17   ? 2301 ILE A CD1   1 
ATOM   6094  N  N     . VAL A 1 2302 ? 158.306 195.174 156.958 1.00 2.87   ? 2302 VAL A N     1 
ATOM   6095  C  CA    . VAL A 1 2302 ? 159.647 194.863 157.434 1.00 2.66   ? 2302 VAL A CA    1 
ATOM   6096  C  C     . VAL A 1 2302 ? 159.546 193.784 158.500 1.00 3.42   ? 2302 VAL A C     1 
ATOM   6097  O  O     . VAL A 1 2302 ? 158.707 193.872 159.406 1.00 5.03   ? 2302 VAL A O     1 
ATOM   6098  C  CB    . VAL A 1 2302 ? 160.350 196.115 157.984 1.00 3.54   ? 2302 VAL A CB    1 
ATOM   6099  C  CG1   . VAL A 1 2302 ? 161.838 195.857 158.149 1.00 3.16   ? 2302 VAL A CG1   1 
ATOM   6100  C  CG2   . VAL A 1 2302 ? 160.110 197.304 157.067 1.00 4.53   ? 2302 VAL A CG2   1 
ATOM   6101  N  N     . PHE A 1 2303 ? 160.381 192.757 158.380 1.00 3.75   ? 2303 PHE A N     1 
ATOM   6102  C  CA    . PHE A 1 2303 ? 160.506 191.697 159.375 1.00 2.72   ? 2303 PHE A CA    1 
ATOM   6103  C  C     . PHE A 1 2303 ? 161.800 191.960 160.140 1.00 4.39   ? 2303 PHE A C     1 
ATOM   6104  O  O     . PHE A 1 2303 ? 162.881 191.542 159.723 1.00 6.52   ? 2303 PHE A O     1 
ATOM   6105  C  CB    . PHE A 1 2303 ? 160.512 190.316 158.727 1.00 3.50   ? 2303 PHE A CB    1 
ATOM   6106  C  CG    . PHE A 1 2303 ? 159.161 189.852 158.264 1.00 3.71   ? 2303 PHE A CG    1 
ATOM   6107  C  CD1   . PHE A 1 2303 ? 158.199 189.458 159.175 1.00 4.06   ? 2303 PHE A CD1   1 
ATOM   6108  C  CD2   . PHE A 1 2303 ? 158.863 189.788 156.916 1.00 3.34   ? 2303 PHE A CD2   1 
ATOM   6109  C  CE1   . PHE A 1 2303 ? 156.960 189.024 158.749 1.00 3.94   ? 2303 PHE A CE1   1 
ATOM   6110  C  CE2   . PHE A 1 2303 ? 157.627 189.354 156.486 1.00 4.14   ? 2303 PHE A CE2   1 
ATOM   6111  C  CZ    . PHE A 1 2303 ? 156.675 188.971 157.403 1.00 3.25   ? 2303 PHE A CZ    1 
ATOM   6112  N  N     . ASP A 1 2304 ? 161.682 192.659 161.265 1.00 5.47   ? 2304 ASP A N     1 
ATOM   6113  C  CA    . ASP A 1 2304 ? 162.842 193.032 162.074 1.00 5.29   ? 2304 ASP A CA    1 
ATOM   6114  C  C     . ASP A 1 2304 ? 163.011 191.986 163.168 1.00 8.22   ? 2304 ASP A C     1 
ATOM   6115  O  O     . ASP A 1 2304 ? 162.496 192.123 164.277 1.00 12.65  ? 2304 ASP A O     1 
ATOM   6116  C  CB    . ASP A 1 2304 ? 162.669 194.432 162.648 1.00 7.25   ? 2304 ASP A CB    1 
ATOM   6117  C  CG    . ASP A 1 2304 ? 163.948 194.979 163.249 1.00 10.84  ? 2304 ASP A CG    1 
ATOM   6118  O  OD1   . ASP A 1 2304 ? 164.980 194.280 163.195 1.00 11.00  ? 2304 ASP A OD1   1 
ATOM   6119  O  OD2   . ASP A 1 2304 ? 163.920 196.108 163.779 1.00 13.31  ? 2304 ASP A OD2   1 
ATOM   6120  N  N     . GLY A 1 2305 ? 163.743 190.926 162.850 1.00 6.41   ? 2305 GLY A N     1 
ATOM   6121  C  CA    . GLY A 1 2305 ? 163.962 189.861 163.809 1.00 7.76   ? 2305 GLY A CA    1 
ATOM   6122  C  C     . GLY A 1 2305 ? 164.785 188.757 163.187 1.00 7.40   ? 2305 GLY A C     1 
ATOM   6123  O  O     . GLY A 1 2305 ? 165.264 188.866 162.055 1.00 8.73   ? 2305 GLY A O     1 
ATOM   6124  N  N     . ASP A 1 2306 ? 164.947 187.684 163.954 1.00 7.47   ? 2306 ASP A N     1 
ATOM   6125  C  CA    . ASP A 1 2306 ? 165.705 186.534 163.485 1.00 6.15   ? 2306 ASP A CA    1 
ATOM   6126  C  C     . ASP A 1 2306 ? 164.942 185.788 162.396 1.00 7.59   ? 2306 ASP A C     1 
ATOM   6127  O  O     . ASP A 1 2306 ? 163.710 185.758 162.374 1.00 10.15  ? 2306 ASP A O     1 
ATOM   6128  C  CB    . ASP A 1 2306 ? 166.013 185.590 164.645 1.00 7.44   ? 2306 ASP A CB    1 
ATOM   6129  C  CG    . ASP A 1 2306 ? 166.999 186.182 165.628 1.00 14.42  ? 2306 ASP A CG    1 
ATOM   6130  O  OD1   . ASP A 1 2306 ? 167.841 186.999 165.206 1.00 34.20  ? 2306 ASP A OD1   1 
ATOM   6131  O  OD2   . ASP A 1 2306 ? 166.932 185.831 166.824 1.00 15.23  ? 2306 ASP A OD2   1 
ATOM   6132  N  N     . VAL A 1 2307 ? 165.696 185.178 161.486 1.00 5.67   ? 2307 VAL A N     1 
ATOM   6133  C  CA    . VAL A 1 2307 ? 165.146 184.440 160.356 1.00 5.08   ? 2307 VAL A CA    1 
ATOM   6134  C  C     . VAL A 1 2307 ? 165.559 182.982 160.497 1.00 8.33   ? 2307 VAL A C     1 
ATOM   6135  O  O     . VAL A 1 2307 ? 166.754 182.677 160.591 1.00 15.67  ? 2307 VAL A O     1 
ATOM   6136  C  CB    . VAL A 1 2307 ? 165.622 185.017 159.014 1.00 4.62   ? 2307 VAL A CB    1 
ATOM   6137  C  CG1   . VAL A 1 2307 ? 165.444 184.000 157.902 1.00 7.72   ? 2307 VAL A CG1   1 
ATOM   6138  C  CG2   . VAL A 1 2307 ? 164.870 186.294 158.689 1.00 3.98   ? 2307 VAL A CG2   1 
ATOM   6139  N  N     . ASP A 1 2308 ? 164.579 182.089 160.516 1.00 9.65   ? 2308 ASP A N     1 
ATOM   6140  C  CA    . ASP A 1 2308 ? 164.808 180.654 160.497 1.00 9.49   ? 2308 ASP A CA    1 
ATOM   6141  C  C     . ASP A 1 2308 ? 163.851 180.012 159.505 1.00 10.09  ? 2308 ASP A C     1 
ATOM   6142  O  O     . ASP A 1 2308 ? 162.803 180.582 159.187 1.00 10.70  ? 2308 ASP A O     1 
ATOM   6143  C  CB    . ASP A 1 2308 ? 164.657 180.036 161.900 1.00 7.80   ? 2308 ASP A CB    1 
ATOM   6144  C  CG    . ASP A 1 2308 ? 163.249 180.153 162.481 1.00 9.93   ? 2308 ASP A CG    1 
ATOM   6145  O  OD1   . ASP A 1 2308 ? 162.278 180.430 161.758 1.00 12.30  ? 2308 ASP A OD1   1 
ATOM   6146  O  OD2   . ASP A 1 2308 ? 163.113 179.956 163.704 1.00 12.74  ? 2308 ASP A OD2   1 
ATOM   6147  N  N     . PRO A 1 2309 ? 164.188 178.827 158.983 1.00 8.96   ? 2309 PRO A N     1 
ATOM   6148  C  CA    . PRO A 1 2309 ? 163.334 178.210 157.955 1.00 8.04   ? 2309 PRO A CA    1 
ATOM   6149  C  C     . PRO A 1 2309 ? 161.929 177.873 158.428 1.00 8.70   ? 2309 PRO A C     1 
ATOM   6150  O  O     . PRO A 1 2309 ? 161.059 177.632 157.583 1.00 7.57   ? 2309 PRO A O     1 
ATOM   6151  C  CB    . PRO A 1 2309 ? 164.106 176.941 157.569 1.00 10.93  ? 2309 PRO A CB    1 
ATOM   6152  C  CG    . PRO A 1 2309 ? 165.031 176.686 158.708 1.00 12.07  ? 2309 PRO A CG    1 
ATOM   6153  C  CD    . PRO A 1 2309 ? 165.399 178.030 159.238 1.00 8.16   ? 2309 PRO A CD    1 
ATOM   6154  N  N     . GLU A 1 2310 ? 161.678 177.839 159.738 1.00 11.88  ? 2310 GLU A N     1 
ATOM   6155  C  CA    . GLU A 1 2310 ? 160.347 177.492 160.223 1.00 10.93  ? 2310 GLU A CA    1 
ATOM   6156  C  C     . GLU A 1 2310 ? 159.303 178.518 159.798 1.00 11.96  ? 2310 GLU A C     1 
ATOM   6157  O  O     . GLU A 1 2310 ? 158.196 178.147 159.390 1.00 21.87  ? 2310 GLU A O     1 
ATOM   6158  C  CB    . GLU A 1 2310 ? 160.364 177.343 161.742 1.00 16.73  ? 2310 GLU A CB    1 
ATOM   6159  C  CG    . GLU A 1 2310 ? 161.171 176.158 162.235 1.00 24.96  ? 2310 GLU A CG    1 
ATOM   6160  C  CD    . GLU A 1 2310 ? 160.505 174.834 161.925 1.00 36.63  ? 2310 GLU A CD    1 
ATOM   6161  O  OE1   . GLU A 1 2310 ? 159.263 174.755 162.031 1.00 41.92  ? 2310 GLU A OE1   1 
ATOM   6162  O  OE2   . GLU A 1 2310 ? 161.222 173.873 161.575 1.00 34.72  ? 2310 GLU A OE2   1 
ATOM   6163  N  N     . TRP A 1 2311 ? 159.625 179.810 159.882 1.00 7.98   ? 2311 TRP A N     1 
ATOM   6164  C  CA    . TRP A 1 2311 ? 158.644 180.842 159.567 1.00 6.06   ? 2311 TRP A CA    1 
ATOM   6165  C  C     . TRP A 1 2311 ? 158.874 181.520 158.224 1.00 5.30   ? 2311 TRP A C     1 
ATOM   6166  O  O     . TRP A 1 2311 ? 157.899 181.893 157.564 1.00 7.18   ? 2311 TRP A O     1 
ATOM   6167  C  CB    . TRP A 1 2311 ? 158.604 181.908 160.676 1.00 4.53   ? 2311 TRP A CB    1 
ATOM   6168  C  CG    . TRP A 1 2311 ? 159.727 182.912 160.643 1.00 4.70   ? 2311 TRP A CG    1 
ATOM   6169  C  CD1   . TRP A 1 2311 ? 160.869 182.881 161.382 1.00 4.17   ? 2311 TRP A CD1   1 
ATOM   6170  C  CD2   . TRP A 1 2311 ? 159.799 184.104 159.849 1.00 6.11   ? 2311 TRP A CD2   1 
ATOM   6171  N  NE1   . TRP A 1 2311 ? 161.657 183.963 161.087 1.00 4.54   ? 2311 TRP A NE1   1 
ATOM   6172  C  CE2   . TRP A 1 2311 ? 161.022 184.731 160.148 1.00 3.71   ? 2311 TRP A CE2   1 
ATOM   6173  C  CE3   . TRP A 1 2311 ? 158.952 184.696 158.908 1.00 3.33   ? 2311 TRP A CE3   1 
ATOM   6174  C  CZ2   . TRP A 1 2311 ? 161.419 185.916 159.543 1.00 3.01   ? 2311 TRP A CZ2   1 
ATOM   6175  C  CZ3   . TRP A 1 2311 ? 159.349 185.871 158.308 1.00 2.78   ? 2311 TRP A CZ3   1 
ATOM   6176  C  CH2   . TRP A 1 2311 ? 160.569 186.471 158.630 1.00 3.42   ? 2311 TRP A CH2   1 
ATOM   6177  N  N     . VAL A 1 2312 ? 160.124 181.689 157.789 1.00 5.10   ? 2312 VAL A N     1 
ATOM   6178  C  CA    . VAL A 1 2312 ? 160.365 182.477 156.584 1.00 4.47   ? 2312 VAL A CA    1 
ATOM   6179  C  C     . VAL A 1 2312 ? 160.072 181.685 155.314 1.00 7.01   ? 2312 VAL A C     1 
ATOM   6180  O  O     . VAL A 1 2312 ? 159.755 182.284 154.279 1.00 9.23   ? 2312 VAL A O     1 
ATOM   6181  C  CB    . VAL A 1 2312 ? 161.805 183.020 156.560 1.00 3.61   ? 2312 VAL A CB    1 
ATOM   6182  C  CG1   . VAL A 1 2312 ? 162.813 181.894 156.409 1.00 6.14   ? 2312 VAL A CG1   1 
ATOM   6183  C  CG2   . VAL A 1 2312 ? 161.975 184.081 155.482 1.00 3.15   ? 2312 VAL A CG2   1 
ATOM   6184  N  N     . GLU A 1 2313 ? 160.150 180.352 155.362 1.00 5.77   ? 2313 GLU A N     1 
ATOM   6185  C  CA    . GLU A 1 2313 ? 159.860 179.552 154.180 1.00 5.34   ? 2313 GLU A CA    1 
ATOM   6186  C  C     . GLU A 1 2313 ? 158.403 179.655 153.754 1.00 7.21   ? 2313 GLU A C     1 
ATOM   6187  O  O     . GLU A 1 2313 ? 158.101 179.442 152.574 1.00 10.11  ? 2313 GLU A O     1 
ATOM   6188  C  CB    . GLU A 1 2313 ? 160.232 178.091 154.427 1.00 7.14   ? 2313 GLU A CB    1 
ATOM   6189  C  CG    . GLU A 1 2313 ? 161.725 177.848 154.523 1.00 10.47  ? 2313 GLU A CG    1 
ATOM   6190  C  CD    . GLU A 1 2313 ? 162.362 177.606 153.176 1.00 18.01  ? 2313 GLU A CD    1 
ATOM   6191  O  OE1   . GLU A 1 2313 ? 161.734 176.931 152.335 1.00 20.85  ? 2313 GLU A OE1   1 
ATOM   6192  O  OE2   . GLU A 1 2313 ? 163.492 178.090 152.955 1.00 19.85  ? 2313 GLU A OE2   1 
ATOM   6193  N  N     . ASN A 1 2314 ? 157.499 180.001 154.673 1.00 7.31   ? 2314 ASN A N     1 
ATOM   6194  C  CA    . ASN A 1 2314 ? 156.117 180.268 154.297 1.00 4.65   ? 2314 ASN A CA    1 
ATOM   6195  C  C     . ASN A 1 2314 ? 156.001 181.424 153.318 1.00 6.89   ? 2314 ASN A C     1 
ATOM   6196  O  O     . ASN A 1 2314 ? 154.973 181.545 152.644 1.00 13.95  ? 2314 ASN A O     1 
ATOM   6197  C  CB    . ASN A 1 2314 ? 155.272 180.569 155.536 1.00 5.73   ? 2314 ASN A CB    1 
ATOM   6198  C  CG    . ASN A 1 2314 ? 154.922 179.325 156.324 1.00 8.36   ? 2314 ASN A CG    1 
ATOM   6199  O  OD1   . ASN A 1 2314 ? 155.795 178.540 156.689 1.00 10.11  ? 2314 ASN A OD1   1 
ATOM   6200  N  ND2   . ASN A 1 2314 ? 153.637 179.144 156.596 1.00 6.09   ? 2314 ASN A ND2   1 
ATOM   6201  N  N     . LEU A 1 2315 ? 157.022 182.272 153.228 1.00 7.24   ? 2315 LEU A N     1 
ATOM   6202  C  CA    . LEU A 1 2315 ? 157.055 183.385 152.295 1.00 6.01   ? 2315 LEU A CA    1 
ATOM   6203  C  C     . LEU A 1 2315 ? 157.722 183.025 150.976 1.00 6.64   ? 2315 LEU A C     1 
ATOM   6204  O  O     . LEU A 1 2315 ? 157.912 183.909 150.135 1.00 9.43   ? 2315 LEU A O     1 
ATOM   6205  C  CB    . LEU A 1 2315 ? 157.777 184.577 152.924 1.00 5.71   ? 2315 LEU A CB    1 
ATOM   6206  C  CG    . LEU A 1 2315 ? 157.219 185.119 154.238 1.00 5.79   ? 2315 LEU A CG    1 
ATOM   6207  C  CD1   . LEU A 1 2315 ? 158.094 186.246 154.752 1.00 5.14   ? 2315 LEU A CD1   1 
ATOM   6208  C  CD2   . LEU A 1 2315 ? 155.790 185.589 154.053 1.00 5.75   ? 2315 LEU A CD2   1 
ATOM   6209  N  N     . ASN A 1 2316 ? 158.093 181.755 150.780 1.00 6.13   ? 2316 ASN A N     1 
ATOM   6210  C  CA    . ASN A 1 2316 ? 158.812 181.375 149.566 1.00 7.27   ? 2316 ASN A CA    1 
ATOM   6211  C  C     . ASN A 1 2316 ? 158.020 181.741 148.318 1.00 7.24   ? 2316 ASN A C     1 
ATOM   6212  O  O     . ASN A 1 2316 ? 158.517 182.458 147.442 1.00 10.49  ? 2316 ASN A O     1 
ATOM   6213  C  CB    . ASN A 1 2316 ? 159.124 179.879 149.586 1.00 7.36   ? 2316 ASN A CB    1 
ATOM   6214  C  CG    . ASN A 1 2316 ? 160.362 179.552 150.395 1.00 5.56   ? 2316 ASN A CG    1 
ATOM   6215  O  OD1   . ASN A 1 2316 ? 160.990 180.434 150.979 1.00 7.46   ? 2316 ASN A OD1   1 
ATOM   6216  N  ND2   . ASN A 1 2316 ? 160.723 178.277 150.429 1.00 6.67   ? 2316 ASN A ND2   1 
ATOM   6217  N  N     . SER A 1 2317 ? 156.763 181.295 148.242 1.00 7.57   ? 2317 SER A N     1 
ATOM   6218  C  CA    . SER A 1 2317 ? 155.924 181.657 147.106 1.00 7.26   ? 2317 SER A CA    1 
ATOM   6219  C  C     . SER A 1 2317 ? 155.691 183.160 147.047 1.00 7.14   ? 2317 SER A C     1 
ATOM   6220  O  O     . SER A 1 2317 ? 155.457 183.711 145.966 1.00 9.42   ? 2317 SER A O     1 
ATOM   6221  C  CB    . SER A 1 2317 ? 154.591 180.914 147.177 1.00 8.74   ? 2317 SER A CB    1 
ATOM   6222  O  OG    . SER A 1 2317 ? 153.964 181.111 148.431 1.00 12.22  ? 2317 SER A OG    1 
ATOM   6223  N  N     . VAL A 1 2318 ? 155.747 183.835 148.196 1.00 8.55   ? 2318 VAL A N     1 
ATOM   6224  C  CA    . VAL A 1 2318 ? 155.650 185.290 148.212 1.00 7.82   ? 2318 VAL A CA    1 
ATOM   6225  C  C     . VAL A 1 2318 ? 156.879 185.910 147.559 1.00 8.93   ? 2318 VAL A C     1 
ATOM   6226  O  O     . VAL A 1 2318 ? 156.779 186.893 146.816 1.00 13.30  ? 2318 VAL A O     1 
ATOM   6227  C  CB    . VAL A 1 2318 ? 155.460 185.798 149.652 1.00 5.99   ? 2318 VAL A CB    1 
ATOM   6228  C  CG1   . VAL A 1 2318 ? 155.344 187.314 149.673 1.00 4.89   ? 2318 VAL A CG1   1 
ATOM   6229  C  CG2   . VAL A 1 2318 ? 154.239 185.156 150.282 1.00 5.13   ? 2318 VAL A CG2   1 
ATOM   6230  N  N     . LEU A 1 2319 ? 158.065 185.401 147.903 1.00 8.76   ? 2319 LEU A N     1 
ATOM   6231  C  CA    . LEU A 1 2319 ? 159.318 186.037 147.414 1.00 8.12   ? 2319 LEU A CA    1 
ATOM   6232  C  C     . LEU A 1 2319 ? 159.748 185.438 146.069 1.00 10.30  ? 2319 LEU A C     1 
ATOM   6233  O  O     . LEU A 1 2319 ? 160.870 185.745 145.619 1.00 18.42  ? 2319 LEU A O     1 
ATOM   6234  C  CB    . LEU A 1 2319 ? 160.389 185.849 148.487 1.00 10.82  ? 2319 LEU A CB    1 
ATOM   6235  C  CG    . LEU A 1 2319 ? 160.002 186.300 149.898 1.00 9.43   ? 2319 LEU A CG    1 
ATOM   6236  C  CD1   . LEU A 1 2319 ? 161.069 185.911 150.904 1.00 9.28   ? 2319 LEU A CD1   1 
ATOM   6237  C  CD2   . LEU A 1 2319 ? 159.748 187.796 149.935 1.00 7.51   ? 2319 LEU A CD2   1 
ATOM   6238  N  N     . ASP A 1 2320 ? 158.889 184.623 145.457 1.00 11.68  ? 2320 ASP A N     1 
ATOM   6239  C  CA    . ASP A 1 2320 ? 159.204 184.009 144.139 1.00 9.54   ? 2320 ASP A CA    1 
ATOM   6240  C  C     . ASP A 1 2320 ? 158.445 184.756 143.041 1.00 12.51  ? 2320 ASP A C     1 
ATOM   6241  O  O     . ASP A 1 2320 ? 157.837 185.801 143.349 1.00 13.45  ? 2320 ASP A O     1 
ATOM   6242  C  CB    . ASP A 1 2320 ? 158.892 182.521 144.134 1.00 10.58  ? 2320 ASP A CB    1 
ATOM   6243  C  CG    . ASP A 1 2320 ? 160.066 181.612 144.460 1.00 19.38  ? 2320 ASP A CG    1 
ATOM   6244  O  OD1   . ASP A 1 2320 ? 161.185 182.141 144.618 1.00 26.91  ? 2320 ASP A OD1   1 
ATOM   6245  O  OD2   . ASP A 1 2320 ? 159.849 180.387 144.561 1.00 20.98  ? 2320 ASP A OD2   1 
ATOM   6246  N  N     . ASP A 1 2321 ? 158.484 184.237 141.813 1.00 15.19  ? 2321 ASP A N     1 
ATOM   6247  C  CA    . ASP A 1 2321 ? 157.739 184.858 140.686 1.00 16.85  ? 2321 ASP A CA    1 
ATOM   6248  C  C     . ASP A 1 2321 ? 156.239 184.759 140.975 1.00 16.20  ? 2321 ASP A C     1 
ATOM   6249  O  O     . ASP A 1 2321 ? 155.477 185.584 140.427 1.00 17.44  ? 2321 ASP A O     1 
ATOM   6250  C  CB    . ASP A 1 2321 ? 158.116 184.208 139.365 1.00 23.26  ? 2321 ASP A CB    1 
ATOM   6251  C  CG    . ASP A 1 2321 ? 159.597 184.238 139.016 1.00 38.20  ? 2321 ASP A CG    1 
ATOM   6252  O  OD1   . ASP A 1 2321 ? 159.956 183.713 137.941 1.00 29.47  ? 2321 ASP A OD1   1 
ATOM   6253  O  OD2   . ASP A 1 2321 ? 160.378 184.787 139.821 1.00 37.24  ? 2321 ASP A OD2   1 
ATOM   6254  N  N     . ASN A 1 2322 ? 155.837 183.796 141.808 1.00 14.64  ? 2322 ASN A N     1 
ATOM   6255  C  CA    . ASN A 1 2322 ? 154.397 183.582 142.119 1.00 12.09  ? 2322 ASN A CA    1 
ATOM   6256  C  C     . ASN A 1 2322 ? 153.823 184.804 142.837 1.00 11.64  ? 2322 ASN A C     1 
ATOM   6257  O  O     . ASN A 1 2322 ? 152.616 185.070 142.663 1.00 16.24  ? 2322 ASN A O     1 
ATOM   6258  C  CB    . ASN A 1 2322 ? 154.198 182.323 142.954 1.00 10.32  ? 2322 ASN A CB    1 
ATOM   6259  C  CG    . ASN A 1 2322 ? 155.029 181.170 142.446 1.00 14.61  ? 2322 ASN A CG    1 
ATOM   6260  O  OD1   . ASN A 1 2322 ? 154.866 180.745 141.297 1.00 20.18  ? 2322 ASN A OD1   1 
ATOM   6261  N  ND2   . ASN A 1 2322 ? 155.922 180.655 143.278 1.00 11.83  ? 2322 ASN A ND2   1 
ATOM   6262  N  N     . LYS A 1 2323 ? 154.646 185.518 143.609 1.00 11.85  ? 2323 LYS A N     1 
ATOM   6263  C  CA    . LYS A 1 2323 ? 154.158 186.655 144.391 1.00 10.12  ? 2323 LYS A CA    1 
ATOM   6264  C  C     . LYS A 1 2323 ? 152.796 186.343 145.001 1.00 7.72   ? 2323 LYS A C     1 
ATOM   6265  O  O     . LYS A 1 2323 ? 151.836 187.107 144.886 1.00 11.45  ? 2323 LYS A O     1 
ATOM   6266  C  CB    . LYS A 1 2323 ? 154.105 187.927 143.547 1.00 9.23   ? 2323 LYS A CB    1 
ATOM   6267  C  CG    . LYS A 1 2323 ? 155.462 188.415 143.078 1.00 8.36   ? 2323 LYS A CG    1 
ATOM   6268  C  CD    . LYS A 1 2323 ? 155.336 189.697 142.276 1.00 8.15   ? 2323 LYS A CD    1 
ATOM   6269  C  CE    . LYS A 1 2323 ? 156.514 189.876 141.336 1.00 11.64  ? 2323 LYS A CE    1 
ATOM   6270  N  NZ    . LYS A 1 2323 ? 157.013 191.277 141.338 1.00 9.42   ? 2323 LYS A NZ    1 
ATOM   6271  N  N     . LEU A 1 2324 ? 152.719 185.188 145.656 1.00 6.22   ? 2324 LEU A N     1 
ATOM   6272  C  CA    . LEU A 1 2324 ? 151.462 184.676 146.179 1.00 7.87   ? 2324 LEU A CA    1 
ATOM   6273  C  C     . LEU A 1 2324 ? 151.689 184.074 147.555 1.00 8.31   ? 2324 LEU A C     1 
ATOM   6274  O  O     . LEU A 1 2324 ? 152.655 183.335 147.760 1.00 12.43  ? 2324 LEU A O     1 
ATOM   6275  C  CB    . LEU A 1 2324 ? 150.872 183.626 145.232 1.00 7.40   ? 2324 LEU A CB    1 
ATOM   6276  C  CG    . LEU A 1 2324 ? 149.380 183.322 145.336 1.00 9.55   ? 2324 LEU A CG    1 
ATOM   6277  C  CD1   . LEU A 1 2324 ? 148.563 184.436 144.715 1.00 10.75  ? 2324 LEU A CD1   1 
ATOM   6278  C  CD2   . LEU A 1 2324 ? 149.084 182.005 144.654 1.00 9.26   ? 2324 LEU A CD2   1 
ATOM   6279  N  N     . LEU A 1 2325 ? 150.804 184.393 148.492 1.00 5.92   ? 2325 LEU A N     1 
ATOM   6280  C  CA    . LEU A 1 2325 ? 150.795 183.781 149.813 1.00 6.39   ? 2325 LEU A CA    1 
ATOM   6281  C  C     . LEU A 1 2325 ? 149.678 182.749 149.848 1.00 8.79   ? 2325 LEU A C     1 
ATOM   6282  O  O     . LEU A 1 2325 ? 148.503 183.097 149.681 1.00 13.61  ? 2325 LEU A O     1 
ATOM   6283  C  CB    . LEU A 1 2325 ? 150.597 184.830 150.906 1.00 6.90   ? 2325 LEU A CB    1 
ATOM   6284  C  CG    . LEU A 1 2325 ? 150.485 184.301 152.337 1.00 4.96   ? 2325 LEU A CG    1 
ATOM   6285  C  CD1   . LEU A 1 2325 ? 151.845 183.871 152.855 1.00 3.80   ? 2325 LEU A CD1   1 
ATOM   6286  C  CD2   . LEU A 1 2325 ? 149.863 185.340 153.252 1.00 7.18   ? 2325 LEU A CD2   1 
ATOM   6287  N  N     . THR A 1 2326 ? 150.046 181.489 150.049 1.00 7.59   ? 2326 THR A N     1 
ATOM   6288  C  CA    . THR A 1 2326 ? 149.097 180.386 150.078 1.00 10.21  ? 2326 THR A CA    1 
ATOM   6289  C  C     . THR A 1 2326 ? 148.893 179.929 151.515 1.00 9.14   ? 2326 THR A C     1 
ATOM   6290  O  O     . THR A 1 2326 ? 149.863 179.681 152.238 1.00 7.64   ? 2326 THR A O     1 
ATOM   6291  C  CB    . THR A 1 2326 ? 149.583 179.217 149.217 1.00 9.17   ? 2326 THR A CB    1 
ATOM   6292  O  OG1   . THR A 1 2326 ? 150.600 178.494 149.919 1.00 8.34   ? 2326 THR A OG1   1 
ATOM   6293  C  CG2   . THR A 1 2326 ? 150.145 179.722 147.899 1.00 6.20   ? 2326 THR A CG2   1 
ATOM   6294  N  N     . LEU A 1 2327 ? 147.637 179.824 151.921 1.00 9.28   ? 2327 LEU A N     1 
ATOM   6295  C  CA    . LEU A 1 2327 ? 147.264 179.406 153.258 1.00 10.08  ? 2327 LEU A CA    1 
ATOM   6296  C  C     . LEU A 1 2327 ? 146.686 177.997 153.232 1.00 11.57  ? 2327 LEU A C     1 
ATOM   6297  O  O     . LEU A 1 2327 ? 146.179 177.542 152.202 1.00 16.01  ? 2327 LEU A O     1 
ATOM   6298  C  CB    . LEU A 1 2327 ? 146.242 180.381 153.857 1.00 11.83  ? 2327 LEU A CB    1 
ATOM   6299  C  CG    . LEU A 1 2327 ? 146.662 181.852 153.851 1.00 9.00   ? 2327 LEU A CG    1 
ATOM   6300  C  CD1   . LEU A 1 2327 ? 145.487 182.751 154.190 1.00 10.99  ? 2327 LEU A CD1   1 
ATOM   6301  C  CD2   . LEU A 1 2327 ? 147.818 182.084 154.810 1.00 7.49   ? 2327 LEU A CD2   1 
ATOM   6302  N  N     . PRO A 1 2328 ? 146.762 177.268 154.349 1.00 9.98   ? 2328 PRO A N     1 
ATOM   6303  C  CA    . PRO A 1 2328 ? 146.247 175.888 154.355 1.00 12.77  ? 2328 PRO A CA    1 
ATOM   6304  C  C     . PRO A 1 2328 ? 144.769 175.783 154.023 1.00 15.90  ? 2328 PRO A C     1 
ATOM   6305  O  O     . PRO A 1 2328 ? 144.333 174.743 153.515 1.00 17.86  ? 2328 PRO A O     1 
ATOM   6306  C  CB    . PRO A 1 2328 ? 146.540 175.408 155.784 1.00 12.06  ? 2328 PRO A CB    1 
ATOM   6307  C  CG    . PRO A 1 2328 ? 146.811 176.645 156.574 1.00 11.88  ? 2328 PRO A CG    1 
ATOM   6308  C  CD    . PRO A 1 2328 ? 147.412 177.617 155.621 1.00 8.94   ? 2328 PRO A CD    1 
ATOM   6309  N  N     . ASN A 1 2329 ? 143.983 176.825 154.284 1.00 12.53  ? 2329 ASN A N     1 
ATOM   6310  C  CA    . ASN A 1 2329 ? 142.557 176.806 153.984 1.00 10.21  ? 2329 ASN A CA    1 
ATOM   6311  C  C     . ASN A 1 2329 ? 142.256 177.012 152.504 1.00 15.19  ? 2329 ASN A C     1 
ATOM   6312  O  O     . ASN A 1 2329 ? 141.092 177.216 152.147 1.00 15.27  ? 2329 ASN A O     1 
ATOM   6313  C  CB    . ASN A 1 2329 ? 141.832 177.865 154.819 1.00 15.47  ? 2329 ASN A CB    1 
ATOM   6314  C  CG    . ASN A 1 2329 ? 142.023 179.267 154.279 1.00 17.54  ? 2329 ASN A CG    1 
ATOM   6315  O  OD1   . ASN A 1 2329 ? 143.128 179.657 153.908 1.00 14.70  ? 2329 ASN A OD1   1 
ATOM   6316  N  ND2   . ASN A 1 2329 ? 140.942 180.036 154.238 1.00 19.37  ? 2329 ASN A ND2   1 
ATOM   6317  N  N     . GLY A 1 2330 ? 143.269 176.958 151.640 1.00 15.15  ? 2330 GLY A N     1 
ATOM   6318  C  CA    . GLY A 1 2330 ? 143.076 177.094 150.214 1.00 11.29  ? 2330 GLY A CA    1 
ATOM   6319  C  C     . GLY A 1 2330 ? 143.042 178.514 149.700 1.00 14.09  ? 2330 GLY A C     1 
ATOM   6320  O  O     . GLY A 1 2330 ? 142.939 178.712 148.483 1.00 17.33  ? 2330 GLY A O     1 
ATOM   6321  N  N     . GLU A 1 2331 ? 143.128 179.506 150.579 1.00 16.22  ? 2331 GLU A N     1 
ATOM   6322  C  CA    . GLU A 1 2331 ? 143.098 180.898 150.158 1.00 16.02  ? 2331 GLU A CA    1 
ATOM   6323  C  C     . GLU A 1 2331 ? 144.467 181.326 149.646 1.00 13.34  ? 2331 GLU A C     1 
ATOM   6324  O  O     . GLU A 1 2331 ? 145.501 180.967 150.216 1.00 14.90  ? 2331 GLU A O     1 
ATOM   6325  C  CB    . GLU A 1 2331 ? 142.663 181.791 151.318 1.00 19.12  ? 2331 GLU A CB    1 
ATOM   6326  C  CG    . GLU A 1 2331 ? 142.271 183.198 150.914 1.00 24.75  ? 2331 GLU A CG    1 
ATOM   6327  C  CD    . GLU A 1 2331 ? 141.438 183.888 151.973 1.00 39.71  ? 2331 GLU A CD    1 
ATOM   6328  O  OE1   . GLU A 1 2331 ? 141.440 183.416 153.130 1.00 36.08  ? 2331 GLU A OE1   1 
ATOM   6329  O  OE2   . GLU A 1 2331 ? 140.781 184.900 151.650 1.00 46.41  ? 2331 GLU A OE2   1 
ATOM   6330  N  N     . ARG A 1 2332 ? 144.467 182.090 148.557 1.00 15.23  ? 2332 ARG A N     1 
ATOM   6331  C  CA    . ARG A 1 2332 ? 145.690 182.600 147.953 1.00 12.80  ? 2332 ARG A CA    1 
ATOM   6332  C  C     . ARG A 1 2332 ? 145.578 184.108 147.807 1.00 12.04  ? 2332 ARG A C     1 
ATOM   6333  O  O     . ARG A 1 2332 ? 144.626 184.605 147.197 1.00 12.02  ? 2332 ARG A O     1 
ATOM   6334  C  CB    . ARG A 1 2332 ? 145.950 181.952 146.590 1.00 10.27  ? 2332 ARG A CB    1 
ATOM   6335  C  CG    . ARG A 1 2332 ? 145.793 180.444 146.584 1.00 12.88  ? 2332 ARG A CG    1 
ATOM   6336  C  CD    . ARG A 1 2332 ? 145.185 179.959 145.282 1.00 11.74  ? 2332 ARG A CD    1 
ATOM   6337  N  NE    . ARG A 1 2332 ? 146.141 180.011 144.183 1.00 12.47  ? 2332 ARG A NE    1 
ATOM   6338  C  CZ    . ARG A 1 2332 ? 147.152 179.169 144.026 1.00 11.31  ? 2332 ARG A CZ    1 
ATOM   6339  N  NH1   . ARG A 1 2332 ? 147.366 178.178 144.877 1.00 7.56   ? 2332 ARG A NH1   1 
ATOM   6340  N  NH2   . ARG A 1 2332 ? 147.970 179.323 142.989 1.00 11.88  ? 2332 ARG A NH2   1 
ATOM   6341  N  N     . LEU A 1 2333 ? 146.550 184.830 148.357 1.00 9.97   ? 2333 LEU A N     1 
ATOM   6342  C  CA    . LEU A 1 2333 ? 146.575 186.287 148.310 1.00 7.81   ? 2333 LEU A CA    1 
ATOM   6343  C  C     . LEU A 1 2333 ? 147.736 186.733 147.434 1.00 9.28   ? 2333 LEU A C     1 
ATOM   6344  O  O     . LEU A 1 2333 ? 148.885 186.368 147.692 1.00 13.37  ? 2333 LEU A O     1 
ATOM   6345  C  CB    . LEU A 1 2333 ? 146.704 186.880 149.712 1.00 10.31  ? 2333 LEU A CB    1 
ATOM   6346  C  CG    . LEU A 1 2333 ? 145.570 186.601 150.702 1.00 10.13  ? 2333 LEU A CG    1 
ATOM   6347  C  CD1   . LEU A 1 2333 ? 145.898 185.403 151.573 1.00 15.57  ? 2333 LEU A CD1   1 
ATOM   6348  C  CD2   . LEU A 1 2333 ? 145.298 187.823 151.556 1.00 8.75   ? 2333 LEU A CD2   1 
ATOM   6349  N  N     . SER A 1 2334 ? 147.438 187.524 146.408 1.00 10.98  ? 2334 SER A N     1 
ATOM   6350  C  CA    . SER A 1 2334 ? 148.472 188.003 145.503 1.00 8.95   ? 2334 SER A CA    1 
ATOM   6351  C  C     . SER A 1 2334 ? 149.162 189.231 146.082 1.00 10.14  ? 2334 SER A C     1 
ATOM   6352  O  O     . SER A 1 2334 ? 148.515 190.116 146.647 1.00 11.79  ? 2334 SER A O     1 
ATOM   6353  C  CB    . SER A 1 2334 ? 147.876 188.330 144.135 1.00 9.89   ? 2334 SER A CB    1 
ATOM   6354  O  OG    . SER A 1 2334 ? 148.868 188.824 143.253 1.00 16.52  ? 2334 SER A OG    1 
ATOM   6355  N  N     . LEU A 1 2335 ? 150.481 189.279 145.938 1.00 9.61   ? 2335 LEU A N     1 
ATOM   6356  C  CA    . LEU A 1 2335 ? 151.256 190.403 146.449 1.00 7.33   ? 2335 LEU A CA    1 
ATOM   6357  C  C     . LEU A 1 2335 ? 151.073 191.615 145.544 1.00 8.70   ? 2335 LEU A C     1 
ATOM   6358  O  O     . LEU A 1 2335 ? 151.376 191.532 144.348 1.00 9.83   ? 2335 LEU A O     1 
ATOM   6359  C  CB    . LEU A 1 2335 ? 152.731 190.037 146.545 1.00 6.15   ? 2335 LEU A CB    1 
ATOM   6360  C  CG    . LEU A 1 2335 ? 153.597 190.960 147.402 1.00 7.08   ? 2335 LEU A CG    1 
ATOM   6361  C  CD1   . LEU A 1 2335 ? 153.380 190.679 148.876 1.00 11.06  ? 2335 LEU A CD1   1 
ATOM   6362  C  CD2   . LEU A 1 2335 ? 155.064 190.811 147.041 1.00 8.28   ? 2335 LEU A CD2   1 
ATOM   6363  N  N     . PRO A 1 2336 ? 150.583 192.743 146.061 1.00 8.00   ? 2336 PRO A N     1 
ATOM   6364  C  CA    . PRO A 1 2336 ? 150.406 193.917 145.211 1.00 6.44   ? 2336 PRO A CA    1 
ATOM   6365  C  C     . PRO A 1 2336 ? 151.746 194.470 144.759 1.00 8.54   ? 2336 PRO A C     1 
ATOM   6366  O  O     . PRO A 1 2336 ? 152.760 194.330 145.463 1.00 10.47  ? 2336 PRO A O     1 
ATOM   6367  C  CB    . PRO A 1 2336 ? 149.670 194.910 146.128 1.00 7.58   ? 2336 PRO A CB    1 
ATOM   6368  C  CG    . PRO A 1 2336 ? 149.078 194.071 147.211 1.00 9.08   ? 2336 PRO A CG    1 
ATOM   6369  C  CD    . PRO A 1 2336 ? 150.045 192.954 147.414 1.00 10.60  ? 2336 PRO A CD    1 
ATOM   6370  N  N     . PRO A 1 2337 ? 151.798 195.111 143.587 1.00 8.98   ? 2337 PRO A N     1 
ATOM   6371  C  CA    . PRO A 1 2337 ? 153.083 195.628 143.086 1.00 10.46  ? 2337 PRO A CA    1 
ATOM   6372  C  C     . PRO A 1 2337 ? 153.683 196.737 143.935 1.00 8.54   ? 2337 PRO A C     1 
ATOM   6373  O  O     . PRO A 1 2337 ? 154.883 197.005 143.805 1.00 9.99   ? 2337 PRO A O     1 
ATOM   6374  C  CB    . PRO A 1 2337 ? 152.735 196.132 141.679 1.00 5.82   ? 2337 PRO A CB    1 
ATOM   6375  C  CG    . PRO A 1 2337 ? 151.267 196.384 141.720 1.00 10.16  ? 2337 PRO A CG    1 
ATOM   6376  C  CD    . PRO A 1 2337 ? 150.695 195.357 142.645 1.00 7.38   ? 2337 PRO A CD    1 
ATOM   6377  N  N     . ASN A 1 2338 ? 152.901 197.393 144.786 1.00 7.14   ? 2338 ASN A N     1 
ATOM   6378  C  CA    . ASN A 1 2338 ? 153.400 198.487 145.609 1.00 8.73   ? 2338 ASN A CA    1 
ATOM   6379  C  C     . ASN A 1 2338 ? 153.929 198.023 146.958 1.00 9.84   ? 2338 ASN A C     1 
ATOM   6380  O  O     . ASN A 1 2338 ? 154.321 198.862 147.775 1.00 9.42   ? 2338 ASN A O     1 
ATOM   6381  C  CB    . ASN A 1 2338 ? 152.299 199.530 145.824 1.00 10.84  ? 2338 ASN A CB    1 
ATOM   6382  C  CG    . ASN A 1 2338 ? 151.167 199.013 146.687 1.00 10.61  ? 2338 ASN A CG    1 
ATOM   6383  O  OD1   . ASN A 1 2338 ? 150.596 197.960 146.414 1.00 12.64  ? 2338 ASN A OD1   1 
ATOM   6384  N  ND2   . ASN A 1 2338 ? 150.834 199.756 147.734 1.00 11.03  ? 2338 ASN A ND2   1 
ATOM   6385  N  N     . VAL A 1 2339 ? 153.953 196.718 147.212 1.00 9.52   ? 2339 VAL A N     1 
ATOM   6386  C  CA    . VAL A 1 2339 ? 154.364 196.168 148.497 1.00 5.82   ? 2339 VAL A CA    1 
ATOM   6387  C  C     . VAL A 1 2339 ? 155.750 195.558 148.354 1.00 6.61   ? 2339 VAL A C     1 
ATOM   6388  O  O     . VAL A 1 2339 ? 156.011 194.801 147.411 1.00 10.59  ? 2339 VAL A O     1 
ATOM   6389  C  CB    . VAL A 1 2339 ? 153.355 195.125 149.003 1.00 5.90   ? 2339 VAL A CB    1 
ATOM   6390  C  CG1   . VAL A 1 2339 ? 153.788 194.581 150.354 1.00 7.31   ? 2339 VAL A CG1   1 
ATOM   6391  C  CG2   . VAL A 1 2339 ? 151.970 195.736 149.090 1.00 6.56   ? 2339 VAL A CG2   1 
ATOM   6392  N  N     . ARG A 1 2340 ? 156.641 195.893 149.284 1.00 5.99   ? 2340 ARG A N     1 
ATOM   6393  C  CA    . ARG A 1 2340 ? 157.971 195.309 149.356 1.00 4.61   ? 2340 ARG A CA    1 
ATOM   6394  C  C     . ARG A 1 2340 ? 158.104 194.544 150.664 1.00 5.09   ? 2340 ARG A C     1 
ATOM   6395  O  O     . ARG A 1 2340 ? 157.811 195.085 151.734 1.00 9.59   ? 2340 ARG A O     1 
ATOM   6396  C  CB    . ARG A 1 2340 ? 159.060 196.381 149.263 1.00 4.80   ? 2340 ARG A CB    1 
ATOM   6397  C  CG    . ARG A 1 2340 ? 159.050 197.171 147.972 1.00 4.38   ? 2340 ARG A CG    1 
ATOM   6398  C  CD    . ARG A 1 2340 ? 159.607 196.354 146.822 1.00 4.18   ? 2340 ARG A CD    1 
ATOM   6399  N  NE    . ARG A 1 2340 ? 159.643 197.118 145.581 1.00 4.81   ? 2340 ARG A NE    1 
ATOM   6400  C  CZ    . ARG A 1 2340 ? 158.579 197.402 144.844 1.00 6.32   ? 2340 ARG A CZ    1 
ATOM   6401  N  NH1   . ARG A 1 2340 ? 157.366 197.015 145.201 1.00 8.02   ? 2340 ARG A NH1   1 
ATOM   6402  N  NH2   . ARG A 1 2340 ? 158.735 198.096 143.721 1.00 8.33   ? 2340 ARG A NH2   1 
ATOM   6403  N  N     . ILE A 1 2341 ? 158.546 193.294 150.575 1.00 5.65   ? 2341 ILE A N     1 
ATOM   6404  C  CA    . ILE A 1 2341 ? 158.783 192.467 151.752 1.00 3.69   ? 2341 ILE A CA    1 
ATOM   6405  C  C     . ILE A 1 2341 ? 160.253 192.608 152.123 1.00 4.66   ? 2341 ILE A C     1 
ATOM   6406  O  O     . ILE A 1 2341 ? 161.136 192.210 151.359 1.00 6.28   ? 2341 ILE A O     1 
ATOM   6407  C  CB    . ILE A 1 2341 ? 158.407 191.002 151.497 1.00 4.31   ? 2341 ILE A CB    1 
ATOM   6408  C  CG1   . ILE A 1 2341 ? 156.986 190.905 150.942 1.00 5.53   ? 2341 ILE A CG1   1 
ATOM   6409  C  CG2   . ILE A 1 2341 ? 158.535 190.190 152.773 1.00 5.07   ? 2341 ILE A CG2   1 
ATOM   6410  C  CD1   . ILE A 1 2341 ? 155.921 191.360 151.907 1.00 5.65   ? 2341 ILE A CD1   1 
ATOM   6411  N  N     . MET A 1 2342 ? 160.519 193.172 153.296 1.00 6.03   ? 2342 MET A N     1 
ATOM   6412  C  CA    . MET A 1 2342 ? 161.873 193.464 153.736 1.00 3.63   ? 2342 MET A CA    1 
ATOM   6413  C  C     . MET A 1 2342 ? 162.177 192.742 155.040 1.00 3.72   ? 2342 MET A C     1 
ATOM   6414  O  O     . MET A 1 2342 ? 161.297 192.540 155.880 1.00 3.72   ? 2342 MET A O     1 
ATOM   6415  C  CB    . MET A 1 2342 ? 162.084 194.970 153.919 1.00 3.41   ? 2342 MET A CB    1 
ATOM   6416  C  CG    . MET A 1 2342 ? 162.240 195.731 152.619 1.00 5.69   ? 2342 MET A CG    1 
ATOM   6417  S  SD    . MET A 1 2342 ? 162.266 197.516 152.851 1.00 23.65  ? 2342 MET A SD    1 
ATOM   6418  C  CE    . MET A 1 2342 ? 162.252 198.067 151.149 1.00 8.22   ? 2342 MET A CE    1 
ATOM   6419  N  N     . PHE A 1 2343 ? 163.437 192.347 155.194 1.00 4.25   ? 2343 PHE A N     1 
ATOM   6420  C  CA    . PHE A 1 2343 ? 163.931 191.728 156.415 1.00 3.28   ? 2343 PHE A CA    1 
ATOM   6421  C  C     . PHE A 1 2343 ? 165.127 192.521 156.916 1.00 4.74   ? 2343 PHE A C     1 
ATOM   6422  O  O     . PHE A 1 2343 ? 166.054 192.803 156.150 1.00 7.58   ? 2343 PHE A O     1 
ATOM   6423  C  CB    . PHE A 1 2343 ? 164.332 190.264 156.191 1.00 3.35   ? 2343 PHE A CB    1 
ATOM   6424  C  CG    . PHE A 1 2343 ? 163.284 189.439 155.498 1.00 3.38   ? 2343 PHE A CG    1 
ATOM   6425  C  CD1   . PHE A 1 2343 ? 163.130 189.493 154.124 1.00 5.07   ? 2343 PHE A CD1   1 
ATOM   6426  C  CD2   . PHE A 1 2343 ? 162.457 188.602 156.224 1.00 2.90   ? 2343 PHE A CD2   1 
ATOM   6427  C  CE1   . PHE A 1 2343 ? 162.169 188.736 153.491 1.00 4.43   ? 2343 PHE A CE1   1 
ATOM   6428  C  CE2   . PHE A 1 2343 ? 161.496 187.842 155.594 1.00 3.61   ? 2343 PHE A CE2   1 
ATOM   6429  C  CZ    . PHE A 1 2343 ? 161.352 187.909 154.227 1.00 4.18   ? 2343 PHE A CZ    1 
ATOM   6430  N  N     . GLU A 1 2344 ? 165.104 192.879 158.193 1.00 3.72   ? 2344 GLU A N     1 
ATOM   6431  C  CA    . GLU A 1 2344 ? 166.223 193.545 158.851 1.00 2.42   ? 2344 GLU A CA    1 
ATOM   6432  C  C     . GLU A 1 2344 ? 166.776 192.568 159.881 1.00 3.14   ? 2344 GLU A C     1 
ATOM   6433  O  O     . GLU A 1 2344 ? 166.171 192.353 160.934 1.00 4.99   ? 2344 GLU A O     1 
ATOM   6434  C  CB    . GLU A 1 2344 ? 165.788 194.857 159.489 1.00 4.86   ? 2344 GLU A CB    1 
ATOM   6435  C  CG    . GLU A 1 2344 ? 166.940 195.725 159.952 1.00 4.54   ? 2344 GLU A CG    1 
ATOM   6436  C  CD    . GLU A 1 2344 ? 166.494 196.828 160.878 1.00 5.24   ? 2344 GLU A CD    1 
ATOM   6437  O  OE1   . GLU A 1 2344 ? 165.498 197.506 160.555 1.00 10.16  ? 2344 GLU A OE1   1 
ATOM   6438  O  OE2   . GLU A 1 2344 ? 167.139 197.025 161.927 1.00 5.03   ? 2344 GLU A OE2   1 
ATOM   6439  N  N     . VAL A 1 2345 ? 167.924 191.974 159.569 1.00 3.87   ? 2345 VAL A N     1 
ATOM   6440  C  CA    . VAL A 1 2345 ? 168.502 190.911 160.375 1.00 2.97   ? 2345 VAL A CA    1 
ATOM   6441  C  C     . VAL A 1 2345 ? 169.953 191.256 160.673 1.00 3.78   ? 2345 VAL A C     1 
ATOM   6442  O  O     . VAL A 1 2345 ? 170.562 192.112 160.027 1.00 5.11   ? 2345 VAL A O     1 
ATOM   6443  C  CB    . VAL A 1 2345 ? 168.407 189.539 159.678 1.00 3.52   ? 2345 VAL A CB    1 
ATOM   6444  C  CG1   . VAL A 1 2345 ? 166.963 189.193 159.373 1.00 3.65   ? 2345 VAL A CG1   1 
ATOM   6445  C  CG2   . VAL A 1 2345 ? 169.241 189.530 158.408 1.00 3.53   ? 2345 VAL A CG2   1 
ATOM   6446  N  N     . GLN A 1 2346 ? 170.505 190.576 161.676 1.00 5.18   ? 2346 GLN A N     1 
ATOM   6447  C  CA    . GLN A 1 2346 ? 171.916 190.714 162.000 1.00 4.78   ? 2346 GLN A CA    1 
ATOM   6448  C  C     . GLN A 1 2346 ? 172.773 189.594 161.430 1.00 7.81   ? 2346 GLN A C     1 
ATOM   6449  O  O     . GLN A 1 2346 ? 173.996 189.753 161.345 1.00 7.98   ? 2346 GLN A O     1 
ATOM   6450  C  CB    . GLN A 1 2346 ? 172.111 190.794 163.519 1.00 4.68   ? 2346 GLN A CB    1 
ATOM   6451  C  CG    . GLN A 1 2346 ? 172.169 189.458 164.233 1.00 6.13   ? 2346 GLN A CG    1 
ATOM   6452  C  CD    . GLN A 1 2346 ? 172.174 189.612 165.740 1.00 8.75   ? 2346 GLN A CD    1 
ATOM   6453  O  OE1   . GLN A 1 2346 ? 172.686 190.595 166.272 1.00 8.22   ? 2346 GLN A OE1   1 
ATOM   6454  N  NE2   . GLN A 1 2346 ? 171.598 188.641 166.437 1.00 13.82  ? 2346 GLN A NE2   1 
ATOM   6455  N  N     . ASP A 1 2347 ? 172.166 188.478 161.035 1.00 7.22   ? 2347 ASP A N     1 
ATOM   6456  C  CA    . ASP A 1 2347 ? 172.895 187.386 160.407 1.00 7.06   ? 2347 ASP A CA    1 
ATOM   6457  C  C     . ASP A 1 2347 ? 171.901 186.488 159.690 1.00 8.82   ? 2347 ASP A C     1 
ATOM   6458  O  O     . ASP A 1 2347 ? 170.685 186.630 159.843 1.00 6.95   ? 2347 ASP A O     1 
ATOM   6459  C  CB    . ASP A 1 2347 ? 173.713 186.581 161.425 1.00 5.73   ? 2347 ASP A CB    1 
ATOM   6460  C  CG    . ASP A 1 2347 ? 172.856 185.977 162.523 1.00 11.80  ? 2347 ASP A CG    1 
ATOM   6461  O  OD1   . ASP A 1 2347 ? 172.110 185.015 162.248 1.00 18.60  ? 2347 ASP A OD1   1 
ATOM   6462  O  OD2   . ASP A 1 2347 ? 172.943 186.457 163.672 1.00 13.21  ? 2347 ASP A OD2   1 
ATOM   6463  N  N     . LEU A 1 2348 ? 172.438 185.563 158.903 1.00 9.29   ? 2348 LEU A N     1 
ATOM   6464  C  CA    . LEU A 1 2348 ? 171.652 184.560 158.199 1.00 8.52   ? 2348 LEU A CA    1 
ATOM   6465  C  C     . LEU A 1 2348 ? 172.253 183.178 158.389 1.00 11.26  ? 2348 LEU A C     1 
ATOM   6466  O  O     . LEU A 1 2348 ? 172.220 182.340 157.486 1.00 19.02  ? 2348 LEU A O     1 
ATOM   6467  C  CB    . LEU A 1 2348 ? 171.543 184.889 156.711 1.00 8.80   ? 2348 LEU A CB    1 
ATOM   6468  C  CG    . LEU A 1 2348 ? 170.640 186.054 156.305 1.00 7.36   ? 2348 LEU A CG    1 
ATOM   6469  C  CD1   . LEU A 1 2348 ? 170.822 186.389 154.841 1.00 9.34   ? 2348 LEU A CD1   1 
ATOM   6470  C  CD2   . LEU A 1 2348 ? 169.191 185.722 156.590 1.00 5.14   ? 2348 LEU A CD2   1 
ATOM   6471  N  N     . LYS A 1 2349 ? 172.813 182.907 159.569 1.00 10.54  ? 2349 LYS A N     1 
ATOM   6472  C  CA    . LYS A 1 2349 ? 173.473 181.622 159.760 1.00 16.37  ? 2349 LYS A CA    1 
ATOM   6473  C  C     . LYS A 1 2349 ? 172.490 180.469 159.905 1.00 10.06  ? 2349 LYS A C     1 
ATOM   6474  O  O     . LYS A 1 2349 ? 172.923 179.312 159.920 1.00 13.06  ? 2349 LYS A O     1 
ATOM   6475  C  CB    . LYS A 1 2349 ? 174.397 181.665 160.977 1.00 18.03  ? 2349 LYS A CB    1 
ATOM   6476  C  CG    . LYS A 1 2349 ? 173.672 181.660 162.301 1.00 17.14  ? 2349 LYS A CG    1 
ATOM   6477  C  CD    . LYS A 1 2349 ? 174.639 181.778 163.466 1.00 23.43  ? 2349 LYS A CD    1 
ATOM   6478  C  CE    . LYS A 1 2349 ? 175.676 180.665 163.453 1.00 29.02  ? 2349 LYS A CE    1 
ATOM   6479  N  NZ    . LYS A 1 2349 ? 175.063 179.319 163.617 1.00 26.70  ? 2349 LYS A NZ    1 
ATOM   6480  N  N     . TYR A 1 2350 ? 171.192 180.746 160.024 1.00 10.69  ? 2350 TYR A N     1 
ATOM   6481  C  CA    . TYR A 1 2350 ? 170.190 179.695 160.119 1.00 7.85   ? 2350 TYR A CA    1 
ATOM   6482  C  C     . TYR A 1 2350 ? 169.230 179.663 158.940 1.00 12.97  ? 2350 TYR A C     1 
ATOM   6483  O  O     . TYR A 1 2350 ? 168.510 178.672 158.780 1.00 18.46  ? 2350 TYR A O     1 
ATOM   6484  C  CB    . TYR A 1 2350 ? 169.395 179.835 161.425 1.00 8.41   ? 2350 TYR A CB    1 
ATOM   6485  C  CG    . TYR A 1 2350 ? 170.217 179.499 162.646 1.00 10.86  ? 2350 TYR A CG    1 
ATOM   6486  C  CD1   . TYR A 1 2350 ? 170.599 178.192 162.909 1.00 10.26  ? 2350 TYR A CD1   1 
ATOM   6487  C  CD2   . TYR A 1 2350 ? 170.625 180.489 163.525 1.00 10.46  ? 2350 TYR A CD2   1 
ATOM   6488  C  CE1   . TYR A 1 2350 ? 171.359 177.881 164.016 1.00 14.35  ? 2350 TYR A CE1   1 
ATOM   6489  C  CE2   . TYR A 1 2350 ? 171.387 180.188 164.635 1.00 11.62  ? 2350 TYR A CE2   1 
ATOM   6490  C  CZ    . TYR A 1 2350 ? 171.749 178.882 164.876 1.00 18.51  ? 2350 TYR A CZ    1 
ATOM   6491  O  OH    . TYR A 1 2350 ? 172.505 178.573 165.982 1.00 28.76  ? 2350 TYR A OH    1 
ATOM   6492  N  N     . ALA A 1 2351 ? 169.200 180.705 158.116 1.00 14.56  ? 2351 ALA A N     1 
ATOM   6493  C  CA    . ALA A 1 2351 ? 168.365 180.694 156.923 1.00 8.40   ? 2351 ALA A CA    1 
ATOM   6494  C  C     . ALA A 1 2351 ? 168.940 179.749 155.876 1.00 8.20   ? 2351 ALA A C     1 
ATOM   6495  O  O     . ALA A 1 2351 ? 170.156 179.678 155.679 1.00 10.34  ? 2351 ALA A O     1 
ATOM   6496  C  CB    . ALA A 1 2351 ? 168.242 182.102 156.345 1.00 8.73   ? 2351 ALA A CB    1 
ATOM   6497  N  N     . THR A 1 2352 ? 168.056 179.021 155.204 1.00 9.78   ? 2352 THR A N     1 
ATOM   6498  C  CA    . THR A 1 2352 ? 168.469 178.137 154.129 1.00 7.49   ? 2352 THR A CA    1 
ATOM   6499  C  C     . THR A 1 2352 ? 168.716 178.934 152.851 1.00 7.09   ? 2352 THR A C     1 
ATOM   6500  O  O     . THR A 1 2352 ? 168.357 180.109 152.736 1.00 7.45   ? 2352 THR A O     1 
ATOM   6501  C  CB    . THR A 1 2352 ? 167.417 177.056 153.887 1.00 9.37   ? 2352 THR A CB    1 
ATOM   6502  O  OG1   . THR A 1 2352 ? 166.149 177.670 153.624 1.00 12.99  ? 2352 THR A OG1   1 
ATOM   6503  C  CG2   . THR A 1 2352 ? 167.293 176.153 155.102 1.00 12.07  ? 2352 THR A CG2   1 
ATOM   6504  N  N     . LEU A 1 2353 ? 169.317 178.276 151.855 1.00 10.31  ? 2353 LEU A N     1 
ATOM   6505  C  CA    . LEU A 1 2353 ? 169.600 178.955 150.561 1.00 9.69   ? 2353 LEU A CA    1 
ATOM   6506  C  C     . LEU A 1 2353 ? 168.276 179.318 149.870 1.00 9.00   ? 2353 LEU A C     1 
ATOM   6507  O  O     . LEU A 1 2353 ? 168.261 180.305 149.103 1.00 11.82  ? 2353 LEU A O     1 
ATOM   6508  C  CB    . LEU A 1 2353 ? 170.459 178.060 149.670 1.00 11.70  ? 2353 LEU A CB    1 
ATOM   6509  C  CG    . LEU A 1 2353 ? 170.695 178.570 148.245 1.00 17.04  ? 2353 LEU A CG    1 
ATOM   6510  C  CD1   . LEU A 1 2353 ? 171.438 179.895 148.257 1.00 16.50  ? 2353 LEU A CD1   1 
ATOM   6511  C  CD2   . LEU A 1 2353 ? 171.437 177.542 147.409 1.00 17.60  ? 2353 LEU A CD2   1 
ATOM   6512  N  N     . ALA A 1 2354 ? 167.212 178.557 150.137 1.00 8.68   ? 2354 ALA A N     1 
ATOM   6513  C  CA    . ALA A 1 2354 ? 165.907 178.811 149.481 1.00 7.95   ? 2354 ALA A CA    1 
ATOM   6514  C  C     . ALA A 1 2354 ? 165.483 180.256 149.740 1.00 7.21   ? 2354 ALA A C     1 
ATOM   6515  O  O     . ALA A 1 2354 ? 164.969 180.910 148.810 1.00 7.89   ? 2354 ALA A O     1 
ATOM   6516  C  CB    . ALA A 1 2354 ? 164.874 177.835 149.995 1.00 10.21  ? 2354 ALA A CB    1 
ATOM   6517  N  N     . THR A 1 2355 ? 165.699 180.739 150.965 1.00 8.11   ? 2355 THR A N     1 
ATOM   6518  C  CA    . THR A 1 2355 ? 165.312 182.119 151.324 1.00 7.54   ? 2355 THR A CA    1 
ATOM   6519  C  C     . THR A 1 2355 ? 166.361 183.080 150.812 1.00 8.48   ? 2355 THR A C     1 
ATOM   6520  O  O     . THR A 1 2355 ? 165.976 184.147 150.288 1.00 8.19   ? 2355 THR A O     1 
ATOM   6521  C  CB    . THR A 1 2355 ? 165.152 182.217 152.840 1.00 7.21   ? 2355 THR A CB    1 
ATOM   6522  O  OG1   . THR A 1 2355 ? 164.083 181.333 153.159 1.00 8.97   ? 2355 THR A OG1   1 
ATOM   6523  C  CG2   . THR A 1 2355 ? 164.820 183.624 153.300 1.00 6.28   ? 2355 THR A CG2   1 
ATOM   6524  N  N     . VAL A 1 2356 ? 167.642 182.725 150.945 1.00 8.54   ? 2356 VAL A N     1 
ATOM   6525  C  CA    . VAL A 1 2356 ? 168.709 183.640 150.551 1.00 7.53   ? 2356 VAL A CA    1 
ATOM   6526  C  C     . VAL A 1 2356 ? 168.611 183.974 149.067 1.00 10.49  ? 2356 VAL A C     1 
ATOM   6527  O  O     . VAL A 1 2356 ? 168.774 185.132 148.663 1.00 12.41  ? 2356 VAL A O     1 
ATOM   6528  C  CB    . VAL A 1 2356 ? 170.080 183.041 150.913 1.00 9.48   ? 2356 VAL A CB    1 
ATOM   6529  C  CG1   . VAL A 1 2356 ? 171.203 183.802 150.226 1.00 10.83  ? 2356 VAL A CG1   1 
ATOM   6530  C  CG2   . VAL A 1 2356 ? 170.272 183.038 152.419 1.00 8.54   ? 2356 VAL A CG2   1 
ATOM   6531  N  N     . SER A 1 2357 ? 168.309 182.960 148.252 1.00 7.50   ? 2357 SER A N     1 
ATOM   6532  C  CA    . SER A 1 2357 ? 168.258 183.148 146.778 1.00 5.42   ? 2357 SER A CA    1 
ATOM   6533  C  C     . SER A 1 2357 ? 167.042 183.979 146.349 1.00 7.92   ? 2357 SER A C     1 
ATOM   6534  O  O     . SER A 1 2357 ? 167.097 184.558 145.245 1.00 10.63  ? 2357 SER A O     1 
ATOM   6535  C  CB    . SER A 1 2357 ? 168.251 181.813 146.088 1.00 9.22   ? 2357 SER A CB    1 
ATOM   6536  O  OG    . SER A 1 2357 ? 167.127 181.043 146.490 1.00 10.87  ? 2357 SER A OG    1 
ATOM   6537  N  N     . ARG A 1 2358 ? 165.994 184.044 147.172 1.00 8.47   ? 2358 ARG A N     1 
ATOM   6538  C  CA    . ARG A 1 2358 ? 164.749 184.737 146.749 1.00 6.66   ? 2358 ARG A CA    1 
ATOM   6539  C  C     . ARG A 1 2358 ? 164.741 186.194 147.230 1.00 11.70  ? 2358 ARG A C     1 
ATOM   6540  O  O     . ARG A 1 2358 ? 163.651 186.807 147.209 1.00 16.36  ? 2358 ARG A O     1 
ATOM   6541  C  CB    . ARG A 1 2358 ? 163.511 184.048 147.334 1.00 9.59   ? 2358 ARG A CB    1 
ATOM   6542  C  CG    . ARG A 1 2358 ? 163.190 182.632 146.884 1.00 6.27   ? 2358 ARG A CG    1 
ATOM   6543  C  CD    . ARG A 1 2358 ? 161.982 182.132 147.664 1.00 7.09   ? 2358 ARG A CD    1 
ATOM   6544  N  NE    . ARG A 1 2358 ? 161.355 180.930 147.103 1.00 7.33   ? 2358 ARG A NE    1 
ATOM   6545  C  CZ    . ARG A 1 2358 ? 161.939 179.748 146.970 1.00 6.06   ? 2358 ARG A CZ    1 
ATOM   6546  N  NH1   . ARG A 1 2358 ? 163.149 179.546 147.457 1.00 8.46   ? 2358 ARG A NH1   1 
ATOM   6547  N  NH2   . ARG A 1 2358 ? 161.305 178.768 146.354 1.00 6.27   ? 2358 ARG A NH2   1 
ATOM   6548  N  N     . CYS A 1 2359 ? 165.889 186.731 147.647 1.00 11.22  ? 2359 CYS A N     1 
ATOM   6549  C  CA    . CYS A 1 2359 ? 165.884 188.103 148.220 1.00 7.74   ? 2359 CYS A CA    1 
ATOM   6550  C  C     . CYS A 1 2359 ? 167.124 188.898 147.799 1.00 10.70  ? 2359 CYS A C     1 
ATOM   6551  O  O     . CYS A 1 2359 ? 168.218 188.296 147.743 1.00 14.28  ? 2359 CYS A O     1 
ATOM   6552  C  CB    . CYS A 1 2359 ? 165.852 188.058 149.743 1.00 8.96   ? 2359 CYS A CB    1 
ATOM   6553  S  SG    . CYS A 1 2359 ? 164.257 187.540 150.429 1.00 22.81  ? 2359 CYS A SG    1 
ATOM   6554  N  N     . GLY A 1 2360 ? 166.957 190.192 147.508 1.00 8.32   ? 2360 GLY A N     1 
ATOM   6555  C  CA    . GLY A 1 2360 ? 168.092 191.049 147.210 1.00 4.19   ? 2360 GLY A CA    1 
ATOM   6556  C  C     . GLY A 1 2360 ? 168.737 191.515 148.500 1.00 4.33   ? 2360 GLY A C     1 
ATOM   6557  O  O     . GLY A 1 2360 ? 168.070 192.074 149.376 1.00 9.74   ? 2360 GLY A O     1 
ATOM   6558  N  N     . MET A 1 2361 ? 170.040 191.289 148.620 1.00 3.64   ? 2361 MET A N     1 
ATOM   6559  C  CA    . MET A 1 2361 ? 170.755 191.523 149.865 1.00 5.15   ? 2361 MET A CA    1 
ATOM   6560  C  C     . MET A 1 2361 ? 171.526 192.833 149.813 1.00 4.13   ? 2361 MET A C     1 
ATOM   6561  O  O     . MET A 1 2361 ? 172.212 193.127 148.830 1.00 5.07   ? 2361 MET A O     1 
ATOM   6562  C  CB    . MET A 1 2361 ? 171.718 190.372 150.162 1.00 6.48   ? 2361 MET A CB    1 
ATOM   6563  C  CG    . MET A 1 2361 ? 171.075 189.005 150.106 1.00 8.31   ? 2361 MET A CG    1 
ATOM   6564  S  SD    . MET A 1 2361 ? 169.916 188.761 151.459 1.00 15.55  ? 2361 MET A SD    1 
ATOM   6565  C  CE    . MET A 1 2361 ? 169.758 186.983 151.443 1.00 8.54   ? 2361 MET A CE    1 
ATOM   6566  N  N     . VAL A 1 2362 ? 171.404 193.619 150.879 1.00 4.21   ? 2362 VAL A N     1 
ATOM   6567  C  CA    . VAL A 1 2362 ? 172.236 194.796 151.093 1.00 4.66   ? 2362 VAL A CA    1 
ATOM   6568  C  C     . VAL A 1 2362 ? 172.992 194.583 152.396 1.00 6.31   ? 2362 VAL A C     1 
ATOM   6569  O  O     . VAL A 1 2362 ? 172.377 194.451 153.461 1.00 8.62   ? 2362 VAL A O     1 
ATOM   6570  C  CB    . VAL A 1 2362 ? 171.408 196.090 151.139 1.00 5.93   ? 2362 VAL A CB    1 
ATOM   6571  C  CG1   . VAL A 1 2362 ? 172.324 197.300 151.114 1.00 5.98   ? 2362 VAL A CG1   1 
ATOM   6572  C  CG2   . VAL A 1 2362 ? 170.434 196.137 149.977 1.00 6.06   ? 2362 VAL A CG2   1 
ATOM   6573  N  N     . TRP A 1 2363 ? 174.319 194.551 152.312 1.00 4.30   ? 2363 TRP A N     1 
ATOM   6574  C  CA    . TRP A 1 2363 ? 175.170 194.228 153.451 1.00 3.82   ? 2363 TRP A CA    1 
ATOM   6575  C  C     . TRP A 1 2363 ? 175.607 195.513 154.141 1.00 5.12   ? 2363 TRP A C     1 
ATOM   6576  O  O     . TRP A 1 2363 ? 176.200 196.392 153.509 1.00 9.15   ? 2363 TRP A O     1 
ATOM   6577  C  CB    . TRP A 1 2363 ? 176.386 193.415 153.011 1.00 4.14   ? 2363 TRP A CB    1 
ATOM   6578  C  CG    . TRP A 1 2363 ? 177.444 193.318 154.063 1.00 4.17   ? 2363 TRP A CG    1 
ATOM   6579  C  CD1   . TRP A 1 2363 ? 178.633 193.982 154.092 1.00 4.13   ? 2363 TRP A CD1   1 
ATOM   6580  C  CD2   . TRP A 1 2363 ? 177.404 192.516 155.248 1.00 4.16   ? 2363 TRP A CD2   1 
ATOM   6581  N  NE1   . TRP A 1 2363 ? 179.339 193.642 155.218 1.00 3.94   ? 2363 TRP A NE1   1 
ATOM   6582  C  CE2   . TRP A 1 2363 ? 178.606 192.743 155.945 1.00 3.22   ? 2363 TRP A CE2   1 
ATOM   6583  C  CE3   . TRP A 1 2363 ? 176.470 191.627 155.786 1.00 4.63   ? 2363 TRP A CE3   1 
ATOM   6584  C  CZ2   . TRP A 1 2363 ? 178.898 192.113 157.151 1.00 2.70   ? 2363 TRP A CZ2   1 
ATOM   6585  C  CZ3   . TRP A 1 2363 ? 176.763 191.003 156.983 1.00 4.17   ? 2363 TRP A CZ3   1 
ATOM   6586  C  CH2   . TRP A 1 2363 ? 177.965 191.249 157.652 1.00 3.68   ? 2363 TRP A CH2   1 
ATOM   6587  N  N     . PHE A 1 2364 ? 175.321 195.614 155.435 1.00 3.11   ? 2364 PHE A N     1 
ATOM   6588  C  CA    . PHE A 1 2364 ? 175.679 196.774 156.246 1.00 3.42   ? 2364 PHE A CA    1 
ATOM   6589  C  C     . PHE A 1 2364 ? 176.785 196.355 157.208 1.00 5.56   ? 2364 PHE A C     1 
ATOM   6590  O  O     . PHE A 1 2364 ? 176.514 195.752 158.248 1.00 6.94   ? 2364 PHE A O     1 
ATOM   6591  C  CB    . PHE A 1 2364 ? 174.472 197.304 157.014 1.00 3.51   ? 2364 PHE A CB    1 
ATOM   6592  C  CG    . PHE A 1 2364 ? 173.437 197.967 156.156 1.00 3.87   ? 2364 PHE A CG    1 
ATOM   6593  C  CD1   . PHE A 1 2364 ? 172.513 197.213 155.454 1.00 4.53   ? 2364 PHE A CD1   1 
ATOM   6594  C  CD2   . PHE A 1 2364 ? 173.366 199.344 156.076 1.00 2.64   ? 2364 PHE A CD2   1 
ATOM   6595  C  CE1   . PHE A 1 2364 ? 171.554 197.821 154.677 1.00 3.19   ? 2364 PHE A CE1   1 
ATOM   6596  C  CE2   . PHE A 1 2364 ? 172.408 199.956 155.300 1.00 2.22   ? 2364 PHE A CE2   1 
ATOM   6597  C  CZ    . PHE A 1 2364 ? 171.502 199.194 154.600 1.00 2.88   ? 2364 PHE A CZ    1 
ATOM   6598  N  N     . SER A 1 2365 ? 178.028 196.679 156.871 1.00 6.00   ? 2365 SER A N     1 
ATOM   6599  C  CA    . SER A 1 2365 ? 179.112 196.440 157.809 1.00 6.21   ? 2365 SER A CA    1 
ATOM   6600  C  C     . SER A 1 2365 ? 179.081 197.481 158.925 1.00 12.86  ? 2365 SER A C     1 
ATOM   6601  O  O     . SER A 1 2365 ? 178.476 198.549 158.799 1.00 12.23  ? 2365 SER A O     1 
ATOM   6602  C  CB    . SER A 1 2365 ? 180.463 196.471 157.096 1.00 8.43   ? 2365 SER A CB    1 
ATOM   6603  O  OG    . SER A 1 2365 ? 180.626 197.673 156.367 1.00 21.41  ? 2365 SER A OG    1 
ATOM   6604  N  N     . GLU A 1 2366 ? 179.742 197.154 160.037 1.00 17.66  ? 2366 GLU A N     1 
ATOM   6605  C  CA    . GLU A 1 2366 ? 179.856 198.112 161.130 1.00 15.87  ? 2366 GLU A CA    1 
ATOM   6606  C  C     . GLU A 1 2366 ? 180.651 199.344 160.727 1.00 19.93  ? 2366 GLU A C     1 
ATOM   6607  O  O     . GLU A 1 2366 ? 180.495 200.401 161.347 1.00 21.16  ? 2366 GLU A O     1 
ATOM   6608  C  CB    . GLU A 1 2366 ? 180.503 197.455 162.349 1.00 15.87  ? 2366 GLU A CB    1 
ATOM   6609  C  CG    . GLU A 1 2366 ? 179.522 196.761 163.277 1.00 25.88  ? 2366 GLU A CG    1 
ATOM   6610  C  CD    . GLU A 1 2366 ? 180.145 196.389 164.609 1.00 37.39  ? 2366 GLU A CD    1 
ATOM   6611  O  OE1   . GLU A 1 2366 ? 180.530 197.308 165.363 1.00 26.84  ? 2366 GLU A OE1   1 
ATOM   6612  O  OE2   . GLU A 1 2366 ? 180.251 195.179 164.900 1.00 31.09  ? 2366 GLU A OE2   1 
ATOM   6613  N  N     . ASP A 1 2367 ? 181.500 199.232 159.707 1.00 21.07  ? 2367 ASP A N     1 
ATOM   6614  C  CA    . ASP A 1 2367 ? 182.248 200.371 159.197 1.00 16.91  ? 2367 ASP A CA    1 
ATOM   6615  C  C     . ASP A 1 2367 ? 181.379 201.348 158.419 1.00 18.58  ? 2367 ASP A C     1 
ATOM   6616  O  O     . ASP A 1 2367 ? 181.799 202.491 158.209 1.00 20.25  ? 2367 ASP A O     1 
ATOM   6617  C  CB    . ASP A 1 2367 ? 183.395 199.882 158.311 1.00 22.79  ? 2367 ASP A CB    1 
ATOM   6618  C  CG    . ASP A 1 2367 ? 184.378 199.011 159.065 1.00 41.53  ? 2367 ASP A CG    1 
ATOM   6619  O  OD1   . ASP A 1 2367 ? 184.315 197.773 158.913 1.00 51.28  ? 2367 ASP A OD1   1 
ATOM   6620  O  OD2   . ASP A 1 2367 ? 185.214 199.564 159.810 1.00 47.67  ? 2367 ASP A OD2   1 
ATOM   6621  N  N     . VAL A 1 2368 ? 180.191 200.925 157.982 1.00 16.28  ? 2368 VAL A N     1 
ATOM   6622  C  CA    . VAL A 1 2368 ? 179.283 201.831 157.282 1.00 12.24  ? 2368 VAL A CA    1 
ATOM   6623  C  C     . VAL A 1 2368 ? 178.858 202.966 158.205 1.00 11.32  ? 2368 VAL A C     1 
ATOM   6624  O  O     . VAL A 1 2368 ? 178.850 204.139 157.816 1.00 13.77  ? 2368 VAL A O     1 
ATOM   6625  C  CB    . VAL A 1 2368 ? 178.069 201.054 156.740 1.00 9.76   ? 2368 VAL A CB    1 
ATOM   6626  C  CG1   . VAL A 1 2368 ? 176.930 201.999 156.414 1.00 10.19  ? 2368 VAL A CG1   1 
ATOM   6627  C  CG2   . VAL A 1 2368 ? 178.462 200.249 155.516 1.00 11.41  ? 2368 VAL A CG2   1 
ATOM   6628  N  N     . LEU A 1 2369 ? 178.509 202.632 159.443 1.00 12.26  ? 2369 LEU A N     1 
ATOM   6629  C  CA    . LEU A 1 2369 ? 178.140 203.616 160.457 1.00 9.29   ? 2369 LEU A CA    1 
ATOM   6630  C  C     . LEU A 1 2369 ? 179.356 203.860 161.342 1.00 8.34   ? 2369 LEU A C     1 
ATOM   6631  O  O     . LEU A 1 2369 ? 179.687 203.041 162.202 1.00 11.36  ? 2369 LEU A O     1 
ATOM   6632  C  CB    . LEU A 1 2369 ? 176.944 203.132 161.270 1.00 7.87   ? 2369 LEU A CB    1 
ATOM   6633  C  CG    . LEU A 1 2369 ? 176.514 204.037 162.423 1.00 10.36  ? 2369 LEU A CG    1 
ATOM   6634  C  CD1   . LEU A 1 2369 ? 175.648 205.171 161.914 1.00 9.77   ? 2369 LEU A CD1   1 
ATOM   6635  C  CD2   . LEU A 1 2369 ? 175.779 203.232 163.479 1.00 5.89   ? 2369 LEU A CD2   1 
ATOM   6636  N  N     . SER A 1 2370 ? 180.022 204.989 161.128 1.00 8.49   ? 2370 SER A N     1 
ATOM   6637  C  CA    . SER A 1 2370 ? 181.192 205.326 161.921 1.00 9.55   ? 2370 SER A CA    1 
ATOM   6638  C  C     . SER A 1 2370 ? 180.778 205.881 163.280 1.00 9.49   ? 2370 SER A C     1 
ATOM   6639  O  O     . SER A 1 2370 ? 179.644 206.322 163.487 1.00 9.85   ? 2370 SER A O     1 
ATOM   6640  C  CB    . SER A 1 2370 ? 182.071 206.337 161.186 1.00 13.01  ? 2370 SER A CB    1 
ATOM   6641  O  OG    . SER A 1 2370 ? 181.346 207.509 160.865 1.00 12.47  ? 2370 SER A OG    1 
ATOM   6642  N  N     . THR A 1 2371 ? 181.725 205.848 164.218 1.00 10.70  ? 2371 THR A N     1 
ATOM   6643  C  CA    . THR A 1 2371 ? 181.464 206.356 165.560 1.00 10.40  ? 2371 THR A CA    1 
ATOM   6644  C  C     . THR A 1 2371 ? 181.248 207.866 165.549 1.00 10.29  ? 2371 THR A C     1 
ATOM   6645  O  O     . THR A 1 2371 ? 180.461 208.389 166.351 1.00 12.92  ? 2371 THR A O     1 
ATOM   6646  C  CB    . THR A 1 2371 ? 182.621 205.975 166.484 1.00 8.67   ? 2371 THR A CB    1 
ATOM   6647  O  OG1   . THR A 1 2371 ? 182.758 204.549 166.508 1.00 13.58  ? 2371 THR A OG1   1 
ATOM   6648  C  CG2   . THR A 1 2371 ? 182.357 206.446 167.890 1.00 12.17  ? 2371 THR A CG2   1 
ATOM   6649  N  N     . ASP A 1 2372 ? 181.926 208.576 164.643 1.00 10.36  ? 2372 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2372 ? 181.709 210.011 164.498 1.00 11.22  ? 2372 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2372 ? 180.261 210.315 164.144 1.00 11.99  ? 2372 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2372 ? 179.702 211.321 164.594 1.00 12.33  ? 2372 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2372 ? 182.645 210.575 163.430 1.00 20.20  ? 2372 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2372 ? 184.095 210.558 163.857 1.00 43.71  ? 2372 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2372 ? 184.359 210.652 165.074 1.00 55.39  ? 2372 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2372 ? 184.972 210.449 162.975 1.00 48.35  ? 2372 ASP A OD2   1 
ATOM   6657  N  N     . MET A 1 2373 ? 179.640 209.460 163.328 1.00 10.76  ? 2373 MET A N     1 
ATOM   6658  C  CA    . MET A 1 2373 ? 178.236 209.643 162.978 1.00 7.42   ? 2373 MET A CA    1 
ATOM   6659  C  C     . MET A 1 2373 ? 177.346 209.552 164.210 1.00 10.03  ? 2373 MET A C     1 
ATOM   6660  O  O     . MET A 1 2373 ? 176.427 210.360 164.386 1.00 13.85  ? 2373 MET A O     1 
ATOM   6661  C  CB    . MET A 1 2373 ? 177.828 208.593 161.947 1.00 9.94   ? 2373 MET A CB    1 
ATOM   6662  C  CG    . MET A 1 2373 ? 178.448 208.785 160.580 1.00 10.22  ? 2373 MET A CG    1 
ATOM   6663  S  SD    . MET A 1 2373 ? 178.063 207.422 159.470 1.00 11.97  ? 2373 MET A SD    1 
ATOM   6664  C  CE    . MET A 1 2373 ? 176.421 207.869 158.939 1.00 6.34   ? 2373 MET A CE    1 
ATOM   6665  N  N     . ILE A 1 2374 ? 177.608 208.571 165.075 1.00 11.03  ? 2374 ILE A N     1 
ATOM   6666  C  CA    . ILE A 1 2374 ? 176.821 208.411 166.294 1.00 7.77   ? 2374 ILE A CA    1 
ATOM   6667  C  C     . ILE A 1 2374 ? 177.024 209.605 167.216 1.00 8.51   ? 2374 ILE A C     1 
ATOM   6668  O  O     . ILE A 1 2374 ? 176.074 210.099 167.838 1.00 10.37  ? 2374 ILE A O     1 
ATOM   6669  C  CB    . ILE A 1 2374 ? 177.183 207.086 166.987 1.00 7.15   ? 2374 ILE A CB    1 
ATOM   6670  C  CG1   . ILE A 1 2374 ? 177.216 205.952 165.964 1.00 8.88   ? 2374 ILE A CG1   1 
ATOM   6671  C  CG2   . ILE A 1 2374 ? 176.189 206.773 168.088 1.00 11.56  ? 2374 ILE A CG2   1 
ATOM   6672  C  CD1   . ILE A 1 2374 ? 177.789 204.665 166.494 1.00 9.06   ? 2374 ILE A CD1   1 
ATOM   6673  N  N     . PHE A 1 2375 ? 178.265 210.085 167.320 1.00 9.13   ? 2375 PHE A N     1 
ATOM   6674  C  CA    . PHE A 1 2375 ? 178.531 211.267 168.135 1.00 9.39   ? 2375 PHE A CA    1 
ATOM   6675  C  C     . PHE A 1 2375 ? 177.793 212.487 167.597 1.00 12.34  ? 2375 PHE A C     1 
ATOM   6676  O  O     . PHE A 1 2375 ? 177.216 213.264 168.368 1.00 15.47  ? 2375 PHE A O     1 
ATOM   6677  C  CB    . PHE A 1 2375 ? 180.033 211.534 168.197 1.00 9.07   ? 2375 PHE A CB    1 
ATOM   6678  C  CG    . PHE A 1 2375 ? 180.797 210.517 168.992 1.00 9.38   ? 2375 PHE A CG    1 
ATOM   6679  C  CD1   . PHE A 1 2375 ? 180.140 209.649 169.845 1.00 10.51  ? 2375 PHE A CD1   1 
ATOM   6680  C  CD2   . PHE A 1 2375 ? 182.174 210.437 168.895 1.00 10.56  ? 2375 PHE A CD2   1 
ATOM   6681  C  CE1   . PHE A 1 2375 ? 180.840 208.718 170.579 1.00 10.58  ? 2375 PHE A CE1   1 
ATOM   6682  C  CE2   . PHE A 1 2375 ? 182.878 209.509 169.629 1.00 12.43  ? 2375 PHE A CE2   1 
ATOM   6683  C  CZ    . PHE A 1 2375 ? 182.210 208.650 170.472 1.00 11.38  ? 2375 PHE A CZ    1 
ATOM   6684  N  N     . ASN A 1 2376 ? 177.803 212.671 166.275 1.00 11.00  ? 2376 ASN A N     1 
ATOM   6685  C  CA    . ASN A 1 2376 ? 177.090 213.793 165.674 1.00 8.29   ? 2376 ASN A CA    1 
ATOM   6686  C  C     . ASN A 1 2376 ? 175.594 213.693 165.929 1.00 9.56   ? 2376 ASN A C     1 
ATOM   6687  O  O     . ASN A 1 2376 ? 174.943 214.697 166.235 1.00 12.66  ? 2376 ASN A O     1 
ATOM   6688  C  CB    . ASN A 1 2376 ? 177.372 213.851 164.173 1.00 7.78   ? 2376 ASN A CB    1 
ATOM   6689  C  CG    . ASN A 1 2376 ? 178.802 214.238 163.863 1.00 11.39  ? 2376 ASN A CG    1 
ATOM   6690  O  OD1   . ASN A 1 2376 ? 179.568 214.594 164.757 1.00 20.64  ? 2376 ASN A OD1   1 
ATOM   6691  N  ND2   . ASN A 1 2376 ? 179.170 214.169 162.591 1.00 9.30   ? 2376 ASN A ND2   1 
ATOM   6692  N  N     . ASN A 1 2377 ? 175.030 212.489 165.799 1.00 9.24   ? 2377 ASN A N     1 
ATOM   6693  C  CA    . ASN A 1 2377 ? 173.606 212.307 166.066 1.00 7.91   ? 2377 ASN A CA    1 
ATOM   6694  C  C     . ASN A 1 2377 ? 173.272 212.641 167.513 1.00 8.45   ? 2377 ASN A C     1 
ATOM   6695  O  O     . ASN A 1 2377 ? 172.289 213.341 167.787 1.00 10.09  ? 2377 ASN A O     1 
ATOM   6696  C  CB    . ASN A 1 2377 ? 173.189 210.874 165.736 1.00 6.56   ? 2377 ASN A CB    1 
ATOM   6697  C  CG    . ASN A 1 2377 ? 171.746 210.586 166.101 1.00 6.60   ? 2377 ASN A CG    1 
ATOM   6698  O  OD1   . ASN A 1 2377 ? 171.465 209.723 166.931 1.00 7.04   ? 2377 ASN A OD1   1 
ATOM   6699  N  ND2   . ASN A 1 2377 ? 170.823 211.308 165.481 1.00 8.99   ? 2377 ASN A ND2   1 
ATOM   6700  N  N     . PHE A 1 2378 ? 174.091 212.160 168.452 1.00 10.14  ? 2378 PHE A N     1 
ATOM   6701  C  CA    . PHE A 1 2378 ? 173.848 212.437 169.864 1.00 7.54   ? 2378 PHE A CA    1 
ATOM   6702  C  C     . PHE A 1 2378 ? 173.923 213.931 170.151 1.00 7.82   ? 2378 PHE A C     1 
ATOM   6703  O  O     . PHE A 1 2378 ? 173.069 214.484 170.853 1.00 8.52   ? 2378 PHE A O     1 
ATOM   6704  C  CB    . PHE A 1 2378 ? 174.852 211.671 170.725 1.00 5.91   ? 2378 PHE A CB    1 
ATOM   6705  C  CG    . PHE A 1 2378 ? 175.013 212.229 172.110 1.00 6.90   ? 2378 PHE A CG    1 
ATOM   6706  C  CD1   . PHE A 1 2378 ? 173.976 212.160 173.024 1.00 8.12   ? 2378 PHE A CD1   1 
ATOM   6707  C  CD2   . PHE A 1 2378 ? 176.202 212.825 172.497 1.00 5.79   ? 2378 PHE A CD2   1 
ATOM   6708  C  CE1   . PHE A 1 2378 ? 174.122 212.673 174.297 1.00 5.94   ? 2378 PHE A CE1   1 
ATOM   6709  C  CE2   . PHE A 1 2378 ? 176.352 213.339 173.768 1.00 5.42   ? 2378 PHE A CE2   1 
ATOM   6710  C  CZ    . PHE A 1 2378 ? 175.310 213.263 174.668 1.00 5.30   ? 2378 PHE A CZ    1 
ATOM   6711  N  N     . LEU A 1 2379 ? 174.939 214.605 169.606 1.00 7.86   ? 2379 LEU A N     1 
ATOM   6712  C  CA    . LEU A 1 2379 ? 175.095 216.033 169.864 1.00 7.84   ? 2379 LEU A CA    1 
ATOM   6713  C  C     . LEU A 1 2379 ? 173.967 216.842 169.233 1.00 9.85   ? 2379 LEU A C     1 
ATOM   6714  O  O     . LEU A 1 2379 ? 173.480 217.806 169.834 1.00 12.82  ? 2379 LEU A O     1 
ATOM   6715  C  CB    . LEU A 1 2379 ? 176.456 216.509 169.360 1.00 9.38   ? 2379 LEU A CB    1 
ATOM   6716  C  CG    . LEU A 1 2379 ? 177.651 215.997 170.168 1.00 8.29   ? 2379 LEU A CG    1 
ATOM   6717  C  CD1   . LEU A 1 2379 ? 178.959 216.374 169.500 1.00 10.73  ? 2379 LEU A CD1   1 
ATOM   6718  C  CD2   . LEU A 1 2379 ? 177.602 216.522 171.593 1.00 8.54   ? 2379 LEU A CD2   1 
ATOM   6719  N  N     . ALA A 1 2380 ? 173.537 216.467 168.025 1.00 8.15   ? 2380 ALA A N     1 
ATOM   6720  C  CA    . ALA A 1 2380 ? 172.427 217.167 167.388 1.00 8.87   ? 2380 ALA A CA    1 
ATOM   6721  C  C     . ALA A 1 2380 ? 171.138 216.991 168.178 1.00 10.72  ? 2380 ALA A C     1 
ATOM   6722  O  O     . ALA A 1 2380 ? 170.384 217.952 168.373 1.00 14.58  ? 2380 ALA A O     1 
ATOM   6723  C  CB    . ALA A 1 2380 ? 172.250 216.673 165.953 1.00 8.40   ? 2380 ALA A CB    1 
ATOM   6724  N  N     . ARG A 1 2381 ? 170.870 215.769 168.648 1.00 9.89   ? 2381 ARG A N     1 
ATOM   6725  C  CA    . ARG A 1 2381 ? 169.682 215.541 169.463 1.00 10.52  ? 2381 ARG A CA    1 
ATOM   6726  C  C     . ARG A 1 2381 ? 169.754 216.322 170.769 1.00 12.90  ? 2381 ARG A C     1 
ATOM   6727  O  O     . ARG A 1 2381 ? 168.746 216.868 171.231 1.00 15.93  ? 2381 ARG A O     1 
ATOM   6728  C  CB    . ARG A 1 2381 ? 169.512 214.049 169.737 1.00 11.07  ? 2381 ARG A CB    1 
ATOM   6729  C  CG    . ARG A 1 2381 ? 169.177 213.229 168.507 1.00 10.79  ? 2381 ARG A CG    1 
ATOM   6730  C  CD    . ARG A 1 2381 ? 169.039 211.757 168.848 1.00 12.98  ? 2381 ARG A CD    1 
ATOM   6731  N  NE    . ARG A 1 2381 ? 168.005 211.529 169.848 1.00 18.63  ? 2381 ARG A NE    1 
ATOM   6732  C  CZ    . ARG A 1 2381 ? 166.705 211.498 169.587 1.00 19.36  ? 2381 ARG A CZ    1 
ATOM   6733  N  NH1   . ARG A 1 2381 ? 166.243 211.671 168.361 1.00 15.06  ? 2381 ARG A NH1   1 
ATOM   6734  N  NH2   . ARG A 1 2381 ? 165.849 211.289 170.582 1.00 27.56  ? 2381 ARG A NH2   1 
ATOM   6735  N  N     . LEU A 1 2382 ? 170.939 216.381 171.382 1.00 11.69  ? 2382 LEU A N     1 
ATOM   6736  C  CA    . LEU A 1 2382 ? 171.099 217.141 172.617 1.00 11.74  ? 2382 LEU A CA    1 
ATOM   6737  C  C     . LEU A 1 2382 ? 170.855 218.627 172.391 1.00 14.01  ? 2382 LEU A C     1 
ATOM   6738  O  O     . LEU A 1 2382 ? 170.211 219.290 173.211 1.00 16.76  ? 2382 LEU A O     1 
ATOM   6739  C  CB    . LEU A 1 2382 ? 172.495 216.906 173.195 1.00 11.48  ? 2382 LEU A CB    1 
ATOM   6740  C  CG    . LEU A 1 2382 ? 172.752 217.396 174.620 1.00 11.60  ? 2382 LEU A CG    1 
ATOM   6741  C  CD1   . LEU A 1 2382 ? 171.894 216.633 175.613 1.00 13.13  ? 2382 LEU A CD1   1 
ATOM   6742  C  CD2   . LEU A 1 2382 ? 174.223 217.256 174.963 1.00 12.07  ? 2382 LEU A CD2   1 
ATOM   6743  N  N     . ARG A 1 2383 ? 171.364 219.169 171.282 1.00 13.19  ? 2383 ARG A N     1 
ATOM   6744  C  CA    . ARG A 1 2383 ? 171.199 220.591 171.005 1.00 13.80  ? 2383 ARG A CA    1 
ATOM   6745  C  C     . ARG A 1 2383 ? 169.793 220.943 170.541 1.00 14.72  ? 2383 ARG A C     1 
ATOM   6746  O  O     . ARG A 1 2383 ? 169.387 222.102 170.673 1.00 15.56  ? 2383 ARG A O     1 
ATOM   6747  C  CB    . ARG A 1 2383 ? 172.212 221.047 169.956 1.00 10.97  ? 2383 ARG A CB    1 
ATOM   6748  C  CG    . ARG A 1 2383 ? 173.633 221.148 170.468 1.00 12.50  ? 2383 ARG A CG    1 
ATOM   6749  C  CD    . ARG A 1 2383 ? 174.594 221.468 169.342 1.00 12.61  ? 2383 ARG A CD    1 
ATOM   6750  N  NE    . ARG A 1 2383 ? 175.910 221.850 169.838 1.00 17.57  ? 2383 ARG A NE    1 
ATOM   6751  C  CZ    . ARG A 1 2383 ? 177.040 221.243 169.505 1.00 19.95  ? 2383 ARG A CZ    1 
ATOM   6752  N  NH1   . ARG A 1 2383 ? 177.051 220.203 168.689 1.00 11.91  ? 2383 ARG A NH1   1 
ATOM   6753  N  NH2   . ARG A 1 2383 ? 178.188 221.690 170.005 1.00 19.36  ? 2383 ARG A NH2   1 
ATOM   6754  N  N     . SER A 1 2384 ? 169.043 219.985 169.998 1.00 15.61  ? 2384 SER A N     1 
ATOM   6755  C  CA    . SER A 1 2384 ? 167.726 220.277 169.443 1.00 16.56  ? 2384 SER A CA    1 
ATOM   6756  C  C     . SER A 1 2384 ? 166.581 219.846 170.352 1.00 19.62  ? 2384 SER A C     1 
ATOM   6757  O  O     . SER A 1 2384 ? 165.645 220.620 170.574 1.00 21.76  ? 2384 SER A O     1 
ATOM   6758  C  CB    . SER A 1 2384 ? 167.580 219.608 168.073 1.00 17.80  ? 2384 SER A CB    1 
ATOM   6759  O  OG    . SER A 1 2384 ? 166.495 220.161 167.348 1.00 24.31  ? 2384 SER A OG    1 
ATOM   6760  N  N     . ILE A 1 2385 ? 166.630 218.630 170.881 1.00 18.57  ? 2385 ILE A N     1 
ATOM   6761  C  CA    . ILE A 1 2385 ? 165.512 218.046 171.615 1.00 18.63  ? 2385 ILE A CA    1 
ATOM   6762  C  C     . ILE A 1 2385 ? 165.678 218.386 173.093 1.00 22.77  ? 2385 ILE A C     1 
ATOM   6763  O  O     . ILE A 1 2385 ? 166.701 218.012 173.689 1.00 26.64  ? 2385 ILE A O     1 
ATOM   6764  C  CB    . ILE A 1 2385 ? 165.439 216.530 171.409 1.00 15.45  ? 2385 ILE A CB    1 
ATOM   6765  C  CG1   . ILE A 1 2385 ? 165.299 216.204 169.921 1.00 20.14  ? 2385 ILE A CG1   1 
ATOM   6766  C  CG2   . ILE A 1 2385 ? 164.283 215.945 172.198 1.00 15.55  ? 2385 ILE A CG2   1 
ATOM   6767  C  CD1   . ILE A 1 2385 ? 165.208 214.726 169.627 1.00 20.24  ? 2385 ILE A CD1   1 
ATOM   6768  N  N     . PRO A 1 2386 ? 164.726 219.082 173.711 1.00 21.99  ? 2386 PRO A N     1 
ATOM   6769  C  CA    . PRO A 1 2386 ? 164.794 219.296 175.160 1.00 23.12  ? 2386 PRO A CA    1 
ATOM   6770  C  C     . PRO A 1 2386 ? 164.605 217.993 175.922 1.00 23.51  ? 2386 PRO A C     1 
ATOM   6771  O  O     . PRO A 1 2386 ? 163.902 217.082 175.480 1.00 27.92  ? 2386 PRO A O     1 
ATOM   6772  C  CB    . PRO A 1 2386 ? 163.642 220.273 175.435 1.00 24.45  ? 2386 PRO A CB    1 
ATOM   6773  C  CG    . PRO A 1 2386 ? 163.218 220.789 174.094 1.00 22.32  ? 2386 PRO A CG    1 
ATOM   6774  C  CD    . PRO A 1 2386 ? 163.544 219.718 173.112 1.00 22.43  ? 2386 PRO A CD    1 
ATOM   6775  N  N     . LEU A 1 2387 ? 165.245 217.916 177.089 1.00 22.19  ? 2387 LEU A N     1 
ATOM   6776  C  CA    . LEU A 1 2387 ? 165.173 216.698 177.888 1.00 22.82  ? 2387 LEU A CA    1 
ATOM   6777  C  C     . LEU A 1 2387 ? 163.925 216.666 178.763 1.00 30.86  ? 2387 LEU A C     1 
ATOM   6778  O  O     . LEU A 1 2387 ? 163.385 215.589 179.037 1.00 32.86  ? 2387 LEU A O     1 
ATOM   6779  C  CB    . LEU A 1 2387 ? 166.430 216.560 178.745 1.00 17.83  ? 2387 LEU A CB    1 
ATOM   6780  C  CG    . LEU A 1 2387 ? 167.653 215.981 178.032 1.00 13.51  ? 2387 LEU A CG    1 
ATOM   6781  C  CD1   . LEU A 1 2387 ? 168.830 215.881 178.981 1.00 16.89  ? 2387 LEU A CD1   1 
ATOM   6782  C  CD2   . LEU A 1 2387 ? 167.329 214.626 177.428 1.00 12.95  ? 2387 LEU A CD2   1 
ATOM   6783  N  N     . ASP A 1 2388 ? 163.459 217.831 179.218 1.00 35.13  ? 2388 ASP A N     1 
ATOM   6784  C  CA    . ASP A 1 2388 ? 162.283 217.869 180.082 1.00 33.93  ? 2388 ASP A CA    1 
ATOM   6785  C  C     . ASP A 1 2388 ? 161.018 217.487 179.323 1.00 42.54  ? 2388 ASP A C     1 
ATOM   6786  O  O     . ASP A 1 2388 ? 160.131 216.828 179.878 1.00 50.50  ? 2388 ASP A O     1 
ATOM   6787  C  CB    . ASP A 1 2388 ? 162.139 219.253 180.712 1.00 31.28  ? 2388 ASP A CB    1 
ATOM   6788  C  CG    . ASP A 1 2388 ? 162.314 220.371 179.708 1.00 41.26  ? 2388 ASP A CG    1 
ATOM   6789  O  OD1   . ASP A 1 2388 ? 162.659 220.077 178.545 1.00 44.65  ? 2388 ASP A OD1   1 
ATOM   6790  O  OD2   . ASP A 1 2388 ? 162.106 221.543 180.081 1.00 54.37  ? 2388 ASP A OD2   1 
ATOM   6791  N  N     . GLU A 1 2389 ? 160.912 217.891 178.062 1.00 43.17  ? 2389 GLU A N     1 
ATOM   6792  C  CA    . GLU A 1 2389 ? 159.743 217.564 177.253 1.00 44.05  ? 2389 GLU A CA    1 
ATOM   6793  C  C     . GLU A 1 2389 ? 160.102 217.521 175.773 1.00 38.71  ? 2389 GLU A C     1 
ATOM   6794  O  O     . GLU A 1 2389 ? 160.946 218.285 175.306 0.00 37.62  ? 2389 GLU A O     1 
ATOM   6795  C  CB    . GLU A 1 2389 ? 158.621 218.578 177.493 1.00 53.65  ? 2389 GLU A CB    1 
ATOM   6796  C  CG    . GLU A 1 2389 ? 157.337 218.295 176.725 1.00 61.76  ? 2389 GLU A CG    1 
ATOM   6797  C  CD    . GLU A 1 2389 ? 156.653 217.012 177.163 1.00 66.19  ? 2389 GLU A CD    1 
ATOM   6798  O  OE1   . GLU A 1 2389 ? 156.848 216.596 178.325 1.00 65.94  ? 2389 GLU A OE1   1 
ATOM   6799  O  OE2   . GLU A 1 2389 ? 155.918 216.421 176.344 1.00 63.27  ? 2389 GLU A OE2   1 
ATOM   6800  N  N     . SER A 1 2410 ? 163.623 227.827 176.246 1.00 37.26  ? 2410 SER A N     1 
ATOM   6801  C  CA    . SER A 1 2410 ? 163.636 226.866 177.342 1.00 34.97  ? 2410 SER A CA    1 
ATOM   6802  C  C     . SER A 1 2410 ? 165.009 226.804 177.999 1.00 30.94  ? 2410 SER A C     1 
ATOM   6803  O  O     . SER A 1 2410 ? 166.010 226.565 177.325 1.00 31.91  ? 2410 SER A O     1 
ATOM   6804  C  CB    . SER A 1 2410 ? 163.230 225.479 176.844 1.00 28.57  ? 2410 SER A CB    1 
ATOM   6805  O  OG    . SER A 1 2410 ? 163.294 224.524 177.889 1.00 35.73  ? 2410 SER A OG    1 
ATOM   6806  N  N     . PRO A 1 2411 ? 165.056 227.032 179.314 1.00 33.29  ? 2411 PRO A N     1 
ATOM   6807  C  CA    . PRO A 1 2411 ? 166.342 226.937 180.026 1.00 33.60  ? 2411 PRO A CA    1 
ATOM   6808  C  C     . PRO A 1 2411 ? 166.974 225.561 179.944 1.00 30.59  ? 2411 PRO A C     1 
ATOM   6809  O  O     . PRO A 1 2411 ? 168.207 225.453 179.912 1.00 34.83  ? 2411 PRO A O     1 
ATOM   6810  C  CB    . PRO A 1 2411 ? 165.970 227.306 181.469 1.00 32.35  ? 2411 PRO A CB    1 
ATOM   6811  C  CG    . PRO A 1 2411 ? 164.505 227.029 181.569 1.00 27.47  ? 2411 PRO A CG    1 
ATOM   6812  C  CD    . PRO A 1 2411 ? 163.939 227.344 180.222 1.00 31.52  ? 2411 PRO A CD    1 
ATOM   6813  N  N     . MET A 1 2412 ? 166.162 224.501 179.910 1.00 24.83  ? 2412 MET A N     1 
ATOM   6814  C  CA    . MET A 1 2412 ? 166.707 223.154 179.779 1.00 25.94  ? 2412 MET A CA    1 
ATOM   6815  C  C     . MET A 1 2412 ? 167.443 222.989 178.456 1.00 26.19  ? 2412 MET A C     1 
ATOM   6816  O  O     . MET A 1 2412 ? 168.526 222.394 178.408 1.00 26.16  ? 2412 MET A O     1 
ATOM   6817  C  CB    . MET A 1 2412 ? 165.585 222.123 179.902 1.00 28.39  ? 2412 MET A CB    1 
ATOM   6818  C  CG    . MET A 1 2412 ? 166.068 220.686 179.938 1.00 29.62  ? 2412 MET A CG    1 
ATOM   6819  S  SD    . MET A 1 2412 ? 167.026 220.352 181.425 1.00 39.85  ? 2412 MET A SD    1 
ATOM   6820  C  CE    . MET A 1 2412 ? 168.017 218.960 180.899 1.00 25.50  ? 2412 MET A CE    1 
ATOM   6821  N  N     . LEU A 1 2413 ? 166.869 223.514 177.371 1.00 27.03  ? 2413 LEU A N     1 
ATOM   6822  C  CA    . LEU A 1 2413 ? 167.534 223.444 176.075 1.00 21.47  ? 2413 LEU A CA    1 
ATOM   6823  C  C     . LEU A 1 2413 ? 168.825 224.251 176.075 1.00 22.32  ? 2413 LEU A C     1 
ATOM   6824  O  O     . LEU A 1 2413 ? 169.814 223.846 175.456 1.00 29.49  ? 2413 LEU A O     1 
ATOM   6825  C  CB    . LEU A 1 2413 ? 166.592 223.928 174.974 1.00 26.65  ? 2413 LEU A CB    1 
ATOM   6826  C  CG    . LEU A 1 2413 ? 166.917 223.467 173.552 1.00 23.52  ? 2413 LEU A CG    1 
ATOM   6827  C  CD1   . LEU A 1 2413 ? 167.034 221.956 173.497 1.00 21.79  ? 2413 LEU A CD1   1 
ATOM   6828  C  CD2   . LEU A 1 2413 ? 165.864 223.958 172.575 1.00 20.67  ? 2413 LEU A CD2   1 
ATOM   6829  N  N     . GLN A 1 2414 ? 168.835 225.398 176.759 1.00 25.79  ? 2414 GLN A N     1 
ATOM   6830  C  CA    . GLN A 1 2414 ? 170.063 226.181 176.868 1.00 28.78  ? 2414 GLN A CA    1 
ATOM   6831  C  C     . GLN A 1 2414 ? 171.144 225.410 177.616 1.00 28.42  ? 2414 GLN A C     1 
ATOM   6832  O  O     . GLN A 1 2414 ? 172.315 225.416 177.213 1.00 24.02  ? 2414 GLN A O     1 
ATOM   6833  C  CB    . GLN A 1 2414 ? 169.776 227.512 177.561 1.00 23.85  ? 2414 GLN A CB    1 
ATOM   6834  C  CG    . GLN A 1 2414 ? 170.953 228.473 177.572 1.00 25.57  ? 2414 GLN A CG    1 
ATOM   6835  C  CD    . GLN A 1 2414 ? 171.518 228.717 176.188 1.00 32.50  ? 2414 GLN A CD    1 
ATOM   6836  O  OE1   . GLN A 1 2414 ? 170.778 228.984 175.242 1.00 33.46  ? 2414 GLN A OE1   1 
ATOM   6837  N  NE2   . GLN A 1 2414 ? 172.836 228.629 176.063 1.00 37.02  ? 2414 GLN A NE2   1 
ATOM   6838  N  N     . ILE A 1 2415 ? 170.771 224.742 178.709 1.00 27.03  ? 2415 ILE A N     1 
ATOM   6839  C  CA    . ILE A 1 2415 ? 171.736 223.936 179.453 1.00 25.20  ? 2415 ILE A CA    1 
ATOM   6840  C  C     . ILE A 1 2415 ? 172.263 222.805 178.581 1.00 24.25  ? 2415 ILE A C     1 
ATOM   6841  O  O     . ILE A 1 2415 ? 173.466 222.512 178.576 1.00 25.84  ? 2415 ILE A O     1 
ATOM   6842  C  CB    . ILE A 1 2415 ? 171.102 223.402 180.751 1.00 26.87  ? 2415 ILE A CB    1 
ATOM   6843  C  CG1   . ILE A 1 2415 ? 170.831 224.548 181.725 1.00 22.55  ? 2415 ILE A CG1   1 
ATOM   6844  C  CG2   . ILE A 1 2415 ? 172.000 222.358 181.395 1.00 22.41  ? 2415 ILE A CG2   1 
ATOM   6845  C  CD1   . ILE A 1 2415 ? 169.949 224.159 182.886 1.00 20.21  ? 2415 ILE A CD1   1 
ATOM   6846  N  N     . GLN A 1 2416 ? 171.371 222.151 177.833 1.00 23.62  ? 2416 GLN A N     1 
ATOM   6847  C  CA    . GLN A 1 2416 ? 171.795 221.073 176.946 1.00 18.10  ? 2416 GLN A CA    1 
ATOM   6848  C  C     . GLN A 1 2416 ? 172.760 221.580 175.882 1.00 22.20  ? 2416 GLN A C     1 
ATOM   6849  O  O     . GLN A 1 2416 ? 173.762 220.924 175.582 1.00 24.88  ? 2416 GLN A O     1 
ATOM   6850  C  CB    . GLN A 1 2416 ? 170.576 220.422 176.295 1.00 18.47  ? 2416 GLN A CB    1 
ATOM   6851  C  CG    . GLN A 1 2416 ? 169.755 219.560 177.231 1.00 16.39  ? 2416 GLN A CG    1 
ATOM   6852  C  CD    . GLN A 1 2416 ? 168.418 219.173 176.635 1.00 18.62  ? 2416 GLN A CD    1 
ATOM   6853  O  OE1   . GLN A 1 2416 ? 167.380 219.292 177.282 1.00 22.47  ? 2416 GLN A OE1   1 
ATOM   6854  N  NE2   . GLN A 1 2416 ? 168.437 218.708 175.393 1.00 18.26  ? 2416 GLN A NE2   1 
ATOM   6855  N  N     . ARG A 1 2417 ? 172.470 222.744 175.296 1.00 26.26  ? 2417 ARG A N     1 
ATOM   6856  C  CA    . ARG A 1 2417 ? 173.347 223.301 174.269 1.00 19.17  ? 2417 ARG A CA    1 
ATOM   6857  C  C     . ARG A 1 2417 ? 174.710 223.667 174.842 1.00 19.41  ? 2417 ARG A C     1 
ATOM   6858  O  O     . ARG A 1 2417 ? 175.744 223.417 174.210 1.00 23.97  ? 2417 ARG A O     1 
ATOM   6859  C  CB    . ARG A 1 2417 ? 172.690 224.520 173.624 1.00 17.06  ? 2417 ARG A CB    1 
ATOM   6860  C  CG    . ARG A 1 2417 ? 171.520 224.180 172.720 1.00 14.03  ? 2417 ARG A CG    1 
ATOM   6861  C  CD    . ARG A 1 2417 ? 171.084 225.382 171.908 1.00 16.97  ? 2417 ARG A CD    1 
ATOM   6862  N  NE    . ARG A 1 2417 ? 170.071 225.029 170.922 1.00 19.48  ? 2417 ARG A NE    1 
ATOM   6863  C  CZ    . ARG A 1 2417 ? 168.828 225.491 170.926 1.00 23.12  ? 2417 ARG A CZ    1 
ATOM   6864  N  NH1   . ARG A 1 2417 ? 168.406 226.330 171.857 1.00 18.68  ? 2417 ARG A NH1   1 
ATOM   6865  N  NH2   . ARG A 1 2417 ? 167.988 225.101 169.972 1.00 23.64  ? 2417 ARG A NH2   1 
ATOM   6866  N  N     . ASP A 1 2418 ? 174.733 224.264 176.036 1.00 21.66  ? 2418 ASP A N     1 
ATOM   6867  C  CA    . ASP A 1 2418 ? 176.007 224.587 176.669 1.00 19.51  ? 2418 ASP A CA    1 
ATOM   6868  C  C     . ASP A 1 2418 ? 176.810 223.327 176.964 1.00 20.79  ? 2418 ASP A C     1 
ATOM   6869  O  O     . ASP A 1 2418 ? 178.023 223.282 176.724 1.00 20.31  ? 2418 ASP A O     1 
ATOM   6870  C  CB    . ASP A 1 2418 ? 175.770 225.387 177.949 1.00 25.90  ? 2418 ASP A CB    1 
ATOM   6871  C  CG    . ASP A 1 2418 ? 175.291 226.797 177.675 1.00 37.71  ? 2418 ASP A CG    1 
ATOM   6872  O  OD1   . ASP A 1 2418 ? 174.685 227.024 176.608 1.00 39.16  ? 2418 ASP A OD1   1 
ATOM   6873  O  OD2   . ASP A 1 2418 ? 175.522 227.680 178.526 1.00 40.92  ? 2418 ASP A OD2   1 
ATOM   6874  N  N     . ALA A 1 2419 ? 176.148 222.287 177.476 1.00 21.38  ? 2419 ALA A N     1 
ATOM   6875  C  CA    . ALA A 1 2419 ? 176.841 221.035 177.758 1.00 16.34  ? 2419 ALA A CA    1 
ATOM   6876  C  C     . ALA A 1 2419 ? 177.372 220.398 176.481 1.00 18.74  ? 2419 ALA A C     1 
ATOM   6877  O  O     . ALA A 1 2419 ? 178.476 219.843 176.469 1.00 18.14  ? 2419 ALA A O     1 
ATOM   6878  C  CB    . ALA A 1 2419 ? 175.911 220.072 178.494 1.00 19.43  ? 2419 ALA A CB    1 
ATOM   6879  N  N     . ALA A 1 2420 ? 176.592 220.457 175.398 1.00 20.45  ? 2420 ALA A N     1 
ATOM   6880  C  CA    . ALA A 1 2420 ? 177.051 219.923 174.120 1.00 16.14  ? 2420 ALA A CA    1 
ATOM   6881  C  C     . ALA A 1 2420 ? 178.267 220.684 173.614 1.00 18.33  ? 2420 ALA A C     1 
ATOM   6882  O  O     . ALA A 1 2420 ? 179.218 220.081 173.102 1.00 22.46  ? 2420 ALA A O     1 
ATOM   6883  C  CB    . ALA A 1 2420 ? 175.921 219.973 173.094 1.00 13.72  ? 2420 ALA A CB    1 
ATOM   6884  N  N     . THR A 1 2421 ? 178.256 222.011 173.750 1.00 18.65  ? 2421 THR A N     1 
ATOM   6885  C  CA    . THR A 1 2421 ? 179.421 222.802 173.368 1.00 18.59  ? 2421 THR A CA    1 
ATOM   6886  C  C     . THR A 1 2421 ? 180.640 222.427 174.199 1.00 18.34  ? 2421 THR A C     1 
ATOM   6887  O  O     . THR A 1 2421 ? 181.758 222.370 173.674 1.00 18.31  ? 2421 THR A O     1 
ATOM   6888  C  CB    . THR A 1 2421 ? 179.118 224.293 173.516 1.00 23.75  ? 2421 THR A CB    1 
ATOM   6889  O  OG1   . THR A 1 2421 ? 177.917 224.613 172.803 1.00 24.34  ? 2421 THR A OG1   1 
ATOM   6890  C  CG2   . THR A 1 2421 ? 180.263 225.128 172.965 1.00 27.23  ? 2421 THR A CG2   1 
ATOM   6891  N  N     . ILE A 1 2422 ? 180.444 222.169 175.493 1.00 21.40  ? 2422 ILE A N     1 
ATOM   6892  C  CA    . ILE A 1 2422 ? 181.566 221.806 176.354 1.00 18.98  ? 2422 ILE A CA    1 
ATOM   6893  C  C     . ILE A 1 2422 ? 182.117 220.433 175.985 1.00 18.72  ? 2422 ILE A C     1 
ATOM   6894  O  O     . ILE A 1 2422 ? 183.336 220.228 175.958 1.00 18.44  ? 2422 ILE A O     1 
ATOM   6895  C  CB    . ILE A 1 2422 ? 181.143 221.873 177.832 1.00 19.34  ? 2422 ILE A CB    1 
ATOM   6896  C  CG1   . ILE A 1 2422 ? 180.762 223.304 178.205 1.00 19.47  ? 2422 ILE A CG1   1 
ATOM   6897  C  CG2   . ILE A 1 2422 ? 182.260 221.374 178.735 1.00 23.82  ? 2422 ILE A CG2   1 
ATOM   6898  C  CD1   . ILE A 1 2422 ? 180.093 223.422 179.546 1.00 21.36  ? 2422 ILE A CD1   1 
ATOM   6899  N  N     . MET A 1 2423 ? 181.238 219.470 175.697 1.00 18.63  ? 2423 MET A N     1 
ATOM   6900  C  CA    . MET A 1 2423 ? 181.692 218.106 175.446 1.00 19.80  ? 2423 MET A CA    1 
ATOM   6901  C  C     . MET A 1 2423 ? 182.017 217.836 173.982 1.00 19.60  ? 2423 MET A C     1 
ATOM   6902  O  O     . MET A 1 2423 ? 182.431 216.718 173.659 1.00 21.49  ? 2423 MET A O     1 
ATOM   6903  C  CB    . MET A 1 2423 ? 180.650 217.088 175.925 1.00 16.26  ? 2423 MET A CB    1 
ATOM   6904  C  CG    . MET A 1 2423 ? 179.325 217.131 175.186 1.00 19.77  ? 2423 MET A CG    1 
ATOM   6905  S  SD    . MET A 1 2423 ? 178.116 215.978 175.866 1.00 24.96  ? 2423 MET A SD    1 
ATOM   6906  C  CE    . MET A 1 2423 ? 177.671 216.794 177.394 1.00 14.83  ? 2423 MET A CE    1 
ATOM   6907  N  N     . GLN A 1 2424 ? 181.828 218.813 173.096 1.00 18.13  ? 2424 GLN A N     1 
ATOM   6908  C  CA    . GLN A 1 2424 ? 182.197 218.642 171.691 1.00 16.66  ? 2424 GLN A CA    1 
ATOM   6909  C  C     . GLN A 1 2424 ? 183.651 218.233 171.470 1.00 19.61  ? 2424 GLN A C     1 
ATOM   6910  O  O     . GLN A 1 2424 ? 183.889 217.322 170.660 1.00 18.43  ? 2424 GLN A O     1 
ATOM   6911  C  CB    . GLN A 1 2424 ? 181.869 219.935 170.930 1.00 17.09  ? 2424 GLN A CB    1 
ATOM   6912  C  CG    . GLN A 1 2424 ? 182.336 219.943 169.486 1.00 19.84  ? 2424 GLN A CG    1 
ATOM   6913  C  CD    . GLN A 1 2424 ? 181.612 218.921 168.636 1.00 20.06  ? 2424 GLN A CD    1 
ATOM   6914  O  OE1   . GLN A 1 2424 ? 180.424 219.064 168.351 1.00 19.85  ? 2424 GLN A OE1   1 
ATOM   6915  N  NE2   . GLN A 1 2424 ? 182.325 217.879 168.229 1.00 19.95  ? 2424 GLN A NE2   1 
ATOM   6916  N  N     . PRO A 1 2425 ? 184.655 218.839 172.121 1.00 19.14  ? 2425 PRO A N     1 
ATOM   6917  C  CA    . PRO A 1 2425 ? 186.044 218.447 171.822 1.00 16.76  ? 2425 PRO A CA    1 
ATOM   6918  C  C     . PRO A 1 2425 ? 186.358 216.989 172.112 1.00 16.99  ? 2425 PRO A C     1 
ATOM   6919  O  O     . PRO A 1 2425 ? 187.287 216.438 171.508 1.00 17.45  ? 2425 PRO A O     1 
ATOM   6920  C  CB    . PRO A 1 2425 ? 186.871 219.381 172.717 1.00 13.20  ? 2425 PRO A CB    1 
ATOM   6921  C  CG    . PRO A 1 2425 ? 185.999 220.546 172.949 1.00 17.61  ? 2425 PRO A CG    1 
ATOM   6922  C  CD    . PRO A 1 2425 ? 184.612 219.998 173.031 1.00 16.77  ? 2425 PRO A CD    1 
ATOM   6923  N  N     . TYR A 1 2426 ? 185.627 216.348 173.019 1.00 18.82  ? 2426 TYR A N     1 
ATOM   6924  C  CA    . TYR A 1 2426 ? 185.904 214.965 173.381 1.00 18.10  ? 2426 TYR A CA    1 
ATOM   6925  C  C     . TYR A 1 2426 ? 185.172 213.953 172.510 1.00 18.30  ? 2426 TYR A C     1 
ATOM   6926  O  O     . TYR A 1 2426 ? 185.481 212.760 172.585 1.00 20.18  ? 2426 TYR A O     1 
ATOM   6927  C  CB    . TYR A 1 2426 ? 185.543 214.725 174.849 1.00 16.40  ? 2426 TYR A CB    1 
ATOM   6928  C  CG    . TYR A 1 2426 ? 186.163 215.728 175.790 1.00 16.85  ? 2426 TYR A CG    1 
ATOM   6929  C  CD1   . TYR A 1 2426 ? 187.496 215.625 176.163 1.00 13.09  ? 2426 TYR A CD1   1 
ATOM   6930  C  CD2   . TYR A 1 2426 ? 185.421 216.784 176.299 1.00 15.54  ? 2426 TYR A CD2   1 
ATOM   6931  C  CE1   . TYR A 1 2426 ? 188.069 216.542 177.019 1.00 16.11  ? 2426 TYR A CE1   1 
ATOM   6932  C  CE2   . TYR A 1 2426 ? 185.986 217.705 177.157 1.00 16.95  ? 2426 TYR A CE2   1 
ATOM   6933  C  CZ    . TYR A 1 2426 ? 187.309 217.579 177.513 1.00 18.74  ? 2426 TYR A CZ    1 
ATOM   6934  O  OH    . TYR A 1 2426 ? 187.878 218.493 178.367 1.00 30.86  ? 2426 TYR A OH    1 
ATOM   6935  N  N     . PHE A 1 2427 ? 184.224 214.395 171.683 1.00 18.81  ? 2427 PHE A N     1 
ATOM   6936  C  CA    . PHE A 1 2427 ? 183.440 213.507 170.836 1.00 13.20  ? 2427 PHE A CA    1 
ATOM   6937  C  C     . PHE A 1 2427 ? 183.863 213.579 169.374 1.00 18.84  ? 2427 PHE A C     1 
ATOM   6938  O  O     . PHE A 1 2427 ? 183.022 213.468 168.476 1.00 25.77  ? 2427 PHE A O     1 
ATOM   6939  C  CB    . PHE A 1 2427 ? 181.953 213.823 170.976 1.00 12.81  ? 2427 PHE A CB    1 
ATOM   6940  C  CG    . PHE A 1 2427 ? 181.313 213.207 172.184 1.00 13.33  ? 2427 PHE A CG    1 
ATOM   6941  C  CD1   . PHE A 1 2427 ? 181.198 211.834 172.297 1.00 11.84  ? 2427 PHE A CD1   1 
ATOM   6942  C  CD2   . PHE A 1 2427 ? 180.827 214.001 173.207 1.00 11.31  ? 2427 PHE A CD2   1 
ATOM   6943  C  CE1   . PHE A 1 2427 ? 180.608 211.264 173.406 1.00 10.67  ? 2427 PHE A CE1   1 
ATOM   6944  C  CE2   . PHE A 1 2427 ? 180.238 213.437 174.318 1.00 10.68  ? 2427 PHE A CE2   1 
ATOM   6945  C  CZ    . PHE A 1 2427 ? 180.128 212.067 174.417 1.00 10.78  ? 2427 PHE A CZ    1 
ATOM   6946  N  N     . THR A 1 2428 ? 185.152 213.766 169.118 1.00 21.26  ? 2428 THR A N     1 
ATOM   6947  C  CA    . THR A 1 2428 ? 185.685 213.855 167.770 1.00 28.15  ? 2428 THR A CA    1 
ATOM   6948  C  C     . THR A 1 2428 ? 186.491 212.606 167.441 1.00 33.95  ? 2428 THR A C     1 
ATOM   6949  O  O     . THR A 1 2428 ? 186.818 211.802 168.317 1.00 41.60  ? 2428 THR A O     1 
ATOM   6950  C  CB    . THR A 1 2428 ? 186.564 215.100 167.609 1.00 26.90  ? 2428 THR A CB    1 
ATOM   6951  O  OG1   . THR A 1 2428 ? 187.769 214.936 168.367 1.00 22.59  ? 2428 THR A OG1   1 
ATOM   6952  C  CG2   . THR A 1 2428 ? 185.827 216.335 168.100 1.00 22.60  ? 2428 THR A CG2   1 
ATOM   6953  N  N     . SER A 1 2429 ? 186.796 212.448 166.155 1.00 31.07  ? 2429 SER A N     1 
ATOM   6954  C  CA    . SER A 1 2429 ? 187.642 211.345 165.721 1.00 35.21  ? 2429 SER A CA    1 
ATOM   6955  C  C     . SER A 1 2429 ? 189.003 211.432 166.398 1.00 47.19  ? 2429 SER A C     1 
ATOM   6956  O  O     . SER A 1 2429 ? 189.588 212.513 166.515 1.00 48.26  ? 2429 SER A O     1 
ATOM   6957  C  CB    . SER A 1 2429 ? 187.804 211.366 164.201 1.00 43.62  ? 2429 SER A CB    1 
ATOM   6958  O  OG    . SER A 1 2429 ? 188.503 212.525 163.781 1.00 53.38  ? 2429 SER A OG    1 
ATOM   6959  N  N     . ASN A 1 2430 ? 189.504 210.281 166.846 1.00 38.74  ? 2430 ASN A N     1 
ATOM   6960  C  CA    . ASN A 1 2430 ? 190.723 210.193 167.647 1.00 40.64  ? 2430 ASN A CA    1 
ATOM   6961  C  C     . ASN A 1 2430 ? 190.633 211.077 168.891 1.00 45.40  ? 2430 ASN A C     1 
ATOM   6962  O  O     . ASN A 1 2430 ? 191.603 211.746 169.263 1.00 46.91  ? 2430 ASN A O     1 
ATOM   6963  C  CB    . ASN A 1 2430 ? 191.962 210.544 166.809 1.00 54.54  ? 2430 ASN A CB    1 
ATOM   6964  C  CG    . ASN A 1 2430 ? 193.271 210.197 167.505 1.00 60.85  ? 2430 ASN A CG    1 
ATOM   6965  O  OD1   . ASN A 1 2430 ? 193.283 209.699 168.630 1.00 60.47  ? 2430 ASN A OD1   1 
ATOM   6966  N  ND2   . ASN A 1 2430 ? 194.384 210.465 166.831 1.00 63.12  ? 2430 ASN A ND2   1 
ATOM   6967  N  N     . GLY A 1 2431 ? 189.465 211.114 169.523 1.00 41.26  ? 2431 GLY A N     1 
ATOM   6968  C  CA    . GLY A 1 2431 ? 189.254 211.883 170.731 1.00 29.03  ? 2431 GLY A CA    1 
ATOM   6969  C  C     . GLY A 1 2431 ? 189.358 211.030 171.976 1.00 26.87  ? 2431 GLY A C     1 
ATOM   6970  O  O     . GLY A 1 2431 ? 189.865 209.906 171.955 1.00 27.51  ? 2431 GLY A O     1 
ATOM   6971  N  N     . LEU A 1 2432 ? 188.868 211.584 173.086 1.00 25.33  ? 2432 LEU A N     1 
ATOM   6972  C  CA    . LEU A 1 2432 ? 188.905 210.857 174.351 1.00 16.05  ? 2432 LEU A CA    1 
ATOM   6973  C  C     . LEU A 1 2432 ? 187.962 209.661 174.324 1.00 20.18  ? 2432 LEU A C     1 
ATOM   6974  O  O     . LEU A 1 2432 ? 188.350 208.543 174.685 1.00 23.18  ? 2432 LEU A O     1 
ATOM   6975  C  CB    . LEU A 1 2432 ? 188.552 211.798 175.502 1.00 13.53  ? 2432 LEU A CB    1 
ATOM   6976  C  CG    . LEU A 1 2432 ? 188.206 211.151 176.843 1.00 20.74  ? 2432 LEU A CG    1 
ATOM   6977  C  CD1   . LEU A 1 2432 ? 189.434 210.507 177.465 1.00 19.65  ? 2432 LEU A CD1   1 
ATOM   6978  C  CD2   . LEU A 1 2432 ? 187.598 212.173 177.787 1.00 27.76  ? 2432 LEU A CD2   1 
ATOM   6979  N  N     . VAL A 1 2433 ? 186.720 209.875 173.885 1.00 17.45  ? 2433 VAL A N     1 
ATOM   6980  C  CA    . VAL A 1 2433 ? 185.725 208.808 173.903 1.00 12.63  ? 2433 VAL A CA    1 
ATOM   6981  C  C     . VAL A 1 2433 ? 186.104 207.697 172.932 1.00 14.29  ? 2433 VAL A C     1 
ATOM   6982  O  O     . VAL A 1 2433 ? 185.944 206.511 173.238 1.00 17.68  ? 2433 VAL A O     1 
ATOM   6983  C  CB    . VAL A 1 2433 ? 184.327 209.375 173.597 1.00 13.27  ? 2433 VAL A CB    1 
ATOM   6984  C  CG1   . VAL A 1 2433 ? 183.272 208.298 173.773 1.00 11.99  ? 2433 VAL A CG1   1 
ATOM   6985  C  CG2   . VAL A 1 2433 ? 184.029 210.560 174.496 1.00 14.56  ? 2433 VAL A CG2   1 
ATOM   6986  N  N     . THR A 1 2434 ? 186.603 208.056 171.748 1.00 21.24  ? 2434 THR A N     1 
ATOM   6987  C  CA    . THR A 1 2434 ? 186.948 207.045 170.753 1.00 17.75  ? 2434 THR A CA    1 
ATOM   6988  C  C     . THR A 1 2434 ? 188.095 206.163 171.232 1.00 16.80  ? 2434 THR A C     1 
ATOM   6989  O  O     . THR A 1 2434 ? 188.028 204.931 171.134 1.00 17.07  ? 2434 THR A O     1 
ATOM   6990  C  CB    . THR A 1 2434 ? 187.303 207.717 169.426 1.00 19.43  ? 2434 THR A CB    1 
ATOM   6991  O  OG1   . THR A 1 2434 ? 186.240 208.595 169.036 1.00 24.23  ? 2434 THR A OG1   1 
ATOM   6992  C  CG2   . THR A 1 2434 ? 187.512 206.674 168.341 1.00 21.32  ? 2434 THR A CG2   1 
ATOM   6993  N  N     . LYS A 1 2435 ? 189.161 206.776 171.753 1.00 16.96  ? 2435 LYS A N     1 
ATOM   6994  C  CA    . LYS A 1 2435 ? 190.284 205.997 172.265 1.00 17.94  ? 2435 LYS A CA    1 
ATOM   6995  C  C     . LYS A 1 2435 ? 189.875 205.172 173.478 1.00 16.22  ? 2435 LYS A C     1 
ATOM   6996  O  O     . LYS A 1 2435 ? 190.321 204.029 173.638 1.00 17.23  ? 2435 LYS A O     1 
ATOM   6997  C  CB    . LYS A 1 2435 ? 191.454 206.919 172.604 1.00 21.61  ? 2435 LYS A CB    1 
ATOM   6998  C  CG    . LYS A 1 2435 ? 192.033 207.643 171.401 1.00 30.32  ? 2435 LYS A CG    1 
ATOM   6999  C  CD    . LYS A 1 2435 ? 193.023 208.718 171.815 1.00 32.07  ? 2435 LYS A CD    1 
ATOM   7000  C  CE    . LYS A 1 2435 ? 194.390 208.133 172.106 1.00 33.51  ? 2435 LYS A CE    1 
ATOM   7001  N  NZ    . LYS A 1 2435 ? 195.394 209.198 172.370 1.00 43.97  ? 2435 LYS A NZ    1 
ATOM   7002  N  N     . ALA A 1 2436 ? 189.025 205.732 174.341 1.00 18.48  ? 2436 ALA A N     1 
ATOM   7003  C  CA    . ALA A 1 2436 ? 188.534 204.976 175.487 1.00 13.15  ? 2436 ALA A CA    1 
ATOM   7004  C  C     . ALA A 1 2436 ? 187.741 203.755 175.043 1.00 13.82  ? 2436 ALA A C     1 
ATOM   7005  O  O     . ALA A 1 2436 ? 187.890 202.671 175.614 1.00 18.41  ? 2436 ALA A O     1 
ATOM   7006  C  CB    . ALA A 1 2436 ? 187.683 205.874 176.383 1.00 12.85  ? 2436 ALA A CB    1 
ATOM   7007  N  N     . LEU A 1 2437 ? 186.887 203.912 174.029 1.00 12.23  ? 2437 LEU A N     1 
ATOM   7008  C  CA    . LEU A 1 2437 ? 186.114 202.784 173.518 1.00 10.89  ? 2437 LEU A CA    1 
ATOM   7009  C  C     . LEU A 1 2437 ? 187.019 201.738 172.880 1.00 11.98  ? 2437 LEU A C     1 
ATOM   7010  O  O     . LEU A 1 2437 ? 186.822 200.530 173.075 1.00 15.76  ? 2437 LEU A O     1 
ATOM   7011  C  CB    . LEU A 1 2437 ? 185.071 203.285 172.519 1.00 10.42  ? 2437 LEU A CB    1 
ATOM   7012  C  CG    . LEU A 1 2437 ? 184.066 202.286 171.949 1.00 10.80  ? 2437 LEU A CG    1 
ATOM   7013  C  CD1   . LEU A 1 2437 ? 183.104 201.817 173.024 1.00 13.81  ? 2437 LEU A CD1   1 
ATOM   7014  C  CD2   . LEU A 1 2437 ? 183.312 202.909 170.789 1.00 12.92  ? 2437 LEU A CD2   1 
ATOM   7015  N  N     . GLU A 1 2438 ? 188.022 202.186 172.122 1.00 16.23  ? 2438 GLU A N     1 
ATOM   7016  C  CA    . GLU A 1 2438 ? 188.961 201.254 171.508 1.00 16.69  ? 2438 GLU A CA    1 
ATOM   7017  C  C     . GLU A 1 2438 ? 189.711 200.458 172.566 1.00 15.11  ? 2438 GLU A C     1 
ATOM   7018  O  O     . GLU A 1 2438 ? 189.923 199.249 172.411 1.00 15.22  ? 2438 GLU A O     1 
ATOM   7019  C  CB    . GLU A 1 2438 ? 189.937 202.012 170.609 1.00 20.80  ? 2438 GLU A CB    1 
ATOM   7020  C  CG    . GLU A 1 2438 ? 190.798 201.118 169.732 1.00 34.91  ? 2438 GLU A CG    1 
ATOM   7021  C  CD    . GLU A 1 2438 ? 190.085 200.683 168.467 1.00 55.33  ? 2438 GLU A CD    1 
ATOM   7022  O  OE1   . GLU A 1 2438 ? 190.545 199.714 167.827 1.00 58.64  ? 2438 GLU A OE1   1 
ATOM   7023  O  OE2   . GLU A 1 2438 ? 189.064 201.310 168.111 1.00 51.45  ? 2438 GLU A OE2   1 
ATOM   7024  N  N     . HIS A 1 2439 ? 190.124 201.118 173.650 1.00 15.04  ? 2439 HIS A N     1 
ATOM   7025  C  CA    . HIS A 1 2439 ? 190.815 200.410 174.722 1.00 16.47  ? 2439 HIS A CA    1 
ATOM   7026  C  C     . HIS A 1 2439 ? 189.873 199.470 175.465 1.00 17.60  ? 2439 HIS A C     1 
ATOM   7027  O  O     . HIS A 1 2439 ? 190.259 198.351 175.821 1.00 18.41  ? 2439 HIS A O     1 
ATOM   7028  C  CB    . HIS A 1 2439 ? 191.446 201.407 175.689 1.00 16.75  ? 2439 HIS A CB    1 
ATOM   7029  C  CG    . HIS A 1 2439 ? 192.317 200.770 176.726 1.00 24.58  ? 2439 HIS A CG    1 
ATOM   7030  N  ND1   . HIS A 1 2439 ? 193.578 200.292 176.445 1.00 23.51  ? 2439 HIS A ND1   1 
ATOM   7031  C  CD2   . HIS A 1 2439 ? 192.107 200.527 178.041 1.00 28.11  ? 2439 HIS A CD2   1 
ATOM   7032  C  CE1   . HIS A 1 2439 ? 194.109 199.784 177.542 1.00 28.94  ? 2439 HIS A CE1   1 
ATOM   7033  N  NE2   . HIS A 1 2439 ? 193.237 199.914 178.525 1.00 28.51  ? 2439 HIS A NE2   1 
ATOM   7034  N  N     . ALA A 1 2440 ? 188.637 199.909 175.713 1.00 17.87  ? 2440 ALA A N     1 
ATOM   7035  C  CA    . ALA A 1 2440 ? 187.679 199.083 176.437 1.00 13.54  ? 2440 ALA A CA    1 
ATOM   7036  C  C     . ALA A 1 2440 ? 187.309 197.835 175.652 1.00 12.97  ? 2440 ALA A C     1 
ATOM   7037  O  O     . ALA A 1 2440 ? 186.980 196.805 176.251 1.00 17.22  ? 2440 ALA A O     1 
ATOM   7038  C  CB    . ALA A 1 2440 ? 186.428 199.895 176.766 1.00 13.27  ? 2440 ALA A CB    1 
ATOM   7039  N  N     . PHE A 1 2441 ? 187.353 197.901 174.320 1.00 14.36  ? 2441 PHE A N     1 
ATOM   7040  C  CA    . PHE A 1 2441 ? 187.109 196.701 173.529 1.00 14.51  ? 2441 PHE A CA    1 
ATOM   7041  C  C     . PHE A 1 2441 ? 188.183 195.641 173.743 1.00 16.44  ? 2441 PHE A C     1 
ATOM   7042  O  O     . PHE A 1 2441 ? 187.974 194.480 173.377 1.00 12.94  ? 2441 PHE A O     1 
ATOM   7043  C  CB    . PHE A 1 2441 ? 187.011 197.050 172.045 1.00 13.93  ? 2441 PHE A CB    1 
ATOM   7044  C  CG    . PHE A 1 2441 ? 185.603 197.235 171.561 1.00 16.71  ? 2441 PHE A CG    1 
ATOM   7045  C  CD1   . PHE A 1 2441 ? 184.808 196.140 171.274 1.00 17.75  ? 2441 PHE A CD1   1 
ATOM   7046  C  CD2   . PHE A 1 2441 ? 185.078 198.502 171.384 1.00 14.04  ? 2441 PHE A CD2   1 
ATOM   7047  C  CE1   . PHE A 1 2441 ? 183.512 196.305 170.827 1.00 17.55  ? 2441 PHE A CE1   1 
ATOM   7048  C  CE2   . PHE A 1 2441 ? 183.784 198.674 170.936 1.00 17.53  ? 2441 PHE A CE2   1 
ATOM   7049  C  CZ    . PHE A 1 2441 ? 183.001 197.574 170.657 1.00 15.95  ? 2441 PHE A CZ    1 
ATOM   7050  N  N     . GLN A 1 2442 ? 189.324 196.011 174.321 1.00 20.35  ? 2442 GLN A N     1 
ATOM   7051  C  CA    . GLN A 1 2442 ? 190.399 195.074 174.614 1.00 14.95  ? 2442 GLN A CA    1 
ATOM   7052  C  C     . GLN A 1 2442 ? 190.329 194.508 176.026 1.00 16.54  ? 2442 GLN A C     1 
ATOM   7053  O  O     . GLN A 1 2442 ? 191.199 193.716 176.403 1.00 18.62  ? 2442 GLN A O     1 
ATOM   7054  C  CB    . GLN A 1 2442 ? 191.758 195.749 174.400 1.00 18.42  ? 2442 GLN A CB    1 
ATOM   7055  C  CG    . GLN A 1 2442 ? 192.043 196.128 172.956 1.00 23.88  ? 2442 GLN A CG    1 
ATOM   7056  C  CD    . GLN A 1 2442 ? 191.759 194.995 171.989 1.00 26.30  ? 2442 GLN A CD    1 
ATOM   7057  O  OE1   . GLN A 1 2442 ? 192.282 193.891 172.137 1.00 26.80  ? 2442 GLN A OE1   1 
ATOM   7058  N  NE2   . GLN A 1 2442 ? 190.926 195.264 170.991 1.00 21.55  ? 2442 GLN A NE2   1 
ATOM   7059  N  N     . LEU A 1 2443 ? 189.329 194.892 176.814 1.00 18.69  ? 2443 LEU A N     1 
ATOM   7060  C  CA    . LEU A 1 2443 ? 189.179 194.394 178.170 1.00 15.33  ? 2443 LEU A CA    1 
ATOM   7061  C  C     . LEU A 1 2443 ? 188.238 193.191 178.194 1.00 17.21  ? 2443 LEU A C     1 
ATOM   7062  O  O     . LEU A 1 2443 ? 187.670 192.789 177.176 1.00 19.02  ? 2443 LEU A O     1 
ATOM   7063  C  CB    . LEU A 1 2443 ? 188.674 195.500 179.094 1.00 15.08  ? 2443 LEU A CB    1 
ATOM   7064  C  CG    . LEU A 1 2443 ? 189.474 196.802 179.124 1.00 17.08  ? 2443 LEU A CG    1 
ATOM   7065  C  CD1   . LEU A 1 2443 ? 188.825 197.800 180.069 1.00 15.50  ? 2443 LEU A CD1   1 
ATOM   7066  C  CD2   . LEU A 1 2443 ? 190.912 196.537 179.530 1.00 21.07  ? 2443 LEU A CD2   1 
ATOM   7067  N  N     . GLU A 1 2444 ? 188.069 192.609 179.377 1.00 13.77  ? 2444 GLU A N     1 
ATOM   7068  C  CA    . GLU A 1 2444 ? 187.187 191.467 179.582 1.00 13.14  ? 2444 GLU A CA    1 
ATOM   7069  C  C     . GLU A 1 2444 ? 185.922 191.948 180.276 1.00 15.83  ? 2444 GLU A C     1 
ATOM   7070  O  O     . GLU A 1 2444 ? 185.993 192.616 181.313 1.00 16.06  ? 2444 GLU A O     1 
ATOM   7071  C  CB    . GLU A 1 2444 ? 187.879 190.380 180.404 1.00 15.57  ? 2444 GLU A CB    1 
ATOM   7072  C  CG    . GLU A 1 2444 ? 189.043 189.716 179.691 1.00 27.08  ? 2444 GLU A CG    1 
ATOM   7073  C  CD    . GLU A 1 2444 ? 189.720 188.657 180.536 1.00 55.09  ? 2444 GLU A CD    1 
ATOM   7074  O  OE1   . GLU A 1 2444 ? 189.363 188.525 181.725 1.00 58.30  ? 2444 GLU A OE1   1 
ATOM   7075  O  OE2   . GLU A 1 2444 ? 190.611 187.957 180.011 1.00 60.48  ? 2444 GLU A OE2   1 
ATOM   7076  N  N     . HIS A 1 2445 ? 184.771 191.609 179.705 1.00 11.26  ? 2445 HIS A N     1 
ATOM   7077  C  CA    . HIS A 1 2445 ? 183.482 192.033 180.222 1.00 8.80   ? 2445 HIS A CA    1 
ATOM   7078  C  C     . HIS A 1 2445 ? 182.611 190.814 180.489 1.00 9.18   ? 2445 HIS A C     1 
ATOM   7079  O  O     . HIS A 1 2445 ? 182.781 189.761 179.868 1.00 12.22  ? 2445 HIS A O     1 
ATOM   7080  C  CB    . HIS A 1 2445 ? 182.779 192.980 179.243 1.00 9.37   ? 2445 HIS A CB    1 
ATOM   7081  C  CG    . HIS A 1 2445 ? 183.630 194.129 178.798 1.00 11.33  ? 2445 HIS A CG    1 
ATOM   7082  N  ND1   . HIS A 1 2445 ? 183.822 195.256 179.566 1.00 13.97  ? 2445 HIS A ND1   1 
ATOM   7083  C  CD2   . HIS A 1 2445 ? 184.345 194.321 177.664 1.00 9.80   ? 2445 HIS A CD2   1 
ATOM   7084  C  CE1   . HIS A 1 2445 ? 184.616 196.094 178.924 1.00 11.82  ? 2445 HIS A CE1   1 
ATOM   7085  N  NE2   . HIS A 1 2445 ? 184.947 195.550 177.768 1.00 10.05  ? 2445 HIS A NE2   1 
ATOM   7086  N  N     . ILE A 1 2446 ? 181.674 190.965 181.429 1.00 7.44   ? 2446 ILE A N     1 
ATOM   7087  C  CA    . ILE A 1 2446 ? 180.793 189.860 181.784 1.00 7.27   ? 2446 ILE A CA    1 
ATOM   7088  C  C     . ILE A 1 2446 ? 179.887 189.470 180.622 1.00 9.08   ? 2446 ILE A C     1 
ATOM   7089  O  O     . ILE A 1 2446 ? 179.377 188.345 180.589 1.00 11.22  ? 2446 ILE A O     1 
ATOM   7090  C  CB    . ILE A 1 2446 ? 179.973 190.213 183.041 1.00 7.58   ? 2446 ILE A CB    1 
ATOM   7091  C  CG1   . ILE A 1 2446 ? 179.570 188.944 183.792 1.00 8.24   ? 2446 ILE A CG1   1 
ATOM   7092  C  CG2   . ILE A 1 2446 ? 178.749 191.040 182.680 1.00 8.34   ? 2446 ILE A CG2   1 
ATOM   7093  C  CD1   . ILE A 1 2446 ? 180.743 188.091 184.216 1.00 7.88   ? 2446 ILE A CD1   1 
ATOM   7094  N  N     . MET A 1 2447 ? 179.675 190.369 179.665 1.00 8.51   ? 2447 MET A N     1 
ATOM   7095  C  CA    . MET A 1 2447 ? 178.939 190.066 178.449 1.00 6.98   ? 2447 MET A CA    1 
ATOM   7096  C  C     . MET A 1 2447 ? 179.711 190.594 177.250 1.00 9.76   ? 2447 MET A C     1 
ATOM   7097  O  O     . MET A 1 2447 ? 180.666 191.360 177.390 1.00 10.90  ? 2447 MET A O     1 
ATOM   7098  C  CB    . MET A 1 2447 ? 177.530 190.669 178.463 1.00 9.26   ? 2447 MET A CB    1 
ATOM   7099  C  CG    . MET A 1 2447 ? 176.602 190.058 179.485 1.00 7.90   ? 2447 MET A CG    1 
ATOM   7100  S  SD    . MET A 1 2447 ? 174.979 190.827 179.434 1.00 27.83  ? 2447 MET A SD    1 
ATOM   7101  C  CE    . MET A 1 2447 ? 174.180 189.978 180.782 1.00 15.13  ? 2447 MET A CE    1 
ATOM   7102  N  N     . ASP A 1 2448 ? 179.287 190.164 176.065 1.00 14.19  ? 2448 ASP A N     1 
ATOM   7103  C  CA    . ASP A 1 2448 ? 179.901 190.646 174.837 1.00 11.47  ? 2448 ASP A CA    1 
ATOM   7104  C  C     . ASP A 1 2448 ? 179.719 192.153 174.719 1.00 13.33  ? 2448 ASP A C     1 
ATOM   7105  O  O     . ASP A 1 2448 ? 178.614 192.674 174.889 1.00 17.09  ? 2448 ASP A O     1 
ATOM   7106  C  CB    . ASP A 1 2448 ? 179.290 189.940 173.628 1.00 9.63   ? 2448 ASP A CB    1 
ATOM   7107  C  CG    . ASP A 1 2448 ? 179.873 188.560 173.405 1.00 24.49  ? 2448 ASP A CG    1 
ATOM   7108  O  OD1   . ASP A 1 2448 ? 179.670 187.999 172.309 1.00 29.52  ? 2448 ASP A OD1   1 
ATOM   7109  O  OD2   . ASP A 1 2448 ? 180.537 188.037 174.324 1.00 33.91  ? 2448 ASP A OD2   1 
ATOM   7110  N  N     . LEU A 1 2449 ? 180.810 192.852 174.427 1.00 11.81  ? 2449 LEU A N     1 
ATOM   7111  C  CA    . LEU A 1 2449 ? 180.797 194.305 174.359 1.00 10.16  ? 2449 LEU A CA    1 
ATOM   7112  C  C     . LEU A 1 2449 ? 180.455 194.760 172.948 1.00 14.13  ? 2449 LEU A C     1 
ATOM   7113  O  O     . LEU A 1 2449 ? 181.116 194.367 171.982 1.00 14.60  ? 2449 LEU A O     1 
ATOM   7114  C  CB    . LEU A 1 2449 ? 182.147 194.881 174.781 1.00 12.49  ? 2449 LEU A CB    1 
ATOM   7115  C  CG    . LEU A 1 2449 ? 182.122 196.353 175.192 1.00 12.16  ? 2449 LEU A CG    1 
ATOM   7116  C  CD1   . LEU A 1 2449 ? 181.616 196.496 176.616 1.00 14.22  ? 2449 LEU A CD1   1 
ATOM   7117  C  CD2   . LEU A 1 2449 ? 183.497 196.981 175.039 1.00 11.96  ? 2449 LEU A CD2   1 
ATOM   7118  N  N     . THR A 1 2450 ? 179.425 195.590 172.838 1.00 15.66  ? 2450 THR A N     1 
ATOM   7119  C  CA    . THR A 1 2450 ? 179.051 196.224 171.585 1.00 12.99  ? 2450 THR A CA    1 
ATOM   7120  C  C     . THR A 1 2450 ? 179.188 197.731 171.735 1.00 11.27  ? 2450 THR A C     1 
ATOM   7121  O  O     . THR A 1 2450 ? 179.047 198.277 172.833 1.00 13.89  ? 2450 THR A O     1 
ATOM   7122  C  CB    . THR A 1 2450 ? 177.620 195.865 171.169 1.00 12.76  ? 2450 THR A CB    1 
ATOM   7123  O  OG1   . THR A 1 2450 ? 176.697 196.347 172.153 1.00 21.11  ? 2450 THR A OG1   1 
ATOM   7124  C  CG2   . THR A 1 2450 ? 177.470 194.360 171.027 1.00 12.43  ? 2450 THR A CG2   1 
ATOM   7125  N  N     . ARG A 1 2451 ? 179.477 198.395 170.616 1.00 10.28  ? 2451 ARG A N     1 
ATOM   7126  C  CA    . ARG A 1 2451 ? 179.738 199.829 170.653 1.00 10.43  ? 2451 ARG A CA    1 
ATOM   7127  C  C     . ARG A 1 2451 ? 178.516 200.610 171.121 1.00 10.11  ? 2451 ARG A C     1 
ATOM   7128  O  O     . ARG A 1 2451 ? 178.632 201.517 171.956 1.00 12.67  ? 2451 ARG A O     1 
ATOM   7129  C  CB    . ARG A 1 2451 ? 180.193 200.301 169.272 1.00 11.48  ? 2451 ARG A CB    1 
ATOM   7130  C  CG    . ARG A 1 2451 ? 180.209 201.802 169.088 1.00 11.23  ? 2451 ARG A CG    1 
ATOM   7131  C  CD    . ARG A 1 2451 ? 180.541 202.163 167.653 1.00 16.19  ? 2451 ARG A CD    1 
ATOM   7132  N  NE    . ARG A 1 2451 ? 179.628 201.539 166.703 1.00 18.67  ? 2451 ARG A NE    1 
ATOM   7133  C  CZ    . ARG A 1 2451 ? 179.676 201.721 165.390 1.00 11.43  ? 2451 ARG A CZ    1 
ATOM   7134  N  NH1   . ARG A 1 2451 ? 180.587 202.501 164.834 1.00 8.61   ? 2451 ARG A NH1   1 
ATOM   7135  N  NH2   . ARG A 1 2451 ? 178.788 201.104 164.616 1.00 9.06   ? 2451 ARG A NH2   1 
ATOM   7136  N  N     . LEU A 1 2452 ? 177.331 200.258 170.618 1.00 9.17   ? 2452 LEU A N     1 
ATOM   7137  C  CA    . LEU A 1 2452 ? 176.154 201.064 170.921 1.00 7.58   ? 2452 LEU A CA    1 
ATOM   7138  C  C     . LEU A 1 2452 ? 175.665 200.873 172.348 1.00 7.31   ? 2452 LEU A C     1 
ATOM   7139  O  O     . LEU A 1 2452 ? 175.046 201.784 172.897 1.00 9.95   ? 2452 LEU A O     1 
ATOM   7140  C  CB    . LEU A 1 2452 ? 175.022 200.777 169.941 1.00 8.11   ? 2452 LEU A CB    1 
ATOM   7141  C  CG    . LEU A 1 2452 ? 175.290 201.229 168.510 1.00 6.59   ? 2452 LEU A CG    1 
ATOM   7142  C  CD1   . LEU A 1 2452 ? 174.150 200.797 167.643 1.00 6.38   ? 2452 LEU A CD1   1 
ATOM   7143  C  CD2   . LEU A 1 2452 ? 175.462 202.732 168.455 1.00 7.60   ? 2452 LEU A CD2   1 
ATOM   7144  N  N     . ARG A 1 2453 ? 175.925 199.724 172.972 1.00 8.37   ? 2453 ARG A N     1 
ATOM   7145  C  CA    . ARG A 1 2453 ? 175.557 199.581 174.378 1.00 8.06   ? 2453 ARG A CA    1 
ATOM   7146  C  C     . ARG A 1 2453 ? 176.292 200.606 175.233 1.00 9.14   ? 2453 ARG A C     1 
ATOM   7147  O  O     . ARG A 1 2453 ? 175.672 201.367 175.991 1.00 9.86   ? 2453 ARG A O     1 
ATOM   7148  C  CB    . ARG A 1 2453 ? 175.852 198.162 174.864 1.00 7.06   ? 2453 ARG A CB    1 
ATOM   7149  C  CG    . ARG A 1 2453 ? 175.787 198.020 176.375 1.00 8.50   ? 2453 ARG A CG    1 
ATOM   7150  C  CD    . ARG A 1 2453 ? 175.592 196.578 176.805 1.00 5.97   ? 2453 ARG A CD    1 
ATOM   7151  N  NE    . ARG A 1 2453 ? 176.763 195.751 176.546 1.00 10.43  ? 2453 ARG A NE    1 
ATOM   7152  C  CZ    . ARG A 1 2453 ? 177.719 195.516 177.434 1.00 9.17   ? 2453 ARG A CZ    1 
ATOM   7153  N  NH1   . ARG A 1 2453 ? 177.687 196.053 178.642 1.00 5.93   ? 2453 ARG A NH1   1 
ATOM   7154  N  NH2   . ARG A 1 2453 ? 178.732 194.721 177.102 1.00 10.09  ? 2453 ARG A NH2   1 
ATOM   7155  N  N     . CYS A 1 2454 ? 177.618 200.663 175.092 1.00 11.03  ? 2454 CYS A N     1 
ATOM   7156  C  CA    . CYS A 1 2454 ? 178.408 201.639 175.833 1.00 9.59   ? 2454 CYS A CA    1 
ATOM   7157  C  C     . CYS A 1 2454 ? 178.031 203.062 175.447 1.00 9.58   ? 2454 CYS A C     1 
ATOM   7158  O  O     . CYS A 1 2454 ? 177.940 203.943 176.310 1.00 9.18   ? 2454 CYS A O     1 
ATOM   7159  C  CB    . CYS A 1 2454 ? 179.898 201.403 175.588 1.00 7.99   ? 2454 CYS A CB    1 
ATOM   7160  S  SG    . CYS A 1 2454 ? 180.395 199.674 175.579 1.00 39.60  ? 2454 CYS A SG    1 
ATOM   7161  N  N     . LEU A 1 2455 ? 177.820 203.309 174.151 1.00 8.39   ? 2455 LEU A N     1 
ATOM   7162  C  CA    . LEU A 1 2455 ? 177.501 204.663 173.711 1.00 6.35   ? 2455 LEU A CA    1 
ATOM   7163  C  C     . LEU A 1 2455 ? 176.159 205.131 174.262 1.00 6.23   ? 2455 LEU A C     1 
ATOM   7164  O  O     . LEU A 1 2455 ? 176.038 206.272 174.718 1.00 11.13  ? 2455 LEU A O     1 
ATOM   7165  C  CB    . LEU A 1 2455 ? 177.524 204.738 172.186 1.00 9.04   ? 2455 LEU A CB    1 
ATOM   7166  C  CG    . LEU A 1 2455 ? 178.919 204.702 171.556 1.00 7.52   ? 2455 LEU A CG    1 
ATOM   7167  C  CD1   . LEU A 1 2455 ? 178.881 205.217 170.130 1.00 10.53  ? 2455 LEU A CD1   1 
ATOM   7168  C  CD2   . LEU A 1 2455 ? 179.909 205.502 172.387 1.00 6.53   ? 2455 LEU A CD2   1 
ATOM   7169  N  N     . GLY A 1 2456 ? 175.142 204.268 174.237 1.00 4.63   ? 2456 GLY A N     1 
ATOM   7170  C  CA    . GLY A 1 2456 ? 173.854 204.638 174.795 1.00 6.21   ? 2456 GLY A CA    1 
ATOM   7171  C  C     . GLY A 1 2456 ? 173.905 204.825 176.296 1.00 7.43   ? 2456 GLY A C     1 
ATOM   7172  O  O     . GLY A 1 2456 ? 173.256 205.725 176.840 1.00 9.23   ? 2456 GLY A O     1 
ATOM   7173  N  N     . SER A 1 2457 ? 174.681 203.987 176.989 1.00 8.39   ? 2457 SER A N     1 
ATOM   7174  C  CA    . SER A 1 2457 ? 174.882 204.194 178.418 1.00 5.97   ? 2457 SER A CA    1 
ATOM   7175  C  C     . SER A 1 2457 ? 175.490 205.565 178.682 1.00 8.85   ? 2457 SER A C     1 
ATOM   7176  O  O     . SER A 1 2457 ? 175.007 206.323 179.533 1.00 12.50  ? 2457 SER A O     1 
ATOM   7177  C  CB    . SER A 1 2457 ? 175.778 203.093 178.980 1.00 5.81   ? 2457 SER A CB    1 
ATOM   7178  O  OG    . SER A 1 2457 ? 175.342 201.819 178.549 1.00 13.93  ? 2457 SER A OG    1 
ATOM   7179  N  N     . LEU A 1 2458 ? 176.539 205.910 177.931 1.00 6.10   ? 2458 LEU A N     1 
ATOM   7180  C  CA    . LEU A 1 2458 ? 177.203 207.196 178.110 1.00 5.18   ? 2458 LEU A CA    1 
ATOM   7181  C  C     . LEU A 1 2458 ? 176.257 208.353 177.813 1.00 8.00   ? 2458 LEU A C     1 
ATOM   7182  O  O     . LEU A 1 2458 ? 176.242 209.354 178.538 1.00 10.63  ? 2458 LEU A O     1 
ATOM   7183  C  CB    . LEU A 1 2458 ? 178.443 207.261 177.217 1.00 6.24   ? 2458 LEU A CB    1 
ATOM   7184  C  CG    . LEU A 1 2458 ? 179.142 208.604 177.011 1.00 7.17   ? 2458 LEU A CG    1 
ATOM   7185  C  CD1   . LEU A 1 2458 ? 179.741 209.100 178.311 1.00 8.88   ? 2458 LEU A CD1   1 
ATOM   7186  C  CD2   . LEU A 1 2458 ? 180.214 208.476 175.949 1.00 7.71   ? 2458 LEU A CD2   1 
ATOM   7187  N  N     . PHE A 1 2459 ? 175.459 208.231 176.751 1.00 6.45   ? 2459 PHE A N     1 
ATOM   7188  C  CA    . PHE A 1 2459 ? 174.527 209.296 176.395 1.00 7.09   ? 2459 PHE A CA    1 
ATOM   7189  C  C     . PHE A 1 2459 ? 173.465 209.483 177.471 1.00 8.96   ? 2459 PHE A C     1 
ATOM   7190  O  O     . PHE A 1 2459 ? 173.098 210.617 177.803 1.00 11.71  ? 2459 PHE A O     1 
ATOM   7191  C  CB    . PHE A 1 2459 ? 173.879 208.995 175.043 1.00 5.76   ? 2459 PHE A CB    1 
ATOM   7192  C  CG    . PHE A 1 2459 ? 174.859 208.891 173.908 1.00 5.12   ? 2459 PHE A CG    1 
ATOM   7193  C  CD1   . PHE A 1 2459 ? 176.099 209.502 173.983 1.00 4.50   ? 2459 PHE A CD1   1 
ATOM   7194  C  CD2   . PHE A 1 2459 ? 174.543 208.171 172.769 1.00 4.94   ? 2459 PHE A CD2   1 
ATOM   7195  C  CE1   . PHE A 1 2459 ? 177.000 209.402 172.944 1.00 5.33   ? 2459 PHE A CE1   1 
ATOM   7196  C  CE2   . PHE A 1 2459 ? 175.441 208.067 171.727 1.00 4.09   ? 2459 PHE A CE2   1 
ATOM   7197  C  CZ    . PHE A 1 2459 ? 176.670 208.684 171.814 1.00 5.24   ? 2459 PHE A CZ    1 
ATOM   7198  N  N     . SER A 1 2460 ? 172.956 208.381 178.028 1.00 7.20   ? 2460 SER A N     1 
ATOM   7199  C  CA    . SER A 1 2460 ? 171.980 208.485 179.106 1.00 6.11   ? 2460 SER A CA    1 
ATOM   7200  C  C     . SER A 1 2460 ? 172.587 209.139 180.341 1.00 12.07  ? 2460 SER A C     1 
ATOM   7201  O  O     . SER A 1 2460 ? 171.939 209.963 180.999 1.00 12.39  ? 2460 SER A O     1 
ATOM   7202  C  CB    . SER A 1 2460 ? 171.425 207.103 179.444 1.00 8.01   ? 2460 SER A CB    1 
ATOM   7203  O  OG    . SER A 1 2460 ? 170.710 206.565 178.347 1.00 11.66  ? 2460 SER A OG    1 
ATOM   7204  N  N     . MET A 1 2461 ? 173.832 208.790 180.674 1.00 9.55   ? 2461 MET A N     1 
ATOM   7205  C  CA    . MET A 1 2461 ? 174.469 209.421 181.827 1.00 8.19   ? 2461 MET A CA    1 
ATOM   7206  C  C     . MET A 1 2461 ? 174.722 210.906 181.582 1.00 8.65   ? 2461 MET A C     1 
ATOM   7207  O  O     . MET A 1 2461 ? 174.623 211.717 182.508 1.00 14.19  ? 2461 MET A O     1 
ATOM   7208  C  CB    . MET A 1 2461 ? 175.766 208.696 182.190 1.00 10.31  ? 2461 MET A CB    1 
ATOM   7209  C  CG    . MET A 1 2461 ? 175.614 207.189 182.312 1.00 7.16   ? 2461 MET A CG    1 
ATOM   7210  S  SD    . MET A 1 2461 ? 176.988 206.384 183.147 1.00 8.84   ? 2461 MET A SD    1 
ATOM   7211  C  CE    . MET A 1 2461 ? 177.278 207.541 184.476 1.00 10.63  ? 2461 MET A CE    1 
ATOM   7212  N  N     . LEU A 1 2462 ? 175.038 211.290 180.344 1.00 8.90   ? 2462 LEU A N     1 
ATOM   7213  C  CA    . LEU A 1 2462 ? 175.210 212.711 180.048 1.00 8.71   ? 2462 LEU A CA    1 
ATOM   7214  C  C     . LEU A 1 2462 ? 173.882 213.460 180.123 1.00 10.26  ? 2462 LEU A C     1 
ATOM   7215  O  O     . LEU A 1 2462 ? 173.834 214.613 180.574 1.00 14.06  ? 2462 LEU A O     1 
ATOM   7216  C  CB    . LEU A 1 2462 ? 175.862 212.890 178.678 1.00 6.73   ? 2462 LEU A CB    1 
ATOM   7217  C  CG    . LEU A 1 2462 ? 177.285 212.337 178.567 1.00 7.72   ? 2462 LEU A CG    1 
ATOM   7218  C  CD1   . LEU A 1 2462 ? 177.811 212.466 177.149 1.00 7.82   ? 2462 LEU A CD1   1 
ATOM   7219  C  CD2   . LEU A 1 2462 ? 178.212 213.028 179.554 1.00 8.26   ? 2462 LEU A CD2   1 
ATOM   7220  N  N     . HIS A 1 2463 ? 172.793 212.824 179.686 1.00 8.63   ? 2463 HIS A N     1 
ATOM   7221  C  CA    . HIS A 1 2463 ? 171.472 213.418 179.873 1.00 11.87  ? 2463 HIS A CA    1 
ATOM   7222  C  C     . HIS A 1 2463 ? 171.162 213.597 181.354 1.00 13.83  ? 2463 HIS A C     1 
ATOM   7223  O  O     . HIS A 1 2463 ? 170.592 214.616 181.763 1.00 15.38  ? 2463 HIS A O     1 
ATOM   7224  C  CB    . HIS A 1 2463 ? 170.403 212.554 179.204 1.00 11.10  ? 2463 HIS A CB    1 
ATOM   7225  C  CG    . HIS A 1 2463 ? 170.439 212.596 177.709 1.00 10.92  ? 2463 HIS A CG    1 
ATOM   7226  N  ND1   . HIS A 1 2463 ? 169.731 211.711 176.925 1.00 9.42   ? 2463 HIS A ND1   1 
ATOM   7227  C  CD2   . HIS A 1 2463 ? 171.091 213.418 176.855 1.00 13.53  ? 2463 HIS A CD2   1 
ATOM   7228  C  CE1   . HIS A 1 2463 ? 169.949 211.985 175.651 1.00 15.95  ? 2463 HIS A CE1   1 
ATOM   7229  N  NE2   . HIS A 1 2463 ? 170.770 213.016 175.581 1.00 17.86  ? 2463 HIS A NE2   1 
ATOM   7230  N  N     . GLN A 1 2464 ? 171.528 212.608 182.171 1.00 16.81  ? 2464 GLN A N     1 
ATOM   7231  C  CA    . GLN A 1 2464 ? 171.356 212.737 183.614 1.00 16.98  ? 2464 GLN A CA    1 
ATOM   7232  C  C     . GLN A 1 2464 ? 172.198 213.877 184.173 1.00 17.27  ? 2464 GLN A C     1 
ATOM   7233  O  O     . GLN A 1 2464 ? 171.772 214.573 185.098 1.00 23.15  ? 2464 GLN A O     1 
ATOM   7234  C  CB    . GLN A 1 2464 ? 171.705 211.421 184.306 1.00 17.79  ? 2464 GLN A CB    1 
ATOM   7235  C  CG    . GLN A 1 2464 ? 171.312 211.372 185.773 1.00 20.05  ? 2464 GLN A CG    1 
ATOM   7236  C  CD    . GLN A 1 2464 ? 169.863 211.748 186.004 1.00 26.80  ? 2464 GLN A CD    1 
ATOM   7237  O  OE1   . GLN A 1 2464 ? 168.964 211.258 185.322 1.00 23.61  ? 2464 GLN A OE1   1 
ATOM   7238  N  NE2   . GLN A 1 2464 ? 169.629 212.625 186.973 1.00 25.30  ? 2464 GLN A NE2   1 
ATOM   7239  N  N     . ALA A 1 2465 ? 173.404 214.073 183.637 1.00 13.04  ? 2465 ALA A N     1 
ATOM   7240  C  CA    . ALA A 1 2465 ? 174.234 215.196 184.069 1.00 13.25  ? 2465 ALA A CA    1 
ATOM   7241  C  C     . ALA A 1 2465 ? 173.578 216.531 183.736 1.00 13.91  ? 2465 ALA A C     1 
ATOM   7242  O  O     . ALA A 1 2465 ? 173.603 217.470 184.543 1.00 17.73  ? 2465 ALA A O     1 
ATOM   7243  C  CB    . ALA A 1 2465 ? 175.614 215.106 183.424 1.00 12.79  ? 2465 ALA A CB    1 
ATOM   7244  N  N     . CYS A 1 2466 ? 172.997 216.638 182.540 1.00 14.45  ? 2466 CYS A N     1 
ATOM   7245  C  CA    . CYS A 1 2466 ? 172.275 217.855 182.180 1.00 17.32  ? 2466 CYS A CA    1 
ATOM   7246  C  C     . CYS A 1 2466 ? 171.084 218.079 183.105 1.00 18.30  ? 2466 CYS A C     1 
ATOM   7247  O  O     . CYS A 1 2466 ? 170.808 219.214 183.517 1.00 18.93  ? 2466 CYS A O     1 
ATOM   7248  C  CB    . CYS A 1 2466 ? 171.823 217.788 180.722 1.00 15.93  ? 2466 CYS A CB    1 
ATOM   7249  S  SG    . CYS A 1 2466 ? 173.174 217.778 179.526 1.00 25.70  ? 2466 CYS A SG    1 
ATOM   7250  N  N     . ARG A 1 2467 ? 170.367 217.006 183.445 1.00 15.22  ? 2467 ARG A N     1 
ATOM   7251  C  CA    . ARG A 1 2467 ? 169.259 217.130 184.387 1.00 20.47  ? 2467 ARG A CA    1 
ATOM   7252  C  C     . ARG A 1 2467 ? 169.751 217.542 185.770 1.00 21.86  ? 2467 ARG A C     1 
ATOM   7253  O  O     . ARG A 1 2467 ? 169.066 218.276 186.488 1.00 25.70  ? 2467 ARG A O     1 
ATOM   7254  C  CB    . ARG A 1 2467 ? 168.479 215.819 184.461 1.00 18.28  ? 2467 ARG A CB    1 
ATOM   7255  C  CG    . ARG A 1 2467 ? 167.621 215.548 183.239 1.00 19.23  ? 2467 ARG A CG    1 
ATOM   7256  C  CD    . ARG A 1 2467 ? 166.886 214.231 183.369 1.00 24.65  ? 2467 ARG A CD    1 
ATOM   7257  N  NE    . ARG A 1 2467 ? 166.351 213.774 182.093 1.00 29.01  ? 2467 ARG A NE    1 
ATOM   7258  C  CZ    . ARG A 1 2467 ? 165.191 214.165 181.583 1.00 31.77  ? 2467 ARG A CZ    1 
ATOM   7259  N  NH1   . ARG A 1 2467 ? 164.415 215.030 182.215 1.00 29.31  ? 2467 ARG A NH1   1 
ATOM   7260  N  NH2   . ARG A 1 2467 ? 164.799 213.673 180.411 1.00 28.24  ? 2467 ARG A NH2   1 
ATOM   7261  N  N     . ASN A 1 2468 ? 170.934 217.067 186.164 1.00 16.74  ? 2468 ASN A N     1 
ATOM   7262  C  CA    . ASN A 1 2468 ? 171.523 217.486 187.432 1.00 17.98  ? 2468 ASN A CA    1 
ATOM   7263  C  C     . ASN A 1 2468 ? 171.827 218.977 187.426 1.00 20.26  ? 2468 ASN A C     1 
ATOM   7264  O  O     . ASN A 1 2468 ? 171.588 219.673 188.420 1.00 28.36  ? 2468 ASN A O     1 
ATOM   7265  C  CB    . ASN A 1 2468 ? 172.794 216.685 187.712 1.00 18.31  ? 2468 ASN A CB    1 
ATOM   7266  C  CG    . ASN A 1 2468 ? 172.514 215.221 187.974 1.00 19.13  ? 2468 ASN A CG    1 
ATOM   7267  O  OD1   . ASN A 1 2468 ? 171.361 214.804 188.063 1.00 29.30  ? 2468 ASN A OD1   1 
ATOM   7268  N  ND2   . ASN A 1 2468 ? 173.572 214.430 188.094 1.00 16.85  ? 2468 ASN A ND2   1 
ATOM   7269  N  N     . VAL A 1 2469 ? 172.366 219.482 186.316 1.00 19.61  ? 2469 VAL A N     1 
ATOM   7270  C  CA    . VAL A 1 2469 ? 172.624 220.917 186.205 1.00 22.99  ? 2469 VAL A CA    1 
ATOM   7271  C  C     . VAL A 1 2469 ? 171.317 221.699 186.273 1.00 24.12  ? 2469 VAL A C     1 
ATOM   7272  O  O     . VAL A 1 2469 ? 171.237 222.758 186.911 1.00 27.14  ? 2469 VAL A O     1 
ATOM   7273  C  CB    . VAL A 1 2469 ? 173.405 221.225 184.915 1.00 22.22  ? 2469 VAL A CB    1 
ATOM   7274  C  CG1   . VAL A 1 2469 ? 173.597 222.723 184.756 1.00 23.89  ? 2469 VAL A CG1   1 
ATOM   7275  C  CG2   . VAL A 1 2469 ? 174.744 220.518 184.934 1.00 18.40  ? 2469 VAL A CG2   1 
ATOM   7276  N  N     . ALA A 1 2470 ? 170.273 221.192 185.614 1.00 24.60  ? 2470 ALA A N     1 
ATOM   7277  C  CA    . ALA A 1 2470 ? 168.971 221.852 185.671 1.00 22.05  ? 2470 ALA A CA    1 
ATOM   7278  C  C     . ALA A 1 2470 ? 168.423 221.876 187.093 1.00 28.56  ? 2470 ALA A C     1 
ATOM   7279  O  O     . ALA A 1 2470 ? 167.857 222.884 187.533 1.00 33.55  ? 2470 ALA A O     1 
ATOM   7280  C  CB    . ALA A 1 2470 ? 167.989 221.157 184.732 1.00 17.72  ? 2470 ALA A CB    1 
ATOM   7281  N  N     . GLN A 1 2471 ? 168.572 220.769 187.823 1.00 35.34  ? 2471 GLN A N     1 
ATOM   7282  C  CA    . GLN A 1 2471 ? 168.122 220.723 189.210 1.00 34.47  ? 2471 GLN A CA    1 
ATOM   7283  C  C     . GLN A 1 2471 ? 168.917 221.688 190.079 1.00 34.04  ? 2471 GLN A C     1 
ATOM   7284  O  O     . GLN A 1 2471 ? 168.359 222.318 190.984 1.00 43.50  ? 2471 GLN A O     1 
ATOM   7285  C  CB    . GLN A 1 2471 ? 168.230 219.299 189.753 1.00 37.80  ? 2471 GLN A CB    1 
ATOM   7286  C  CG    . GLN A 1 2471 ? 167.562 219.100 191.104 1.00 42.39  ? 2471 GLN A CG    1 
ATOM   7287  C  CD    . GLN A 1 2471 ? 167.457 217.640 191.496 1.00 54.04  ? 2471 GLN A CD    1 
ATOM   7288  O  OE1   . GLN A 1 2471 ? 168.309 216.827 191.139 1.00 54.01  ? 2471 GLN A OE1   1 
ATOM   7289  N  NE2   . GLN A 1 2471 ? 166.410 217.301 192.236 1.00 56.68  ? 2471 GLN A NE2   1 
ATOM   7290  N  N     . TYR A 1 2472 ? 170.223 221.805 189.831 1.00 30.23  ? 2472 TYR A N     1 
ATOM   7291  C  CA    . TYR A 1 2472 ? 171.027 222.784 190.555 1.00 31.44  ? 2472 TYR A CA    1 
ATOM   7292  C  C     . TYR A 1 2472 ? 170.538 224.200 190.287 1.00 30.01  ? 2472 TYR A C     1 
ATOM   7293  O  O     . TYR A 1 2472 ? 170.445 225.019 191.208 1.00 35.31  ? 2472 TYR A O     1 
ATOM   7294  C  CB    . TYR A 1 2472 ? 172.498 222.651 190.165 1.00 34.52  ? 2472 TYR A CB    1 
ATOM   7295  C  CG    . TYR A 1 2472 ? 173.415 223.602 190.898 1.00 37.80  ? 2472 TYR A CG    1 
ATOM   7296  C  CD1   . TYR A 1 2472 ? 173.771 223.375 192.220 1.00 43.14  ? 2472 TYR A CD1   1 
ATOM   7297  C  CD2   . TYR A 1 2472 ? 173.919 224.733 190.272 1.00 37.00  ? 2472 TYR A CD2   1 
ATOM   7298  C  CE1   . TYR A 1 2472 ? 174.608 224.241 192.895 1.00 43.19  ? 2472 TYR A CE1   1 
ATOM   7299  C  CE2   . TYR A 1 2472 ? 174.756 225.606 190.938 1.00 39.70  ? 2472 TYR A CE2   1 
ATOM   7300  C  CZ    . TYR A 1 2472 ? 175.096 225.355 192.250 1.00 44.96  ? 2472 TYR A CZ    1 
ATOM   7301  O  OH    . TYR A 1 2472 ? 175.931 226.222 192.920 1.00 50.95  ? 2472 TYR A OH    1 
ATOM   7302  N  N     . ASN A 1 2473 ? 170.227 224.506 189.026 1.00 36.02  ? 2473 ASN A N     1 
ATOM   7303  C  CA    . ASN A 1 2473 ? 169.725 225.835 188.688 1.00 34.31  ? 2473 ASN A CA    1 
ATOM   7304  C  C     . ASN A 1 2473 ? 168.377 226.100 189.347 1.00 33.23  ? 2473 ASN A C     1 
ATOM   7305  O  O     . ASN A 1 2473 ? 168.111 227.215 189.810 1.00 34.08  ? 2473 ASN A O     1 
ATOM   7306  C  CB    . ASN A 1 2473 ? 169.621 225.988 187.172 1.00 30.63  ? 2473 ASN A CB    1 
ATOM   7307  C  CG    . ASN A 1 2473 ? 170.946 226.339 186.534 1.00 36.84  ? 2473 ASN A CG    1 
ATOM   7308  O  OD1   . ASN A 1 2473 ? 171.952 226.510 187.221 1.00 38.80  ? 2473 ASN A OD1   1 
ATOM   7309  N  ND2   . ASN A 1 2473 ? 170.954 226.452 185.212 1.00 44.19  ? 2473 ASN A ND2   1 
ATOM   7310  N  N     . ALA A 1 2474 ? 167.507 225.089 189.386 1.00 34.86  ? 2474 ALA A N     1 
ATOM   7311  C  CA    . ALA A 1 2474 ? 166.211 225.250 190.037 1.00 36.97  ? 2474 ALA A CA    1 
ATOM   7312  C  C     . ALA A 1 2474 ? 166.365 225.447 191.541 1.00 40.05  ? 2474 ALA A C     1 
ATOM   7313  O  O     . ALA A 1 2474 ? 165.637 226.241 192.147 1.00 42.88  ? 2474 ALA A O     1 
ATOM   7314  C  CB    . ALA A 1 2474 ? 165.320 224.045 189.740 1.00 30.63  ? 2474 ALA A CB    1 
ATOM   7315  N  N     . ASN A 1 2475 ? 167.304 224.729 192.160 1.00 38.80  ? 2475 ASN A N     1 
ATOM   7316  C  CA    . ASN A 1 2475 ? 167.528 224.853 193.595 1.00 40.24  ? 2475 ASN A CA    1 
ATOM   7317  C  C     . ASN A 1 2475 ? 168.150 226.190 193.974 1.00 43.08  ? 2475 ASN A C     1 
ATOM   7318  O  O     . ASN A 1 2475 ? 168.019 226.615 195.126 1.00 45.25  ? 2475 ASN A O     1 
ATOM   7319  C  CB    . ASN A 1 2475 ? 168.424 223.715 194.087 1.00 43.56  ? 2475 ASN A CB    1 
ATOM   7320  C  CG    . ASN A 1 2475 ? 167.639 222.477 194.468 1.00 52.07  ? 2475 ASN A CG    1 
ATOM   7321  O  OD1   . ASN A 1 2475 ? 166.429 222.536 194.689 1.00 58.85  ? 2475 ASN A OD1   1 
ATOM   7322  N  ND2   . ASN A 1 2475 ? 168.326 221.344 194.548 1.00 44.37  ? 2475 ASN A ND2   1 
ATOM   7323  N  N     . HIS A 1 2476 ? 168.819 226.859 193.037 1.00 42.88  ? 2476 HIS A N     1 
ATOM   7324  C  CA    . HIS A 1 2476 ? 169.510 228.122 193.294 1.00 44.49  ? 2476 HIS A CA    1 
ATOM   7325  C  C     . HIS A 1 2476 ? 169.016 229.165 192.300 1.00 54.28  ? 2476 HIS A C     1 
ATOM   7326  O  O     . HIS A 1 2476 ? 169.725 229.525 191.353 1.00 58.38  ? 2476 HIS A O     1 
ATOM   7327  C  CB    . HIS A 1 2476 ? 171.027 227.953 193.190 1.00 41.17  ? 2476 HIS A CB    1 
ATOM   7328  C  CG    . HIS A 1 2476 ? 171.623 227.110 194.275 1.00 47.08  ? 2476 HIS A CG    1 
ATOM   7329  N  ND1   . HIS A 1 2476 ? 171.146 225.858 194.596 1.00 42.32  ? 2476 HIS A ND1   1 
ATOM   7330  C  CD2   . HIS A 1 2476 ? 172.670 227.337 195.104 1.00 46.54  ? 2476 HIS A CD2   1 
ATOM   7331  C  CE1   . HIS A 1 2476 ? 171.867 225.353 195.581 1.00 43.28  ? 2476 HIS A CE1   1 
ATOM   7332  N  NE2   . HIS A 1 2476 ? 172.798 226.231 195.907 1.00 45.18  ? 2476 HIS A NE2   1 
ATOM   7333  N  N     . PRO A 1 2477 ? 167.790 229.664 192.481 1.00 52.93  ? 2477 PRO A N     1 
ATOM   7334  C  CA    . PRO A 1 2477 ? 167.273 230.677 191.548 1.00 52.86  ? 2477 PRO A CA    1 
ATOM   7335  C  C     . PRO A 1 2477 ? 168.096 231.952 191.526 1.00 63.77  ? 2477 PRO A C     1 
ATOM   7336  O  O     . PRO A 1 2477 ? 168.193 232.600 190.476 1.00 64.98  ? 2477 PRO A O     1 
ATOM   7337  C  CB    . PRO A 1 2477 ? 165.847 230.933 192.061 1.00 54.76  ? 2477 PRO A CB    1 
ATOM   7338  C  CG    . PRO A 1 2477 ? 165.530 229.766 192.953 1.00 52.29  ? 2477 PRO A CG    1 
ATOM   7339  C  CD    . PRO A 1 2477 ? 166.832 229.365 193.557 1.00 45.68  ? 2477 PRO A CD    1 
ATOM   7340  N  N     . ASP A 1 2478 ? 168.691 232.334 192.657 1.00 63.47  ? 2478 ASP A N     1 
ATOM   7341  C  CA    . ASP A 1 2478 ? 169.461 233.572 192.710 1.00 73.69  ? 2478 ASP A CA    1 
ATOM   7342  C  C     . ASP A 1 2478 ? 170.807 233.423 192.010 1.00 72.35  ? 2478 ASP A C     1 
ATOM   7343  O  O     . ASP A 1 2478 ? 171.283 234.362 191.362 1.00 70.75  ? 2478 ASP A O     1 
ATOM   7344  C  CB    . ASP A 1 2478 ? 169.656 234.000 194.165 1.00 82.20  ? 2478 ASP A CB    1 
ATOM   7345  C  CG    . ASP A 1 2478 ? 170.128 235.437 194.297 1.00 91.16  ? 2478 ASP A CG    1 
ATOM   7346  O  OD1   . ASP A 1 2478 ? 170.243 236.130 193.264 1.00 86.19  ? 2478 ASP A OD1   1 
ATOM   7347  O  OD2   . ASP A 1 2478 ? 170.383 235.874 195.438 1.00 96.85  ? 2478 ASP A OD2   1 
ATOM   7348  N  N     . PHE A 1 2479 ? 171.435 232.254 192.124 1.00 67.51  ? 2479 PHE A N     1 
ATOM   7349  C  CA    . PHE A 1 2479 ? 172.780 232.019 191.600 1.00 63.03  ? 2479 PHE A CA    1 
ATOM   7350  C  C     . PHE A 1 2479 ? 172.772 230.789 190.704 1.00 63.91  ? 2479 PHE A C     1 
ATOM   7351  O  O     . PHE A 1 2479 ? 173.110 229.681 191.145 1.00 62.03  ? 2479 PHE A O     1 
ATOM   7352  C  CB    . PHE A 1 2479 ? 173.793 231.864 192.734 1.00 67.11  ? 2479 PHE A CB    1 
ATOM   7353  C  CG    . PHE A 1 2479 ? 174.110 233.148 193.442 1.00 69.47  ? 2479 PHE A CG    1 
ATOM   7354  C  CD1   . PHE A 1 2479 ? 174.789 234.162 192.790 1.00 68.73  ? 2479 PHE A CD1   1 
ATOM   7355  C  CD2   . PHE A 1 2479 ? 173.727 233.342 194.757 1.00 74.06  ? 2479 PHE A CD2   1 
ATOM   7356  C  CE1   . PHE A 1 2479 ? 175.081 235.347 193.437 1.00 74.98  ? 2479 PHE A CE1   1 
ATOM   7357  C  CE2   . PHE A 1 2479 ? 174.017 234.525 195.410 1.00 74.69  ? 2479 PHE A CE2   1 
ATOM   7358  C  CZ    . PHE A 1 2479 ? 174.695 235.528 194.748 1.00 79.11  ? 2479 PHE A CZ    1 
ATOM   7359  N  N     . PRO A 1 2480 ? 172.391 230.945 189.439 1.00 60.83  ? 2480 PRO A N     1 
ATOM   7360  C  CA    . PRO A 1 2480 ? 172.462 229.820 188.503 1.00 55.16  ? 2480 PRO A CA    1 
ATOM   7361  C  C     . PRO A 1 2480 ? 173.904 229.426 188.224 1.00 51.95  ? 2480 PRO A C     1 
ATOM   7362  O  O     . PRO A 1 2480 ? 174.835 230.225 188.352 1.00 55.13  ? 2480 PRO A O     1 
ATOM   7363  C  CB    . PRO A 1 2480 ? 171.779 230.362 187.244 1.00 50.35  ? 2480 PRO A CB    1 
ATOM   7364  C  CG    . PRO A 1 2480 ? 171.986 231.835 187.320 1.00 57.84  ? 2480 PRO A CG    1 
ATOM   7365  C  CD    . PRO A 1 2480 ? 171.935 232.183 188.785 1.00 59.13  ? 2480 PRO A CD    1 
ATOM   7366  N  N     . MET A 1 2481 ? 174.078 228.161 187.849 1.00 43.62  ? 2481 MET A N     1 
ATOM   7367  C  CA    . MET A 1 2481 ? 175.409 227.636 187.576 1.00 41.39  ? 2481 MET A CA    1 
ATOM   7368  C  C     . MET A 1 2481 ? 176.056 228.393 186.424 1.00 46.10  ? 2481 MET A C     1 
ATOM   7369  O  O     . MET A 1 2481 ? 175.436 228.611 185.379 1.00 49.57  ? 2481 MET A O     1 
ATOM   7370  C  CB    . MET A 1 2481 ? 175.328 226.145 187.255 1.00 34.37  ? 2481 MET A CB    1 
ATOM   7371  C  CG    . MET A 1 2481 ? 176.673 225.446 187.222 1.00 33.76  ? 2481 MET A CG    1 
ATOM   7372  S  SD    . MET A 1 2481 ? 176.576 223.796 186.509 1.00 44.41  ? 2481 MET A SD    1 
ATOM   7373  C  CE    . MET A 1 2481 ? 176.351 222.806 187.982 1.00 34.31  ? 2481 MET A CE    1 
ATOM   7374  N  N     . GLN A 1 2482 ? 177.308 228.794 186.618 1.00 47.54  ? 2482 GLN A N     1 
ATOM   7375  C  CA    . GLN A 1 2482 ? 178.019 229.590 185.632 1.00 48.88  ? 2482 GLN A CA    1 
ATOM   7376  C  C     . GLN A 1 2482 ? 178.759 228.690 184.646 1.00 43.31  ? 2482 GLN A C     1 
ATOM   7377  O  O     . GLN A 1 2482 ? 178.791 227.465 184.780 1.00 42.90  ? 2482 GLN A O     1 
ATOM   7378  C  CB    . GLN A 1 2482 ? 178.989 230.552 186.321 1.00 50.03  ? 2482 GLN A CB    1 
ATOM   7379  C  CG    . GLN A 1 2482 ? 178.360 231.507 187.350 1.00 52.57  ? 2482 GLN A CG    1 
ATOM   7380  C  CD    . GLN A 1 2482 ? 177.108 232.245 186.875 1.00 53.30  ? 2482 GLN A CD    1 
ATOM   7381  O  OE1   . GLN A 1 2482 ? 176.763 232.246 185.693 1.00 50.74  ? 2482 GLN A OE1   1 
ATOM   7382  N  NE2   . GLN A 1 2482 ? 176.418 232.878 187.817 1.00 52.63  ? 2482 GLN A NE2   1 
ATOM   7383  N  N     . ILE A 1 2483 ? 179.363 229.322 183.637 1.00 43.99  ? 2483 ILE A N     1 
ATOM   7384  C  CA    . ILE A 1 2483 ? 179.967 228.570 182.543 1.00 41.12  ? 2483 ILE A CA    1 
ATOM   7385  C  C     . ILE A 1 2483 ? 181.202 227.802 183.006 1.00 41.92  ? 2483 ILE A C     1 
ATOM   7386  O  O     . ILE A 1 2483 ? 181.466 226.698 182.519 1.00 40.11  ? 2483 ILE A O     1 
ATOM   7387  C  CB    . ILE A 1 2483 ? 180.279 229.508 181.360 1.00 43.16  ? 2483 ILE A CB    1 
ATOM   7388  C  CG1   . ILE A 1 2483 ? 180.614 228.696 180.107 1.00 48.07  ? 2483 ILE A CG1   1 
ATOM   7389  C  CG2   . ILE A 1 2483 ? 181.398 230.485 181.703 1.00 44.66  ? 2483 ILE A CG2   1 
ATOM   7390  C  CD1   . ILE A 1 2483 ? 179.448 227.889 179.577 1.00 35.54  ? 2483 ILE A CD1   1 
ATOM   7391  N  N     . GLU A 1 2484 ? 181.973 228.353 183.946 1.00 39.07  ? 2484 GLU A N     1 
ATOM   7392  C  CA    . GLU A 1 2484 ? 183.181 227.670 184.405 1.00 40.66  ? 2484 GLU A CA    1 
ATOM   7393  C  C     . GLU A 1 2484 ? 182.837 226.455 185.260 1.00 42.77  ? 2484 GLU A C     1 
ATOM   7394  O  O     . GLU A 1 2484 ? 183.410 225.369 185.082 1.00 40.03  ? 2484 GLU A O     1 
ATOM   7395  C  CB    . GLU A 1 2484 ? 184.064 228.647 185.181 1.00 42.08  ? 2484 GLU A CB    1 
ATOM   7396  C  CG    . GLU A 1 2484 ? 184.651 229.758 184.325 1.00 56.47  ? 2484 GLU A CG    1 
ATOM   7397  C  CD    . GLU A 1 2484 ? 185.505 230.722 185.124 1.00 70.15  ? 2484 GLU A CD    1 
ATOM   7398  O  OE1   . GLU A 1 2484 ? 185.541 230.598 186.366 1.00 71.04  ? 2484 GLU A OE1   1 
ATOM   7399  O  OE2   . GLU A 1 2484 ? 186.142 231.604 184.510 1.00 67.31  ? 2484 GLU A OE2   1 
ATOM   7400  N  N     . GLN A 1 2485 ? 181.901 226.622 186.197 1.00 44.33  ? 2485 GLN A N     1 
ATOM   7401  C  CA    . GLN A 1 2485 ? 181.452 225.493 187.004 1.00 39.11  ? 2485 GLN A CA    1 
ATOM   7402  C  C     . GLN A 1 2485 ? 180.803 224.430 186.132 1.00 38.52  ? 2485 GLN A C     1 
ATOM   7403  O  O     . GLN A 1 2485 ? 181.034 223.230 186.324 1.00 41.31  ? 2485 GLN A O     1 
ATOM   7404  C  CB    . GLN A 1 2485 ? 180.477 225.972 188.078 1.00 33.78  ? 2485 GLN A CB    1 
ATOM   7405  C  CG    . GLN A 1 2485 ? 180.249 224.977 189.200 1.00 40.11  ? 2485 GLN A CG    1 
ATOM   7406  C  CD    . GLN A 1 2485 ? 179.066 225.346 190.071 1.00 41.97  ? 2485 GLN A CD    1 
ATOM   7407  O  OE1   . GLN A 1 2485 ? 178.262 224.491 190.440 1.00 36.42  ? 2485 GLN A OE1   1 
ATOM   7408  N  NE2   . GLN A 1 2485 ? 178.951 226.627 190.399 1.00 40.31  ? 2485 GLN A NE2   1 
ATOM   7409  N  N     . LEU A 1 2486 ? 179.993 224.856 185.160 1.00 35.25  ? 2486 LEU A N     1 
ATOM   7410  C  CA    . LEU A 1 2486 ? 179.373 223.910 184.242 1.00 31.88  ? 2486 LEU A CA    1 
ATOM   7411  C  C     . LEU A 1 2486 ? 180.425 223.162 183.437 1.00 28.40  ? 2486 LEU A C     1 
ATOM   7412  O  O     . LEU A 1 2486 ? 180.304 221.953 183.222 1.00 30.11  ? 2486 LEU A O     1 
ATOM   7413  C  CB    . LEU A 1 2486 ? 178.401 224.637 183.314 1.00 26.74  ? 2486 LEU A CB    1 
ATOM   7414  C  CG    . LEU A 1 2486 ? 177.691 223.780 182.266 1.00 24.98  ? 2486 LEU A CG    1 
ATOM   7415  C  CD1   . LEU A 1 2486 ? 176.914 222.662 182.932 1.00 29.40  ? 2486 LEU A CD1   1 
ATOM   7416  C  CD2   . LEU A 1 2486 ? 176.776 224.630 181.404 1.00 27.41  ? 2486 LEU A CD2   1 
ATOM   7417  N  N     . GLU A 1 2487 ? 181.468 223.862 182.989 1.00 27.38  ? 2487 GLU A N     1 
ATOM   7418  C  CA    . GLU A 1 2487 ? 182.517 223.214 182.210 1.00 31.14  ? 2487 GLU A CA    1 
ATOM   7419  C  C     . GLU A 1 2487 ? 183.244 222.163 183.037 1.00 28.52  ? 2487 GLU A C     1 
ATOM   7420  O  O     . GLU A 1 2487 ? 183.448 221.029 182.584 1.00 30.38  ? 2487 GLU A O     1 
ATOM   7421  C  CB    . GLU A 1 2487 ? 183.496 224.263 181.683 1.00 32.09  ? 2487 GLU A CB    1 
ATOM   7422  C  CG    . GLU A 1 2487 ? 184.767 223.687 181.092 1.00 31.79  ? 2487 GLU A CG    1 
ATOM   7423  C  CD    . GLU A 1 2487 ? 185.405 224.616 180.081 1.00 52.80  ? 2487 GLU A CD    1 
ATOM   7424  O  OE1   . GLU A 1 2487 ? 184.703 225.519 179.578 1.00 47.20  ? 2487 GLU A OE1   1 
ATOM   7425  O  OE2   . GLU A 1 2487 ? 186.608 224.446 179.790 1.00 58.06  ? 2487 GLU A OE2   1 
ATOM   7426  N  N     . ARG A 1 2488 ? 183.638 222.522 184.262 1.00 32.27  ? 2488 ARG A N     1 
ATOM   7427  C  CA    . ARG A 1 2488 ? 184.332 221.565 185.119 1.00 25.22  ? 2488 ARG A CA    1 
ATOM   7428  C  C     . ARG A 1 2488 ? 183.451 220.357 185.414 1.00 26.63  ? 2488 ARG A C     1 
ATOM   7429  O  O     . ARG A 1 2488 ? 183.897 219.203 185.315 1.00 25.65  ? 2488 ARG A O     1 
ATOM   7430  C  CB    . ARG A 1 2488 ? 184.768 222.238 186.420 1.00 28.40  ? 2488 ARG A CB    1 
ATOM   7431  C  CG    . ARG A 1 2488 ? 185.859 223.278 186.258 1.00 40.43  ? 2488 ARG A CG    1 
ATOM   7432  C  CD    . ARG A 1 2488 ? 186.375 223.738 187.612 1.00 39.31  ? 2488 ARG A CD    1 
ATOM   7433  N  NE    . ARG A 1 2488 ? 185.343 224.410 188.392 1.00 45.83  ? 2488 ARG A NE    1 
ATOM   7434  C  CZ    . ARG A 1 2488 ? 185.085 225.709 188.332 1.00 51.55  ? 2488 ARG A CZ    1 
ATOM   7435  N  NH1   . ARG A 1 2488 ? 185.773 226.515 187.540 1.00 50.20  ? 2488 ARG A NH1   1 
ATOM   7436  N  NH2   . ARG A 1 2488 ? 184.113 226.213 189.087 1.00 42.42  ? 2488 ARG A NH2   1 
ATOM   7437  N  N     . TYR A 1 2489 ? 182.185 220.607 185.762 1.00 25.45  ? 2489 TYR A N     1 
ATOM   7438  C  CA    . TYR A 1 2489 ? 181.276 219.515 186.081 1.00 17.74  ? 2489 TYR A CA    1 
ATOM   7439  C  C     . TYR A 1 2489 ? 181.063 218.608 184.879 1.00 18.62  ? 2489 TYR A C     1 
ATOM   7440  O  O     . TYR A 1 2489 ? 181.083 217.381 185.012 1.00 19.87  ? 2489 TYR A O     1 
ATOM   7441  C  CB    . TYR A 1 2489 ? 179.940 220.067 186.573 1.00 16.09  ? 2489 TYR A CB    1 
ATOM   7442  C  CG    . TYR A 1 2489 ? 178.910 218.995 186.840 1.00 21.66  ? 2489 TYR A CG    1 
ATOM   7443  C  CD1   . TYR A 1 2489 ? 179.123 218.032 187.816 1.00 24.04  ? 2489 TYR A CD1   1 
ATOM   7444  C  CD2   . TYR A 1 2489 ? 177.733 218.936 186.109 1.00 18.36  ? 2489 TYR A CD2   1 
ATOM   7445  C  CE1   . TYR A 1 2489 ? 178.189 217.046 188.063 1.00 18.12  ? 2489 TYR A CE1   1 
ATOM   7446  C  CE2   . TYR A 1 2489 ? 176.795 217.955 186.348 1.00 16.96  ? 2489 TYR A CE2   1 
ATOM   7447  C  CZ    . TYR A 1 2489 ? 177.028 217.012 187.326 1.00 20.85  ? 2489 TYR A CZ    1 
ATOM   7448  O  OH    . TYR A 1 2489 ? 176.094 216.032 187.568 1.00 26.58  ? 2489 TYR A OH    1 
ATOM   7449  N  N     . ILE A 1 2490 ? 180.874 219.191 183.694 1.00 18.38  ? 2490 ILE A N     1 
ATOM   7450  C  CA    . ILE A 1 2490 ? 180.599 218.390 182.508 1.00 14.80  ? 2490 ILE A CA    1 
ATOM   7451  C  C     . ILE A 1 2490 ? 181.816 217.560 182.127 1.00 15.28  ? 2490 ILE A C     1 
ATOM   7452  O  O     . ILE A 1 2490 ? 181.685 216.386 181.773 1.00 15.25  ? 2490 ILE A O     1 
ATOM   7453  C  CB    . ILE A 1 2490 ? 180.127 219.288 181.351 1.00 19.09  ? 2490 ILE A CB    1 
ATOM   7454  C  CG1   . ILE A 1 2490 ? 178.689 219.748 181.593 1.00 17.18  ? 2490 ILE A CG1   1 
ATOM   7455  C  CG2   . ILE A 1 2490 ? 180.215 218.552 180.023 1.00 15.29  ? 2490 ILE A CG2   1 
ATOM   7456  C  CD1   . ILE A 1 2490 ? 177.718 218.619 181.843 1.00 15.68  ? 2490 ILE A CD1   1 
ATOM   7457  N  N     . GLN A 1 2491 ? 183.018 218.136 182.208 1.00 14.69  ? 2491 GLN A N     1 
ATOM   7458  C  CA    . GLN A 1 2491 ? 184.214 217.370 181.862 1.00 13.02  ? 2491 GLN A CA    1 
ATOM   7459  C  C     . GLN A 1 2491 ? 184.429 216.210 182.831 1.00 16.57  ? 2491 GLN A C     1 
ATOM   7460  O  O     . GLN A 1 2491 ? 184.659 215.061 182.413 1.00 18.50  ? 2491 GLN A O     1 
ATOM   7461  C  CB    . GLN A 1 2491 ? 185.438 218.286 181.837 1.00 16.43  ? 2491 GLN A CB    1 
ATOM   7462  C  CG    . GLN A 1 2491 ? 185.461 219.261 180.674 1.00 19.99  ? 2491 GLN A CG    1 
ATOM   7463  C  CD    . GLN A 1 2491 ? 186.666 220.176 180.707 1.00 26.98  ? 2491 GLN A CD    1 
ATOM   7464  O  OE1   . GLN A 1 2491 ? 187.480 220.116 181.627 1.00 30.82  ? 2491 GLN A OE1   1 
ATOM   7465  N  NE2   . GLN A 1 2491 ? 186.787 221.032 179.700 1.00 29.37  ? 2491 GLN A NE2   1 
ATOM   7466  N  N     . ARG A 1 2492 ? 184.353 216.489 184.136 1.00 16.77  ? 2492 ARG A N     1 
ATOM   7467  C  CA    . ARG A 1 2492 ? 184.567 215.427 185.113 1.00 15.12  ? 2492 ARG A CA    1 
ATOM   7468  C  C     . ARG A 1 2492 ? 183.489 214.356 185.008 1.00 12.92  ? 2492 ARG A C     1 
ATOM   7469  O  O     . ARG A 1 2492 ? 183.783 213.157 185.092 1.00 13.72  ? 2492 ARG A O     1 
ATOM   7470  C  CB    . ARG A 1 2492 ? 184.621 216.015 186.522 1.00 20.66  ? 2492 ARG A CB    1 
ATOM   7471  C  CG    . ARG A 1 2492 ? 185.895 216.788 186.814 1.00 20.96  ? 2492 ARG A CG    1 
ATOM   7472  C  CD    . ARG A 1 2492 ? 185.694 217.770 187.953 1.00 30.67  ? 2492 ARG A CD    1 
ATOM   7473  N  NE    . ARG A 1 2492 ? 186.933 218.430 188.344 1.00 32.98  ? 2492 ARG A NE    1 
ATOM   7474  C  CZ    . ARG A 1 2492 ? 187.530 219.386 187.645 1.00 31.53  ? 2492 ARG A CZ    1 
ATOM   7475  N  NH1   . ARG A 1 2492 ? 187.032 219.817 186.498 1.00 32.13  ? 2492 ARG A NH1   1 
ATOM   7476  N  NH2   . ARG A 1 2492 ? 188.654 219.923 188.108 1.00 34.91  ? 2492 ARG A NH2   1 
ATOM   7477  N  N     . TYR A 1 2493 ? 182.234 214.766 184.806 1.00 11.30  ? 2493 TYR A N     1 
ATOM   7478  C  CA    . TYR A 1 2493 ? 181.159 213.796 184.666 1.00 12.08  ? 2493 TYR A CA    1 
ATOM   7479  C  C     . TYR A 1 2493 ? 181.284 213.010 183.373 1.00 10.86  ? 2493 TYR A C     1 
ATOM   7480  O  O     . TYR A 1 2493 ? 180.869 211.853 183.320 1.00 13.25  ? 2493 TYR A O     1 
ATOM   7481  C  CB    . TYR A 1 2493 ? 179.801 214.494 184.730 1.00 12.87  ? 2493 TYR A CB    1 
ATOM   7482  C  CG    . TYR A 1 2493 ? 178.664 213.566 185.086 1.00 10.19  ? 2493 TYR A CG    1 
ATOM   7483  C  CD1   . TYR A 1 2493 ? 178.063 212.770 184.122 1.00 8.43   ? 2493 TYR A CD1   1 
ATOM   7484  C  CD2   . TYR A 1 2493 ? 178.191 213.486 186.387 1.00 13.14  ? 2493 TYR A CD2   1 
ATOM   7485  C  CE1   . TYR A 1 2493 ? 177.028 211.921 184.443 1.00 10.65  ? 2493 TYR A CE1   1 
ATOM   7486  C  CE2   . TYR A 1 2493 ? 177.153 212.642 186.717 1.00 16.15  ? 2493 TYR A CE2   1 
ATOM   7487  C  CZ    . TYR A 1 2493 ? 176.575 211.861 185.741 1.00 16.75  ? 2493 TYR A CZ    1 
ATOM   7488  O  OH    . TYR A 1 2493 ? 175.540 211.016 186.064 1.00 16.85  ? 2493 TYR A OH    1 
ATOM   7489  N  N     . LEU A 1 2494 ? 181.839 213.612 182.321 1.00 11.64  ? 2494 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2494 ? 182.087 212.863 181.098 1.00 10.71  ? 2494 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2494 ? 183.111 211.766 181.336 1.00 10.00  ? 2494 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2494 ? 182.931 210.631 180.881 1.00 11.27  ? 2494 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2494 ? 182.549 213.807 179.990 1.00 12.11  ? 2494 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2494 ? 182.966 213.172 178.664 1.00 13.32  ? 2494 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2494 ? 181.853 212.303 178.104 1.00 12.26  ? 2494 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2494 ? 183.342 214.252 177.676 1.00 14.16  ? 2494 LEU A CD2   1 
ATOM   7497  N  N     . VAL A 1 2495 ? 184.184 212.079 182.065 1.00 10.72  ? 2495 VAL A N     1 
ATOM   7498  C  CA    . VAL A 1 2495 ? 185.156 211.038 182.406 1.00 10.21  ? 2495 VAL A CA    1 
ATOM   7499  C  C     . VAL A 1 2495 ? 184.498 209.945 183.245 1.00 10.83  ? 2495 VAL A C     1 
ATOM   7500  O  O     . VAL A 1 2495 ? 184.681 208.744 182.994 1.00 10.12  ? 2495 VAL A O     1 
ATOM   7501  C  CB    . VAL A 1 2495 ? 186.370 211.651 183.125 1.00 12.64  ? 2495 VAL A CB    1 
ATOM   7502  C  CG1   . VAL A 1 2495 ? 187.285 210.555 183.648 1.00 13.63  ? 2495 VAL A CG1   1 
ATOM   7503  C  CG2   . VAL A 1 2495 ? 187.126 212.574 182.188 1.00 14.44  ? 2495 VAL A CG2   1 
ATOM   7504  N  N     . TYR A 1 2496 ? 183.709 210.348 184.244 1.00 13.23  ? 2496 TYR A N     1 
ATOM   7505  C  CA    . TYR A 1 2496 ? 183.034 209.395 185.122 1.00 11.11  ? 2496 TYR A CA    1 
ATOM   7506  C  C     . TYR A 1 2496 ? 182.074 208.498 184.344 1.00 10.81  ? 2496 TYR A C     1 
ATOM   7507  O  O     . TYR A 1 2496 ? 182.031 207.278 184.557 1.00 11.25  ? 2496 TYR A O     1 
ATOM   7508  C  CB    . TYR A 1 2496 ? 182.312 210.177 186.224 1.00 9.29   ? 2496 TYR A CB    1 
ATOM   7509  C  CG    . TYR A 1 2496 ? 181.202 209.464 186.962 1.00 13.78  ? 2496 TYR A CG    1 
ATOM   7510  C  CD1   . TYR A 1 2496 ? 179.884 209.571 186.539 1.00 12.33  ? 2496 TYR A CD1   1 
ATOM   7511  C  CD2   . TYR A 1 2496 ? 181.463 208.727 188.107 1.00 15.72  ? 2496 TYR A CD2   1 
ATOM   7512  C  CE1   . TYR A 1 2496 ? 178.863 208.941 187.218 1.00 12.16  ? 2496 TYR A CE1   1 
ATOM   7513  C  CE2   . TYR A 1 2496 ? 180.447 208.094 188.796 1.00 14.39  ? 2496 TYR A CE2   1 
ATOM   7514  C  CZ    . TYR A 1 2496 ? 179.149 208.203 188.344 1.00 15.16  ? 2496 TYR A CZ    1 
ATOM   7515  O  OH    . TYR A 1 2496 ? 178.130 207.575 189.021 1.00 19.12  ? 2496 TYR A OH    1 
ATOM   7516  N  N     . ALA A 1 2497 ? 181.311 209.085 183.421 1.00 10.31  ? 2497 ALA A N     1 
ATOM   7517  C  CA    . ALA A 1 2497 ? 180.345 208.324 182.642 1.00 10.37  ? 2497 ALA A CA    1 
ATOM   7518  C  C     . ALA A 1 2497 ? 181.036 207.407 181.645 1.00 10.06  ? 2497 ALA A C     1 
ATOM   7519  O  O     . ALA A 1 2497 ? 180.561 206.297 181.392 1.00 12.24  ? 2497 ALA A O     1 
ATOM   7520  C  CB    . ALA A 1 2497 ? 179.386 209.274 181.927 1.00 12.70  ? 2497 ALA A CB    1 
ATOM   7521  N  N     . ILE A 1 2498 ? 182.158 207.846 181.070 1.00 9.39   ? 2498 ILE A N     1 
ATOM   7522  C  CA    . ILE A 1 2498 ? 182.936 206.957 180.215 1.00 8.66   ? 2498 ILE A CA    1 
ATOM   7523  C  C     . ILE A 1 2498 ? 183.400 205.747 181.009 1.00 8.79   ? 2498 ILE A C     1 
ATOM   7524  O  O     . ILE A 1 2498 ? 183.280 204.601 180.556 1.00 9.53   ? 2498 ILE A O     1 
ATOM   7525  C  CB    . ILE A 1 2498 ? 184.125 207.713 179.593 1.00 8.99   ? 2498 ILE A CB    1 
ATOM   7526  C  CG1   . ILE A 1 2498 ? 183.649 208.663 178.496 1.00 11.33  ? 2498 ILE A CG1   1 
ATOM   7527  C  CG2   . ILE A 1 2498 ? 185.142 206.738 179.029 1.00 11.24  ? 2498 ILE A CG2   1 
ATOM   7528  C  CD1   . ILE A 1 2498 ? 184.747 209.539 177.946 1.00 12.64  ? 2498 ILE A CD1   1 
ATOM   7529  N  N     . LEU A 1 2499 ? 183.911 205.981 182.220 1.00 10.27  ? 2499 LEU A N     1 
ATOM   7530  C  CA    . LEU A 1 2499 ? 184.382 204.876 183.048 1.00 8.42   ? 2499 LEU A CA    1 
ATOM   7531  C  C     . LEU A 1 2499 ? 183.253 203.908 183.378 1.00 9.62   ? 2499 LEU A C     1 
ATOM   7532  O  O     . LEU A 1 2499 ? 183.425 202.686 183.301 1.00 11.21  ? 2499 LEU A O     1 
ATOM   7533  C  CB    . LEU A 1 2499 ? 185.016 205.413 184.328 1.00 10.83  ? 2499 LEU A CB    1 
ATOM   7534  C  CG    . LEU A 1 2499 ? 186.515 205.678 184.240 1.00 18.04  ? 2499 LEU A CG    1 
ATOM   7535  C  CD1   . LEU A 1 2499 ? 187.006 206.290 185.530 1.00 20.32  ? 2499 LEU A CD1   1 
ATOM   7536  C  CD2   . LEU A 1 2499 ? 187.257 204.391 183.930 1.00 19.35  ? 2499 LEU A CD2   1 
ATOM   7537  N  N     . TRP A 1 2500 ? 182.086 204.434 183.748 1.00 9.72   ? 2500 TRP A N     1 
ATOM   7538  C  CA    . TRP A 1 2500 ? 181.000 203.557 184.174 1.00 9.23   ? 2500 TRP A CA    1 
ATOM   7539  C  C     . TRP A 1 2500 ? 180.231 202.940 183.013 1.00 8.40   ? 2500 TRP A C     1 
ATOM   7540  O  O     . TRP A 1 2500 ? 179.512 201.958 183.221 1.00 11.68  ? 2500 TRP A O     1 
ATOM   7541  C  CB    . TRP A 1 2500 ? 180.036 204.314 185.086 1.00 9.50   ? 2500 TRP A CB    1 
ATOM   7542  C  CG    . TRP A 1 2500 ? 180.418 204.216 186.524 1.00 9.58   ? 2500 TRP A CG    1 
ATOM   7543  C  CD1   . TRP A 1 2500 ? 180.792 205.238 187.338 1.00 10.74  ? 2500 TRP A CD1   1 
ATOM   7544  C  CD2   . TRP A 1 2500 ? 180.481 203.025 187.317 1.00 13.29  ? 2500 TRP A CD2   1 
ATOM   7545  N  NE1   . TRP A 1 2500 ? 181.078 204.764 188.594 1.00 14.62  ? 2500 TRP A NE1   1 
ATOM   7546  C  CE2   . TRP A 1 2500 ? 180.895 203.407 188.607 1.00 13.95  ? 2500 TRP A CE2   1 
ATOM   7547  C  CE3   . TRP A 1 2500 ? 180.223 201.675 187.063 1.00 10.05  ? 2500 TRP A CE3   1 
ATOM   7548  C  CZ2   . TRP A 1 2500 ? 181.058 202.489 189.640 1.00 14.46  ? 2500 TRP A CZ2   1 
ATOM   7549  C  CZ3   . TRP A 1 2500 ? 180.386 200.766 188.090 1.00 12.74  ? 2500 TRP A CZ3   1 
ATOM   7550  C  CH2   . TRP A 1 2500 ? 180.799 201.176 189.362 1.00 15.11  ? 2500 TRP A CH2   1 
ATOM   7551  N  N     . SER A 1 2501 ? 180.365 203.478 181.802 1.00 8.88   ? 2501 SER A N     1 
ATOM   7552  C  CA    . SER A 1 2501 ? 179.657 202.935 180.652 1.00 7.59   ? 2501 SER A CA    1 
ATOM   7553  C  C     . SER A 1 2501 ? 180.512 201.959 179.860 1.00 8.14   ? 2501 SER A C     1 
ATOM   7554  O  O     . SER A 1 2501 ? 179.980 201.040 179.229 1.00 10.79  ? 2501 SER A O     1 
ATOM   7555  C  CB    . SER A 1 2501 ? 179.192 204.071 179.740 1.00 7.64   ? 2501 SER A CB    1 
ATOM   7556  O  OG    . SER A 1 2501 ? 178.361 204.976 180.442 1.00 11.51  ? 2501 SER A OG    1 
ATOM   7557  N  N     . LEU A 1 2502 ? 181.828 202.144 179.875 1.00 6.74   ? 2502 LEU A N     1 
ATOM   7558  C  CA    . LEU A 1 2502 ? 182.730 201.287 179.125 1.00 7.17   ? 2502 LEU A CA    1 
ATOM   7559  C  C     . LEU A 1 2502 ? 183.325 200.165 179.962 1.00 8.29   ? 2502 LEU A C     1 
ATOM   7560  O  O     . LEU A 1 2502 ? 183.942 199.254 179.399 1.00 15.59  ? 2502 LEU A O     1 
ATOM   7561  C  CB    . LEU A 1 2502 ? 183.850 202.133 178.512 1.00 12.21  ? 2502 LEU A CB    1 
ATOM   7562  C  CG    . LEU A 1 2502 ? 183.516 202.921 177.242 1.00 6.84   ? 2502 LEU A CG    1 
ATOM   7563  C  CD1   . LEU A 1 2502 ? 182.572 204.082 177.494 1.00 10.51  ? 2502 LEU A CD1   1 
ATOM   7564  C  CD2   . LEU A 1 2502 ? 184.801 203.450 176.683 1.00 10.17  ? 2502 LEU A CD2   1 
ATOM   7565  N  N     . SER A 1 2503 ? 183.155 200.202 181.287 1.00 9.03   ? 2503 SER A N     1 
ATOM   7566  C  CA    . SER A 1 2503 ? 183.670 199.141 182.145 1.00 6.97   ? 2503 SER A CA    1 
ATOM   7567  C  C     . SER A 1 2503 ? 182.693 198.769 183.256 1.00 6.79   ? 2503 SER A C     1 
ATOM   7568  O  O     . SER A 1 2503 ? 183.094 198.119 184.227 1.00 8.14   ? 2503 SER A O     1 
ATOM   7569  C  CB    . SER A 1 2503 ? 185.014 199.538 182.762 1.00 7.70   ? 2503 SER A CB    1 
ATOM   7570  O  OG    . SER A 1 2503 ? 184.846 200.538 183.750 1.00 10.57  ? 2503 SER A OG    1 
ATOM   7571  N  N     . GLY A 1 2504 ? 181.422 199.159 183.139 1.00 5.78   ? 2504 GLY A N     1 
ATOM   7572  C  CA    . GLY A 1 2504 ? 180.463 198.834 184.179 1.00 6.93   ? 2504 GLY A CA    1 
ATOM   7573  C  C     . GLY A 1 2504 ? 180.130 197.359 184.249 1.00 7.40   ? 2504 GLY A C     1 
ATOM   7574  O  O     . GLY A 1 2504 ? 179.687 196.869 185.291 1.00 8.36   ? 2504 GLY A O     1 
ATOM   7575  N  N     . ASP A 1 2505 ? 180.340 196.631 183.152 1.00 8.09   ? 2505 ASP A N     1 
ATOM   7576  C  CA    . ASP A 1 2505 ? 180.070 195.201 183.085 1.00 8.28   ? 2505 ASP A CA    1 
ATOM   7577  C  C     . ASP A 1 2505 ? 181.330 194.366 183.275 1.00 8.01   ? 2505 ASP A C     1 
ATOM   7578  O  O     . ASP A 1 2505 ? 181.378 193.207 182.850 1.00 11.45  ? 2505 ASP A O     1 
ATOM   7579  C  CB    . ASP A 1 2505 ? 179.404 194.852 181.756 1.00 9.80   ? 2505 ASP A CB    1 
ATOM   7580  C  CG    . ASP A 1 2505 ? 180.180 195.373 180.563 1.00 15.75  ? 2505 ASP A CG    1 
ATOM   7581  O  OD1   . ASP A 1 2505 ? 181.003 196.294 180.742 1.00 13.98  ? 2505 ASP A OD1   1 
ATOM   7582  O  OD2   . ASP A 1 2505 ? 179.969 194.857 179.445 1.00 19.26  ? 2505 ASP A OD2   1 
ATOM   7583  N  N     . SER A 1 2506 ? 182.355 194.930 183.906 1.00 8.33   ? 2506 SER A N     1 
ATOM   7584  C  CA    . SER A 1 2506 ? 183.632 194.257 184.066 1.00 12.20  ? 2506 SER A CA    1 
ATOM   7585  C  C     . SER A 1 2506 ? 184.013 194.209 185.539 1.00 11.35  ? 2506 SER A C     1 
ATOM   7586  O  O     . SER A 1 2506 ? 183.410 194.876 186.382 1.00 13.47  ? 2506 SER A O     1 
ATOM   7587  C  CB    . SER A 1 2506 ? 184.734 194.952 183.258 1.00 12.68  ? 2506 SER A CB    1 
ATOM   7588  O  OG    . SER A 1 2506 ? 184.704 196.352 183.456 1.00 11.71  ? 2506 SER A OG    1 
ATOM   7589  N  N     . ARG A 1 2507 ? 185.029 193.404 185.837 1.00 13.79  ? 2507 ARG A N     1 
ATOM   7590  C  CA    . ARG A 1 2507 ? 185.495 193.242 187.204 1.00 11.24  ? 2507 ARG A CA    1 
ATOM   7591  C  C     . ARG A 1 2507 ? 186.309 194.460 187.638 1.00 15.22  ? 2507 ARG A C     1 
ATOM   7592  O  O     . ARG A 1 2507 ? 186.508 195.416 186.885 1.00 21.78  ? 2507 ARG A O     1 
ATOM   7593  C  CB    . ARG A 1 2507 ? 186.307 191.956 187.336 1.00 11.27  ? 2507 ARG A CB    1 
ATOM   7594  C  CG    . ARG A 1 2507 ? 185.712 190.781 186.584 1.00 15.92  ? 2507 ARG A CG    1 
ATOM   7595  C  CD    . ARG A 1 2507 ? 186.672 189.610 186.521 1.00 28.08  ? 2507 ARG A CD    1 
ATOM   7596  N  NE    . ARG A 1 2507 ? 188.061 190.039 186.422 1.00 32.23  ? 2507 ARG A NE    1 
ATOM   7597  C  CZ    . ARG A 1 2507 ? 189.093 189.211 186.345 1.00 45.39  ? 2507 ARG A CZ    1 
ATOM   7598  N  NH1   . ARG A 1 2507 ? 188.929 187.899 186.361 1.00 41.30  ? 2507 ARG A NH1   1 
ATOM   7599  N  NH2   . ARG A 1 2507 ? 190.321 189.712 186.250 1.00 42.12  ? 2507 ARG A NH2   1 
ATOM   7600  N  N     . LEU A 1 2508 ? 186.780 194.417 188.885 1.00 15.80  ? 2508 LEU A N     1 
ATOM   7601  C  CA    . LEU A 1 2508 ? 187.483 195.560 189.460 1.00 20.67  ? 2508 LEU A CA    1 
ATOM   7602  C  C     . LEU A 1 2508 ? 188.791 195.841 188.731 1.00 21.72  ? 2508 LEU A C     1 
ATOM   7603  O  O     . LEU A 1 2508 ? 189.147 197.005 188.510 1.00 18.71  ? 2508 LEU A O     1 
ATOM   7604  C  CB    . LEU A 1 2508 ? 187.740 195.317 190.947 1.00 23.93  ? 2508 LEU A CB    1 
ATOM   7605  C  CG    . LEU A 1 2508 ? 188.014 196.552 191.804 1.00 29.71  ? 2508 LEU A CG    1 
ATOM   7606  C  CD1   . LEU A 1 2508 ? 186.710 197.209 192.224 1.00 30.74  ? 2508 LEU A CD1   1 
ATOM   7607  C  CD2   . LEU A 1 2508 ? 188.843 196.176 193.020 1.00 26.06  ? 2508 LEU A CD2   1 
ATOM   7608  N  N     . LYS A 1 2509 ? 189.527 194.791 188.362 1.00 20.28  ? 2509 LYS A N     1 
ATOM   7609  C  CA    . LYS A 1 2509 ? 190.828 194.993 187.733 1.00 21.27  ? 2509 LYS A CA    1 
ATOM   7610  C  C     . LYS A 1 2509 ? 190.681 195.603 186.344 1.00 27.92  ? 2509 LYS A C     1 
ATOM   7611  O  O     . LYS A 1 2509 ? 191.480 196.459 185.947 1.00 34.13  ? 2509 LYS A O     1 
ATOM   7612  C  CB    . LYS A 1 2509 ? 191.595 193.669 187.692 1.00 31.15  ? 2509 LYS A CB    1 
ATOM   7613  C  CG    . LYS A 1 2509 ? 192.989 193.754 187.094 1.00 47.04  ? 2509 LYS A CG    1 
ATOM   7614  C  CD    . LYS A 1 2509 ? 193.724 192.427 187.237 1.00 46.89  ? 2509 LYS A CD    1 
ATOM   7615  C  CE    . LYS A 1 2509 ? 193.174 191.354 186.318 1.00 45.63  ? 2509 LYS A CE    1 
ATOM   7616  N  NZ    . LYS A 1 2509 ? 193.457 191.652 184.892 1.00 56.39  ? 2509 LYS A NZ    1 
ATOM   7617  N  N     . MET A 1 2510 ? 189.652 195.192 185.597 1.00 25.63  ? 2510 MET A N     1 
ATOM   7618  C  CA    . MET A 1 2510 ? 189.363 195.829 184.314 1.00 20.10  ? 2510 MET A CA    1 
ATOM   7619  C  C     . MET A 1 2510 ? 188.988 197.296 184.478 1.00 17.91  ? 2510 MET A C     1 
ATOM   7620  O  O     . MET A 1 2510 ? 189.423 198.140 183.684 1.00 20.32  ? 2510 MET A O     1 
ATOM   7621  C  CB    . MET A 1 2510 ? 188.239 195.081 183.599 1.00 19.12  ? 2510 MET A CB    1 
ATOM   7622  C  CG    . MET A 1 2510 ? 188.571 193.660 183.178 1.00 21.05  ? 2510 MET A CG    1 
ATOM   7623  S  SD    . MET A 1 2510 ? 189.932 193.575 181.999 1.00 41.43  ? 2510 MET A SD    1 
ATOM   7624  C  CE    . MET A 1 2510 ? 191.276 193.066 183.059 1.00 39.41  ? 2510 MET A CE    1 
ATOM   7625  N  N     . ARG A 1 2511 ? 188.175 197.615 185.487 1.00 14.96  ? 2511 ARG A N     1 
ATOM   7626  C  CA    . ARG A 1 2511 ? 187.809 199.006 185.732 1.00 16.58  ? 2511 ARG A CA    1 
ATOM   7627  C  C     . ARG A 1 2511 ? 189.036 199.839 186.075 1.00 19.86  ? 2511 ARG A C     1 
ATOM   7628  O  O     . ARG A 1 2511 ? 189.187 200.968 185.592 1.00 22.37  ? 2511 ARG A O     1 
ATOM   7629  C  CB    . ARG A 1 2511 ? 186.775 199.081 186.854 1.00 13.03  ? 2511 ARG A CB    1 
ATOM   7630  C  CG    . ARG A 1 2511 ? 185.444 198.440 186.511 1.00 8.45   ? 2511 ARG A CG    1 
ATOM   7631  C  CD    . ARG A 1 2511 ? 184.504 198.465 187.698 1.00 9.02   ? 2511 ARG A CD    1 
ATOM   7632  N  NE    . ARG A 1 2511 ? 183.215 197.859 187.390 1.00 7.84   ? 2511 ARG A NE    1 
ATOM   7633  C  CZ    . ARG A 1 2511 ? 182.211 197.757 188.250 1.00 8.27   ? 2511 ARG A CZ    1 
ATOM   7634  N  NH1   . ARG A 1 2511 ? 182.313 198.215 189.487 1.00 9.90   ? 2511 ARG A NH1   1 
ATOM   7635  N  NH2   . ARG A 1 2511 ? 181.077 197.184 187.860 1.00 7.22   ? 2511 ARG A NH2   1 
ATOM   7636  N  N     . ALA A 1 2512 ? 189.929 199.290 186.901 1.00 19.64  ? 2512 ALA A N     1 
ATOM   7637  C  CA    . ALA A 1 2512 ? 191.163 199.991 187.235 1.00 19.14  ? 2512 ALA A CA    1 
ATOM   7638  C  C     . ALA A 1 2512 ? 192.040 200.183 186.005 1.00 21.97  ? 2512 ALA A C     1 
ATOM   7639  O  O     . ALA A 1 2512 ? 192.655 201.241 185.833 1.00 24.76  ? 2512 ALA A O     1 
ATOM   7640  C  CB    . ALA A 1 2512 ? 191.919 199.229 188.322 1.00 22.44  ? 2512 ALA A CB    1 
ATOM   7641  N  N     . GLU A 1 2513 ? 192.116 199.169 185.141 1.00 21.19  ? 2513 GLU A N     1 
ATOM   7642  C  CA    . GLU A 1 2513 ? 192.912 199.288 183.923 1.00 22.27  ? 2513 GLU A CA    1 
ATOM   7643  C  C     . GLU A 1 2513 ? 192.368 200.385 183.016 1.00 24.85  ? 2513 GLU A C     1 
ATOM   7644  O  O     . GLU A 1 2513 ? 193.131 201.191 182.467 1.00 30.07  ? 2513 GLU A O     1 
ATOM   7645  C  CB    . GLU A 1 2513 ? 192.944 197.948 183.189 1.00 23.97  ? 2513 GLU A CB    1 
ATOM   7646  C  CG    . GLU A 1 2513 ? 194.177 197.742 182.329 1.00 37.33  ? 2513 GLU A CG    1 
ATOM   7647  C  CD    . GLU A 1 2513 ? 194.168 196.408 181.612 1.00 52.81  ? 2513 GLU A CD    1 
ATOM   7648  O  OE1   . GLU A 1 2513 ? 193.571 195.449 182.145 1.00 53.43  ? 2513 GLU A OE1   1 
ATOM   7649  O  OE2   . GLU A 1 2513 ? 194.761 196.317 180.517 1.00 54.29  ? 2513 GLU A OE2   1 
ATOM   7650  N  N     . LEU A 1 2514 ? 191.045 200.428 182.845 1.00 20.79  ? 2514 LEU A N     1 
ATOM   7651  C  CA    . LEU A 1 2514 ? 190.449 201.470 182.013 1.00 21.44  ? 2514 LEU A CA    1 
ATOM   7652  C  C     . LEU A 1 2514 ? 190.665 202.848 182.622 1.00 23.95  ? 2514 LEU A C     1 
ATOM   7653  O  O     . LEU A 1 2514 ? 190.932 203.819 181.903 1.00 25.68  ? 2514 LEU A O     1 
ATOM   7654  C  CB    . LEU A 1 2514 ? 188.959 201.203 181.805 1.00 18.92  ? 2514 LEU A CB    1 
ATOM   7655  C  CG    . LEU A 1 2514 ? 188.275 202.209 180.877 1.00 16.71  ? 2514 LEU A CG    1 
ATOM   7656  C  CD1   . LEU A 1 2514 ? 188.775 202.043 179.453 1.00 19.16  ? 2514 LEU A CD1   1 
ATOM   7657  C  CD2   . LEU A 1 2514 ? 186.766 202.080 180.934 1.00 13.03  ? 2514 LEU A CD2   1 
ATOM   7658  N  N     . GLY A 1 2515 ? 190.550 202.956 183.948 1.00 21.64  ? 2515 GLY A N     1 
ATOM   7659  C  CA    . GLY A 1 2515 ? 190.825 204.224 184.601 1.00 23.30  ? 2515 GLY A CA    1 
ATOM   7660  C  C     . GLY A 1 2515 ? 192.257 204.681 184.406 1.00 23.53  ? 2515 GLY A C     1 
ATOM   7661  O  O     . GLY A 1 2515 ? 192.514 205.862 184.163 1.00 27.96  ? 2515 GLY A O     1 
ATOM   7662  N  N     . GLU A 1 2516 ? 193.210 203.752 184.510 1.00 23.79  ? 2516 GLU A N     1 
ATOM   7663  C  CA    . GLU A 1 2516 ? 194.610 204.100 184.290 1.00 25.93  ? 2516 GLU A CA    1 
ATOM   7664  C  C     . GLU A 1 2516 ? 194.852 204.544 182.853 1.00 27.11  ? 2516 GLU A C     1 
ATOM   7665  O  O     . GLU A 1 2516 ? 195.573 205.520 182.611 1.00 31.65  ? 2516 GLU A O     1 
ATOM   7666  C  CB    . GLU A 1 2516 ? 195.510 202.916 184.646 1.00 24.07  ? 2516 GLU A CB    1 
ATOM   7667  C  CG    . GLU A 1 2516 ? 195.540 202.576 186.128 1.00 28.76  ? 2516 GLU A CG    1 
ATOM   7668  C  CD    . GLU A 1 2516 ? 196.506 203.443 186.915 1.00 46.01  ? 2516 GLU A CD    1 
ATOM   7669  O  OE1   . GLU A 1 2516 ? 196.347 204.682 186.908 1.00 37.09  ? 2516 GLU A OE1   1 
ATOM   7670  O  OE2   . GLU A 1 2516 ? 197.429 202.883 187.544 1.00 48.08  ? 2516 GLU A OE2   1 
ATOM   7671  N  N     . TYR A 1 2517 ? 194.258 203.843 181.885 1.00 20.74  ? 2517 TYR A N     1 
ATOM   7672  C  CA    . TYR A 1 2517 ? 194.412 204.251 180.491 1.00 21.54  ? 2517 TYR A CA    1 
ATOM   7673  C  C     . TYR A 1 2517 ? 193.833 205.641 180.258 1.00 26.67  ? 2517 TYR A C     1 
ATOM   7674  O  O     . TYR A 1 2517 ? 194.456 206.483 179.595 1.00 34.47  ? 2517 TYR A O     1 
ATOM   7675  C  CB    . TYR A 1 2517 ? 193.750 203.236 179.562 1.00 25.11  ? 2517 TYR A CB    1 
ATOM   7676  C  CG    . TYR A 1 2517 ? 193.808 203.628 178.103 1.00 28.63  ? 2517 TYR A CG    1 
ATOM   7677  C  CD1   . TYR A 1 2517 ? 194.950 203.403 177.350 1.00 26.90  ? 2517 TYR A CD1   1 
ATOM   7678  C  CD2   . TYR A 1 2517 ? 192.722 204.226 177.479 1.00 27.25  ? 2517 TYR A CD2   1 
ATOM   7679  C  CE1   . TYR A 1 2517 ? 195.009 203.761 176.018 1.00 31.95  ? 2517 TYR A CE1   1 
ATOM   7680  C  CE2   . TYR A 1 2517 ? 192.773 204.587 176.149 1.00 24.51  ? 2517 TYR A CE2   1 
ATOM   7681  C  CZ    . TYR A 1 2517 ? 193.918 204.353 175.423 1.00 26.64  ? 2517 TYR A CZ    1 
ATOM   7682  O  OH    . TYR A 1 2517 ? 193.970 204.711 174.097 1.00 28.68  ? 2517 TYR A OH    1 
ATOM   7683  N  N     . ILE A 1 2518 ? 192.642 205.903 180.802 1.00 24.46  ? 2518 ILE A N     1 
ATOM   7684  C  CA    . ILE A 1 2518 ? 192.034 207.219 180.649 1.00 23.37  ? 2518 ILE A CA    1 
ATOM   7685  C  C     . ILE A 1 2518 ? 192.923 208.283 181.274 1.00 24.91  ? 2518 ILE A C     1 
ATOM   7686  O  O     . ILE A 1 2518 ? 193.187 209.325 180.664 1.00 33.20  ? 2518 ILE A O     1 
ATOM   7687  C  CB    . ILE A 1 2518 ? 190.618 207.228 181.254 1.00 22.54  ? 2518 ILE A CB    1 
ATOM   7688  C  CG1   . ILE A 1 2518 ? 189.643 206.507 180.325 1.00 20.22  ? 2518 ILE A CG1   1 
ATOM   7689  C  CG2   . ILE A 1 2518 ? 190.151 208.652 181.507 1.00 22.00  ? 2518 ILE A CG2   1 
ATOM   7690  C  CD1   . ILE A 1 2518 ? 188.251 206.385 180.884 1.00 16.45  ? 2518 ILE A CD1   1 
ATOM   7691  N  N     . ARG A 1 2519 ? 193.429 208.022 182.481 1.00 26.41  ? 2519 ARG A N     1 
ATOM   7692  C  CA    . ARG A 1 2519 ? 194.332 208.963 183.136 1.00 28.03  ? 2519 ARG A CA    1 
ATOM   7693  C  C     . ARG A 1 2519 ? 195.557 209.240 182.277 1.00 31.74  ? 2519 ARG A C     1 
ATOM   7694  O  O     . ARG A 1 2519 ? 196.039 210.376 182.216 1.00 32.59  ? 2519 ARG A O     1 
ATOM   7695  C  CB    . ARG A 1 2519 ? 194.749 208.419 184.501 1.00 25.71  ? 2519 ARG A CB    1 
ATOM   7696  C  CG    . ARG A 1 2519 ? 195.623 209.361 185.305 1.00 32.26  ? 2519 ARG A CG    1 
ATOM   7697  C  CD    . ARG A 1 2519 ? 196.086 208.714 186.598 1.00 35.36  ? 2519 ARG A CD    1 
ATOM   7698  N  NE    . ARG A 1 2519 ? 195.046 208.731 187.620 1.00 36.78  ? 2519 ARG A NE    1 
ATOM   7699  C  CZ    . ARG A 1 2519 ? 194.754 209.781 188.373 1.00 37.91  ? 2519 ARG A CZ    1 
ATOM   7700  N  NH1   . ARG A 1 2519 ? 195.404 210.926 188.244 1.00 33.40  ? 2519 ARG A NH1   1 
ATOM   7701  N  NH2   . ARG A 1 2519 ? 193.787 209.681 189.279 1.00 38.50  ? 2519 ARG A NH2   1 
ATOM   7702  N  N     . ARG A 1 2520 ? 196.076 208.209 181.609 1.00 34.69  ? 2520 ARG A N     1 
ATOM   7703  C  CA    . ARG A 1 2520 ? 197.229 208.407 180.739 1.00 31.32  ? 2520 ARG A CA    1 
ATOM   7704  C  C     . ARG A 1 2520 ? 196.880 209.282 179.540 1.00 34.32  ? 2520 ARG A C     1 
ATOM   7705  O  O     . ARG A 1 2520 ? 197.682 210.131 179.135 1.00 37.84  ? 2520 ARG A O     1 
ATOM   7706  C  CB    . ARG A 1 2520 ? 197.782 207.059 180.281 1.00 25.88  ? 2520 ARG A CB    1 
ATOM   7707  C  CG    . ARG A 1 2520 ? 198.845 206.490 181.208 1.00 29.03  ? 2520 ARG A CG    1 
ATOM   7708  C  CD    . ARG A 1 2520 ? 199.848 205.609 180.468 1.00 35.79  ? 2520 ARG A CD    1 
ATOM   7709  N  NE    . ARG A 1 2520 ? 199.257 204.852 179.369 1.00 38.23  ? 2520 ARG A NE    1 
ATOM   7710  C  CZ    . ARG A 1 2520 ? 198.407 203.844 179.515 1.00 36.06  ? 2520 ARG A CZ    1 
ATOM   7711  N  NH1   . ARG A 1 2520 ? 198.021 203.429 180.710 1.00 30.53  ? 2520 ARG A NH1   1 
ATOM   7712  N  NH2   . ARG A 1 2520 ? 197.938 203.231 178.432 1.00 34.40  ? 2520 ARG A NH2   1 
ATOM   7713  N  N     . ILE A 1 2521 ? 195.693 209.100 178.960 1.00 34.12  ? 2521 ILE A N     1 
ATOM   7714  C  CA    . ILE A 1 2521 ? 195.360 209.809 177.727 1.00 30.11  ? 2521 ILE A CA    1 
ATOM   7715  C  C     . ILE A 1 2521 ? 194.579 211.107 177.936 1.00 31.90  ? 2521 ILE A C     1 
ATOM   7716  O  O     . ILE A 1 2521 ? 194.613 211.977 177.053 1.00 39.17  ? 2521 ILE A O     1 
ATOM   7717  C  CB    . ILE A 1 2521 ? 194.589 208.899 176.748 1.00 28.46  ? 2521 ILE A CB    1 
ATOM   7718  C  CG1   . ILE A 1 2521 ? 193.108 208.829 177.124 1.00 30.86  ? 2521 ILE A CG1   1 
ATOM   7719  C  CG2   . ILE A 1 2521 ? 195.215 207.515 176.696 1.00 33.23  ? 2521 ILE A CG2   1 
ATOM   7720  C  CD1   . ILE A 1 2521 ? 192.274 208.010 176.171 1.00 28.19  ? 2521 ILE A CD1   1 
ATOM   7721  N  N     . THR A 1 2522 ? 193.882 211.269 179.057 1.00 31.54  ? 2522 THR A N     1 
ATOM   7722  C  CA    . THR A 1 2522 ? 192.990 212.413 179.164 1.00 35.77  ? 2522 THR A CA    1 
ATOM   7723  C  C     . THR A 1 2522 ? 193.759 213.672 179.553 1.00 40.38  ? 2522 THR A C     1 
ATOM   7724  O  O     . THR A 1 2522 ? 194.913 213.629 179.986 1.00 44.48  ? 2522 THR A O     1 
ATOM   7725  C  CB    . THR A 1 2522 ? 191.881 212.165 180.185 1.00 39.22  ? 2522 THR A CB    1 
ATOM   7726  O  OG1   . THR A 1 2522 ? 190.936 213.239 180.123 1.00 43.45  ? 2522 THR A OG1   1 
ATOM   7727  C  CG2   . THR A 1 2522 ? 192.458 212.138 181.589 1.00 35.14  ? 2522 THR A CG2   1 
ATOM   7728  N  N     . THR A 1 2523 ? 193.091 214.812 179.380 1.00 36.10  ? 2523 THR A N     1 
ATOM   7729  C  CA    . THR A 1 2523 ? 193.576 216.093 179.869 1.00 37.02  ? 2523 THR A CA    1 
ATOM   7730  C  C     . THR A 1 2523 ? 192.647 216.701 180.910 1.00 41.50  ? 2523 THR A C     1 
ATOM   7731  O  O     . THR A 1 2523 ? 192.958 217.768 181.451 1.00 45.37  ? 2523 THR A O     1 
ATOM   7732  C  CB    . THR A 1 2523 ? 193.763 217.078 178.707 1.00 40.54  ? 2523 THR A CB    1 
ATOM   7733  O  OG1   . THR A 1 2523 ? 194.551 218.192 179.143 1.00 50.00  ? 2523 THR A OG1   1 
ATOM   7734  C  CG2   . THR A 1 2523 ? 192.417 217.577 178.203 1.00 37.72  ? 2523 THR A CG2   1 
ATOM   7735  N  N     . VAL A 1 2524 ? 191.523 216.058 181.197 1.00 35.35  ? 2524 VAL A N     1 
ATOM   7736  C  CA    . VAL A 1 2524 ? 190.599 216.541 182.230 1.00 35.71  ? 2524 VAL A CA    1 
ATOM   7737  C  C     . VAL A 1 2524 ? 191.270 216.426 183.593 1.00 38.32  ? 2524 VAL A C     1 
ATOM   7738  O  O     . VAL A 1 2524 ? 191.958 215.422 183.855 1.00 35.98  ? 2524 VAL A O     1 
ATOM   7739  C  CB    . VAL A 1 2524 ? 189.295 215.739 182.186 1.00 29.78  ? 2524 VAL A CB    1 
ATOM   7740  C  CG1   . VAL A 1 2524 ? 188.267 216.319 183.143 1.00 26.72  ? 2524 VAL A CG1   1 
ATOM   7741  C  CG2   . VAL A 1 2524 ? 188.747 215.698 180.769 1.00 24.53  ? 2524 VAL A CG2   1 
ATOM   7742  N  N     . PRO A 1 2525 ? 191.128 217.413 184.477 1.00 33.84  ? 2525 PRO A N     1 
ATOM   7743  C  CA    . PRO A 1 2525 ? 191.673 217.271 185.836 1.00 32.07  ? 2525 PRO A CA    1 
ATOM   7744  C  C     . PRO A 1 2525 ? 191.068 216.067 186.543 1.00 37.44  ? 2525 PRO A C     1 
ATOM   7745  O  O     . PRO A 1 2525 ? 189.848 215.902 186.597 1.00 37.99  ? 2525 PRO A O     1 
ATOM   7746  C  CB    . PRO A 1 2525 ? 191.282 218.590 186.512 1.00 28.92  ? 2525 PRO A CB    1 
ATOM   7747  C  CG    . PRO A 1 2525 ? 191.116 219.552 185.389 1.00 35.01  ? 2525 PRO A CG    1 
ATOM   7748  C  CD    . PRO A 1 2525 ? 190.567 218.755 184.245 1.00 35.27  ? 2525 PRO A CD    1 
ATOM   7749  N  N     . LEU A 1 2526 ? 191.937 215.229 187.088 1.00 37.53  ? 2526 LEU A N     1 
ATOM   7750  C  CA    . LEU A 1 2526 ? 191.574 213.966 187.703 1.00 29.77  ? 2526 LEU A CA    1 
ATOM   7751  C  C     . LEU A 1 2526 ? 191.975 213.945 189.171 1.00 33.25  ? 2526 LEU A C     1 
ATOM   7752  O  O     . LEU A 1 2526 ? 192.807 214.747 189.608 1.00 41.48  ? 2526 LEU A O     1 
ATOM   7753  C  CB    . LEU A 1 2526 ? 192.257 212.807 186.964 1.00 34.83  ? 2526 LEU A CB    1 
ATOM   7754  C  CG    . LEU A 1 2526 ? 191.673 212.453 185.597 1.00 35.80  ? 2526 LEU A CG    1 
ATOM   7755  C  CD1   . LEU A 1 2526 ? 192.260 211.153 185.106 1.00 31.16  ? 2526 LEU A CD1   1 
ATOM   7756  C  CD2   . LEU A 1 2526 ? 190.159 212.359 185.667 1.00 31.63  ? 2526 LEU A CD2   1 
ATOM   7757  N  N     . PRO A 1 2527 ? 191.382 213.058 189.972 1.00 36.58  ? 2527 PRO A N     1 
ATOM   7758  C  CA    . PRO A 1 2527 ? 191.807 212.940 191.373 1.00 34.02  ? 2527 PRO A CA    1 
ATOM   7759  C  C     . PRO A 1 2527 ? 193.284 212.589 191.471 1.00 36.43  ? 2527 PRO A C     1 
ATOM   7760  O  O     . PRO A 1 2527 ? 193.809 211.798 190.685 1.00 39.70  ? 2527 PRO A O     1 
ATOM   7761  C  CB    . PRO A 1 2527 ? 190.920 211.817 191.917 1.00 32.90  ? 2527 PRO A CB    1 
ATOM   7762  C  CG    . PRO A 1 2527 ? 189.715 211.841 191.046 1.00 24.73  ? 2527 PRO A CG    1 
ATOM   7763  C  CD    . PRO A 1 2527 ? 190.201 212.225 189.684 1.00 30.23  ? 2527 PRO A CD    1 
ATOM   7764  N  N     . THR A 1 2528 ? 193.950 213.181 192.459 1.00 40.34  ? 2528 THR A N     1 
ATOM   7765  C  CA    . THR A 1 2528 ? 195.402 213.140 192.565 1.00 47.98  ? 2528 THR A CA    1 
ATOM   7766  C  C     . THR A 1 2528 ? 195.909 212.051 193.503 1.00 52.13  ? 2528 THR A C     1 
ATOM   7767  O  O     . THR A 1 2528 ? 197.097 212.048 193.839 1.00 56.69  ? 2528 THR A O     1 
ATOM   7768  C  CB    . THR A 1 2528 ? 195.932 214.500 193.021 1.00 48.69  ? 2528 THR A CB    1 
ATOM   7769  O  OG1   . THR A 1 2528 ? 195.399 214.810 194.315 1.00 55.61  ? 2528 THR A OG1   1 
ATOM   7770  C  CG2   . THR A 1 2528 ? 195.524 215.586 192.039 1.00 41.04  ? 2528 THR A CG2   1 
ATOM   7771  N  N     . ALA A 1 2529 ? 195.050 211.139 193.938 1.00 52.52  ? 2529 ALA A N     1 
ATOM   7772  C  CA    . ALA A 1 2529 ? 195.492 210.083 194.842 1.00 61.05  ? 2529 ALA A CA    1 
ATOM   7773  C  C     . ALA A 1 2529 ? 196.461 209.150 194.125 1.00 66.86  ? 2529 ALA A C     1 
ATOM   7774  O  O     . ALA A 1 2529 ? 196.168 208.696 193.012 1.00 66.30  ? 2529 ALA A O     1 
ATOM   7775  C  CB    . ALA A 1 2529 ? 194.304 209.294 195.377 1.00 53.77  ? 2529 ALA A CB    1 
ATOM   7776  N  N     . PRO A 1 2530 ? 197.619 208.851 194.716 1.00 62.34  ? 2530 PRO A N     1 
ATOM   7777  C  CA    . PRO A 1 2530 ? 198.588 207.977 194.034 1.00 66.20  ? 2530 PRO A CA    1 
ATOM   7778  C  C     . PRO A 1 2530 ? 198.076 206.570 193.774 1.00 65.59  ? 2530 PRO A C     1 
ATOM   7779  O  O     . PRO A 1 2530 ? 198.487 205.948 192.786 1.00 62.23  ? 2530 PRO A O     1 
ATOM   7780  C  CB    . PRO A 1 2530 ? 199.788 207.969 194.993 1.00 66.98  ? 2530 PRO A CB    1 
ATOM   7781  C  CG    . PRO A 1 2530 ? 199.236 208.392 196.316 1.00 68.45  ? 2530 PRO A CG    1 
ATOM   7782  C  CD    . PRO A 1 2530 ? 198.112 209.330 196.017 1.00 58.18  ? 2530 PRO A CD    1 
ATOM   7783  N  N     . ASN A 1 2531 ? 197.196 206.043 194.627 1.00 63.95  ? 2531 ASN A N     1 
ATOM   7784  C  CA    . ASN A 1 2531 ? 196.789 204.648 194.540 1.00 62.65  ? 2531 ASN A CA    1 
ATOM   7785  C  C     . ASN A 1 2531 ? 195.292 204.420 194.379 1.00 53.77  ? 2531 ASN A C     1 
ATOM   7786  O  O     . ASN A 1 2531 ? 194.904 203.344 193.912 1.00 46.25  ? 2531 ASN A O     1 
ATOM   7787  C  CB    . ASN A 1 2531 ? 197.285 203.874 195.775 1.00 64.07  ? 2531 ASN A CB    1 
ATOM   7788  C  CG    . ASN A 1 2531 ? 196.671 204.374 197.074 1.00 73.37  ? 2531 ASN A CG    1 
ATOM   7789  O  OD1   . ASN A 1 2531 ? 195.779 205.222 197.077 1.00 73.03  ? 2531 ASN A OD1   1 
ATOM   7790  N  ND2   . ASN A 1 2531 ? 197.155 203.845 198.192 1.00 73.80  ? 2531 ASN A ND2   1 
ATOM   7791  N  N     . ILE A 1 2532 ? 194.450 205.376 194.745 1.00 50.97  ? 2532 ILE A N     1 
ATOM   7792  C  CA    . ILE A 1 2532 ? 193.002 205.183 194.637 1.00 41.44  ? 2532 ILE A CA    1 
ATOM   7793  C  C     . ILE A 1 2532 ? 192.599 205.297 193.169 1.00 36.87  ? 2532 ILE A C     1 
ATOM   7794  O  O     . ILE A 1 2532 ? 192.909 206.313 192.528 1.00 42.84  ? 2532 ILE A O     1 
ATOM   7795  C  CB    . ILE A 1 2532 ? 192.258 206.202 195.490 1.00 42.51  ? 2532 ILE A CB    1 
ATOM   7796  C  CG1   . ILE A 1 2532 ? 192.604 206.018 196.967 1.00 51.33  ? 2532 ILE A CG1   1 
ATOM   7797  C  CG2   . ILE A 1 2532 ? 190.761 206.057 195.294 1.00 29.91  ? 2532 ILE A CG2   1 
ATOM   7798  C  CD1   . ILE A 1 2532 ? 192.116 207.145 197.849 1.00 43.68  ? 2532 ILE A CD1   1 
ATOM   7799  N  N     . PRO A 1 2533 ? 191.924 204.297 192.607 1.00 29.20  ? 2533 PRO A N     1 
ATOM   7800  C  CA    . PRO A 1 2533 ? 191.481 204.395 191.213 1.00 26.18  ? 2533 PRO A CA    1 
ATOM   7801  C  C     . PRO A 1 2533 ? 190.384 205.435 191.042 1.00 24.06  ? 2533 PRO A C     1 
ATOM   7802  O  O     . PRO A 1 2533 ? 189.686 205.813 191.986 1.00 33.55  ? 2533 PRO A O     1 
ATOM   7803  C  CB    . PRO A 1 2533 ? 190.966 202.987 190.901 1.00 22.36  ? 2533 PRO A CB    1 
ATOM   7804  C  CG    . PRO A 1 2533 ? 190.607 202.417 192.220 1.00 18.61  ? 2533 PRO A CG    1 
ATOM   7805  C  CD    . PRO A 1 2533 ? 191.575 202.999 193.208 1.00 28.34  ? 2533 PRO A CD    1 
ATOM   7806  N  N     . ILE A 1 2534 ? 190.247 205.905 189.800 1.00 19.13  ? 2534 ILE A N     1 
ATOM   7807  C  CA    . ILE A 1 2534 ? 189.281 206.955 189.492 1.00 21.78  ? 2534 ILE A CA    1 
ATOM   7808  C  C     . ILE A 1 2534 ? 187.857 206.457 189.697 1.00 20.15  ? 2534 ILE A C     1 
ATOM   7809  O  O     . ILE A 1 2534 ? 186.952 207.242 190.007 1.00 18.77  ? 2534 ILE A O     1 
ATOM   7810  C  CB    . ILE A 1 2534 ? 189.502 207.468 188.055 1.00 13.88  ? 2534 ILE A CB    1 
ATOM   7811  C  CG1   . ILE A 1 2534 ? 190.935 207.964 187.889 1.00 24.42  ? 2534 ILE A CG1   1 
ATOM   7812  C  CG2   . ILE A 1 2534 ? 188.556 208.609 187.740 1.00 11.40  ? 2534 ILE A CG2   1 
ATOM   7813  C  CD1   . ILE A 1 2534 ? 191.415 207.946 186.461 1.00 28.82  ? 2534 ILE A CD1   1 
ATOM   7814  N  N     . ILE A 1 2535 ? 187.634 205.150 189.546 1.00 19.07  ? 2535 ILE A N     1 
ATOM   7815  C  CA    . ILE A 1 2535 ? 186.308 204.571 189.707 1.00 20.45  ? 2535 ILE A CA    1 
ATOM   7816  C  C     . ILE A 1 2535 ? 185.762 204.731 191.119 1.00 19.85  ? 2535 ILE A C     1 
ATOM   7817  O  O     . ILE A 1 2535 ? 184.563 204.533 191.336 1.00 17.62  ? 2535 ILE A O     1 
ATOM   7818  C  CB    . ILE A 1 2535 ? 186.331 203.079 189.302 1.00 21.00  ? 2535 ILE A CB    1 
ATOM   7819  C  CG1   . ILE A 1 2535 ? 184.966 202.646 188.762 1.00 23.21  ? 2535 ILE A CG1   1 
ATOM   7820  C  CG2   . ILE A 1 2535 ? 186.756 202.205 190.473 1.00 16.01  ? 2535 ILE A CG2   1 
ATOM   7821  C  CD1   . ILE A 1 2535 ? 184.639 203.214 187.401 1.00 17.14  ? 2535 ILE A CD1   1 
ATOM   7822  N  N     . ASP A 1 2536 ? 186.604 205.096 192.082 1.00 19.07  ? 2536 ASP A N     1 
ATOM   7823  C  CA    . ASP A 1 2536 ? 186.174 205.283 193.460 1.00 17.15  ? 2536 ASP A CA    1 
ATOM   7824  C  C     . ASP A 1 2536 ? 185.710 206.704 193.748 1.00 21.51  ? 2536 ASP A C     1 
ATOM   7825  O  O     . ASP A 1 2536 ? 185.400 207.015 194.903 1.00 25.20  ? 2536 ASP A O     1 
ATOM   7826  C  CB    . ASP A 1 2536 ? 187.302 204.911 194.425 1.00 18.61  ? 2536 ASP A CB    1 
ATOM   7827  C  CG    . ASP A 1 2536 ? 187.597 203.427 194.430 1.00 28.98  ? 2536 ASP A CG    1 
ATOM   7828  O  OD1   . ASP A 1 2536 ? 186.670 202.635 194.166 1.00 38.42  ? 2536 ASP A OD1   1 
ATOM   7829  O  OD2   . ASP A 1 2536 ? 188.749 203.050 194.723 1.00 30.55  ? 2536 ASP A OD2   1 
ATOM   7830  N  N     . TYR A 1 2537 ? 185.659 207.568 192.740 1.00 17.09  ? 2537 TYR A N     1 
ATOM   7831  C  CA    . TYR A 1 2537 ? 185.241 208.950 192.906 1.00 15.26  ? 2537 TYR A CA    1 
ATOM   7832  C  C     . TYR A 1 2537 ? 183.952 209.219 192.146 1.00 17.15  ? 2537 TYR A C     1 
ATOM   7833  O  O     . TYR A 1 2537 ? 183.625 208.537 191.171 1.00 23.34  ? 2537 TYR A O     1 
ATOM   7834  C  CB    . TYR A 1 2537 ? 186.317 209.922 192.418 1.00 23.15  ? 2537 TYR A CB    1 
ATOM   7835  C  CG    . TYR A 1 2537 ? 187.628 209.822 193.151 1.00 23.73  ? 2537 TYR A CG    1 
ATOM   7836  C  CD1   . TYR A 1 2537 ? 188.596 208.909 192.761 1.00 20.74  ? 2537 TYR A CD1   1 
ATOM   7837  C  CD2   . TYR A 1 2537 ? 187.902 210.650 194.229 1.00 19.67  ? 2537 TYR A CD2   1 
ATOM   7838  C  CE1   . TYR A 1 2537 ? 189.795 208.822 193.427 1.00 24.48  ? 2537 TYR A CE1   1 
ATOM   7839  C  CE2   . TYR A 1 2537 ? 189.096 210.569 194.901 1.00 23.00  ? 2537 TYR A CE2   1 
ATOM   7840  C  CZ    . TYR A 1 2537 ? 190.039 209.653 194.496 1.00 34.89  ? 2537 TYR A CZ    1 
ATOM   7841  O  OH    . TYR A 1 2537 ? 191.233 209.571 195.167 1.00 43.23  ? 2537 TYR A OH    1 
ATOM   7842  N  N     . GLU A 1 2538 ? 183.223 210.226 192.610 1.00 19.76  ? 2538 GLU A N     1 
ATOM   7843  C  CA    . GLU A 1 2538 ? 182.067 210.774 191.926 1.00 16.28  ? 2538 GLU A CA    1 
ATOM   7844  C  C     . GLU A 1 2538 ? 182.305 212.254 191.662 1.00 22.66  ? 2538 GLU A C     1 
ATOM   7845  O  O     . GLU A 1 2538 ? 183.270 212.851 192.147 1.00 26.47  ? 2538 GLU A O     1 
ATOM   7846  C  CB    . GLU A 1 2538 ? 180.789 210.569 192.746 1.00 14.24  ? 2538 GLU A CB    1 
ATOM   7847  C  CG    . GLU A 1 2538 ? 180.809 211.237 194.108 1.00 19.84  ? 2538 GLU A CG    1 
ATOM   7848  C  CD    . GLU A 1 2538 ? 179.422 211.605 194.594 1.00 29.95  ? 2538 GLU A CD    1 
ATOM   7849  O  OE1   . GLU A 1 2538 ? 178.472 211.548 193.786 1.00 24.31  ? 2538 GLU A OE1   1 
ATOM   7850  O  OE2   . GLU A 1 2538 ? 179.280 211.946 195.786 1.00 38.48  ? 2538 GLU A OE2   1 
ATOM   7851  N  N     . VAL A 1 2539 ? 181.416 212.845 190.876 1.00 19.41  ? 2539 VAL A N     1 
ATOM   7852  C  CA    . VAL A 1 2539 ? 181.510 214.249 190.502 1.00 15.58  ? 2539 VAL A CA    1 
ATOM   7853  C  C     . VAL A 1 2539 ? 180.423 214.999 191.255 1.00 23.23  ? 2539 VAL A C     1 
ATOM   7854  O  O     . VAL A 1 2539 ? 179.228 214.743 191.061 1.00 24.42  ? 2539 VAL A O     1 
ATOM   7855  C  CB    . VAL A 1 2539 ? 181.376 214.447 188.987 1.00 18.40  ? 2539 VAL A CB    1 
ATOM   7856  C  CG1   . VAL A 1 2539 ? 181.720 215.876 188.615 1.00 19.95  ? 2539 VAL A CG1   1 
ATOM   7857  C  CG2   . VAL A 1 2539 ? 182.268 213.468 188.246 1.00 14.57  ? 2539 VAL A CG2   1 
ATOM   7858  N  N     . SER A 1 2540 ? 180.834 215.920 192.121 1.00 24.03  ? 2540 SER A N     1 
ATOM   7859  C  CA    . SER A 1 2540 ? 179.877 216.766 192.813 1.00 21.86  ? 2540 SER A CA    1 
ATOM   7860  C  C     . SER A 1 2540 ? 179.306 217.804 191.857 1.00 26.43  ? 2540 SER A C     1 
ATOM   7861  O  O     . SER A 1 2540 ? 179.919 218.155 190.846 1.00 28.17  ? 2540 SER A O     1 
ATOM   7862  C  CB    . SER A 1 2540 ? 180.536 217.459 194.005 1.00 24.99  ? 2540 SER A CB    1 
ATOM   7863  O  OG    . SER A 1 2540 ? 181.757 218.068 193.628 1.00 34.25  ? 2540 SER A OG    1 
ATOM   7864  N  N     . ILE A 1 2541 ? 178.109 218.296 192.185 1.00 27.57  ? 2541 ILE A N     1 
ATOM   7865  C  CA    . ILE A 1 2541 ? 177.480 219.316 191.358 1.00 19.30  ? 2541 ILE A CA    1 
ATOM   7866  C  C     . ILE A 1 2541 ? 178.291 220.605 191.365 1.00 26.30  ? 2541 ILE A C     1 
ATOM   7867  O  O     . ILE A 1 2541 ? 178.165 221.421 190.444 1.00 35.42  ? 2541 ILE A O     1 
ATOM   7868  C  CB    . ILE A 1 2541 ? 176.032 219.556 191.824 1.00 22.75  ? 2541 ILE A CB    1 
ATOM   7869  C  CG1   . ILE A 1 2541 ? 175.260 220.374 190.788 1.00 30.78  ? 2541 ILE A CG1   1 
ATOM   7870  C  CG2   . ILE A 1 2541 ? 176.010 220.244 193.179 1.00 30.99  ? 2541 ILE A CG2   1 
ATOM   7871  C  CD1   . ILE A 1 2541 ? 175.055 219.652 189.475 1.00 23.19  ? 2541 ILE A CD1   1 
ATOM   7872  N  N     . SER A 1 2542 ? 179.139 220.804 192.376 1.00 24.77  ? 2542 SER A N     1 
ATOM   7873  C  CA    . SER A 1 2542 ? 180.035 221.952 192.411 1.00 31.78  ? 2542 SER A CA    1 
ATOM   7874  C  C     . SER A 1 2542 ? 181.165 221.848 191.395 1.00 33.98  ? 2542 SER A C     1 
ATOM   7875  O  O     . SER A 1 2542 ? 181.891 222.829 191.202 1.00 41.53  ? 2542 SER A O     1 
ATOM   7876  C  CB    . SER A 1 2542 ? 180.622 222.115 193.813 1.00 34.36  ? 2542 SER A CB    1 
ATOM   7877  O  OG    . SER A 1 2542 ? 181.600 221.124 194.072 1.00 32.52  ? 2542 SER A OG    1 
ATOM   7878  N  N     . GLY A 1 2543 ? 181.338 220.696 190.753 1.00 27.04  ? 2543 GLY A N     1 
ATOM   7879  C  CA    . GLY A 1 2543 ? 182.360 220.544 189.741 1.00 28.78  ? 2543 GLY A CA    1 
ATOM   7880  C  C     . GLY A 1 2543 ? 183.699 220.060 190.242 1.00 32.05  ? 2543 GLY A C     1 
ATOM   7881  O  O     . GLY A 1 2543 ? 184.730 220.405 189.652 1.00 33.39  ? 2543 GLY A O     1 
ATOM   7882  N  N     . GLU A 1 2544 ? 183.723 219.273 191.312 1.00 29.34  ? 2544 GLU A N     1 
ATOM   7883  C  CA    . GLU A 1 2544 ? 184.960 218.755 191.875 1.00 29.88  ? 2544 GLU A CA    1 
ATOM   7884  C  C     . GLU A 1 2544 ? 184.812 217.267 192.155 1.00 29.66  ? 2544 GLU A C     1 
ATOM   7885  O  O     . GLU A 1 2544 ? 183.727 216.789 192.496 1.00 30.91  ? 2544 GLU A O     1 
ATOM   7886  C  CB    . GLU A 1 2544 ? 185.341 219.504 193.163 1.00 36.86  ? 2544 GLU A CB    1 
ATOM   7887  C  CG    . GLU A 1 2544 ? 186.648 219.053 193.794 1.00 44.53  ? 2544 GLU A CG    1 
ATOM   7888  C  CD    . GLU A 1 2544 ? 187.851 219.343 192.918 1.00 46.45  ? 2544 GLU A CD    1 
ATOM   7889  O  OE1   . GLU A 1 2544 ? 187.782 220.282 192.097 1.00 44.54  ? 2544 GLU A OE1   1 
ATOM   7890  O  OE2   . GLU A 1 2544 ? 188.866 218.626 193.048 1.00 43.81  ? 2544 GLU A OE2   1 
ATOM   7891  N  N     . TRP A 1 2545 ? 185.913 216.537 191.996 1.00 31.07  ? 2545 TRP A N     1 
ATOM   7892  C  CA    . TRP A 1 2545 ? 185.929 215.121 192.331 1.00 28.04  ? 2545 TRP A CA    1 
ATOM   7893  C  C     . TRP A 1 2545 ? 185.777 214.941 193.837 1.00 30.75  ? 2545 TRP A C     1 
ATOM   7894  O  O     . TRP A 1 2545 ? 186.409 215.651 194.624 1.00 34.52  ? 2545 TRP A O     1 
ATOM   7895  C  CB    . TRP A 1 2545 ? 187.231 214.475 191.861 1.00 28.04  ? 2545 TRP A CB    1 
ATOM   7896  C  CG    . TRP A 1 2545 ? 187.365 214.342 190.376 1.00 23.31  ? 2545 TRP A CG    1 
ATOM   7897  C  CD1   . TRP A 1 2545 ? 188.148 215.098 189.557 1.00 27.16  ? 2545 TRP A CD1   1 
ATOM   7898  C  CD2   . TRP A 1 2545 ? 186.701 213.394 189.533 1.00 23.53  ? 2545 TRP A CD2   1 
ATOM   7899  N  NE1   . TRP A 1 2545 ? 188.017 214.679 188.257 1.00 27.21  ? 2545 TRP A NE1   1 
ATOM   7900  C  CE2   . TRP A 1 2545 ? 187.132 213.634 188.215 1.00 21.73  ? 2545 TRP A CE2   1 
ATOM   7901  C  CE3   . TRP A 1 2545 ? 185.784 212.364 189.766 1.00 24.49  ? 2545 TRP A CE3   1 
ATOM   7902  C  CZ2   . TRP A 1 2545 ? 186.679 212.885 187.133 1.00 18.33  ? 2545 TRP A CZ2   1 
ATOM   7903  C  CZ3   . TRP A 1 2545 ? 185.336 211.622 188.690 1.00 19.88  ? 2545 TRP A CZ3   1 
ATOM   7904  C  CH2   . TRP A 1 2545 ? 185.782 211.886 187.391 1.00 16.29  ? 2545 TRP A CH2   1 
ATOM   7905  N  N     . SER A 1 2546 ? 184.939 213.987 194.240 1.00 26.58  ? 2546 SER A N     1 
ATOM   7906  C  CA    . SER A 1 2546 ? 184.753 213.669 195.647 1.00 22.89  ? 2546 SER A CA    1 
ATOM   7907  C  C     . SER A 1 2546 ? 184.804 212.156 195.816 1.00 23.99  ? 2546 SER A C     1 
ATOM   7908  O  O     . SER A 1 2546 ? 184.146 211.427 195.057 1.00 26.42  ? 2546 SER A O     1 
ATOM   7909  C  CB    . SER A 1 2546 ? 183.423 214.224 196.171 1.00 28.32  ? 2546 SER A CB    1 
ATOM   7910  O  OG    . SER A 1 2546 ? 182.352 213.875 195.312 1.00 35.58  ? 2546 SER A OG    1 
ATOM   7911  N  N     . PRO A 1 2547 ? 185.560 211.643 196.784 1.00 29.94  ? 2547 PRO A N     1 
ATOM   7912  C  CA    . PRO A 1 2547 ? 185.616 210.191 196.975 1.00 27.37  ? 2547 PRO A CA    1 
ATOM   7913  C  C     . PRO A 1 2547 ? 184.263 209.631 197.389 1.00 24.97  ? 2547 PRO A C     1 
ATOM   7914  O  O     . PRO A 1 2547 ? 183.491 210.272 198.105 1.00 24.99  ? 2547 PRO A O     1 
ATOM   7915  C  CB    . PRO A 1 2547 ? 186.660 210.017 198.083 1.00 22.36  ? 2547 PRO A CB    1 
ATOM   7916  C  CG    . PRO A 1 2547 ? 186.658 211.316 198.809 1.00 21.80  ? 2547 PRO A CG    1 
ATOM   7917  C  CD    . PRO A 1 2547 ? 186.367 212.367 197.780 1.00 21.53  ? 2547 PRO A CD    1 
ATOM   7918  N  N     . TRP A 1 2548 ? 183.979 208.414 196.920 1.00 21.33  ? 2548 TRP A N     1 
ATOM   7919  C  CA    . TRP A 1 2548 ? 182.732 207.746 197.274 1.00 21.46  ? 2548 TRP A CA    1 
ATOM   7920  C  C     . TRP A 1 2548 ? 182.675 207.361 198.745 1.00 21.40  ? 2548 TRP A C     1 
ATOM   7921  O  O     . TRP A 1 2548 ? 181.579 207.165 199.279 1.00 22.15  ? 2548 TRP A O     1 
ATOM   7922  C  CB    . TRP A 1 2548 ? 182.536 206.500 196.411 1.00 20.52  ? 2548 TRP A CB    1 
ATOM   7923  C  CG    . TRP A 1 2548 ? 181.785 206.745 195.143 1.00 15.52  ? 2548 TRP A CG    1 
ATOM   7924  C  CD1   . TRP A 1 2548 ? 182.237 206.549 193.872 1.00 14.12  ? 2548 TRP A CD1   1 
ATOM   7925  C  CD2   . TRP A 1 2548 ? 180.437 207.211 195.022 1.00 14.69  ? 2548 TRP A CD2   1 
ATOM   7926  N  NE1   . TRP A 1 2548 ? 181.257 206.872 192.967 1.00 15.44  ? 2548 TRP A NE1   1 
ATOM   7927  C  CE2   . TRP A 1 2548 ? 180.142 207.281 193.648 1.00 14.02  ? 2548 TRP A CE2   1 
ATOM   7928  C  CE3   . TRP A 1 2548 ? 179.453 207.580 195.942 1.00 14.07  ? 2548 TRP A CE3   1 
ATOM   7929  C  CZ2   . TRP A 1 2548 ? 178.905 207.705 193.173 1.00 12.67  ? 2548 TRP A CZ2   1 
ATOM   7930  C  CZ3   . TRP A 1 2548 ? 178.229 208.000 195.469 1.00 13.78  ? 2548 TRP A CZ3   1 
ATOM   7931  C  CH2   . TRP A 1 2548 ? 177.965 208.061 194.098 1.00 12.48  ? 2548 TRP A CH2   1 
ATOM   7932  N  N     . GLN A 1 2549 ? 183.828 207.255 199.410 1.00 26.53  ? 2549 GLN A N     1 
ATOM   7933  C  CA    . GLN A 1 2549 ? 183.850 206.881 200.818 1.00 27.61  ? 2549 GLN A CA    1 
ATOM   7934  C  C     . GLN A 1 2549 ? 183.133 207.897 201.697 1.00 26.98  ? 2549 GLN A C     1 
ATOM   7935  O  O     . GLN A 1 2549 ? 182.657 207.536 202.779 1.00 33.71  ? 2549 GLN A O     1 
ATOM   7936  C  CB    . GLN A 1 2549 ? 185.294 206.708 201.288 1.00 21.85  ? 2549 GLN A CB    1 
ATOM   7937  C  CG    . GLN A 1 2549 ? 185.445 205.802 202.495 1.00 26.96  ? 2549 GLN A CG    1 
ATOM   7938  C  CD    . GLN A 1 2549 ? 185.137 204.354 202.178 1.00 24.92  ? 2549 GLN A CD    1 
ATOM   7939  O  OE1   . GLN A 1 2549 ? 184.214 203.766 202.740 1.00 26.41  ? 2549 GLN A OE1   1 
ATOM   7940  N  NE2   . GLN A 1 2549 ? 185.911 203.769 201.273 1.00 22.86  ? 2549 GLN A NE2   1 
ATOM   7941  N  N     . ALA A 1 2550 ? 183.044 209.155 201.260 1.00 22.13  ? 2550 ALA A N     1 
ATOM   7942  C  CA    . ALA A 1 2550 ? 182.297 210.148 202.023 1.00 25.21  ? 2550 ALA A CA    1 
ATOM   7943  C  C     . ALA A 1 2550 ? 180.806 209.835 202.041 1.00 24.24  ? 2550 ALA A C     1 
ATOM   7944  O  O     . ALA A 1 2550 ? 180.097 210.257 202.960 1.00 26.67  ? 2550 ALA A O     1 
ATOM   7945  C  CB    . ALA A 1 2550 ? 182.542 211.544 201.452 1.00 25.69  ? 2550 ALA A CB    1 
ATOM   7946  N  N     . LYS A 1 2551 ? 180.316 209.106 201.041 1.00 24.47  ? 2551 LYS A N     1 
ATOM   7947  C  CA    . LYS A 1 2551 ? 178.929 208.664 201.003 1.00 17.36  ? 2551 LYS A CA    1 
ATOM   7948  C  C     . LYS A 1 2551 ? 178.717 207.334 201.707 1.00 23.98  ? 2551 LYS A C     1 
ATOM   7949  O  O     . LYS A 1 2551 ? 177.590 206.828 201.718 1.00 29.73  ? 2551 LYS A O     1 
ATOM   7950  C  CB    . LYS A 1 2551 ? 178.445 208.555 199.555 1.00 19.14  ? 2551 LYS A CB    1 
ATOM   7951  C  CG    . LYS A 1 2551 ? 178.473 209.859 198.785 1.00 24.11  ? 2551 LYS A CG    1 
ATOM   7952  C  CD    . LYS A 1 2551 ? 177.448 210.835 199.331 1.00 22.72  ? 2551 LYS A CD    1 
ATOM   7953  C  CE    . LYS A 1 2551 ? 177.318 212.046 198.433 1.00 24.73  ? 2551 LYS A CE    1 
ATOM   7954  N  NZ    . LYS A 1 2551 ? 176.704 211.681 197.126 1.00 24.13  ? 2551 LYS A NZ    1 
ATOM   7955  N  N     . VAL A 1 2552 ? 179.765 206.757 202.285 1.00 26.39  ? 2552 VAL A N     1 
ATOM   7956  C  CA    . VAL A 1 2552 ? 179.670 205.474 202.975 1.00 25.48  ? 2552 VAL A CA    1 
ATOM   7957  C  C     . VAL A 1 2552 ? 179.904 205.708 204.462 1.00 27.56  ? 2552 VAL A C     1 
ATOM   7958  O  O     . VAL A 1 2552 ? 181.054 205.664 204.923 1.00 31.79  ? 2552 VAL A O     1 
ATOM   7959  C  CB    . VAL A 1 2552 ? 180.675 204.460 202.408 1.00 24.93  ? 2552 VAL A CB    1 
ATOM   7960  C  CG1   . VAL A 1 2552 ? 180.531 203.117 203.106 1.00 23.02  ? 2552 VAL A CG1   1 
ATOM   7961  C  CG2   . VAL A 1 2552 ? 180.493 204.312 200.911 1.00 19.76  ? 2552 VAL A CG2   1 
ATOM   7962  N  N     . PRO A 1 2553 ? 178.862 205.973 205.242 1.00 30.29  ? 2553 PRO A N     1 
ATOM   7963  C  CA    . PRO A 1 2553 ? 179.036 206.148 206.684 1.00 30.74  ? 2553 PRO A CA    1 
ATOM   7964  C  C     . PRO A 1 2553 ? 178.859 204.845 207.444 1.00 37.14  ? 2553 PRO A C     1 
ATOM   7965  O  O     . PRO A 1 2553 ? 178.044 203.989 207.096 1.00 43.30  ? 2553 PRO A O     1 
ATOM   7966  C  CB    . PRO A 1 2553 ? 177.922 207.142 207.038 1.00 39.21  ? 2553 PRO A CB    1 
ATOM   7967  C  CG    . PRO A 1 2553 ? 176.826 206.813 206.064 1.00 39.04  ? 2553 PRO A CG    1 
ATOM   7968  C  CD    . PRO A 1 2553 ? 177.472 206.228 204.823 1.00 30.07  ? 2553 PRO A CD    1 
ATOM   7969  N  N     . GLN A 1 2554 ? 179.653 204.703 208.501 1.00 40.20  ? 2554 GLN A N     1 
ATOM   7970  C  CA    . GLN A 1 2554 ? 179.521 203.556 209.391 1.00 33.98  ? 2554 GLN A CA    1 
ATOM   7971  C  C     . GLN A 1 2554 ? 178.231 203.700 210.187 1.00 33.27  ? 2554 GLN A C     1 
ATOM   7972  O  O     . GLN A 1 2554 ? 178.153 204.507 211.118 1.00 41.73  ? 2554 GLN A O     1 
ATOM   7973  C  CB    . GLN A 1 2554 ? 180.730 203.455 210.314 1.00 34.61  ? 2554 GLN A CB    1 
ATOM   7974  C  CG    . GLN A 1 2554 ? 180.719 202.235 211.218 1.00 40.75  ? 2554 GLN A CG    1 
ATOM   7975  C  CD    . GLN A 1 2554 ? 181.962 202.137 212.078 1.00 55.18  ? 2554 GLN A CD    1 
ATOM   7976  O  OE1   . GLN A 1 2554 ? 182.832 203.006 212.032 1.00 68.76  ? 2554 GLN A OE1   1 
ATOM   7977  N  NE2   . GLN A 1 2554 ? 182.052 201.075 212.871 1.00 51.97  ? 2554 GLN A NE2   1 
ATOM   7978  N  N     . ILE A 1 2555 ? 177.216 202.925 209.821 1.00 30.16  ? 2555 ILE A N     1 
ATOM   7979  C  CA    . ILE A 1 2555 ? 175.911 203.013 210.448 1.00 33.21  ? 2555 ILE A CA    1 
ATOM   7980  C  C     . ILE A 1 2555 ? 175.821 201.973 211.554 1.00 33.67  ? 2555 ILE A C     1 
ATOM   7981  O  O     . ILE A 1 2555 ? 176.612 201.029 211.629 1.00 35.48  ? 2555 ILE A O     1 
ATOM   7982  C  CB    . ILE A 1 2555 ? 174.764 202.825 209.429 1.00 36.85  ? 2555 ILE A CB    1 
ATOM   7983  C  CG1   . ILE A 1 2555 ? 174.784 201.404 208.863 1.00 29.74  ? 2555 ILE A CG1   1 
ATOM   7984  C  CG2   . ILE A 1 2555 ? 174.867 203.853 208.313 1.00 31.29  ? 2555 ILE A CG2   1 
ATOM   7985  C  CD1   . ILE A 1 2555 ? 173.510 201.012 208.155 1.00 25.30  ? 2555 ILE A CD1   1 
ATOM   7986  N  N     . GLU A 1 2556 ? 174.840 202.154 212.433 1.00 34.72  ? 2556 GLU A N     1 
ATOM   7987  C  CA    . GLU A 1 2556 ? 174.526 201.197 213.490 1.00 33.35  ? 2556 GLU A CA    1 
ATOM   7988  C  C     . GLU A 1 2556 ? 173.092 200.731 213.269 1.00 34.43  ? 2556 GLU A C     1 
ATOM   7989  O  O     . GLU A 1 2556 ? 172.141 201.447 213.598 1.00 38.39  ? 2556 GLU A O     1 
ATOM   7990  C  CB    . GLU A 1 2556 ? 174.709 201.816 214.872 1.00 30.96  ? 2556 GLU A CB    1 
ATOM   7991  C  CG    . GLU A 1 2556 ? 176.103 202.361 215.137 1.00 40.32  ? 2556 GLU A CG    1 
ATOM   7992  C  CD    . GLU A 1 2556 ? 177.089 201.284 215.549 1.00 44.53  ? 2556 GLU A CD    1 
ATOM   7993  O  OE1   . GLU A 1 2556 ? 177.365 200.378 214.735 1.00 45.38  ? 2556 GLU A OE1   1 
ATOM   7994  O  OE2   . GLU A 1 2556 ? 177.589 201.344 216.693 1.00 47.35  ? 2556 GLU A OE2   1 
ATOM   7995  N  N     . VAL A 1 2557 ? 172.940 199.534 212.702 1.00 32.49  ? 2557 VAL A N     1 
ATOM   7996  C  CA    . VAL A 1 2557 ? 171.616 198.987 212.439 1.00 28.12  ? 2557 VAL A CA    1 
ATOM   7997  C  C     . VAL A 1 2557 ? 170.897 198.739 213.757 1.00 36.31  ? 2557 VAL A C     1 
ATOM   7998  O  O     . VAL A 1 2557 ? 171.511 198.352 214.760 1.00 37.48  ? 2557 VAL A O     1 
ATOM   7999  C  CB    . VAL A 1 2557 ? 171.728 197.696 211.610 1.00 25.84  ? 2557 VAL A CB    1 
ATOM   8000  C  CG1   . VAL A 1 2557 ? 170.351 197.206 211.188 1.00 29.25  ? 2557 VAL A CG1   1 
ATOM   8001  C  CG2   . VAL A 1 2557 ? 172.608 197.924 210.396 1.00 30.33  ? 2557 VAL A CG2   1 
ATOM   8002  N  N     . GLU A 1 2558 ? 169.587 198.975 213.764 1.00 38.25  ? 2558 GLU A N     1 
ATOM   8003  C  CA    . GLU A 1 2558 ? 168.789 198.721 214.953 1.00 33.27  ? 2558 GLU A CA    1 
ATOM   8004  C  C     . GLU A 1 2558 ? 168.819 197.239 215.306 1.00 33.34  ? 2558 GLU A C     1 
ATOM   8005  O  O     . GLU A 1 2558 ? 168.947 196.371 214.438 1.00 38.55  ? 2558 GLU A O     1 
ATOM   8006  C  CB    . GLU A 1 2558 ? 167.346 199.183 214.741 1.00 42.52  ? 2558 GLU A CB    1 
ATOM   8007  C  CG    . GLU A 1 2558 ? 167.178 200.690 214.601 1.00 50.60  ? 2558 GLU A CG    1 
ATOM   8008  C  CD    . GLU A 1 2558 ? 167.457 201.192 213.197 1.00 59.17  ? 2558 GLU A CD    1 
ATOM   8009  O  OE1   . GLU A 1 2558 ? 167.723 200.359 212.306 1.00 61.18  ? 2558 GLU A OE1   1 
ATOM   8010  O  OE2   . GLU A 1 2558 ? 167.409 202.422 212.985 1.00 49.09  ? 2558 GLU A OE2   1 
ATOM   8011  N  N     . THR A 1 2559 ? 168.707 196.955 216.606 1.00 36.92  ? 2559 THR A N     1 
ATOM   8012  C  CA    . THR A 1 2559 ? 168.835 195.581 217.082 1.00 36.94  ? 2559 THR A CA    1 
ATOM   8013  C  C     . THR A 1 2559 ? 167.739 194.687 216.513 1.00 31.64  ? 2559 THR A C     1 
ATOM   8014  O  O     . THR A 1 2559 ? 167.997 193.537 216.141 1.00 36.74  ? 2559 THR A O     1 
ATOM   8015  C  CB    . THR A 1 2559 ? 168.811 195.554 218.611 1.00 37.54  ? 2559 THR A CB    1 
ATOM   8016  O  OG1   . THR A 1 2559 ? 169.902 196.331 219.119 1.00 39.29  ? 2559 THR A OG1   1 
ATOM   8017  C  CG2   . THR A 1 2559 ? 168.937 194.133 219.120 1.00 37.95  ? 2559 THR A CG2   1 
ATOM   8018  N  N     . HIS A 1 2560 ? 166.513 195.196 216.429 1.00 31.10  ? 2560 HIS A N     1 
ATOM   8019  C  CA    . HIS A 1 2560 ? 165.411 194.408 215.893 1.00 32.63  ? 2560 HIS A CA    1 
ATOM   8020  C  C     . HIS A 1 2560 ? 165.444 194.290 214.376 1.00 33.86  ? 2560 HIS A C     1 
ATOM   8021  O  O     . HIS A 1 2560 ? 164.655 193.523 213.815 1.00 38.64  ? 2560 HIS A O     1 
ATOM   8022  C  CB    . HIS A 1 2560 ? 164.075 195.010 216.334 1.00 33.17  ? 2560 HIS A CB    1 
ATOM   8023  C  CG    . HIS A 1 2560 ? 163.562 196.075 215.418 1.00 42.48  ? 2560 HIS A CG    1 
ATOM   8024  N  ND1   . HIS A 1 2560 ? 163.947 197.394 215.524 1.00 42.24  ? 2560 HIS A ND1   1 
ATOM   8025  C  CD2   . HIS A 1 2560 ? 162.693 196.019 214.381 1.00 43.00  ? 2560 HIS A CD2   1 
ATOM   8026  C  CE1   . HIS A 1 2560 ? 163.339 198.104 214.590 1.00 46.73  ? 2560 HIS A CE1   1 
ATOM   8027  N  NE2   . HIS A 1 2560 ? 162.574 197.293 213.882 1.00 52.00  ? 2560 HIS A NE2   1 
ATOM   8028  N  N     . LYS A 1 2561 ? 166.329 195.024 213.701 1.00 33.25  ? 2561 LYS A N     1 
ATOM   8029  C  CA    . LYS A 1 2561 ? 166.421 195.018 212.246 1.00 32.10  ? 2561 LYS A CA    1 
ATOM   8030  C  C     . LYS A 1 2561 ? 167.677 194.306 211.755 1.00 33.03  ? 2561 LYS A C     1 
ATOM   8031  O  O     . LYS A 1 2561 ? 168.219 194.646 210.701 1.00 37.19  ? 2561 LYS A O     1 
ATOM   8032  C  CB    . LYS A 1 2561 ? 166.376 196.446 211.705 1.00 36.68  ? 2561 LYS A CB    1 
ATOM   8033  C  CG    . LYS A 1 2561 ? 164.985 196.931 211.334 1.00 42.41  ? 2561 LYS A CG    1 
ATOM   8034  C  CD    . LYS A 1 2561 ? 165.051 198.007 210.261 1.00 51.00  ? 2561 LYS A CD    1 
ATOM   8035  C  CE    . LYS A 1 2561 ? 163.872 197.911 209.305 1.00 46.90  ? 2561 LYS A CE    1 
ATOM   8036  N  NZ    . LYS A 1 2561 ? 164.076 198.742 208.086 1.00 30.11  ? 2561 LYS A NZ    1 
ATOM   8037  N  N     . VAL A 1 2562 ? 168.145 193.312 212.502 1.00 31.75  ? 2562 VAL A N     1 
ATOM   8038  C  CA    . VAL A 1 2562 ? 169.377 192.608 212.162 1.00 28.33  ? 2562 VAL A CA    1 
ATOM   8039  C  C     . VAL A 1 2562 ? 169.107 191.674 210.989 1.00 33.61  ? 2562 VAL A C     1 
ATOM   8040  O  O     . VAL A 1 2562 ? 168.221 190.815 211.057 1.00 33.04  ? 2562 VAL A O     1 
ATOM   8041  C  CB    . VAL A 1 2562 ? 169.920 191.833 213.370 1.00 28.13  ? 2562 VAL A CB    1 
ATOM   8042  C  CG1   . VAL A 1 2562 ? 170.966 190.831 212.927 1.00 26.72  ? 2562 VAL A CG1   1 
ATOM   8043  C  CG2   . VAL A 1 2562 ? 170.505 192.788 214.388 1.00 25.85  ? 2562 VAL A CG2   1 
ATOM   8044  N  N     . ALA A 1 2563 ? 169.874 191.845 209.910 1.00 32.76  ? 2563 ALA A N     1 
ATOM   8045  C  CA    . ALA A 1 2563 ? 169.792 190.999 208.718 1.00 28.73  ? 2563 ALA A CA    1 
ATOM   8046  C  C     . ALA A 1 2563 ? 168.384 190.972 208.129 1.00 36.50  ? 2563 ALA A C     1 
ATOM   8047  O  O     . ALA A 1 2563 ? 167.945 189.951 207.594 1.00 35.32  ? 2563 ALA A O     1 
ATOM   8048  C  CB    . ALA A 1 2563 ? 170.276 189.577 209.011 1.00 22.01  ? 2563 ALA A CB    1 
ATOM   8049  N  N     . ALA A 1 2564 ? 167.670 192.089 208.222 1.00 39.68  ? 2564 ALA A N     1 
ATOM   8050  C  CA    . ALA A 1 2564 ? 166.348 192.178 207.627 1.00 37.21  ? 2564 ALA A CA    1 
ATOM   8051  C  C     . ALA A 1 2564 ? 166.462 192.222 206.103 1.00 39.45  ? 2564 ALA A C     1 
ATOM   8052  O  O     . ALA A 1 2564 ? 167.494 192.629 205.563 1.00 40.68  ? 2564 ALA A O     1 
ATOM   8053  C  CB    . ALA A 1 2564 ? 165.615 193.416 208.139 1.00 36.84  ? 2564 ALA A CB    1 
ATOM   8054  N  N     . PRO A 1 2565 ? 165.419 191.793 205.386 1.00 41.56  ? 2565 PRO A N     1 
ATOM   8055  C  CA    . PRO A 1 2565 ? 165.508 191.766 203.915 1.00 43.10  ? 2565 PRO A CA    1 
ATOM   8056  C  C     . PRO A 1 2565 ? 165.750 193.126 203.279 1.00 35.24  ? 2565 PRO A C     1 
ATOM   8057  O  O     . PRO A 1 2565 ? 166.414 193.197 202.237 1.00 37.24  ? 2565 PRO A O     1 
ATOM   8058  C  CB    . PRO A 1 2565 ? 164.153 191.178 203.493 1.00 40.82  ? 2565 PRO A CB    1 
ATOM   8059  C  CG    . PRO A 1 2565 ? 163.256 191.375 204.668 1.00 40.03  ? 2565 PRO A CG    1 
ATOM   8060  C  CD    . PRO A 1 2565 ? 164.138 191.251 205.867 1.00 44.92  ? 2565 PRO A CD    1 
ATOM   8061  N  N     . ASP A 1 2566 ? 165.274 194.209 203.894 1.00 37.35  ? 2566 ASP A N     1 
ATOM   8062  C  CA    . ASP A 1 2566 ? 165.412 195.535 203.224 1.00 37.83  ? 2566 ASP A CA    1 
ATOM   8063  C  C     . ASP A 1 2566 ? 166.446 196.400 203.955 1.00 31.53  ? 2566 ASP A C     1 
ATOM   8064  O  O     . ASP A 1 2566 ? 166.372 197.641 203.830 1.00 25.59  ? 2566 ASP A O     1 
ATOM   8065  C  CB    . ASP A 1 2566 ? 164.066 196.228 203.081 1.00 44.87  ? 2566 ASP A CB    1 
ATOM   8066  C  CG    . ASP A 1 2566 ? 163.063 195.510 202.191 1.00 47.08  ? 2566 ASP A CG    1 
ATOM   8067  O  OD1   . ASP A 1 2566 ? 163.372 195.321 200.997 1.00 41.33  ? 2566 ASP A OD1   1 
ATOM   8068  O  OD2   . ASP A 1 2566 ? 161.985 195.140 202.702 1.00 57.16  ? 2566 ASP A OD2   1 
ATOM   8069  N  N     . VAL A 1 2567 ? 167.376 195.769 204.678 1.00 34.96  ? 2567 VAL A N     1 
ATOM   8070  C  CA    . VAL A 1 2567 ? 168.435 196.528 205.411 1.00 32.02  ? 2567 VAL A CA    1 
ATOM   8071  C  C     . VAL A 1 2567 ? 169.764 196.356 204.661 1.00 22.73  ? 2567 VAL A C     1 
ATOM   8072  O  O     . VAL A 1 2567 ? 170.238 195.207 204.552 1.00 26.03  ? 2567 VAL A O     1 
ATOM   8073  C  CB    . VAL A 1 2567 ? 168.564 196.098 206.885 1.00 28.28  ? 2567 VAL A CB    1 
ATOM   8074  C  CG1   . VAL A 1 2567 ? 169.788 196.716 207.548 1.00 23.60  ? 2567 VAL A CG1   1 
ATOM   8075  C  CG2   . VAL A 1 2567 ? 167.304 196.418 207.679 1.00 27.40  ? 2567 VAL A CG2   1 
ATOM   8076  N  N     . VAL A 1 2568 ? 170.331 197.460 204.168 1.00 17.38  ? 2568 VAL A N     1 
ATOM   8077  C  CA    . VAL A 1 2568 ? 171.608 197.394 203.399 1.00 14.66  ? 2568 VAL A CA    1 
ATOM   8078  C  C     . VAL A 1 2568 ? 172.697 198.128 204.193 1.00 16.75  ? 2568 VAL A C     1 
ATOM   8079  O  O     . VAL A 1 2568 ? 172.449 199.277 204.610 1.00 20.76  ? 2568 VAL A O     1 
ATOM   8080  C  CB    . VAL A 1 2568 ? 171.453 198.000 201.991 1.00 14.15  ? 2568 VAL A CB    1 
ATOM   8081  C  CG1   . VAL A 1 2568 ? 172.731 197.865 201.174 1.00 11.69  ? 2568 VAL A CG1   1 
ATOM   8082  C  CG2   . VAL A 1 2568 ? 170.268 197.402 201.243 1.00 18.12  ? 2568 VAL A CG2   1 
ATOM   8083  N  N     . VAL A 1 2569 ? 173.847 197.484 204.398 1.00 13.69  ? 2569 VAL A N     1 
ATOM   8084  C  CA    . VAL A 1 2569 ? 174.984 198.166 205.082 1.00 11.38  ? 2569 VAL A CA    1 
ATOM   8085  C  C     . VAL A 1 2569 ? 175.731 198.965 204.007 1.00 16.31  ? 2569 VAL A C     1 
ATOM   8086  O  O     . VAL A 1 2569 ? 176.313 198.335 203.101 1.00 22.54  ? 2569 VAL A O     1 
ATOM   8087  C  CB    . VAL A 1 2569 ? 175.917 197.180 205.809 1.00 10.39  ? 2569 VAL A CB    1 
ATOM   8088  C  CG1   . VAL A 1 2569 ? 177.124 197.884 206.416 1.00 10.42  ? 2569 VAL A CG1   1 
ATOM   8089  C  CG2   . VAL A 1 2569 ? 175.173 196.373 206.866 1.00 13.29  ? 2569 VAL A CG2   1 
ATOM   8090  N  N     . PRO A 1 2570 ? 175.727 200.313 204.056 1.00 14.66  ? 2570 PRO A N     1 
ATOM   8091  C  CA    . PRO A 1 2570 ? 176.351 201.104 203.006 1.00 16.78  ? 2570 PRO A CA    1 
ATOM   8092  C  C     . PRO A 1 2570 ? 177.789 200.689 202.746 1.00 18.05  ? 2570 PRO A C     1 
ATOM   8093  O  O     . PRO A 1 2570 ? 178.584 200.641 203.703 1.00 22.63  ? 2570 PRO A O     1 
ATOM   8094  C  CB    . PRO A 1 2570 ? 176.245 202.544 203.543 1.00 22.82  ? 2570 PRO A CB    1 
ATOM   8095  C  CG    . PRO A 1 2570 ? 175.964 202.378 205.019 1.00 19.28  ? 2570 PRO A CG    1 
ATOM   8096  C  CD    . PRO A 1 2570 ? 175.136 201.111 205.112 1.00 17.69  ? 2570 PRO A CD    1 
ATOM   8097  N  N     . THR A 1 2571 ? 178.117 200.399 201.485 1.00 15.48  ? 2571 THR A N     1 
ATOM   8098  C  CA    . THR A 1 2571 ? 179.503 200.043 201.111 1.00 16.34  ? 2571 THR A CA    1 
ATOM   8099  C  C     . THR A 1 2571 ? 179.849 200.780 199.834 1.00 20.56  ? 2571 THR A C     1 
ATOM   8100  O  O     . THR A 1 2571 ? 178.922 201.332 199.205 1.00 23.06  ? 2571 THR A O     1 
ATOM   8101  C  CB    . THR A 1 2571 ? 179.642 198.529 200.953 1.00 15.97  ? 2571 THR A CB    1 
ATOM   8102  O  OG1   . THR A 1 2571 ? 178.696 198.160 199.955 1.00 21.60  ? 2571 THR A OG1   1 
ATOM   8103  C  CG2   . THR A 1 2571 ? 179.360 197.780 202.243 1.00 19.97  ? 2571 THR A CG2   1 
ATOM   8104  N  N     . LEU A 1 2572 ? 181.130 200.801 199.459 1.00 19.73  ? 2572 LEU A N     1 
ATOM   8105  C  CA    . LEU A 1 2572 ? 181.567 201.547 198.250 1.00 17.55  ? 2572 LEU A CA    1 
ATOM   8106  C  C     . LEU A 1 2572 ? 180.764 201.065 197.034 1.00 18.27  ? 2572 LEU A C     1 
ATOM   8107  O  O     . LEU A 1 2572 ? 180.222 201.921 196.304 1.00 21.75  ? 2572 LEU A O     1 
ATOM   8108  C  CB    . LEU A 1 2572 ? 183.066 201.341 198.043 1.00 19.98  ? 2572 LEU A CB    1 
ATOM   8109  C  CG    . LEU A 1 2572 ? 183.646 201.865 196.726 1.00 21.26  ? 2572 LEU A CG    1 
ATOM   8110  C  CD1   . LEU A 1 2572 ? 183.634 203.381 196.692 1.00 21.32  ? 2572 LEU A CD1   1 
ATOM   8111  C  CD2   . LEU A 1 2572 ? 185.054 201.336 196.528 1.00 25.68  ? 2572 LEU A CD2   1 
ATOM   8112  N  N     . ASP A 1 2573 ? 180.684 199.749 196.833 1.00 16.97  ? 2573 ASP A N     1 
ATOM   8113  C  CA    . ASP A 1 2573 ? 179.969 199.196 195.650 1.00 18.31  ? 2573 ASP A CA    1 
ATOM   8114  C  C     . ASP A 1 2573 ? 178.482 199.538 195.766 1.00 18.61  ? 2573 ASP A C     1 
ATOM   8115  O  O     . ASP A 1 2573 ? 177.866 199.864 194.729 1.00 20.87  ? 2573 ASP A O     1 
ATOM   8116  C  CB    . ASP A 1 2573 ? 180.249 197.711 195.491 1.00 17.95  ? 2573 ASP A CB    1 
ATOM   8117  C  CG    . ASP A 1 2573 ? 181.722 197.348 195.378 1.00 29.99  ? 2573 ASP A CG    1 
ATOM   8118  O  OD1   . ASP A 1 2573 ? 182.108 196.779 194.336 1.00 32.98  ? 2573 ASP A OD1   1 
ATOM   8119  O  OD2   . ASP A 1 2573 ? 182.473 197.643 196.332 1.00 29.36  ? 2573 ASP A OD2   1 
ATOM   8120  N  N     . THR A 1 2574 ? 177.937 199.482 196.983 1.00 16.77  ? 2574 THR A N     1 
ATOM   8121  C  CA    . THR A 1 2574 ? 176.513 199.804 197.200 1.00 13.36  ? 2574 THR A CA    1 
ATOM   8122  C  C     . THR A 1 2574 ? 176.251 201.230 196.770 1.00 14.86  ? 2574 THR A C     1 
ATOM   8123  O  O     . THR A 1 2574 ? 175.282 201.444 196.019 1.00 18.58  ? 2574 THR A O     1 
ATOM   8124  C  CB    . THR A 1 2574 ? 176.172 199.587 198.673 1.00 17.46  ? 2574 THR A CB    1 
ATOM   8125  O  OG1   . THR A 1 2574 ? 176.254 198.180 198.872 1.00 22.15  ? 2574 THR A OG1   1 
ATOM   8126  C  CG2   . THR A 1 2574 ? 174.780 200.075 199.030 1.00 18.86  ? 2574 THR A CG2   1 
ATOM   8127  N  N     . VAL A 1 2575 ? 177.089 202.176 197.202 1.00 15.52  ? 2575 VAL A N     1 
ATOM   8128  C  CA    . VAL A 1 2575 ? 176.839 203.618 196.895 1.00 12.46  ? 2575 VAL A CA    1 
ATOM   8129  C  C     . VAL A 1 2575 ? 177.139 203.890 195.410 1.00 13.09  ? 2575 VAL A C     1 
ATOM   8130  O  O     . VAL A 1 2575 ? 176.452 204.754 194.827 1.00 13.39  ? 2575 VAL A O     1 
ATOM   8131  C  CB    . VAL A 1 2575 ? 177.644 204.553 197.820 1.00 12.95  ? 2575 VAL A CB    1 
ATOM   8132  C  CG1   . VAL A 1 2575 ? 177.302 204.326 199.287 1.00 14.81  ? 2575 VAL A CG1   1 
ATOM   8133  C  CG2   . VAL A 1 2575 ? 179.146 204.432 197.593 1.00 14.39  ? 2575 VAL A CG2   1 
ATOM   8134  N  N     . ARG A 1 2576 ? 178.112 203.182 194.823 1.00 13.64  ? 2576 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2576 ? 178.415 203.372 193.407 1.00 10.06  ? 2576 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2576 ? 177.320 202.782 192.526 1.00 10.56  ? 2576 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2576 ? 176.815 203.446 191.609 1.00 14.27  ? 2576 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2576 ? 179.766 202.742 193.067 1.00 13.50  ? 2576 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2576 ? 180.954 203.475 193.644 1.00 16.40  ? 2576 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2576 ? 182.263 202.881 193.160 1.00 17.84  ? 2576 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2576 ? 182.228 201.426 193.112 1.00 16.73  ? 2576 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2576 ? 183.304 200.653 193.149 1.00 23.84  ? 2576 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2576 ? 184.520 201.165 193.237 1.00 13.42  ? 2576 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2576 ? 183.156 199.332 193.098 1.00 31.75  ? 2576 ARG A NH2   1 
ATOM   8145  N  N     . HIS A 1 2577 ? 176.935 201.532 192.795 1.00 11.21  ? 2577 HIS A N     1 
ATOM   8146  C  CA    . HIS A 1 2577 ? 175.895 200.892 192.004 1.00 9.73   ? 2577 HIS A CA    1 
ATOM   8147  C  C     . HIS A 1 2577 ? 174.548 201.567 192.203 1.00 9.51   ? 2577 HIS A C     1 
ATOM   8148  O  O     . HIS A 1 2577 ? 173.764 201.656 191.256 1.00 9.36   ? 2577 HIS A O     1 
ATOM   8149  C  CB    . HIS A 1 2577 ? 175.810 199.408 192.354 1.00 8.66   ? 2577 HIS A CB    1 
ATOM   8150  C  CG    . HIS A 1 2577 ? 177.047 198.638 192.015 1.00 7.90   ? 2577 HIS A CG    1 
ATOM   8151  N  ND1   . HIS A 1 2577 ? 177.253 197.340 192.428 1.00 12.71  ? 2577 HIS A ND1   1 
ATOM   8152  C  CD2   . HIS A 1 2577 ? 178.144 198.983 191.301 1.00 8.30   ? 2577 HIS A CD2   1 
ATOM   8153  C  CE1   . HIS A 1 2577 ? 178.423 196.918 191.983 1.00 13.34  ? 2577 HIS A CE1   1 
ATOM   8154  N  NE2   . HIS A 1 2577 ? 178.984 197.897 191.296 1.00 11.82  ? 2577 HIS A NE2   1 
ATOM   8155  N  N     . GLU A 1 2578 ? 174.264 202.054 193.413 1.00 11.18  ? 2578 GLU A N     1 
ATOM   8156  C  CA    . GLU A 1 2578 ? 173.017 202.773 193.643 1.00 9.34   ? 2578 GLU A CA    1 
ATOM   8157  C  C     . GLU A 1 2578 ? 172.952 204.035 192.797 1.00 11.64  ? 2578 GLU A C     1 
ATOM   8158  O  O     . GLU A 1 2578 ? 171.927 204.314 192.164 1.00 14.35  ? 2578 GLU A O     1 
ATOM   8159  C  CB    . GLU A 1 2578 ? 172.879 203.114 195.126 1.00 12.47  ? 2578 GLU A CB    1 
ATOM   8160  C  CG    . GLU A 1 2578 ? 172.318 201.991 195.981 1.00 16.90  ? 2578 GLU A CG    1 
ATOM   8161  C  CD    . GLU A 1 2578 ? 172.466 202.265 197.465 1.00 32.17  ? 2578 GLU A CD    1 
ATOM   8162  O  OE1   . GLU A 1 2578 ? 171.879 201.518 198.273 1.00 25.34  ? 2578 GLU A OE1   1 
ATOM   8163  O  OE2   . GLU A 1 2578 ? 173.170 203.232 197.826 1.00 31.43  ? 2578 GLU A OE2   1 
ATOM   8164  N  N     . ALA A 1 2579 ? 174.043 204.804 192.761 1.00 11.06  ? 2579 ALA A N     1 
ATOM   8165  C  CA    . ALA A 1 2579 ? 174.066 206.010 191.939 1.00 8.29   ? 2579 ALA A CA    1 
ATOM   8166  C  C     . ALA A 1 2579 ? 173.927 205.678 190.459 1.00 12.14  ? 2579 ALA A C     1 
ATOM   8167  O  O     . ALA A 1 2579 ? 173.177 206.345 189.735 1.00 16.64  ? 2579 ALA A O     1 
ATOM   8168  C  CB    . ALA A 1 2579 ? 175.352 206.792 192.192 1.00 7.00   ? 2579 ALA A CB    1 
ATOM   8169  N  N     . LEU A 1 2580 ? 174.640 204.650 189.991 1.00 11.04  ? 2580 LEU A N     1 
ATOM   8170  C  CA    . LEU A 1 2580 ? 174.560 204.284 188.580 1.00 9.89   ? 2580 LEU A CA    1 
ATOM   8171  C  C     . LEU A 1 2580 ? 173.155 203.826 188.203 1.00 12.15  ? 2580 LEU A C     1 
ATOM   8172  O  O     . LEU A 1 2580 ? 172.626 204.209 187.149 1.00 16.14  ? 2580 LEU A O     1 
ATOM   8173  C  CB    . LEU A 1 2580 ? 175.586 203.198 188.267 1.00 8.77   ? 2580 LEU A CB    1 
ATOM   8174  C  CG    . LEU A 1 2580 ? 175.759 202.812 186.800 1.00 8.62   ? 2580 LEU A CG    1 
ATOM   8175  C  CD1   . LEU A 1 2580 ? 176.329 203.971 186.005 1.00 9.75   ? 2580 LEU A CD1   1 
ATOM   8176  C  CD2   . LEU A 1 2580 ? 176.654 201.595 186.687 1.00 10.22  ? 2580 LEU A CD2   1 
ATOM   8177  N  N     . LEU A 1 2581 ? 172.531 203.007 189.053 1.00 10.76  ? 2581 LEU A N     1 
ATOM   8178  C  CA    . LEU A 1 2581 ? 171.180 202.539 188.773 1.00 9.12   ? 2581 LEU A CA    1 
ATOM   8179  C  C     . LEU A 1 2581 ? 170.178 203.680 188.827 1.00 12.00  ? 2581 LEU A C     1 
ATOM   8180  O  O     . LEU A 1 2581 ? 169.230 203.707 188.041 1.00 12.79  ? 2581 LEU A O     1 
ATOM   8181  C  CB    . LEU A 1 2581 ? 170.785 201.431 189.748 1.00 10.30  ? 2581 LEU A CB    1 
ATOM   8182  C  CG    . LEU A 1 2581 ? 171.541 200.107 189.627 1.00 8.87   ? 2581 LEU A CG    1 
ATOM   8183  C  CD1   . LEU A 1 2581 ? 171.018 199.100 190.636 1.00 7.76   ? 2581 LEU A CD1   1 
ATOM   8184  C  CD2   . LEU A 1 2581 ? 171.441 199.561 188.216 1.00 10.16  ? 2581 LEU A CD2   1 
ATOM   8185  N  N     . TYR A 1 2582 ? 170.359 204.629 189.749 1.00 13.25  ? 2582 TYR A N     1 
ATOM   8186  C  CA    . TYR A 1 2582 ? 169.479 205.793 189.775 1.00 11.37  ? 2582 TYR A CA    1 
ATOM   8187  C  C     . TYR A 1 2582 ? 169.613 206.594 188.487 1.00 12.87  ? 2582 TYR A C     1 
ATOM   8188  O  O     . TYR A 1 2582 ? 168.610 207.035 187.913 1.00 15.54  ? 2582 TYR A O     1 
ATOM   8189  C  CB    . TYR A 1 2582 ? 169.789 206.655 191.002 1.00 10.19  ? 2582 TYR A CB    1 
ATOM   8190  C  CG    . TYR A 1 2582 ? 168.870 207.845 191.217 1.00 16.99  ? 2582 TYR A CG    1 
ATOM   8191  C  CD1   . TYR A 1 2582 ? 168.012 207.888 192.306 1.00 22.04  ? 2582 TYR A CD1   1 
ATOM   8192  C  CD2   . TYR A 1 2582 ? 168.897 208.946 190.367 1.00 20.30  ? 2582 TYR A CD2   1 
ATOM   8193  C  CE1   . TYR A 1 2582 ? 167.179 208.966 192.519 1.00 22.95  ? 2582 TYR A CE1   1 
ATOM   8194  C  CE2   . TYR A 1 2582 ? 168.066 210.028 190.571 1.00 22.39  ? 2582 TYR A CE2   1 
ATOM   8195  C  CZ    . TYR A 1 2582 ? 167.212 210.035 191.650 1.00 26.98  ? 2582 TYR A CZ    1 
ATOM   8196  O  OH    . TYR A 1 2582 ? 166.388 211.117 191.859 1.00 43.61  ? 2582 TYR A OH    1 
ATOM   8197  N  N     . THR A 1 2583 ? 170.847 206.779 188.013 1.00 15.29  ? 2583 THR A N     1 
ATOM   8198  C  CA    . THR A 1 2583 ? 171.059 207.501 186.763 1.00 12.03  ? 2583 THR A CA    1 
ATOM   8199  C  C     . THR A 1 2583 ? 170.374 206.799 185.598 1.00 13.56  ? 2583 THR A C     1 
ATOM   8200  O  O     . THR A 1 2583 ? 169.704 207.443 184.782 1.00 18.84  ? 2583 THR A O     1 
ATOM   8201  C  CB    . THR A 1 2583 ? 172.558 207.647 186.494 1.00 14.26  ? 2583 THR A CB    1 
ATOM   8202  O  OG1   . THR A 1 2583 ? 173.107 208.646 187.362 1.00 25.76  ? 2583 THR A OG1   1 
ATOM   8203  C  CG2   . THR A 1 2583 ? 172.815 208.038 185.047 1.00 14.45  ? 2583 THR A CG2   1 
ATOM   8204  N  N     . TRP A 1 2584 ? 170.517 205.475 185.511 1.00 13.72  ? 2584 TRP A N     1 
ATOM   8205  C  CA    . TRP A 1 2584 ? 169.929 204.756 184.384 1.00 9.30   ? 2584 TRP A CA    1 
ATOM   8206  C  C     . TRP A 1 2584 ? 168.411 204.660 184.489 1.00 10.63  ? 2584 TRP A C     1 
ATOM   8207  O  O     . TRP A 1 2584 ? 167.720 204.680 183.465 1.00 14.55  ? 2584 TRP A O     1 
ATOM   8208  C  CB    . TRP A 1 2584 ? 170.544 203.364 184.268 1.00 8.85   ? 2584 TRP A CB    1 
ATOM   8209  C  CG    . TRP A 1 2584 ? 171.913 203.366 183.672 1.00 11.29  ? 2584 TRP A CG    1 
ATOM   8210  C  CD1   . TRP A 1 2584 ? 172.477 204.351 182.920 1.00 10.15  ? 2584 TRP A CD1   1 
ATOM   8211  C  CD2   . TRP A 1 2584 ? 172.894 202.329 183.777 1.00 13.36  ? 2584 TRP A CD2   1 
ATOM   8212  N  NE1   . TRP A 1 2584 ? 173.750 203.995 182.549 1.00 8.75   ? 2584 TRP A NE1   1 
ATOM   8213  C  CE2   . TRP A 1 2584 ? 174.030 202.757 183.063 1.00 10.07  ? 2584 TRP A CE2   1 
ATOM   8214  C  CE3   . TRP A 1 2584 ? 172.923 201.080 184.405 1.00 7.47   ? 2584 TRP A CE3   1 
ATOM   8215  C  CZ2   . TRP A 1 2584 ? 175.180 201.983 182.962 1.00 10.50  ? 2584 TRP A CZ2   1 
ATOM   8216  C  CZ3   . TRP A 1 2584 ? 174.064 200.313 184.301 1.00 8.09   ? 2584 TRP A CZ3   1 
ATOM   8217  C  CH2   . TRP A 1 2584 ? 175.177 200.766 183.584 1.00 11.83  ? 2584 TRP A CH2   1 
ATOM   8218  N  N     . LEU A 1 2585 ? 167.873 204.553 185.705 1.00 12.70  ? 2585 LEU A N     1 
ATOM   8219  C  CA    . LEU A 1 2585 ? 166.434 204.419 185.894 1.00 10.78  ? 2585 LEU A CA    1 
ATOM   8220  C  C     . LEU A 1 2585 ? 165.703 205.740 185.712 1.00 13.59  ? 2585 LEU A C     1 
ATOM   8221  O  O     . LEU A 1 2585 ? 164.572 205.749 185.215 1.00 17.26  ? 2585 LEU A O     1 
ATOM   8222  C  CB    . LEU A 1 2585 ? 166.140 203.851 187.284 1.00 9.42   ? 2585 LEU A CB    1 
ATOM   8223  C  CG    . LEU A 1 2585 ? 166.371 202.357 187.513 1.00 12.55  ? 2585 LEU A CG    1 
ATOM   8224  C  CD1   . LEU A 1 2585 ? 166.505 202.065 188.997 1.00 12.63  ? 2585 LEU A CD1   1 
ATOM   8225  C  CD2   . LEU A 1 2585 ? 165.240 201.544 186.916 1.00 12.85  ? 2585 LEU A CD2   1 
ATOM   8226  N  N     . ALA A 1 2586 ? 166.321 206.855 186.110 1.00 13.01  ? 2586 ALA A N     1 
ATOM   8227  C  CA    . ALA A 1 2586 ? 165.668 208.152 185.967 1.00 14.03  ? 2586 ALA A CA    1 
ATOM   8228  C  C     . ALA A 1 2586 ? 165.365 208.472 184.510 1.00 14.74  ? 2586 ALA A C     1 
ATOM   8229  O  O     . ALA A 1 2586 ? 164.399 209.186 184.219 1.00 15.87  ? 2586 ALA A O     1 
ATOM   8230  C  CB    . ALA A 1 2586 ? 166.537 209.247 186.585 1.00 18.79  ? 2586 ALA A CB    1 
ATOM   8231  N  N     . GLU A 1 2587 ? 166.169 207.955 183.585 1.00 13.06  ? 2587 GLU A N     1 
ATOM   8232  C  CA    . GLU A 1 2587 ? 165.923 208.108 182.159 1.00 15.35  ? 2587 GLU A CA    1 
ATOM   8233  C  C     . GLU A 1 2587 ? 164.979 207.050 181.608 1.00 13.88  ? 2587 GLU A C     1 
ATOM   8234  O  O     . GLU A 1 2587 ? 164.684 207.071 180.409 1.00 16.72  ? 2587 GLU A O     1 
ATOM   8235  C  CB    . GLU A 1 2587 ? 167.244 208.060 181.386 1.00 17.19  ? 2587 GLU A CB    1 
ATOM   8236  C  CG    . GLU A 1 2587 ? 168.256 209.108 181.807 1.00 24.64  ? 2587 GLU A CG    1 
ATOM   8237  C  CD    . GLU A 1 2587 ? 167.756 210.521 181.588 1.00 37.22  ? 2587 GLU A CD    1 
ATOM   8238  O  OE1   . GLU A 1 2587 ? 167.216 210.801 180.497 1.00 32.77  ? 2587 GLU A OE1   1 
ATOM   8239  O  OE2   . GLU A 1 2587 ? 167.907 211.352 182.506 1.00 30.26  ? 2587 GLU A OE2   1 
ATOM   8240  N  N     . HIS A 1 2588 ? 164.515 206.125 182.450 1.00 11.49  ? 2588 HIS A N     1 
ATOM   8241  C  CA    . HIS A 1 2588 ? 163.672 204.999 182.051 1.00 10.12  ? 2588 HIS A CA    1 
ATOM   8242  C  C     . HIS A 1 2588 ? 164.367 204.088 181.047 1.00 10.24  ? 2588 HIS A C     1 
ATOM   8243  O  O     . HIS A 1 2588 ? 163.708 203.336 180.324 1.00 9.55   ? 2588 HIS A O     1 
ATOM   8244  C  CB    . HIS A 1 2588 ? 162.325 205.476 181.496 1.00 10.47  ? 2588 HIS A CB    1 
ATOM   8245  C  CG    . HIS A 1 2588 ? 161.689 206.559 182.310 1.00 10.26  ? 2588 HIS A CG    1 
ATOM   8246  N  ND1   . HIS A 1 2588 ? 161.493 206.450 183.669 1.00 11.01  ? 2588 HIS A ND1   1 
ATOM   8247  C  CD2   . HIS A 1 2588 ? 161.209 207.775 181.957 1.00 11.80  ? 2588 HIS A CD2   1 
ATOM   8248  C  CE1   . HIS A 1 2588 ? 160.916 207.550 184.118 1.00 11.88  ? 2588 HIS A CE1   1 
ATOM   8249  N  NE2   . HIS A 1 2588 ? 160.732 208.369 183.099 1.00 12.62  ? 2588 HIS A NE2   1 
ATOM   8250  N  N     . LYS A 1 2589 ? 165.689 204.144 180.998 1.00 11.86  ? 2589 LYS A N     1 
ATOM   8251  C  CA    . LYS A 1 2589 ? 166.461 203.292 180.105 1.00 8.99   ? 2589 LYS A CA    1 
ATOM   8252  C  C     . LYS A 1 2589 ? 166.551 201.886 180.687 1.00 7.77   ? 2589 LYS A C     1 
ATOM   8253  O  O     . LYS A 1 2589 ? 166.959 201.727 181.842 1.00 9.55   ? 2589 LYS A O     1 
ATOM   8254  C  CB    . LYS A 1 2589 ? 167.859 203.870 179.902 1.00 8.68   ? 2589 LYS A CB    1 
ATOM   8255  C  CG    . LYS A 1 2589 ? 168.805 202.984 179.113 1.00 10.94  ? 2589 LYS A CG    1 
ATOM   8256  C  CD    . LYS A 1 2589 ? 169.068 203.550 177.731 1.00 8.84   ? 2589 LYS A CD    1 
ATOM   8257  C  CE    . LYS A 1 2589 ? 170.360 203.001 177.151 1.00 11.04  ? 2589 LYS A CE    1 
ATOM   8258  N  NZ    . LYS A 1 2589 ? 170.493 203.300 175.699 1.00 15.29  ? 2589 LYS A NZ    1 
ATOM   8259  N  N     . PRO A 1 2590 ? 166.171 200.853 179.936 1.00 7.15   ? 2590 PRO A N     1 
ATOM   8260  C  CA    . PRO A 1 2590 ? 166.267 199.488 180.465 1.00 6.56   ? 2590 PRO A CA    1 
ATOM   8261  C  C     . PRO A 1 2590 ? 167.709 199.120 180.777 1.00 9.52   ? 2590 PRO A C     1 
ATOM   8262  O  O     . PRO A 1 2590 ? 168.633 199.490 180.053 1.00 10.84  ? 2590 PRO A O     1 
ATOM   8263  C  CB    . PRO A 1 2590 ? 165.693 198.629 179.334 1.00 5.80   ? 2590 PRO A CB    1 
ATOM   8264  C  CG    . PRO A 1 2590 ? 165.869 199.455 178.106 1.00 7.41   ? 2590 PRO A CG    1 
ATOM   8265  C  CD    . PRO A 1 2590 ? 165.689 200.876 178.545 1.00 9.13   ? 2590 PRO A CD    1 
ATOM   8266  N  N     . LEU A 1 2591 ? 167.894 198.378 181.866 1.00 7.36   ? 2591 LEU A N     1 
ATOM   8267  C  CA    . LEU A 1 2591 ? 169.223 198.021 182.339 1.00 5.23   ? 2591 LEU A CA    1 
ATOM   8268  C  C     . LEU A 1 2591 ? 169.223 196.565 182.775 1.00 6.89   ? 2591 LEU A C     1 
ATOM   8269  O  O     . LEU A 1 2591 ? 168.177 195.987 183.079 1.00 9.10   ? 2591 LEU A O     1 
ATOM   8270  C  CB    . LEU A 1 2591 ? 169.675 198.942 183.486 1.00 8.66   ? 2591 LEU A CB    1 
ATOM   8271  C  CG    . LEU A 1 2591 ? 168.878 198.988 184.796 1.00 5.70   ? 2591 LEU A CG    1 
ATOM   8272  C  CD1   . LEU A 1 2591 ? 169.285 197.883 185.760 1.00 6.82   ? 2591 LEU A CD1   1 
ATOM   8273  C  CD2   . LEU A 1 2591 ? 169.004 200.345 185.462 1.00 5.97   ? 2591 LEU A CD2   1 
ATOM   8274  N  N     . VAL A 1 2592 ? 170.416 195.975 182.796 1.00 7.12   ? 2592 VAL A N     1 
ATOM   8275  C  CA    . VAL A 1 2592 ? 170.607 194.587 183.197 1.00 5.14   ? 2592 VAL A CA    1 
ATOM   8276  C  C     . VAL A 1 2592 ? 171.717 194.530 184.237 1.00 5.88   ? 2592 VAL A C     1 
ATOM   8277  O  O     . VAL A 1 2592 ? 172.792 195.106 184.038 1.00 6.52   ? 2592 VAL A O     1 
ATOM   8278  C  CB    . VAL A 1 2592 ? 170.941 193.686 181.992 1.00 4.22   ? 2592 VAL A CB    1 
ATOM   8279  C  CG1   . VAL A 1 2592 ? 171.440 192.332 182.457 1.00 5.33   ? 2592 VAL A CG1   1 
ATOM   8280  C  CG2   . VAL A 1 2592 ? 169.724 193.524 181.101 1.00 5.33   ? 2592 VAL A CG2   1 
ATOM   8281  N  N     . LEU A 1 2593 ? 171.448 193.844 185.344 1.00 6.30   ? 2593 LEU A N     1 
ATOM   8282  C  CA    . LEU A 1 2593 ? 172.438 193.574 186.377 1.00 4.47   ? 2593 LEU A CA    1 
ATOM   8283  C  C     . LEU A 1 2593 ? 172.915 192.135 186.233 1.00 5.14   ? 2593 LEU A C     1 
ATOM   8284  O  O     . LEU A 1 2593 ? 172.120 191.197 186.360 1.00 6.10   ? 2593 LEU A O     1 
ATOM   8285  C  CB    . LEU A 1 2593 ? 171.858 193.804 187.772 1.00 5.31   ? 2593 LEU A CB    1 
ATOM   8286  C  CG    . LEU A 1 2593 ? 171.299 195.187 188.101 1.00 6.02   ? 2593 LEU A CG    1 
ATOM   8287  C  CD1   . LEU A 1 2593 ? 169.783 195.155 188.108 1.00 5.55   ? 2593 LEU A CD1   1 
ATOM   8288  C  CD2   . LEU A 1 2593 ? 171.831 195.670 189.434 1.00 5.37   ? 2593 LEU A CD2   1 
ATOM   8289  N  N     . CYS A 1 2594 ? 174.207 191.964 185.981 1.00 6.66   ? 2594 CYS A N     1 
ATOM   8290  C  CA    . CYS A 1 2594 ? 174.807 190.649 185.835 1.00 5.18   ? 2594 CYS A CA    1 
ATOM   8291  C  C     . CYS A 1 2594 ? 175.762 190.384 186.990 1.00 6.29   ? 2594 CYS A C     1 
ATOM   8292  O  O     . CYS A 1 2594 ? 176.483 191.278 187.441 1.00 9.25   ? 2594 CYS A O     1 
ATOM   8293  C  CB    . CYS A 1 2594 ? 175.551 190.525 184.504 1.00 5.73   ? 2594 CYS A CB    1 
ATOM   8294  S  SG    . CYS A 1 2594 ? 175.727 188.831 183.911 1.00 15.98  ? 2594 CYS A SG    1 
ATOM   8295  N  N     . GLY A 1 2595 ? 175.746 189.149 187.491 1.00 5.42   ? 2595 GLY A N     1 
ATOM   8296  C  CA    . GLY A 1 2595 ? 176.658 188.793 188.590 1.00 5.21   ? 2595 GLY A CA    1 
ATOM   8297  C  C     . GLY A 1 2595 ? 176.322 187.443 189.181 1.00 6.10   ? 2595 GLY A C     1 
ATOM   8298  O  O     . GLY A 1 2595 ? 175.265 186.883 188.828 1.00 7.78   ? 2595 GLY A O     1 
ATOM   8299  N  N     . PRO A 1 2596 ? 177.170 186.902 190.080 1.00 6.82   ? 2596 PRO A N     1 
ATOM   8300  C  CA    . PRO A 1 2596 ? 176.936 185.588 190.655 1.00 6.23   ? 2596 PRO A CA    1 
ATOM   8301  C  C     . PRO A 1 2596 ? 175.688 185.609 191.523 1.00 6.66   ? 2596 PRO A C     1 
ATOM   8302  O  O     . PRO A 1 2596 ? 175.329 186.673 192.060 1.00 7.92   ? 2596 PRO A O     1 
ATOM   8303  C  CB    . PRO A 1 2596 ? 178.211 185.328 191.468 1.00 5.71   ? 2596 PRO A CB    1 
ATOM   8304  C  CG    . PRO A 1 2596 ? 179.208 186.341 190.956 1.00 6.57   ? 2596 PRO A CG    1 
ATOM   8305  C  CD    . PRO A 1 2596 ? 178.372 187.544 190.574 1.00 6.90   ? 2596 PRO A CD    1 
ATOM   8306  N  N     . PRO A 1 2597 ? 174.989 184.467 191.691 1.00 7.97   ? 2597 PRO A N     1 
ATOM   8307  C  CA    . PRO A 1 2597 ? 173.751 184.446 192.458 1.00 8.26   ? 2597 PRO A CA    1 
ATOM   8308  C  C     . PRO A 1 2597 ? 173.971 184.911 193.889 1.00 7.28   ? 2597 PRO A C     1 
ATOM   8309  O  O     . PRO A 1 2597 ? 174.916 184.434 194.540 1.00 12.58  ? 2597 PRO A O     1 
ATOM   8310  C  CB    . PRO A 1 2597 ? 173.313 182.972 192.376 1.00 6.40   ? 2597 PRO A CB    1 
ATOM   8311  C  CG    . PRO A 1 2597 ? 174.580 182.224 192.034 1.00 4.98   ? 2597 PRO A CG    1 
ATOM   8312  C  CD    . PRO A 1 2597 ? 175.367 183.174 191.153 1.00 6.84   ? 2597 PRO A CD    1 
ATOM   8313  N  N     . GLY A 1 2598 ? 173.120 185.820 194.372 1.00 5.93   ? 2598 GLY A N     1 
ATOM   8314  C  CA    . GLY A 1 2598 ? 173.248 186.340 195.747 1.00 6.78   ? 2598 GLY A CA    1 
ATOM   8315  C  C     . GLY A 1 2598 ? 174.276 187.452 195.846 1.00 9.00   ? 2598 GLY A C     1 
ATOM   8316  O  O     . GLY A 1 2598 ? 174.660 187.792 196.982 1.00 12.58  ? 2598 GLY A O     1 
ATOM   8317  N  N     . SER A 1 2599 ? 174.707 188.004 194.707 1.00 8.13   ? 2599 SER A N     1 
ATOM   8318  C  CA    . SER A 1 2599 ? 175.717 189.097 194.693 1.00 6.41   ? 2599 SER A CA    1 
ATOM   8319  C  C     . SER A 1 2599 ? 175.110 190.393 195.252 1.00 7.95   ? 2599 SER A C     1 
ATOM   8320  O  O     . SER A 1 2599 ? 175.886 191.245 195.732 1.00 7.50   ? 2599 SER A O     1 
ATOM   8321  C  CB    . SER A 1 2599 ? 176.277 189.307 193.312 1.00 5.60   ? 2599 SER A CB    1 
ATOM   8322  O  OG    . SER A 1 2599 ? 175.245 189.621 192.388 1.00 6.93   ? 2599 SER A OG    1 
ATOM   8323  N  N     . GLY A 1 2600 ? 173.783 190.533 195.189 1.00 8.44   ? 2600 GLY A N     1 
ATOM   8324  C  CA    . GLY A 1 2600 ? 173.112 191.728 195.736 1.00 6.51   ? 2600 GLY A CA    1 
ATOM   8325  C  C     . GLY A 1 2600 ? 172.456 192.558 194.651 1.00 6.28   ? 2600 GLY A C     1 
ATOM   8326  O  O     . GLY A 1 2600 ? 172.154 193.737 194.916 1.00 8.28   ? 2600 GLY A O     1 
ATOM   8327  N  N     . LYS A 1 2601 ? 172.240 191.970 193.473 1.00 6.65   ? 2601 LYS A N     1 
ATOM   8328  C  CA    . LYS A 1 2601 ? 171.633 192.709 192.336 1.00 5.50   ? 2601 LYS A CA    1 
ATOM   8329  C  C     . LYS A 1 2601 ? 170.226 193.181 192.733 1.00 6.53   ? 2601 LYS A C     1 
ATOM   8330  O  O     . LYS A 1 2601 ? 169.947 194.389 192.583 1.00 10.49  ? 2601 LYS A O     1 
ATOM   8331  C  CB    . LYS A 1 2601 ? 171.615 191.810 191.095 1.00 4.41   ? 2601 LYS A CB    1 
ATOM   8332  C  CG    . LYS A 1 2601 ? 172.987 191.331 190.639 1.00 4.21   ? 2601 LYS A CG    1 
ATOM   8333  C  CD    . LYS A 1 2601 ? 172.945 190.373 189.455 1.00 4.64   ? 2601 LYS A CD    1 
ATOM   8334  C  CE    . LYS A 1 2601 ? 172.302 189.065 189.792 1.00 5.42   ? 2601 LYS A CE    1 
ATOM   8335  N  NZ    . LYS A 1 2601 ? 173.068 188.336 190.806 1.00 5.99   ? 2601 LYS A NZ    1 
ATOM   8336  N  N     . THR A 1 2602 ? 169.390 192.271 193.239 1.00 7.28   ? 2602 THR A N     1 
ATOM   8337  C  CA    . THR A 1 2602 ? 168.014 192.626 193.651 1.00 5.81   ? 2602 THR A CA    1 
ATOM   8338  C  C     . THR A 1 2602 ? 168.078 193.628 194.783 1.00 7.45   ? 2602 THR A C     1 
ATOM   8339  O  O     . THR A 1 2602 ? 167.294 194.602 194.754 1.00 9.14   ? 2602 THR A O     1 
ATOM   8340  C  CB    . THR A 1 2602 ? 167.261 191.360 194.054 1.00 4.84   ? 2602 THR A CB    1 
ATOM   8341  O  OG1   . THR A 1 2602 ? 167.331 190.506 192.917 1.00 12.17  ? 2602 THR A OG1   1 
ATOM   8342  C  CG2   . THR A 1 2602 ? 165.812 191.632 194.412 1.00 6.81   ? 2602 THR A CG2   1 
ATOM   8343  N  N     . MET A 1 2603 ? 168.980 193.411 195.743 1.00 7.20   ? 2603 MET A N     1 
ATOM   8344  C  CA    . MET A 1 2603 ? 169.117 194.325 196.906 1.00 5.27   ? 2603 MET A CA    1 
ATOM   8345  C  C     . MET A 1 2603 ? 169.514 195.724 196.414 1.00 5.99   ? 2603 MET A C     1 
ATOM   8346  O  O     . MET A 1 2603 ? 168.913 196.710 196.887 1.00 10.29  ? 2603 MET A O     1 
ATOM   8347  C  CB    . MET A 1 2603 ? 170.193 193.814 197.869 1.00 6.10   ? 2603 MET A CB    1 
ATOM   8348  C  CG    . MET A 1 2603 ? 170.499 194.766 199.005 1.00 11.34  ? 2603 MET A CG    1 
ATOM   8349  S  SD    . MET A 1 2603 ? 172.078 194.399 199.796 1.00 9.00   ? 2603 MET A SD    1 
ATOM   8350  C  CE    . MET A 1 2603 ? 173.198 194.620 198.408 1.00 6.38   ? 2603 MET A CE    1 
ATOM   8351  N  N     . THR A 1 2604 ? 170.487 195.798 195.504 1.00 6.33   ? 2604 THR A N     1 
ATOM   8352  C  CA    . THR A 1 2604 ? 170.945 197.102 194.980 1.00 6.37   ? 2604 THR A CA    1 
ATOM   8353  C  C     . THR A 1 2604 ? 169.806 197.751 194.226 1.00 7.33   ? 2604 THR A C     1 
ATOM   8354  O  O     . THR A 1 2604 ? 169.599 198.969 194.405 1.00 8.95   ? 2604 THR A O     1 
ATOM   8355  C  CB    . THR A 1 2604 ? 172.175 196.904 194.097 1.00 5.41   ? 2604 THR A CB    1 
ATOM   8356  O  OG1   . THR A 1 2604 ? 173.112 196.219 194.922 1.00 6.31   ? 2604 THR A OG1   1 
ATOM   8357  C  CG2   . THR A 1 2604 ? 172.764 198.218 193.618 1.00 5.82   ? 2604 THR A CG2   1 
ATOM   8358  N  N     . LEU A 1 2605 ? 169.086 196.976 193.410 1.00 6.92   ? 2605 LEU A N     1 
ATOM   8359  C  CA    . LEU A 1 2605 ? 168.025 197.574 192.609 1.00 6.77   ? 2605 LEU A CA    1 
ATOM   8360  C  C     . LEU A 1 2605 ? 166.908 198.119 193.490 1.00 9.64   ? 2605 LEU A C     1 
ATOM   8361  O  O     . LEU A 1 2605 ? 166.397 199.217 193.245 1.00 11.80  ? 2605 LEU A O     1 
ATOM   8362  C  CB    . LEU A 1 2605 ? 167.471 196.557 191.614 1.00 7.05   ? 2605 LEU A CB    1 
ATOM   8363  C  CG    . LEU A 1 2605 ? 166.252 197.045 190.831 1.00 6.47   ? 2605 LEU A CG    1 
ATOM   8364  C  CD1   . LEU A 1 2605 ? 166.680 197.962 189.698 1.00 8.41   ? 2605 LEU A CD1   1 
ATOM   8365  C  CD2   . LEU A 1 2605 ? 165.443 195.877 190.304 1.00 6.48   ? 2605 LEU A CD2   1 
ATOM   8366  N  N     . PHE A 1 2606 ? 166.515 197.367 194.521 1.00 10.20  ? 2606 PHE A N     1 
ATOM   8367  C  CA    . PHE A 1 2606 ? 165.480 197.854 195.429 1.00 8.89   ? 2606 PHE A CA    1 
ATOM   8368  C  C     . PHE A 1 2606 ? 165.961 199.065 196.219 1.00 9.69   ? 2606 PHE A C     1 
ATOM   8369  O  O     . PHE A 1 2606 ? 165.195 200.009 196.447 1.00 11.89  ? 2606 PHE A O     1 
ATOM   8370  C  CB    . PHE A 1 2606 ? 165.030 196.735 196.369 1.00 10.15  ? 2606 PHE A CB    1 
ATOM   8371  C  CG    . PHE A 1 2606 ? 164.214 195.667 195.695 1.00 11.57  ? 2606 PHE A CG    1 
ATOM   8372  C  CD1   . PHE A 1 2606 ? 163.834 194.530 196.386 1.00 17.55  ? 2606 PHE A CD1   1 
ATOM   8373  C  CD2   . PHE A 1 2606 ? 163.816 195.804 194.376 1.00 10.58  ? 2606 PHE A CD2   1 
ATOM   8374  C  CE1   . PHE A 1 2606 ? 163.082 193.548 195.772 1.00 21.01  ? 2606 PHE A CE1   1 
ATOM   8375  C  CE2   . PHE A 1 2606 ? 163.065 194.826 193.758 1.00 10.01  ? 2606 PHE A CE2   1 
ATOM   8376  C  CZ    . PHE A 1 2606 ? 162.697 193.698 194.455 1.00 16.90  ? 2606 PHE A CZ    1 
ATOM   8377  N  N     . SER A 1 2607 ? 167.230 199.061 196.637 1.00 8.98   ? 2607 SER A N     1 
ATOM   8378  C  CA    . SER A 1 2607 ? 167.778 200.213 197.344 1.00 9.09   ? 2607 SER A CA    1 
ATOM   8379  C  C     . SER A 1 2607 ? 167.772 201.455 196.461 1.00 14.46  ? 2607 SER A C     1 
ATOM   8380  O  O     . SER A 1 2607 ? 167.451 202.555 196.926 1.00 15.63  ? 2607 SER A O     1 
ATOM   8381  C  CB    . SER A 1 2607 ? 169.193 199.899 197.825 1.00 10.33  ? 2607 SER A CB    1 
ATOM   8382  O  OG    . SER A 1 2607 ? 169.715 200.955 198.610 1.00 18.58  ? 2607 SER A OG    1 
ATOM   8383  N  N     . ALA A 1 2608 ? 168.131 201.299 195.185 1.00 13.79  ? 2608 ALA A N     1 
ATOM   8384  C  CA    . ALA A 1 2608 ? 168.099 202.427 194.262 1.00 10.05  ? 2608 ALA A CA    1 
ATOM   8385  C  C     . ALA A 1 2608 ? 166.672 202.894 194.001 1.00 10.02  ? 2608 ALA A C     1 
ATOM   8386  O  O     . ALA A 1 2608 ? 166.410 204.100 193.933 1.00 13.68  ? 2608 ALA A O     1 
ATOM   8387  C  CB    . ALA A 1 2608 ? 168.791 202.053 192.952 1.00 11.36  ? 2608 ALA A CB    1 
ATOM   8388  N  N     . LEU A 1 2609 ? 165.736 201.955 193.851 1.00 9.13   ? 2609 LEU A N     1 
ATOM   8389  C  CA    . LEU A 1 2609 ? 164.347 202.315 193.596 1.00 12.20  ? 2609 LEU A CA    1 
ATOM   8390  C  C     . LEU A 1 2609 ? 163.690 202.969 194.801 1.00 14.98  ? 2609 LEU A C     1 
ATOM   8391  O  O     . LEU A 1 2609 ? 162.702 203.690 194.635 1.00 19.55  ? 2609 LEU A O     1 
ATOM   8392  C  CB    . LEU A 1 2609 ? 163.553 201.078 193.176 1.00 11.67  ? 2609 LEU A CB    1 
ATOM   8393  C  CG    . LEU A 1 2609 ? 163.635 200.707 191.695 1.00 9.65   ? 2609 LEU A CG    1 
ATOM   8394  C  CD1   . LEU A 1 2609 ? 162.886 199.414 191.423 1.00 9.69   ? 2609 LEU A CD1   1 
ATOM   8395  C  CD2   . LEU A 1 2609 ? 163.098 201.834 190.832 1.00 11.47  ? 2609 LEU A CD2   1 
ATOM   8396  N  N     . ARG A 1 2610 ? 164.207 202.724 196.006 1.00 16.79  ? 2610 ARG A N     1 
ATOM   8397  C  CA    . ARG A 1 2610 ? 163.697 203.424 197.180 1.00 17.04  ? 2610 ARG A CA    1 
ATOM   8398  C  C     . ARG A 1 2610 ? 163.900 204.929 197.064 1.00 19.69  ? 2610 ARG A C     1 
ATOM   8399  O  O     . ARG A 1 2610 ? 163.138 205.706 197.650 1.00 25.05  ? 2610 ARG A O     1 
ATOM   8400  C  CB    . ARG A 1 2610 ? 164.375 202.891 198.442 1.00 17.83  ? 2610 ARG A CB    1 
ATOM   8401  C  CG    . ARG A 1 2610 ? 163.650 201.723 199.085 1.00 19.19  ? 2610 ARG A CG    1 
ATOM   8402  C  CD    . ARG A 1 2610 ? 164.184 201.446 200.485 1.00 22.42  ? 2610 ARG A CD    1 
ATOM   8403  N  NE    . ARG A 1 2610 ? 165.172 200.372 200.520 1.00 24.29  ? 2610 ARG A NE    1 
ATOM   8404  C  CZ    . ARG A 1 2610 ? 164.959 199.120 200.133 1.00 22.70  ? 2610 ARG A CZ    1 
ATOM   8405  N  NH1   . ARG A 1 2610 ? 163.768 198.712 199.723 1.00 17.63  ? 2610 ARG A NH1   1 
ATOM   8406  N  NH2   . ARG A 1 2610 ? 165.963 198.250 200.175 1.00 21.26  ? 2610 ARG A NH2   1 
ATOM   8407  N  N     . ALA A 1 2611 ? 164.914 205.359 196.312 1.00 20.64  ? 2611 ALA A N     1 
ATOM   8408  C  CA    . ALA A 1 2611 ? 165.151 206.775 196.070 1.00 21.74  ? 2611 ALA A CA    1 
ATOM   8409  C  C     . ALA A 1 2611 ? 164.265 207.343 194.970 1.00 24.04  ? 2611 ALA A C     1 
ATOM   8410  O  O     . ALA A 1 2611 ? 164.305 208.554 194.728 1.00 27.56  ? 2611 ALA A O     1 
ATOM   8411  C  CB    . ALA A 1 2611 ? 166.621 207.009 195.717 1.00 21.32  ? 2611 ALA A CB    1 
ATOM   8412  N  N     . LEU A 1 2612 ? 163.481 206.506 194.298 1.00 20.73  ? 2612 LEU A N     1 
ATOM   8413  C  CA    . LEU A 1 2612 ? 162.546 206.948 193.265 1.00 24.50  ? 2612 LEU A CA    1 
ATOM   8414  C  C     . LEU A 1 2612 ? 161.136 206.577 193.700 1.00 34.05  ? 2612 LEU A C     1 
ATOM   8415  O  O     . LEU A 1 2612 ? 160.690 205.439 193.467 1.00 36.12  ? 2612 LEU A O     1 
ATOM   8416  C  CB    . LEU A 1 2612 ? 162.882 206.314 191.917 1.00 23.71  ? 2612 LEU A CB    1 
ATOM   8417  C  CG    . LEU A 1 2612 ? 164.182 206.781 191.257 1.00 23.62  ? 2612 LEU A CG    1 
ATOM   8418  C  CD1   . LEU A 1 2612 ? 164.705 205.734 190.291 1.00 14.16  ? 2612 LEU A CD1   1 
ATOM   8419  C  CD2   . LEU A 1 2612 ? 163.971 208.106 190.545 1.00 21.67  ? 2612 LEU A CD2   1 
ATOM   8420  N  N     . PRO A 1 2613 ? 160.396 207.492 194.334 1.00 36.32  ? 2613 PRO A N     1 
ATOM   8421  C  CA    . PRO A 1 2613 ? 159.068 207.138 194.857 1.00 38.85  ? 2613 PRO A CA    1 
ATOM   8422  C  C     . PRO A 1 2613 ? 157.992 207.013 193.794 1.00 33.50  ? 2613 PRO A C     1 
ATOM   8423  O  O     . PRO A 1 2613 ? 156.909 206.494 194.097 1.00 30.88  ? 2613 PRO A O     1 
ATOM   8424  C  CB    . PRO A 1 2613 ? 158.744 208.290 195.823 1.00 38.92  ? 2613 PRO A CB    1 
ATOM   8425  C  CG    . PRO A 1 2613 ? 159.734 209.370 195.548 1.00 32.01  ? 2613 PRO A CG    1 
ATOM   8426  C  CD    . PRO A 1 2613 ? 160.754 208.900 194.567 1.00 25.15  ? 2613 PRO A CD    1 
ATOM   8427  N  N     . ASP A 1 2614 ? 158.247 207.463 192.569 1.00 34.89  ? 2614 ASP A N     1 
ATOM   8428  C  CA    . ASP A 1 2614 ? 157.260 207.429 191.500 1.00 35.40  ? 2614 ASP A CA    1 
ATOM   8429  C  C     . ASP A 1 2614 ? 157.298 206.135 190.699 1.00 33.04  ? 2614 ASP A C     1 
ATOM   8430  O  O     . ASP A 1 2614 ? 156.581 206.019 189.701 1.00 29.80  ? 2614 ASP A O     1 
ATOM   8431  C  CB    . ASP A 1 2614 ? 157.459 208.624 190.564 1.00 37.50  ? 2614 ASP A CB    1 
ATOM   8432  C  CG    . ASP A 1 2614 ? 156.921 209.915 191.146 1.00 49.70  ? 2614 ASP A CG    1 
ATOM   8433  O  OD1   . ASP A 1 2614 ? 156.134 209.848 192.115 1.00 50.13  ? 2614 ASP A OD1   1 
ATOM   8434  O  OD2   . ASP A 1 2614 ? 157.281 210.995 190.634 1.00 46.18  ? 2614 ASP A OD2   1 
ATOM   8435  N  N     . MET A 1 2615 ? 158.115 205.167 191.104 1.00 31.15  ? 2615 MET A N     1 
ATOM   8436  C  CA    . MET A 1 2615 ? 158.260 203.907 190.389 1.00 23.86  ? 2615 MET A CA    1 
ATOM   8437  C  C     . MET A 1 2615 ? 157.783 202.760 191.268 1.00 28.54  ? 2615 MET A C     1 
ATOM   8438  O  O     . MET A 1 2615 ? 158.162 202.669 192.440 1.00 34.85  ? 2615 MET A O     1 
ATOM   8439  C  CB    . MET A 1 2615 ? 159.712 203.684 189.963 1.00 18.28  ? 2615 MET A CB    1 
ATOM   8440  C  CG    . MET A 1 2615 ? 160.192 204.668 188.914 1.00 23.15  ? 2615 MET A CG    1 
ATOM   8441  S  SD    . MET A 1 2615 ? 161.901 204.412 188.418 1.00 28.67  ? 2615 MET A SD    1 
ATOM   8442  C  CE    . MET A 1 2615 ? 162.115 205.781 187.287 1.00 15.92  ? 2615 MET A CE    1 
ATOM   8443  N  N     . GLU A 1 2616 ? 156.953 201.892 190.698 1.00 23.71  ? 2616 GLU A N     1 
ATOM   8444  C  CA    . GLU A 1 2616 ? 156.475 200.689 191.365 1.00 24.88  ? 2616 GLU A CA    1 
ATOM   8445  C  C     . GLU A 1 2616 ? 157.061 199.472 190.665 1.00 19.44  ? 2616 GLU A C     1 
ATOM   8446  O  O     . GLU A 1 2616 ? 156.927 199.330 189.446 1.00 20.24  ? 2616 GLU A O     1 
ATOM   8447  C  CB    . GLU A 1 2616 ? 154.946 200.622 191.357 1.00 26.20  ? 2616 GLU A CB    1 
ATOM   8448  C  CG    . GLU A 1 2616 ? 154.264 201.707 192.176 1.00 40.31  ? 2616 GLU A CG    1 
ATOM   8449  C  CD    . GLU A 1 2616 ? 154.526 201.571 193.663 1.00 54.34  ? 2616 GLU A CD    1 
ATOM   8450  O  OE1   . GLU A 1 2616 ? 154.683 200.428 194.141 1.00 51.41  ? 2616 GLU A OE1   1 
ATOM   8451  O  OE2   . GLU A 1 2616 ? 154.575 202.609 194.356 1.00 57.16  ? 2616 GLU A OE2   1 
ATOM   8452  N  N     . VAL A 1 2617 ? 157.704 198.601 191.431 1.00 19.28  ? 2617 VAL A N     1 
ATOM   8453  C  CA    . VAL A 1 2617 ? 158.404 197.449 190.876 1.00 12.20  ? 2617 VAL A CA    1 
ATOM   8454  C  C     . VAL A 1 2617 ? 157.498 196.226 190.921 1.00 11.86  ? 2617 VAL A C     1 
ATOM   8455  O  O     . VAL A 1 2617 ? 156.726 196.030 191.868 1.00 15.77  ? 2617 VAL A O     1 
ATOM   8456  C  CB    . VAL A 1 2617 ? 159.733 197.206 191.622 1.00 11.70  ? 2617 VAL A CB    1 
ATOM   8457  C  CG1   . VAL A 1 2617 ? 159.490 196.652 193.017 1.00 16.25  ? 2617 VAL A CG1   1 
ATOM   8458  C  CG2   . VAL A 1 2617 ? 160.629 196.273 190.823 1.00 11.70  ? 2617 VAL A CG2   1 
ATOM   8459  N  N     . VAL A 1 2618 ? 157.569 195.416 189.868 1.00 13.10  ? 2618 VAL A N     1 
ATOM   8460  C  CA    . VAL A 1 2618 ? 156.808 194.179 189.751 1.00 12.94  ? 2618 VAL A CA    1 
ATOM   8461  C  C     . VAL A 1 2618 ? 157.785 193.074 189.381 1.00 11.05  ? 2618 VAL A C     1 
ATOM   8462  O  O     . VAL A 1 2618 ? 158.484 193.175 188.366 1.00 14.61  ? 2618 VAL A O     1 
ATOM   8463  C  CB    . VAL A 1 2618 ? 155.688 194.287 188.703 1.00 11.16  ? 2618 VAL A CB    1 
ATOM   8464  C  CG1   . VAL A 1 2618 ? 155.228 192.906 188.270 1.00 13.04  ? 2618 VAL A CG1   1 
ATOM   8465  C  CG2   . VAL A 1 2618 ? 154.528 195.090 189.253 1.00 12.03  ? 2618 VAL A CG2   1 
ATOM   8466  N  N     . GLY A 1 2619 ? 157.828 192.021 190.192 1.00 10.25  ? 2619 GLY A N     1 
ATOM   8467  C  CA    . GLY A 1 2619 ? 158.785 190.954 189.985 1.00 7.58   ? 2619 GLY A CA    1 
ATOM   8468  C  C     . GLY A 1 2619 ? 158.298 189.835 189.089 1.00 11.37  ? 2619 GLY A C     1 
ATOM   8469  O  O     . GLY A 1 2619 ? 157.252 189.231 189.343 1.00 17.80  ? 2619 GLY A O     1 
ATOM   8470  N  N     . LEU A 1 2620 ? 159.053 189.557 188.031 1.00 11.84  ? 2620 LEU A N     1 
ATOM   8471  C  CA    . LEU A 1 2620 ? 158.835 188.415 187.158 1.00 9.93   ? 2620 LEU A CA    1 
ATOM   8472  C  C     . LEU A 1 2620 ? 160.064 187.525 187.242 1.00 12.96  ? 2620 LEU A C     1 
ATOM   8473  O  O     . LEU A 1 2620 ? 161.193 188.014 187.155 1.00 18.58  ? 2620 LEU A O     1 
ATOM   8474  C  CB    . LEU A 1 2620 ? 158.597 188.857 185.711 1.00 10.83  ? 2620 LEU A CB    1 
ATOM   8475  C  CG    . LEU A 1 2620 ? 157.253 189.488 185.348 1.00 15.57  ? 2620 LEU A CG    1 
ATOM   8476  C  CD1   . LEU A 1 2620 ? 157.266 190.983 185.615 1.00 10.36  ? 2620 LEU A CD1   1 
ATOM   8477  C  CD2   . LEU A 1 2620 ? 156.922 189.209 183.893 1.00 15.34  ? 2620 LEU A CD2   1 
ATOM   8478  N  N     . ASN A 1 2621 ? 159.849 186.230 187.418 1.00 13.90  ? 2621 ASN A N     1 
ATOM   8479  C  CA    . ASN A 1 2621 ? 160.937 185.266 187.552 1.00 10.77  ? 2621 ASN A CA    1 
ATOM   8480  C  C     . ASN A 1 2621 ? 160.956 184.392 186.306 1.00 15.12  ? 2621 ASN A C     1 
ATOM   8481  O  O     . ASN A 1 2621 ? 160.130 183.489 186.154 1.00 22.25  ? 2621 ASN A O     1 
ATOM   8482  C  CB    . ASN A 1 2621 ? 160.773 184.441 188.821 1.00 14.54  ? 2621 ASN A CB    1 
ATOM   8483  C  CG    . ASN A 1 2621 ? 160.580 185.304 190.041 1.00 20.41  ? 2621 ASN A CG    1 
ATOM   8484  O  OD1   . ASN A 1 2621 ? 161.545 185.760 190.652 1.00 17.81  ? 2621 ASN A OD1   1 
ATOM   8485  N  ND2   . ASN A 1 2621 ? 159.327 185.548 190.396 1.00 18.29  ? 2621 ASN A ND2   1 
ATOM   8486  N  N     . PHE A 1 2622 ? 161.898 184.673 185.416 1.00 13.45  ? 2622 PHE A N     1 
ATOM   8487  C  CA    . PHE A 1 2622 ? 162.025 183.909 184.189 1.00 9.65   ? 2622 PHE A CA    1 
ATOM   8488  C  C     . PHE A 1 2622 ? 162.655 182.552 184.474 1.00 10.80  ? 2622 PHE A C     1 
ATOM   8489  O  O     . PHE A 1 2622 ? 163.375 182.369 185.459 1.00 16.79  ? 2622 PHE A O     1 
ATOM   8490  C  CB    . PHE A 1 2622 ? 162.873 184.665 183.165 1.00 10.61  ? 2622 PHE A CB    1 
ATOM   8491  C  CG    . PHE A 1 2622 ? 162.180 185.844 182.536 1.00 7.96   ? 2622 PHE A CG    1 
ATOM   8492  C  CD1   . PHE A 1 2622 ? 160.971 186.310 183.021 1.00 9.18   ? 2622 PHE A CD1   1 
ATOM   8493  C  CD2   . PHE A 1 2622 ? 162.752 186.490 181.455 1.00 6.93   ? 2622 PHE A CD2   1 
ATOM   8494  C  CE1   . PHE A 1 2622 ? 160.349 187.393 182.439 1.00 9.02   ? 2622 PHE A CE1   1 
ATOM   8495  C  CE2   . PHE A 1 2622 ? 162.133 187.572 180.870 1.00 6.69   ? 2622 PHE A CE2   1 
ATOM   8496  C  CZ    . PHE A 1 2622 ? 160.932 188.025 181.362 1.00 6.05   ? 2622 PHE A CZ    1 
ATOM   8497  N  N     . SER A 1 2623 ? 162.373 181.596 183.595 1.00 12.92  ? 2623 SER A N     1 
ATOM   8498  C  CA    . SER A 1 2623 ? 162.977 180.275 183.652 1.00 11.77  ? 2623 SER A CA    1 
ATOM   8499  C  C     . SER A 1 2623 ? 163.204 179.799 182.225 1.00 13.60  ? 2623 SER A C     1 
ATOM   8500  O  O     . SER A 1 2623 ? 163.029 180.554 181.266 1.00 13.87  ? 2623 SER A O     1 
ATOM   8501  C  CB    . SER A 1 2623 ? 162.104 179.297 184.444 1.00 14.68  ? 2623 SER A CB    1 
ATOM   8502  O  OG    . SER A 1 2623 ? 160.835 179.146 183.839 1.00 14.00  ? 2623 SER A OG    1 
ATOM   8503  N  N     . SER A 1 2624 ? 163.589 178.529 182.084 1.00 15.75  ? 2624 SER A N     1 
ATOM   8504  C  CA    . SER A 1 2624 ? 163.899 177.991 180.764 1.00 11.26  ? 2624 SER A CA    1 
ATOM   8505  C  C     . SER A 1 2624 ? 162.697 178.010 179.830 1.00 13.41  ? 2624 SER A C     1 
ATOM   8506  O  O     . SER A 1 2624 ? 162.868 178.239 178.628 1.00 17.72  ? 2624 SER A O     1 
ATOM   8507  C  CB    . SER A 1 2624 ? 164.439 176.566 180.887 1.00 13.50  ? 2624 SER A CB    1 
ATOM   8508  O  OG    . SER A 1 2624 ? 163.424 175.664 181.285 1.00 25.05  ? 2624 SER A OG    1 
ATOM   8509  N  N     . ALA A 1 2625 ? 161.491 177.780 180.347 1.00 11.64  ? 2625 ALA A N     1 
ATOM   8510  C  CA    . ALA A 1 2625 ? 160.285 177.766 179.533 1.00 13.73  ? 2625 ALA A CA    1 
ATOM   8511  C  C     . ALA A 1 2625 ? 159.490 179.061 179.647 1.00 18.01  ? 2625 ALA A C     1 
ATOM   8512  O  O     . ALA A 1 2625 ? 158.275 179.060 179.419 1.00 17.05  ? 2625 ALA A O     1 
ATOM   8513  C  CB    . ALA A 1 2625 ? 159.409 176.569 179.902 1.00 19.49  ? 2625 ALA A CB    1 
ATOM   8514  N  N     . THR A 1 2626 ? 160.146 180.163 180.001 1.00 21.32  ? 2626 THR A N     1 
ATOM   8515  C  CA    . THR A 1 2626 ? 159.473 181.453 180.047 1.00 12.32  ? 2626 THR A CA    1 
ATOM   8516  C  C     . THR A 1 2626 ? 159.216 181.964 178.635 1.00 11.18  ? 2626 THR A C     1 
ATOM   8517  O  O     . THR A 1 2626 ? 160.117 181.978 177.791 1.00 15.95  ? 2626 THR A O     1 
ATOM   8518  C  CB    . THR A 1 2626 ? 160.310 182.461 180.831 1.00 8.06   ? 2626 THR A CB    1 
ATOM   8519  O  OG1   . THR A 1 2626 ? 160.507 181.978 182.164 1.00 13.67  ? 2626 THR A OG1   1 
ATOM   8520  C  CG2   . THR A 1 2626 ? 159.612 183.807 180.883 1.00 8.16   ? 2626 THR A CG2   1 
ATOM   8521  N  N     . THR A 1 2627 ? 157.986 182.382 178.384 1.00 15.04  ? 2627 THR A N     1 
ATOM   8522  C  CA    . THR A 1 2627 ? 157.529 182.885 177.100 1.00 13.75  ? 2627 THR A CA    1 
ATOM   8523  C  C     . THR A 1 2627 ? 156.792 184.196 177.325 1.00 12.25  ? 2627 THR A C     1 
ATOM   8524  O  O     . THR A 1 2627 ? 156.372 184.492 178.449 1.00 14.88  ? 2627 THR A O     1 
ATOM   8525  C  CB    . THR A 1 2627 ? 156.614 181.867 176.400 1.00 15.55  ? 2627 THR A CB    1 
ATOM   8526  O  OG1   . THR A 1 2627 ? 155.356 181.800 177.083 1.00 15.80  ? 2627 THR A OG1   1 
ATOM   8527  C  CG2   . THR A 1 2627 ? 157.251 180.486 176.370 1.00 23.29  ? 2627 THR A CG2   1 
ATOM   8528  N  N     . PRO A 1 2628 ? 156.634 185.024 176.273 1.00 10.65  ? 2628 PRO A N     1 
ATOM   8529  C  CA    . PRO A 1 2628 ? 156.022 186.352 176.453 1.00 11.29  ? 2628 PRO A CA    1 
ATOM   8530  C  C     . PRO A 1 2628 ? 154.641 186.371 177.101 1.00 12.92  ? 2628 PRO A C     1 
ATOM   8531  O  O     . PRO A 1 2628 ? 154.174 187.441 177.503 1.00 11.72  ? 2628 PRO A O     1 
ATOM   8532  C  CB    . PRO A 1 2628 ? 155.951 186.891 175.020 1.00 7.00   ? 2628 PRO A CB    1 
ATOM   8533  C  CG    . PRO A 1 2628 ? 157.082 186.242 174.327 1.00 7.42   ? 2628 PRO A CG    1 
ATOM   8534  C  CD    . PRO A 1 2628 ? 157.235 184.877 174.934 1.00 9.39   ? 2628 PRO A CD    1 
ATOM   8535  N  N     . GLU A 1 2629 ? 153.970 185.221 177.203 1.00 13.62  ? 2629 GLU A N     1 
ATOM   8536  C  CA    . GLU A 1 2629 ? 152.665 185.202 177.858 1.00 14.22  ? 2629 GLU A CA    1 
ATOM   8537  C  C     . GLU A 1 2629 ? 152.774 185.537 179.341 1.00 13.73  ? 2629 GLU A C     1 
ATOM   8538  O  O     . GLU A 1 2629 ? 151.820 186.047 179.934 1.00 15.89  ? 2629 GLU A O     1 
ATOM   8539  C  CB    . GLU A 1 2629 ? 151.974 183.854 177.650 1.00 19.04  ? 2629 GLU A CB    1 
ATOM   8540  C  CG    . GLU A 1 2629 ? 151.564 183.580 176.205 1.00 35.30  ? 2629 GLU A CG    1 
ATOM   8541  C  CD    . GLU A 1 2629 ? 152.692 183.045 175.357 1.00 36.20  ? 2629 GLU A CD    1 
ATOM   8542  O  OE1   . GLU A 1 2629 ? 153.784 182.827 175.908 1.00 32.07  ? 2629 GLU A OE1   1 
ATOM   8543  O  OE2   . GLU A 1 2629 ? 152.487 182.842 174.143 1.00 38.49  ? 2629 GLU A OE2   1 
ATOM   8544  N  N     . LEU A 1 2630 ? 153.928 185.276 179.958 1.00 11.61  ? 2630 LEU A N     1 
ATOM   8545  C  CA    . LEU A 1 2630 ? 154.140 185.744 181.326 1.00 9.88   ? 2630 LEU A CA    1 
ATOM   8546  C  C     . LEU A 1 2630 ? 154.103 187.266 181.390 1.00 14.65  ? 2630 LEU A C     1 
ATOM   8547  O  O     . LEU A 1 2630 ? 153.457 187.850 182.272 1.00 15.86  ? 2630 LEU A O     1 
ATOM   8548  C  CB    . LEU A 1 2630 ? 155.470 185.212 181.859 1.00 12.17  ? 2630 LEU A CB    1 
ATOM   8549  C  CG    . LEU A 1 2630 ? 155.824 185.522 183.314 1.00 9.91   ? 2630 LEU A CG    1 
ATOM   8550  C  CD1   . LEU A 1 2630 ? 155.164 184.525 184.250 1.00 8.62   ? 2630 LEU A CD1   1 
ATOM   8551  C  CD2   . LEU A 1 2630 ? 157.329 185.520 183.507 1.00 9.85   ? 2630 LEU A CD2   1 
ATOM   8552  N  N     . LEU A 1 2631 ? 154.774 187.924 180.441 1.00 15.99  ? 2631 LEU A N     1 
ATOM   8553  C  CA    . LEU A 1 2631 ? 154.731 189.380 180.364 1.00 11.62  ? 2631 LEU A CA    1 
ATOM   8554  C  C     . LEU A 1 2631 ? 153.314 189.867 180.098 1.00 10.76  ? 2631 LEU A C     1 
ATOM   8555  O  O     . LEU A 1 2631 ? 152.884 190.885 180.651 1.00 10.95  ? 2631 LEU A O     1 
ATOM   8556  C  CB    . LEU A 1 2631 ? 155.675 189.876 179.268 1.00 9.99   ? 2631 LEU A CB    1 
ATOM   8557  C  CG    . LEU A 1 2631 ? 157.172 190.039 179.554 1.00 9.95   ? 2631 LEU A CG    1 
ATOM   8558  C  CD1   . LEU A 1 2631 ? 157.416 191.097 180.611 1.00 8.40   ? 2631 LEU A CD1   1 
ATOM   8559  C  CD2   . LEU A 1 2631 ? 157.812 188.720 179.950 1.00 12.92  ? 2631 LEU A CD2   1 
ATOM   8560  N  N     . LEU A 1 2632 ? 152.578 189.157 179.242 1.00 12.57  ? 2632 LEU A N     1 
ATOM   8561  C  CA    . LEU A 1 2632 ? 151.212 189.558 178.925 1.00 11.92  ? 2632 LEU A CA    1 
ATOM   8562  C  C     . LEU A 1 2632 ? 150.296 189.426 180.138 1.00 16.49  ? 2632 LEU A C     1 
ATOM   8563  O  O     . LEU A 1 2632 ? 149.432 190.279 180.365 1.00 20.32  ? 2632 LEU A O     1 
ATOM   8564  C  CB    . LEU A 1 2632 ? 150.689 188.732 177.753 1.00 11.95  ? 2632 LEU A CB    1 
ATOM   8565  C  CG    . LEU A 1 2632 ? 151.412 188.990 176.429 1.00 9.04   ? 2632 LEU A CG    1 
ATOM   8566  C  CD1   . LEU A 1 2632 ? 150.889 188.077 175.334 1.00 12.84  ? 2632 LEU A CD1   1 
ATOM   8567  C  CD2   . LEU A 1 2632 ? 151.282 190.449 176.026 1.00 8.36   ? 2632 LEU A CD2   1 
ATOM   8568  N  N     . LYS A 1 2633 ? 150.467 188.363 180.928 1.00 13.99  ? 2633 LYS A N     1 
ATOM   8569  C  CA    . LYS A 1 2633 ? 149.698 188.220 182.160 1.00 13.41  ? 2633 LYS A CA    1 
ATOM   8570  C  C     . LYS A 1 2633 ? 150.042 189.322 183.152 1.00 17.11  ? 2633 LYS A C     1 
ATOM   8571  O  O     . LYS A 1 2633 ? 149.155 189.862 183.826 1.00 23.35  ? 2633 LYS A O     1 
ATOM   8572  C  CB    . LYS A 1 2633 ? 149.948 186.847 182.784 1.00 15.86  ? 2633 LYS A CB    1 
ATOM   8573  C  CG    . LYS A 1 2633 ? 149.473 185.679 181.941 1.00 18.79  ? 2633 LYS A CG    1 
ATOM   8574  C  CD    . LYS A 1 2633 ? 147.962 185.557 181.950 1.00 30.59  ? 2633 LYS A CD    1 
ATOM   8575  C  CE    . LYS A 1 2633 ? 147.511 184.387 181.094 1.00 32.96  ? 2633 LYS A CE    1 
ATOM   8576  N  NZ    . LYS A 1 2633 ? 148.374 183.193 181.306 1.00 30.61  ? 2633 LYS A NZ    1 
ATOM   8577  N  N     . THR A 1 2634 ? 151.327 189.668 183.259 1.00 19.54  ? 2634 THR A N     1 
ATOM   8578  C  CA    . THR A 1 2634 ? 151.716 190.769 184.136 1.00 16.25  ? 2634 THR A CA    1 
ATOM   8579  C  C     . THR A 1 2634 ? 151.087 192.082 183.680 1.00 15.60  ? 2634 THR A C     1 
ATOM   8580  O  O     . THR A 1 2634 ? 150.614 192.874 184.504 1.00 21.47  ? 2634 THR A O     1 
ATOM   8581  C  CB    . THR A 1 2634 ? 153.238 190.888 184.188 1.00 15.51  ? 2634 THR A CB    1 
ATOM   8582  O  OG1   . THR A 1 2634 ? 153.788 189.705 184.782 1.00 17.23  ? 2634 THR A OG1   1 
ATOM   8583  C  CG2   . THR A 1 2634 ? 153.655 192.095 185.010 1.00 15.18  ? 2634 THR A CG2   1 
ATOM   8584  N  N     . PHE A 1 2635 ? 151.065 192.323 182.367 1.00 14.88  ? 2635 PHE A N     1 
ATOM   8585  C  CA    . PHE A 1 2635 ? 150.423 193.522 181.838 1.00 14.80  ? 2635 PHE A CA    1 
ATOM   8586  C  C     . PHE A 1 2635 ? 148.929 193.525 182.129 1.00 18.48  ? 2635 PHE A C     1 
ATOM   8587  O  O     . PHE A 1 2635 ? 148.361 194.562 182.486 1.00 22.33  ? 2635 PHE A O     1 
ATOM   8588  C  CB    . PHE A 1 2635 ? 150.673 193.631 180.334 1.00 12.15  ? 2635 PHE A CB    1 
ATOM   8589  C  CG    . PHE A 1 2635 ? 152.087 193.980 179.976 1.00 12.03  ? 2635 PHE A CG    1 
ATOM   8590  C  CD1   . PHE A 1 2635 ? 152.885 194.688 180.857 1.00 13.05  ? 2635 PHE A CD1   1 
ATOM   8591  C  CD2   . PHE A 1 2635 ? 152.620 193.599 178.757 1.00 13.22  ? 2635 PHE A CD2   1 
ATOM   8592  C  CE1   . PHE A 1 2635 ? 154.185 195.010 180.529 1.00 11.18  ? 2635 PHE A CE1   1 
ATOM   8593  C  CE2   . PHE A 1 2635 ? 153.920 193.918 178.424 1.00 10.56  ? 2635 PHE A CE2   1 
ATOM   8594  C  CZ    . PHE A 1 2635 ? 154.704 194.624 179.311 1.00 9.38   ? 2635 PHE A CZ    1 
ATOM   8595  N  N     . ASP A 1 2636 ? 148.273 192.373 181.975 1.00 18.29  ? 2636 ASP A N     1 
ATOM   8596  C  CA    . ASP A 1 2636 ? 146.844 192.292 182.259 1.00 17.62  ? 2636 ASP A CA    1 
ATOM   8597  C  C     . ASP A 1 2636 ? 146.558 192.574 183.727 1.00 24.27  ? 2636 ASP A C     1 
ATOM   8598  O  O     . ASP A 1 2636 ? 145.563 193.229 184.060 1.00 30.63  ? 2636 ASP A O     1 
ATOM   8599  C  CB    . ASP A 1 2636 ? 146.304 190.917 181.865 1.00 19.28  ? 2636 ASP A CB    1 
ATOM   8600  C  CG    . ASP A 1 2636 ? 146.288 190.704 180.365 1.00 42.28  ? 2636 ASP A CG    1 
ATOM   8601  O  OD1   . ASP A 1 2636 ? 146.147 191.699 179.624 1.00 47.78  ? 2636 ASP A OD1   1 
ATOM   8602  O  OD2   . ASP A 1 2636 ? 146.414 189.541 179.927 1.00 40.74  ? 2636 ASP A OD2   1 
ATOM   8603  N  N     . HIS A 1 2637 ? 147.416 192.082 184.621 1.00 22.72  ? 2637 HIS A N     1 
ATOM   8604  C  CA    . HIS A 1 2637 ? 147.179 192.279 186.047 1.00 17.78  ? 2637 HIS A CA    1 
ATOM   8605  C  C     . HIS A 1 2637 ? 147.470 193.712 186.478 1.00 19.05  ? 2637 HIS A C     1 
ATOM   8606  O  O     . HIS A 1 2637 ? 146.725 194.285 187.281 1.00 24.05  ? 2637 HIS A O     1 
ATOM   8607  C  CB    . HIS A 1 2637 ? 148.020 191.297 186.860 1.00 19.78  ? 2637 HIS A CB    1 
ATOM   8608  C  CG    . HIS A 1 2637 ? 147.658 191.254 188.312 1.00 26.10  ? 2637 HIS A CG    1 
ATOM   8609  N  ND1   . HIS A 1 2637 ? 148.007 192.252 189.195 1.00 25.28  ? 2637 HIS A ND1   1 
ATOM   8610  C  CD2   . HIS A 1 2637 ? 146.971 190.337 189.032 1.00 31.42  ? 2637 HIS A CD2   1 
ATOM   8611  C  CE1   . HIS A 1 2637 ? 147.553 191.951 190.398 1.00 31.95  ? 2637 HIS A CE1   1 
ATOM   8612  N  NE2   . HIS A 1 2637 ? 146.922 190.794 190.327 1.00 37.11  ? 2637 HIS A NE2   1 
ATOM   8613  N  N     . TYR A 1 2638 ? 148.547 194.309 185.966 1.00 17.55  ? 2638 TYR A N     1 
ATOM   8614  C  CA    . TYR A 1 2638 ? 149.014 195.591 186.480 1.00 14.67  ? 2638 TYR A CA    1 
ATOM   8615  C  C     . TYR A 1 2638 ? 148.723 196.772 185.567 1.00 18.06  ? 2638 TYR A C     1 
ATOM   8616  O  O     . TYR A 1 2638 ? 148.822 197.918 186.019 1.00 15.63  ? 2638 TYR A O     1 
ATOM   8617  C  CB    . TYR A 1 2638 ? 150.523 195.535 186.747 1.00 11.47  ? 2638 TYR A CB    1 
ATOM   8618  C  CG    . TYR A 1 2638 ? 150.897 194.719 187.960 1.00 13.95  ? 2638 TYR A CG    1 
ATOM   8619  C  CD1   . TYR A 1 2638 ? 150.866 195.275 189.231 1.00 13.30  ? 2638 TYR A CD1   1 
ATOM   8620  C  CD2   . TYR A 1 2638 ? 151.280 193.392 187.836 1.00 13.96  ? 2638 TYR A CD2   1 
ATOM   8621  C  CE1   . TYR A 1 2638 ? 151.206 194.533 190.342 1.00 16.75  ? 2638 TYR A CE1   1 
ATOM   8622  C  CE2   . TYR A 1 2638 ? 151.622 192.642 188.941 1.00 17.39  ? 2638 TYR A CE2   1 
ATOM   8623  C  CZ    . TYR A 1 2638 ? 151.583 193.217 190.192 1.00 19.78  ? 2638 TYR A CZ    1 
ATOM   8624  O  OH    . TYR A 1 2638 ? 151.924 192.473 191.296 1.00 22.15  ? 2638 TYR A OH    1 
ATOM   8625  N  N     . CYS A 1 2639 ? 148.373 196.535 184.307 1.00 20.25  ? 2639 CYS A N     1 
ATOM   8626  C  CA    . CYS A 1 2639 ? 148.177 197.609 183.346 1.00 15.33  ? 2639 CYS A CA    1 
ATOM   8627  C  C     . CYS A 1 2639 ? 146.839 197.435 182.644 1.00 20.50  ? 2639 CYS A C     1 
ATOM   8628  O  O     . CYS A 1 2639 ? 146.144 196.429 182.810 1.00 18.43  ? 2639 CYS A O     1 
ATOM   8629  C  CB    . CYS A 1 2639 ? 149.312 197.654 182.316 1.00 16.15  ? 2639 CYS A CB    1 
ATOM   8630  S  SG    . CYS A 1 2639 ? 150.966 197.534 183.017 1.00 21.20  ? 2639 CYS A SG    1 
ATOM   8631  N  N     . GLU A 1 2640 ? 146.486 198.440 181.848 1.00 22.77  ? 2640 GLU A N     1 
ATOM   8632  C  CA    . GLU A 1 2640 ? 145.256 198.436 181.076 1.00 18.09  ? 2640 GLU A CA    1 
ATOM   8633  C  C     . GLU A 1 2640 ? 145.513 199.051 179.708 1.00 21.85  ? 2640 GLU A C     1 
ATOM   8634  O  O     . GLU A 1 2640 ? 146.418 199.875 179.535 1.00 23.04  ? 2640 GLU A O     1 
ATOM   8635  C  CB    . GLU A 1 2640 ? 144.136 199.195 181.799 1.00 20.71  ? 2640 GLU A CB    1 
ATOM   8636  C  CG    . GLU A 1 2640 ? 144.397 200.682 181.958 1.00 35.20  ? 2640 GLU A CG    1 
ATOM   8637  C  CD    . GLU A 1 2640 ? 143.303 201.388 182.732 1.00 46.54  ? 2640 GLU A CD    1 
ATOM   8638  O  OE1   . GLU A 1 2640 ? 142.348 200.711 183.166 1.00 43.68  ? 2640 GLU A OE1   1 
ATOM   8639  O  OE2   . GLU A 1 2640 ? 143.400 202.621 182.907 1.00 44.15  ? 2640 GLU A OE2   1 
ATOM   8640  N  N     . TYR A 1 2641 ? 144.700 198.633 178.740 1.00 23.34  ? 2641 TYR A N     1 
ATOM   8641  C  CA    . TYR A 1 2641 ? 144.748 199.143 177.377 1.00 19.65  ? 2641 TYR A CA    1 
ATOM   8642  C  C     . TYR A 1 2641 ? 143.637 200.167 177.189 1.00 20.41  ? 2641 TYR A C     1 
ATOM   8643  O  O     . TYR A 1 2641 ? 142.489 199.918 177.572 1.00 26.04  ? 2641 TYR A O     1 
ATOM   8644  C  CB    . TYR A 1 2641 ? 144.579 198.019 176.350 1.00 18.05  ? 2641 TYR A CB    1 
ATOM   8645  C  CG    . TYR A 1 2641 ? 145.502 196.829 176.505 1.00 18.15  ? 2641 TYR A CG    1 
ATOM   8646  C  CD1   . TYR A 1 2641 ? 145.284 195.874 177.489 1.00 23.63  ? 2641 TYR A CD1   1 
ATOM   8647  C  CD2   . TYR A 1 2641 ? 146.574 196.646 175.645 1.00 17.73  ? 2641 TYR A CD2   1 
ATOM   8648  C  CE1   . TYR A 1 2641 ? 146.120 194.782 177.622 1.00 28.64  ? 2641 TYR A CE1   1 
ATOM   8649  C  CE2   . TYR A 1 2641 ? 147.414 195.558 175.769 1.00 17.31  ? 2641 TYR A CE2   1 
ATOM   8650  C  CZ    . TYR A 1 2641 ? 147.183 194.629 176.759 1.00 24.84  ? 2641 TYR A CZ    1 
ATOM   8651  O  OH    . TYR A 1 2641 ? 148.018 193.543 176.890 1.00 25.00  ? 2641 TYR A OH    1 
ATOM   8652  N  N     . ARG A 1 2642 ? 143.976 201.310 176.600 1.00 20.57  ? 2642 ARG A N     1 
ATOM   8653  C  CA    . ARG A 1 2642 ? 142.990 202.327 176.263 1.00 20.86  ? 2642 ARG A CA    1 
ATOM   8654  C  C     . ARG A 1 2642 ? 143.184 202.763 174.819 1.00 26.74  ? 2642 ARG A C     1 
ATOM   8655  O  O     . ARG A 1 2642 ? 144.313 202.845 174.330 1.00 25.09  ? 2642 ARG A O     1 
ATOM   8656  C  CB    . ARG A 1 2642 ? 143.076 203.538 177.206 1.00 21.57  ? 2642 ARG A CB    1 
ATOM   8657  C  CG    . ARG A 1 2642 ? 144.341 204.364 177.074 1.00 29.67  ? 2642 ARG A CG    1 
ATOM   8658  C  CD    . ARG A 1 2642 ? 144.266 205.621 177.924 1.00 35.27  ? 2642 ARG A CD    1 
ATOM   8659  N  NE    . ARG A 1 2642 ? 145.550 206.308 177.996 1.00 47.64  ? 2642 ARG A NE    1 
ATOM   8660  C  CZ    . ARG A 1 2642 ? 146.515 206.001 178.852 1.00 47.60  ? 2642 ARG A CZ    1 
ATOM   8661  N  NH1   . ARG A 1 2642 ? 146.372 205.024 179.733 1.00 40.72  ? 2642 ARG A NH1   1 
ATOM   8662  N  NH2   . ARG A 1 2642 ? 147.650 206.692 178.825 1.00 42.53  ? 2642 ARG A NH2   1 
ATOM   8663  N  N     . ARG A 1 2643 ? 142.074 203.039 174.136 1.00 32.30  ? 2643 ARG A N     1 
ATOM   8664  C  CA    . ARG A 1 2643 ? 142.107 203.403 172.720 1.00 29.23  ? 2643 ARG A CA    1 
ATOM   8665  C  C     . ARG A 1 2643 ? 142.166 204.919 172.597 1.00 28.98  ? 2643 ARG A C     1 
ATOM   8666  O  O     . ARG A 1 2643 ? 141.147 205.597 172.462 1.00 36.70  ? 2643 ARG A O     1 
ATOM   8667  C  CB    . ARG A 1 2643 ? 140.902 202.830 171.986 1.00 35.54  ? 2643 ARG A CB    1 
ATOM   8668  C  CG    . ARG A 1 2643 ? 141.132 202.638 170.496 1.00 37.59  ? 2643 ARG A CG    1 
ATOM   8669  C  CD    . ARG A 1 2643 ? 140.078 201.740 169.872 1.00 40.86  ? 2643 ARG A CD    1 
ATOM   8670  N  NE    . ARG A 1 2643 ? 140.541 200.363 169.736 1.00 48.70  ? 2643 ARG A NE    1 
ATOM   8671  C  CZ    . ARG A 1 2643 ? 141.412 199.949 168.826 1.00 53.60  ? 2643 ARG A CZ    1 
ATOM   8672  N  NH1   . ARG A 1 2643 ? 141.945 200.783 167.947 1.00 44.71  ? 2643 ARG A NH1   1 
ATOM   8673  N  NH2   . ARG A 1 2643 ? 141.758 198.665 168.795 1.00 50.51  ? 2643 ARG A NH2   1 
ATOM   8674  N  N     . THR A 1 2644 ? 143.381 205.459 172.642 1.00 29.30  ? 2644 THR A N     1 
ATOM   8675  C  CA    . THR A 1 2644 ? 143.585 206.866 172.370 1.00 34.60  ? 2644 THR A CA    1 
ATOM   8676  C  C     . THR A 1 2644 ? 143.428 207.120 170.872 1.00 39.61  ? 2644 THR A C     1 
ATOM   8677  O  O     . THR A 1 2644 ? 143.477 206.185 170.069 1.00 40.44  ? 2644 THR A O     1 
ATOM   8678  C  CB    . THR A 1 2644 ? 144.970 207.300 172.844 1.00 36.90  ? 2644 THR A CB    1 
ATOM   8679  O  OG1   . THR A 1 2644 ? 145.957 206.871 171.898 1.00 33.79  ? 2644 THR A OG1   1 
ATOM   8680  C  CG2   . THR A 1 2644 ? 145.281 206.689 174.200 1.00 36.11  ? 2644 THR A CG2   1 
ATOM   8681  N  N     . PRO A 1 2645 ? 143.222 208.378 170.469 1.00 42.66  ? 2645 PRO A N     1 
ATOM   8682  C  CA    . PRO A 1 2645 ? 143.098 208.663 169.029 1.00 44.59  ? 2645 PRO A CA    1 
ATOM   8683  C  C     . PRO A 1 2645 ? 144.298 208.219 168.209 1.00 42.28  ? 2645 PRO A C     1 
ATOM   8684  O  O     . PRO A 1 2645 ? 144.152 207.962 167.008 1.00 43.92  ? 2645 PRO A O     1 
ATOM   8685  C  CB    . PRO A 1 2645 ? 142.923 210.186 168.994 1.00 41.23  ? 2645 PRO A CB    1 
ATOM   8686  C  CG    . PRO A 1 2645 ? 142.280 210.508 170.293 1.00 42.85  ? 2645 PRO A CG    1 
ATOM   8687  C  CD    . PRO A 1 2645 ? 142.852 209.543 171.293 1.00 39.92  ? 2645 PRO A CD    1 
ATOM   8688  N  N     . ASN A 1 2646 ? 145.479 208.118 168.816 1.00 39.22  ? 2646 ASN A N     1 
ATOM   8689  C  CA    . ASN A 1 2646 ? 146.668 207.670 168.104 1.00 39.22  ? 2646 ASN A CA    1 
ATOM   8690  C  C     . ASN A 1 2646 ? 146.805 206.154 168.052 1.00 40.12  ? 2646 ASN A C     1 
ATOM   8691  O  O     . ASN A 1 2646 ? 147.693 205.655 167.352 1.00 35.14  ? 2646 ASN A O     1 
ATOM   8692  C  CB    . ASN A 1 2646 ? 147.924 208.270 168.744 1.00 39.97  ? 2646 ASN A CB    1 
ATOM   8693  C  CG    . ASN A 1 2646 ? 148.051 209.756 168.489 1.00 46.92  ? 2646 ASN A CG    1 
ATOM   8694  O  OD1   . ASN A 1 2646 ? 147.721 210.242 167.407 1.00 49.56  ? 2646 ASN A OD1   1 
ATOM   8695  N  ND2   . ASN A 1 2646 ? 148.534 210.488 169.485 1.00 49.37  ? 2646 ASN A ND2   1 
ATOM   8696  N  N     . GLY A 1 2647 ? 145.964 205.413 168.764 1.00 31.46  ? 2647 GLY A N     1 
ATOM   8697  C  CA    . GLY A 1 2647 ? 146.012 203.970 168.752 1.00 21.88  ? 2647 GLY A CA    1 
ATOM   8698  C  C     . GLY A 1 2647 ? 145.804 203.418 170.143 1.00 23.91  ? 2647 GLY A C     1 
ATOM   8699  O  O     . GLY A 1 2647 ? 145.379 204.120 171.057 1.00 31.00  ? 2647 GLY A O     1 
ATOM   8700  N  N     . VAL A 1 2648 ? 146.107 202.135 170.305 1.00 23.86  ? 2648 VAL A N     1 
ATOM   8701  C  CA    . VAL A 1 2648 ? 145.950 201.474 171.595 1.00 18.28  ? 2648 VAL A CA    1 
ATOM   8702  C  C     . VAL A 1 2648 ? 147.211 201.691 172.421 1.00 17.83  ? 2648 VAL A C     1 
ATOM   8703  O  O     . VAL A 1 2648 ? 148.327 201.438 171.954 1.00 20.00  ? 2648 VAL A O     1 
ATOM   8704  C  CB    . VAL A 1 2648 ? 145.653 199.979 171.411 1.00 19.60  ? 2648 VAL A CB    1 
ATOM   8705  C  CG1   . VAL A 1 2648 ? 145.621 199.274 172.757 1.00 18.19  ? 2648 VAL A CG1   1 
ATOM   8706  C  CG2   . VAL A 1 2648 ? 144.338 199.792 170.685 1.00 26.90  ? 2648 VAL A CG2   1 
ATOM   8707  N  N     . VAL A 1 2649 ? 147.034 202.162 173.652 1.00 19.08  ? 2649 VAL A N     1 
ATOM   8708  C  CA    . VAL A 1 2649 ? 148.132 202.441 174.567 1.00 19.27  ? 2649 VAL A CA    1 
ATOM   8709  C  C     . VAL A 1 2649 ? 147.949 201.584 175.811 1.00 18.26  ? 2649 VAL A C     1 
ATOM   8710  O  O     . VAL A 1 2649 ? 146.870 201.580 176.415 1.00 18.49  ? 2649 VAL A O     1 
ATOM   8711  C  CB    . VAL A 1 2649 ? 148.199 203.934 174.935 1.00 20.92  ? 2649 VAL A CB    1 
ATOM   8712  C  CG1   . VAL A 1 2649 ? 149.181 204.159 176.069 1.00 20.17  ? 2649 VAL A CG1   1 
ATOM   8713  C  CG2   . VAL A 1 2649 ? 148.587 204.759 173.721 1.00 24.31  ? 2649 VAL A CG2   1 
ATOM   8714  N  N     . LEU A 1 2650 ? 148.998 200.858 176.182 1.00 16.51  ? 2650 LEU A N     1 
ATOM   8715  C  CA    . LEU A 1 2650 ? 149.021 200.059 177.400 1.00 15.54  ? 2650 LEU A CA    1 
ATOM   8716  C  C     . LEU A 1 2650 ? 149.775 200.832 178.473 1.00 17.18  ? 2650 LEU A C     1 
ATOM   8717  O  O     . LEU A 1 2650 ? 150.960 201.142 178.302 1.00 15.31  ? 2650 LEU A O     1 
ATOM   8718  C  CB    . LEU A 1 2650 ? 149.678 198.703 177.154 1.00 15.11  ? 2650 LEU A CB    1 
ATOM   8719  C  CG    . LEU A 1 2650 ? 149.814 197.780 178.365 1.00 17.26  ? 2650 LEU A CG    1 
ATOM   8720  C  CD1   . LEU A 1 2650 ? 148.457 197.262 178.801 1.00 18.48  ? 2650 LEU A CD1   1 
ATOM   8721  C  CD2   . LEU A 1 2650 ? 150.754 196.630 178.053 1.00 15.33  ? 2650 LEU A CD2   1 
ATOM   8722  N  N     . ALA A 1 2651 ? 149.092 201.138 179.572 1.00 18.47  ? 2651 ALA A N     1 
ATOM   8723  C  CA    . ALA A 1 2651 ? 149.676 201.933 180.641 1.00 14.07  ? 2651 ALA A CA    1 
ATOM   8724  C  C     . ALA A 1 2651 ? 149.294 201.340 181.987 1.00 21.61  ? 2651 ALA A C     1 
ATOM   8725  O  O     . ALA A 1 2651 ? 148.244 200.700 182.108 1.00 23.07  ? 2651 ALA A O     1 
ATOM   8726  C  CB    . ALA A 1 2651 ? 149.213 203.397 180.568 1.00 17.68  ? 2651 ALA A CB    1 
ATOM   8727  N  N     . PRO A 1 2652 ? 150.119 201.541 183.016 1.00 20.70  ? 2652 PRO A N     1 
ATOM   8728  C  CA    . PRO A 1 2652 ? 149.788 201.003 184.340 1.00 20.21  ? 2652 PRO A CA    1 
ATOM   8729  C  C     . PRO A 1 2652 ? 148.493 201.591 184.879 1.00 25.48  ? 2652 PRO A C     1 
ATOM   8730  O  O     . PRO A 1 2652 ? 148.127 202.729 184.579 1.00 26.52  ? 2652 PRO A O     1 
ATOM   8731  C  CB    . PRO A 1 2652 ? 150.987 201.413 185.202 1.00 17.74  ? 2652 PRO A CB    1 
ATOM   8732  C  CG    . PRO A 1 2652 ? 152.089 201.654 184.239 1.00 17.94  ? 2652 PRO A CG    1 
ATOM   8733  C  CD    . PRO A 1 2652 ? 151.443 202.183 183.000 1.00 18.10  ? 2652 PRO A CD    1 
ATOM   8734  N  N     . VAL A 1 2653 ? 147.792 200.786 185.681 1.00 30.30  ? 2653 VAL A N     1 
ATOM   8735  C  CA    . VAL A 1 2653 ? 146.540 201.237 186.284 1.00 25.96  ? 2653 VAL A CA    1 
ATOM   8736  C  C     . VAL A 1 2653 ? 146.788 202.424 187.204 1.00 28.20  ? 2653 VAL A C     1 
ATOM   8737  O  O     . VAL A 1 2653 ? 146.035 203.405 187.194 1.00 25.99  ? 2653 VAL A O     1 
ATOM   8738  C  CB    . VAL A 1 2653 ? 145.858 200.074 187.030 1.00 27.70  ? 2653 VAL A CB    1 
ATOM   8739  C  CG1   . VAL A 1 2653 ? 144.610 200.561 187.748 1.00 40.37  ? 2653 VAL A CG1   1 
ATOM   8740  C  CG2   . VAL A 1 2653 ? 145.517 198.953 186.063 1.00 21.05  ? 2653 VAL A CG2   1 
ATOM   8741  N  N     . GLN A 1 2654 ? 147.846 202.358 188.009 1.00 30.60  ? 2654 GLN A N     1 
ATOM   8742  C  CA    . GLN A 1 2654 ? 148.196 203.451 188.911 1.00 33.06  ? 2654 GLN A CA    1 
ATOM   8743  C  C     . GLN A 1 2654 ? 148.675 204.646 188.096 1.00 28.06  ? 2654 GLN A C     1 
ATOM   8744  O  O     . GLN A 1 2654 ? 149.768 204.616 187.523 1.00 29.14  ? 2654 GLN A O     1 
ATOM   8745  C  CB    . GLN A 1 2654 ? 149.273 203.000 189.893 1.00 32.30  ? 2654 GLN A CB    1 
ATOM   8746  C  CG    . GLN A 1 2654 ? 148.961 201.703 190.617 1.00 36.51  ? 2654 GLN A CG    1 
ATOM   8747  C  CD    . GLN A 1 2654 ? 149.949 201.407 191.728 1.00 50.37  ? 2654 GLN A CD    1 
ATOM   8748  O  OE1   . GLN A 1 2654 ? 150.137 202.214 192.639 1.00 53.37  ? 2654 GLN A OE1   1 
ATOM   8749  N  NE2   . GLN A 1 2654 ? 150.590 200.246 191.658 1.00 52.64  ? 2654 GLN A NE2   1 
ATOM   8750  N  N     . LEU A 1 2655 ? 147.861 205.697 188.041 1.00 26.91  ? 2655 LEU A N     1 
ATOM   8751  C  CA    . LEU A 1 2655 ? 148.252 206.904 187.326 1.00 30.84  ? 2655 LEU A CA    1 
ATOM   8752  C  C     . LEU A 1 2655 ? 149.417 207.587 188.031 1.00 33.69  ? 2655 LEU A C     1 
ATOM   8753  O  O     . LEU A 1 2655 ? 149.523 207.563 189.260 1.00 33.07  ? 2655 LEU A O     1 
ATOM   8754  C  CB    . LEU A 1 2655 ? 147.074 207.872 187.208 1.00 33.23  ? 2655 LEU A CB    1 
ATOM   8755  C  CG    . LEU A 1 2655 ? 145.985 207.605 186.164 1.00 36.07  ? 2655 LEU A CG    1 
ATOM   8756  C  CD1   . LEU A 1 2655 ? 145.111 206.419 186.540 1.00 35.47  ? 2655 LEU A CD1   1 
ATOM   8757  C  CD2   . LEU A 1 2655 ? 145.138 208.851 185.953 1.00 33.50  ? 2655 LEU A CD2   1 
ATOM   8758  N  N     . GLY A 1 2656 ? 150.298 208.195 187.241 1.00 28.77  ? 2656 GLY A N     1 
ATOM   8759  C  CA    . GLY A 1 2656 ? 151.422 208.932 187.775 1.00 25.15  ? 2656 GLY A CA    1 
ATOM   8760  C  C     . GLY A 1 2656 ? 152.593 208.091 188.224 1.00 28.64  ? 2656 GLY A C     1 
ATOM   8761  O  O     . GLY A 1 2656 ? 153.568 208.647 188.744 1.00 34.76  ? 2656 GLY A O     1 
ATOM   8762  N  N     . LYS A 1 2657 ? 152.538 206.776 188.041 1.00 27.22  ? 2657 LYS A N     1 
ATOM   8763  C  CA    . LYS A 1 2657 ? 153.592 205.876 188.480 1.00 27.22  ? 2657 LYS A CA    1 
ATOM   8764  C  C     . LYS A 1 2657 ? 154.169 205.130 187.287 1.00 21.94  ? 2657 LYS A C     1 
ATOM   8765  O  O     . LYS A 1 2657 ? 153.440 204.747 186.368 1.00 22.54  ? 2657 LYS A O     1 
ATOM   8766  C  CB    . LYS A 1 2657 ? 153.070 204.877 189.518 1.00 27.87  ? 2657 LYS A CB    1 
ATOM   8767  C  CG    . LYS A 1 2657 ? 152.277 205.513 190.645 1.00 33.42  ? 2657 LYS A CG    1 
ATOM   8768  C  CD    . LYS A 1 2657 ? 153.179 205.872 191.811 1.00 34.50  ? 2657 LYS A CD    1 
ATOM   8769  C  CE    . LYS A 1 2657 ? 152.376 206.376 192.997 1.00 37.32  ? 2657 LYS A CE    1 
ATOM   8770  N  NZ    . LYS A 1 2657 ? 153.001 207.578 193.613 1.00 41.40  ? 2657 LYS A NZ    1 
ATOM   8771  N  N     . TRP A 1 2658 ? 155.482 204.928 187.311 1.00 18.05  ? 2658 TRP A N     1 
ATOM   8772  C  CA    . TRP A 1 2658 ? 156.183 204.160 186.293 1.00 12.87  ? 2658 TRP A CA    1 
ATOM   8773  C  C     . TRP A 1 2658 ? 156.334 202.722 186.765 1.00 18.04  ? 2658 TRP A C     1 
ATOM   8774  O  O     . TRP A 1 2658 ? 156.849 202.474 187.860 1.00 28.96  ? 2658 TRP A O     1 
ATOM   8775  C  CB    . TRP A 1 2658 ? 157.554 204.771 185.997 1.00 14.53  ? 2658 TRP A CB    1 
ATOM   8776  C  CG    . TRP A 1 2658 ? 157.514 205.825 184.940 1.00 12.00  ? 2658 TRP A CG    1 
ATOM   8777  C  CD1   . TRP A 1 2658 ? 157.120 207.120 185.087 1.00 8.89   ? 2658 TRP A CD1   1 
ATOM   8778  C  CD2   . TRP A 1 2658 ? 157.885 205.671 183.566 1.00 11.37  ? 2658 TRP A CD2   1 
ATOM   8779  N  NE1   . TRP A 1 2658 ? 157.219 207.784 183.890 1.00 10.63  ? 2658 TRP A NE1   1 
ATOM   8780  C  CE2   . TRP A 1 2658 ? 157.687 206.916 182.940 1.00 12.39  ? 2658 TRP A CE2   1 
ATOM   8781  C  CE3   . TRP A 1 2658 ? 158.365 204.602 182.805 1.00 10.01  ? 2658 TRP A CE3   1 
ATOM   8782  C  CZ2   . TRP A 1 2658 ? 157.950 207.121 181.589 1.00 11.10  ? 2658 TRP A CZ2   1 
ATOM   8783  C  CZ3   . TRP A 1 2658 ? 158.625 204.807 181.465 1.00 11.91  ? 2658 TRP A CZ3   1 
ATOM   8784  C  CH2   . TRP A 1 2658 ? 158.418 206.056 180.871 1.00 12.89  ? 2658 TRP A CH2   1 
ATOM   8785  N  N     . LEU A 1 2659 ? 155.889 201.780 185.941 1.00 14.24  ? 2659 LEU A N     1 
ATOM   8786  C  CA    . LEU A 1 2659 ? 155.943 200.366 186.288 1.00 11.64  ? 2659 LEU A CA    1 
ATOM   8787  C  C     . LEU A 1 2659 ? 157.280 199.791 185.838 1.00 14.62  ? 2659 LEU A C     1 
ATOM   8788  O  O     . LEU A 1 2659 ? 157.611 199.831 184.648 1.00 15.68  ? 2659 LEU A O     1 
ATOM   8789  C  CB    . LEU A 1 2659 ? 154.788 199.604 185.644 1.00 12.47  ? 2659 LEU A CB    1 
ATOM   8790  C  CG    . LEU A 1 2659 ? 154.555 198.208 186.219 1.00 18.26  ? 2659 LEU A CG    1 
ATOM   8791  C  CD1   . LEU A 1 2659 ? 154.062 198.313 187.651 1.00 17.11  ? 2659 LEU A CD1   1 
ATOM   8792  C  CD2   . LEU A 1 2659 ? 153.577 197.429 185.370 1.00 14.29  ? 2659 LEU A CD2   1 
ATOM   8793  N  N     . VAL A 1 2660 ? 158.041 199.258 186.786 1.00 15.27  ? 2660 VAL A N     1 
ATOM   8794  C  CA    . VAL A 1 2660 ? 159.347 198.668 186.524 1.00 13.63  ? 2660 VAL A CA    1 
ATOM   8795  C  C     . VAL A 1 2660 ? 159.184 197.157 186.584 1.00 10.95  ? 2660 VAL A C     1 
ATOM   8796  O  O     . VAL A 1 2660 ? 159.026 196.584 187.668 1.00 15.24  ? 2660 VAL A O     1 
ATOM   8797  C  CB    . VAL A 1 2660 ? 160.404 199.150 187.526 1.00 9.32   ? 2660 VAL A CB    1 
ATOM   8798  C  CG1   . VAL A 1 2660 ? 161.742 198.513 187.227 1.00 11.20  ? 2660 VAL A CG1   1 
ATOM   8799  C  CG2   . VAL A 1 2660 ? 160.514 200.664 187.496 1.00 14.81  ? 2660 VAL A CG2   1 
ATOM   8800  N  N     . LEU A 1 2661 ? 159.229 196.506 185.426 1.00 9.98   ? 2661 LEU A N     1 
ATOM   8801  C  CA    . LEU A 1 2661 ? 159.134 195.052 185.361 1.00 8.88   ? 2661 LEU A CA    1 
ATOM   8802  C  C     . LEU A 1 2661 ? 160.525 194.465 185.561 1.00 10.41  ? 2661 LEU A C     1 
ATOM   8803  O  O     . LEU A 1 2661 ? 161.362 194.508 184.654 1.00 10.94  ? 2661 LEU A O     1 
ATOM   8804  C  CB    . LEU A 1 2661 ? 158.531 194.609 184.032 1.00 8.25   ? 2661 LEU A CB    1 
ATOM   8805  C  CG    . LEU A 1 2661 ? 157.005 194.691 183.924 1.00 9.91   ? 2661 LEU A CG    1 
ATOM   8806  C  CD1   . LEU A 1 2661 ? 156.545 196.102 183.600 1.00 15.87  ? 2661 LEU A CD1   1 
ATOM   8807  C  CD2   . LEU A 1 2661 ? 156.483 193.708 182.897 1.00 10.29  ? 2661 LEU A CD2   1 
ATOM   8808  N  N     . PHE A 1 2662 ? 160.774 193.917 186.749 1.00 8.88   ? 2662 PHE A N     1 
ATOM   8809  C  CA    . PHE A 1 2662 ? 162.078 193.382 187.120 1.00 9.03   ? 2662 PHE A CA    1 
ATOM   8810  C  C     . PHE A 1 2662 ? 162.102 191.884 186.840 1.00 10.23  ? 2662 PHE A C     1 
ATOM   8811  O  O     . PHE A 1 2662 ? 161.402 191.114 187.502 1.00 11.79  ? 2662 PHE A O     1 
ATOM   8812  C  CB    . PHE A 1 2662 ? 162.374 193.664 188.590 1.00 8.68   ? 2662 PHE A CB    1 
ATOM   8813  C  CG    . PHE A 1 2662 ? 163.621 193.002 189.091 1.00 8.95   ? 2662 PHE A CG    1 
ATOM   8814  C  CD1   . PHE A 1 2662 ? 164.791 193.053 188.356 1.00 8.21   ? 2662 PHE A CD1   1 
ATOM   8815  C  CD2   . PHE A 1 2662 ? 163.619 192.317 190.292 1.00 5.81   ? 2662 PHE A CD2   1 
ATOM   8816  C  CE1   . PHE A 1 2662 ? 165.935 192.442 188.816 1.00 9.16   ? 2662 PHE A CE1   1 
ATOM   8817  C  CE2   . PHE A 1 2662 ? 164.762 191.703 190.754 1.00 5.72   ? 2662 PHE A CE2   1 
ATOM   8818  C  CZ    . PHE A 1 2662 ? 165.921 191.765 190.016 1.00 7.04   ? 2662 PHE A CZ    1 
ATOM   8819  N  N     . CYS A 1 2663 ? 162.923 191.473 185.876 1.00 10.87  ? 2663 CYS A N     1 
ATOM   8820  C  CA    . CYS A 1 2663 ? 163.066 190.068 185.519 1.00 10.22  ? 2663 CYS A CA    1 
ATOM   8821  C  C     . CYS A 1 2663 ? 164.244 189.471 186.282 1.00 13.85  ? 2663 CYS A C     1 
ATOM   8822  O  O     . CYS A 1 2663 ? 165.361 189.994 186.218 1.00 14.29  ? 2663 CYS A O     1 
ATOM   8823  C  CB    . CYS A 1 2663 ? 163.258 189.916 184.011 1.00 10.43  ? 2663 CYS A CB    1 
ATOM   8824  S  SG    . CYS A 1 2663 ? 162.159 190.958 183.023 1.00 16.42  ? 2663 CYS A SG    1 
ATOM   8825  N  N     . ASP A 1 2664 ? 163.990 188.375 187.003 1.00 16.41  ? 2664 ASP A N     1 
ATOM   8826  C  CA    . ASP A 1 2664 ? 164.998 187.828 187.907 1.00 14.91  ? 2664 ASP A CA    1 
ATOM   8827  C  C     . ASP A 1 2664 ? 166.131 187.138 187.156 1.00 20.57  ? 2664 ASP A C     1 
ATOM   8828  O  O     . ASP A 1 2664 ? 167.304 187.315 187.503 1.00 24.86  ? 2664 ASP A O     1 
ATOM   8829  C  CB    . ASP A 1 2664 ? 164.351 186.855 188.890 1.00 23.91  ? 2664 ASP A CB    1 
ATOM   8830  C  CG    . ASP A 1 2664 ? 165.255 186.530 190.064 1.00 35.36  ? 2664 ASP A CG    1 
ATOM   8831  O  OD1   . ASP A 1 2664 ? 166.241 187.266 190.276 1.00 30.54  ? 2664 ASP A OD1   1 
ATOM   8832  O  OD2   . ASP A 1 2664 ? 164.983 185.536 190.769 1.00 31.57  ? 2664 ASP A OD2   1 
ATOM   8833  N  N     . GLU A 1 2665 ? 165.806 186.317 186.152 1.00 12.47  ? 2665 GLU A N     1 
ATOM   8834  C  CA    . GLU A 1 2665 ? 166.804 185.529 185.417 1.00 10.59  ? 2665 GLU A CA    1 
ATOM   8835  C  C     . GLU A 1 2665 ? 166.550 185.707 183.921 1.00 11.43  ? 2665 GLU A C     1 
ATOM   8836  O  O     . GLU A 1 2665 ? 165.914 184.868 183.284 1.00 15.95  ? 2665 GLU A O     1 
ATOM   8837  C  CB    . GLU A 1 2665 ? 166.744 184.061 185.830 1.00 13.56  ? 2665 GLU A CB    1 
ATOM   8838  C  CG    . GLU A 1 2665 ? 166.895 183.818 187.322 1.00 19.80  ? 2665 GLU A CG    1 
ATOM   8839  C  CD    . GLU A 1 2665 ? 168.324 183.526 187.728 1.00 22.05  ? 2665 GLU A CD    1 
ATOM   8840  O  OE1   . GLU A 1 2665 ? 169.185 183.389 186.835 1.00 24.59  ? 2665 GLU A OE1   1 
ATOM   8841  O  OE2   . GLU A 1 2665 ? 168.587 183.436 188.945 1.00 25.99  ? 2665 GLU A OE2   1 
ATOM   8842  N  N     . ILE A 1 2666 ? 167.097 186.781 183.352 1.00 10.09  ? 2666 ILE A N     1 
ATOM   8843  C  CA    . ILE A 1 2666 ? 166.737 187.157 181.989 1.00 6.32   ? 2666 ILE A CA    1 
ATOM   8844  C  C     . ILE A 1 2666 ? 167.407 186.285 180.931 1.00 6.76   ? 2666 ILE A C     1 
ATOM   8845  O  O     . ILE A 1 2666 ? 166.964 186.284 179.776 1.00 10.44  ? 2666 ILE A O     1 
ATOM   8846  C  CB    . ILE A 1 2666 ? 167.060 188.642 181.752 1.00 9.12   ? 2666 ILE A CB    1 
ATOM   8847  C  CG1   . ILE A 1 2666 ? 166.134 189.229 180.683 1.00 9.51   ? 2666 ILE A CG1   1 
ATOM   8848  C  CG2   . ILE A 1 2666 ? 168.521 188.827 181.375 1.00 7.28   ? 2666 ILE A CG2   1 
ATOM   8849  C  CD1   . ILE A 1 2666 ? 166.104 190.737 180.667 1.00 8.53   ? 2666 ILE A CD1   1 
ATOM   8850  N  N     . ASN A 1 2667 ? 168.450 185.534 181.282 1.00 8.21   ? 2667 ASN A N     1 
ATOM   8851  C  CA    . ASN A 1 2667 ? 169.167 184.712 180.314 1.00 6.56   ? 2667 ASN A CA    1 
ATOM   8852  C  C     . ASN A 1 2667 ? 168.852 183.225 180.439 1.00 8.64   ? 2667 ASN A C     1 
ATOM   8853  O  O     . ASN A 1 2667 ? 169.488 182.409 179.765 1.00 8.25   ? 2667 ASN A O     1 
ATOM   8854  C  CB    . ASN A 1 2667 ? 170.675 184.943 180.435 1.00 6.53   ? 2667 ASN A CB    1 
ATOM   8855  C  CG    . ASN A 1 2667 ? 171.190 184.731 181.842 1.00 7.11   ? 2667 ASN A CG    1 
ATOM   8856  O  OD1   . ASN A 1 2667 ? 170.425 184.443 182.760 1.00 11.41  ? 2667 ASN A OD1   1 
ATOM   8857  N  ND2   . ASN A 1 2667 ? 172.497 184.873 182.019 1.00 4.67   ? 2667 ASN A ND2   1 
ATOM   8858  N  N     . LEU A 1 2668 ? 167.892 182.853 181.280 1.00 9.81   ? 2668 LEU A N     1 
ATOM   8859  C  CA    . LEU A 1 2668 ? 167.458 181.466 181.424 1.00 9.44   ? 2668 LEU A CA    1 
ATOM   8860  C  C     . LEU A 1 2668 ? 166.558 180.941 180.304 1.00 10.15  ? 2668 LEU A C     1 
ATOM   8861  O  O     . LEU A 1 2668 ? 166.653 179.750 179.982 1.00 12.09  ? 2668 LEU A O     1 
ATOM   8862  C  CB    . LEU A 1 2668 ? 166.747 181.262 182.764 1.00 10.63  ? 2668 LEU A CB    1 
ATOM   8863  C  CG    . LEU A 1 2668 ? 167.640 180.836 183.927 1.00 10.16  ? 2668 LEU A CG    1 
ATOM   8864  C  CD1   . LEU A 1 2668 ? 166.813 180.600 185.169 1.00 17.25  ? 2668 LEU A CD1   1 
ATOM   8865  C  CD2   . LEU A 1 2668 ? 168.411 179.586 183.563 1.00 11.12  ? 2668 LEU A CD2   1 
ATOM   8866  N  N     . PRO A 1 2669 ? 165.661 181.742 179.712 1.00 9.56   ? 2669 PRO A N     1 
ATOM   8867  C  CA    . PRO A 1 2669 ? 164.741 181.187 178.709 1.00 8.31   ? 2669 PRO A CA    1 
ATOM   8868  C  C     . PRO A 1 2669 ? 165.463 180.441 177.597 1.00 9.62   ? 2669 PRO A C     1 
ATOM   8869  O  O     . PRO A 1 2669 ? 166.507 180.871 177.102 1.00 15.63  ? 2669 PRO A O     1 
ATOM   8870  C  CB    . PRO A 1 2669 ? 164.019 182.426 178.177 1.00 8.21   ? 2669 PRO A CB    1 
ATOM   8871  C  CG    . PRO A 1 2669 ? 163.973 183.323 179.334 1.00 13.12  ? 2669 PRO A CG    1 
ATOM   8872  C  CD    . PRO A 1 2669 ? 165.267 183.119 180.070 1.00 11.14  ? 2669 PRO A CD    1 
ATOM   8873  N  N     . ASP A 1 2670 ? 164.891 179.302 177.217 1.00 9.55   ? 2670 ASP A N     1 
ATOM   8874  C  CA    . ASP A 1 2670 ? 165.540 178.400 176.278 1.00 12.15  ? 2670 ASP A CA    1 
ATOM   8875  C  C     . ASP A 1 2670 ? 165.619 179.013 174.887 1.00 15.12  ? 2670 ASP A C     1 
ATOM   8876  O  O     . ASP A 1 2670 ? 164.669 179.636 174.406 1.00 13.43  ? 2670 ASP A O     1 
ATOM   8877  C  CB    . ASP A 1 2670 ? 164.783 177.075 176.211 1.00 14.45  ? 2670 ASP A CB    1 
ATOM   8878  C  CG    . ASP A 1 2670 ? 165.323 176.045 177.177 1.00 30.59  ? 2670 ASP A CG    1 
ATOM   8879  O  OD1   . ASP A 1 2670 ? 166.544 176.053 177.437 1.00 31.26  ? 2670 ASP A OD1   1 
ATOM   8880  O  OD2   . ASP A 1 2670 ? 164.525 175.221 177.672 1.00 35.72  ? 2670 ASP A OD2   1 
ATOM   8881  N  N     . MET A 1 2671 ? 166.765 178.830 174.242 1.00 13.20  ? 2671 MET A N     1 
ATOM   8882  C  CA    . MET A 1 2671 ? 166.896 179.146 172.830 1.00 9.63   ? 2671 MET A CA    1 
ATOM   8883  C  C     . MET A 1 2671 ? 166.380 177.983 171.997 1.00 9.37   ? 2671 MET A C     1 
ATOM   8884  O  O     . MET A 1 2671 ? 166.595 176.815 172.335 1.00 13.30  ? 2671 MET A O     1 
ATOM   8885  C  CB    . MET A 1 2671 ? 168.353 179.435 172.472 1.00 8.37   ? 2671 MET A CB    1 
ATOM   8886  C  CG    . MET A 1 2671 ? 168.893 180.729 173.039 1.00 10.52  ? 2671 MET A CG    1 
ATOM   8887  S  SD    . MET A 1 2671 ? 170.378 181.284 172.189 1.00 24.07  ? 2671 MET A SD    1 
ATOM   8888  C  CE    . MET A 1 2671 ? 170.520 182.950 172.823 1.00 15.42  ? 2671 MET A CE    1 
ATOM   8889  N  N     . ASP A 1 2672 ? 165.694 178.304 170.905 1.00 8.78   ? 2672 ASP A N     1 
ATOM   8890  C  CA    . ASP A 1 2672 ? 165.278 177.274 169.969 1.00 9.03   ? 2672 ASP A CA    1 
ATOM   8891  C  C     . ASP A 1 2672 ? 166.499 176.750 169.214 1.00 11.42  ? 2672 ASP A C     1 
ATOM   8892  O  O     . ASP A 1 2672 ? 167.638 177.164 169.449 1.00 11.78  ? 2672 ASP A O     1 
ATOM   8893  C  CB    . ASP A 1 2672 ? 164.218 177.820 169.016 1.00 10.36  ? 2672 ASP A CB    1 
ATOM   8894  C  CG    . ASP A 1 2672 ? 164.673 179.069 168.287 1.00 10.75  ? 2672 ASP A CG    1 
ATOM   8895  O  OD1   . ASP A 1 2672 ? 165.690 179.664 168.695 1.00 10.77  ? 2672 ASP A OD1   1 
ATOM   8896  O  OD2   . ASP A 1 2672 ? 164.010 179.458 167.306 1.00 15.77  ? 2672 ASP A OD2   1 
ATOM   8897  N  N     . LYS A 1 2673 ? 166.263 175.827 168.283 1.00 10.79  ? 2673 LYS A N     1 
ATOM   8898  C  CA    . LYS A 1 2673 ? 167.374 175.283 167.511 1.00 12.12  ? 2673 LYS A CA    1 
ATOM   8899  C  C     . LYS A 1 2673 ? 167.980 176.298 166.551 1.00 10.50  ? 2673 LYS A C     1 
ATOM   8900  O  O     . LYS A 1 2673 ? 168.899 175.944 165.804 1.00 11.25  ? 2673 LYS A O     1 
ATOM   8901  C  CB    . LYS A 1 2673 ? 166.926 174.039 166.743 1.00 14.95  ? 2673 LYS A CB    1 
ATOM   8902  C  CG    . LYS A 1 2673 ? 165.919 174.310 165.650 1.00 12.38  ? 2673 LYS A CG    1 
ATOM   8903  C  CD    . LYS A 1 2673 ? 165.602 173.052 164.862 1.00 15.70  ? 2673 LYS A CD    1 
ATOM   8904  C  CE    . LYS A 1 2673 ? 164.659 172.140 165.623 1.00 17.50  ? 2673 LYS A CE    1 
ATOM   8905  N  NZ    . LYS A 1 2673 ? 163.298 172.730 165.738 1.00 24.41  ? 2673 LYS A NZ    1 
ATOM   8906  N  N     . TYR A 1 2674 ? 167.494 177.542 166.551 1.00 11.55  ? 2674 TYR A N     1 
ATOM   8907  C  CA    . TYR A 1 2674 ? 168.029 178.601 165.705 1.00 8.95   ? 2674 TYR A CA    1 
ATOM   8908  C  C     . TYR A 1 2674 ? 168.558 179.775 166.521 1.00 11.16  ? 2674 TYR A C     1 
ATOM   8909  O  O     . TYR A 1 2674 ? 168.685 180.884 165.994 1.00 13.68  ? 2674 TYR A O     1 
ATOM   8910  C  CB    . TYR A 1 2674 ? 166.964 179.074 164.716 1.00 7.56   ? 2674 TYR A CB    1 
ATOM   8911  C  CG    . TYR A 1 2674 ? 166.278 177.946 163.986 1.00 10.26  ? 2674 TYR A CG    1 
ATOM   8912  C  CD1   . TYR A 1 2674 ? 166.926 177.256 162.972 1.00 11.85  ? 2674 TYR A CD1   1 
ATOM   8913  C  CD2   . TYR A 1 2674 ? 164.983 177.569 164.310 1.00 8.83   ? 2674 TYR A CD2   1 
ATOM   8914  C  CE1   . TYR A 1 2674 ? 166.303 176.224 162.301 1.00 11.72  ? 2674 TYR A CE1   1 
ATOM   8915  C  CE2   . TYR A 1 2674 ? 164.350 176.544 163.641 1.00 11.53  ? 2674 TYR A CE2   1 
ATOM   8916  C  CZ    . TYR A 1 2674 ? 165.016 175.872 162.640 1.00 15.89  ? 2674 TYR A CZ    1 
ATOM   8917  O  OH    . TYR A 1 2674 ? 164.393 174.844 161.972 1.00 27.79  ? 2674 TYR A OH    1 
ATOM   8918  N  N     . GLY A 1 2675 ? 168.863 179.556 167.797 1.00 11.42  ? 2675 GLY A N     1 
ATOM   8919  C  CA    . GLY A 1 2675 ? 169.487 180.569 168.627 1.00 11.26  ? 2675 GLY A CA    1 
ATOM   8920  C  C     . GLY A 1 2675 ? 168.658 181.811 168.877 1.00 9.42   ? 2675 GLY A C     1 
ATOM   8921  O  O     . GLY A 1 2675 ? 169.165 182.930 168.763 1.00 9.17   ? 2675 GLY A O     1 
ATOM   8922  N  N     . THR A 1 2676 ? 167.385 181.637 169.222 1.00 8.93   ? 2676 THR A N     1 
ATOM   8923  C  CA    . THR A 1 2676 ? 166.507 182.766 169.497 1.00 7.35   ? 2676 THR A CA    1 
ATOM   8924  C  C     . THR A 1 2676 ? 165.674 182.479 170.735 1.00 6.76   ? 2676 THR A C     1 
ATOM   8925  O  O     . THR A 1 2676 ? 165.081 181.403 170.853 1.00 9.35   ? 2676 THR A O     1 
ATOM   8926  C  CB    . THR A 1 2676 ? 165.589 183.058 168.303 1.00 7.06   ? 2676 THR A CB    1 
ATOM   8927  O  OG1   . THR A 1 2676 ? 166.349 183.659 167.250 1.00 12.54  ? 2676 THR A OG1   1 
ATOM   8928  C  CG2   . THR A 1 2676 ? 164.466 184.000 168.703 1.00 5.17   ? 2676 THR A CG2   1 
ATOM   8929  N  N     . GLN A 1 2677 ? 165.638 183.439 171.655 1.00 7.53   ? 2677 GLN A N     1 
ATOM   8930  C  CA    . GLN A 1 2677 ? 164.722 183.413 172.786 1.00 5.66   ? 2677 GLN A CA    1 
ATOM   8931  C  C     . GLN A 1 2677 ? 163.541 184.319 172.464 1.00 5.50   ? 2677 GLN A C     1 
ATOM   8932  O  O     . GLN A 1 2677 ? 163.725 185.514 172.211 1.00 8.93   ? 2677 GLN A O     1 
ATOM   8933  C  CB    . GLN A 1 2677 ? 165.417 183.865 174.069 1.00 4.85   ? 2677 GLN A CB    1 
ATOM   8934  C  CG    . GLN A 1 2677 ? 166.528 182.945 174.523 1.00 7.22   ? 2677 GLN A CG    1 
ATOM   8935  C  CD    . GLN A 1 2677 ? 167.601 183.670 175.301 1.00 9.34   ? 2677 GLN A CD    1 
ATOM   8936  O  OE1   . GLN A 1 2677 ? 168.165 184.657 174.830 1.00 15.17  ? 2677 GLN A OE1   1 
ATOM   8937  N  NE2   . GLN A 1 2677 ? 167.893 183.184 176.501 1.00 8.33   ? 2677 GLN A NE2   1 
ATOM   8938  N  N     . ARG A 1 2678 ? 162.335 183.749 172.471 1.00 4.90   ? 2678 ARG A N     1 
ATOM   8939  C  CA    . ARG A 1 2678 ? 161.157 184.508 172.064 1.00 4.97   ? 2678 ARG A CA    1 
ATOM   8940  C  C     . ARG A 1 2678 ? 160.883 185.672 173.007 1.00 5.61   ? 2678 ARG A C     1 
ATOM   8941  O  O     . ARG A 1 2678 ? 160.543 186.772 172.559 1.00 6.76   ? 2678 ARG A O     1 
ATOM   8942  C  CB    . ARG A 1 2678 ? 159.940 183.587 171.980 1.00 3.95   ? 2678 ARG A CB    1 
ATOM   8943  C  CG    . ARG A 1 2678 ? 158.673 184.291 171.531 1.00 5.10   ? 2678 ARG A CG    1 
ATOM   8944  C  CD    . ARG A 1 2678 ? 157.487 183.350 171.508 1.00 5.45   ? 2678 ARG A CD    1 
ATOM   8945  N  NE    . ARG A 1 2678 ? 157.679 182.263 170.558 1.00 8.66   ? 2678 ARG A NE    1 
ATOM   8946  C  CZ    . ARG A 1 2678 ? 156.873 181.217 170.445 1.00 7.03   ? 2678 ARG A CZ    1 
ATOM   8947  N  NH1   . ARG A 1 2678 ? 155.800 181.087 171.206 1.00 6.64   ? 2678 ARG A NH1   1 
ATOM   8948  N  NH2   . ARG A 1 2678 ? 157.150 180.280 169.544 1.00 5.41   ? 2678 ARG A NH2   1 
ATOM   8949  N  N     . VAL A 1 2679 ? 161.018 185.452 174.316 1.00 5.55   ? 2679 VAL A N     1 
ATOM   8950  C  CA    . VAL A 1 2679 ? 160.741 186.518 175.274 1.00 5.64   ? 2679 VAL A CA    1 
ATOM   8951  C  C     . VAL A 1 2679 ? 161.778 187.631 175.154 1.00 6.49   ? 2679 VAL A C     1 
ATOM   8952  O  O     . VAL A 1 2679 ? 161.461 188.815 175.324 1.00 8.33   ? 2679 VAL A O     1 
ATOM   8953  C  CB    . VAL A 1 2679 ? 160.664 185.948 176.704 1.00 5.71   ? 2679 VAL A CB    1 
ATOM   8954  C  CG1   . VAL A 1 2679 ? 161.951 185.239 177.074 1.00 5.93   ? 2679 VAL A CG1   1 
ATOM   8955  C  CG2   . VAL A 1 2679 ? 160.339 187.045 177.706 1.00 4.62   ? 2679 VAL A CG2   1 
ATOM   8956  N  N     . ILE A 1 2680 ? 163.029 187.275 174.858 1.00 4.42   ? 2680 ILE A N     1 
ATOM   8957  C  CA    . ILE A 1 2680 ? 164.059 188.290 174.666 1.00 4.04   ? 2680 ILE A CA    1 
ATOM   8958  C  C     . ILE A 1 2680 ? 163.749 189.139 173.440 1.00 6.03   ? 2680 ILE A C     1 
ATOM   8959  O  O     . ILE A 1 2680 ? 163.904 190.365 173.463 1.00 7.96   ? 2680 ILE A O     1 
ATOM   8960  C  CB    . ILE A 1 2680 ? 165.446 187.631 174.573 1.00 5.44   ? 2680 ILE A CB    1 
ATOM   8961  C  CG1   . ILE A 1 2680 ? 165.801 186.967 175.902 1.00 8.10   ? 2680 ILE A CG1   1 
ATOM   8962  C  CG2   . ILE A 1 2680 ? 166.503 188.654 174.197 1.00 4.61   ? 2680 ILE A CG2   1 
ATOM   8963  C  CD1   . ILE A 1 2680 ? 165.777 187.913 177.078 1.00 6.93   ? 2680 ILE A CD1   1 
ATOM   8964  N  N     . SER A 1 2681 ? 163.299 188.507 172.354 1.00 6.67   ? 2681 SER A N     1 
ATOM   8965  C  CA    . SER A 1 2681 ? 162.882 189.263 171.177 1.00 4.35   ? 2681 SER A CA    1 
ATOM   8966  C  C     . SER A 1 2681 ? 161.672 190.136 171.483 1.00 5.14   ? 2681 SER A C     1 
ATOM   8967  O  O     . SER A 1 2681 ? 161.566 191.259 170.979 1.00 9.50   ? 2681 SER A O     1 
ATOM   8968  C  CB    . SER A 1 2681 ? 162.577 188.312 170.022 1.00 5.42   ? 2681 SER A CB    1 
ATOM   8969  O  OG    . SER A 1 2681 ? 163.759 187.704 169.537 1.00 11.03  ? 2681 SER A OG    1 
ATOM   8970  N  N     . PHE A 1 2682 ? 160.752 189.636 172.308 1.00 5.48   ? 2682 PHE A N     1 
ATOM   8971  C  CA    . PHE A 1 2682 ? 159.581 190.415 172.698 1.00 5.02   ? 2682 PHE A CA    1 
ATOM   8972  C  C     . PHE A 1 2682 ? 159.991 191.668 173.465 1.00 6.94   ? 2682 PHE A C     1 
ATOM   8973  O  O     . PHE A 1 2682 ? 159.488 192.769 173.206 1.00 5.93   ? 2682 PHE A O     1 
ATOM   8974  C  CB    . PHE A 1 2682 ? 158.653 189.538 173.539 1.00 3.91   ? 2682 PHE A CB    1 
ATOM   8975  C  CG    . PHE A 1 2682 ? 157.317 190.154 173.821 1.00 6.80   ? 2682 PHE A CG    1 
ATOM   8976  C  CD1   . PHE A 1 2682 ? 156.464 190.487 172.785 1.00 6.91   ? 2682 PHE A CD1   1 
ATOM   8977  C  CD2   . PHE A 1 2682 ? 156.907 190.388 175.122 1.00 5.62   ? 2682 PHE A CD2   1 
ATOM   8978  C  CE1   . PHE A 1 2682 ? 155.229 191.045 173.043 1.00 7.59   ? 2682 PHE A CE1   1 
ATOM   8979  C  CE2   . PHE A 1 2682 ? 155.677 190.952 175.384 1.00 5.70   ? 2682 PHE A CE2   1 
ATOM   8980  C  CZ    . PHE A 1 2682 ? 154.837 191.282 174.345 1.00 6.48   ? 2682 PHE A CZ    1 
ATOM   8981  N  N     . ILE A 1 2683 ? 160.919 191.517 174.411 1.00 5.52   ? 2683 ILE A N     1 
ATOM   8982  C  CA    . ILE A 1 2683 ? 161.396 192.660 175.184 1.00 5.17   ? 2683 ILE A CA    1 
ATOM   8983  C  C     . ILE A 1 2683 ? 162.164 193.627 174.292 1.00 5.99   ? 2683 ILE A C     1 
ATOM   8984  O  O     . ILE A 1 2683 ? 162.041 194.851 174.427 1.00 9.49   ? 2683 ILE A O     1 
ATOM   8985  C  CB    . ILE A 1 2683 ? 162.248 192.183 176.374 1.00 7.15   ? 2683 ILE A CB    1 
ATOM   8986  C  CG1   . ILE A 1 2683 ? 161.402 191.344 177.333 1.00 6.46   ? 2683 ILE A CG1   1 
ATOM   8987  C  CG2   . ILE A 1 2683 ? 162.857 193.364 177.110 1.00 4.20   ? 2683 ILE A CG2   1 
ATOM   8988  C  CD1   . ILE A 1 2683 ? 162.188 190.745 178.474 1.00 6.48   ? 2683 ILE A CD1   1 
ATOM   8989  N  N     . ARG A 1 2684 ? 162.967 193.097 173.367 1.00 5.03   ? 2684 ARG A N     1 
ATOM   8990  C  CA    . ARG A 1 2684 ? 163.695 193.956 172.441 1.00 5.85   ? 2684 ARG A CA    1 
ATOM   8991  C  C     . ARG A 1 2684 ? 162.735 194.757 171.573 1.00 7.02   ? 2684 ARG A C     1 
ATOM   8992  O  O     . ARG A 1 2684 ? 162.987 195.931 171.281 1.00 9.53   ? 2684 ARG A O     1 
ATOM   8993  C  CB    . ARG A 1 2684 ? 164.638 193.113 171.583 1.00 5.21   ? 2684 ARG A CB    1 
ATOM   8994  C  CG    . ARG A 1 2684 ? 165.539 193.910 170.657 1.00 4.00   ? 2684 ARG A CG    1 
ATOM   8995  C  CD    . ARG A 1 2684 ? 165.173 193.689 169.204 1.00 5.98   ? 2684 ARG A CD    1 
ATOM   8996  N  NE    . ARG A 1 2684 ? 165.944 194.547 168.315 1.00 8.32   ? 2684 ARG A NE    1 
ATOM   8997  C  CZ    . ARG A 1 2684 ? 165.756 194.631 167.006 1.00 6.23   ? 2684 ARG A CZ    1 
ATOM   8998  N  NH1   . ARG A 1 2684 ? 164.835 193.907 166.393 1.00 6.26   ? 2684 ARG A NH1   1 
ATOM   8999  N  NH2   . ARG A 1 2684 ? 166.514 195.457 166.294 1.00 8.21   ? 2684 ARG A NH2   1 
ATOM   9000  N  N     . GLN A 1 2685 ? 161.635 194.137 171.145 1.00 6.02   ? 2685 GLN A N     1 
ATOM   9001  C  CA    . GLN A 1 2685 ? 160.624 194.870 170.393 1.00 5.85   ? 2685 GLN A CA    1 
ATOM   9002  C  C     . GLN A 1 2685 ? 159.958 195.940 171.251 1.00 7.14   ? 2685 GLN A C     1 
ATOM   9003  O  O     . GLN A 1 2685 ? 159.747 197.066 170.789 1.00 8.22   ? 2685 GLN A O     1 
ATOM   9004  C  CB    . GLN A 1 2685 ? 159.585 193.905 169.828 1.00 5.01   ? 2685 GLN A CB    1 
ATOM   9005  C  CG    . GLN A 1 2685 ? 158.359 194.590 169.255 1.00 4.51   ? 2685 GLN A CG    1 
ATOM   9006  C  CD    . GLN A 1 2685 ? 157.394 193.618 168.618 1.00 5.56   ? 2685 GLN A CD    1 
ATOM   9007  O  OE1   . GLN A 1 2685 ? 156.951 192.661 169.249 1.00 5.35   ? 2685 GLN A OE1   1 
ATOM   9008  N  NE2   . GLN A 1 2685 ? 157.067 193.855 167.355 1.00 7.41   ? 2685 GLN A NE2   1 
ATOM   9009  N  N     . MET A 1 2686 ? 159.618 195.613 172.503 1.00 7.33   ? 2686 MET A N     1 
ATOM   9010  C  CA    . MET A 1 2686 ? 158.984 196.615 173.357 1.00 6.55   ? 2686 MET A CA    1 
ATOM   9011  C  C     . MET A 1 2686 ? 159.919 197.768 173.688 1.00 6.70   ? 2686 MET A C     1 
ATOM   9012  O  O     . MET A 1 2686 ? 159.444 198.868 173.984 1.00 7.63   ? 2686 MET A O     1 
ATOM   9013  C  CB    . MET A 1 2686 ? 158.475 196.007 174.666 1.00 6.00   ? 2686 MET A CB    1 
ATOM   9014  C  CG    . MET A 1 2686 ? 157.335 195.018 174.525 1.00 7.40   ? 2686 MET A CG    1 
ATOM   9015  S  SD    . MET A 1 2686 ? 156.773 194.430 176.135 1.00 23.67  ? 2686 MET A SD    1 
ATOM   9016  C  CE    . MET A 1 2686 ? 158.102 193.329 176.597 1.00 6.13   ? 2686 MET A CE    1 
ATOM   9017  N  N     . VAL A 1 2687 ? 161.227 197.544 173.656 1.00 7.08   ? 2687 VAL A N     1 
ATOM   9018  C  CA    . VAL A 1 2687 ? 162.180 198.597 173.991 1.00 6.64   ? 2687 VAL A CA    1 
ATOM   9019  C  C     . VAL A 1 2687 ? 162.542 199.435 172.772 1.00 9.17   ? 2687 VAL A C     1 
ATOM   9020  O  O     . VAL A 1 2687 ? 162.481 200.666 172.812 1.00 16.38  ? 2687 VAL A O     1 
ATOM   9021  C  CB    . VAL A 1 2687 ? 163.434 197.980 174.645 1.00 6.41   ? 2687 VAL A CB    1 
ATOM   9022  C  CG1   . VAL A 1 2687 ? 164.565 198.991 174.676 1.00 11.05  ? 2687 VAL A CG1   1 
ATOM   9023  C  CG2   . VAL A 1 2687 ? 163.112 197.493 176.047 1.00 6.64   ? 2687 VAL A CG2   1 
ATOM   9024  N  N     . GLU A 1 2688 ? 162.919 198.787 171.668 1.00 9.67   ? 2688 GLU A N     1 
ATOM   9025  C  CA    . GLU A 1 2688 ? 163.411 199.521 170.507 1.00 7.73   ? 2688 GLU A CA    1 
ATOM   9026  C  C     . GLU A 1 2688 ? 162.265 200.166 169.732 1.00 7.36   ? 2688 GLU A C     1 
ATOM   9027  O  O     . GLU A 1 2688 ? 162.413 201.268 169.191 1.00 15.55  ? 2688 GLU A O     1 
ATOM   9028  C  CB    . GLU A 1 2688 ? 164.239 198.585 169.620 1.00 8.30   ? 2688 GLU A CB    1 
ATOM   9029  C  CG    . GLU A 1 2688 ? 165.018 199.260 168.491 1.00 11.12  ? 2688 GLU A CG    1 
ATOM   9030  C  CD    . GLU A 1 2688 ? 164.192 199.499 167.251 1.00 22.45  ? 2688 GLU A CD    1 
ATOM   9031  O  OE1   . GLU A 1 2688 ? 163.254 198.718 167.019 1.00 24.55  ? 2688 GLU A OE1   1 
ATOM   9032  O  OE2   . GLU A 1 2688 ? 164.481 200.463 166.511 1.00 26.26  ? 2688 GLU A OE2   1 
ATOM   9033  N  N     . HIS A 1 2689 ? 161.115 199.497 169.666 1.00 7.02   ? 2689 HIS A N     1 
ATOM   9034  C  CA    . HIS A 1 2689 ? 159.936 200.039 169.000 1.00 7.59   ? 2689 HIS A CA    1 
ATOM   9035  C  C     . HIS A 1 2689 ? 158.932 200.667 169.957 1.00 10.18  ? 2689 HIS A C     1 
ATOM   9036  O  O     . HIS A 1 2689 ? 157.964 201.280 169.497 1.00 13.66  ? 2689 HIS A O     1 
ATOM   9037  C  CB    . HIS A 1 2689 ? 159.243 198.951 168.174 1.00 6.97   ? 2689 HIS A CB    1 
ATOM   9038  C  CG    . HIS A 1 2689 ? 160.089 198.399 167.071 1.00 8.50   ? 2689 HIS A CG    1 
ATOM   9039  N  ND1   . HIS A 1 2689 ? 160.480 197.079 167.020 1.00 9.99   ? 2689 HIS A ND1   1 
ATOM   9040  C  CD2   . HIS A 1 2689 ? 160.597 198.985 165.962 1.00 9.17   ? 2689 HIS A CD2   1 
ATOM   9041  C  CE1   . HIS A 1 2689 ? 161.207 196.879 165.936 1.00 13.64  ? 2689 HIS A CE1   1 
ATOM   9042  N  NE2   . HIS A 1 2689 ? 161.296 198.020 165.278 1.00 10.16  ? 2689 HIS A NE2   1 
ATOM   9043  N  N     . GLY A 1 2690 ? 159.135 200.538 171.264 1.00 8.45   ? 2690 GLY A N     1 
ATOM   9044  C  CA    . GLY A 1 2690 ? 158.222 201.143 172.222 1.00 6.65   ? 2690 GLY A CA    1 
ATOM   9045  C  C     . GLY A 1 2690 ? 156.824 200.566 172.199 1.00 7.30   ? 2690 GLY A C     1 
ATOM   9046  O  O     . GLY A 1 2690 ? 155.846 201.309 172.354 1.00 10.11  ? 2690 GLY A O     1 
ATOM   9047  N  N     . GLY A 1 2691 ? 156.704 199.262 172.017 1.00 7.51   ? 2691 GLY A N     1 
ATOM   9048  C  CA    . GLY A 1 2691 ? 155.402 198.630 171.974 1.00 8.03   ? 2691 GLY A CA    1 
ATOM   9049  C  C     . GLY A 1 2691 ? 155.499 197.233 171.403 1.00 8.35   ? 2691 GLY A C     1 
ATOM   9050  O  O     . GLY A 1 2691 ? 156.576 196.743 171.065 1.00 8.33   ? 2691 GLY A O     1 
ATOM   9051  N  N     . PHE A 1 2692 ? 154.334 196.601 171.299 1.00 8.59   ? 2692 PHE A N     1 
ATOM   9052  C  CA    . PHE A 1 2692 ? 154.241 195.236 170.791 1.00 6.45   ? 2692 PHE A CA    1 
ATOM   9053  C  C     . PHE A 1 2692 ? 152.953 195.102 169.987 1.00 9.13   ? 2692 PHE A C     1 
ATOM   9054  O  O     . PHE A 1 2692 ? 152.286 196.091 169.672 1.00 11.23  ? 2692 PHE A O     1 
ATOM   9055  C  CB    . PHE A 1 2692 ? 154.314 194.217 171.937 1.00 6.11   ? 2692 PHE A CB    1 
ATOM   9056  C  CG    . PHE A 1 2692 ? 153.198 194.339 172.934 1.00 8.04   ? 2692 PHE A CG    1 
ATOM   9057  C  CD1   . PHE A 1 2692 ? 153.289 195.227 173.991 1.00 8.85   ? 2692 PHE A CD1   1 
ATOM   9058  C  CD2   . PHE A 1 2692 ? 152.059 193.563 172.816 1.00 7.24   ? 2692 PHE A CD2   1 
ATOM   9059  C  CE1   . PHE A 1 2692 ? 152.265 195.339 174.907 1.00 11.39  ? 2692 PHE A CE1   1 
ATOM   9060  C  CE2   . PHE A 1 2692 ? 151.033 193.673 173.728 1.00 7.97   ? 2692 PHE A CE2   1 
ATOM   9061  C  CZ    . PHE A 1 2692 ? 151.136 194.562 174.775 1.00 12.27  ? 2692 PHE A CZ    1 
ATOM   9062  N  N     . TYR A 1 2693 ? 152.605 193.865 169.644 1.00 8.73   ? 2693 TYR A N     1 
ATOM   9063  C  CA    . TYR A 1 2693 ? 151.408 193.567 168.868 1.00 8.38   ? 2693 TYR A CA    1 
ATOM   9064  C  C     . TYR A 1 2693 ? 150.470 192.713 169.706 1.00 11.74  ? 2693 TYR A C     1 
ATOM   9065  O  O     . TYR A 1 2693 ? 150.865 191.651 170.198 1.00 15.72  ? 2693 TYR A O     1 
ATOM   9066  C  CB    . TYR A 1 2693 ? 151.762 192.842 167.567 1.00 7.71   ? 2693 TYR A CB    1 
ATOM   9067  C  CG    . TYR A 1 2693 ? 151.976 193.755 166.383 1.00 7.57   ? 2693 TYR A CG    1 
ATOM   9068  C  CD1   . TYR A 1 2693 ? 150.912 194.421 165.794 1.00 7.02   ? 2693 TYR A CD1   1 
ATOM   9069  C  CD2   . TYR A 1 2693 ? 153.242 193.942 165.849 1.00 8.93   ? 2693 TYR A CD2   1 
ATOM   9070  C  CE1   . TYR A 1 2693 ? 151.104 195.252 164.712 1.00 7.10   ? 2693 TYR A CE1   1 
ATOM   9071  C  CE2   . TYR A 1 2693 ? 153.443 194.770 164.765 1.00 6.76   ? 2693 TYR A CE2   1 
ATOM   9072  C  CZ    . TYR A 1 2693 ? 152.372 195.423 164.201 1.00 7.31   ? 2693 TYR A CZ    1 
ATOM   9073  O  OH    . TYR A 1 2693 ? 152.569 196.250 163.121 1.00 18.07  ? 2693 TYR A OH    1 
ATOM   9074  N  N     . ARG A 1 2694 ? 149.234 193.177 169.869 1.00 9.09   ? 2694 ARG A N     1 
ATOM   9075  C  CA    . ARG A 1 2694 ? 148.179 192.370 170.461 1.00 11.68  ? 2694 ARG A CA    1 
ATOM   9076  C  C     . ARG A 1 2694 ? 147.638 191.426 169.396 1.00 15.11  ? 2694 ARG A C     1 
ATOM   9077  O  O     . ARG A 1 2694 ? 147.146 191.875 168.351 1.00 19.66  ? 2694 ARG A O     1 
ATOM   9078  C  CB    . ARG A 1 2694 ? 147.071 193.260 171.015 1.00 18.15  ? 2694 ARG A CB    1 
ATOM   9079  C  CG    . ARG A 1 2694 ? 146.033 192.524 171.843 1.00 18.19  ? 2694 ARG A CG    1 
ATOM   9080  C  CD    . ARG A 1 2694 ? 145.113 193.497 172.557 1.00 20.23  ? 2694 ARG A CD    1 
ATOM   9081  N  NE    . ARG A 1 2694 ? 144.503 194.449 171.637 1.00 19.61  ? 2694 ARG A NE    1 
ATOM   9082  C  CZ    . ARG A 1 2694 ? 143.701 195.438 172.006 1.00 20.92  ? 2694 ARG A CZ    1 
ATOM   9083  N  NH1   . ARG A 1 2694 ? 143.401 195.645 173.277 1.00 15.26  ? 2694 ARG A NH1   1 
ATOM   9084  N  NH2   . ARG A 1 2694 ? 143.187 196.238 171.077 1.00 25.21  ? 2694 ARG A NH2   1 
ATOM   9085  N  N     . THR A 1 2695 ? 147.744 190.124 169.660 1.00 13.86  ? 2695 THR A N     1 
ATOM   9086  C  CA    . THR A 1 2695 ? 147.384 189.093 168.697 1.00 15.19  ? 2695 THR A CA    1 
ATOM   9087  C  C     . THR A 1 2695 ? 145.903 188.747 168.717 1.00 17.67  ? 2695 THR A C     1 
ATOM   9088  O  O     . THR A 1 2695 ? 145.463 187.944 167.888 1.00 26.29  ? 2695 THR A O     1 
ATOM   9089  C  CB    . THR A 1 2695 ? 148.201 187.824 168.954 1.00 13.39  ? 2695 THR A CB    1 
ATOM   9090  O  OG1   . THR A 1 2695 ? 147.918 187.330 170.268 1.00 15.56  ? 2695 THR A OG1   1 
ATOM   9091  C  CG2   . THR A 1 2695 ? 149.688 188.119 168.844 1.00 10.17  ? 2695 THR A CG2   1 
ATOM   9092  N  N     . SER A 1 2696 ? 145.129 189.310 169.646 1.00 18.68  ? 2696 SER A N     1 
ATOM   9093  C  CA    . SER A 1 2696 ? 143.687 189.098 169.617 1.00 17.97  ? 2696 SER A CA    1 
ATOM   9094  C  C     . SER A 1 2696 ? 143.074 189.710 168.365 1.00 20.17  ? 2696 SER A C     1 
ATOM   9095  O  O     . SER A 1 2696 ? 142.193 189.111 167.737 1.00 24.99  ? 2696 SER A O     1 
ATOM   9096  C  CB    . SER A 1 2696 ? 143.043 189.683 170.873 1.00 19.62  ? 2696 SER A CB    1 
ATOM   9097  O  OG    . SER A 1 2696 ? 142.720 191.050 170.692 1.00 19.20  ? 2696 SER A OG    1 
ATOM   9098  N  N     . ASP A 1 2697 ? 143.532 190.904 167.985 1.00 16.65  ? 2697 ASP A N     1 
ATOM   9099  C  CA    . ASP A 1 2697 ? 143.029 191.592 166.805 1.00 17.21  ? 2697 ASP A CA    1 
ATOM   9100  C  C     . ASP A 1 2697 ? 144.147 192.141 165.929 1.00 18.87  ? 2697 ASP A C     1 
ATOM   9101  O  O     . ASP A 1 2697 ? 143.871 192.940 165.026 1.00 19.54  ? 2697 ASP A O     1 
ATOM   9102  C  CB    . ASP A 1 2697 ? 142.082 192.727 167.212 1.00 21.45  ? 2697 ASP A CB    1 
ATOM   9103  C  CG    . ASP A 1 2697 ? 142.759 193.762 168.082 1.00 24.38  ? 2697 ASP A CG    1 
ATOM   9104  O  OD1   . ASP A 1 2697 ? 143.533 193.372 168.981 1.00 23.26  ? 2697 ASP A OD1   1 
ATOM   9105  O  OD2   . ASP A 1 2697 ? 142.515 194.968 167.872 1.00 30.06  ? 2697 ASP A OD2   1 
ATOM   9106  N  N     . GLN A 1 2698 ? 145.396 191.734 166.171 1.00 18.55  ? 2698 GLN A N     1 
ATOM   9107  C  CA    . GLN A 1 2698 ? 146.550 192.189 165.395 1.00 17.34  ? 2698 GLN A CA    1 
ATOM   9108  C  C     . GLN A 1 2698 ? 146.670 193.712 165.427 1.00 14.76  ? 2698 GLN A C     1 
ATOM   9109  O  O     . GLN A 1 2698 ? 146.720 194.376 164.390 1.00 17.40  ? 2698 GLN A O     1 
ATOM   9110  C  CB    . GLN A 1 2698 ? 146.486 191.680 163.951 1.00 14.15  ? 2698 GLN A CB    1 
ATOM   9111  C  CG    . GLN A 1 2698 ? 146.770 190.199 163.774 1.00 11.57  ? 2698 GLN A CG    1 
ATOM   9112  C  CD    . GLN A 1 2698 ? 145.673 189.315 164.325 1.00 14.72  ? 2698 GLN A CD    1 
ATOM   9113  O  OE1   . GLN A 1 2698 ? 145.905 188.505 165.219 1.00 21.46  ? 2698 GLN A OE1   1 
ATOM   9114  N  NE2   . GLN A 1 2698 ? 144.469 189.461 163.788 1.00 16.90  ? 2698 GLN A NE2   1 
ATOM   9115  N  N     . THR A 1 2699 ? 146.718 194.269 166.633 1.00 14.96  ? 2699 THR A N     1 
ATOM   9116  C  CA    . THR A 1 2699 ? 146.740 195.717 166.812 1.00 14.73  ? 2699 THR A CA    1 
ATOM   9117  C  C     . THR A 1 2699 ? 148.032 196.139 167.495 1.00 15.00  ? 2699 THR A C     1 
ATOM   9118  O  O     . THR A 1 2699 ? 148.434 195.539 168.494 1.00 17.27  ? 2699 THR A O     1 
ATOM   9119  C  CB    . THR A 1 2699 ? 145.532 196.187 167.628 1.00 18.03  ? 2699 THR A CB    1 
ATOM   9120  O  OG1   . THR A 1 2699 ? 144.338 196.015 166.857 1.00 27.45  ? 2699 THR A OG1   1 
ATOM   9121  C  CG2   . THR A 1 2699 ? 145.670 197.653 167.998 1.00 16.81  ? 2699 THR A CG2   1 
ATOM   9122  N  N     . TRP A 1 2700 ? 148.680 197.169 166.959 1.00 10.00  ? 2700 TRP A N     1 
ATOM   9123  C  CA    . TRP A 1 2700 ? 149.889 197.689 167.583 1.00 8.78   ? 2700 TRP A CA    1 
ATOM   9124  C  C     . TRP A 1 2700 ? 149.533 198.407 168.880 1.00 13.60  ? 2700 TRP A C     1 
ATOM   9125  O  O     . TRP A 1 2700 ? 148.740 199.355 168.877 1.00 15.44  ? 2700 TRP A O     1 
ATOM   9126  C  CB    . TRP A 1 2700 ? 150.620 198.632 166.632 1.00 9.42   ? 2700 TRP A CB    1 
ATOM   9127  C  CG    . TRP A 1 2700 ? 151.840 199.243 167.242 1.00 7.55   ? 2700 TRP A CG    1 
ATOM   9128  C  CD1   . TRP A 1 2700 ? 151.967 200.511 167.725 1.00 8.99   ? 2700 TRP A CD1   1 
ATOM   9129  C  CD2   . TRP A 1 2700 ? 153.107 198.607 167.446 1.00 8.39   ? 2700 TRP A CD2   1 
ATOM   9130  N  NE1   . TRP A 1 2700 ? 153.235 200.707 168.213 1.00 11.55  ? 2700 TRP A NE1   1 
ATOM   9131  C  CE2   . TRP A 1 2700 ? 153.955 199.552 168.054 1.00 11.84  ? 2700 TRP A CE2   1 
ATOM   9132  C  CE3   . TRP A 1 2700 ? 153.607 197.332 167.170 1.00 6.01   ? 2700 TRP A CE3   1 
ATOM   9133  C  CZ2   . TRP A 1 2700 ? 155.274 199.263 168.390 1.00 8.44   ? 2700 TRP A CZ2   1 
ATOM   9134  C  CZ3   . TRP A 1 2700 ? 154.914 197.046 167.507 1.00 6.18   ? 2700 TRP A CZ3   1 
ATOM   9135  C  CH2   . TRP A 1 2700 ? 155.733 198.007 168.109 1.00 7.48   ? 2700 TRP A CH2   1 
ATOM   9136  N  N     . VAL A 1 2701 ? 150.118 197.957 169.985 1.00 12.46  ? 2701 VAL A N     1 
ATOM   9137  C  CA    . VAL A 1 2701 ? 149.915 198.550 171.300 1.00 11.05  ? 2701 VAL A CA    1 
ATOM   9138  C  C     . VAL A 1 2701 ? 151.203 199.255 171.694 1.00 12.98  ? 2701 VAL A C     1 
ATOM   9139  O  O     . VAL A 1 2701 ? 152.284 198.652 171.667 1.00 13.40  ? 2701 VAL A O     1 
ATOM   9140  C  CB    . VAL A 1 2701 ? 149.524 197.496 172.346 1.00 11.38  ? 2701 VAL A CB    1 
ATOM   9141  C  CG1   . VAL A 1 2701 ? 148.997 198.169 173.596 1.00 13.12  ? 2701 VAL A CG1   1 
ATOM   9142  C  CG2   . VAL A 1 2701 ? 148.491 196.543 171.774 1.00 14.56  ? 2701 VAL A CG2   1 
ATOM   9143  N  N     . LYS A 1 2702 ? 151.088 200.529 172.054 1.00 11.28  ? 2702 LYS A N     1 
ATOM   9144  C  CA    . LYS A 1 2702 ? 152.228 201.344 172.452 1.00 11.08  ? 2702 LYS A CA    1 
ATOM   9145  C  C     . LYS A 1 2702 ? 152.321 201.387 173.971 1.00 12.54  ? 2702 LYS A C     1 
ATOM   9146  O  O     . LYS A 1 2702 ? 151.323 201.642 174.651 1.00 16.83  ? 2702 LYS A O     1 
ATOM   9147  C  CB    . LYS A 1 2702 ? 152.105 202.759 171.887 1.00 11.96  ? 2702 LYS A CB    1 
ATOM   9148  C  CG    . LYS A 1 2702 ? 153.271 203.666 172.224 1.00 13.95  ? 2702 LYS A CG    1 
ATOM   9149  C  CD    . LYS A 1 2702 ? 153.147 205.002 171.517 1.00 20.24  ? 2702 LYS A CD    1 
ATOM   9150  C  CE    . LYS A 1 2702 ? 152.030 205.838 172.118 1.00 25.95  ? 2702 LYS A CE    1 
ATOM   9151  N  NZ    . LYS A 1 2702 ? 152.351 206.284 173.500 1.00 22.96  ? 2702 LYS A NZ    1 
ATOM   9152  N  N     . LEU A 1 2703 ? 153.515 201.132 174.496 1.00 10.23  ? 2703 LEU A N     1 
ATOM   9153  C  CA    . LEU A 1 2703 ? 153.730 201.146 175.935 1.00 10.37  ? 2703 LEU A CA    1 
ATOM   9154  C  C     . LEU A 1 2703 ? 153.838 202.575 176.449 1.00 14.32  ? 2703 LEU A C     1 
ATOM   9155  O  O     . LEU A 1 2703 ? 154.446 203.437 175.808 1.00 15.34  ? 2703 LEU A O     1 
ATOM   9156  C  CB    . LEU A 1 2703 ? 154.999 200.373 176.293 1.00 9.99   ? 2703 LEU A CB    1 
ATOM   9157  C  CG    . LEU A 1 2703 ? 155.013 198.873 176.004 1.00 9.20   ? 2703 LEU A CG    1 
ATOM   9158  C  CD1   . LEU A 1 2703 ? 156.149 198.208 176.754 1.00 9.40   ? 2703 LEU A CD1   1 
ATOM   9159  C  CD2   . LEU A 1 2703 ? 153.686 198.249 176.385 1.00 13.23  ? 2703 LEU A CD2   1 
ATOM   9160  N  N     . GLU A 1 2704 ? 153.245 202.824 177.615 1.00 14.55  ? 2704 GLU A N     1 
ATOM   9161  C  CA    . GLU A 1 2704 ? 153.373 204.113 178.280 1.00 16.59  ? 2704 GLU A CA    1 
ATOM   9162  C  C     . GLU A 1 2704 ? 153.675 203.877 179.750 1.00 16.14  ? 2704 GLU A C     1 
ATOM   9163  O  O     . GLU A 1 2704 ? 153.038 203.032 180.386 1.00 23.98  ? 2704 GLU A O     1 
ATOM   9164  C  CB    . GLU A 1 2704 ? 152.101 204.953 178.128 1.00 18.85  ? 2704 GLU A CB    1 
ATOM   9165  C  CG    . GLU A 1 2704 ? 152.212 206.352 178.713 1.00 27.74  ? 2704 GLU A CG    1 
ATOM   9166  C  CD    . GLU A 1 2704 ? 150.869 206.927 179.121 1.00 44.60  ? 2704 GLU A CD    1 
ATOM   9167  O  OE1   . GLU A 1 2704 ? 150.665 207.167 180.330 1.00 41.12  ? 2704 GLU A OE1   1 
ATOM   9168  O  OE2   . GLU A 1 2704 ? 150.017 207.141 178.233 1.00 47.44  ? 2704 GLU A OE2   1 
ATOM   9169  N  N     . ARG A 1 2705 ? 154.650 204.619 180.279 1.00 11.38  ? 2705 ARG A N     1 
ATOM   9170  C  CA    . ARG A 1 2705 ? 155.023 204.555 181.693 1.00 11.66  ? 2705 ARG A CA    1 
ATOM   9171  C  C     . ARG A 1 2705 ? 155.397 203.135 182.114 1.00 13.36  ? 2705 ARG A C     1 
ATOM   9172  O  O     . ARG A 1 2705 ? 155.090 202.696 183.224 1.00 15.80  ? 2705 ARG A O     1 
ATOM   9173  C  CB    . ARG A 1 2705 ? 153.910 205.110 182.584 1.00 13.15  ? 2705 ARG A CB    1 
ATOM   9174  C  CG    . ARG A 1 2705 ? 153.851 206.626 182.627 1.00 10.42  ? 2705 ARG A CG    1 
ATOM   9175  C  CD    . ARG A 1 2705 ? 152.763 207.114 183.568 1.00 11.30  ? 2705 ARG A CD    1 
ATOM   9176  N  NE    . ARG A 1 2705 ? 151.440 206.659 183.160 1.00 18.58  ? 2705 ARG A NE    1 
ATOM   9177  C  CZ    . ARG A 1 2705 ? 150.665 205.863 183.885 1.00 21.60  ? 2705 ARG A CZ    1 
ATOM   9178  N  NH1   . ARG A 1 2705 ? 151.048 205.418 185.070 1.00 17.97  ? 2705 ARG A NH1   1 
ATOM   9179  N  NH2   . ARG A 1 2705 ? 149.476 205.506 183.409 1.00 24.11  ? 2705 ARG A NH2   1 
ATOM   9180  N  N     . ILE A 1 2706 ? 156.069 202.410 181.222 1.00 14.14  ? 2706 ILE A N     1 
ATOM   9181  C  CA    . ILE A 1 2706 ? 156.522 201.050 181.484 1.00 10.71  ? 2706 ILE A CA    1 
ATOM   9182  C  C     . ILE A 1 2706 ? 157.993 200.952 181.107 1.00 13.83  ? 2706 ILE A C     1 
ATOM   9183  O  O     . ILE A 1 2706 ? 158.376 201.313 179.989 1.00 17.62  ? 2706 ILE A O     1 
ATOM   9184  C  CB    . ILE A 1 2706 ? 155.696 200.008 180.705 1.00 10.80  ? 2706 ILE A CB    1 
ATOM   9185  C  CG1   . ILE A 1 2706 ? 154.275 199.923 181.264 1.00 10.84  ? 2706 ILE A CG1   1 
ATOM   9186  C  CG2   . ILE A 1 2706 ? 156.370 198.647 180.755 1.00 9.27   ? 2706 ILE A CG2   1 
ATOM   9187  C  CD1   . ILE A 1 2706 ? 153.317 199.166 180.375 1.00 10.80  ? 2706 ILE A CD1   1 
ATOM   9188  N  N     . GLN A 1 2707 ? 158.812 200.465 182.035 1.00 11.80  ? 2707 GLN A N     1 
ATOM   9189  C  CA    . GLN A 1 2707 ? 160.226 200.235 181.792 1.00 8.32   ? 2707 GLN A CA    1 
ATOM   9190  C  C     . GLN A 1 2707 ? 160.612 198.872 182.346 1.00 8.28   ? 2707 GLN A C     1 
ATOM   9191  O  O     . GLN A 1 2707 ? 159.937 198.318 183.217 1.00 9.11   ? 2707 GLN A O     1 
ATOM   9192  C  CB    . GLN A 1 2707 ? 161.093 201.334 182.416 1.00 8.29   ? 2707 GLN A CB    1 
ATOM   9193  C  CG    . GLN A 1 2707 ? 160.825 201.576 183.886 1.00 10.29  ? 2707 GLN A CG    1 
ATOM   9194  C  CD    . GLN A 1 2707 ? 161.812 202.542 184.499 1.00 11.09  ? 2707 GLN A CD    1 
ATOM   9195  O  OE1   . GLN A 1 2707 ? 161.428 203.585 185.021 1.00 12.98  ? 2707 GLN A OE1   1 
ATOM   9196  N  NE2   . GLN A 1 2707 ? 163.092 202.204 184.432 1.00 13.51  ? 2707 GLN A NE2   1 
ATOM   9197  N  N     . PHE A 1 2708 ? 161.710 198.331 181.828 1.00 7.06   ? 2708 PHE A N     1 
ATOM   9198  C  CA    . PHE A 1 2708 ? 162.143 196.979 182.143 1.00 6.91   ? 2708 PHE A CA    1 
ATOM   9199  C  C     . PHE A 1 2708 ? 163.522 196.991 182.786 1.00 7.76   ? 2708 PHE A C     1 
ATOM   9200  O  O     . PHE A 1 2708 ? 164.413 197.730 182.360 1.00 9.17   ? 2708 PHE A O     1 
ATOM   9201  C  CB    . PHE A 1 2708 ? 162.166 196.099 180.888 1.00 7.58   ? 2708 PHE A CB    1 
ATOM   9202  C  CG    . PHE A 1 2708 ? 160.913 196.181 180.069 1.00 9.47   ? 2708 PHE A CG    1 
ATOM   9203  C  CD1   . PHE A 1 2708 ? 159.834 195.362 180.352 1.00 8.66   ? 2708 PHE A CD1   1 
ATOM   9204  C  CD2   . PHE A 1 2708 ? 160.808 197.081 179.023 1.00 11.03  ? 2708 PHE A CD2   1 
ATOM   9205  C  CE1   . PHE A 1 2708 ? 158.678 195.434 179.605 1.00 12.11  ? 2708 PHE A CE1   1 
ATOM   9206  C  CE2   . PHE A 1 2708 ? 159.654 197.159 178.273 1.00 9.40   ? 2708 PHE A CE2   1 
ATOM   9207  C  CZ    . PHE A 1 2708 ? 158.588 196.334 178.564 1.00 11.61  ? 2708 PHE A CZ    1 
ATOM   9208  N  N     . VAL A 1 2709 ? 163.681 196.170 183.819 1.00 8.53   ? 2709 VAL A N     1 
ATOM   9209  C  CA    . VAL A 1 2709 ? 164.965 195.919 184.458 1.00 6.22   ? 2709 VAL A CA    1 
ATOM   9210  C  C     . VAL A 1 2709 ? 165.173 194.413 184.488 1.00 9.35   ? 2709 VAL A C     1 
ATOM   9211  O  O     . VAL A 1 2709 ? 164.266 193.667 184.870 1.00 7.16   ? 2709 VAL A O     1 
ATOM   9212  C  CB    . VAL A 1 2709 ? 165.029 196.507 185.881 1.00 6.07   ? 2709 VAL A CB    1 
ATOM   9213  C  CG1   . VAL A 1 2709 ? 166.255 195.993 186.614 1.00 7.32   ? 2709 VAL A CG1   1 
ATOM   9214  C  CG2   . VAL A 1 2709 ? 165.044 198.020 185.826 1.00 9.23   ? 2709 VAL A CG2   1 
ATOM   9215  N  N     . GLY A 1 2710 ? 166.351 193.965 184.072 1.00 7.30   ? 2710 GLY A N     1 
ATOM   9216  C  CA    . GLY A 1 2710 ? 166.676 192.554 184.060 1.00 4.94   ? 2710 GLY A CA    1 
ATOM   9217  C  C     . GLY A 1 2710 ? 167.821 192.250 185.005 1.00 5.83   ? 2710 GLY A C     1 
ATOM   9218  O  O     . GLY A 1 2710 ? 168.681 193.093 185.255 1.00 8.59   ? 2710 GLY A O     1 
ATOM   9219  N  N     . ALA A 1 2711 ? 167.813 191.037 185.543 1.00 8.64   ? 2711 ALA A N     1 
ATOM   9220  C  CA    . ALA A 1 2711 ? 168.922 190.522 186.328 1.00 5.68   ? 2711 ALA A CA    1 
ATOM   9221  C  C     . ALA A 1 2711 ? 169.267 189.136 185.813 1.00 9.33   ? 2711 ALA A C     1 
ATOM   9222  O  O     . ALA A 1 2711 ? 168.400 188.411 185.318 1.00 10.75  ? 2711 ALA A O     1 
ATOM   9223  C  CB    . ALA A 1 2711 ? 168.595 190.464 187.822 1.00 4.34   ? 2711 ALA A CB    1 
ATOM   9224  N  N     . CYS A 1 2712 ? 170.543 188.779 185.908 1.00 7.46   ? 2712 CYS A N     1 
ATOM   9225  C  CA    . CYS A 1 2712 ? 170.962 187.480 185.404 1.00 5.64   ? 2712 CYS A CA    1 
ATOM   9226  C  C     . CYS A 1 2712 ? 172.324 187.117 185.969 1.00 6.40   ? 2712 CYS A C     1 
ATOM   9227  O  O     . CYS A 1 2712 ? 173.095 187.978 186.397 1.00 6.55   ? 2712 CYS A O     1 
ATOM   9228  C  CB    . CYS A 1 2712 ? 171.003 187.462 183.874 1.00 5.89   ? 2712 CYS A CB    1 
ATOM   9229  S  SG    . CYS A 1 2712 ? 171.917 188.828 183.145 1.00 11.03  ? 2712 CYS A SG    1 
ATOM   9230  N  N     . ASN A 1 2713 ? 172.597 185.819 185.970 1.00 6.18   ? 2713 ASN A N     1 
ATOM   9231  C  CA    . ASN A 1 2713 ? 173.923 185.300 186.231 1.00 4.65   ? 2713 ASN A CA    1 
ATOM   9232  C  C     . ASN A 1 2713 ? 174.778 185.434 184.975 1.00 6.24   ? 2713 ASN A C     1 
ATOM   9233  O  O     . ASN A 1 2713 ? 174.250 185.632 183.879 1.00 7.87   ? 2713 ASN A O     1 
ATOM   9234  C  CB    . ASN A 1 2713 ? 173.831 183.842 186.672 1.00 8.27   ? 2713 ASN A CB    1 
ATOM   9235  C  CG    . ASN A 1 2713 ? 173.128 183.680 188.005 1.00 6.83   ? 2713 ASN A CG    1 
ATOM   9236  O  OD1   . ASN A 1 2713 ? 172.737 184.659 188.639 1.00 7.15   ? 2713 ASN A OD1   1 
ATOM   9237  N  ND2   . ASN A 1 2713 ? 172.963 182.437 188.438 1.00 5.66   ? 2713 ASN A ND2   1 
ATOM   9238  N  N     . PRO A 1 2714 ? 176.101 185.351 185.106 1.00 9.37   ? 2714 PRO A N     1 
ATOM   9239  C  CA    . PRO A 1 2714 ? 176.969 185.450 183.927 1.00 8.79   ? 2714 PRO A CA    1 
ATOM   9240  C  C     . PRO A 1 2714 ? 176.610 184.400 182.892 1.00 6.32   ? 2714 PRO A C     1 
ATOM   9241  O  O     . PRO A 1 2714 ? 176.255 183.266 183.242 1.00 7.39   ? 2714 PRO A O     1 
ATOM   9242  C  CB    . PRO A 1 2714 ? 178.371 185.210 184.503 1.00 7.55   ? 2714 PRO A CB    1 
ATOM   9243  C  CG    . PRO A 1 2714 ? 178.271 185.684 185.902 1.00 6.96   ? 2714 PRO A CG    1 
ATOM   9244  C  CD    . PRO A 1 2714 ? 176.880 185.344 186.357 1.00 7.03   ? 2714 PRO A CD    1 
ATOM   9245  N  N     . PRO A 1 2715 ? 176.678 184.746 181.603 1.00 8.42   ? 2715 PRO A N     1 
ATOM   9246  C  CA    . PRO A 1 2715 ? 176.260 183.792 180.562 1.00 7.57   ? 2715 PRO A CA    1 
ATOM   9247  C  C     . PRO A 1 2715 ? 177.105 182.534 180.511 1.00 8.62   ? 2715 PRO A C     1 
ATOM   9248  O  O     . PRO A 1 2715 ? 176.663 181.534 179.933 1.00 11.86  ? 2715 PRO A O     1 
ATOM   9249  C  CB    . PRO A 1 2715 ? 176.384 184.607 179.268 1.00 6.41   ? 2715 PRO A CB    1 
ATOM   9250  C  CG    . PRO A 1 2715 ? 177.351 185.691 179.590 1.00 7.00   ? 2715 PRO A CG    1 
ATOM   9251  C  CD    . PRO A 1 2715 ? 177.138 186.023 181.034 1.00 8.24   ? 2715 PRO A CD    1 
ATOM   9252  N  N     . THR A 1 2716 ? 178.307 182.551 181.085 1.00 7.89   ? 2716 THR A N     1 
ATOM   9253  C  CA    . THR A 1 2716 ? 179.136 181.356 181.155 1.00 8.24   ? 2716 THR A CA    1 
ATOM   9254  C  C     . THR A 1 2716 ? 178.651 180.357 182.196 1.00 8.19   ? 2716 THR A C     1 
ATOM   9255  O  O     . THR A 1 2716 ? 179.130 179.219 182.207 1.00 11.47  ? 2716 THR A O     1 
ATOM   9256  C  CB    . THR A 1 2716 ? 180.586 181.743 181.454 1.00 9.59   ? 2716 THR A CB    1 
ATOM   9257  O  OG1   . THR A 1 2716 ? 180.664 182.339 182.754 1.00 12.21  ? 2716 THR A OG1   1 
ATOM   9258  C  CG2   . THR A 1 2716 ? 181.094 182.731 180.418 1.00 6.44   ? 2716 THR A CG2   1 
ATOM   9259  N  N     . ASP A 1 2717 ? 177.724 180.751 183.065 1.00 8.86   ? 2717 ASP A N     1 
ATOM   9260  C  CA    . ASP A 1 2717 ? 177.199 179.840 184.066 1.00 8.64   ? 2717 ASP A CA    1 
ATOM   9261  C  C     . ASP A 1 2717 ? 176.305 178.790 183.407 1.00 8.61   ? 2717 ASP A C     1 
ATOM   9262  O  O     . ASP A 1 2717 ? 175.684 179.054 182.374 1.00 8.45   ? 2717 ASP A O     1 
ATOM   9263  C  CB    . ASP A 1 2717 ? 176.412 180.610 185.122 1.00 9.63   ? 2717 ASP A CB    1 
ATOM   9264  C  CG    . ASP A 1 2717 ? 177.310 181.364 186.079 1.00 13.28  ? 2717 ASP A CG    1 
ATOM   9265  O  OD1   . ASP A 1 2717 ? 178.529 181.432 185.818 1.00 11.13  ? 2717 ASP A OD1   1 
ATOM   9266  O  OD2   . ASP A 1 2717 ? 176.799 181.888 187.090 1.00 15.40  ? 2717 ASP A OD2   1 
ATOM   9267  N  N     . PRO A 1 2718 ? 176.231 177.587 183.979 1.00 11.29  ? 2718 PRO A N     1 
ATOM   9268  C  CA    . PRO A 1 2718 ? 175.414 176.533 183.364 1.00 8.15   ? 2718 PRO A CA    1 
ATOM   9269  C  C     . PRO A 1 2718 ? 173.943 176.917 183.321 1.00 7.10   ? 2718 PRO A C     1 
ATOM   9270  O  O     . PRO A 1 2718 ? 173.398 177.484 184.270 1.00 9.21   ? 2718 PRO A O     1 
ATOM   9271  C  CB    . PRO A 1 2718 ? 175.655 175.320 184.270 1.00 6.55   ? 2718 PRO A CB    1 
ATOM   9272  C  CG    . PRO A 1 2718 ? 176.146 175.887 185.554 1.00 9.54   ? 2718 PRO A CG    1 
ATOM   9273  C  CD    . PRO A 1 2718 ? 176.907 177.122 185.201 1.00 12.46  ? 2718 PRO A CD    1 
ATOM   9274  N  N     . GLY A 1 2719 ? 173.300 176.594 182.202 1.00 7.31   ? 2719 GLY A N     1 
ATOM   9275  C  CA    . GLY A 1 2719 ? 171.907 176.920 181.995 1.00 6.71   ? 2719 GLY A CA    1 
ATOM   9276  C  C     . GLY A 1 2719 ? 171.641 178.328 181.513 1.00 8.41   ? 2719 GLY A C     1 
ATOM   9277  O  O     . GLY A 1 2719 ? 170.478 178.666 181.260 1.00 10.77  ? 2719 GLY A O     1 
ATOM   9278  N  N     . ARG A 1 2720 ? 172.671 179.155 181.371 1.00 8.58   ? 2720 ARG A N     1 
ATOM   9279  C  CA    . ARG A 1 2720 ? 172.523 180.547 180.968 1.00 7.57   ? 2720 ARG A CA    1 
ATOM   9280  C  C     . ARG A 1 2720 ? 173.017 180.714 179.538 1.00 7.18   ? 2720 ARG A C     1 
ATOM   9281  O  O     . ARG A 1 2720 ? 174.076 180.191 179.178 1.00 9.46   ? 2720 ARG A O     1 
ATOM   9282  C  CB    . ARG A 1 2720 ? 173.297 181.476 181.906 1.00 8.06   ? 2720 ARG A CB    1 
ATOM   9283  C  CG    . ARG A 1 2720 ? 173.075 181.205 183.385 1.00 6.84   ? 2720 ARG A CG    1 
ATOM   9284  C  CD    . ARG A 1 2720 ? 171.605 181.275 183.747 1.00 7.92   ? 2720 ARG A CD    1 
ATOM   9285  N  NE    . ARG A 1 2720 ? 171.390 181.249 185.189 1.00 15.83  ? 2720 ARG A NE    1 
ATOM   9286  C  CZ    . ARG A 1 2720 ? 171.391 180.150 185.930 1.00 10.11  ? 2720 ARG A CZ    1 
ATOM   9287  N  NH1   . ARG A 1 2720 ? 171.602 178.957 185.399 1.00 6.79   ? 2720 ARG A NH1   1 
ATOM   9288  N  NH2   . ARG A 1 2720 ? 171.175 180.249 187.238 1.00 7.96   ? 2720 ARG A NH2   1 
ATOM   9289  N  N     . LYS A 1 2721 ? 172.249 181.439 178.730 1.00 6.26   ? 2721 LYS A N     1 
ATOM   9290  C  CA    . LYS A 1 2721 ? 172.600 181.675 177.341 1.00 7.32   ? 2721 LYS A CA    1 
ATOM   9291  C  C     . LYS A 1 2721 ? 173.000 183.129 177.129 1.00 8.67   ? 2721 LYS A C     1 
ATOM   9292  O  O     . LYS A 1 2721 ? 172.444 184.023 177.776 1.00 8.89   ? 2721 LYS A O     1 
ATOM   9293  C  CB    . LYS A 1 2721 ? 171.428 181.334 176.412 1.00 7.73   ? 2721 LYS A CB    1 
ATOM   9294  C  CG    . LYS A 1 2721 ? 171.359 179.875 176.001 1.00 9.82   ? 2721 LYS A CG    1 
ATOM   9295  C  CD    . LYS A 1 2721 ? 170.790 179.009 177.111 1.00 10.81  ? 2721 LYS A CD    1 
ATOM   9296  C  CE    . LYS A 1 2721 ? 169.434 179.511 177.567 1.00 9.72   ? 2721 LYS A CE    1 
ATOM   9297  N  NZ    . LYS A 1 2721 ? 168.871 178.660 178.650 1.00 10.33  ? 2721 LYS A NZ    1 
ATOM   9298  N  N     . PRO A 1 2722 ? 173.962 183.397 176.247 1.00 7.33   ? 2722 PRO A N     1 
ATOM   9299  C  CA    . PRO A 1 2722 ? 174.319 184.790 175.953 1.00 6.43   ? 2722 PRO A CA    1 
ATOM   9300  C  C     . PRO A 1 2722 ? 173.152 185.540 175.330 1.00 8.14   ? 2722 PRO A C     1 
ATOM   9301  O  O     . PRO A 1 2722 ? 172.384 184.989 174.539 1.00 7.45   ? 2722 PRO A O     1 
ATOM   9302  C  CB    . PRO A 1 2722 ? 175.495 184.658 174.979 1.00 4.12   ? 2722 PRO A CB    1 
ATOM   9303  C  CG    . PRO A 1 2722 ? 175.364 183.294 174.402 1.00 6.43   ? 2722 PRO A CG    1 
ATOM   9304  C  CD    . PRO A 1 2722 ? 174.778 182.442 175.481 1.00 6.60   ? 2722 PRO A CD    1 
ATOM   9305  N  N     . LEU A 1 2723 ? 173.025 186.810 175.695 1.00 6.10   ? 2723 LEU A N     1 
ATOM   9306  C  CA    . LEU A 1 2723 ? 171.934 187.633 175.201 1.00 4.48   ? 2723 LEU A CA    1 
ATOM   9307  C  C     . LEU A 1 2723 ? 172.221 188.110 173.783 1.00 5.87   ? 2723 LEU A C     1 
ATOM   9308  O  O     . LEU A 1 2723 ? 173.376 188.243 173.370 1.00 13.18  ? 2723 LEU A O     1 
ATOM   9309  C  CB    . LEU A 1 2723 ? 171.706 188.828 176.125 1.00 5.94   ? 2723 LEU A CB    1 
ATOM   9310  C  CG    . LEU A 1 2723 ? 171.035 188.508 177.463 1.00 6.08   ? 2723 LEU A CG    1 
ATOM   9311  C  CD1   . LEU A 1 2723 ? 171.160 189.673 178.430 1.00 6.24   ? 2723 LEU A CD1   1 
ATOM   9312  C  CD2   . LEU A 1 2723 ? 169.577 188.136 177.254 1.00 5.22   ? 2723 LEU A CD2   1 
ATOM   9313  N  N     . SER A 1 2724 ? 171.149 188.360 173.035 1.00 4.42   ? 2724 SER A N     1 
ATOM   9314  C  CA    . SER A 1 2724 ? 171.284 188.827 171.663 1.00 3.69   ? 2724 SER A CA    1 
ATOM   9315  C  C     . SER A 1 2724 ? 171.930 190.206 171.625 1.00 5.56   ? 2724 SER A C     1 
ATOM   9316  O  O     . SER A 1 2724 ? 171.710 191.047 172.501 1.00 6.33   ? 2724 SER A O     1 
ATOM   9317  C  CB    . SER A 1 2724 ? 169.917 188.868 170.980 1.00 4.53   ? 2724 SER A CB    1 
ATOM   9318  O  OG    . SER A 1 2724 ? 170.012 189.409 169.674 1.00 5.62   ? 2724 SER A OG    1 
ATOM   9319  N  N     . HIS A 1 2725 ? 172.744 190.434 170.592 1.00 5.25   ? 2725 HIS A N     1 
ATOM   9320  C  CA    . HIS A 1 2725 ? 173.410 191.723 170.451 1.00 5.92   ? 2725 HIS A CA    1 
ATOM   9321  C  C     . HIS A 1 2725 ? 172.415 192.837 170.154 1.00 5.69   ? 2725 HIS A C     1 
ATOM   9322  O  O     . HIS A 1 2725 ? 172.625 193.981 170.572 1.00 6.51   ? 2725 HIS A O     1 
ATOM   9323  C  CB    . HIS A 1 2725 ? 174.471 191.648 169.356 1.00 9.01   ? 2725 HIS A CB    1 
ATOM   9324  C  CG    . HIS A 1 2725 ? 175.766 191.053 169.814 1.00 8.69   ? 2725 HIS A CG    1 
ATOM   9325  N  ND1   . HIS A 1 2725 ? 176.862 190.929 168.988 1.00 16.17  ? 2725 HIS A ND1   1 
ATOM   9326  C  CD2   . HIS A 1 2725 ? 176.135 190.535 171.008 1.00 9.06   ? 2725 HIS A CD2   1 
ATOM   9327  C  CE1   . HIS A 1 2725 ? 177.853 190.368 169.657 1.00 13.71  ? 2725 HIS A CE1   1 
ATOM   9328  N  NE2   . HIS A 1 2725 ? 177.438 190.118 170.885 1.00 12.07  ? 2725 HIS A NE2   1 
ATOM   9329  N  N     . ARG A 1 2726 ? 171.336 192.529 169.432 1.00 5.09   ? 2726 ARG A N     1 
ATOM   9330  C  CA    . ARG A 1 2726 ? 170.298 193.521 169.185 1.00 3.76   ? 2726 ARG A CA    1 
ATOM   9331  C  C     . ARG A 1 2726 ? 169.516 193.860 170.445 1.00 5.50   ? 2726 ARG A C     1 
ATOM   9332  O  O     . ARG A 1 2726 ? 168.922 194.941 170.519 1.00 9.90   ? 2726 ARG A O     1 
ATOM   9333  C  CB    . ARG A 1 2726 ? 169.353 193.030 168.088 1.00 3.48   ? 2726 ARG A CB    1 
ATOM   9334  C  CG    . ARG A 1 2726 ? 170.066 192.651 166.800 1.00 3.81   ? 2726 ARG A CG    1 
ATOM   9335  C  CD    . ARG A 1 2726 ? 169.100 192.158 165.744 1.00 4.06   ? 2726 ARG A CD    1 
ATOM   9336  N  NE    . ARG A 1 2726 ? 168.678 193.227 164.848 1.00 4.55   ? 2726 ARG A NE    1 
ATOM   9337  C  CZ    . ARG A 1 2726 ? 167.799 193.078 163.868 1.00 3.83   ? 2726 ARG A CZ    1 
ATOM   9338  N  NH1   . ARG A 1 2726 ? 167.233 191.910 163.618 1.00 4.94   ? 2726 ARG A NH1   1 
ATOM   9339  N  NH2   . ARG A 1 2726 ? 167.481 194.128 163.117 1.00 3.49   ? 2726 ARG A NH2   1 
ATOM   9340  N  N     . PHE A 1 2727 ? 169.497 192.964 171.434 1.00 4.66   ? 2727 PHE A N     1 
ATOM   9341  C  CA    . PHE A 1 2727 ? 168.882 193.286 172.716 1.00 3.65   ? 2727 PHE A CA    1 
ATOM   9342  C  C     . PHE A 1 2727 ? 169.848 194.037 173.622 1.00 5.29   ? 2727 PHE A C     1 
ATOM   9343  O  O     . PHE A 1 2727 ? 169.460 195.012 174.275 1.00 5.04   ? 2727 PHE A O     1 
ATOM   9344  C  CB    . PHE A 1 2727 ? 168.393 192.009 173.401 1.00 4.14   ? 2727 PHE A CB    1 
ATOM   9345  C  CG    . PHE A 1 2727 ? 167.964 192.213 174.826 1.00 5.90   ? 2727 PHE A CG    1 
ATOM   9346  C  CD1   . PHE A 1 2727 ? 166.733 192.774 175.118 1.00 6.43   ? 2727 PHE A CD1   1 
ATOM   9347  C  CD2   . PHE A 1 2727 ? 168.790 191.845 175.874 1.00 4.28   ? 2727 PHE A CD2   1 
ATOM   9348  C  CE1   . PHE A 1 2727 ? 166.337 192.964 176.425 1.00 5.03   ? 2727 PHE A CE1   1 
ATOM   9349  C  CE2   . PHE A 1 2727 ? 168.398 192.034 177.182 1.00 4.62   ? 2727 PHE A CE2   1 
ATOM   9350  C  CZ    . PHE A 1 2727 ? 167.170 192.593 177.458 1.00 3.93   ? 2727 PHE A CZ    1 
ATOM   9351  N  N     . LEU A 1 2728 ? 171.109 193.601 173.670 1.00 6.04   ? 2728 LEU A N     1 
ATOM   9352  C  CA    . LEU A 1 2728 ? 172.098 194.241 174.527 1.00 4.57   ? 2728 LEU A CA    1 
ATOM   9353  C  C     . LEU A 1 2728 ? 172.441 195.651 174.068 1.00 5.81   ? 2728 LEU A C     1 
ATOM   9354  O  O     . LEU A 1 2728 ? 173.049 196.407 174.832 1.00 8.13   ? 2728 LEU A O     1 
ATOM   9355  C  CB    . LEU A 1 2728 ? 173.368 193.391 174.589 1.00 5.74   ? 2728 LEU A CB    1 
ATOM   9356  C  CG    . LEU A 1 2728 ? 173.333 192.186 175.530 1.00 5.37   ? 2728 LEU A CG    1 
ATOM   9357  C  CD1   . LEU A 1 2728 ? 174.676 191.476 175.548 1.00 6.59   ? 2728 LEU A CD1   1 
ATOM   9358  C  CD2   . LEU A 1 2728 ? 172.933 192.610 176.931 1.00 5.37   ? 2728 LEU A CD2   1 
ATOM   9359  N  N     . ARG A 1 2729 ? 172.070 196.017 172.840 1.00 6.50   ? 2729 ARG A N     1 
ATOM   9360  C  CA    . ARG A 1 2729 ? 172.354 197.358 172.345 1.00 5.25   ? 2729 ARG A CA    1 
ATOM   9361  C  C     . ARG A 1 2729 ? 171.629 198.423 173.157 1.00 5.00   ? 2729 ARG A C     1 
ATOM   9362  O  O     . ARG A 1 2729 ? 172.156 199.525 173.348 1.00 6.69   ? 2729 ARG A O     1 
ATOM   9363  C  CB    . ARG A 1 2729 ? 171.975 197.450 170.865 1.00 4.36   ? 2729 ARG A CB    1 
ATOM   9364  C  CG    . ARG A 1 2729 ? 171.671 198.849 170.367 1.00 4.66   ? 2729 ARG A CG    1 
ATOM   9365  C  CD    . ARG A 1 2729 ? 171.343 198.849 168.885 1.00 5.32   ? 2729 ARG A CD    1 
ATOM   9366  N  NE    . ARG A 1 2729 ? 170.924 200.168 168.426 1.00 4.77   ? 2729 ARG A NE    1 
ATOM   9367  C  CZ    . ARG A 1 2729 ? 169.794 200.415 167.780 1.00 4.15   ? 2729 ARG A CZ    1 
ATOM   9368  N  NH1   . ARG A 1 2729 ? 168.950 199.446 167.467 1.00 5.21   ? 2729 ARG A NH1   1 
ATOM   9369  N  NH2   . ARG A 1 2729 ? 169.505 201.666 167.435 1.00 5.27   ? 2729 ARG A NH2   1 
ATOM   9370  N  N     . HIS A 1 2730 ? 170.436 198.112 173.659 1.00 5.60   ? 2730 HIS A N     1 
ATOM   9371  C  CA    . HIS A 1 2730 ? 169.612 199.089 174.354 1.00 4.09   ? 2730 HIS A CA    1 
ATOM   9372  C  C     . HIS A 1 2730 ? 169.685 198.987 175.870 1.00 6.24   ? 2730 HIS A C     1 
ATOM   9373  O  O     . HIS A 1 2730 ? 169.178 199.881 176.555 1.00 9.39   ? 2730 HIS A O     1 
ATOM   9374  C  CB    . HIS A 1 2730 ? 168.151 198.952 173.914 1.00 3.60   ? 2730 HIS A CB    1 
ATOM   9375  C  CG    . HIS A 1 2730 ? 167.972 198.906 172.431 1.00 6.51   ? 2730 HIS A CG    1 
ATOM   9376  N  ND1   . HIS A 1 2730 ? 168.114 197.747 171.700 1.00 6.30   ? 2730 HIS A ND1   1 
ATOM   9377  C  CD2   . HIS A 1 2730 ? 167.673 199.880 171.539 1.00 5.96   ? 2730 HIS A CD2   1 
ATOM   9378  C  CE1   . HIS A 1 2730 ? 167.904 198.007 170.422 1.00 6.23   ? 2730 HIS A CE1   1 
ATOM   9379  N  NE2   . HIS A 1 2730 ? 167.637 199.294 170.298 1.00 7.46   ? 2730 HIS A NE2   1 
ATOM   9380  N  N     . VAL A 1 2731 ? 170.286 197.934 176.413 1.00 6.57   ? 2731 VAL A N     1 
ATOM   9381  C  CA    . VAL A 1 2731 ? 170.333 197.737 177.857 1.00 6.89   ? 2731 VAL A CA    1 
ATOM   9382  C  C     . VAL A 1 2731 ? 171.788 197.857 178.314 1.00 6.62   ? 2731 VAL A C     1 
ATOM   9383  O  O     . VAL A 1 2731 ? 172.632 197.029 177.943 1.00 7.14   ? 2731 VAL A O     1 
ATOM   9384  C  CB    . VAL A 1 2731 ? 169.700 196.399 178.273 1.00 6.31   ? 2731 VAL A CB    1 
ATOM   9385  C  CG1   . VAL A 1 2731 ? 168.234 196.386 177.890 1.00 6.75   ? 2731 VAL A CG1   1 
ATOM   9386  C  CG2   . VAL A 1 2731 ? 170.379 195.219 177.601 1.00 6.17   ? 2731 VAL A CG2   1 
ATOM   9387  N  N     . PRO A 1 2732 ? 172.141 198.899 179.065 1.00 6.45   ? 2732 PRO A N     1 
ATOM   9388  C  CA    . PRO A 1 2732 ? 173.434 198.898 179.755 1.00 5.53   ? 2732 PRO A CA    1 
ATOM   9389  C  C     . PRO A 1 2732 ? 173.505 197.767 180.768 1.00 6.80   ? 2732 PRO A C     1 
ATOM   9390  O  O     . PRO A 1 2732 ? 172.520 197.442 181.434 1.00 8.36   ? 2732 PRO A O     1 
ATOM   9391  C  CB    . PRO A 1 2732 ? 173.476 200.270 180.439 1.00 5.58   ? 2732 PRO A CB    1 
ATOM   9392  C  CG    . PRO A 1 2732 ? 172.075 200.783 180.395 1.00 7.51   ? 2732 PRO A CG    1 
ATOM   9393  C  CD    . PRO A 1 2732 ? 171.474 200.204 179.163 1.00 7.39   ? 2732 PRO A CD    1 
ATOM   9394  N  N     . VAL A 1 2733 ? 174.692 197.182 180.895 1.00 5.54   ? 2733 VAL A N     1 
ATOM   9395  C  CA    . VAL A 1 2733 ? 174.930 196.057 181.790 1.00 4.76   ? 2733 VAL A CA    1 
ATOM   9396  C  C     . VAL A 1 2733 ? 175.868 196.513 182.896 1.00 6.62   ? 2733 VAL A C     1 
ATOM   9397  O  O     . VAL A 1 2733 ? 176.931 197.083 182.624 1.00 7.03   ? 2733 VAL A O     1 
ATOM   9398  C  CB    . VAL A 1 2733 ? 175.515 194.851 181.036 1.00 5.02   ? 2733 VAL A CB    1 
ATOM   9399  C  CG1   . VAL A 1 2733 ? 175.792 193.710 181.998 1.00 5.54   ? 2733 VAL A CG1   1 
ATOM   9400  C  CG2   . VAL A 1 2733 ? 174.567 194.407 179.934 1.00 6.45   ? 2733 VAL A CG2   1 
ATOM   9401  N  N     . VAL A 1 2734 ? 175.472 196.267 184.141 1.00 6.92   ? 2734 VAL A N     1 
ATOM   9402  C  CA    . VAL A 1 2734 ? 176.300 196.554 185.306 1.00 4.90   ? 2734 VAL A CA    1 
ATOM   9403  C  C     . VAL A 1 2734 ? 176.648 195.235 185.982 1.00 4.79   ? 2734 VAL A C     1 
ATOM   9404  O  O     . VAL A 1 2734 ? 175.772 194.391 186.204 1.00 6.36   ? 2734 VAL A O     1 
ATOM   9405  C  CB    . VAL A 1 2734 ? 175.609 197.533 186.277 1.00 5.36   ? 2734 VAL A CB    1 
ATOM   9406  C  CG1   . VAL A 1 2734 ? 174.349 196.931 186.881 1.00 9.61   ? 2734 VAL A CG1   1 
ATOM   9407  C  CG2   . VAL A 1 2734 ? 176.572 197.954 187.374 1.00 5.50   ? 2734 VAL A CG2   1 
ATOM   9408  N  N     . TYR A 1 2735 ? 177.930 195.047 186.277 1.00 7.04   ? 2735 TYR A N     1 
ATOM   9409  C  CA    . TYR A 1 2735 ? 178.417 193.814 186.885 1.00 6.85   ? 2735 TYR A CA    1 
ATOM   9410  C  C     . TYR A 1 2735 ? 178.514 194.009 188.393 1.00 9.41   ? 2735 TYR A C     1 
ATOM   9411  O  O     . TYR A 1 2735 ? 179.355 194.773 188.876 1.00 13.02  ? 2735 TYR A O     1 
ATOM   9412  C  CB    . TYR A 1 2735 ? 179.768 193.414 186.301 1.00 6.27   ? 2735 TYR A CB    1 
ATOM   9413  C  CG    . TYR A 1 2735 ? 180.334 192.150 186.904 1.00 8.91   ? 2735 TYR A CG    1 
ATOM   9414  C  CD1   . TYR A 1 2735 ? 179.658 190.943 186.797 1.00 8.54   ? 2735 TYR A CD1   1 
ATOM   9415  C  CD2   . TYR A 1 2735 ? 181.540 192.165 187.589 1.00 10.69  ? 2735 TYR A CD2   1 
ATOM   9416  C  CE1   . TYR A 1 2735 ? 180.170 189.787 187.350 1.00 10.08  ? 2735 TYR A CE1   1 
ATOM   9417  C  CE2   . TYR A 1 2735 ? 182.060 191.014 188.146 1.00 9.37   ? 2735 TYR A CE2   1 
ATOM   9418  C  CZ    . TYR A 1 2735 ? 181.371 189.828 188.024 1.00 11.47  ? 2735 TYR A CZ    1 
ATOM   9419  O  OH    . TYR A 1 2735 ? 181.886 188.678 188.577 1.00 14.11  ? 2735 TYR A OH    1 
ATOM   9420  N  N     . VAL A 1 2736 ? 177.656 193.318 189.132 1.00 8.15   ? 2736 VAL A N     1 
ATOM   9421  C  CA    . VAL A 1 2736 ? 177.702 193.305 190.588 1.00 8.69   ? 2736 VAL A CA    1 
ATOM   9422  C  C     . VAL A 1 2736 ? 178.414 192.026 191.003 1.00 7.74   ? 2736 VAL A C     1 
ATOM   9423  O  O     . VAL A 1 2736 ? 177.888 190.923 190.822 1.00 9.41   ? 2736 VAL A O     1 
ATOM   9424  C  CB    . VAL A 1 2736 ? 176.299 193.396 191.202 1.00 8.16   ? 2736 VAL A CB    1 
ATOM   9425  C  CG1   . VAL A 1 2736 ? 176.390 193.593 192.704 1.00 6.16   ? 2736 VAL A CG1   1 
ATOM   9426  C  CG2   . VAL A 1 2736 ? 175.517 194.528 190.560 1.00 9.53   ? 2736 VAL A CG2   1 
ATOM   9427  N  N     . ASP A 1 2737 ? 179.613 192.171 191.550 1.00 6.82   ? 2737 ASP A N     1 
ATOM   9428  C  CA    . ASP A 1 2737 ? 180.407 191.035 191.984 1.00 8.55   ? 2737 ASP A CA    1 
ATOM   9429  C  C     . ASP A 1 2737 ? 180.136 190.726 193.453 1.00 8.71   ? 2737 ASP A C     1 
ATOM   9430  O  O     . ASP A 1 2737 ? 179.483 191.488 194.168 1.00 9.73   ? 2737 ASP A O     1 
ATOM   9431  C  CB    . ASP A 1 2737 ? 181.894 191.309 191.757 1.00 11.47  ? 2737 ASP A CB    1 
ATOM   9432  C  CG    . ASP A 1 2737 ? 182.716 190.039 191.668 1.00 12.30  ? 2737 ASP A CG    1 
ATOM   9433  O  OD1   . ASP A 1 2737 ? 182.137 188.943 191.815 1.00 11.06  ? 2737 ASP A OD1   1 
ATOM   9434  O  OD2   . ASP A 1 2737 ? 183.941 190.138 191.450 1.00 12.94  ? 2737 ASP A OD2   1 
ATOM   9435  N  N     . TYR A 1 2738 ? 180.618 189.570 193.913 1.00 10.11  ? 2738 TYR A N     1 
ATOM   9436  C  CA    . TYR A 1 2738 ? 180.434 189.193 195.341 1.00 7.31   ? 2738 TYR A CA    1 
ATOM   9437  C  C     . TYR A 1 2738 ? 181.226 190.162 196.210 1.00 8.42   ? 2738 TYR A C     1 
ATOM   9438  O  O     . TYR A 1 2738 ? 182.366 190.515 195.842 1.00 8.59   ? 2738 TYR A O     1 
ATOM   9439  C  CB    . TYR A 1 2738 ? 180.882 187.752 195.597 1.00 5.04   ? 2738 TYR A CB    1 
ATOM   9440  C  CG    . TYR A 1 2738 ? 179.879 186.664 195.240 1.00 5.92   ? 2738 TYR A CG    1 
ATOM   9441  C  CD1   . TYR A 1 2738 ? 178.511 186.890 195.317 1.00 7.24   ? 2738 TYR A CD1   1 
ATOM   9442  C  CD2   . TYR A 1 2738 ? 180.307 185.405 194.839 1.00 5.46   ? 2738 TYR A CD2   1 
ATOM   9443  C  CE1   . TYR A 1 2738 ? 177.598 185.899 194.998 1.00 6.52   ? 2738 TYR A CE1   1 
ATOM   9444  C  CE2   . TYR A 1 2738 ? 179.405 184.405 194.519 1.00 5.49   ? 2738 TYR A CE2   1 
ATOM   9445  C  CZ    . TYR A 1 2738 ? 178.047 184.653 194.599 1.00 6.51   ? 2738 TYR A CZ    1 
ATOM   9446  O  OH    . TYR A 1 2738 ? 177.164 183.664 194.279 1.00 10.47  ? 2738 TYR A OH    1 
ATOM   9447  N  N     . PRO A 1 2739 ? 180.679 190.621 197.356 1.00 7.06   ? 2739 PRO A N     1 
ATOM   9448  C  CA    . PRO A 1 2739 ? 181.434 191.478 198.258 1.00 7.99   ? 2739 PRO A CA    1 
ATOM   9449  C  C     . PRO A 1 2739 ? 182.737 190.804 198.659 1.00 12.20  ? 2739 PRO A C     1 
ATOM   9450  O  O     . PRO A 1 2739 ? 182.739 189.580 198.900 1.00 15.99  ? 2739 PRO A O     1 
ATOM   9451  C  CB    . PRO A 1 2739 ? 180.482 191.658 199.445 1.00 9.05   ? 2739 PRO A CB    1 
ATOM   9452  C  CG    . PRO A 1 2739 ? 179.110 191.428 198.854 1.00 6.28   ? 2739 PRO A CG    1 
ATOM   9453  C  CD    . PRO A 1 2739 ? 179.322 190.357 197.799 1.00 6.16   ? 2739 PRO A CD    1 
ATOM   9454  N  N     . GLY A 1 2740 ? 183.826 191.575 198.721 1.00 14.65  ? 2740 GLY A N     1 
ATOM   9455  C  CA    . GLY A 1 2740 ? 185.145 191.016 199.075 1.00 13.96  ? 2740 GLY A CA    1 
ATOM   9456  C  C     . GLY A 1 2740 ? 185.297 190.867 200.574 1.00 18.49  ? 2740 GLY A C     1 
ATOM   9457  O  O     . GLY A 1 2740 ? 184.379 191.296 201.304 1.00 19.59  ? 2740 GLY A O     1 
ATOM   9458  N  N     . PRO A 1 2741 ? 186.402 190.280 201.084 1.00 19.20  ? 2741 PRO A N     1 
ATOM   9459  C  CA    . PRO A 1 2741 ? 186.543 190.025 202.528 1.00 15.82  ? 2741 PRO A CA    1 
ATOM   9460  C  C     . PRO A 1 2741 ? 186.409 191.277 203.377 1.00 18.85  ? 2741 PRO A C     1 
ATOM   9461  O  O     . PRO A 1 2741 ? 185.828 191.217 204.466 1.00 18.27  ? 2741 PRO A O     1 
ATOM   9462  C  CB    . PRO A 1 2741 ? 187.944 189.407 202.635 1.00 16.23  ? 2741 PRO A CB    1 
ATOM   9463  C  CG    . PRO A 1 2741 ? 188.210 188.838 201.282 1.00 21.71  ? 2741 PRO A CG    1 
ATOM   9464  C  CD    . PRO A 1 2741 ? 187.548 189.769 200.315 1.00 18.68  ? 2741 PRO A CD    1 
ATOM   9465  N  N     . ALA A 1 2742 ? 186.917 192.416 202.903 1.00 17.03  ? 2742 ALA A N     1 
ATOM   9466  C  CA    . ALA A 1 2742 ? 186.788 193.656 203.663 1.00 15.20  ? 2742 ALA A CA    1 
ATOM   9467  C  C     . ALA A 1 2742 ? 185.342 194.140 203.692 1.00 15.81  ? 2742 ALA A C     1 
ATOM   9468  O  O     . ALA A 1 2742 ? 184.825 194.521 204.749 1.00 16.93  ? 2742 ALA A O     1 
ATOM   9469  C  CB    . ALA A 1 2742 ? 187.705 194.727 203.073 1.00 18.04  ? 2742 ALA A CB    1 
ATOM   9470  N  N     . SER A 1 2743 ? 184.675 194.140 202.536 1.00 17.47  ? 2743 SER A N     1 
ATOM   9471  C  CA    . SER A 1 2743 ? 183.283 194.576 202.485 1.00 15.43  ? 2743 SER A CA    1 
ATOM   9472  C  C     . SER A 1 2743 ? 182.376 193.629 203.261 1.00 17.99  ? 2743 SER A C     1 
ATOM   9473  O  O     . SER A 1 2743 ? 181.476 194.074 203.987 1.00 19.89  ? 2743 SER A O     1 
ATOM   9474  C  CB    . SER A 1 2743 ? 182.826 194.692 201.031 1.00 15.94  ? 2743 SER A CB    1 
ATOM   9475  O  OG    . SER A 1 2743 ? 181.467 195.084 200.953 1.00 32.17  ? 2743 SER A OG    1 
ATOM   9476  N  N     . LEU A 1 2744 ? 182.593 192.319 203.114 1.00 16.65  ? 2744 LEU A N     1 
ATOM   9477  C  CA    . LEU A 1 2744 ? 181.830 191.349 203.892 1.00 14.86  ? 2744 LEU A CA    1 
ATOM   9478  C  C     . LEU A 1 2744 ? 182.067 191.548 205.380 1.00 12.99  ? 2744 LEU A C     1 
ATOM   9479  O  O     . LEU A 1 2744 ? 181.126 191.491 206.182 1.00 16.12  ? 2744 LEU A O     1 
ATOM   9480  C  CB    . LEU A 1 2744 ? 182.213 189.928 203.482 1.00 15.15  ? 2744 LEU A CB    1 
ATOM   9481  C  CG    . LEU A 1 2744 ? 181.666 189.383 202.164 1.00 13.82  ? 2744 LEU A CG    1 
ATOM   9482  C  CD1   . LEU A 1 2744 ? 182.266 188.022 201.884 1.00 10.97  ? 2744 LEU A CD1   1 
ATOM   9483  C  CD2   . LEU A 1 2744 ? 180.152 189.307 202.192 1.00 13.73  ? 2744 LEU A CD2   1 
ATOM   9484  N  N     . THR A 1 2745 ? 183.323 191.785 205.764 1.00 15.03  ? 2745 THR A N     1 
ATOM   9485  C  CA    . THR A 1 2745 ? 183.641 192.030 207.163 1.00 13.02  ? 2745 THR A CA    1 
ATOM   9486  C  C     . THR A 1 2745 ? 182.906 193.255 207.680 1.00 12.50  ? 2745 THR A C     1 
ATOM   9487  O  O     . THR A 1 2745 ? 182.331 193.220 208.766 1.00 18.22  ? 2745 THR A O     1 
ATOM   9488  C  CB    . THR A 1 2745 ? 185.150 192.194 207.339 1.00 11.64  ? 2745 THR A CB    1 
ATOM   9489  O  OG1   . THR A 1 2745 ? 185.816 191.017 206.869 1.00 22.31  ? 2745 THR A OG1   1 
ATOM   9490  C  CG2   . THR A 1 2745 ? 185.494 192.408 208.802 1.00 10.35  ? 2745 THR A CG2   1 
ATOM   9491  N  N     . GLN A 1 2746 ? 182.843 194.304 206.859 1.00 14.36  ? 2746 GLN A N     1 
ATOM   9492  C  CA    . GLN A 1 2746 ? 182.110 195.537 207.248 1.00 18.85  ? 2746 GLN A CA    1 
ATOM   9493  C  C     . GLN A 1 2746 ? 180.603 195.252 207.353 1.00 14.99  ? 2746 GLN A C     1 
ATOM   9494  O  O     . GLN A 1 2746 ? 180.022 195.552 208.419 1.00 16.18  ? 2746 GLN A O     1 
ATOM   9495  C  CB    . GLN A 1 2746 ? 182.367 196.638 206.219 1.00 21.84  ? 2746 GLN A CB    1 
ATOM   9496  C  CG    . GLN A 1 2746 ? 181.652 197.949 206.527 1.00 35.13  ? 2746 GLN A CG    1 
ATOM   9497  C  CD    . GLN A 1 2746 ? 181.769 198.969 205.416 1.00 39.78  ? 2746 GLN A CD    1 
ATOM   9498  O  OE1   . GLN A 1 2746 ? 180.768 199.440 204.865 1.00 27.29  ? 2746 GLN A OE1   1 
ATOM   9499  N  NE2   . GLN A 1 2746 ? 183.000 199.323 205.077 1.00 43.34  ? 2746 GLN A NE2   1 
ATOM   9500  N  N     . ILE A 1 2747 ? 179.999 194.688 206.303 1.00 14.02  ? 2747 ILE A N     1 
ATOM   9501  C  CA    . ILE A 1 2747 ? 178.521 194.455 206.286 1.00 12.95  ? 2747 ILE A CA    1 
ATOM   9502  C  C     . ILE A 1 2747 ? 178.112 193.546 207.454 1.00 12.20  ? 2747 ILE A C     1 
ATOM   9503  O  O     . ILE A 1 2747 ? 177.233 193.959 208.245 1.00 14.38  ? 2747 ILE A O     1 
ATOM   9504  C  CB    . ILE A 1 2747 ? 178.091 193.834 204.945 1.00 10.37  ? 2747 ILE A CB    1 
ATOM   9505  C  CG1   . ILE A 1 2747 ? 178.491 194.710 203.760 1.00 17.27  ? 2747 ILE A CG1   1 
ATOM   9506  C  CG2   . ILE A 1 2747 ? 176.595 193.522 204.940 1.00 10.99  ? 2747 ILE A CG2   1 
ATOM   9507  C  CD1   . ILE A 1 2747 ? 178.442 193.995 202.422 1.00 12.85  ? 2747 ILE A CD1   1 
ATOM   9508  N  N     . TYR A 1 2748 ? 178.730 192.369 207.568 1.00 10.52  ? 2748 TYR A N     1 
ATOM   9509  C  CA    . TYR A 1 2748 ? 178.292 191.396 208.608 1.00 11.50  ? 2748 TYR A CA    1 
ATOM   9510  C  C     . TYR A 1 2748 ? 178.846 191.809 209.969 1.00 13.45  ? 2748 TYR A C     1 
ATOM   9511  O  O     . TYR A 1 2748 ? 178.235 191.443 210.994 1.00 17.55  ? 2748 TYR A O     1 
ATOM   9512  C  CB    . TYR A 1 2748 ? 178.636 189.992 208.100 1.00 13.34  ? 2748 TYR A CB    1 
ATOM   9513  C  CG    . TYR A 1 2748 ? 177.772 189.646 206.896 1.00 11.33  ? 2748 TYR A CG    1 
ATOM   9514  C  CD1   . TYR A 1 2748 ? 176.498 189.117 207.059 1.00 8.78   ? 2748 TYR A CD1   1 
ATOM   9515  C  CD2   . TYR A 1 2748 ? 178.214 189.885 205.601 1.00 9.89   ? 2748 TYR A CD2   1 
ATOM   9516  C  CE1   . TYR A 1 2748 ? 175.696 188.820 205.971 1.00 9.90   ? 2748 TYR A CE1   1 
ATOM   9517  C  CE2   . TYR A 1 2748 ? 177.423 189.588 204.504 1.00 11.57  ? 2748 TYR A CE2   1 
ATOM   9518  C  CZ    . TYR A 1 2748 ? 176.161 189.054 204.690 1.00 11.83  ? 2748 TYR A CZ    1 
ATOM   9519  O  OH    . TYR A 1 2748 ? 175.375 188.759 203.614 1.00 12.97  ? 2748 TYR A OH    1 
ATOM   9520  N  N     . GLY A 1 2749 ? 179.950 192.557 209.991 1.00 10.98  ? 2749 GLY A N     1 
ATOM   9521  C  CA    . GLY A 1 2749 ? 180.448 193.070 211.280 1.00 11.45  ? 2749 GLY A CA    1 
ATOM   9522  C  C     . GLY A 1 2749 ? 179.404 193.981 211.889 1.00 14.27  ? 2749 GLY A C     1 
ATOM   9523  O  O     . GLY A 1 2749 ? 179.186 193.898 213.115 1.00 18.27  ? 2749 GLY A O     1 
ATOM   9524  N  N     . THR A 1 2750 ? 178.765 194.807 211.058 1.00 12.82  ? 2750 THR A N     1 
ATOM   9525  C  CA    . THR A 1 2750 ? 177.719 195.732 211.539 1.00 15.16  ? 2750 THR A CA    1 
ATOM   9526  C  C     . THR A 1 2750 ? 176.546 194.926 212.045 1.00 17.71  ? 2750 THR A C     1 
ATOM   9527  O  O     . THR A 1 2750 ? 176.033 195.249 213.136 1.00 22.30  ? 2750 THR A O     1 
ATOM   9528  C  CB    . THR A 1 2750 ? 177.310 196.660 210.397 1.00 14.58  ? 2750 THR A CB    1 
ATOM   9529  O  OG1   . THR A 1 2750 ? 178.510 197.312 209.995 1.00 15.02  ? 2750 THR A OG1   1 
ATOM   9530  C  CG2   . THR A 1 2750 ? 176.272 197.684 210.821 1.00 21.12  ? 2750 THR A CG2   1 
ATOM   9531  N  N     . PHE A 1 2751 ? 176.131 193.911 211.283 1.00 17.26  ? 2751 PHE A N     1 
ATOM   9532  C  CA    . PHE A 1 2751 ? 174.957 193.082 211.671 1.00 13.85  ? 2751 PHE A CA    1 
ATOM   9533  C  C     . PHE A 1 2751 ? 175.264 192.345 212.972 1.00 15.60  ? 2751 PHE A C     1 
ATOM   9534  O  O     . PHE A 1 2751 ? 174.354 192.191 213.812 1.00 18.50  ? 2751 PHE A O     1 
ATOM   9535  C  CB    . PHE A 1 2751 ? 174.605 192.130 210.525 1.00 16.42  ? 2751 PHE A CB    1 
ATOM   9536  C  CG    . PHE A 1 2751 ? 173.718 192.743 209.450 1.00 14.50  ? 2751 PHE A CG    1 
ATOM   9537  C  CD1   . PHE A 1 2751 ? 172.789 193.726 209.770 1.00 15.36  ? 2751 PHE A CD1   1 
ATOM   9538  C  CD2   . PHE A 1 2751 ? 173.816 192.335 208.125 1.00 15.49  ? 2751 PHE A CD2   1 
ATOM   9539  C  CE1   . PHE A 1 2751 ? 171.981 194.281 208.792 1.00 19.70  ? 2751 PHE A CE1   1 
ATOM   9540  C  CE2   . PHE A 1 2751 ? 173.005 192.896 207.151 1.00 19.92  ? 2751 PHE A CE2   1 
ATOM   9541  C  CZ    . PHE A 1 2751 ? 172.091 193.867 207.486 1.00 19.76  ? 2751 PHE A CZ    1 
ATOM   9542  N  N     . ASN A 1 2752 ? 176.512 191.902 213.139 1.00 13.72  ? 2752 ASN A N     1 
ATOM   9543  C  CA    . ASN A 1 2752 ? 176.889 191.123 214.352 1.00 12.79  ? 2752 ASN A CA    1 
ATOM   9544  C  C     . ASN A 1 2752 ? 176.862 192.049 215.573 1.00 16.25  ? 2752 ASN A C     1 
ATOM   9545  O  O     . ASN A 1 2752 ? 176.312 191.630 216.612 1.00 20.27  ? 2752 ASN A O     1 
ATOM   9546  C  CB    . ASN A 1 2752 ? 178.215 190.394 214.160 1.00 10.09  ? 2752 ASN A CB    1 
ATOM   9547  C  CG    . ASN A 1 2752 ? 178.065 189.175 213.281 1.00 11.41  ? 2752 ASN A CG    1 
ATOM   9548  O  OD1   . ASN A 1 2752 ? 176.963 188.882 212.807 1.00 13.72  ? 2752 ASN A OD1   1 
ATOM   9549  N  ND2   . ASN A 1 2752 ? 179.151 188.452 213.054 1.00 17.24  ? 2752 ASN A ND2   1 
ATOM   9550  N  N     . ARG A 1 2753 ? 177.426 193.254 215.453 1.00 16.92  ? 2753 ARG A N     1 
ATOM   9551  C  CA    . ARG A 1 2753 ? 177.389 194.208 216.556 1.00 17.16  ? 2753 ARG A CA    1 
ATOM   9552  C  C     . ARG A 1 2753 ? 175.953 194.508 216.963 1.00 19.40  ? 2753 ARG A C     1 
ATOM   9553  O  O     . ARG A 1 2753 ? 175.615 194.502 218.155 1.00 22.82  ? 2753 ARG A O     1 
ATOM   9554  C  CB    . ARG A 1 2753 ? 178.120 195.489 216.156 1.00 19.28  ? 2753 ARG A CB    1 
ATOM   9555  C  CG    . ARG A 1 2753 ? 179.625 195.427 216.347 1.00 25.99  ? 2753 ARG A CG    1 
ATOM   9556  C  CD    . ARG A 1 2753 ? 180.243 196.813 216.326 1.00 26.80  ? 2753 ARG A CD    1 
ATOM   9557  N  NE    . ARG A 1 2753 ? 179.539 197.707 215.415 1.00 27.55  ? 2753 ARG A NE    1 
ATOM   9558  C  CZ    . ARG A 1 2753 ? 179.857 197.876 214.139 1.00 26.98  ? 2753 ARG A CZ    1 
ATOM   9559  N  NH1   . ARG A 1 2753 ? 180.862 197.219 213.584 1.00 13.02  ? 2753 ARG A NH1   1 
ATOM   9560  N  NH2   . ARG A 1 2753 ? 179.146 198.723 213.399 1.00 27.83  ? 2753 ARG A NH2   1 
ATOM   9561  N  N     . ALA A 1 2754 ? 175.083 194.744 215.977 1.00 17.10  ? 2754 ALA A N     1 
ATOM   9562  C  CA    . ALA A 1 2754 ? 173.681 194.997 216.292 1.00 19.65  ? 2754 ALA A CA    1 
ATOM   9563  C  C     . ALA A 1 2754 ? 173.042 193.789 216.967 1.00 27.59  ? 2754 ALA A C     1 
ATOM   9564  O  O     . ALA A 1 2754 ? 172.225 193.938 217.884 1.00 31.61  ? 2754 ALA A O     1 
ATOM   9565  C  CB    . ALA A 1 2754 ? 172.919 195.375 215.023 1.00 21.92  ? 2754 ALA A CB    1 
ATOM   9566  N  N     . MET A 1 2755 ? 173.404 192.583 216.526 1.00 24.17  ? 2755 MET A N     1 
ATOM   9567  C  CA    . MET A 1 2755 ? 172.865 191.364 217.122 1.00 18.45  ? 2755 MET A CA    1 
ATOM   9568  C  C     . MET A 1 2755 ? 173.360 191.173 218.551 1.00 24.32  ? 2755 MET A C     1 
ATOM   9569  O  O     . MET A 1 2755 ? 172.570 190.907 219.463 1.00 32.67  ? 2755 MET A O     1 
ATOM   9570  C  CB    . MET A 1 2755 ? 173.248 190.166 216.256 1.00 20.76  ? 2755 MET A CB    1 
ATOM   9571  C  CG    . MET A 1 2755 ? 172.713 188.833 216.727 1.00 18.82  ? 2755 MET A CG    1 
ATOM   9572  S  SD    . MET A 1 2755 ? 173.220 187.522 215.601 1.00 33.08  ? 2755 MET A SD    1 
ATOM   9573  C  CE    . MET A 1 2755 ? 174.965 187.419 215.986 1.00 21.82  ? 2755 MET A CE    1 
ATOM   9574  N  N     . LEU A 1 2756 ? 174.669 191.305 218.765 1.00 23.56  ? 2756 LEU A N     1 
ATOM   9575  C  CA    . LEU A 1 2756 ? 175.269 191.059 220.067 1.00 24.38  ? 2756 LEU A CA    1 
ATOM   9576  C  C     . LEU A 1 2756 ? 175.005 192.183 221.055 1.00 32.60  ? 2756 LEU A C     1 
ATOM   9577  O  O     . LEU A 1 2756 ? 175.322 192.029 222.238 1.00 37.26  ? 2756 LEU A O     1 
ATOM   9578  C  CB    . LEU A 1 2756 ? 176.774 190.839 219.913 1.00 23.34  ? 2756 LEU A CB    1 
ATOM   9579  C  CG    . LEU A 1 2756 ? 177.178 189.487 219.320 1.00 26.68  ? 2756 LEU A CG    1 
ATOM   9580  C  CD1   . LEU A 1 2756 ? 178.642 189.192 219.589 1.00 29.60  ? 2756 LEU A CD1   1 
ATOM   9581  C  CD2   . LEU A 1 2756 ? 176.298 188.370 219.857 1.00 26.30  ? 2756 LEU A CD2   1 
ATOM   9582  N  N     . ARG A 1 2757 ? 174.446 193.307 220.601 1.00 37.69  ? 2757 ARG A N     1 
ATOM   9583  C  CA    . ARG A 1 2757 ? 173.955 194.303 221.546 1.00 33.48  ? 2757 ARG A CA    1 
ATOM   9584  C  C     . ARG A 1 2757 ? 172.849 193.749 222.437 1.00 35.66  ? 2757 ARG A C     1 
ATOM   9585  O  O     . ARG A 1 2757 ? 172.573 194.327 223.493 1.00 42.44  ? 2757 ARG A O     1 
ATOM   9586  C  CB    . ARG A 1 2757 ? 173.459 195.537 220.793 1.00 30.31  ? 2757 ARG A CB    1 
ATOM   9587  C  CG    . ARG A 1 2757 ? 174.537 196.578 220.544 1.00 29.40  ? 2757 ARG A CG    1 
ATOM   9588  C  CD    . ARG A 1 2757 ? 173.934 197.943 220.280 1.00 32.13  ? 2757 ARG A CD    1 
ATOM   9589  N  NE    . ARG A 1 2757 ? 172.960 197.902 219.197 1.00 36.93  ? 2757 ARG A NE    1 
ATOM   9590  C  CZ    . ARG A 1 2757 ? 173.148 198.441 218.000 1.00 37.21  ? 2757 ARG A CZ    1 
ATOM   9591  N  NH1   . ARG A 1 2757 ? 174.274 199.064 217.693 1.00 35.10  ? 2757 ARG A NH1   1 
ATOM   9592  N  NH2   . ARG A 1 2757 ? 172.185 198.349 217.088 1.00 36.31  ? 2757 ARG A NH2   1 
ATOM   9593  N  N     . LEU A 1 2758 ? 172.210 192.647 222.032 1.00 37.18  ? 2758 LEU A N     1 
ATOM   9594  C  CA    . LEU A 1 2758 ? 171.200 192.012 222.875 1.00 43.49  ? 2758 LEU A CA    1 
ATOM   9595  C  C     . LEU A 1 2758 ? 171.800 191.536 224.193 1.00 42.65  ? 2758 LEU A C     1 
ATOM   9596  O  O     . LEU A 1 2758 ? 171.209 191.724 225.262 1.00 49.62  ? 2758 LEU A O     1 
ATOM   9597  C  CB    . LEU A 1 2758 ? 170.559 190.839 222.133 1.00 41.40  ? 2758 LEU A CB    1 
ATOM   9598  C  CG    . LEU A 1 2758 ? 169.473 191.153 221.106 1.00 38.28  ? 2758 LEU A CG    1 
ATOM   9599  C  CD1   . LEU A 1 2758 ? 169.242 189.956 220.201 1.00 35.68  ? 2758 LEU A CD1   1 
ATOM   9600  C  CD2   . LEU A 1 2758 ? 168.184 191.558 221.801 1.00 39.03  ? 2758 LEU A CD2   1 
ATOM   9601  N  N     . ILE A 1 2759 ? 172.970 190.909 224.133 1.00 38.72  ? 2759 ILE A N     1 
ATOM   9602  C  CA    . ILE A 1 2759 ? 173.642 190.397 225.325 1.00 41.60  ? 2759 ILE A CA    1 
ATOM   9603  C  C     . ILE A 1 2759 ? 174.905 191.216 225.561 1.00 45.02  ? 2759 ILE A C     1 
ATOM   9604  O  O     . ILE A 1 2759 ? 175.905 191.026 224.854 1.00 47.05  ? 2759 ILE A O     1 
ATOM   9605  C  CB    . ILE A 1 2759 ? 173.964 188.902 225.183 1.00 42.23  ? 2759 ILE A CB    1 
ATOM   9606  C  CG1   . ILE A 1 2759 ? 172.749 188.147 224.642 1.00 38.65  ? 2759 ILE A CG1   1 
ATOM   9607  C  CG2   . ILE A 1 2759 ? 174.403 188.323 226.518 1.00 45.39  ? 2759 ILE A CG2   1 
ATOM   9608  C  CD1   . ILE A 1 2759 ? 172.915 186.646 224.629 1.00 32.42  ? 2759 ILE A CD1   1 
ATOM   9609  N  N     . PRO A 1 2760 ? 174.903 192.136 226.530 1.00 47.39  ? 2760 PRO A N     1 
ATOM   9610  C  CA    . PRO A 1 2760 ? 176.092 192.985 226.734 1.00 49.43  ? 2760 PRO A CA    1 
ATOM   9611  C  C     . PRO A 1 2760 ? 177.358 192.200 227.028 1.00 47.48  ? 2760 PRO A C     1 
ATOM   9612  O  O     . PRO A 1 2760 ? 178.440 192.583 226.564 1.00 45.58  ? 2760 PRO A O     1 
ATOM   9613  C  CB    . PRO A 1 2760 ? 175.696 193.878 227.919 1.00 48.53  ? 2760 PRO A CB    1 
ATOM   9614  C  CG    . PRO A 1 2760 ? 174.222 193.769 228.049 1.00 54.95  ? 2760 PRO A CG    1 
ATOM   9615  C  CD    . PRO A 1 2760 ? 173.772 192.505 227.397 1.00 46.59  ? 2760 PRO A CD    1 
ATOM   9616  N  N     . SER A 1 2761 ? 177.252 191.099 227.777 1.00 41.54  ? 2761 SER A N     1 
ATOM   9617  C  CA    . SER A 1 2761 ? 178.431 190.322 228.137 1.00 36.95  ? 2761 SER A CA    1 
ATOM   9618  C  C     . SER A 1 2761 ? 179.127 189.722 226.922 1.00 40.67  ? 2761 SER A C     1 
ATOM   9619  O  O     . SER A 1 2761 ? 180.312 189.384 227.005 1.00 37.96  ? 2761 SER A O     1 
ATOM   9620  C  CB    . SER A 1 2761 ? 178.047 189.214 229.118 1.00 45.78  ? 2761 SER A CB    1 
ATOM   9621  O  OG    . SER A 1 2761 ? 177.195 188.263 228.503 1.00 49.34  ? 2761 SER A OG    1 
ATOM   9622  N  N     . LEU A 1 2762 ? 178.420 189.576 225.804 1.00 41.67  ? 2762 LEU A N     1 
ATOM   9623  C  CA    . LEU A 1 2762 ? 179.001 189.073 224.568 1.00 35.48  ? 2762 LEU A CA    1 
ATOM   9624  C  C     . LEU A 1 2762 ? 179.392 190.182 223.602 1.00 38.41  ? 2762 LEU A C     1 
ATOM   9625  O  O     . LEU A 1 2762 ? 179.858 189.884 222.498 1.00 38.56  ? 2762 LEU A O     1 
ATOM   9626  C  CB    . LEU A 1 2762 ? 178.025 188.115 223.879 1.00 36.95  ? 2762 LEU A CB    1 
ATOM   9627  C  CG    . LEU A 1 2762 ? 177.832 186.743 224.526 1.00 37.75  ? 2762 LEU A CG    1 
ATOM   9628  C  CD1   . LEU A 1 2762 ? 176.791 185.939 223.766 1.00 25.57  ? 2762 LEU A CD1   1 
ATOM   9629  C  CD2   . LEU A 1 2762 ? 179.152 185.996 224.586 1.00 32.98  ? 2762 LEU A CD2   1 
ATOM   9630  N  N     . ARG A 1 2763 ? 179.228 191.450 223.995 1.00 41.48  ? 2763 ARG A N     1 
ATOM   9631  C  CA    . ARG A 1 2763 ? 179.431 192.554 223.061 1.00 38.68  ? 2763 ARG A CA    1 
ATOM   9632  C  C     . ARG A 1 2763 ? 180.853 192.595 222.520 1.00 37.58  ? 2763 ARG A C     1 
ATOM   9633  O  O     . ARG A 1 2763 ? 181.080 193.092 221.411 1.00 43.26  ? 2763 ARG A O     1 
ATOM   9634  C  CB    . ARG A 1 2763 ? 179.089 193.881 223.735 1.00 38.81  ? 2763 ARG A CB    1 
ATOM   9635  C  CG    . ARG A 1 2763 ? 177.780 194.495 223.275 1.00 40.12  ? 2763 ARG A CG    1 
ATOM   9636  C  CD    . ARG A 1 2763 ? 177.772 195.996 223.510 1.00 56.88  ? 2763 ARG A CD    1 
ATOM   9637  N  NE    . ARG A 1 2763 ? 177.511 196.330 224.905 1.00 62.41  ? 2763 ARG A NE    1 
ATOM   9638  C  CZ    . ARG A 1 2763 ? 176.332 196.710 225.377 1.00 60.10  ? 2763 ARG A CZ    1 
ATOM   9639  N  NH1   . ARG A 1 2763 ? 175.273 196.813 224.590 1.00 55.84  ? 2763 ARG A NH1   1 
ATOM   9640  N  NH2   . ARG A 1 2763 ? 176.211 196.993 226.670 1.00 56.61  ? 2763 ARG A NH2   1 
ATOM   9641  N  N     . THR A 1 2764 ? 181.820 192.079 223.276 1.00 38.24  ? 2764 THR A N     1 
ATOM   9642  C  CA    . THR A 1 2764 ? 183.210 192.104 222.843 1.00 34.42  ? 2764 THR A CA    1 
ATOM   9643  C  C     . THR A 1 2764 ? 183.549 190.997 221.856 1.00 29.76  ? 2764 THR A C     1 
ATOM   9644  O  O     . THR A 1 2764 ? 184.674 190.971 221.346 1.00 31.93  ? 2764 THR A O     1 
ATOM   9645  C  CB    . THR A 1 2764 ? 184.143 192.007 224.053 1.00 34.32  ? 2764 THR A CB    1 
ATOM   9646  O  OG1   . THR A 1 2764 ? 185.497 192.205 223.631 1.00 40.24  ? 2764 THR A OG1   1 
ATOM   9647  C  CG2   . THR A 1 2764 ? 184.019 190.644 224.710 1.00 27.82  ? 2764 THR A CG2   1 
ATOM   9648  N  N     . TYR A 1 2765 ? 182.619 190.086 221.574 1.00 29.38  ? 2765 TYR A N     1 
ATOM   9649  C  CA    . TYR A 1 2765 ? 182.875 188.978 220.665 1.00 25.14  ? 2765 TYR A CA    1 
ATOM   9650  C  C     . TYR A 1 2765 ? 182.347 189.228 219.259 1.00 27.31  ? 2765 TYR A C     1 
ATOM   9651  O  O     . TYR A 1 2765 ? 182.375 188.314 218.430 1.00 27.12  ? 2765 TYR A O     1 
ATOM   9652  C  CB    . TYR A 1 2765 ? 182.278 187.684 221.221 1.00 24.73  ? 2765 TYR A CB    1 
ATOM   9653  C  CG    . TYR A 1 2765 ? 182.943 187.201 222.487 1.00 23.82  ? 2765 TYR A CG    1 
ATOM   9654  C  CD1   . TYR A 1 2765 ? 184.047 186.364 222.435 1.00 22.24  ? 2765 TYR A CD1   1 
ATOM   9655  C  CD2   . TYR A 1 2765 ? 182.459 187.571 223.733 1.00 27.39  ? 2765 TYR A CD2   1 
ATOM   9656  C  CE1   . TYR A 1 2765 ? 184.657 185.918 223.587 1.00 20.43  ? 2765 TYR A CE1   1 
ATOM   9657  C  CE2   . TYR A 1 2765 ? 183.062 187.128 224.891 1.00 26.91  ? 2765 TYR A CE2   1 
ATOM   9658  C  CZ    . TYR A 1 2765 ? 184.160 186.301 224.812 1.00 21.26  ? 2765 TYR A CZ    1 
ATOM   9659  O  OH    . TYR A 1 2765 ? 184.767 185.855 225.963 1.00 31.76  ? 2765 TYR A OH    1 
ATOM   9660  N  N     . ALA A 1 2766 ? 181.861 190.437 218.971 1.00 28.15  ? 2766 ALA A N     1 
ATOM   9661  C  CA    . ALA A 1 2766 ? 181.353 190.727 217.634 1.00 20.20  ? 2766 ALA A CA    1 
ATOM   9662  C  C     . ALA A 1 2766 ? 182.463 190.672 216.591 1.00 22.22  ? 2766 ALA A C     1 
ATOM   9663  O  O     . ALA A 1 2766 ? 182.280 190.095 215.513 1.00 21.90  ? 2766 ALA A O     1 
ATOM   9664  C  CB    . ALA A 1 2766 ? 180.670 192.092 217.618 1.00 24.86  ? 2766 ALA A CB    1 
ATOM   9665  N  N     . GLU A 1 2767 ? 183.616 191.269 216.890 1.00 24.00  ? 2767 GLU A N     1 
ATOM   9666  C  CA    . GLU A 1 2767 ? 184.714 191.280 215.925 1.00 25.27  ? 2767 GLU A CA    1 
ATOM   9667  C  C     . GLU A 1 2767 ? 185.257 189.888 215.620 1.00 23.10  ? 2767 GLU A C     1 
ATOM   9668  O  O     . GLU A 1 2767 ? 185.441 189.574 214.431 1.00 18.66  ? 2767 GLU A O     1 
ATOM   9669  C  CB    . GLU A 1 2767 ? 185.819 192.223 216.413 1.00 24.35  ? 2767 GLU A CB    1 
ATOM   9670  C  CG    . GLU A 1 2767 ? 186.974 192.369 215.440 1.00 38.64  ? 2767 GLU A CG    1 
ATOM   9671  C  CD    . GLU A 1 2767 ? 188.028 193.345 215.923 1.00 64.96  ? 2767 GLU A CD    1 
ATOM   9672  O  OE1   . GLU A 1 2767 ? 187.866 193.896 217.032 1.00 65.70  ? 2767 GLU A OE1   1 
ATOM   9673  O  OE2   . GLU A 1 2767 ? 189.018 193.560 215.194 1.00 79.25  ? 2767 GLU A OE2   1 
ATOM   9674  N  N     . PRO A 1 2768 ? 185.541 189.019 216.599 1.00 23.23  ? 2768 PRO A N     1 
ATOM   9675  C  CA    . PRO A 1 2768 ? 186.028 187.679 216.229 1.00 22.30  ? 2768 PRO A CA    1 
ATOM   9676  C  C     . PRO A 1 2768 ? 184.969 186.822 215.560 1.00 16.90  ? 2768 PRO A C     1 
ATOM   9677  O  O     . PRO A 1 2768 ? 185.267 186.156 214.560 1.00 17.03  ? 2768 PRO A O     1 
ATOM   9678  C  CB    . PRO A 1 2768 ? 186.482 187.087 217.570 1.00 23.05  ? 2768 PRO A CB    1 
ATOM   9679  C  CG    . PRO A 1 2768 ? 185.699 187.821 218.588 1.00 21.83  ? 2768 PRO A CG    1 
ATOM   9680  C  CD    . PRO A 1 2768 ? 185.556 189.212 218.061 1.00 20.23  ? 2768 PRO A CD    1 
ATOM   9681  N  N     . LEU A 1 2769 ? 183.737 186.831 216.078 1.00 14.62  ? 2769 LEU A N     1 
ATOM   9682  C  CA    . LEU A 1 2769 ? 182.671 186.014 215.504 1.00 15.93  ? 2769 LEU A CA    1 
ATOM   9683  C  C     . LEU A 1 2769 ? 182.490 186.311 214.022 1.00 14.79  ? 2769 LEU A C     1 
ATOM   9684  O  O     . LEU A 1 2769 ? 182.463 185.396 213.190 1.00 15.61  ? 2769 LEU A O     1 
ATOM   9685  C  CB    . LEU A 1 2769 ? 181.366 186.254 216.264 1.00 15.93  ? 2769 LEU A CB    1 
ATOM   9686  C  CG    . LEU A 1 2769 ? 180.121 185.510 215.778 1.00 15.33  ? 2769 LEU A CG    1 
ATOM   9687  C  CD1   . LEU A 1 2769 ? 180.108 184.089 216.313 1.00 15.92  ? 2769 LEU A CD1   1 
ATOM   9688  C  CD2   . LEU A 1 2769 ? 178.859 186.251 216.187 1.00 9.91   ? 2769 LEU A CD2   1 
ATOM   9689  N  N     . THR A 1 2770 ? 182.394 187.597 213.674 1.00 13.72  ? 2770 THR A N     1 
ATOM   9690  C  CA    . THR A 1 2770 ? 182.304 187.991 212.272 1.00 11.25  ? 2770 THR A CA    1 
ATOM   9691  C  C     . THR A 1 2770 ? 183.447 187.392 211.467 1.00 9.76   ? 2770 THR A C     1 
ATOM   9692  O  O     . THR A 1 2770 ? 183.237 186.839 210.381 1.00 10.77  ? 2770 THR A O     1 
ATOM   9693  C  CB    . THR A 1 2770 ? 182.310 189.516 212.154 1.00 11.75  ? 2770 THR A CB    1 
ATOM   9694  O  OG1   . THR A 1 2770 ? 181.221 190.061 212.909 1.00 11.31  ? 2770 THR A OG1   1 
ATOM   9695  C  CG2   . THR A 1 2770 ? 182.177 189.938 210.702 1.00 10.97  ? 2770 THR A CG2   1 
ATOM   9696  N  N     . ALA A 1 2771 ? 184.668 187.467 212.003 1.00 10.56  ? 2771 ALA A N     1 
ATOM   9697  C  CA    . ALA A 1 2771 ? 185.808 186.866 211.323 1.00 10.58  ? 2771 ALA A CA    1 
ATOM   9698  C  C     . ALA A 1 2771 ? 185.590 185.372 211.133 1.00 11.61  ? 2771 ALA A C     1 
ATOM   9699  O  O     . ALA A 1 2771 ? 185.781 184.838 210.034 1.00 12.19  ? 2771 ALA A O     1 
ATOM   9700  C  CB    . ALA A 1 2771 ? 187.091 187.136 212.107 1.00 10.43  ? 2771 ALA A CB    1 
ATOM   9701  N  N     . ALA A 1 2772 ? 185.143 184.687 212.191 1.00 14.16  ? 2772 ALA A N     1 
ATOM   9702  C  CA    . ALA A 1 2772 ? 184.820 183.272 212.063 1.00 12.77  ? 2772 ALA A CA    1 
ATOM   9703  C  C     . ALA A 1 2772 ? 183.714 183.057 211.045 1.00 13.28  ? 2772 ALA A C     1 
ATOM   9704  O  O     . ALA A 1 2772 ? 183.707 182.044 210.335 1.00 16.08  ? 2772 ALA A O     1 
ATOM   9705  C  CB    . ALA A 1 2772 ? 184.418 182.699 213.421 1.00 11.50  ? 2772 ALA A CB    1 
ATOM   9706  N  N     . MET A 1 2773 ? 182.774 183.999 210.957 1.00 13.57  ? 2773 MET A N     1 
ATOM   9707  C  CA    . MET A 1 2773 ? 181.771 183.951 209.903 1.00 9.06   ? 2773 MET A CA    1 
ATOM   9708  C  C     . MET A 1 2773 ? 182.412 184.113 208.531 1.00 12.37  ? 2773 MET A C     1 
ATOM   9709  O  O     . MET A 1 2773 ? 182.078 183.383 207.592 1.00 14.16  ? 2773 MET A O     1 
ATOM   9710  C  CB    . MET A 1 2773 ? 180.730 185.044 210.131 1.00 9.66   ? 2773 MET A CB    1 
ATOM   9711  C  CG    . MET A 1 2773 ? 179.647 184.703 211.134 1.00 9.92   ? 2773 MET A CG    1 
ATOM   9712  S  SD    . MET A 1 2773 ? 178.086 185.474 210.676 1.00 30.03  ? 2773 MET A SD    1 
ATOM   9713  C  CE    . MET A 1 2773 ? 176.970 184.698 211.832 1.00 12.86  ? 2773 MET A CE    1 
ATOM   9714  N  N     . VAL A 1 2774 ? 183.340 185.065 208.400 1.00 14.43  ? 2774 VAL A N     1 
ATOM   9715  C  CA    . VAL A 1 2774 ? 183.864 185.410 207.084 1.00 12.38  ? 2774 VAL A CA    1 
ATOM   9716  C  C     . VAL A 1 2774 ? 184.790 184.319 206.566 1.00 14.47  ? 2774 VAL A C     1 
ATOM   9717  O  O     . VAL A 1 2774 ? 184.714 183.927 205.395 1.00 19.99  ? 2774 VAL A O     1 
ATOM   9718  C  CB    . VAL A 1 2774 ? 184.567 186.779 207.135 1.00 12.59  ? 2774 VAL A CB    1 
ATOM   9719  C  CG1   . VAL A 1 2774 ? 185.434 186.983 205.901 1.00 13.35  ? 2774 VAL A CG1   1 
ATOM   9720  C  CG2   . VAL A 1 2774 ? 183.542 187.893 207.257 1.00 13.18  ? 2774 VAL A CG2   1 
ATOM   9721  N  N     . GLU A 1 2775 ? 185.675 183.808 207.423 1.00 14.23  ? 2775 GLU A N     1 
ATOM   9722  C  CA    . GLU A 1 2775 ? 186.670 182.842 206.970 1.00 15.00  ? 2775 GLU A CA    1 
ATOM   9723  C  C     . GLU A 1 2775 ? 186.015 181.554 206.490 1.00 16.07  ? 2775 GLU A C     1 
ATOM   9724  O  O     . GLU A 1 2775 ? 186.242 181.115 205.356 1.00 20.25  ? 2775 GLU A O     1 
ATOM   9725  C  CB    . GLU A 1 2775 ? 187.665 182.551 208.093 1.00 19.28  ? 2775 GLU A CB    1 
ATOM   9726  C  CG    . GLU A 1 2775 ? 188.470 181.280 207.885 1.00 22.44  ? 2775 GLU A CG    1 
ATOM   9727  C  CD    . GLU A 1 2775 ? 189.664 181.189 208.809 1.00 33.41  ? 2775 GLU A CD    1 
ATOM   9728  O  OE1   . GLU A 1 2775 ? 189.511 181.488 210.011 1.00 33.26  ? 2775 GLU A OE1   1 
ATOM   9729  O  OE2   . GLU A 1 2775 ? 190.756 180.817 208.333 1.00 44.86  ? 2775 GLU A OE2   1 
ATOM   9730  N  N     . PHE A 1 2776 ? 185.166 180.954 207.329 1.00 14.04  ? 2776 PHE A N     1 
ATOM   9731  C  CA    . PHE A 1 2776 ? 184.576 179.665 206.984 1.00 13.06  ? 2776 PHE A CA    1 
ATOM   9732  C  C     . PHE A 1 2776 ? 183.758 179.766 205.704 1.00 14.25  ? 2776 PHE A C     1 
ATOM   9733  O  O     . PHE A 1 2776 ? 183.905 178.943 204.793 1.00 17.56  ? 2776 PHE A O     1 
ATOM   9734  C  CB    . PHE A 1 2776 ? 183.710 179.151 208.134 1.00 13.41  ? 2776 PHE A CB    1 
ATOM   9735  C  CG    . PHE A 1 2776 ? 183.025 177.852 207.831 1.00 14.90  ? 2776 PHE A CG    1 
ATOM   9736  C  CD1   . PHE A 1 2776 ? 183.763 176.720 207.534 1.00 18.81  ? 2776 PHE A CD1   1 
ATOM   9737  C  CD2   . PHE A 1 2776 ? 181.645 177.767 207.816 1.00 16.09  ? 2776 PHE A CD2   1 
ATOM   9738  C  CE1   . PHE A 1 2776 ? 183.139 175.526 207.244 1.00 21.16  ? 2776 PHE A CE1   1 
ATOM   9739  C  CE2   . PHE A 1 2776 ? 181.016 176.575 207.525 1.00 12.76  ? 2776 PHE A CE2   1 
ATOM   9740  C  CZ    . PHE A 1 2776 ? 181.763 175.455 207.237 1.00 13.04  ? 2776 PHE A CZ    1 
ATOM   9741  N  N     . TYR A 1 2777 ? 182.914 180.798 205.607 1.00 14.24  ? 2777 TYR A N     1 
ATOM   9742  C  CA    . TYR A 1 2777 ? 182.138 181.017 204.393 1.00 13.11  ? 2777 TYR A CA    1 
ATOM   9743  C  C     . TYR A 1 2777 ? 183.044 181.095 203.176 1.00 14.19  ? 2777 TYR A C     1 
ATOM   9744  O  O     . TYR A 1 2777 ? 182.706 180.582 202.103 1.00 18.22  ? 2777 TYR A O     1 
ATOM   9745  C  CB    . TYR A 1 2777 ? 181.313 182.299 204.516 1.00 11.41  ? 2777 TYR A CB    1 
ATOM   9746  C  CG    . TYR A 1 2777 ? 180.988 182.938 203.185 1.00 13.10  ? 2777 TYR A CG    1 
ATOM   9747  C  CD1   . TYR A 1 2777 ? 179.982 182.427 202.377 1.00 12.37  ? 2777 TYR A CD1   1 
ATOM   9748  C  CD2   . TYR A 1 2777 ? 181.700 184.038 202.725 1.00 14.01  ? 2777 TYR A CD2   1 
ATOM   9749  C  CE1   . TYR A 1 2777 ? 179.683 183.002 201.160 1.00 10.09  ? 2777 TYR A CE1   1 
ATOM   9750  C  CE2   . TYR A 1 2777 ? 181.408 184.618 201.507 1.00 10.00  ? 2777 TYR A CE2   1 
ATOM   9751  C  CZ    . TYR A 1 2777 ? 180.399 184.096 200.730 1.00 9.99   ? 2777 TYR A CZ    1 
ATOM   9752  O  OH    . TYR A 1 2777 ? 180.106 184.671 199.515 1.00 11.88  ? 2777 TYR A OH    1 
ATOM   9753  N  N     . THR A 1 2778 ? 184.204 181.739 203.323 1.00 12.76  ? 2778 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2778 ? 185.163 181.772 202.227 1.00 13.35  ? 2778 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2778 ? 185.648 180.368 201.900 1.00 16.90  ? 2778 THR A C     1 
ATOM   9756  O  O     . THR A 1 2778 ? 185.589 179.930 200.744 1.00 21.31  ? 2778 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2778 ? 186.339 182.680 202.585 1.00 18.17  ? 2778 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2778 ? 185.847 183.961 202.997 1.00 17.40  ? 2778 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2778 ? 187.260 182.855 201.389 1.00 18.68  ? 2778 THR A CG2   1 
ATOM   9760  N  N     . MET A 1 2779 ? 186.082 179.627 202.925 1.00 16.42  ? 2779 MET A N     1 
ATOM   9761  C  CA    . MET A 1 2779 ? 186.678 178.315 202.700 1.00 13.02  ? 2779 MET A CA    1 
ATOM   9762  C  C     . MET A 1 2779 ? 185.708 177.397 201.970 1.00 14.65  ? 2779 MET A C     1 
ATOM   9763  O  O     . MET A 1 2779 ? 186.044 176.821 200.928 1.00 20.94  ? 2779 MET A O     1 
ATOM   9764  C  CB    . MET A 1 2779 ? 187.101 177.705 204.035 1.00 17.82  ? 2779 MET A CB    1 
ATOM   9765  C  CG    . MET A 1 2779 ? 188.233 178.448 204.721 1.00 23.84  ? 2779 MET A CG    1 
ATOM   9766  S  SD    . MET A 1 2779 ? 188.645 177.749 206.329 1.00 39.33  ? 2779 MET A SD    1 
ATOM   9767  C  CE    . MET A 1 2779 ? 189.401 176.206 205.836 1.00 22.65  ? 2779 MET A CE    1 
ATOM   9768  N  N     . SER A 1 2780 ? 184.481 177.290 202.483 1.00 13.34  ? 2780 SER A N     1 
ATOM   9769  C  CA    . SER A 1 2780 ? 183.467 176.481 201.817 1.00 12.74  ? 2780 SER A CA    1 
ATOM   9770  C  C     . SER A 1 2780 ? 183.261 176.943 200.382 1.00 13.05  ? 2780 SER A C     1 
ATOM   9771  O  O     . SER A 1 2780 ? 183.173 176.118 199.465 1.00 13.12  ? 2780 SER A O     1 
ATOM   9772  C  CB    . SER A 1 2780 ? 182.155 176.544 202.595 1.00 12.27  ? 2780 SER A CB    1 
ATOM   9773  O  OG    . SER A 1 2780 ? 182.326 176.072 203.919 1.00 22.70  ? 2780 SER A OG    1 
ATOM   9774  N  N     . GLN A 1 2781 ? 183.218 178.261 200.165 1.00 12.09  ? 2781 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2781 ? 183.029 178.774 198.814 1.00 11.68  ? 2781 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2781 ? 184.141 178.308 197.889 1.00 14.47  ? 2781 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2781 ? 183.897 178.048 196.706 1.00 17.31  ? 2781 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2781 ? 182.951 180.300 198.835 1.00 10.48  ? 2781 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2781 ? 182.266 180.899 197.620 1.00 9.21   ? 2781 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2781 ? 182.285 182.411 197.629 1.00 20.23  ? 2781 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2781 ? 181.293 183.059 197.300 1.00 18.00  ? 2781 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2781 ? 183.420 182.984 198.009 1.00 27.12  ? 2781 GLN A NE2   1 
ATOM   9783  N  N     . GLU A 1 2782 ? 185.364 178.192 198.407 1.00 12.89  ? 2782 GLU A N     1 
ATOM   9784  C  CA    . GLU A 1 2782 ? 186.443 177.634 197.605 1.00 15.28  ? 2782 GLU A CA    1 
ATOM   9785  C  C     . GLU A 1 2782 ? 186.344 176.116 197.522 1.00 17.00  ? 2782 GLU A C     1 
ATOM   9786  O  O     . GLU A 1 2782 ? 186.648 175.527 196.479 1.00 15.42  ? 2782 GLU A O     1 
ATOM   9787  C  CB    . GLU A 1 2782 ? 187.796 178.056 198.180 1.00 18.88  ? 2782 GLU A CB    1 
ATOM   9788  C  CG    . GLU A 1 2782 ? 188.996 177.559 197.388 1.00 31.87  ? 2782 GLU A CG    1 
ATOM   9789  C  CD    . GLU A 1 2782 ? 189.071 178.153 195.994 1.00 42.21  ? 2782 GLU A CD    1 
ATOM   9790  O  OE1   . GLU A 1 2782 ? 188.538 179.263 195.785 1.00 44.75  ? 2782 GLU A OE1   1 
ATOM   9791  O  OE2   . GLU A 1 2782 ? 189.662 177.505 195.105 1.00 48.17  ? 2782 GLU A OE2   1 
ATOM   9792  N  N     . ARG A 1 2783 ? 185.912 175.468 198.607 1.00 17.04  ? 2783 ARG A N     1 
ATOM   9793  C  CA    . ARG A 1 2783 ? 185.953 174.010 198.657 1.00 13.54  ? 2783 ARG A CA    1 
ATOM   9794  C  C     . ARG A 1 2783 ? 184.853 173.391 197.803 1.00 15.45  ? 2783 ARG A C     1 
ATOM   9795  O  O     . ARG A 1 2783 ? 185.095 172.432 197.062 1.00 14.16  ? 2783 ARG A O     1 
ATOM   9796  C  CB    . ARG A 1 2783 ? 185.842 173.534 200.104 1.00 12.73  ? 2783 ARG A CB    1 
ATOM   9797  C  CG    . ARG A 1 2783 ? 185.701 172.032 200.243 1.00 17.54  ? 2783 ARG A CG    1 
ATOM   9798  C  CD    . ARG A 1 2783 ? 186.995 171.321 199.879 1.00 18.85  ? 2783 ARG A CD    1 
ATOM   9799  N  NE    . ARG A 1 2783 ? 187.009 169.941 200.347 1.00 27.59  ? 2783 ARG A NE    1 
ATOM   9800  C  CZ    . ARG A 1 2783 ? 186.343 168.948 199.774 1.00 31.25  ? 2783 ARG A CZ    1 
ATOM   9801  N  NH1   . ARG A 1 2783 ? 185.610 169.142 198.689 1.00 26.80  ? 2783 ARG A NH1   1 
ATOM   9802  N  NH2   . ARG A 1 2783 ? 186.413 167.730 200.302 1.00 33.80  ? 2783 ARG A NH2   1 
ATOM   9803  N  N     . PHE A 1 2784 ? 183.640 173.925 197.891 1.00 15.92  ? 2784 PHE A N     1 
ATOM   9804  C  CA    . PHE A 1 2784 ? 182.485 173.385 197.183 1.00 12.42  ? 2784 PHE A CA    1 
ATOM   9805  C  C     . PHE A 1 2784 ? 182.078 174.373 196.100 1.00 17.24  ? 2784 PHE A C     1 
ATOM   9806  O  O     . PHE A 1 2784 ? 181.626 175.482 196.401 1.00 21.41  ? 2784 PHE A O     1 
ATOM   9807  C  CB    . PHE A 1 2784 ? 181.333 173.113 198.147 1.00 12.67  ? 2784 PHE A CB    1 
ATOM   9808  C  CG    . PHE A 1 2784 ? 181.746 172.379 199.388 1.00 12.65  ? 2784 PHE A CG    1 
ATOM   9809  C  CD1   . PHE A 1 2784 ? 182.209 171.077 199.314 1.00 12.81  ? 2784 PHE A CD1   1 
ATOM   9810  C  CD2   . PHE A 1 2784 ? 181.675 172.990 200.627 1.00 13.44  ? 2784 PHE A CD2   1 
ATOM   9811  C  CE1   . PHE A 1 2784 ? 182.592 170.399 200.451 1.00 14.36  ? 2784 PHE A CE1   1 
ATOM   9812  C  CE2   . PHE A 1 2784 ? 182.055 172.317 201.768 1.00 13.54  ? 2784 PHE A CE2   1 
ATOM   9813  C  CZ    . PHE A 1 2784 ? 182.514 171.018 201.680 1.00 17.63  ? 2784 PHE A CZ    1 
ATOM   9814  N  N     . THR A 1 2785 ? 182.238 173.969 194.847 1.00 19.76  ? 2785 THR A N     1 
ATOM   9815  C  CA    . THR A 1 2785 ? 181.918 174.799 193.698 1.00 17.72  ? 2785 THR A CA    1 
ATOM   9816  C  C     . THR A 1 2785 ? 180.856 174.113 192.850 1.00 17.85  ? 2785 THR A C     1 
ATOM   9817  O  O     . THR A 1 2785 ? 180.505 172.951 193.068 1.00 19.78  ? 2785 THR A O     1 
ATOM   9818  C  CB    . THR A 1 2785 ? 183.169 175.083 192.855 1.00 23.48  ? 2785 THR A CB    1 
ATOM   9819  O  OG1   . THR A 1 2785 ? 183.653 173.859 192.289 1.00 30.59  ? 2785 THR A OG1   1 
ATOM   9820  C  CG2   . THR A 1 2785 ? 184.260 175.701 193.714 1.00 17.29  ? 2785 THR A CG2   1 
ATOM   9821  N  N     . GLN A 1 2786 ? 180.346 174.851 191.864 1.00 22.36  ? 2786 GLN A N     1 
ATOM   9822  C  CA    . GLN A 1 2786 ? 179.348 174.306 190.954 1.00 22.15  ? 2786 GLN A CA    1 
ATOM   9823  C  C     . GLN A 1 2786 ? 179.913 173.218 190.051 1.00 24.01  ? 2786 GLN A C     1 
ATOM   9824  O  O     . GLN A 1 2786 ? 179.135 172.517 189.394 1.00 24.31  ? 2786 GLN A O     1 
ATOM   9825  C  CB    . GLN A 1 2786 ? 178.746 175.428 190.107 1.00 18.34  ? 2786 GLN A CB    1 
ATOM   9826  C  CG    . GLN A 1 2786 ? 177.300 175.198 189.711 1.00 21.51  ? 2786 GLN A CG    1 
ATOM   9827  C  CD    . GLN A 1 2786 ? 176.688 176.394 189.012 1.00 28.95  ? 2786 GLN A CD    1 
ATOM   9828  O  OE1   . GLN A 1 2786 ? 177.378 177.364 188.698 1.00 36.91  ? 2786 GLN A OE1   1 
ATOM   9829  N  NE2   . GLN A 1 2786 ? 175.385 176.332 188.766 1.00 31.91  ? 2786 GLN A NE2   1 
ATOM   9830  N  N     . ASP A 1 2787 ? 181.238 173.065 189.997 1.00 24.08  ? 2787 ASP A N     1 
ATOM   9831  C  CA    . ASP A 1 2787 ? 181.832 171.990 189.211 1.00 25.55  ? 2787 ASP A CA    1 
ATOM   9832  C  C     . ASP A 1 2787 ? 181.463 170.623 189.774 1.00 25.91  ? 2787 ASP A C     1 
ATOM   9833  O  O     . ASP A 1 2787 ? 181.217 169.680 189.014 1.00 29.27  ? 2787 ASP A O     1 
ATOM   9834  C  CB    . ASP A 1 2787 ? 183.350 172.159 189.157 1.00 30.39  ? 2787 ASP A CB    1 
ATOM   9835  C  CG    . ASP A 1 2787 ? 183.816 172.827 187.878 1.00 54.66  ? 2787 ASP A CG    1 
ATOM   9836  O  OD1   . ASP A 1 2787 ? 182.971 173.072 186.991 1.00 51.69  ? 2787 ASP A OD1   1 
ATOM   9837  O  OD2   . ASP A 1 2787 ? 185.027 173.105 187.757 1.00 65.47  ? 2787 ASP A OD2   1 
ATOM   9838  N  N     . THR A 1 2788 ? 181.427 170.494 191.102 1.00 26.17  ? 2788 THR A N     1 
ATOM   9839  C  CA    . THR A 1 2788 ? 181.069 169.219 191.717 1.00 20.85  ? 2788 THR A CA    1 
ATOM   9840  C  C     . THR A 1 2788 ? 179.574 168.950 191.593 1.00 17.58  ? 2788 THR A C     1 
ATOM   9841  O  O     . THR A 1 2788 ? 179.155 167.975 190.959 1.00 15.98  ? 2788 THR A O     1 
ATOM   9842  C  CB    . THR A 1 2788 ? 181.499 169.205 193.185 1.00 21.10  ? 2788 THR A CB    1 
ATOM   9843  O  OG1   . THR A 1 2788 ? 182.838 169.700 193.297 1.00 32.57  ? 2788 THR A OG1   1 
ATOM   9844  C  CG2   . THR A 1 2788 ? 181.437 167.793 193.744 1.00 22.60  ? 2788 THR A CG2   1 
ATOM   9845  N  N     . GLN A 1 2789 ? 178.753 169.807 192.192 1.00 18.85  ? 2789 GLN A N     1 
ATOM   9846  C  CA    . GLN A 1 2789 ? 177.307 169.674 192.139 1.00 17.83  ? 2789 GLN A CA    1 
ATOM   9847  C  C     . GLN A 1 2789 ? 176.677 171.001 191.748 1.00 17.56  ? 2789 GLN A C     1 
ATOM   9848  O  O     . GLN A 1 2789 ? 177.198 172.066 192.093 1.00 18.50  ? 2789 GLN A O     1 
ATOM   9849  C  CB    . GLN A 1 2789 ? 176.741 169.211 193.490 1.00 12.01  ? 2789 GLN A CB    1 
ATOM   9850  C  CG    . GLN A 1 2789 ? 177.394 167.954 194.036 1.00 13.84  ? 2789 GLN A CG    1 
ATOM   9851  C  CD    . GLN A 1 2789 ? 176.802 166.685 193.458 1.00 14.00  ? 2789 GLN A CD    1 
ATOM   9852  O  OE1   . GLN A 1 2789 ? 175.713 166.697 192.888 1.00 13.54  ? 2789 GLN A OE1   1 
ATOM   9853  N  NE2   . GLN A 1 2789 ? 177.524 165.581 193.597 1.00 15.40  ? 2789 GLN A NE2   1 
ATOM   9854  N  N     . PRO A 1 2790 ? 175.556 170.965 191.024 1.00 20.17  ? 2790 PRO A N     1 
ATOM   9855  C  CA    . PRO A 1 2790 ? 174.933 172.222 190.576 1.00 19.87  ? 2790 PRO A CA    1 
ATOM   9856  C  C     . PRO A 1 2790 ? 174.492 173.132 191.707 1.00 17.88  ? 2790 PRO A C     1 
ATOM   9857  O  O     . PRO A 1 2790 ? 174.526 174.359 191.549 1.00 16.80  ? 2790 PRO A O     1 
ATOM   9858  C  CB    . PRO A 1 2790 ? 173.737 171.738 189.743 1.00 23.90  ? 2790 PRO A CB    1 
ATOM   9859  C  CG    . PRO A 1 2790 ? 173.467 170.355 190.228 1.00 22.82  ? 2790 PRO A CG    1 
ATOM   9860  C  CD    . PRO A 1 2790 ? 174.806 169.785 190.564 1.00 19.23  ? 2790 PRO A CD    1 
ATOM   9861  N  N     . HIS A 1 2791 ? 174.076 172.577 192.842 1.00 20.07  ? 2791 HIS A N     1 
ATOM   9862  C  CA    . HIS A 1 2791 ? 173.538 173.368 193.939 1.00 13.49  ? 2791 HIS A CA    1 
ATOM   9863  C  C     . HIS A 1 2791 ? 174.609 173.894 194.885 1.00 12.07  ? 2791 HIS A C     1 
ATOM   9864  O  O     . HIS A 1 2791 ? 174.274 174.603 195.839 1.00 17.73  ? 2791 HIS A O     1 
ATOM   9865  C  CB    . HIS A 1 2791 ? 172.515 172.545 194.729 1.00 11.48  ? 2791 HIS A CB    1 
ATOM   9866  C  CG    . HIS A 1 2791 ? 173.056 171.252 195.253 1.00 13.99  ? 2791 HIS A CG    1 
ATOM   9867  N  ND1   . HIS A 1 2791 ? 173.205 170.133 194.463 1.00 16.16  ? 2791 HIS A ND1   1 
ATOM   9868  C  CD2   . HIS A 1 2791 ? 173.479 170.898 196.489 1.00 13.02  ? 2791 HIS A CD2   1 
ATOM   9869  C  CE1   . HIS A 1 2791 ? 173.700 169.147 195.189 1.00 16.71  ? 2791 HIS A CE1   1 
ATOM   9870  N  NE2   . HIS A 1 2791 ? 173.876 169.585 196.422 1.00 14.93  ? 2791 HIS A NE2   1 
ATOM   9871  N  N     . TYR A 1 2792 ? 175.882 173.576 194.651 1.00 10.22  ? 2792 TYR A N     1 
ATOM   9872  C  CA    . TYR A 1 2792 ? 176.968 174.046 195.513 1.00 11.59  ? 2792 TYR A CA    1 
ATOM   9873  C  C     . TYR A 1 2792 ? 177.259 175.516 195.208 1.00 15.15  ? 2792 TYR A C     1 
ATOM   9874  O  O     . TYR A 1 2792 ? 178.289 175.885 194.642 1.00 19.81  ? 2792 TYR A O     1 
ATOM   9875  C  CB    . TYR A 1 2792 ? 178.211 173.187 195.333 1.00 12.81  ? 2792 TYR A CB    1 
ATOM   9876  C  CG    . TYR A 1 2792 ? 178.150 171.838 196.009 1.00 14.87  ? 2792 TYR A CG    1 
ATOM   9877  C  CD1   . TYR A 1 2792 ? 177.038 171.454 196.746 1.00 15.12  ? 2792 TYR A CD1   1 
ATOM   9878  C  CD2   . TYR A 1 2792 ? 179.210 170.950 195.914 1.00 15.32  ? 2792 TYR A CD2   1 
ATOM   9879  C  CE1   . TYR A 1 2792 ? 176.984 170.221 197.363 1.00 13.69  ? 2792 TYR A CE1   1 
ATOM   9880  C  CE2   . TYR A 1 2792 ? 179.165 169.718 196.528 1.00 17.41  ? 2792 TYR A CE2   1 
ATOM   9881  C  CZ    . TYR A 1 2792 ? 178.051 169.357 197.249 1.00 16.42  ? 2792 TYR A CZ    1 
ATOM   9882  O  OH    . TYR A 1 2792 ? 178.007 168.127 197.862 1.00 19.73  ? 2792 TYR A OH    1 
ATOM   9883  N  N     . ILE A 1 2793 ? 176.316 176.365 195.603 1.00 13.72  ? 2793 ILE A N     1 
ATOM   9884  C  CA    . ILE A 1 2793 ? 176.409 177.806 195.401 1.00 11.41  ? 2793 ILE A CA    1 
ATOM   9885  C  C     . ILE A 1 2793 ? 176.395 178.468 196.769 1.00 9.33   ? 2793 ILE A C     1 
ATOM   9886  O  O     . ILE A 1 2793 ? 175.458 178.269 197.551 1.00 11.16  ? 2793 ILE A O     1 
ATOM   9887  C  CB    . ILE A 1 2793 ? 175.264 178.336 194.525 1.00 12.27  ? 2793 ILE A CB    1 
ATOM   9888  C  CG1   . ILE A 1 2793 ? 175.337 177.725 193.126 1.00 12.97  ? 2793 ILE A CG1   1 
ATOM   9889  C  CG2   . ILE A 1 2793 ? 175.312 179.853 194.450 1.00 11.21  ? 2793 ILE A CG2   1 
ATOM   9890  C  CD1   . ILE A 1 2793 ? 174.111 177.989 192.286 1.00 18.51  ? 2793 ILE A CD1   1 
ATOM   9891  N  N     . TYR A 1 2794 ? 177.428 179.253 197.056 1.00 7.98   ? 2794 TYR A N     1 
ATOM   9892  C  CA    . TYR A 1 2794 ? 177.548 179.962 198.321 1.00 8.14   ? 2794 TYR A CA    1 
ATOM   9893  C  C     . TYR A 1 2794 ? 177.700 181.449 198.047 1.00 9.69   ? 2794 TYR A C     1 
ATOM   9894  O  O     . TYR A 1 2794 ? 178.521 181.853 197.217 1.00 11.73  ? 2794 TYR A O     1 
ATOM   9895  C  CB    . TYR A 1 2794 ? 178.727 179.432 199.136 1.00 9.00   ? 2794 TYR A CB    1 
ATOM   9896  C  CG    . TYR A 1 2794 ? 178.552 177.990 199.544 1.00 12.31  ? 2794 TYR A CG    1 
ATOM   9897  C  CD1   . TYR A 1 2794 ? 177.657 177.638 200.544 1.00 14.47  ? 2794 TYR A CD1   1 
ATOM   9898  C  CD2   . TYR A 1 2794 ? 179.269 176.979 198.922 1.00 15.03  ? 2794 TYR A CD2   1 
ATOM   9899  C  CE1   . TYR A 1 2794 ? 177.486 176.323 200.918 1.00 13.23  ? 2794 TYR A CE1   1 
ATOM   9900  C  CE2   . TYR A 1 2794 ? 179.105 175.659 199.291 1.00 13.96  ? 2794 TYR A CE2   1 
ATOM   9901  C  CZ    . TYR A 1 2794 ? 178.213 175.338 200.290 1.00 15.95  ? 2794 TYR A CZ    1 
ATOM   9902  O  OH    . TYR A 1 2794 ? 178.045 174.024 200.662 1.00 28.81  ? 2794 TYR A OH    1 
ATOM   9903  N  N     . SER A 1 2795 ? 176.876 182.251 198.726 1.00 8.40   ? 2795 SER A N     1 
ATOM   9904  C  CA    . SER A 1 2795 ? 176.875 183.714 198.483 1.00 7.83   ? 2795 SER A CA    1 
ATOM   9905  C  C     . SER A 1 2795 ? 176.629 184.453 199.802 1.00 10.16  ? 2795 SER A C     1 
ATOM   9906  O  O     . SER A 1 2795 ? 176.391 183.776 200.824 1.00 9.42   ? 2795 SER A O     1 
ATOM   9907  C  CB    . SER A 1 2795 ? 175.821 184.064 197.475 1.00 9.11   ? 2795 SER A CB    1 
ATOM   9908  O  OG    . SER A 1 2795 ? 174.525 183.770 197.978 1.00 14.20  ? 2795 SER A OG    1 
ATOM   9909  N  N     . PRO A 1 2796 ? 176.668 185.802 199.828 1.00 8.58   ? 2796 PRO A N     1 
ATOM   9910  C  CA    . PRO A 1 2796 ? 176.355 186.539 201.043 1.00 8.57   ? 2796 PRO A CA    1 
ATOM   9911  C  C     . PRO A 1 2796 ? 174.988 186.169 201.606 1.00 8.58   ? 2796 PRO A C     1 
ATOM   9912  O  O     . PRO A 1 2796 ? 174.723 186.463 202.787 1.00 12.33  ? 2796 PRO A O     1 
ATOM   9913  C  CB    . PRO A 1 2796 ? 176.409 187.993 200.556 1.00 9.35   ? 2796 PRO A CB    1 
ATOM   9914  C  CG    . PRO A 1 2796 ? 177.398 187.957 199.419 1.00 8.19   ? 2796 PRO A CG    1 
ATOM   9915  C  CD    . PRO A 1 2796 ? 177.076 186.652 198.720 1.00 5.90   ? 2796 PRO A CD    1 
ATOM   9916  N  N     . ARG A 1 2797 ? 174.134 185.551 200.786 1.00 9.05   ? 2797 ARG A N     1 
ATOM   9917  C  CA    . ARG A 1 2797 ? 172.775 185.150 201.240 1.00 8.99   ? 2797 ARG A CA    1 
ATOM   9918  C  C     . ARG A 1 2797 ? 172.904 184.148 202.398 1.00 11.76  ? 2797 ARG A C     1 
ATOM   9919  O  O     . ARG A 1 2797 ? 172.121 184.258 203.366 1.00 12.78  ? 2797 ARG A O     1 
ATOM   9920  C  CB    . ARG A 1 2797 ? 171.954 184.575 200.081 1.00 7.40   ? 2797 ARG A CB    1 
ATOM   9921  C  CG    . ARG A 1 2797 ? 171.530 185.627 199.066 1.00 10.38  ? 2797 ARG A CG    1 
ATOM   9922  C  CD    . ARG A 1 2797 ? 170.328 185.183 198.251 1.00 8.98   ? 2797 ARG A CD    1 
ATOM   9923  N  NE    . ARG A 1 2797 ? 170.629 184.044 197.378 1.00 15.44  ? 2797 ARG A NE    1 
ATOM   9924  C  CZ    . ARG A 1 2797 ? 170.491 184.058 196.059 1.00 20.66  ? 2797 ARG A CZ    1 
ATOM   9925  N  NH1   . ARG A 1 2797 ? 169.949 185.106 195.465 1.00 11.59  ? 2797 ARG A NH1   1 
ATOM   9926  N  NH2   . ARG A 1 2797 ? 170.890 183.024 195.341 1.00 20.19  ? 2797 ARG A NH2   1 
ATOM   9927  N  N     . GLU A 1 2798 ? 173.858 183.219 202.305 1.00 12.84  ? 2798 GLU A N     1 
ATOM   9928  C  CA    . GLU A 1 2798 ? 174.089 182.251 203.406 1.00 8.98   ? 2798 GLU A CA    1 
ATOM   9929  C  C     . GLU A 1 2798 ? 174.480 183.033 204.665 1.00 8.78   ? 2798 GLU A C     1 
ATOM   9930  O  O     . GLU A 1 2798 ? 173.979 182.691 205.756 1.00 12.25  ? 2798 GLU A O     1 
ATOM   9931  C  CB    . GLU A 1 2798 ? 175.200 181.270 203.033 1.00 12.19  ? 2798 GLU A CB    1 
ATOM   9932  C  CG    . GLU A 1 2798 ? 175.202 180.881 201.557 1.00 15.18  ? 2798 GLU A CG    1 
ATOM   9933  C  CD    . GLU A 1 2798 ? 174.073 179.962 201.128 1.00 20.37  ? 2798 GLU A CD    1 
ATOM   9934  O  OE1   . GLU A 1 2798 ? 173.260 179.573 201.991 1.00 30.83  ? 2798 GLU A OE1   1 
ATOM   9935  O  OE2   . GLU A 1 2798 ? 174.008 179.636 199.925 1.00 18.03  ? 2798 GLU A OE2   1 
ATOM   9936  N  N     . MET A 1 2799 ? 175.332 184.050 204.511 1.00 10.15  ? 2799 MET A N     1 
ATOM   9937  C  CA    . MET A 1 2799 ? 175.810 184.837 205.678 1.00 11.40  ? 2799 MET A CA    1 
ATOM   9938  C  C     . MET A 1 2799 ? 174.640 185.615 206.299 1.00 9.04   ? 2799 MET A C     1 
ATOM   9939  O  O     . MET A 1 2799 ? 174.587 185.700 207.542 1.00 13.18  ? 2799 MET A O     1 
ATOM   9940  C  CB    . MET A 1 2799 ? 176.934 185.794 205.268 1.00 10.18  ? 2799 MET A CB    1 
ATOM   9941  C  CG    . MET A 1 2799 ? 178.195 185.093 204.806 1.00 11.30  ? 2799 MET A CG    1 
ATOM   9942  S  SD    . MET A 1 2799 ? 179.664 186.109 205.052 1.00 46.36  ? 2799 MET A SD    1 
ATOM   9943  C  CE    . MET A 1 2799 ? 179.627 186.308 206.838 1.00 13.54  ? 2799 MET A CE    1 
ATOM   9944  N  N     . THR A 1 2800 ? 173.747 186.157 205.470 1.00 7.31   ? 2800 THR A N     1 
ATOM   9945  C  CA    . THR A 1 2800 ? 172.561 186.859 206.004 1.00 8.49   ? 2800 THR A CA    1 
ATOM   9946  C  C     . THR A 1 2800 ? 171.735 185.864 206.788 1.00 10.23  ? 2800 THR A C     1 
ATOM   9947  O  O     . THR A 1 2800 ? 171.336 186.191 207.925 1.00 12.81  ? 2800 THR A O     1 
ATOM   9948  C  CB    . THR A 1 2800 ? 171.768 187.481 204.856 1.00 7.57   ? 2800 THR A CB    1 
ATOM   9949  O  OG1   . THR A 1 2800 ? 172.680 188.363 204.209 1.00 11.41  ? 2800 THR A OG1   1 
ATOM   9950  C  CG2   . THR A 1 2800 ? 170.552 188.250 205.338 1.00 7.26   ? 2800 THR A CG2   1 
ATOM   9951  N  N     . ARG A 1 2801 ? 171.505 184.681 206.215 1.00 11.27  ? 2801 ARG A N     1 
ATOM   9952  C  CA    . ARG A 1 2801 ? 170.724 183.623 206.905 1.00 9.94   ? 2801 ARG A CA    1 
ATOM   9953  C  C     . ARG A 1 2801 ? 171.448 183.251 208.206 1.00 11.15  ? 2801 ARG A C     1 
ATOM   9954  O  O     . ARG A 1 2801 ? 170.758 183.065 209.230 1.00 18.30  ? 2801 ARG A O     1 
ATOM   9955  C  CB    . ARG A 1 2801 ? 170.567 182.426 205.963 1.00 10.90  ? 2801 ARG A CB    1 
ATOM   9956  C  CG    . ARG A 1 2801 ? 169.252 181.671 206.085 1.00 18.00  ? 2801 ARG A CG    1 
ATOM   9957  C  CD    . ARG A 1 2801 ? 169.084 180.733 204.902 1.00 31.38  ? 2801 ARG A CD    1 
ATOM   9958  N  NE    . ARG A 1 2801 ? 169.118 181.470 203.634 1.00 39.61  ? 2801 ARG A NE    1 
ATOM   9959  C  CZ    . ARG A 1 2801 ? 170.035 181.303 202.690 1.00 41.67  ? 2801 ARG A CZ    1 
ATOM   9960  N  NH1   . ARG A 1 2801 ? 171.015 180.438 202.871 1.00 27.79  ? 2801 ARG A NH1   1 
ATOM   9961  N  NH2   . ARG A 1 2801 ? 169.972 182.005 201.573 1.00 47.00  ? 2801 ARG A NH2   1 
ATOM   9962  N  N     . TRP A 1 2802 ? 172.779 183.156 208.166 1.00 7.01   ? 2802 TRP A N     1 
ATOM   9963  C  CA    . TRP A 1 2802 ? 173.552 182.851 209.369 1.00 8.24   ? 2802 TRP A CA    1 
ATOM   9964  C  C     . TRP A 1 2802 ? 173.286 183.865 210.472 1.00 9.59   ? 2802 TRP A C     1 
ATOM   9965  O  O     . TRP A 1 2802 ? 172.946 183.502 211.608 1.00 14.21  ? 2802 TRP A O     1 
ATOM   9966  C  CB    . TRP A 1 2802 ? 175.041 182.849 209.016 1.00 10.31  ? 2802 TRP A CB    1 
ATOM   9967  C  CG    . TRP A 1 2802 ? 175.913 181.979 209.859 1.00 9.82   ? 2802 TRP A CG    1 
ATOM   9968  C  CD1   . TRP A 1 2802 ? 175.625 181.469 211.086 1.00 9.20   ? 2802 TRP A CD1   1 
ATOM   9969  C  CD2   . TRP A 1 2802 ? 177.243 181.554 209.548 1.00 8.05   ? 2802 TRP A CD2   1 
ATOM   9970  N  NE1   . TRP A 1 2802 ? 176.685 180.733 211.552 1.00 8.68   ? 2802 TRP A NE1   1 
ATOM   9971  C  CE2   . TRP A 1 2802 ? 177.693 180.772 210.626 1.00 7.62   ? 2802 TRP A CE2   1 
ATOM   9972  C  CE3   . TRP A 1 2802 ? 178.095 181.752 208.458 1.00 11.17  ? 2802 TRP A CE3   1 
ATOM   9973  C  CZ2   . TRP A 1 2802 ? 178.954 180.187 210.645 1.00 8.97   ? 2802 TRP A CZ2   1 
ATOM   9974  C  CZ3   . TRP A 1 2802 ? 179.346 181.170 208.480 1.00 11.32  ? 2802 TRP A CZ3   1 
ATOM   9975  C  CH2   . TRP A 1 2802 ? 179.764 180.397 209.566 1.00 10.23  ? 2802 TRP A CH2   1 
ATOM   9976  N  N     . VAL A 1 2803 ? 173.453 185.148 210.150 1.00 12.29  ? 2803 VAL A N     1 
ATOM   9977  C  CA    . VAL A 1 2803 ? 173.258 186.199 211.142 1.00 12.24  ? 2803 VAL A CA    1 
ATOM   9978  C  C     . VAL A 1 2803 ? 171.814 186.208 211.620 1.00 11.47  ? 2803 VAL A C     1 
ATOM   9979  O  O     . VAL A 1 2803 ? 171.542 186.355 212.816 1.00 14.55  ? 2803 VAL A O     1 
ATOM   9980  C  CB    . VAL A 1 2803 ? 173.680 187.563 210.566 1.00 11.91  ? 2803 VAL A CB    1 
ATOM   9981  C  CG1   . VAL A 1 2803 ? 173.491 188.655 211.597 1.00 11.51  ? 2803 VAL A CG1   1 
ATOM   9982  C  CG2   . VAL A 1 2803 ? 175.125 187.517 210.111 1.00 12.73  ? 2803 VAL A CG2   1 
ATOM   9983  N  N     . ARG A 1 2804 ? 170.867 186.031 210.696 1.00 10.80  ? 2804 ARG A N     1 
ATOM   9984  C  CA    . ARG A 1 2804 ? 169.454 186.021 211.062 1.00 14.78  ? 2804 ARG A CA    1 
ATOM   9985  C  C     . ARG A 1 2804 ? 169.123 184.859 211.994 1.00 14.91  ? 2804 ARG A C     1 
ATOM   9986  O  O     . ARG A 1 2804 ? 168.381 185.029 212.968 1.00 18.97  ? 2804 ARG A O     1 
ATOM   9987  C  CB    . ARG A 1 2804 ? 168.599 185.971 209.796 1.00 17.53  ? 2804 ARG A CB    1 
ATOM   9988  C  CG    . ARG A 1 2804 ? 167.107 185.983 210.042 1.00 22.63  ? 2804 ARG A CG    1 
ATOM   9989  C  CD    . ARG A 1 2804 ? 166.644 187.297 210.640 1.00 38.78  ? 2804 ARG A CD    1 
ATOM   9990  N  NE    . ARG A 1 2804 ? 165.199 187.317 210.833 1.00 44.81  ? 2804 ARG A NE    1 
ATOM   9991  C  CZ    . ARG A 1 2804 ? 164.543 188.267 211.485 1.00 42.83  ? 2804 ARG A CZ    1 
ATOM   9992  N  NH1   . ARG A 1 2804 ? 165.173 189.299 212.020 1.00 37.10  ? 2804 ARG A NH1   1 
ATOM   9993  N  NH2   . ARG A 1 2804 ? 163.221 188.177 211.604 1.00 44.89  ? 2804 ARG A NH2   1 
ATOM   9994  N  N     . GLY A 1 2805 ? 169.664 183.671 211.715 1.00 11.89  ? 2805 GLY A N     1 
ATOM   9995  C  CA    . GLY A 1 2805 ? 169.403 182.527 212.572 1.00 10.43  ? 2805 GLY A CA    1 
ATOM   9996  C  C     . GLY A 1 2805 ? 169.999 182.680 213.957 1.00 13.50  ? 2805 GLY A C     1 
ATOM   9997  O  O     . GLY A 1 2805 ? 169.350 182.364 214.961 1.00 20.18  ? 2805 GLY A O     1 
ATOM   9998  N  N     . ILE A 1 2806 ? 171.241 183.164 214.037 1.00 12.73  ? 2806 ILE A N     1 
ATOM   9999  C  CA    . ILE A 1 2806 ? 171.836 183.401 215.350 1.00 12.24  ? 2806 ILE A CA    1 
ATOM   10000 C  C     . ILE A 1 2806 ? 171.057 184.475 216.100 1.00 14.54  ? 2806 ILE A C     1 
ATOM   10001 O  O     . ILE A 1 2806 ? 170.883 184.398 217.322 1.00 16.07  ? 2806 ILE A O     1 
ATOM   10002 C  CB    . ILE A 1 2806 ? 173.327 183.760 215.218 1.00 10.07  ? 2806 ILE A CB    1 
ATOM   10003 C  CG1   . ILE A 1 2806 ? 174.078 182.635 214.507 1.00 12.61  ? 2806 ILE A CG1   1 
ATOM   10004 C  CG2   . ILE A 1 2806 ? 173.941 183.998 216.586 1.00 7.78   ? 2806 ILE A CG2   1 
ATOM   10005 C  CD1   . ILE A 1 2806 ? 175.574 182.814 214.497 1.00 12.30  ? 2806 ILE A CD1   1 
ATOM   10006 N  N     . PHE A 1 2807 ? 170.558 185.484 215.382 1.00 15.49  ? 2807 PHE A N     1 
ATOM   10007 C  CA    . PHE A 1 2807 ? 169.763 186.526 216.021 1.00 15.25  ? 2807 PHE A CA    1 
ATOM   10008 C  C     . PHE A 1 2807 ? 168.454 185.973 216.570 1.00 18.65  ? 2807 PHE A C     1 
ATOM   10009 O  O     . PHE A 1 2807 ? 168.031 186.341 217.672 1.00 24.79  ? 2807 PHE A O     1 
ATOM   10010 C  CB    . PHE A 1 2807 ? 169.504 187.658 215.029 1.00 19.08  ? 2807 PHE A CB    1 
ATOM   10011 C  CG    . PHE A 1 2807 ? 168.529 188.683 215.521 1.00 24.38  ? 2807 PHE A CG    1 
ATOM   10012 C  CD1   . PHE A 1 2807 ? 168.887 189.576 216.514 1.00 23.76  ? 2807 PHE A CD1   1 
ATOM   10013 C  CD2   . PHE A 1 2807 ? 167.260 188.766 214.978 1.00 25.28  ? 2807 PHE A CD2   1 
ATOM   10014 C  CE1   . PHE A 1 2807 ? 167.994 190.522 216.963 1.00 30.02  ? 2807 PHE A CE1   1 
ATOM   10015 C  CE2   . PHE A 1 2807 ? 166.365 189.712 215.422 1.00 25.66  ? 2807 PHE A CE2   1 
ATOM   10016 C  CZ    . PHE A 1 2807 ? 166.731 190.591 216.417 1.00 26.80  ? 2807 PHE A CZ    1 
ATOM   10017 N  N     . GLU A 1 2808 ? 167.788 185.097 215.811 1.00 17.72  ? 2808 GLU A N     1 
ATOM   10018 C  CA    . GLU A 1 2808 ? 166.581 184.461 216.332 1.00 20.47  ? 2808 GLU A CA    1 
ATOM   10019 C  C     . GLU A 1 2808 ? 166.894 183.615 217.558 1.00 22.44  ? 2808 GLU A C     1 
ATOM   10020 O  O     . GLU A 1 2808 ? 166.126 183.608 218.528 1.00 24.11  ? 2808 GLU A O     1 
ATOM   10021 C  CB    . GLU A 1 2808 ? 165.902 183.602 215.265 1.00 20.93  ? 2808 GLU A CB    1 
ATOM   10022 C  CG    . GLU A 1 2808 ? 165.461 184.330 214.011 1.00 28.46  ? 2808 GLU A CG    1 
ATOM   10023 C  CD    . GLU A 1 2808 ? 165.498 183.436 212.788 1.00 42.40  ? 2808 GLU A CD    1 
ATOM   10024 O  OE1   . GLU A 1 2808 ? 165.440 183.961 211.659 1.00 43.62  ? 2808 GLU A OE1   1 
ATOM   10025 O  OE2   . GLU A 1 2808 ? 165.581 182.201 212.958 1.00 35.44  ? 2808 GLU A OE2   1 
ATOM   10026 N  N     . ALA A 1 2809 ? 168.014 182.890 217.531 1.00 21.70  ? 2809 ALA A N     1 
ATOM   10027 C  CA    . ALA A 1 2809 ? 168.405 182.100 218.694 1.00 17.98  ? 2809 ALA A CA    1 
ATOM   10028 C  C     . ALA A 1 2809 ? 168.686 182.988 219.901 1.00 22.34  ? 2809 ALA A C     1 
ATOM   10029 O  O     . ALA A 1 2809 ? 168.440 182.587 221.044 1.00 29.81  ? 2809 ALA A O     1 
ATOM   10030 C  CB    . ALA A 1 2809 ? 169.625 181.246 218.360 1.00 15.26  ? 2809 ALA A CB    1 
ATOM   10031 N  N     . LEU A 1 2810 ? 169.204 184.194 219.668 1.00 22.77  ? 2810 LEU A N     1 
ATOM   10032 C  CA    . LEU A 1 2810 ? 169.591 185.080 220.759 1.00 19.96  ? 2810 LEU A CA    1 
ATOM   10033 C  C     . LEU A 1 2810 ? 168.477 186.013 221.220 1.00 24.99  ? 2810 LEU A C     1 
ATOM   10034 O  O     . LEU A 1 2810 ? 168.642 186.671 222.252 1.00 30.56  ? 2810 LEU A O     1 
ATOM   10035 C  CB    . LEU A 1 2810 ? 170.804 185.917 220.345 1.00 21.34  ? 2810 LEU A CB    1 
ATOM   10036 C  CG    . LEU A 1 2810 ? 172.137 185.178 220.250 1.00 15.33  ? 2810 LEU A CG    1 
ATOM   10037 C  CD1   . LEU A 1 2810 ? 173.288 186.157 220.093 1.00 20.97  ? 2810 LEU A CD1   1 
ATOM   10038 C  CD2   . LEU A 1 2810 ? 172.335 184.309 221.468 1.00 19.64  ? 2810 LEU A CD2   1 
ATOM   10039 N  N     . ARG A 1 2811 ? 167.363 186.098 220.491 1.00 28.32  ? 2811 ARG A N     1 
ATOM   10040 C  CA    . ARG A 1 2811 ? 166.295 187.015 220.890 1.00 30.74  ? 2811 ARG A CA    1 
ATOM   10041 C  C     . ARG A 1 2811 ? 165.739 186.740 222.283 1.00 32.30  ? 2811 ARG A C     1 
ATOM   10042 O  O     . ARG A 1 2811 ? 165.684 187.681 223.093 1.00 36.09  ? 2811 ARG A O     1 
ATOM   10043 C  CB    . ARG A 1 2811 ? 165.170 187.005 219.848 1.00 29.54  ? 2811 ARG A CB    1 
ATOM   10044 C  CG    . ARG A 1 2811 ? 165.307 188.023 218.733 1.00 26.63  ? 2811 ARG A CG    1 
ATOM   10045 C  CD    . ARG A 1 2811 ? 164.065 187.993 217.839 1.00 35.71  ? 2811 ARG A CD    1 
ATOM   10046 N  NE    . ARG A 1 2811 ? 163.810 189.250 217.141 1.00 47.73  ? 2811 ARG A NE    1 
ATOM   10047 C  CZ    . ARG A 1 2811 ? 163.595 190.423 217.726 1.00 45.60  ? 2811 ARG A CZ    1 
ATOM   10048 N  NH1   . ARG A 1 2811 ? 163.536 190.542 219.043 1.00 43.03  ? 2811 ARG A NH1   1 
ATOM   10049 N  NH2   . ARG A 1 2811 ? 163.418 191.502 216.970 1.00 30.73  ? 2811 ARG A NH2   1 
ATOM   10050 N  N     . PRO A 1 2812 ? 165.318 185.518 222.639 1.00 34.24  ? 2812 PRO A N     1 
ATOM   10051 C  CA    . PRO A 1 2812 ? 164.662 185.341 223.942 1.00 32.42  ? 2812 PRO A CA    1 
ATOM   10052 C  C     . PRO A 1 2812 ? 165.618 185.228 225.117 1.00 35.07  ? 2812 PRO A C     1 
ATOM   10053 O  O     . PRO A 1 2812 ? 165.193 185.468 226.255 1.00 43.04  ? 2812 PRO A O     1 
ATOM   10054 C  CB    . PRO A 1 2812 ? 163.870 184.042 223.759 1.00 35.36  ? 2812 PRO A CB    1 
ATOM   10055 C  CG    . PRO A 1 2812 ? 164.684 183.265 222.800 1.00 32.55  ? 2812 PRO A CG    1 
ATOM   10056 C  CD    . PRO A 1 2812 ? 165.329 184.258 221.869 1.00 29.00  ? 2812 PRO A CD    1 
ATOM   10057 N  N     . LEU A 1 2813 ? 166.880 184.876 224.887 1.00 33.16  ? 2813 LEU A N     1 
ATOM   10058 C  CA    . LEU A 1 2813 ? 167.800 184.620 225.987 1.00 34.99  ? 2813 LEU A CA    1 
ATOM   10059 C  C     . LEU A 1 2813 ? 168.152 185.912 226.712 1.00 40.92  ? 2813 LEU A C     1 
ATOM   10060 O  O     . LEU A 1 2813 ? 168.506 186.914 226.084 1.00 43.15  ? 2813 LEU A O     1 
ATOM   10061 C  CB    . LEU A 1 2813 ? 169.068 183.946 225.468 1.00 35.03  ? 2813 LEU A CB    1 
ATOM   10062 C  CG    . LEU A 1 2813 ? 168.887 182.793 224.480 1.00 28.09  ? 2813 LEU A CG    1 
ATOM   10063 C  CD1   . LEU A 1 2813 ? 170.236 182.211 224.095 1.00 22.64  ? 2813 LEU A CD1   1 
ATOM   10064 C  CD2   . LEU A 1 2813 ? 167.986 181.717 225.065 1.00 33.08  ? 2813 LEU A CD2   1 
ATOM   10065 N  N     . GLU A 1 2814 ? 168.052 185.887 228.043 1.00 40.33  ? 2814 GLU A N     1 
ATOM   10066 C  CA    . GLU A 1 2814 ? 168.464 187.034 228.844 1.00 46.67  ? 2814 GLU A CA    1 
ATOM   10067 C  C     . GLU A 1 2814 ? 169.979 187.122 228.973 1.00 44.90  ? 2814 GLU A C     1 
ATOM   10068 O  O     . GLU A 1 2814 ? 170.520 188.223 229.123 1.00 42.70  ? 2814 GLU A O     1 
ATOM   10069 C  CB    . GLU A 1 2814 ? 167.815 186.971 230.229 1.00 50.72  ? 2814 GLU A CB    1 
ATOM   10070 C  CG    . GLU A 1 2814 ? 168.353 185.871 231.131 1.00 53.80  ? 2814 GLU A CG    1 
ATOM   10071 C  CD    . GLU A 1 2814 ? 167.360 185.452 232.195 1.00 66.10  ? 2814 GLU A CD    1 
ATOM   10072 O  OE1   . GLU A 1 2814 ? 166.827 186.338 232.895 1.00 61.00  ? 2814 GLU A OE1   1 
ATOM   10073 O  OE2   . GLU A 1 2814 ? 167.112 184.235 232.334 1.00 74.22  ? 2814 GLU A OE2   1 
ATOM   10074 N  N     . THR A 1 2815 ? 170.669 185.986 228.922 1.00 45.47  ? 2815 THR A N     1 
ATOM   10075 C  CA    . THR A 1 2815 ? 172.123 185.948 228.975 1.00 40.99  ? 2815 THR A CA    1 
ATOM   10076 C  C     . THR A 1 2815 ? 172.585 184.620 228.396 1.00 37.84  ? 2815 THR A C     1 
ATOM   10077 O  O     . THR A 1 2815 ? 171.803 183.674 228.269 1.00 37.64  ? 2815 THR A O     1 
ATOM   10078 C  CB    . THR A 1 2815 ? 172.648 186.129 230.403 1.00 44.17  ? 2815 THR A CB    1 
ATOM   10079 O  OG1   . THR A 1 2815 ? 174.053 186.408 230.366 1.00 43.85  ? 2815 THR A OG1   1 
ATOM   10080 C  CG2   . THR A 1 2815 ? 172.405 184.873 231.227 1.00 34.39  ? 2815 THR A CG2   1 
ATOM   10081 N  N     . LEU A 1 2816 ? 173.869 184.564 228.042 1.00 36.31  ? 2816 LEU A N     1 
ATOM   10082 C  CA    . LEU A 1 2816 ? 174.438 183.356 227.459 1.00 29.24  ? 2816 LEU A CA    1 
ATOM   10083 C  C     . LEU A 1 2816 ? 175.960 183.446 227.472 1.00 29.68  ? 2816 LEU A C     1 
ATOM   10084 O  O     . LEU A 1 2816 ? 176.521 184.489 227.113 1.00 36.02  ? 2816 LEU A O     1 
ATOM   10085 C  CB    . LEU A 1 2816 ? 173.927 183.163 226.030 1.00 26.16  ? 2816 LEU A CB    1 
ATOM   10086 C  CG    . LEU A 1 2816 ? 174.665 182.168 225.135 1.00 29.62  ? 2816 LEU A CG    1 
ATOM   10087 C  CD1   . LEU A 1 2816 ? 174.251 180.749 225.484 1.00 30.42  ? 2816 LEU A CD1   1 
ATOM   10088 C  CD2   . LEU A 1 2816 ? 174.407 182.457 223.673 1.00 27.44  ? 2816 LEU A CD2   1 
ATOM   10089 N  N     . PRO A 1 2817 ? 176.661 182.391 227.879 1.00 31.40  ? 2817 PRO A N     1 
ATOM   10090 C  CA    . PRO A 1 2817 ? 178.127 182.414 227.833 1.00 26.89  ? 2817 PRO A CA    1 
ATOM   10091 C  C     . PRO A 1 2817 ? 178.639 182.350 226.401 1.00 29.87  ? 2817 PRO A C     1 
ATOM   10092 O  O     . PRO A 1 2817 ? 177.892 182.143 225.444 1.00 32.35  ? 2817 PRO A O     1 
ATOM   10093 C  CB    . PRO A 1 2817 ? 178.529 181.170 228.629 1.00 28.85  ? 2817 PRO A CB    1 
ATOM   10094 C  CG    . PRO A 1 2817 ? 177.361 180.256 228.506 1.00 30.28  ? 2817 PRO A CG    1 
ATOM   10095 C  CD    . PRO A 1 2817 ? 176.145 181.138 228.456 1.00 27.25  ? 2817 PRO A CD    1 
ATOM   10096 N  N     . VAL A 1 2818 ? 179.953 182.541 226.268 1.00 33.50  ? 2818 VAL A N     1 
ATOM   10097 C  CA    . VAL A 1 2818 ? 180.574 182.537 224.946 1.00 28.23  ? 2818 VAL A CA    1 
ATOM   10098 C  C     . VAL A 1 2818 ? 180.475 181.156 224.309 1.00 30.71  ? 2818 VAL A C     1 
ATOM   10099 O  O     . VAL A 1 2818 ? 180.309 181.029 223.089 1.00 29.98  ? 2818 VAL A O     1 
ATOM   10100 C  CB    . VAL A 1 2818 ? 182.034 183.022 225.042 1.00 22.56  ? 2818 VAL A CB    1 
ATOM   10101 C  CG1   . VAL A 1 2818 ? 182.808 182.204 226.064 1.00 22.74  ? 2818 VAL A CG1   1 
ATOM   10102 C  CG2   . VAL A 1 2818 ? 182.708 182.966 223.679 1.00 24.70  ? 2818 VAL A CG2   1 
ATOM   10103 N  N     . GLU A 1 2819 ? 180.570 180.101 225.121 1.00 31.79  ? 2819 GLU A N     1 
ATOM   10104 C  CA    . GLU A 1 2819 ? 180.508 178.746 224.585 1.00 29.44  ? 2819 GLU A CA    1 
ATOM   10105 C  C     . GLU A 1 2819 ? 179.157 178.468 223.937 1.00 29.83  ? 2819 GLU A C     1 
ATOM   10106 O  O     . GLU A 1 2819 ? 179.087 177.829 222.882 1.00 22.25  ? 2819 GLU A O     1 
ATOM   10107 C  CB    . GLU A 1 2819 ? 180.800 177.735 225.692 1.00 36.97  ? 2819 GLU A CB    1 
ATOM   10108 C  CG    . GLU A 1 2819 ? 182.251 177.726 226.140 1.00 38.86  ? 2819 GLU A CG    1 
ATOM   10109 C  CD    . GLU A 1 2819 ? 182.500 178.647 227.318 1.00 46.77  ? 2819 GLU A CD    1 
ATOM   10110 O  OE1   . GLU A 1 2819 ? 181.516 179.152 227.898 1.00 46.76  ? 2819 GLU A OE1   1 
ATOM   10111 O  OE2   . GLU A 1 2819 ? 183.681 178.871 227.661 1.00 47.68  ? 2819 GLU A OE2   1 
ATOM   10112 N  N     . GLY A 1 2820 ? 178.073 178.948 224.548 1.00 29.83  ? 2820 GLY A N     1 
ATOM   10113 C  CA    . GLY A 1 2820 ? 176.764 178.786 223.938 1.00 23.38  ? 2820 GLY A CA    1 
ATOM   10114 C  C     . GLY A 1 2820 ? 176.625 179.552 222.635 1.00 23.52  ? 2820 GLY A C     1 
ATOM   10115 O  O     . GLY A 1 2820 ? 176.002 179.072 221.684 1.00 24.40  ? 2820 GLY A O     1 
ATOM   10116 N  N     . LEU A 1 2821 ? 177.197 180.757 222.576 1.00 24.74  ? 2821 LEU A N     1 
ATOM   10117 C  CA    . LEU A 1 2821 ? 177.185 181.520 221.331 1.00 18.80  ? 2821 LEU A CA    1 
ATOM   10118 C  C     . LEU A 1 2821 ? 177.952 180.792 220.236 1.00 15.93  ? 2821 LEU A C     1 
ATOM   10119 O  O     . LEU A 1 2821 ? 177.511 180.746 219.081 1.00 21.16  ? 2821 LEU A O     1 
ATOM   10120 C  CB    . LEU A 1 2821 ? 177.771 182.913 221.564 1.00 20.78  ? 2821 LEU A CB    1 
ATOM   10121 C  CG    . LEU A 1 2821 ? 178.101 183.744 220.322 1.00 19.84  ? 2821 LEU A CG    1 
ATOM   10122 C  CD1   . LEU A 1 2821 ? 176.859 184.430 219.778 1.00 13.37  ? 2821 LEU A CD1   1 
ATOM   10123 C  CD2   . LEU A 1 2821 ? 179.189 184.760 220.625 1.00 14.61  ? 2821 LEU A CD2   1 
ATOM   10124 N  N     . ILE A 1 2822 ? 179.100 180.209 220.581 1.00 14.31  ? 2822 ILE A N     1 
ATOM   10125 C  CA    . ILE A 1 2822 ? 179.872 179.449 219.603 1.00 17.63  ? 2822 ILE A CA    1 
ATOM   10126 C  C     . ILE A 1 2822 ? 179.100 178.210 219.167 1.00 18.17  ? 2822 ILE A C     1 
ATOM   10127 O  O     . ILE A 1 2822 ? 179.156 177.801 218.002 1.00 22.01  ? 2822 ILE A O     1 
ATOM   10128 C  CB    . ILE A 1 2822 ? 181.254 179.092 220.179 1.00 21.75  ? 2822 ILE A CB    1 
ATOM   10129 C  CG1   . ILE A 1 2822 ? 182.048 180.363 220.465 1.00 18.00  ? 2822 ILE A CG1   1 
ATOM   10130 C  CG2   . ILE A 1 2822 ? 182.031 178.223 219.212 1.00 18.75  ? 2822 ILE A CG2   1 
ATOM   10131 C  CD1   . ILE A 1 2822 ? 183.296 180.122 221.267 1.00 27.21  ? 2822 ILE A CD1   1 
ATOM   10132 N  N     . ARG A 1 2823 ? 178.369 177.590 220.097 1.00 16.31  ? 2823 ARG A N     1 
ATOM   10133 C  CA    . ARG A 1 2823 ? 177.532 176.449 219.743 1.00 16.69  ? 2823 ARG A CA    1 
ATOM   10134 C  C     . ARG A 1 2823 ? 176.439 176.846 218.760 1.00 14.51  ? 2823 ARG A C     1 
ATOM   10135 O  O     . ARG A 1 2823 ? 176.162 176.117 217.802 1.00 17.34  ? 2823 ARG A O     1 
ATOM   10136 C  CB    . ARG A 1 2823 ? 176.922 175.834 221.002 1.00 18.63  ? 2823 ARG A CB    1 
ATOM   10137 C  CG    . ARG A 1 2823 ? 176.436 174.410 220.814 1.00 16.11  ? 2823 ARG A CG    1 
ATOM   10138 C  CD    . ARG A 1 2823 ? 176.217 173.709 222.142 1.00 19.08  ? 2823 ARG A CD    1 
ATOM   10139 N  NE    . ARG A 1 2823 ? 175.626 172.388 221.958 1.00 24.31  ? 2823 ARG A NE    1 
ATOM   10140 C  CZ    . ARG A 1 2823 ? 176.288 171.323 221.530 1.00 21.75  ? 2823 ARG A CZ    1 
ATOM   10141 N  NH1   . ARG A 1 2823 ? 177.580 171.376 221.255 1.00 27.71  ? 2823 ARG A NH1   1 
ATOM   10142 N  NH2   . ARG A 1 2823 ? 175.637 170.175 221.374 1.00 26.10  ? 2823 ARG A NH2   1 
ATOM   10143 N  N     . ILE A 1 2824 ? 175.801 177.995 218.985 1.00 14.42  ? 2824 ILE A N     1 
ATOM   10144 C  CA    . ILE A 1 2824 ? 174.787 178.480 218.050 1.00 15.25  ? 2824 ILE A CA    1 
ATOM   10145 C  C     . ILE A 1 2824 ? 175.413 178.759 216.689 1.00 13.46  ? 2824 ILE A C     1 
ATOM   10146 O  O     . ILE A 1 2824 ? 174.840 178.433 215.640 1.00 18.77  ? 2824 ILE A O     1 
ATOM   10147 C  CB    . ILE A 1 2824 ? 174.086 179.727 218.618 1.00 13.11  ? 2824 ILE A CB    1 
ATOM   10148 C  CG1   . ILE A 1 2824 ? 173.342 179.381 219.908 1.00 18.26  ? 2824 ILE A CG1   1 
ATOM   10149 C  CG2   . ILE A 1 2824 ? 173.124 180.311 217.598 1.00 10.03  ? 2824 ILE A CG2   1 
ATOM   10150 C  CD1   . ILE A 1 2824 ? 172.845 180.590 220.667 1.00 22.18  ? 2824 ILE A CD1   1 
ATOM   10151 N  N     . TRP A 1 2825 ? 176.598 179.373 216.689 1.00 11.58  ? 2825 TRP A N     1 
ATOM   10152 C  CA    . TRP A 1 2825 ? 177.307 179.659 215.447 1.00 10.63  ? 2825 TRP A CA    1 
ATOM   10153 C  C     . TRP A 1 2825 ? 177.593 178.378 214.673 1.00 12.38  ? 2825 TRP A C     1 
ATOM   10154 O  O     . TRP A 1 2825 ? 177.349 178.298 213.462 1.00 11.74  ? 2825 TRP A O     1 
ATOM   10155 C  CB    . TRP A 1 2825 ? 178.599 180.412 215.777 1.00 9.91   ? 2825 TRP A CB    1 
ATOM   10156 C  CG    . TRP A 1 2825 ? 179.546 180.628 214.638 1.00 11.85  ? 2825 TRP A CG    1 
ATOM   10157 C  CD1   . TRP A 1 2825 ? 179.576 181.697 213.794 1.00 10.06  ? 2825 TRP A CD1   1 
ATOM   10158 C  CD2   . TRP A 1 2825 ? 180.627 179.775 214.245 1.00 11.04  ? 2825 TRP A CD2   1 
ATOM   10159 N  NE1   . TRP A 1 2825 ? 180.598 181.556 212.889 1.00 11.34  ? 2825 TRP A NE1   1 
ATOM   10160 C  CE2   . TRP A 1 2825 ? 181.257 180.384 213.143 1.00 11.44  ? 2825 TRP A CE2   1 
ATOM   10161 C  CE3   . TRP A 1 2825 ? 181.117 178.552 214.710 1.00 13.75  ? 2825 TRP A CE3   1 
ATOM   10162 C  CZ2   . TRP A 1 2825 ? 182.351 179.811 212.500 1.00 14.85  ? 2825 TRP A CZ2   1 
ATOM   10163 C  CZ3   . TRP A 1 2825 ? 182.202 177.985 214.069 1.00 15.96  ? 2825 TRP A CZ3   1 
ATOM   10164 C  CH2   . TRP A 1 2825 ? 182.807 178.614 212.977 1.00 17.95  ? 2825 TRP A CH2   1 
ATOM   10165 N  N     . ALA A 1 2826 ? 178.085 177.351 215.368 1.00 12.56  ? 2826 ALA A N     1 
ATOM   10166 C  CA    . ALA A 1 2826 ? 178.391 176.079 214.722 1.00 11.99  ? 2826 ALA A CA    1 
ATOM   10167 C  C     . ALA A 1 2826 ? 177.130 175.379 214.232 1.00 12.60  ? 2826 ALA A C     1 
ATOM   10168 O  O     . ALA A 1 2826 ? 177.131 174.771 213.156 1.00 12.23  ? 2826 ALA A O     1 
ATOM   10169 C  CB    . ALA A 1 2826 ? 179.165 175.178 215.681 1.00 17.93  ? 2826 ALA A CB    1 
ATOM   10170 N  N     . HIS A 1 2827 ? 176.048 175.439 215.011 1.00 10.19  ? 2827 HIS A N     1 
ATOM   10171 C  CA    . HIS A 1 2827 ? 174.798 174.819 214.587 1.00 9.67   ? 2827 HIS A CA    1 
ATOM   10172 C  C     . HIS A 1 2827 ? 174.265 175.471 213.320 1.00 12.59  ? 2827 HIS A C     1 
ATOM   10173 O  O     . HIS A 1 2827 ? 173.820 174.781 212.395 1.00 13.13  ? 2827 HIS A O     1 
ATOM   10174 C  CB    . HIS A 1 2827 ? 173.763 174.907 215.707 1.00 12.19  ? 2827 HIS A CB    1 
ATOM   10175 C  CG    . HIS A 1 2827 ? 172.413 174.387 215.324 1.00 11.98  ? 2827 HIS A CG    1 
ATOM   10176 N  ND1   . HIS A 1 2827 ? 172.151 173.044 215.160 1.00 14.26  ? 2827 HIS A ND1   1 
ATOM   10177 C  CD2   . HIS A 1 2827 ? 171.250 175.031 215.065 1.00 12.54  ? 2827 HIS A CD2   1 
ATOM   10178 C  CE1   . HIS A 1 2827 ? 170.885 172.883 214.821 1.00 15.19  ? 2827 HIS A CE1   1 
ATOM   10179 N  NE2   . HIS A 1 2827 ? 170.316 174.073 214.755 1.00 15.10  ? 2827 HIS A NE2   1 
ATOM   10180 N  N     . GLU A 1 2828 ? 174.303 176.803 213.258 1.00 13.79  ? 2828 GLU A N     1 
ATOM   10181 C  CA    . GLU A 1 2828 ? 173.838 177.490 212.058 1.00 9.80   ? 2828 GLU A CA    1 
ATOM   10182 C  C     . GLU A 1 2828 ? 174.754 177.210 210.874 1.00 10.70  ? 2828 GLU A C     1 
ATOM   10183 O  O     . GLU A 1 2828 ? 174.283 177.065 209.739 1.00 14.69  ? 2828 GLU A O     1 
ATOM   10184 C  CB    . GLU A 1 2828 ? 173.722 178.990 212.324 1.00 11.14  ? 2828 GLU A CB    1 
ATOM   10185 C  CG    . GLU A 1 2828 ? 172.671 179.403 213.369 1.00 14.29  ? 2828 GLU A CG    1 
ATOM   10186 C  CD    . GLU A 1 2828 ? 171.271 178.824 213.153 1.00 25.66  ? 2828 GLU A CD    1 
ATOM   10187 O  OE1   . GLU A 1 2828 ? 170.412 179.044 214.032 1.00 32.11  ? 2828 GLU A OE1   1 
ATOM   10188 O  OE2   . GLU A 1 2828 ? 170.994 178.206 212.104 1.00 21.56  ? 2828 GLU A OE2   1 
ATOM   10189 N  N     . ALA A 1 2829 ? 176.064 177.114 211.117 1.00 8.33   ? 2829 ALA A N     1 
ATOM   10190 C  CA    . ALA A 1 2829 ? 176.981 176.733 210.048 1.00 8.15   ? 2829 ALA A CA    1 
ATOM   10191 C  C     . ALA A 1 2829 ? 176.655 175.344 209.517 1.00 13.42  ? 2829 ALA A C     1 
ATOM   10192 O  O     . ALA A 1 2829 ? 176.714 175.104 208.306 1.00 18.47  ? 2829 ALA A O     1 
ATOM   10193 C  CB    . ALA A 1 2829 ? 178.423 176.789 210.546 1.00 10.74  ? 2829 ALA A CB    1 
ATOM   10194 N  N     . LEU A 1 2830 ? 176.327 174.411 210.412 1.00 12.70  ? 2830 LEU A N     1 
ATOM   10195 C  CA    . LEU A 1 2830 ? 175.934 173.073 209.982 1.00 8.25   ? 2830 LEU A CA    1 
ATOM   10196 C  C     . LEU A 1 2830 ? 174.647 173.110 209.170 1.00 9.80   ? 2830 LEU A C     1 
ATOM   10197 O  O     . LEU A 1 2830 ? 174.535 172.439 208.138 1.00 12.75  ? 2830 LEU A O     1 
ATOM   10198 C  CB    . LEU A 1 2830 ? 175.771 172.161 211.196 1.00 11.62  ? 2830 LEU A CB    1 
ATOM   10199 C  CG    . LEU A 1 2830 ? 177.067 171.711 211.866 1.00 13.76  ? 2830 LEU A CG    1 
ATOM   10200 C  CD1   . LEU A 1 2830 ? 176.779 170.962 213.157 1.00 11.25  ? 2830 LEU A CD1   1 
ATOM   10201 C  CD2   . LEU A 1 2830 ? 177.870 170.855 210.912 1.00 13.67  ? 2830 LEU A CD2   1 
ATOM   10202 N  N     . ARG A 1 2831 ? 173.662 173.889 209.619 1.00 12.82  ? 2831 ARG A N     1 
ATOM   10203 C  CA    . ARG A 1 2831 ? 172.385 173.943 208.917 1.00 10.81  ? 2831 ARG A CA    1 
ATOM   10204 C  C     . ARG A 1 2831 ? 172.482 174.677 207.587 1.00 9.82   ? 2831 ARG A C     1 
ATOM   10205 O  O     . ARG A 1 2831 ? 171.610 174.497 206.731 1.00 11.87  ? 2831 ARG A O     1 
ATOM   10206 C  CB    . ARG A 1 2831 ? 171.321 174.601 209.796 1.00 11.44  ? 2831 ARG A CB    1 
ATOM   10207 C  CG    . ARG A 1 2831 ? 171.068 173.876 211.108 1.00 11.01  ? 2831 ARG A CG    1 
ATOM   10208 C  CD    . ARG A 1 2831 ? 170.238 172.612 210.917 1.00 10.47  ? 2831 ARG A CD    1 
ATOM   10209 N  NE    . ARG A 1 2831 ? 171.042 171.491 210.441 1.00 11.17  ? 2831 ARG A NE    1 
ATOM   10210 C  CZ    . ARG A 1 2831 ? 171.934 170.837 211.172 1.00 10.77  ? 2831 ARG A CZ    1 
ATOM   10211 N  NH1   . ARG A 1 2831 ? 172.158 171.152 212.436 1.00 8.32   ? 2831 ARG A NH1   1 
ATOM   10212 N  NH2   . ARG A 1 2831 ? 172.622 169.843 210.618 1.00 13.66  ? 2831 ARG A NH2   1 
ATOM   10213 N  N     . LEU A 1 2832 ? 173.512 175.497 207.395 1.00 9.56   ? 2832 LEU A N     1 
ATOM   10214 C  CA    . LEU A 1 2832 ? 173.682 176.237 206.151 1.00 8.01   ? 2832 LEU A CA    1 
ATOM   10215 C  C     . LEU A 1 2832 ? 174.594 175.546 205.149 1.00 9.72   ? 2832 LEU A C     1 
ATOM   10216 O  O     . LEU A 1 2832 ? 174.238 175.433 203.973 1.00 15.90  ? 2832 LEU A O     1 
ATOM   10217 C  CB    . LEU A 1 2832 ? 174.237 177.631 206.444 1.00 9.87   ? 2832 LEU A CB    1 
ATOM   10218 C  CG    . LEU A 1 2832 ? 173.267 178.601 207.107 1.00 10.76  ? 2832 LEU A CG    1 
ATOM   10219 C  CD1   . LEU A 1 2832 ? 173.978 179.896 207.383 1.00 12.19  ? 2832 LEU A CD1   1 
ATOM   10220 C  CD2   . LEU A 1 2832 ? 172.065 178.828 206.223 1.00 11.85  ? 2832 LEU A CD2   1 
ATOM   10221 N  N     . PHE A 1 2833 ? 175.766 175.085 205.584 1.00 8.69   ? 2833 PHE A N     1 
ATOM   10222 C  CA    . PHE A 1 2833 ? 176.792 174.607 204.670 1.00 11.27  ? 2833 PHE A CA    1 
ATOM   10223 C  C     . PHE A 1 2833 ? 176.858 173.091 204.553 1.00 14.04  ? 2833 PHE A C     1 
ATOM   10224 O  O     . PHE A 1 2833 ? 177.474 172.589 203.607 1.00 16.16  ? 2833 PHE A O     1 
ATOM   10225 C  CB    . PHE A 1 2833 ? 178.166 175.129 205.108 1.00 11.57  ? 2833 PHE A CB    1 
ATOM   10226 C  CG    . PHE A 1 2833 ? 178.279 176.626 205.086 1.00 11.15  ? 2833 PHE A CG    1 
ATOM   10227 C  CD1   . PHE A 1 2833 ? 178.713 177.283 203.949 1.00 9.43   ? 2833 PHE A CD1   1 
ATOM   10228 C  CD2   . PHE A 1 2833 ? 177.947 177.376 206.200 1.00 9.05   ? 2833 PHE A CD2   1 
ATOM   10229 C  CE1   . PHE A 1 2833 ? 178.817 178.658 203.925 1.00 10.53  ? 2833 PHE A CE1   1 
ATOM   10230 C  CE2   . PHE A 1 2833 ? 178.048 178.750 206.182 1.00 8.46   ? 2833 PHE A CE2   1 
ATOM   10231 C  CZ    . PHE A 1 2833 ? 178.484 179.391 205.043 1.00 13.17  ? 2833 PHE A CZ    1 
ATOM   10232 N  N     . GLN A 1 2834 ? 176.245 172.351 205.476 1.00 12.75  ? 2834 GLN A N     1 
ATOM   10233 C  CA    . GLN A 1 2834 ? 176.368 170.900 205.485 1.00 11.20  ? 2834 GLN A CA    1 
ATOM   10234 C  C     . GLN A 1 2834 ? 175.110 170.174 205.030 1.00 13.53  ? 2834 GLN A C     1 
ATOM   10235 O  O     . GLN A 1 2834 ? 175.205 169.018 204.606 1.00 18.38  ? 2834 GLN A O     1 
ATOM   10236 C  CB    . GLN A 1 2834 ? 176.742 170.410 206.889 1.00 10.63  ? 2834 GLN A CB    1 
ATOM   10237 C  CG    . GLN A 1 2834 ? 177.411 169.053 206.900 1.00 12.68  ? 2834 GLN A CG    1 
ATOM   10238 C  CD    . GLN A 1 2834 ? 177.545 168.475 208.289 1.00 17.92  ? 2834 GLN A CD    1 
ATOM   10239 O  OE1   . GLN A 1 2834 ? 176.564 168.353 209.020 1.00 24.65  ? 2834 GLN A OE1   1 
ATOM   10240 N  NE2   . GLN A 1 2834 ? 178.764 168.103 208.658 1.00 17.27  ? 2834 GLN A NE2   1 
ATOM   10241 N  N     . ASP A 1 2835 ? 173.944 170.818 205.101 1.00 11.95  ? 2835 ASP A N     1 
ATOM   10242 C  CA    . ASP A 1 2835 ? 172.696 170.124 204.797 1.00 9.49   ? 2835 ASP A CA    1 
ATOM   10243 C  C     . ASP A 1 2835 ? 172.603 169.754 203.321 1.00 12.03  ? 2835 ASP A C     1 
ATOM   10244 O  O     . ASP A 1 2835 ? 172.036 168.713 202.972 1.00 16.31  ? 2835 ASP A O     1 
ATOM   10245 C  CB    . ASP A 1 2835 ? 171.505 170.985 205.210 1.00 13.26  ? 2835 ASP A CB    1 
ATOM   10246 C  CG    . ASP A 1 2835 ? 171.283 170.987 206.708 1.00 22.48  ? 2835 ASP A CG    1 
ATOM   10247 O  OD1   . ASP A 1 2835 ? 172.121 170.413 207.433 1.00 19.98  ? 2835 ASP A OD1   1 
ATOM   10248 O  OD2   . ASP A 1 2835 ? 170.270 171.560 207.161 1.00 20.98  ? 2835 ASP A OD2   1 
ATOM   10249 N  N     . ARG A 1 2836 ? 173.145 170.594 202.441 1.00 13.02  ? 2836 ARG A N     1 
ATOM   10250 C  CA    . ARG A 1 2836 ? 173.060 170.351 201.008 1.00 11.88  ? 2836 ARG A CA    1 
ATOM   10251 C  C     . ARG A 1 2836 ? 174.167 169.447 200.484 1.00 14.46  ? 2836 ARG A C     1 
ATOM   10252 O  O     . ARG A 1 2836 ? 174.106 169.038 199.319 1.00 20.37  ? 2836 ARG A O     1 
ATOM   10253 C  CB    . ARG A 1 2836 ? 173.091 171.678 200.249 1.00 16.28  ? 2836 ARG A CB    1 
ATOM   10254 C  CG    . ARG A 1 2836 ? 174.485 172.251 200.074 1.00 16.40  ? 2836 ARG A CG    1 
ATOM   10255 C  CD    . ARG A 1 2836 ? 174.441 173.578 199.348 1.00 16.44  ? 2836 ARG A CD    1 
ATOM   10256 N  NE    . ARG A 1 2836 ? 173.995 174.655 200.222 1.00 19.73  ? 2836 ARG A NE    1 
ATOM   10257 C  CZ    . ARG A 1 2836 ? 173.757 175.895 199.819 1.00 13.99  ? 2836 ARG A CZ    1 
ATOM   10258 N  NH1   . ARG A 1 2836 ? 173.911 176.252 198.556 1.00 15.02  ? 2836 ARG A NH1   1 
ATOM   10259 N  NH2   . ARG A 1 2836 ? 173.352 176.798 200.706 1.00 12.44  ? 2836 ARG A NH2   1 
ATOM   10260 N  N     . LEU A 1 2837 ? 175.166 169.131 201.300 1.00 13.59  ? 2837 LEU A N     1 
ATOM   10261 C  CA    . LEU A 1 2837 ? 176.281 168.314 200.842 1.00 13.50  ? 2837 LEU A CA    1 
ATOM   10262 C  C     . LEU A 1 2837 ? 175.825 166.892 200.539 1.00 13.46  ? 2837 LEU A C     1 
ATOM   10263 O  O     . LEU A 1 2837 ? 174.963 166.337 201.225 1.00 17.12  ? 2837 LEU A O     1 
ATOM   10264 C  CB    . LEU A 1 2837 ? 177.390 168.304 201.889 1.00 15.91  ? 2837 LEU A CB    1 
ATOM   10265 C  CG    . LEU A 1 2837 ? 178.044 169.663 202.136 1.00 12.49  ? 2837 LEU A CG    1 
ATOM   10266 C  CD1   . LEU A 1 2837 ? 179.185 169.526 203.116 1.00 11.11  ? 2837 LEU A CD1   1 
ATOM   10267 C  CD2   . LEU A 1 2837 ? 178.531 170.266 200.829 1.00 11.01  ? 2837 LEU A CD2   1 
ATOM   10268 N  N     . VAL A 1 2838 ? 176.417 166.301 199.503 1.00 15.29  ? 2838 VAL A N     1 
ATOM   10269 C  CA    . VAL A 1 2838 ? 176.014 164.985 199.023 1.00 15.83  ? 2838 VAL A CA    1 
ATOM   10270 C  C     . VAL A 1 2838 ? 176.882 163.901 199.648 1.00 18.74  ? 2838 VAL A C     1 
ATOM   10271 O  O     . VAL A 1 2838 ? 176.369 162.941 200.233 1.00 20.53  ? 2838 VAL A O     1 
ATOM   10272 C  CB    . VAL A 1 2838 ? 176.082 164.918 197.486 1.00 11.99  ? 2838 VAL A CB    1 
ATOM   10273 C  CG1   . VAL A 1 2838 ? 175.553 163.586 196.989 1.00 11.91  ? 2838 VAL A CG1   1 
ATOM   10274 C  CG2   . VAL A 1 2838 ? 175.304 166.068 196.872 1.00 12.14  ? 2838 VAL A CG2   1 
ATOM   10275 N  N     . GLU A 1 2839 ? 178.198 164.043 199.528 1.00 20.15  ? 2839 GLU A N     1 
ATOM   10276 C  CA    . GLU A 1 2839 ? 179.114 163.000 199.961 1.00 20.50  ? 2839 GLU A CA    1 
ATOM   10277 C  C     . GLU A 1 2839 ? 179.419 163.106 201.451 1.00 24.29  ? 2839 GLU A C     1 
ATOM   10278 O  O     . GLU A 1 2839 ? 179.330 164.179 202.054 1.00 26.03  ? 2839 GLU A O     1 
ATOM   10279 C  CB    . GLU A 1 2839 ? 180.414 163.065 199.160 1.00 24.26  ? 2839 GLU A CB    1 
ATOM   10280 C  CG    . GLU A 1 2839 ? 180.212 163.313 197.676 1.00 25.03  ? 2839 GLU A CG    1 
ATOM   10281 C  CD    . GLU A 1 2839 ? 179.788 162.066 196.927 1.00 30.82  ? 2839 GLU A CD    1 
ATOM   10282 O  OE1   . GLU A 1 2839 ? 179.797 160.974 197.531 1.00 32.89  ? 2839 GLU A OE1   1 
ATOM   10283 O  OE2   . GLU A 1 2839 ? 179.449 162.178 195.731 1.00 34.24  ? 2839 GLU A OE2   1 
ATOM   10284 N  N     . ASP A 1 2840 ? 179.781 161.964 202.042 1.00 29.84  ? 2840 ASP A N     1 
ATOM   10285 C  CA    . ASP A 1 2840 ? 180.144 161.928 203.455 1.00 25.90  ? 2840 ASP A CA    1 
ATOM   10286 C  C     . ASP A 1 2840 ? 181.429 162.697 203.729 1.00 30.51  ? 2840 ASP A C     1 
ATOM   10287 O  O     . ASP A 1 2840 ? 181.541 163.366 204.764 1.00 29.88  ? 2840 ASP A O     1 
ATOM   10288 C  CB    . ASP A 1 2840 ? 180.297 160.480 203.920 1.00 37.83  ? 2840 ASP A CB    1 
ATOM   10289 C  CG    . ASP A 1 2840 ? 178.979 159.734 203.955 1.00 53.74  ? 2840 ASP A CG    1 
ATOM   10290 O  OD1   . ASP A 1 2840 ? 177.934 160.380 204.170 1.00 56.33  ? 2840 ASP A OD1   1 
ATOM   10291 O  OD2   . ASP A 1 2840 ? 178.988 158.499 203.768 1.00 54.87  ? 2840 ASP A OD2   1 
ATOM   10292 N  N     . GLU A 1 2841 ? 182.411 162.601 202.829 1.00 30.22  ? 2841 GLU A N     1 
ATOM   10293 C  CA    . GLU A 1 2841 ? 183.686 163.276 203.049 1.00 32.22  ? 2841 GLU A CA    1 
ATOM   10294 C  C     . GLU A 1 2841 ? 183.526 164.789 203.057 1.00 32.24  ? 2841 GLU A C     1 
ATOM   10295 O  O     . GLU A 1 2841 ? 184.234 165.479 203.797 1.00 36.52  ? 2841 GLU A O     1 
ATOM   10296 C  CB    . GLU A 1 2841 ? 184.703 162.841 201.992 1.00 35.30  ? 2841 GLU A CB    1 
ATOM   10297 C  CG    . GLU A 1 2841 ? 184.308 163.153 200.558 1.00 41.20  ? 2841 GLU A CG    1 
ATOM   10298 C  CD    . GLU A 1 2841 ? 184.889 164.464 200.063 1.00 50.33  ? 2841 GLU A CD    1 
ATOM   10299 O  OE1   . GLU A 1 2841 ? 185.850 164.963 200.686 1.00 47.62  ? 2841 GLU A OE1   1 
ATOM   10300 O  OE2   . GLU A 1 2841 ? 184.387 164.995 199.050 1.00 44.25  ? 2841 GLU A OE2   1 
ATOM   10301 N  N     . GLU A 1 2842 ? 182.597 165.320 202.259 1.00 29.80  ? 2842 GLU A N     1 
ATOM   10302 C  CA    . GLU A 1 2842 ? 182.329 166.753 202.291 1.00 25.76  ? 2842 GLU A CA    1 
ATOM   10303 C  C     . GLU A 1 2842 ? 181.797 167.182 203.653 1.00 20.96  ? 2842 GLU A C     1 
ATOM   10304 O  O     . GLU A 1 2842 ? 182.208 168.215 204.194 1.00 25.31  ? 2842 GLU A O     1 
ATOM   10305 C  CB    . GLU A 1 2842 ? 181.342 167.121 201.185 1.00 21.29  ? 2842 GLU A CB    1 
ATOM   10306 C  CG    . GLU A 1 2842 ? 181.913 166.991 199.784 1.00 21.50  ? 2842 GLU A CG    1 
ATOM   10307 C  CD    . GLU A 1 2842 ? 180.839 166.945 198.719 1.00 32.94  ? 2842 GLU A CD    1 
ATOM   10308 O  OE1   . GLU A 1 2842 ? 179.644 166.946 199.077 1.00 31.83  ? 2842 GLU A OE1   1 
ATOM   10309 O  OE2   . GLU A 1 2842 ? 181.191 166.909 197.521 1.00 37.88  ? 2842 GLU A OE2   1 
ATOM   10310 N  N     . ARG A 1 2843 ? 180.888 166.394 204.229 1.00 15.71  ? 2843 ARG A N     1 
ATOM   10311 C  CA    . ARG A 1 2843 ? 180.345 166.734 205.539 1.00 18.21  ? 2843 ARG A CA    1 
ATOM   10312 C  C     . ARG A 1 2843 ? 181.398 166.586 206.633 1.00 24.86  ? 2843 ARG A C     1 
ATOM   10313 O  O     . ARG A 1 2843 ? 181.423 167.372 207.589 1.00 25.54  ? 2843 ARG A O     1 
ATOM   10314 C  CB    . ARG A 1 2843 ? 179.115 165.873 205.832 1.00 20.04  ? 2843 ARG A CB    1 
ATOM   10315 C  CG    . ARG A 1 2843 ? 177.928 166.212 204.941 1.00 15.72  ? 2843 ARG A CG    1 
ATOM   10316 C  CD    . ARG A 1 2843 ? 176.650 165.520 205.383 1.00 18.84  ? 2843 ARG A CD    1 
ATOM   10317 N  NE    . ARG A 1 2843 ? 176.714 164.069 205.270 1.00 23.31  ? 2843 ARG A NE    1 
ATOM   10318 C  CZ    . ARG A 1 2843 ? 176.380 163.393 204.180 1.00 31.36  ? 2843 ARG A CZ    1 
ATOM   10319 N  NH1   . ARG A 1 2843 ? 175.966 164.008 203.085 1.00 20.64  ? 2843 ARG A NH1   1 
ATOM   10320 N  NH2   . ARG A 1 2843 ? 176.456 162.066 204.190 1.00 34.88  ? 2843 ARG A NH2   1 
ATOM   10321 N  N     . ARG A 1 2844 ? 182.278 165.590 206.509 1.00 27.28  ? 2844 ARG A N     1 
ATOM   10322 C  CA    . ARG A 1 2844 ? 183.385 165.465 207.453 1.00 25.09  ? 2844 ARG A CA    1 
ATOM   10323 C  C     . ARG A 1 2844 ? 184.316 166.670 207.369 1.00 24.01  ? 2844 ARG A C     1 
ATOM   10324 O  O     . ARG A 1 2844 ? 184.766 167.194 208.397 1.00 25.28  ? 2844 ARG A O     1 
ATOM   10325 C  CB    . ARG A 1 2844 ? 184.155 164.172 207.190 1.00 30.79  ? 2844 ARG A CB    1 
ATOM   10326 C  CG    . ARG A 1 2844 ? 184.703 163.508 208.442 1.00 34.81  ? 2844 ARG A CG    1 
ATOM   10327 C  CD    . ARG A 1 2844 ? 185.547 162.276 208.125 1.00 34.70  ? 2844 ARG A CD    1 
ATOM   10328 N  NE    . ARG A 1 2844 ? 186.478 162.489 207.022 1.00 49.49  ? 2844 ARG A NE    1 
ATOM   10329 C  CZ    . ARG A 1 2844 ? 186.279 162.075 205.778 1.00 54.33  ? 2844 ARG A CZ    1 
ATOM   10330 N  NH1   . ARG A 1 2844 ? 185.190 161.404 205.438 1.00 42.24  ? 2844 ARG A NH1   1 
ATOM   10331 N  NH2   . ARG A 1 2844 ? 187.196 162.339 204.851 1.00 44.59  ? 2844 ARG A NH2   1 
ATOM   10332 N  N     . TRP A 1 2845 ? 184.615 167.117 206.146 1.00 21.79  ? 2845 TRP A N     1 
ATOM   10333 C  CA    . TRP A 1 2845 ? 185.395 168.334 205.951 1.00 21.95  ? 2845 TRP A CA    1 
ATOM   10334 C  C     . TRP A 1 2845 ? 184.718 169.527 206.606 1.00 21.32  ? 2845 TRP A C     1 
ATOM   10335 O  O     . TRP A 1 2845 ? 185.375 170.343 207.265 1.00 24.17  ? 2845 TRP A O     1 
ATOM   10336 C  CB    . TRP A 1 2845 ? 185.588 168.579 204.453 1.00 23.97  ? 2845 TRP A CB    1 
ATOM   10337 C  CG    . TRP A 1 2845 ? 186.402 169.790 204.096 1.00 26.83  ? 2845 TRP A CG    1 
ATOM   10338 C  CD1   . TRP A 1 2845 ? 187.722 169.818 203.764 1.00 23.71  ? 2845 TRP A CD1   1 
ATOM   10339 C  CD2   . TRP A 1 2845 ? 185.936 171.144 204.005 1.00 25.99  ? 2845 TRP A CD2   1 
ATOM   10340 N  NE1   . TRP A 1 2845 ? 188.113 171.105 203.485 1.00 23.17  ? 2845 TRP A NE1   1 
ATOM   10341 C  CE2   . TRP A 1 2845 ? 187.034 171.937 203.624 1.00 21.36  ? 2845 TRP A CE2   1 
ATOM   10342 C  CE3   . TRP A 1 2845 ? 184.700 171.761 204.215 1.00 22.41  ? 2845 TRP A CE3   1 
ATOM   10343 C  CZ2   . TRP A 1 2845 ? 186.932 173.316 203.449 1.00 24.65  ? 2845 TRP A CZ2   1 
ATOM   10344 C  CZ3   . TRP A 1 2845 ? 184.602 173.128 204.043 1.00 16.45  ? 2845 TRP A CZ3   1 
ATOM   10345 C  CH2   . TRP A 1 2845 ? 185.711 173.891 203.665 1.00 21.02  ? 2845 TRP A CH2   1 
ATOM   10346 N  N     . THR A 1 2846 ? 183.401 169.646 206.427 1.00 20.83  ? 2846 THR A N     1 
ATOM   10347 C  CA    . THR A 1 2846 ? 182.668 170.758 207.021 1.00 18.83  ? 2846 THR A CA    1 
ATOM   10348 C  C     . THR A 1 2846 ? 182.768 170.737 208.540 1.00 22.98  ? 2846 THR A C     1 
ATOM   10349 O  O     . THR A 1 2846 ? 183.042 171.768 209.161 1.00 31.96  ? 2846 THR A O     1 
ATOM   10350 C  CB    . THR A 1 2846 ? 181.207 170.719 206.575 1.00 16.45  ? 2846 THR A CB    1 
ATOM   10351 O  OG1   . THR A 1 2846 ? 181.140 170.888 205.156 1.00 18.04  ? 2846 THR A OG1   1 
ATOM   10352 C  CG2   . THR A 1 2846 ? 180.414 171.828 207.241 1.00 19.63  ? 2846 THR A CG2   1 
ATOM   10353 N  N     . ASP A 1 2847 ? 182.574 169.567 209.155 1.00 20.47  ? 2847 ASP A N     1 
ATOM   10354 C  CA    . ASP A 1 2847 ? 182.689 169.465 210.609 1.00 24.30  ? 2847 ASP A CA    1 
ATOM   10355 C  C     . ASP A 1 2847 ? 184.086 169.849 211.079 1.00 31.68  ? 2847 ASP A C     1 
ATOM   10356 O  O     . ASP A 1 2847 ? 184.251 170.675 211.992 1.00 33.33  ? 2847 ASP A O     1 
ATOM   10357 C  CB    . ASP A 1 2847 ? 182.358 168.045 211.068 1.00 26.01  ? 2847 ASP A CB    1 
ATOM   10358 C  CG    . ASP A 1 2847 ? 180.901 167.696 210.890 1.00 36.24  ? 2847 ASP A CG    1 
ATOM   10359 O  OD1   . ASP A 1 2847 ? 180.059 168.613 210.952 1.00 39.65  ? 2847 ASP A OD1   1 
ATOM   10360 O  OD2   . ASP A 1 2847 ? 180.596 166.502 210.691 1.00 45.96  ? 2847 ASP A OD2   1 
ATOM   10361 N  N     . GLU A 1 2848 ? 185.109 169.253 210.461 1.00 29.89  ? 2848 GLU A N     1 
ATOM   10362 C  CA    . GLU A 1 2848 ? 186.475 169.475 210.914 1.00 28.77  ? 2848 GLU A CA    1 
ATOM   10363 C  C     . GLU A 1 2848 ? 186.869 170.936 210.776 1.00 32.02  ? 2848 GLU A C     1 
ATOM   10364 O  O     . GLU A 1 2848 ? 187.482 171.509 211.684 1.00 35.91  ? 2848 GLU A O     1 
ATOM   10365 C  CB    . GLU A 1 2848 ? 187.439 168.580 210.136 1.00 29.90  ? 2848 GLU A CB    1 
ATOM   10366 C  CG    . GLU A 1 2848 ? 188.889 168.701 210.576 1.00 44.87  ? 2848 GLU A CG    1 
ATOM   10367 C  CD    . GLU A 1 2848 ? 189.113 168.218 211.998 1.00 51.21  ? 2848 GLU A CD    1 
ATOM   10368 O  OE1   . GLU A 1 2848 ? 188.331 167.368 212.473 1.00 40.98  ? 2848 GLU A OE1   1 
ATOM   10369 O  OE2   . GLU A 1 2848 ? 190.073 168.691 212.642 1.00 56.78  ? 2848 GLU A OE2   1 
ATOM   10370 N  N     . ASN A 1 2849 ? 186.510 171.572 209.661 1.00 32.31  ? 2849 ASN A N     1 
ATOM   10371 C  CA    . ASN A 1 2849 ? 186.923 172.956 209.481 1.00 27.25  ? 2849 ASN A CA    1 
ATOM   10372 C  C     . ASN A 1 2849 ? 186.041 173.935 210.244 1.00 25.23  ? 2849 ASN A C     1 
ATOM   10373 O  O     . ASN A 1 2849 ? 186.505 175.026 210.580 1.00 30.86  ? 2849 ASN A O     1 
ATOM   10374 C  CB    . ASN A 1 2849 ? 186.984 173.302 207.997 1.00 25.18  ? 2849 ASN A CB    1 
ATOM   10375 C  CG    . ASN A 1 2849 ? 188.264 172.810 207.353 1.00 32.41  ? 2849 ASN A CG    1 
ATOM   10376 O  OD1   . ASN A 1 2849 ? 189.119 172.228 208.020 1.00 37.20  ? 2849 ASN A OD1   1 
ATOM   10377 N  ND2   . ASN A 1 2849 ? 188.417 173.064 206.066 1.00 34.05  ? 2849 ASN A ND2   1 
ATOM   10378 N  N     . ILE A 1 2850 ? 184.798 173.570 210.567 1.00 26.23  ? 2850 ILE A N     1 
ATOM   10379 C  CA    . ILE A 1 2850 ? 184.031 174.371 211.516 1.00 27.22  ? 2850 ILE A CA    1 
ATOM   10380 C  C     . ILE A 1 2850 ? 184.739 174.391 212.862 1.00 28.60  ? 2850 ILE A C     1 
ATOM   10381 O  O     . ILE A 1 2850 ? 184.927 175.452 213.474 1.00 33.96  ? 2850 ILE A O     1 
ATOM   10382 C  CB    . ILE A 1 2850 ? 182.594 173.835 211.643 1.00 22.92  ? 2850 ILE A CB    1 
ATOM   10383 C  CG1   . ILE A 1 2850 ? 181.732 174.327 210.483 1.00 23.67  ? 2850 ILE A CG1   1 
ATOM   10384 C  CG2   . ILE A 1 2850 ? 181.982 174.248 212.971 1.00 25.90  ? 2850 ILE A CG2   1 
ATOM   10385 C  CD1   . ILE A 1 2850 ? 180.381 173.662 210.410 1.00 21.02  ? 2850 ILE A CD1   1 
ATOM   10386 N  N     . ASP A 1 2851 ? 185.168 173.215 213.328 1.00 32.86  ? 2851 ASP A N     1 
ATOM   10387 C  CA    . ASP A 1 2851 ? 185.920 173.156 214.579 1.00 33.80  ? 2851 ASP A CA    1 
ATOM   10388 C  C     . ASP A 1 2851 ? 187.213 173.957 214.479 1.00 32.04  ? 2851 ASP A C     1 
ATOM   10389 O  O     . ASP A 1 2851 ? 187.569 174.695 215.406 1.00 29.54  ? 2851 ASP A O     1 
ATOM   10390 C  CB    . ASP A 1 2851 ? 186.217 171.703 214.946 1.00 37.58  ? 2851 ASP A CB    1 
ATOM   10391 C  CG    . ASP A 1 2851 ? 184.960 170.893 215.183 1.00 48.09  ? 2851 ASP A CG    1 
ATOM   10392 O  OD1   . ASP A 1 2851 ? 183.870 171.496 215.263 1.00 49.11  ? 2851 ASP A OD1   1 
ATOM   10393 O  OD2   . ASP A 1 2851 ? 185.062 169.652 215.292 1.00 52.38  ? 2851 ASP A OD2   1 
ATOM   10394 N  N     . THR A 1 2852 ? 187.924 173.826 213.357 1.00 30.09  ? 2852 THR A N     1 
ATOM   10395 C  CA    . THR A 1 2852 ? 189.203 174.510 213.190 1.00 25.12  ? 2852 THR A CA    1 
ATOM   10396 C  C     . THR A 1 2852 ? 189.030 176.024 213.210 1.00 27.79  ? 2852 THR A C     1 
ATOM   10397 O  O     . THR A 1 2852 ? 189.782 176.736 213.885 1.00 34.89  ? 2852 THR A O     1 
ATOM   10398 C  CB    . THR A 1 2852 ? 189.864 174.065 211.886 1.00 26.01  ? 2852 THR A CB    1 
ATOM   10399 O  OG1   . THR A 1 2852 ? 189.896 172.634 211.830 1.00 23.19  ? 2852 THR A OG1   1 
ATOM   10400 C  CG2   . THR A 1 2852 ? 191.282 174.603 211.798 1.00 28.62  ? 2852 THR A CG2   1 
ATOM   10401 N  N     . VAL A 1 2853 ? 188.039 176.535 212.476 1.00 29.37  ? 2853 VAL A N     1 
ATOM   10402 C  CA    . VAL A 1 2853 ? 187.795 177.972 212.436 1.00 26.75  ? 2853 VAL A CA    1 
ATOM   10403 C  C     . VAL A 1 2853 ? 187.370 178.482 213.806 1.00 26.83  ? 2853 VAL A C     1 
ATOM   10404 O  O     . VAL A 1 2853 ? 187.844 179.529 214.269 1.00 30.74  ? 2853 VAL A O     1 
ATOM   10405 C  CB    . VAL A 1 2853 ? 186.752 178.301 211.352 1.00 25.01  ? 2853 VAL A CB    1 
ATOM   10406 C  CG1   . VAL A 1 2853 ? 186.221 179.714 211.529 1.00 22.50  ? 2853 VAL A CG1   1 
ATOM   10407 C  CG2   . VAL A 1 2853 ? 187.355 178.124 209.966 1.00 21.75  ? 2853 VAL A CG2   1 
ATOM   10408 N  N     . ALA A 1 2854 ? 186.478 177.750 214.483 1.00 25.26  ? 2854 ALA A N     1 
ATOM   10409 C  CA    . ALA A 1 2854 ? 186.024 178.184 215.798 1.00 25.95  ? 2854 ALA A CA    1 
ATOM   10410 C  C     . ALA A 1 2854 ? 187.175 178.229 216.793 1.00 31.80  ? 2854 ALA A C     1 
ATOM   10411 O  O     . ALA A 1 2854 ? 187.270 179.160 217.600 1.00 34.30  ? 2854 ALA A O     1 
ATOM   10412 C  CB    . ALA A 1 2854 ? 184.916 177.260 216.302 1.00 23.88  ? 2854 ALA A CB    1 
ATOM   10413 N  N     . LEU A 1 2855 ? 188.064 177.234 216.752 1.00 32.08  ? 2855 LEU A N     1 
ATOM   10414 C  CA    . LEU A 1 2855 ? 189.201 177.237 217.664 1.00 35.70  ? 2855 LEU A CA    1 
ATOM   10415 C  C     . LEU A 1 2855 ? 190.211 178.317 217.301 1.00 38.40  ? 2855 LEU A C     1 
ATOM   10416 O  O     . LEU A 1 2855 ? 190.847 178.892 218.192 1.00 42.10  ? 2855 LEU A O     1 
ATOM   10417 C  CB    . LEU A 1 2855 ? 189.870 175.864 217.682 1.00 37.86  ? 2855 LEU A CB    1 
ATOM   10418 C  CG    . LEU A 1 2855 ? 189.396 174.912 218.781 1.00 42.65  ? 2855 LEU A CG    1 
ATOM   10419 C  CD1   . LEU A 1 2855 ? 189.734 175.484 220.148 1.00 47.46  ? 2855 LEU A CD1   1 
ATOM   10420 C  CD2   . LEU A 1 2855 ? 187.906 174.631 218.665 1.00 47.94  ? 2855 LEU A CD2   1 
ATOM   10421 N  N     . LYS A 1 2856 ? 190.379 178.601 216.008 1.00 29.53  ? 2856 LYS A N     1 
ATOM   10422 C  CA    . LYS A 1 2856 ? 191.298 179.654 215.592 1.00 29.73  ? 2856 LYS A CA    1 
ATOM   10423 C  C     . LYS A 1 2856 ? 190.822 181.021 216.067 1.00 29.62  ? 2856 LYS A C     1 
ATOM   10424 O  O     . LYS A 1 2856 ? 191.614 181.823 216.575 1.00 32.73  ? 2856 LYS A O     1 
ATOM   10425 C  CB    . LYS A 1 2856 ? 191.457 179.635 214.071 1.00 27.92  ? 2856 LYS A CB    1 
ATOM   10426 C  CG    . LYS A 1 2856 ? 192.120 180.874 213.497 1.00 30.73  ? 2856 LYS A CG    1 
ATOM   10427 C  CD    . LYS A 1 2856 ? 192.219 180.791 211.984 1.00 34.32  ? 2856 LYS A CD    1 
ATOM   10428 C  CE    . LYS A 1 2856 ? 192.885 182.029 211.407 1.00 36.28  ? 2856 LYS A CE    1 
ATOM   10429 N  NZ    . LYS A 1 2856 ? 192.942 181.988 209.921 1.00 32.57  ? 2856 LYS A NZ    1 
ATOM   10430 N  N     . HIS A 1 2857 ? 189.531 181.305 215.915 1.00 28.62  ? 2857 HIS A N     1 
ATOM   10431 C  CA    . HIS A 1 2857 ? 189.018 182.625 216.259 1.00 27.43  ? 2857 HIS A CA    1 
ATOM   10432 C  C     . HIS A 1 2857 ? 188.558 182.742 217.707 1.00 28.67  ? 2857 HIS A C     1 
ATOM   10433 O  O     . HIS A 1 2857 ? 188.348 183.863 218.182 1.00 24.45  ? 2857 HIS A O     1 
ATOM   10434 C  CB    . HIS A 1 2857 ? 187.874 183.003 215.317 1.00 23.84  ? 2857 HIS A CB    1 
ATOM   10435 C  CG    . HIS A 1 2857 ? 188.315 183.236 213.906 1.00 18.58  ? 2857 HIS A CG    1 
ATOM   10436 N  ND1   . HIS A 1 2857 ? 188.980 184.378 213.515 1.00 19.73  ? 2857 HIS A ND1   1 
ATOM   10437 C  CD2   . HIS A 1 2857 ? 188.200 182.470 212.797 1.00 22.59  ? 2857 HIS A CD2   1 
ATOM   10438 C  CE1   . HIS A 1 2857 ? 189.250 184.307 212.224 1.00 24.01  ? 2857 HIS A CE1   1 
ATOM   10439 N  NE2   . HIS A 1 2857 ? 188.787 183.159 211.764 1.00 25.28  ? 2857 HIS A NE2   1 
ATOM   10440 N  N     . PHE A 1 2858 ? 188.400 181.626 218.418 1.00 29.52  ? 2858 PHE A N     1 
ATOM   10441 C  CA    . PHE A 1 2858 ? 188.042 181.623 219.836 1.00 30.00  ? 2858 PHE A CA    1 
ATOM   10442 C  C     . PHE A 1 2858 ? 189.003 180.696 220.569 1.00 40.96  ? 2858 PHE A C     1 
ATOM   10443 O  O     . PHE A 1 2858 ? 188.682 179.531 220.835 1.00 45.81  ? 2858 PHE A O     1 
ATOM   10444 C  CB    . PHE A 1 2858 ? 186.587 181.202 220.043 1.00 26.87  ? 2858 PHE A CB    1 
ATOM   10445 C  CG    . PHE A 1 2858 ? 185.589 182.182 219.495 1.00 25.63  ? 2858 PHE A CG    1 
ATOM   10446 C  CD1   . PHE A 1 2858 ? 185.211 182.137 218.164 1.00 24.74  ? 2858 PHE A CD1   1 
ATOM   10447 C  CD2   . PHE A 1 2858 ? 185.026 183.146 220.313 1.00 22.44  ? 2858 PHE A CD2   1 
ATOM   10448 C  CE1   . PHE A 1 2858 ? 184.295 183.037 217.660 1.00 16.76  ? 2858 PHE A CE1   1 
ATOM   10449 C  CE2   . PHE A 1 2858 ? 184.108 184.047 219.813 1.00 21.46  ? 2858 PHE A CE2   1 
ATOM   10450 C  CZ    . PHE A 1 2858 ? 183.743 183.992 218.486 1.00 18.55  ? 2858 PHE A CZ    1 
ATOM   10451 N  N     . PRO A 1 2859 ? 190.201 181.181 220.903 1.00 44.53  ? 2859 PRO A N     1 
ATOM   10452 C  CA    . PRO A 1 2859 ? 191.216 180.304 221.504 1.00 41.74  ? 2859 PRO A CA    1 
ATOM   10453 C  C     . PRO A 1 2859 ? 190.869 179.819 222.904 1.00 49.96  ? 2859 PRO A C     1 
ATOM   10454 O  O     . PRO A 1 2859 ? 190.938 178.618 223.183 1.00 55.96  ? 2859 PRO A O     1 
ATOM   10455 C  CB    . PRO A 1 2859 ? 192.474 181.186 221.524 1.00 45.36  ? 2859 PRO A CB    1 
ATOM   10456 C  CG    . PRO A 1 2859 ? 192.176 182.332 220.598 1.00 39.67  ? 2859 PRO A CG    1 
ATOM   10457 C  CD    . PRO A 1 2859 ? 190.706 182.545 220.691 1.00 34.91  ? 2859 PRO A CD    1 
ATOM   10458 N  N     . ASN A 1 2860 ? 190.500 180.740 223.794 1.00 45.83  ? 2860 ASN A N     1 
ATOM   10459 C  CA    . ASN A 1 2860 ? 190.335 180.424 225.214 1.00 48.55  ? 2860 ASN A CA    1 
ATOM   10460 C  C     . ASN A 1 2860 ? 188.877 180.069 225.511 1.00 48.57  ? 2860 ASN A C     1 
ATOM   10461 O  O     . ASN A 1 2860 ? 188.135 180.806 226.161 1.00 49.84  ? 2860 ASN A O     1 
ATOM   10462 C  CB    . ASN A 1 2860 ? 190.814 181.588 226.072 1.00 53.00  ? 2860 ASN A CB    1 
ATOM   10463 C  CG    . ASN A 1 2860 ? 192.148 182.139 225.611 1.00 54.82  ? 2860 ASN A CG    1 
ATOM   10464 O  OD1   . ASN A 1 2860 ? 193.136 181.411 225.524 1.00 56.42  ? 2860 ASN A OD1   1 
ATOM   10465 N  ND2   . ASN A 1 2860 ? 192.183 183.432 225.312 1.00 55.84  ? 2860 ASN A ND2   1 
ATOM   10466 N  N     . ILE A 1 2861 ? 188.475 178.897 225.020 1.00 49.56  ? 2861 ILE A N     1 
ATOM   10467 C  CA    . ILE A 1 2861 ? 187.116 178.401 225.179 1.00 53.03  ? 2861 ILE A CA    1 
ATOM   10468 C  C     . ILE A 1 2861 ? 187.167 176.938 225.600 1.00 57.15  ? 2861 ILE A C     1 
ATOM   10469 O  O     . ILE A 1 2861 ? 188.196 176.270 225.497 1.00 64.96  ? 2861 ILE A O     1 
ATOM   10470 C  CB    . ILE A 1 2861 ? 186.277 178.554 223.893 1.00 48.55  ? 2861 ILE A CB    1 
ATOM   10471 C  CG1   . ILE A 1 2861 ? 186.894 177.730 222.761 1.00 50.36  ? 2861 ILE A CG1   1 
ATOM   10472 C  CG2   . ILE A 1 2861 ? 186.153 180.017 223.504 1.00 41.51  ? 2861 ILE A CG2   1 
ATOM   10473 C  CD1   . ILE A 1 2861 ? 186.022 177.626 221.530 1.00 45.29  ? 2861 ILE A CD1   1 
ATOM   10474 N  N     . ASP A 1 2862 ? 186.028 176.448 226.084 1.00 51.93  ? 2862 ASP A N     1 
ATOM   10475 C  CA    . ASP A 1 2862 ? 185.854 175.035 226.404 1.00 58.71  ? 2862 ASP A CA    1 
ATOM   10476 C  C     . ASP A 1 2862 ? 185.399 174.315 225.140 1.00 56.10  ? 2862 ASP A C     1 
ATOM   10477 O  O     . ASP A 1 2862 ? 184.268 174.506 224.681 1.00 60.49  ? 2862 ASP A O     1 
ATOM   10478 C  CB    . ASP A 1 2862 ? 184.848 174.860 227.538 1.00 61.54  ? 2862 ASP A CB    1 
ATOM   10479 C  CG    . ASP A 1 2862 ? 184.854 173.457 228.110 1.00 63.56  ? 2862 ASP A CG    1 
ATOM   10480 O  OD1   . ASP A 1 2862 ? 185.701 172.642 227.689 1.00 56.26  ? 2862 ASP A OD1   1 
ATOM   10481 O  OD2   . ASP A 1 2862 ? 184.011 173.171 228.986 1.00 69.00  ? 2862 ASP A OD2   1 
ATOM   10482 N  N     . ARG A 1 2863 ? 186.284 173.491 224.574 1.00 51.05  ? 2863 ARG A N     1 
ATOM   10483 C  CA    . ARG A 1 2863 ? 185.988 172.844 223.299 1.00 51.43  ? 2863 ARG A CA    1 
ATOM   10484 C  C     . ARG A 1 2863 ? 184.805 171.890 223.412 1.00 57.93  ? 2863 ARG A C     1 
ATOM   10485 O  O     . ARG A 1 2863 ? 183.927 171.877 222.542 1.00 53.83  ? 2863 ARG A O     1 
ATOM   10486 C  CB    . ARG A 1 2863 ? 187.224 172.101 222.794 1.00 54.32  ? 2863 ARG A CB    1 
ATOM   10487 C  CG    . ARG A 1 2863 ? 187.465 172.235 221.301 1.00 53.50  ? 2863 ARG A CG    1 
ATOM   10488 C  CD    . ARG A 1 2863 ? 188.748 171.534 220.884 1.00 56.51  ? 2863 ARG A CD    1 
ATOM   10489 N  NE    . ARG A 1 2863 ? 189.930 172.334 221.182 1.00 61.04  ? 2863 ARG A NE    1 
ATOM   10490 C  CZ    . ARG A 1 2863 ? 191.111 172.172 220.600 1.00 63.69  ? 2863 ARG A CZ    1 
ATOM   10491 N  NH1   . ARG A 1 2863 ? 191.307 171.241 219.682 1.00 66.45  ? 2863 ARG A NH1   1 
ATOM   10492 N  NH2   . ARG A 1 2863 ? 192.120 172.966 220.949 1.00 52.98  ? 2863 ARG A NH2   1 
ATOM   10493 N  N     . GLU A 1 2864 ? 184.762 171.086 224.475 1.00 62.58  ? 2864 GLU A N     1 
ATOM   10494 C  CA    . GLU A 1 2864 ? 183.710 170.081 224.593 1.00 58.50  ? 2864 GLU A CA    1 
ATOM   10495 C  C     . GLU A 1 2864 ? 182.353 170.718 224.863 1.00 54.49  ? 2864 GLU A C     1 
ATOM   10496 O  O     . GLU A 1 2864 ? 181.346 170.317 224.268 1.00 58.67  ? 2864 GLU A O     1 
ATOM   10497 C  CB    . GLU A 1 2864 ? 184.060 169.080 225.693 1.00 57.09  ? 2864 GLU A CB    1 
ATOM   10498 C  CG    . GLU A 1 2864 ? 183.284 167.775 225.608 1.00 60.92  ? 2864 GLU A CG    1 
ATOM   10499 C  CD    . GLU A 1 2864 ? 183.572 167.001 224.335 1.00 64.77  ? 2864 GLU A CD    1 
ATOM   10500 O  OE1   . GLU A 1 2864 ? 184.696 167.116 223.804 1.00 65.34  ? 2864 GLU A OE1   1 
ATOM   10501 O  OE2   . GLU A 1 2864 ? 182.671 166.277 223.863 1.00 58.66  ? 2864 GLU A OE2   1 
ATOM   10502 N  N     . LYS A 1 2865 ? 182.305 171.710 225.753 1.00 55.80  ? 2865 LYS A N     1 
ATOM   10503 C  CA    . LYS A 1 2865 ? 181.038 172.348 226.092 1.00 56.41  ? 2865 LYS A CA    1 
ATOM   10504 C  C     . LYS A 1 2865 ? 180.405 173.050 224.898 1.00 54.50  ? 2865 LYS A C     1 
ATOM   10505 O  O     . LYS A 1 2865 ? 179.176 173.159 224.838 1.00 52.35  ? 2865 LYS A O     1 
ATOM   10506 C  CB    . LYS A 1 2865 ? 181.242 173.341 227.237 1.00 51.69  ? 2865 LYS A CB    1 
ATOM   10507 C  CG    . LYS A 1 2865 ? 179.956 173.884 227.837 1.00 52.50  ? 2865 LYS A CG    1 
ATOM   10508 C  CD    . LYS A 1 2865 ? 180.140 174.236 229.305 1.00 60.74  ? 2865 LYS A CD    1 
ATOM   10509 C  CE    . LYS A 1 2865 ? 179.028 175.145 229.798 1.00 62.75  ? 2865 LYS A CE    1 
ATOM   10510 N  NZ    . LYS A 1 2865 ? 178.781 176.273 228.858 1.00 50.73  ? 2865 LYS A NZ    1 
ATOM   10511 N  N     . ALA A 1 2866 ? 181.212 173.521 223.945 1.00 52.62  ? 2866 ALA A N     1 
ATOM   10512 C  CA    . ALA A 1 2866 ? 180.699 174.210 222.771 1.00 41.84  ? 2866 ALA A CA    1 
ATOM   10513 C  C     . ALA A 1 2866 ? 180.589 173.332 221.534 1.00 41.00  ? 2866 ALA A C     1 
ATOM   10514 O  O     . ALA A 1 2866 ? 179.859 173.696 220.608 1.00 38.53  ? 2866 ALA A O     1 
ATOM   10515 C  CB    . ALA A 1 2866 ? 181.583 175.420 222.436 1.00 34.27  ? 2866 ALA A CB    1 
ATOM   10516 N  N     . MET A 1 2867 ? 181.281 172.196 221.493 1.00 46.29  ? 2867 MET A N     1 
ATOM   10517 C  CA    . MET A 1 2867 ? 181.349 171.368 220.294 1.00 42.52  ? 2867 MET A CA    1 
ATOM   10518 C  C     . MET A 1 2867 ? 181.057 169.909 220.607 1.00 48.93  ? 2867 MET A C     1 
ATOM   10519 O  O     . MET A 1 2867 ? 181.735 169.003 220.113 1.00 54.31  ? 2867 MET A O     1 
ATOM   10520 C  CB    . MET A 1 2867 ? 182.710 171.500 219.616 1.00 45.13  ? 2867 MET A CB    1 
ATOM   10521 C  CG    . MET A 1 2867 ? 183.008 172.881 219.067 1.00 47.19  ? 2867 MET A CG    1 
ATOM   10522 S  SD    . MET A 1 2867 ? 181.875 173.348 217.749 1.00 69.86  ? 2867 MET A SD    1 
ATOM   10523 C  CE    . MET A 1 2867 ? 182.341 175.054 217.509 1.00 42.65  ? 2867 MET A CE    1 
ATOM   10524 N  N     . SER A 1 2868 ? 180.049 169.648 221.434 1.00 42.36  ? 2868 SER A N     1 
ATOM   10525 C  CA    . SER A 1 2868 ? 179.536 168.291 221.553 1.00 38.40  ? 2868 SER A CA    1 
ATOM   10526 C  C     . SER A 1 2868 ? 178.911 167.888 220.225 1.00 39.21  ? 2868 SER A C     1 
ATOM   10527 O  O     . SER A 1 2868 ? 177.929 168.494 219.790 1.00 38.15  ? 2868 SER A O     1 
ATOM   10528 C  CB    . SER A 1 2868 ? 178.512 168.202 222.683 1.00 45.89  ? 2868 SER A CB    1 
ATOM   10529 O  OG    . SER A 1 2868 ? 179.076 168.613 223.916 1.00 46.29  ? 2868 SER A OG    1 
ATOM   10530 N  N     . ARG A 1 2869 ? 179.479 166.864 219.591 1.00 43.39  ? 2869 ARG A N     1 
ATOM   10531 C  CA    . ARG A 1 2869 ? 179.197 166.598 218.181 1.00 46.39  ? 2869 ARG A CA    1 
ATOM   10532 C  C     . ARG A 1 2869 ? 177.713 166.492 217.842 1.00 48.32  ? 2869 ARG A C     1 
ATOM   10533 O  O     . ARG A 1 2869 ? 177.318 167.020 216.788 1.00 51.74  ? 2869 ARG A O     1 
ATOM   10534 C  CB    . ARG A 1 2869 ? 179.948 165.337 217.733 1.00 56.11  ? 2869 ARG A CB    1 
ATOM   10535 C  CG    . ARG A 1 2869 ? 181.364 165.611 217.241 1.00 59.04  ? 2869 ARG A CG    1 
ATOM   10536 C  CD    . ARG A 1 2869 ? 181.369 166.529 216.023 1.00 60.51  ? 2869 ARG A CD    1 
ATOM   10537 N  NE    . ARG A 1 2869 ? 181.618 167.921 216.383 1.00 58.23  ? 2869 ARG A NE    1 
ATOM   10538 C  CZ    . ARG A 1 2869 ? 181.244 168.966 215.656 1.00 51.89  ? 2869 ARG A CZ    1 
ATOM   10539 N  NH1   . ARG A 1 2869 ? 180.585 168.817 214.518 1.00 42.33  ? 2869 ARG A NH1   1 
ATOM   10540 N  NH2   . ARG A 1 2869 ? 181.539 170.191 216.081 1.00 46.47  ? 2869 ARG A NH2   1 
ATOM   10541 N  N     . PRO A 1 2870 ? 176.850 165.847 218.640 1.00 42.26  ? 2870 PRO A N     1 
ATOM   10542 C  CA    . PRO A 1 2870 ? 175.411 165.944 218.357 1.00 36.34  ? 2870 PRO A CA    1 
ATOM   10543 C  C     . PRO A 1 2870 ? 174.866 167.329 218.672 1.00 32.05  ? 2870 PRO A C     1 
ATOM   10544 O  O     . PRO A 1 2870 ? 174.204 167.525 219.695 1.00 40.01  ? 2870 PRO A O     1 
ATOM   10545 C  CB    . PRO A 1 2870 ? 174.793 164.873 219.267 1.00 29.97  ? 2870 PRO A CB    1 
ATOM   10546 C  CG    . PRO A 1 2870 ? 175.922 163.977 219.640 1.00 41.25  ? 2870 PRO A CG    1 
ATOM   10547 C  CD    . PRO A 1 2870 ? 177.123 164.860 219.698 1.00 38.24  ? 2870 PRO A CD    1 
ATOM   10548 N  N     . ILE A 1 2871 ? 175.144 168.299 217.801 1.00 22.87  ? 2871 ILE A N     1 
ATOM   10549 C  CA    . ILE A 1 2871 ? 174.681 169.673 217.989 1.00 21.69  ? 2871 ILE A CA    1 
ATOM   10550 C  C     . ILE A 1 2871 ? 173.227 169.727 217.528 1.00 18.17  ? 2871 ILE A C     1 
ATOM   10551 O  O     . ILE A 1 2871 ? 172.945 169.750 216.330 1.00 15.61  ? 2871 ILE A O     1 
ATOM   10552 C  CB    . ILE A 1 2871 ? 175.548 170.681 217.233 1.00 23.00  ? 2871 ILE A CB    1 
ATOM   10553 C  CG1   . ILE A 1 2871 ? 177.030 170.437 217.516 1.00 24.07  ? 2871 ILE A CG1   1 
ATOM   10554 C  CG2   . ILE A 1 2871 ? 175.167 172.099 217.622 1.00 15.08  ? 2871 ILE A CG2   1 
ATOM   10555 C  CD1   . ILE A 1 2871 ? 177.941 171.513 216.974 1.00 21.26  ? 2871 ILE A CD1   1 
ATOM   10556 N  N     . LEU A 1 2872 ? 172.299 169.749 218.481 1.00 17.18  ? 2872 LEU A N     1 
ATOM   10557 C  CA    . LEU A 1 2872 ? 170.875 169.772 218.185 1.00 14.36  ? 2872 LEU A CA    1 
ATOM   10558 C  C     . LEU A 1 2872 ? 170.219 170.929 218.920 1.00 15.40  ? 2872 LEU A C     1 
ATOM   10559 O  O     . LEU A 1 2872 ? 170.481 171.152 220.105 1.00 15.28  ? 2872 LEU A O     1 
ATOM   10560 C  CB    . LEU A 1 2872 ? 170.200 168.456 218.585 1.00 17.27  ? 2872 LEU A CB    1 
ATOM   10561 C  CG    . LEU A 1 2872 ? 170.682 167.191 217.877 1.00 18.85  ? 2872 LEU A CG    1 
ATOM   10562 C  CD1   . LEU A 1 2872 ? 169.991 165.968 218.455 1.00 20.10  ? 2872 LEU A CD1   1 
ATOM   10563 C  CD2   . LEU A 1 2872 ? 170.445 167.289 216.380 1.00 14.36  ? 2872 LEU A CD2   1 
ATOM   10564 N  N     . TYR A 1 2873 ? 169.368 171.663 218.208 1.00 18.09  ? 2873 TYR A N     1 
ATOM   10565 C  CA    . TYR A 1 2873 ? 168.607 172.766 218.772 1.00 13.82  ? 2873 TYR A CA    1 
ATOM   10566 C  C     . TYR A 1 2873 ? 167.136 172.572 218.444 1.00 14.13  ? 2873 TYR A C     1 
ATOM   10567 O  O     . TYR A 1 2873 ? 166.788 172.199 217.320 1.00 19.05  ? 2873 TYR A O     1 
ATOM   10568 C  CB    . TYR A 1 2873 ? 169.084 174.118 218.228 1.00 14.35  ? 2873 TYR A CB    1 
ATOM   10569 C  CG    . TYR A 1 2873 ? 170.284 174.695 218.938 1.00 11.16  ? 2873 TYR A CG    1 
ATOM   10570 C  CD1   . TYR A 1 2873 ? 171.537 174.115 218.811 1.00 12.83  ? 2873 TYR A CD1   1 
ATOM   10571 C  CD2   . TYR A 1 2873 ? 170.164 175.825 219.734 1.00 11.61  ? 2873 TYR A CD2   1 
ATOM   10572 C  CE1   . TYR A 1 2873 ? 172.636 174.643 219.457 1.00 14.07  ? 2873 TYR A CE1   1 
ATOM   10573 C  CE2   . TYR A 1 2873 ? 171.257 176.359 220.384 1.00 15.32  ? 2873 TYR A CE2   1 
ATOM   10574 C  CZ    . TYR A 1 2873 ? 172.491 175.764 220.243 1.00 18.17  ? 2873 TYR A CZ    1 
ATOM   10575 O  OH    . TYR A 1 2873 ? 173.583 176.291 220.889 1.00 16.84  ? 2873 TYR A OH    1 
ATOM   10576 N  N     . SER A 1 2874 ? 166.274 172.827 219.424 1.00 16.01  ? 2874 SER A N     1 
ATOM   10577 C  CA    . SER A 1 2874 ? 164.842 172.686 219.209 1.00 15.79  ? 2874 SER A CA    1 
ATOM   10578 C  C     . SER A 1 2874 ? 164.096 173.553 220.210 1.00 16.63  ? 2874 SER A C     1 
ATOM   10579 O  O     . SER A 1 2874 ? 164.608 173.862 221.288 1.00 22.67  ? 2874 SER A O     1 
ATOM   10580 C  CB    . SER A 1 2874 ? 164.396 171.226 219.336 1.00 16.62  ? 2874 SER A CB    1 
ATOM   10581 O  OG    . SER A 1 2874 ? 163.026 171.083 219.007 1.00 17.57  ? 2874 SER A OG    1 
ATOM   10582 N  N     . ASN A 1 2875 ? 162.879 173.942 219.833 1.00 16.21  ? 2875 ASN A N     1 
ATOM   10583 C  CA    . ASN A 1 2875 ? 161.965 174.654 220.716 1.00 20.39  ? 2875 ASN A CA    1 
ATOM   10584 C  C     . ASN A 1 2875 ? 160.735 173.811 221.040 1.00 22.43  ? 2875 ASN A C     1 
ATOM   10585 O  O     . ASN A 1 2875 ? 159.654 174.346 221.294 1.00 25.74  ? 2875 ASN A O     1 
ATOM   10586 C  CB    . ASN A 1 2875 ? 161.549 175.989 220.102 1.00 23.55  ? 2875 ASN A CB    1 
ATOM   10587 C  CG    . ASN A 1 2875 ? 160.926 175.833 218.730 1.00 24.86  ? 2875 ASN A CG    1 
ATOM   10588 O  OD1   . ASN A 1 2875 ? 160.851 174.731 218.190 1.00 28.30  ? 2875 ASN A OD1   1 
ATOM   10589 N  ND2   . ASN A 1 2875 ? 160.472 176.941 218.160 1.00 32.54  ? 2875 ASN A ND2   1 
ATOM   10590 N  N     . TRP A 1 2876 ? 160.888 172.489 221.018 1.00 23.45  ? 2876 TRP A N     1 
ATOM   10591 C  CA    . TRP A 1 2876 ? 159.786 171.579 221.301 1.00 22.07  ? 2876 TRP A CA    1 
ATOM   10592 C  C     . TRP A 1 2876 ? 159.682 171.272 222.789 1.00 25.94  ? 2876 TRP A C     1 
ATOM   10593 O  O     . TRP A 1 2876 ? 158.585 171.287 223.356 1.00 35.87  ? 2876 TRP A O     1 
ATOM   10594 C  CB    . TRP A 1 2876 ? 159.960 170.283 220.505 1.00 20.07  ? 2876 TRP A CB    1 
ATOM   10595 C  CG    . TRP A 1 2876 ? 159.560 170.396 219.069 1.00 19.17  ? 2876 TRP A CG    1 
ATOM   10596 C  CD1   . TRP A 1 2876 ? 158.802 171.377 218.504 1.00 19.09  ? 2876 TRP A CD1   1 
ATOM   10597 C  CD2   . TRP A 1 2876 ? 159.890 169.487 218.014 1.00 19.52  ? 2876 TRP A CD2   1 
ATOM   10598 N  NE1   . TRP A 1 2876 ? 158.643 171.139 217.162 1.00 16.85  ? 2876 TRP A NE1   1 
ATOM   10599 C  CE2   . TRP A 1 2876 ? 159.301 169.983 216.836 1.00 18.33  ? 2876 TRP A CE2   1 
ATOM   10600 C  CE3   . TRP A 1 2876 ? 160.628 168.301 217.951 1.00 16.73  ? 2876 TRP A CE3   1 
ATOM   10601 C  CZ2   . TRP A 1 2876 ? 159.427 169.336 215.609 1.00 17.10  ? 2876 TRP A CZ2   1 
ATOM   10602 C  CZ3   . TRP A 1 2876 ? 160.752 167.662 216.734 1.00 16.82  ? 2876 TRP A CZ3   1 
ATOM   10603 C  CH2   . TRP A 1 2876 ? 160.155 168.180 215.579 1.00 17.05  ? 2876 TRP A CH2   1 
ATOM   10604 N  N     . LEU A 1 2877 ? 160.815 170.988 223.432 1.00 22.54  ? 2877 LEU A N     1 
ATOM   10605 C  CA    . LEU A 1 2877 ? 160.802 170.677 224.856 1.00 23.78  ? 2877 LEU A CA    1 
ATOM   10606 C  C     . LEU A 1 2877 ? 160.511 171.916 225.692 1.00 30.80  ? 2877 LEU A C     1 
ATOM   10607 O  O     . LEU A 1 2877 ? 159.783 171.843 226.689 1.00 36.79  ? 2877 LEU A O     1 
ATOM   10608 C  CB    . LEU A 1 2877 ? 162.134 170.051 225.266 1.00 21.02  ? 2877 LEU A CB    1 
ATOM   10609 C  CG    . LEU A 1 2877 ? 162.252 168.529 225.152 1.00 22.96  ? 2877 LEU A CG    1 
ATOM   10610 C  CD1   . LEU A 1 2877 ? 162.274 168.081 223.700 1.00 22.06  ? 2877 LEU A CD1   1 
ATOM   10611 C  CD2   . LEU A 1 2877 ? 163.493 168.044 225.877 1.00 28.79  ? 2877 LEU A CD2   1 
ATOM   10612 N  N     . SER A 1 2878 ? 161.064 173.061 225.304 1.00 28.89  ? 2878 SER A N     1 
ATOM   10613 C  CA    . SER A 1 2878 ? 160.908 174.306 226.042 1.00 29.86  ? 2878 SER A CA    1 
ATOM   10614 C  C     . SER A 1 2878 ? 160.341 175.373 225.114 1.00 36.97  ? 2878 SER A C     1 
ATOM   10615 O  O     . SER A 1 2878 ? 160.145 175.148 223.917 1.00 39.97  ? 2878 SER A O     1 
ATOM   10616 C  CB    . SER A 1 2878 ? 162.243 174.758 226.646 1.00 30.02  ? 2878 SER A CB    1 
ATOM   10617 O  OG    . SER A 1 2878 ? 163.136 175.182 225.634 1.00 37.90  ? 2878 SER A OG    1 
ATOM   10618 N  N     . LYS A 1 2879 ? 160.069 176.550 225.680 1.00 37.64  ? 2879 LYS A N     1 
ATOM   10619 C  CA    . LYS A 1 2879 ? 159.511 177.643 224.892 1.00 35.95  ? 2879 LYS A CA    1 
ATOM   10620 C  C     . LYS A 1 2879 ? 160.554 178.297 223.995 1.00 35.26  ? 2879 LYS A C     1 
ATOM   10621 O  O     . LYS A 1 2879 ? 160.206 178.820 222.931 1.00 41.79  ? 2879 LYS A O     1 
ATOM   10622 C  CB    . LYS A 1 2879 ? 158.885 178.691 225.814 1.00 37.70  ? 2879 LYS A CB    1 
ATOM   10623 C  CG    . LYS A 1 2879 ? 159.741 179.046 227.016 1.00 42.20  ? 2879 LYS A CG    1 
ATOM   10624 C  CD    . LYS A 1 2879 ? 159.458 180.458 227.499 1.00 46.58  ? 2879 LYS A CD    1 
ATOM   10625 C  CE    . LYS A 1 2879 ? 160.335 180.821 228.684 1.00 54.17  ? 2879 LYS A CE    1 
ATOM   10626 N  NZ    . LYS A 1 2879 ? 160.574 182.287 228.767 1.00 54.09  ? 2879 LYS A NZ    1 
ATOM   10627 N  N     . ASP A 1 2880 ? 161.818 178.279 224.399 1.00 34.11  ? 2880 ASP A N     1 
ATOM   10628 C  CA    . ASP A 1 2880 ? 162.886 178.921 223.651 1.00 32.00  ? 2880 ASP A CA    1 
ATOM   10629 C  C     . ASP A 1 2880 ? 163.608 177.913 222.764 1.00 25.89  ? 2880 ASP A C     1 
ATOM   10630 O  O     . ASP A 1 2880 ? 163.445 176.698 222.890 1.00 29.56  ? 2880 ASP A O     1 
ATOM   10631 C  CB    . ASP A 1 2880 ? 163.877 179.598 224.603 1.00 33.37  ? 2880 ASP A CB    1 
ATOM   10632 C  CG    . ASP A 1 2880 ? 163.322 180.867 225.212 1.00 41.50  ? 2880 ASP A CG    1 
ATOM   10633 O  OD1   . ASP A 1 2880 ? 162.225 181.296 224.797 1.00 40.43  ? 2880 ASP A OD1   1 
ATOM   10634 O  OD2   . ASP A 1 2880 ? 163.984 181.437 226.103 1.00 48.50  ? 2880 ASP A OD2   1 
ATOM   10635 N  N     . TYR A 1 2881 ? 164.421 178.443 221.854 1.00 25.25  ? 2881 TYR A N     1 
ATOM   10636 C  CA    . TYR A 1 2881 ? 165.192 177.627 220.918 1.00 18.44  ? 2881 TYR A CA    1 
ATOM   10637 C  C     . TYR A 1 2881 ? 166.558 177.280 221.515 1.00 20.73  ? 2881 TYR A C     1 
ATOM   10638 O  O     . TYR A 1 2881 ? 167.616 177.579 220.963 1.00 26.86  ? 2881 TYR A O     1 
ATOM   10639 C  CB    . TYR A 1 2881 ? 165.331 178.353 219.585 1.00 21.49  ? 2881 TYR A CB    1 
ATOM   10640 C  CG    . TYR A 1 2881 ? 165.861 177.495 218.463 1.00 19.37  ? 2881 TYR A CG    1 
ATOM   10641 C  CD1   . TYR A 1 2881 ? 165.147 176.398 218.005 1.00 16.50  ? 2881 TYR A CD1   1 
ATOM   10642 C  CD2   . TYR A 1 2881 ? 167.075 177.787 217.857 1.00 17.02  ? 2881 TYR A CD2   1 
ATOM   10643 C  CE1   . TYR A 1 2881 ? 165.628 175.614 216.979 1.00 14.45  ? 2881 TYR A CE1   1 
ATOM   10644 C  CE2   . TYR A 1 2881 ? 167.564 177.010 216.831 1.00 17.19  ? 2881 TYR A CE2   1 
ATOM   10645 C  CZ    . TYR A 1 2881 ? 166.836 175.926 216.395 1.00 14.62  ? 2881 TYR A CZ    1 
ATOM   10646 O  OH    . TYR A 1 2881 ? 167.322 175.147 215.374 1.00 12.24  ? 2881 TYR A OH    1 
ATOM   10647 N  N     . ILE A 1 2882 ? 166.511 176.639 222.677 1.00 20.18  ? 2882 ILE A N     1 
ATOM   10648 C  CA    . ILE A 1 2882 ? 167.711 176.230 223.401 1.00 16.48  ? 2882 ILE A CA    1 
ATOM   10649 C  C     . ILE A 1 2882 ? 168.189 174.895 222.839 1.00 18.50  ? 2882 ILE A C     1 
ATOM   10650 O  O     . ILE A 1 2882 ? 167.411 174.197 222.173 1.00 19.82  ? 2882 ILE A O     1 
ATOM   10651 C  CB    . ILE A 1 2882 ? 167.442 176.137 224.911 1.00 19.75  ? 2882 ILE A CB    1 
ATOM   10652 C  CG1   . ILE A 1 2882 ? 166.383 175.073 225.199 1.00 15.07  ? 2882 ILE A CG1   1 
ATOM   10653 C  CG2   . ILE A 1 2882 ? 167.010 177.487 225.455 1.00 27.64  ? 2882 ILE A CG2   1 
ATOM   10654 C  CD1   . ILE A 1 2882 ? 166.230 174.750 226.664 1.00 25.45  ? 2882 ILE A CD1   1 
ATOM   10655 N  N     . PRO A 1 2883 ? 169.447 174.508 223.056 1.00 17.84  ? 2883 PRO A N     1 
ATOM   10656 C  CA    . PRO A 1 2883 ? 169.887 173.179 222.616 1.00 16.18  ? 2883 PRO A CA    1 
ATOM   10657 C  C     . PRO A 1 2883 ? 169.124 172.078 223.337 1.00 16.89  ? 2883 PRO A C     1 
ATOM   10658 O  O     . PRO A 1 2883 ? 168.709 172.227 224.488 1.00 16.92  ? 2883 PRO A O     1 
ATOM   10659 C  CB    . PRO A 1 2883 ? 171.378 173.158 222.976 1.00 14.55  ? 2883 PRO A CB    1 
ATOM   10660 C  CG    . PRO A 1 2883 ? 171.546 174.233 223.994 1.00 13.38  ? 2883 PRO A CG    1 
ATOM   10661 C  CD    . PRO A 1 2883 ? 170.554 175.286 223.635 1.00 12.39  ? 2883 PRO A CD    1 
ATOM   10662 N  N     . VAL A 1 2884 ? 168.939 170.960 222.640 1.00 18.54  ? 2884 VAL A N     1 
ATOM   10663 C  CA    . VAL A 1 2884 ? 168.177 169.829 223.151 1.00 16.07  ? 2884 VAL A CA    1 
ATOM   10664 C  C     . VAL A 1 2884 ? 169.078 168.602 223.183 1.00 20.13  ? 2884 VAL A C     1 
ATOM   10665 O  O     . VAL A 1 2884 ? 169.969 168.449 222.340 1.00 22.03  ? 2884 VAL A O     1 
ATOM   10666 C  CB    . VAL A 1 2884 ? 166.908 169.571 222.308 1.00 14.75  ? 2884 VAL A CB    1 
ATOM   10667 C  CG1   . VAL A 1 2884 ? 167.249 168.898 220.987 1.00 14.21  ? 2884 VAL A CG1   1 
ATOM   10668 C  CG2   . VAL A 1 2884 ? 165.908 168.739 223.092 1.00 19.59  ? 2884 VAL A CG2   1 
ATOM   10669 N  N     . ASP A 1 2885 ? 168.869 167.752 224.184 1.00 25.00  ? 2885 ASP A N     1 
ATOM   10670 C  CA    . ASP A 1 2885 ? 169.595 166.495 224.268 1.00 25.70  ? 2885 ASP A CA    1 
ATOM   10671 C  C     . ASP A 1 2885 ? 168.988 165.474 223.312 1.00 24.53  ? 2885 ASP A C     1 
ATOM   10672 O  O     . ASP A 1 2885 ? 167.782 165.473 223.053 1.00 22.28  ? 2885 ASP A O     1 
ATOM   10673 C  CB    . ASP A 1 2885 ? 169.576 165.965 225.703 1.00 28.18  ? 2885 ASP A CB    1 
ATOM   10674 C  CG    . ASP A 1 2885 ? 169.997 164.512 225.797 1.00 34.16  ? 2885 ASP A CG    1 
ATOM   10675 O  OD1   . ASP A 1 2885 ? 171.115 164.187 225.347 1.00 42.98  ? 2885 ASP A OD1   1 
ATOM   10676 O  OD2   . ASP A 1 2885 ? 169.214 163.695 226.321 1.00 33.00  ? 2885 ASP A OD2   1 
ATOM   10677 N  N     . GLN A 1 2886 ? 169.844 164.599 222.778 1.00 27.81  ? 2886 GLN A N     1 
ATOM   10678 C  CA    . GLN A 1 2886 ? 169.391 163.625 221.790 1.00 21.95  ? 2886 GLN A CA    1 
ATOM   10679 C  C     . GLN A 1 2886 ? 168.389 162.642 222.386 1.00 27.50  ? 2886 GLN A C     1 
ATOM   10680 O  O     . GLN A 1 2886 ? 167.408 162.277 221.729 1.00 26.95  ? 2886 GLN A O     1 
ATOM   10681 C  CB    . GLN A 1 2886 ? 170.589 162.881 221.202 1.00 17.45  ? 2886 GLN A CB    1 
ATOM   10682 C  CG    . GLN A 1 2886 ? 170.259 162.049 219.975 1.00 19.08  ? 2886 GLN A CG    1 
ATOM   10683 C  CD    . GLN A 1 2886 ? 171.488 161.683 219.170 1.00 20.31  ? 2886 GLN A CD    1 
ATOM   10684 O  OE1   . GLN A 1 2886 ? 172.402 161.031 219.671 1.00 28.11  ? 2886 GLN A OE1   1 
ATOM   10685 N  NE2   . GLN A 1 2886 ? 171.516 162.103 217.911 1.00 20.42  ? 2886 GLN A NE2   1 
ATOM   10686 N  N     . GLU A 1 2887 ? 168.613 162.205 223.627 1.00 27.89  ? 2887 GLU A N     1 
ATOM   10687 C  CA    . GLU A 1 2887 ? 167.732 161.204 224.224 1.00 27.06  ? 2887 GLU A CA    1 
ATOM   10688 C  C     . GLU A 1 2887 ? 166.371 161.792 224.583 1.00 27.56  ? 2887 GLU A C     1 
ATOM   10689 O  O     . GLU A 1 2887 ? 165.333 161.173 224.316 1.00 34.71  ? 2887 GLU A O     1 
ATOM   10690 C  CB    . GLU A 1 2887 ? 168.399 160.590 225.453 1.00 28.97  ? 2887 GLU A CB    1 
ATOM   10691 C  CG    . GLU A 1 2887 ? 169.694 159.858 225.142 1.00 33.61  ? 2887 GLU A CG    1 
ATOM   10692 C  CD    . GLU A 1 2887 ? 169.554 158.900 223.974 1.00 41.74  ? 2887 GLU A CD    1 
ATOM   10693 O  OE1   . GLU A 1 2887 ? 168.608 158.084 223.981 1.00 36.88  ? 2887 GLU A OE1   1 
ATOM   10694 O  OE2   . GLU A 1 2887 ? 170.389 158.963 223.047 1.00 36.64  ? 2887 GLU A OE2   1 
ATOM   10695 N  N     . GLU A 1 2888 ? 166.352 162.978 225.195 1.00 25.59  ? 2888 GLU A N     1 
ATOM   10696 C  CA    . GLU A 1 2888 ? 165.078 163.622 225.502 1.00 27.53  ? 2888 GLU A CA    1 
ATOM   10697 C  C     . GLU A 1 2888 ? 164.316 163.957 224.228 1.00 28.19  ? 2888 GLU A C     1 
ATOM   10698 O  O     . GLU A 1 2888 ? 163.087 163.814 224.172 1.00 29.80  ? 2888 GLU A O     1 
ATOM   10699 C  CB    . GLU A 1 2888 ? 165.311 164.879 226.340 1.00 25.59  ? 2888 GLU A CB    1 
ATOM   10700 C  CG    . GLU A 1 2888 ? 166.405 164.734 227.378 1.00 32.67  ? 2888 GLU A CG    1 
ATOM   10701 C  CD    . GLU A 1 2888 ? 166.488 165.926 228.309 1.00 60.12  ? 2888 GLU A CD    1 
ATOM   10702 O  OE1   . GLU A 1 2888 ? 165.813 166.941 228.037 1.00 63.29  ? 2888 GLU A OE1   1 
ATOM   10703 O  OE2   . GLU A 1 2888 ? 167.229 165.848 229.312 1.00 58.02  ? 2888 GLU A OE2   1 
ATOM   10704 N  N     . LEU A 1 2889 ? 165.029 164.404 223.193 1.00 21.58  ? 2889 LEU A N     1 
ATOM   10705 C  CA    . LEU A 1 2889 ? 164.386 164.658 221.910 1.00 22.35  ? 2889 LEU A CA    1 
ATOM   10706 C  C     . LEU A 1 2889 ? 163.803 163.377 221.330 1.00 25.75  ? 2889 LEU A C     1 
ATOM   10707 O  O     . LEU A 1 2889 ? 162.698 163.386 220.780 1.00 23.19  ? 2889 LEU A O     1 
ATOM   10708 C  CB    . LEU A 1 2889 ? 165.382 165.288 220.937 1.00 17.52  ? 2889 LEU A CB    1 
ATOM   10709 C  CG    . LEU A 1 2889 ? 164.924 165.407 219.483 1.00 18.93  ? 2889 LEU A CG    1 
ATOM   10710 C  CD1   . LEU A 1 2889 ? 163.837 166.459 219.354 1.00 15.41  ? 2889 LEU A CD1   1 
ATOM   10711 C  CD2   . LEU A 1 2889 ? 166.098 165.728 218.574 1.00 20.07  ? 2889 LEU A CD2   1 
ATOM   10712 N  N     . ARG A 1 2890 ? 164.530 162.264 221.449 1.00 26.46  ? 2890 ARG A N     1 
ATOM   10713 C  CA    . ARG A 1 2890 ? 164.021 160.991 220.951 1.00 23.89  ? 2890 ARG A CA    1 
ATOM   10714 C  C     . ARG A 1 2890 ? 162.758 160.570 221.690 1.00 26.20  ? 2890 ARG A C     1 
ATOM   10715 O  O     . ARG A 1 2890 ? 161.797 160.102 221.071 1.00 31.33  ? 2890 ARG A O     1 
ATOM   10716 C  CB    . ARG A 1 2890 ? 165.095 159.912 221.068 1.00 25.92  ? 2890 ARG A CB    1 
ATOM   10717 C  CG    . ARG A 1 2890 ? 164.776 158.637 220.305 1.00 25.53  ? 2890 ARG A CG    1 
ATOM   10718 C  CD    . ARG A 1 2890 ? 165.659 157.490 220.758 1.00 24.02  ? 2890 ARG A CD    1 
ATOM   10719 N  NE    . ARG A 1 2890 ? 167.075 157.830 220.683 1.00 27.89  ? 2890 ARG A NE    1 
ATOM   10720 C  CZ    . ARG A 1 2890 ? 167.801 157.763 219.576 1.00 33.93  ? 2890 ARG A CZ    1 
ATOM   10721 N  NH1   . ARG A 1 2890 ? 167.278 157.365 218.428 1.00 28.59  ? 2890 ARG A NH1   1 
ATOM   10722 N  NH2   . ARG A 1 2890 ? 169.087 158.102 219.622 1.00 28.87  ? 2890 ARG A NH2   1 
ATOM   10723 N  N     . ASP A 1 2891 ? 162.739 160.727 223.016 1.00 24.19  ? 2891 ASP A N     1 
ATOM   10724 C  CA    . ASP A 1 2891 ? 161.541 160.377 223.778 1.00 26.19  ? 2891 ASP A CA    1 
ATOM   10725 C  C     . ASP A 1 2891 ? 160.359 161.262 223.395 1.00 26.73  ? 2891 ASP A C     1 
ATOM   10726 O  O     . ASP A 1 2891 ? 159.229 160.774 223.235 1.00 27.03  ? 2891 ASP A O     1 
ATOM   10727 C  CB    . ASP A 1 2891 ? 161.814 160.472 225.279 1.00 31.68  ? 2891 ASP A CB    1 
ATOM   10728 C  CG    . ASP A 1 2891 ? 163.116 159.810 225.678 1.00 43.03  ? 2891 ASP A CG    1 
ATOM   10729 O  OD1   . ASP A 1 2891 ? 163.481 158.790 225.056 1.00 41.41  ? 2891 ASP A OD1   1 
ATOM   10730 O  OD2   . ASP A 1 2891 ? 163.775 160.308 226.615 1.00 40.67  ? 2891 ASP A OD2   1 
ATOM   10731 N  N     . TYR A 1 2892 ? 160.598 162.568 223.248 1.00 26.47  ? 2892 TYR A N     1 
ATOM   10732 C  CA    . TYR A 1 2892 ? 159.518 163.471 222.865 1.00 24.97  ? 2892 TYR A CA    1 
ATOM   10733 C  C     . TYR A 1 2892 ? 158.984 163.130 221.480 1.00 24.80  ? 2892 TYR A C     1 
ATOM   10734 O  O     . TYR A 1 2892 ? 157.767 163.135 221.257 1.00 24.99  ? 2892 TYR A O     1 
ATOM   10735 C  CB    . TYR A 1 2892 ? 160.000 164.920 222.917 1.00 22.40  ? 2892 TYR A CB    1 
ATOM   10736 C  CG    . TYR A 1 2892 ? 158.951 165.925 222.504 1.00 22.45  ? 2892 TYR A CG    1 
ATOM   10737 C  CD1   . TYR A 1 2892 ? 157.968 166.333 223.393 1.00 25.16  ? 2892 TYR A CD1   1 
ATOM   10738 C  CD2   . TYR A 1 2892 ? 158.942 166.463 221.225 1.00 23.13  ? 2892 TYR A CD2   1 
ATOM   10739 C  CE1   . TYR A 1 2892 ? 157.005 167.249 223.021 1.00 25.50  ? 2892 TYR A CE1   1 
ATOM   10740 C  CE2   . TYR A 1 2892 ? 157.982 167.379 220.844 1.00 24.35  ? 2892 TYR A CE2   1 
ATOM   10741 C  CZ    . TYR A 1 2892 ? 157.017 167.768 221.747 1.00 23.73  ? 2892 TYR A CZ    1 
ATOM   10742 O  OH    . TYR A 1 2892 ? 156.059 168.681 221.375 1.00 30.25  ? 2892 TYR A OH    1 
ATOM   10743 N  N     . VAL A 1 2893 ? 159.879 162.821 220.539 1.00 23.51  ? 2893 VAL A N     1 
ATOM   10744 C  CA    . VAL A 1 2893 ? 159.447 162.452 219.197 1.00 24.47  ? 2893 VAL A CA    1 
ATOM   10745 C  C     . VAL A 1 2893 ? 158.689 161.132 219.224 1.00 26.52  ? 2893 VAL A C     1 
ATOM   10746 O  O     . VAL A 1 2893 ? 157.733 160.943 218.471 1.00 31.59  ? 2893 VAL A O     1 
ATOM   10747 C  CB    . VAL A 1 2893 ? 160.650 162.405 218.236 1.00 28.37  ? 2893 VAL A CB    1 
ATOM   10748 C  CG1   . VAL A 1 2893 ? 160.238 161.844 216.885 1.00 24.28  ? 2893 VAL A CG1   1 
ATOM   10749 C  CG2   . VAL A 1 2893 ? 161.233 163.795 218.055 1.00 25.77  ? 2893 VAL A CG2   1 
ATOM   10750 N  N     . LYS A 1 2894 ? 159.090 160.203 220.094 1.00 26.21  ? 2894 LYS A N     1 
ATOM   10751 C  CA    . LYS A 1 2894 ? 158.367 158.940 220.212 1.00 25.13  ? 2894 LYS A CA    1 
ATOM   10752 C  C     . LYS A 1 2894 ? 156.940 159.166 220.702 1.00 24.50  ? 2894 LYS A C     1 
ATOM   10753 O  O     . LYS A 1 2894 ? 155.983 158.595 220.161 1.00 27.77  ? 2894 LYS A O     1 
ATOM   10754 C  CB    . LYS A 1 2894 ? 159.121 157.997 221.151 1.00 27.08  ? 2894 LYS A CB    1 
ATOM   10755 C  CG    . LYS A 1 2894 ? 158.484 156.627 221.310 1.00 32.12  ? 2894 LYS A CG    1 
ATOM   10756 C  CD    . LYS A 1 2894 ? 158.445 155.878 219.989 1.00 34.00  ? 2894 LYS A CD    1 
ATOM   10757 C  CE    . LYS A 1 2894 ? 159.845 155.552 219.498 1.00 30.36  ? 2894 LYS A CE    1 
ATOM   10758 N  NZ    . LYS A 1 2894 ? 160.521 154.552 220.370 1.00 27.21  ? 2894 LYS A NZ    1 
ATOM   10759 N  N     . ALA A 1 2895 ? 156.777 160.005 221.726 1.00 25.95  ? 2895 ALA A N     1 
ATOM   10760 C  CA    . ALA A 1 2895 ? 155.436 160.304 222.227 1.00 25.88  ? 2895 ALA A CA    1 
ATOM   10761 C  C     . ALA A 1 2895 ? 154.597 161.011 221.166 1.00 25.76  ? 2895 ALA A C     1 
ATOM   10762 O  O     . ALA A 1 2895 ? 153.422 160.672 220.944 1.00 28.23  ? 2895 ALA A O     1 
ATOM   10763 C  CB    . ALA A 1 2895 ? 155.527 161.148 223.497 1.00 23.18  ? 2895 ALA A CB    1 
ATOM   10764 N  N     . ARG A 1 2896 ? 155.189 162.000 220.490 1.00 25.39  ? 2896 ARG A N     1 
ATOM   10765 C  CA    . ARG A 1 2896 ? 154.459 162.714 219.451 1.00 26.38  ? 2896 ARG A CA    1 
ATOM   10766 C  C     . ARG A 1 2896 ? 154.125 161.805 218.278 1.00 25.60  ? 2896 ARG A C     1 
ATOM   10767 O  O     . ARG A 1 2896 ? 153.087 161.986 217.642 1.00 23.10  ? 2896 ARG A O     1 
ATOM   10768 C  CB    . ARG A 1 2896 ? 155.257 163.928 218.977 1.00 25.93  ? 2896 ARG A CB    1 
ATOM   10769 C  CG    . ARG A 1 2896 ? 155.498 164.977 220.052 1.00 26.72  ? 2896 ARG A CG    1 
ATOM   10770 C  CD    . ARG A 1 2896 ? 154.275 165.183 220.929 1.00 23.51  ? 2896 ARG A CD    1 
ATOM   10771 N  NE    . ARG A 1 2896 ? 153.186 165.838 220.216 1.00 21.22  ? 2896 ARG A NE    1 
ATOM   10772 C  CZ    . ARG A 1 2896 ? 151.918 165.808 220.601 1.00 25.82  ? 2896 ARG A CZ    1 
ATOM   10773 N  NH1   . ARG A 1 2896 ? 151.541 165.154 221.687 1.00 19.97  ? 2896 ARG A NH1   1 
ATOM   10774 N  NH2   . ARG A 1 2896 ? 151.005 166.450 219.879 1.00 30.49  ? 2896 ARG A NH2   1 
ATOM   10775 N  N     . LEU A 1 2897 ? 154.973 160.816 217.987 1.00 23.83  ? 2897 LEU A N     1 
ATOM   10776 C  CA    . LEU A 1 2897 ? 154.667 159.850 216.939 1.00 22.12  ? 2897 LEU A CA    1 
ATOM   10777 C  C     . LEU A 1 2897 ? 153.546 158.912 217.349 1.00 26.91  ? 2897 LEU A C     1 
ATOM   10778 O  O     . LEU A 1 2897 ? 152.753 158.499 216.501 1.00 27.59  ? 2897 LEU A O     1 
ATOM   10779 C  CB    . LEU A 1 2897 ? 155.911 159.045 216.571 1.00 18.04  ? 2897 LEU A CB    1 
ATOM   10780 C  CG    . LEU A 1 2897 ? 156.872 159.675 215.568 1.00 25.64  ? 2897 LEU A CG    1 
ATOM   10781 C  CD1   . LEU A 1 2897 ? 158.066 158.771 215.364 1.00 25.05  ? 2897 LEU A CD1   1 
ATOM   10782 C  CD2   . LEU A 1 2897 ? 156.160 159.909 214.250 1.00 24.01  ? 2897 LEU A CD2   1 
ATOM   10783 N  N     . LYS A 1 2898 ? 153.469 158.548 218.629 1.00 26.68  ? 2898 LYS A N     1 
ATOM   10784 C  CA    . LYS A 1 2898 ? 152.316 157.784 219.095 1.00 27.27  ? 2898 LYS A CA    1 
ATOM   10785 C  C     . LYS A 1 2898 ? 151.028 158.572 218.881 1.00 25.95  ? 2898 LYS A C     1 
ATOM   10786 O  O     . LYS A 1 2898 ? 150.035 158.048 218.351 1.00 29.61  ? 2898 LYS A O     1 
ATOM   10787 C  CB    . LYS A 1 2898 ? 152.491 157.421 220.568 1.00 27.18  ? 2898 LYS A CB    1 
ATOM   10788 C  CG    . LYS A 1 2898 ? 151.370 156.571 221.130 1.00 32.22  ? 2898 LYS A CG    1 
ATOM   10789 C  CD    . LYS A 1 2898 ? 151.411 156.541 222.645 1.00 33.65  ? 2898 LYS A CD    1 
ATOM   10790 C  CE    . LYS A 1 2898 ? 150.011 156.617 223.227 1.00 35.77  ? 2898 LYS A CE    1 
ATOM   10791 N  NZ    . LYS A 1 2898 ? 149.378 157.937 222.953 1.00 32.25  ? 2898 LYS A NZ    1 
ATOM   10792 N  N     . VAL A 1 2899 ? 151.038 159.849 219.267 1.00 27.80  ? 2899 VAL A N     1 
ATOM   10793 C  CA    . VAL A 1 2899 ? 149.860 160.690 219.052 1.00 28.28  ? 2899 VAL A CA    1 
ATOM   10794 C  C     . VAL A 1 2899 ? 149.577 160.845 217.560 1.00 27.99  ? 2899 VAL A C     1 
ATOM   10795 O  O     . VAL A 1 2899 ? 148.418 160.882 217.131 1.00 28.26  ? 2899 VAL A O     1 
ATOM   10796 C  CB    . VAL A 1 2899 ? 150.041 162.054 219.743 1.00 28.88  ? 2899 VAL A CB    1 
ATOM   10797 C  CG1   . VAL A 1 2899 ? 148.772 162.883 219.622 1.00 24.80  ? 2899 VAL A CG1   1 
ATOM   10798 C  CG2   . VAL A 1 2899 ? 150.416 161.858 221.202 1.00 24.55  ? 2899 VAL A CG2   1 
ATOM   10799 N  N     . PHE A 1 2900 ? 150.635 160.940 216.752 1.00 29.78  ? 2900 PHE A N     1 
ATOM   10800 C  CA    . PHE A 1 2900 ? 150.496 161.064 215.305 1.00 21.52  ? 2900 PHE A CA    1 
ATOM   10801 C  C     . PHE A 1 2900 ? 149.847 159.824 214.705 1.00 25.20  ? 2900 PHE A C     1 
ATOM   10802 O  O     . PHE A 1 2900 ? 148.983 159.928 213.829 1.00 27.70  ? 2900 PHE A O     1 
ATOM   10803 C  CB    . PHE A 1 2900 ? 151.878 161.312 214.696 1.00 19.95  ? 2900 PHE A CB    1 
ATOM   10804 C  CG    . PHE A 1 2900 ? 151.874 161.545 213.213 1.00 18.42  ? 2900 PHE A CG    1 
ATOM   10805 C  CD1   . PHE A 1 2900 ? 151.302 162.684 212.677 1.00 13.85  ? 2900 PHE A CD1   1 
ATOM   10806 C  CD2   . PHE A 1 2900 ? 152.471 160.635 212.357 1.00 20.29  ? 2900 PHE A CD2   1 
ATOM   10807 C  CE1   . PHE A 1 2900 ? 151.315 162.904 211.314 1.00 13.91  ? 2900 PHE A CE1   1 
ATOM   10808 C  CE2   . PHE A 1 2900 ? 152.481 160.849 210.993 1.00 15.11  ? 2900 PHE A CE2   1 
ATOM   10809 C  CZ    . PHE A 1 2900 ? 151.902 161.982 210.472 1.00 13.14  ? 2900 PHE A CZ    1 
ATOM   10810 N  N     . TYR A 1 2901 ? 150.256 158.639 215.163 1.00 29.74  ? 2901 TYR A N     1 
ATOM   10811 C  CA    . TYR A 1 2901 ? 149.626 157.403 214.713 1.00 24.96  ? 2901 TYR A CA    1 
ATOM   10812 C  C     . TYR A 1 2901 ? 148.156 157.377 215.093 1.00 28.58  ? 2901 TYR A C     1 
ATOM   10813 O  O     . TYR A 1 2901 ? 147.304 156.982 214.289 1.00 34.89  ? 2901 TYR A O     1 
ATOM   10814 C  CB    . TYR A 1 2901 ? 150.336 156.189 215.314 1.00 26.18  ? 2901 TYR A CB    1 
ATOM   10815 C  CG    . TYR A 1 2901 ? 151.813 156.091 215.014 1.00 23.63  ? 2901 TYR A CG    1 
ATOM   10816 C  CD1   . TYR A 1 2901 ? 152.355 156.665 213.874 1.00 25.92  ? 2901 TYR A CD1   1 
ATOM   10817 C  CD2   . TYR A 1 2901 ? 152.667 155.422 215.879 1.00 22.05  ? 2901 TYR A CD2   1 
ATOM   10818 C  CE1   . TYR A 1 2901 ? 153.707 156.574 213.605 1.00 28.82  ? 2901 TYR A CE1   1 
ATOM   10819 C  CE2   . TYR A 1 2901 ? 154.017 155.327 215.619 1.00 24.05  ? 2901 TYR A CE2   1 
ATOM   10820 C  CZ    . TYR A 1 2901 ? 154.532 155.903 214.481 1.00 25.80  ? 2901 TYR A CZ    1 
ATOM   10821 O  OH    . TYR A 1 2901 ? 155.879 155.809 214.220 1.00 29.24  ? 2901 TYR A OH    1 
ATOM   10822 N  N     . GLU A 1 2902 ? 147.839 157.792 216.323 1.00 33.87  ? 2902 GLU A N     1 
ATOM   10823 C  CA    . GLU A 1 2902 ? 146.447 157.776 216.763 1.00 28.40  ? 2902 GLU A CA    1 
ATOM   10824 C  C     . GLU A 1 2902 ? 145.589 158.742 215.952 1.00 28.52  ? 2902 GLU A C     1 
ATOM   10825 O  O     . GLU A 1 2902 ? 144.459 158.411 215.574 1.00 36.17  ? 2902 GLU A O     1 
ATOM   10826 C  CB    . GLU A 1 2902 ? 146.363 158.104 218.252 1.00 35.86  ? 2902 GLU A CB    1 
ATOM   10827 C  CG    . GLU A 1 2902 ? 146.969 157.041 219.151 1.00 37.79  ? 2902 GLU A CG    1 
ATOM   10828 C  CD    . GLU A 1 2902 ? 146.929 157.428 220.614 1.00 45.45  ? 2902 GLU A CD    1 
ATOM   10829 O  OE1   . GLU A 1 2902 ? 146.527 158.571 220.918 1.00 47.36  ? 2902 GLU A OE1   1 
ATOM   10830 O  OE2   . GLU A 1 2902 ? 147.294 156.587 221.461 1.00 44.86  ? 2902 GLU A OE2   1 
ATOM   10831 N  N     . GLU A 1 2903 ? 146.108 159.936 215.666 1.00 32.12  ? 2903 GLU A N     1 
ATOM   10832 C  CA    . GLU A 1 2903 ? 145.317 160.990 215.037 1.00 36.53  ? 2903 GLU A CA    1 
ATOM   10833 C  C     . GLU A 1 2903 ? 145.501 161.054 213.526 1.00 35.04  ? 2903 GLU A C     1 
ATOM   10834 O  O     . GLU A 1 2903 ? 144.556 161.376 212.799 1.00 37.36  ? 2903 GLU A O     1 
ATOM   10835 C  CB    . GLU A 1 2903 ? 145.676 162.346 215.648 1.00 35.14  ? 2903 GLU A CB    1 
ATOM   10836 C  CG    . GLU A 1 2903 ? 145.459 162.438 217.147 1.00 42.26  ? 2903 GLU A CG    1 
ATOM   10837 C  CD    . GLU A 1 2903 ? 144.990 163.813 217.576 1.00 58.88  ? 2903 GLU A CD    1 
ATOM   10838 O  OE1   . GLU A 1 2903 ? 145.629 164.809 217.178 1.00 49.29  ? 2903 GLU A OE1   1 
ATOM   10839 O  OE2   . GLU A 1 2903 ? 143.983 163.899 218.309 1.00 64.64  ? 2903 GLU A OE2   1 
ATOM   10840 N  N     . GLU A 1 2904 ? 146.701 160.760 213.042 1.00 35.07  ? 2904 GLU A N     1 
ATOM   10841 C  CA    . GLU A 1 2904 ? 147.041 160.904 211.632 1.00 32.85  ? 2904 GLU A CA    1 
ATOM   10842 C  C     . GLU A 1 2904 ? 147.604 159.570 211.149 1.00 32.98  ? 2904 GLU A C     1 
ATOM   10843 O  O     . GLU A 1 2904 ? 147.419 158.527 211.787 1.00 41.92  ? 2904 GLU A O     1 
ATOM   10844 C  CB    . GLU A 1 2904 ? 148.016 162.067 211.414 1.00 34.05  ? 2904 GLU A CB    1 
ATOM   10845 C  CG    . GLU A 1 2904 ? 147.519 163.413 211.903 1.00 34.96  ? 2904 GLU A CG    1 
ATOM   10846 C  CD    . GLU A 1 2904 ? 146.549 164.060 210.938 1.00 41.25  ? 2904 GLU A CD    1 
ATOM   10847 O  OE1   . GLU A 1 2904 ? 146.926 164.265 209.765 1.00 38.36  ? 2904 GLU A OE1   1 
ATOM   10848 O  OE2   . GLU A 1 2904 ? 145.413 164.369 211.351 1.00 49.36  ? 2904 GLU A OE2   1 
ATOM   10849 N  N     . LEU A 1 2905 ? 148.262 159.607 209.989 1.00 29.21  ? 2905 LEU A N     1 
ATOM   10850 C  CA    . LEU A 1 2905 ? 148.840 158.438 209.333 1.00 31.95  ? 2905 LEU A CA    1 
ATOM   10851 C  C     . LEU A 1 2905 ? 149.437 157.455 210.333 1.00 33.21  ? 2905 LEU A C     1 
ATOM   10852 O  O     . LEU A 1 2905 ? 150.252 157.827 211.180 1.00 28.87  ? 2905 LEU A O     1 
ATOM   10853 C  CB    . LEU A 1 2905 ? 149.919 158.899 208.353 1.00 30.52  ? 2905 LEU A CB    1 
ATOM   10854 C  CG    . LEU A 1 2905 ? 150.130 158.035 207.118 1.00 28.96  ? 2905 LEU A CG    1 
ATOM   10855 C  CD1   . LEU A 1 2905 ? 148.865 158.078 206.290 1.00 34.45  ? 2905 LEU A CD1   1 
ATOM   10856 C  CD2   . LEU A 1 2905 ? 151.320 158.533 206.319 1.00 26.44  ? 2905 LEU A CD2   1 
ATOM   10857 N  N     . ASP A 1 2906 ? 149.023 156.192 210.222 1.00 32.33  ? 2906 ASP A N     1 
ATOM   10858 C  CA    . ASP A 1 2906 ? 149.353 155.164 211.198 1.00 29.90  ? 2906 ASP A CA    1 
ATOM   10859 C  C     . ASP A 1 2906 ? 150.434 154.219 210.674 1.00 32.87  ? 2906 ASP A C     1 
ATOM   10860 O  O     . ASP A 1 2906 ? 150.336 153.001 210.853 1.00 37.22  ? 2906 ASP A O     1 
ATOM   10861 C  CB    . ASP A 1 2906 ? 148.082 154.394 211.584 1.00 35.27  ? 2906 ASP A CB    1 
ATOM   10862 C  CG    . ASP A 1 2906 ? 148.240 153.556 212.857 1.00 38.78  ? 2906 ASP A CG    1 
ATOM   10863 O  OD1   . ASP A 1 2906 ? 149.350 153.091 213.184 1.00 30.91  ? 2906 ASP A OD1   1 
ATOM   10864 O  OD2   . ASP A 1 2906 ? 147.217 153.361 213.546 1.00 50.67  ? 2906 ASP A OD2   1 
ATOM   10865 N  N     . VAL A 1 2907 ? 151.430 154.747 209.973 1.00 32.32  ? 2907 VAL A N     1 
ATOM   10866 C  CA    . VAL A 1 2907 ? 152.559 153.930 209.539 1.00 29.66  ? 2907 VAL A CA    1 
ATOM   10867 C  C     . VAL A 1 2907 ? 153.630 153.986 210.623 1.00 31.64  ? 2907 VAL A C     1 
ATOM   10868 O  O     . VAL A 1 2907 ? 154.121 155.072 210.963 1.00 33.54  ? 2907 VAL A O     1 
ATOM   10869 C  CB    . VAL A 1 2907 ? 153.080 154.374 208.159 1.00 29.47  ? 2907 VAL A CB    1 
ATOM   10870 C  CG1   . VAL A 1 2907 ? 151.992 154.198 207.115 1.00 33.57  ? 2907 VAL A CG1   1 
ATOM   10871 C  CG2   . VAL A 1 2907 ? 153.526 155.828 208.171 1.00 28.12  ? 2907 VAL A CG2   1 
ATOM   10872 N  N     . PRO A 1 2908 ? 153.984 152.856 211.230 1.00 31.14  ? 2908 PRO A N     1 
ATOM   10873 C  CA    . PRO A 1 2908 ? 155.009 152.875 212.278 1.00 25.07  ? 2908 PRO A CA    1 
ATOM   10874 C  C     . PRO A 1 2908 ? 156.362 153.278 211.718 1.00 26.85  ? 2908 PRO A C     1 
ATOM   10875 O  O     . PRO A 1 2908 ? 156.715 152.953 210.582 1.00 32.95  ? 2908 PRO A O     1 
ATOM   10876 C  CB    . PRO A 1 2908 ? 155.025 151.432 212.794 1.00 28.66  ? 2908 PRO A CB    1 
ATOM   10877 C  CG    . PRO A 1 2908 ? 153.756 150.814 212.285 1.00 33.65  ? 2908 PRO A CG    1 
ATOM   10878 C  CD    . PRO A 1 2908 ? 153.460 151.502 210.997 1.00 31.61  ? 2908 PRO A CD    1 
ATOM   10879 N  N     . LEU A 1 2909 ? 157.126 153.994 212.537 1.00 20.93  ? 2909 LEU A N     1 
ATOM   10880 C  CA    . LEU A 1 2909 ? 158.427 154.503 212.139 1.00 19.65  ? 2909 LEU A CA    1 
ATOM   10881 C  C     . LEU A 1 2909 ? 159.481 154.080 213.148 1.00 25.45  ? 2909 LEU A C     1 
ATOM   10882 O  O     . LEU A 1 2909 ? 159.208 153.953 214.344 1.00 31.41  ? 2909 LEU A O     1 
ATOM   10883 C  CB    . LEU A 1 2909 ? 158.421 156.033 212.012 1.00 19.51  ? 2909 LEU A CB    1 
ATOM   10884 C  CG    . LEU A 1 2909 ? 157.365 156.658 211.100 1.00 18.94  ? 2909 LEU A CG    1 
ATOM   10885 C  CD1   . LEU A 1 2909 ? 157.538 158.166 211.055 1.00 24.62  ? 2909 LEU A CD1   1 
ATOM   10886 C  CD2   . LEU A 1 2909 ? 157.436 156.067 209.704 1.00 16.35  ? 2909 LEU A CD2   1 
ATOM   10887 N  N     . VAL A 1 2910 ? 160.693 153.862 212.649 1.00 24.09  ? 2910 VAL A N     1 
ATOM   10888 C  CA    . VAL A 1 2910 ? 161.845 153.542 213.482 1.00 22.67  ? 2910 VAL A CA    1 
ATOM   10889 C  C     . VAL A 1 2910 ? 162.668 154.811 213.638 1.00 23.51  ? 2910 VAL A C     1 
ATOM   10890 O  O     . VAL A 1 2910 ? 163.053 155.438 212.643 1.00 22.49  ? 2910 VAL A O     1 
ATOM   10891 C  CB    . VAL A 1 2910 ? 162.685 152.408 212.873 1.00 15.58  ? 2910 VAL A CB    1 
ATOM   10892 C  CG1   . VAL A 1 2910 ? 163.873 152.096 213.764 1.00 14.97  ? 2910 VAL A CG1   1 
ATOM   10893 C  CG2   . VAL A 1 2910 ? 161.829 151.171 212.659 1.00 17.25  ? 2910 VAL A CG2   1 
ATOM   10894 N  N     . LEU A 1 2911 ? 162.934 155.195 214.881 1.00 18.99  ? 2911 LEU A N     1 
ATOM   10895 C  CA    . LEU A 1 2911 ? 163.672 156.415 215.167 1.00 18.80  ? 2911 LEU A CA    1 
ATOM   10896 C  C     . LEU A 1 2911 ? 165.162 156.124 215.266 1.00 28.31  ? 2911 LEU A C     1 
ATOM   10897 O  O     . LEU A 1 2911 ? 165.589 155.294 216.074 1.00 42.02  ? 2911 LEU A O     1 
ATOM   10898 C  CB    . LEU A 1 2911 ? 163.180 157.055 216.464 1.00 21.46  ? 2911 LEU A CB    1 
ATOM   10899 C  CG    . LEU A 1 2911 ? 161.787 157.676 216.433 1.00 23.60  ? 2911 LEU A CG    1 
ATOM   10900 C  CD1   . LEU A 1 2911 ? 161.556 158.504 217.680 1.00 23.51  ? 2911 LEU A CD1   1 
ATOM   10901 C  CD2   . LEU A 1 2911 ? 161.633 158.529 215.188 1.00 24.81  ? 2911 LEU A CD2   1 
ATOM   10902 N  N     . PHE A 1 2912 ? 165.945 156.806 214.436 1.00 21.24  ? 2912 PHE A N     1 
ATOM   10903 C  CA    . PHE A 1 2912 ? 167.391 156.855 214.571 1.00 19.99  ? 2912 PHE A CA    1 
ATOM   10904 C  C     . PHE A 1 2912 ? 167.819 158.318 214.544 1.00 18.43  ? 2912 PHE A C     1 
ATOM   10905 O  O     . PHE A 1 2912 ? 166.991 159.225 214.424 1.00 23.06  ? 2912 PHE A O     1 
ATOM   10906 C  CB    . PHE A 1 2912 ? 168.103 156.030 213.486 1.00 16.08  ? 2912 PHE A CB    1 
ATOM   10907 C  CG    . PHE A 1 2912 ? 167.515 156.171 212.107 1.00 15.42  ? 2912 PHE A CG    1 
ATOM   10908 C  CD1   . PHE A 1 2912 ? 166.394 155.449 211.736 1.00 14.11  ? 2912 PHE A CD1   1 
ATOM   10909 C  CD2   . PHE A 1 2912 ? 168.101 157.007 211.174 1.00 15.96  ? 2912 PHE A CD2   1 
ATOM   10910 C  CE1   . PHE A 1 2912 ? 165.862 155.572 210.466 1.00 14.10  ? 2912 PHE A CE1   1 
ATOM   10911 C  CE2   . PHE A 1 2912 ? 167.572 157.133 209.904 1.00 11.01  ? 2912 PHE A CE2   1 
ATOM   10912 C  CZ    . PHE A 1 2912 ? 166.454 156.413 209.550 1.00 9.76   ? 2912 PHE A CZ    1 
ATOM   10913 N  N     . ASN A 1 2913 ? 169.128 158.546 214.666 1.00 16.42  ? 2913 ASN A N     1 
ATOM   10914 C  CA    . ASN A 1 2913 ? 169.631 159.908 214.817 1.00 19.80  ? 2913 ASN A CA    1 
ATOM   10915 C  C     . ASN A 1 2913 ? 169.318 160.761 213.592 1.00 24.29  ? 2913 ASN A C     1 
ATOM   10916 O  O     . ASN A 1 2913 ? 168.981 161.947 213.719 1.00 26.81  ? 2913 ASN A O     1 
ATOM   10917 C  CB    . ASN A 1 2913 ? 171.134 159.876 215.088 1.00 23.59  ? 2913 ASN A CB    1 
ATOM   10918 C  CG    . ASN A 1 2913 ? 171.493 158.979 216.256 1.00 21.52  ? 2913 ASN A CG    1 
ATOM   10919 O  OD1   . ASN A 1 2913 ? 170.618 158.408 216.906 1.00 14.67  ? 2913 ASN A OD1   1 
ATOM   10920 N  ND2   . ASN A 1 2913 ? 172.785 158.851 216.529 1.00 23.81  ? 2913 ASN A ND2   1 
ATOM   10921 N  N     . GLU A 1 2914 ? 169.422 160.175 212.398 1.00 19.53  ? 2914 GLU A N     1 
ATOM   10922 C  CA    . GLU A 1 2914 ? 169.159 160.931 211.178 1.00 17.82  ? 2914 GLU A CA    1 
ATOM   10923 C  C     . GLU A 1 2914 ? 167.712 161.404 211.120 1.00 18.41  ? 2914 GLU A C     1 
ATOM   10924 O  O     . GLU A 1 2914 ? 167.432 162.498 210.621 1.00 22.20  ? 2914 GLU A O     1 
ATOM   10925 C  CB    . GLU A 1 2914 ? 169.504 160.086 209.954 1.00 19.21  ? 2914 GLU A CB    1 
ATOM   10926 C  CG    . GLU A 1 2914 ? 170.980 159.744 209.840 1.00 23.69  ? 2914 GLU A CG    1 
ATOM   10927 C  CD    . GLU A 1 2914 ? 171.412 159.481 208.411 1.00 35.07  ? 2914 GLU A CD    1 
ATOM   10928 O  OE1   . GLU A 1 2914 ? 170.584 158.981 207.618 1.00 33.90  ? 2914 GLU A OE1   1 
ATOM   10929 O  OE2   . GLU A 1 2914 ? 172.580 159.772 208.080 1.00 32.20  ? 2914 GLU A OE2   1 
ATOM   10930 N  N     . VAL A 1 2915 ? 166.777 160.595 211.626 1.00 15.65  ? 2915 VAL A N     1 
ATOM   10931 C  CA    . VAL A 1 2915 ? 165.379 161.018 211.667 1.00 16.18  ? 2915 VAL A CA    1 
ATOM   10932 C  C     . VAL A 1 2915 ? 165.219 162.249 212.546 1.00 14.45  ? 2915 VAL A C     1 
ATOM   10933 O  O     . VAL A 1 2915 ? 164.514 163.200 212.187 1.00 15.19  ? 2915 VAL A O     1 
ATOM   10934 C  CB    . VAL A 1 2915 ? 164.477 159.866 212.148 1.00 15.05  ? 2915 VAL A CB    1 
ATOM   10935 C  CG1   . VAL A 1 2915 ? 163.047 160.350 212.307 1.00 16.10  ? 2915 VAL A CG1   1 
ATOM   10936 C  CG2   . VAL A 1 2915 ? 164.524 158.724 211.170 1.00 13.57  ? 2915 VAL A CG2   1 
ATOM   10937 N  N     . LEU A 1 2916 ? 165.857 162.245 213.718 1.00 13.75  ? 2916 LEU A N     1 
ATOM   10938 C  CA    . LEU A 1 2916 ? 165.769 163.397 214.608 1.00 15.65  ? 2916 LEU A CA    1 
ATOM   10939 C  C     . LEU A 1 2916 ? 166.369 164.637 213.959 1.00 15.82  ? 2916 LEU A C     1 
ATOM   10940 O  O     . LEU A 1 2916 ? 165.783 165.726 214.020 1.00 14.36  ? 2916 LEU A O     1 
ATOM   10941 C  CB    . LEU A 1 2916 ? 166.464 163.085 215.932 1.00 20.64  ? 2916 LEU A CB    1 
ATOM   10942 C  CG    . LEU A 1 2916 ? 165.950 161.848 216.672 1.00 16.52  ? 2916 LEU A CG    1 
ATOM   10943 C  CD1   . LEU A 1 2916 ? 166.651 161.685 218.009 1.00 17.07  ? 2916 LEU A CD1   1 
ATOM   10944 C  CD2   . LEU A 1 2916 ? 164.445 161.928 216.864 1.00 15.51  ? 2916 LEU A CD2   1 
ATOM   10945 N  N     . ASP A 1 2917 ? 167.527 164.488 213.312 1.00 19.74  ? 2917 ASP A N     1 
ATOM   10946 C  CA    . ASP A 1 2917 ? 168.135 165.628 212.633 1.00 15.53  ? 2917 ASP A CA    1 
ATOM   10947 C  C     . ASP A 1 2917 ? 167.228 166.163 211.530 1.00 16.07  ? 2917 ASP A C     1 
ATOM   10948 O  O     . ASP A 1 2917 ? 167.048 167.381 211.398 1.00 27.15  ? 2917 ASP A O     1 
ATOM   10949 C  CB    . ASP A 1 2917 ? 169.496 165.232 212.062 1.00 17.53  ? 2917 ASP A CB    1 
ATOM   10950 C  CG    . ASP A 1 2917 ? 170.389 164.574 213.092 1.00 33.55  ? 2917 ASP A CG    1 
ATOM   10951 O  OD1   . ASP A 1 2917 ? 170.069 164.658 214.296 1.00 39.42  ? 2917 ASP A OD1   1 
ATOM   10952 O  OD2   . ASP A 1 2917 ? 171.411 163.972 212.700 1.00 38.14  ? 2917 ASP A OD2   1 
ATOM   10953 N  N     . HIS A 1 2918 ? 166.636 165.268 210.739 1.00 12.69  ? 2918 HIS A N     1 
ATOM   10954 C  CA    . HIS A 1 2918 ? 165.790 165.698 209.632 1.00 13.17  ? 2918 HIS A CA    1 
ATOM   10955 C  C     . HIS A 1 2918 ? 164.525 166.388 210.126 1.00 14.21  ? 2918 HIS A C     1 
ATOM   10956 O  O     . HIS A 1 2918 ? 164.111 167.407 209.561 1.00 24.85  ? 2918 HIS A O     1 
ATOM   10957 C  CB    . HIS A 1 2918 ? 165.443 164.504 208.745 1.00 16.95  ? 2918 HIS A CB    1 
ATOM   10958 C  CG    . HIS A 1 2918 ? 166.622 163.926 208.026 1.00 17.20  ? 2918 HIS A CG    1 
ATOM   10959 N  ND1   . HIS A 1 2918 ? 166.603 162.676 207.447 1.00 15.48  ? 2918 HIS A ND1   1 
ATOM   10960 C  CD2   . HIS A 1 2918 ? 167.859 164.428 207.797 1.00 16.42  ? 2918 HIS A CD2   1 
ATOM   10961 C  CE1   . HIS A 1 2918 ? 167.775 162.434 206.889 1.00 22.03  ? 2918 HIS A CE1   1 
ATOM   10962 N  NE2   . HIS A 1 2918 ? 168.555 163.481 207.088 1.00 19.71  ? 2918 HIS A NE2   1 
ATOM   10963 N  N     . VAL A 1 2919 ? 163.887 165.848 211.167 1.00 13.59  ? 2919 VAL A N     1 
ATOM   10964 C  CA    . VAL A 1 2919 ? 162.678 166.489 211.674 1.00 12.47  ? 2919 VAL A CA    1 
ATOM   10965 C  C     . VAL A 1 2919 ? 163.015 167.838 212.295 1.00 10.86  ? 2919 VAL A C     1 
ATOM   10966 O  O     . VAL A 1 2919 ? 162.236 168.791 212.188 1.00 12.93  ? 2919 VAL A O     1 
ATOM   10967 C  CB    . VAL A 1 2919 ? 161.920 165.569 212.654 1.00 13.10  ? 2919 VAL A CB    1 
ATOM   10968 C  CG1   . VAL A 1 2919 ? 161.537 164.266 211.973 1.00 12.07  ? 2919 VAL A CG1   1 
ATOM   10969 C  CG2   . VAL A 1 2919 ? 162.720 165.307 213.914 1.00 10.26  ? 2919 VAL A CG2   1 
ATOM   10970 N  N     . LEU A 1 2920 ? 164.185 167.954 212.932 1.00 10.45  ? 2920 LEU A N     1 
ATOM   10971 C  CA    . LEU A 1 2920 ? 164.605 169.254 213.446 1.00 9.68   ? 2920 LEU A CA    1 
ATOM   10972 C  C     . LEU A 1 2920 ? 164.804 170.258 212.316 1.00 12.29  ? 2920 LEU A C     1 
ATOM   10973 O  O     . LEU A 1 2920 ? 164.386 171.416 212.426 1.00 12.22  ? 2920 LEU A O     1 
ATOM   10974 C  CB    . LEU A 1 2920 ? 165.883 169.107 214.269 1.00 8.74   ? 2920 LEU A CB    1 
ATOM   10975 C  CG    . LEU A 1 2920 ? 165.707 168.524 215.671 1.00 9.16   ? 2920 LEU A CG    1 
ATOM   10976 C  CD1   . LEU A 1 2920 ? 166.959 168.736 216.501 1.00 10.71  ? 2920 LEU A CD1   1 
ATOM   10977 C  CD2   . LEU A 1 2920 ? 164.495 169.128 216.357 1.00 9.26   ? 2920 LEU A CD2   1 
ATOM   10978 N  N     . ARG A 1 2921 ? 165.432 169.831 211.217 1.00 11.23  ? 2921 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2921 ? 165.623 170.730 210.081 1.00 11.61  ? 2921 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2921 ? 164.289 171.159 209.477 1.00 15.02  ? 2921 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2921 ? 164.093 172.337 209.140 1.00 22.78  ? 2921 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2921 ? 166.496 170.056 209.023 1.00 12.18  ? 2921 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2921 ? 167.901 169.732 209.495 1.00 13.52  ? 2921 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2921 ? 168.674 168.957 208.446 1.00 12.83  ? 2921 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2921 ? 169.747 168.170 209.038 1.00 14.62  ? 2921 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2921 ? 170.546 167.361 208.357 1.00 21.02  ? 2921 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2921 ? 170.423 167.210 207.049 1.00 19.91  ? 2921 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2921 ? 171.493 166.688 209.004 1.00 18.95  ? 2921 ARG A NH2   1 
ATOM   10989 N  N     . ILE A 1 2922 ? 163.357 170.217 209.332 1.00 9.15   ? 2922 ILE A N     1 
ATOM   10990 C  CA    . ILE A 1 2922 ? 162.062 170.544 208.747 1.00 10.60  ? 2922 ILE A CA    1 
ATOM   10991 C  C     . ILE A 1 2922 ? 161.283 171.483 209.662 1.00 12.93  ? 2922 ILE A C     1 
ATOM   10992 O  O     . ILE A 1 2922 ? 160.603 172.406 209.195 1.00 13.80  ? 2922 ILE A O     1 
ATOM   10993 C  CB    . ILE A 1 2922 ? 161.280 169.254 208.439 1.00 14.17  ? 2922 ILE A CB    1 
ATOM   10994 C  CG1   . ILE A 1 2922 ? 162.025 168.419 207.398 1.00 11.46  ? 2922 ILE A CG1   1 
ATOM   10995 C  CG2   . ILE A 1 2922 ? 159.902 169.580 207.912 1.00 10.98  ? 2922 ILE A CG2   1 
ATOM   10996 C  CD1   . ILE A 1 2922 ? 161.421 167.055 207.168 1.00 9.39   ? 2922 ILE A CD1   1 
ATOM   10997 N  N     . ASP A 1 2923 ? 161.374 171.271 210.979 1.00 13.16  ? 2923 ASP A N     1 
ATOM   10998 C  CA    . ASP A 1 2923 ? 160.739 172.184 211.925 1.00 13.08  ? 2923 ASP A CA    1 
ATOM   10999 C  C     . ASP A 1 2923 ? 161.367 173.568 211.857 1.00 15.40  ? 2923 ASP A C     1 
ATOM   11000 O  O     . ASP A 1 2923 ? 160.674 174.581 212.007 1.00 18.37  ? 2923 ASP A O     1 
ATOM   11001 C  CB    . ASP A 1 2923 ? 160.837 171.618 213.340 1.00 13.97  ? 2923 ASP A CB    1 
ATOM   11002 C  CG    . ASP A 1 2923 ? 160.245 172.545 214.381 1.00 22.47  ? 2923 ASP A CG    1 
ATOM   11003 O  OD1   . ASP A 1 2923 ? 159.104 173.010 214.187 1.00 24.93  ? 2923 ASP A OD1   1 
ATOM   11004 O  OD2   . ASP A 1 2923 ? 160.922 172.810 215.397 1.00 23.13  ? 2923 ASP A OD2   1 
ATOM   11005 N  N     . ARG A 1 2924 ? 162.683 173.629 211.646 1.00 15.87  ? 2924 ARG A N     1 
ATOM   11006 C  CA    . ARG A 1 2924 ? 163.351 174.909 211.450 1.00 12.50  ? 2924 ARG A CA    1 
ATOM   11007 C  C     . ARG A 1 2924 ? 162.780 175.639 210.243 1.00 14.28  ? 2924 ARG A C     1 
ATOM   11008 O  O     . ARG A 1 2924 ? 162.505 176.843 210.298 1.00 18.11  ? 2924 ARG A O     1 
ATOM   11009 C  CB    . ARG A 1 2924 ? 164.853 174.687 211.272 1.00 12.39  ? 2924 ARG A CB    1 
ATOM   11010 C  CG    . ARG A 1 2924 ? 165.650 174.706 212.553 1.00 19.24  ? 2924 ARG A CG    1 
ATOM   11011 C  CD    . ARG A 1 2924 ? 167.137 174.659 212.258 1.00 18.48  ? 2924 ARG A CD    1 
ATOM   11012 N  NE    . ARG A 1 2924 ? 167.478 175.383 211.041 1.00 14.86  ? 2924 ARG A NE    1 
ATOM   11013 C  CZ    . ARG A 1 2924 ? 168.083 176.562 211.016 1.00 19.46  ? 2924 ARG A CZ    1 
ATOM   11014 N  NH1   . ARG A 1 2924 ? 168.421 177.188 212.132 1.00 17.27  ? 2924 ARG A NH1   1 
ATOM   11015 N  NH2   . ARG A 1 2924 ? 168.358 177.125 209.844 1.00 23.52  ? 2924 ARG A NH2   1 
ATOM   11016 N  N     . ILE A 1 2925 ? 162.596 174.918 209.137 1.00 16.13  ? 2925 ILE A N     1 
ATOM   11017 C  CA    . ILE A 1 2925 ? 162.139 175.568 207.911 1.00 16.05  ? 2925 ILE A CA    1 
ATOM   11018 C  C     . ILE A 1 2925 ? 160.678 175.999 208.023 1.00 13.27  ? 2925 ILE A C     1 
ATOM   11019 O  O     . ILE A 1 2925 ? 160.315 177.102 207.597 1.00 17.41  ? 2925 ILE A O     1 
ATOM   11020 C  CB    . ILE A 1 2925 ? 162.378 174.657 206.695 1.00 17.41  ? 2925 ILE A CB    1 
ATOM   11021 C  CG1   . ILE A 1 2925 ? 163.859 174.292 206.602 1.00 17.37  ? 2925 ILE A CG1   1 
ATOM   11022 C  CG2   . ILE A 1 2925 ? 161.927 175.349 205.422 1.00 11.12  ? 2925 ILE A CG2   1 
ATOM   11023 C  CD1   . ILE A 1 2925 ? 164.793 175.477 206.713 1.00 16.60  ? 2925 ILE A CD1   1 
ATOM   11024 N  N     . PHE A 1 2926 ? 159.816 175.150 208.594 1.00 13.94  ? 2926 PHE A N     1 
ATOM   11025 C  CA    . PHE A 1 2926 ? 158.400 175.502 208.704 1.00 14.84  ? 2926 PHE A CA    1 
ATOM   11026 C  C     . PHE A 1 2926 ? 158.145 176.696 209.614 1.00 19.82  ? 2926 PHE A C     1 
ATOM   11027 O  O     . PHE A 1 2926 ? 157.053 177.271 209.562 1.00 19.05  ? 2926 PHE A O     1 
ATOM   11028 C  CB    . PHE A 1 2926 ? 157.570 174.319 209.207 1.00 15.62  ? 2926 PHE A CB    1 
ATOM   11029 C  CG    . PHE A 1 2926 ? 157.405 173.215 208.206 1.00 14.32  ? 2926 PHE A CG    1 
ATOM   11030 C  CD1   . PHE A 1 2926 ? 157.700 173.420 206.870 1.00 17.21  ? 2926 PHE A CD1   1 
ATOM   11031 C  CD2   . PHE A 1 2926 ? 156.919 171.980 208.597 1.00 11.43  ? 2926 PHE A CD2   1 
ATOM   11032 C  CE1   . PHE A 1 2926 ? 157.535 172.407 205.949 1.00 18.29  ? 2926 PHE A CE1   1 
ATOM   11033 C  CE2   . PHE A 1 2926 ? 156.749 170.966 207.679 1.00 9.90   ? 2926 PHE A CE2   1 
ATOM   11034 C  CZ    . PHE A 1 2926 ? 157.059 171.179 206.354 1.00 11.73  ? 2926 PHE A CZ    1 
ATOM   11035 N  N     . ARG A 1 2927 ? 159.112 177.081 210.445 1.00 23.37  ? 2927 ARG A N     1 
ATOM   11036 C  CA    . ARG A 1 2927 ? 158.939 178.177 211.389 1.00 17.65  ? 2927 ARG A CA    1 
ATOM   11037 C  C     . ARG A 1 2927 ? 159.396 179.517 210.807 1.00 17.68  ? 2927 ARG A C     1 
ATOM   11038 O  O     . ARG A 1 2927 ? 159.422 180.533 211.512 1.00 21.36  ? 2927 ARG A O     1 
ATOM   11039 C  CB    . ARG A 1 2927 ? 159.674 177.835 212.690 1.00 21.73  ? 2927 ARG A CB    1 
ATOM   11040 C  CG    . ARG A 1 2927 ? 159.503 178.799 213.855 1.00 29.77  ? 2927 ARG A CG    1 
ATOM   11041 C  CD    . ARG A 1 2927 ? 160.229 178.289 215.087 1.00 31.13  ? 2927 ARG A CD    1 
ATOM   11042 N  NE    . ARG A 1 2927 ? 161.672 178.232 214.888 1.00 35.21  ? 2927 ARG A NE    1 
ATOM   11043 C  CZ    . ARG A 1 2927 ? 162.378 177.111 214.852 1.00 28.10  ? 2927 ARG A CZ    1 
ATOM   11044 N  NH1   . ARG A 1 2927 ? 161.804 175.929 215.000 1.00 21.54  ? 2927 ARG A NH1   1 
ATOM   11045 N  NH2   . ARG A 1 2927 ? 163.692 177.177 214.660 1.00 22.65  ? 2927 ARG A NH2   1 
ATOM   11046 N  N     . GLN A 1 2928 ? 159.715 179.551 209.517 1.00 20.76  ? 2928 GLN A N     1 
ATOM   11047 C  CA    . GLN A 1 2928 ? 160.210 180.744 208.852 1.00 15.61  ? 2928 GLN A CA    1 
ATOM   11048 C  C     . GLN A 1 2928 ? 159.196 181.238 207.834 1.00 20.17  ? 2928 GLN A C     1 
ATOM   11049 O  O     . GLN A 1 2928 ? 158.479 180.438 207.226 1.00 18.24  ? 2928 GLN A O     1 
ATOM   11050 C  CB    . GLN A 1 2928 ? 161.543 180.465 208.143 1.00 12.33  ? 2928 GLN A CB    1 
ATOM   11051 C  CG    . GLN A 1 2928 ? 162.761 180.566 209.039 1.00 20.96  ? 2928 GLN A CG    1 
ATOM   11052 C  CD    . GLN A 1 2928 ? 163.921 179.735 208.531 1.00 29.17  ? 2928 GLN A CD    1 
ATOM   11053 O  OE1   . GLN A 1 2928 ? 164.220 179.731 207.338 1.00 31.06  ? 2928 GLN A OE1   1 
ATOM   11054 N  NE2   . GLN A 1 2928 ? 164.579 179.022 209.437 1.00 28.12  ? 2928 GLN A NE2   1 
ATOM   11055 N  N     . PRO A 1 2929 ? 159.112 182.553 207.629 1.00 24.11  ? 2929 PRO A N     1 
ATOM   11056 C  CA    . PRO A 1 2929 ? 158.224 183.074 206.584 1.00 15.65  ? 2929 PRO A CA    1 
ATOM   11057 C  C     . PRO A 1 2929 ? 158.737 182.712 205.200 1.00 14.93  ? 2929 PRO A C     1 
ATOM   11058 O  O     . PRO A 1 2929 ? 159.937 182.780 204.926 1.00 16.34  ? 2929 PRO A O     1 
ATOM   11059 C  CB    . PRO A 1 2929 ? 158.255 184.588 206.815 1.00 18.97  ? 2929 PRO A CB    1 
ATOM   11060 C  CG    . PRO A 1 2929 ? 159.571 184.834 207.461 1.00 18.04  ? 2929 PRO A CG    1 
ATOM   11061 C  CD    . PRO A 1 2929 ? 159.843 183.629 208.320 1.00 22.76  ? 2929 PRO A CD    1 
ATOM   11062 N  N     . GLN A 1 2930 ? 157.805 182.331 204.325 1.00 20.01  ? 2930 GLN A N     1 
ATOM   11063 C  CA    . GLN A 1 2930 ? 158.128 181.898 202.964 1.00 14.01  ? 2930 GLN A CA    1 
ATOM   11064 C  C     . GLN A 1 2930 ? 159.143 180.758 202.979 1.00 12.05  ? 2930 GLN A C     1 
ATOM   11065 O  O     . GLN A 1 2930 ? 160.024 180.672 202.121 1.00 7.78   ? 2930 GLN A O     1 
ATOM   11066 C  CB    . GLN A 1 2930 ? 158.629 183.068 202.115 1.00 9.86   ? 2930 GLN A CB    1 
ATOM   11067 C  CG    . GLN A 1 2930 ? 158.185 183.015 200.667 1.00 14.47  ? 2930 GLN A CG    1 
ATOM   11068 C  CD    . GLN A 1 2930 ? 158.702 184.184 199.859 1.00 16.69  ? 2930 GLN A CD    1 
ATOM   11069 O  OE1   . GLN A 1 2930 ? 159.322 185.099 200.398 1.00 18.11  ? 2930 GLN A OE1   1 
ATOM   11070 N  NE2   . GLN A 1 2930 ? 158.449 184.161 198.556 1.00 20.64  ? 2930 GLN A NE2   1 
ATOM   11071 N  N     . GLY A 1 2931 ? 159.014 179.872 203.963 1.00 13.39  ? 2931 GLY A N     1 
ATOM   11072 C  CA    . GLY A 1 2931 ? 159.946 178.777 204.132 1.00 7.91   ? 2931 GLY A CA    1 
ATOM   11073 C  C     . GLY A 1 2931 ? 159.592 177.565 203.301 1.00 11.08  ? 2931 GLY A C     1 
ATOM   11074 O  O     . GLY A 1 2931 ? 158.665 176.822 203.633 1.00 12.82  ? 2931 GLY A O     1 
ATOM   11075 N  N     . HIS A 1 2932 ? 160.326 177.357 202.215 1.00 14.35  ? 2932 HIS A N     1 
ATOM   11076 C  CA    . HIS A 1 2932 ? 160.092 176.252 201.302 1.00 8.92   ? 2932 HIS A CA    1 
ATOM   11077 C  C     . HIS A 1 2932 ? 161.243 175.259 201.382 1.00 9.02   ? 2932 HIS A C     1 
ATOM   11078 O  O     . HIS A 1 2932 ? 162.398 175.637 201.586 1.00 11.43  ? 2932 HIS A O     1 
ATOM   11079 C  CB    . HIS A 1 2932 ? 159.931 176.754 199.866 1.00 9.37   ? 2932 HIS A CB    1 
ATOM   11080 C  CG    . HIS A 1 2932 ? 158.948 177.873 199.727 1.00 9.46   ? 2932 HIS A CG    1 
ATOM   11081 N  ND1   . HIS A 1 2932 ? 157.640 177.770 200.146 1.00 9.12   ? 2932 HIS A ND1   1 
ATOM   11082 C  CD2   . HIS A 1 2932 ? 159.083 179.121 199.220 1.00 11.77  ? 2932 HIS A CD2   1 
ATOM   11083 C  CE1   . HIS A 1 2932 ? 157.010 178.905 199.899 1.00 11.96  ? 2932 HIS A CE1   1 
ATOM   11084 N  NE2   . HIS A 1 2932 ? 157.864 179.741 199.337 1.00 11.62  ? 2932 HIS A NE2   1 
ATOM   11085 N  N     . LEU A 1 2933 ? 160.915 173.982 201.215 1.00 10.34  ? 2933 LEU A N     1 
ATOM   11086 C  CA    . LEU A 1 2933 ? 161.874 172.898 201.354 1.00 8.37   ? 2933 LEU A CA    1 
ATOM   11087 C  C     . LEU A 1 2933 ? 162.105 172.197 200.024 1.00 9.27   ? 2933 LEU A C     1 
ATOM   11088 O  O     . LEU A 1 2933 ? 161.222 172.146 199.164 1.00 12.40  ? 2933 LEU A O     1 
ATOM   11089 C  CB    . LEU A 1 2933 ? 161.398 171.873 202.387 1.00 7.43   ? 2933 LEU A CB    1 
ATOM   11090 C  CG    . LEU A 1 2933 ? 161.875 172.066 203.823 1.00 8.44   ? 2933 LEU A CG    1 
ATOM   11091 C  CD1   . LEU A 1 2933 ? 161.379 170.932 204.696 1.00 12.63  ? 2933 LEU A CD1   1 
ATOM   11092 C  CD2   . LEU A 1 2933 ? 163.388 172.138 203.848 1.00 14.44  ? 2933 LEU A CD2   1 
ATOM   11093 N  N     . LEU A 1 2934 ? 163.310 171.653 199.869 1.00 9.48   ? 2934 LEU A N     1 
ATOM   11094 C  CA    . LEU A 1 2934 ? 163.641 170.765 198.757 1.00 9.76   ? 2934 LEU A CA    1 
ATOM   11095 C  C     . LEU A 1 2934 ? 164.387 169.579 199.359 1.00 12.33  ? 2934 LEU A C     1 
ATOM   11096 O  O     . LEU A 1 2934 ? 165.598 169.652 199.586 1.00 13.42  ? 2934 LEU A O     1 
ATOM   11097 C  CB    . LEU A 1 2934 ? 164.474 171.470 197.694 1.00 9.64   ? 2934 LEU A CB    1 
ATOM   11098 C  CG    . LEU A 1 2934 ? 164.906 170.610 196.503 1.00 10.47  ? 2934 LEU A CG    1 
ATOM   11099 C  CD1   . LEU A 1 2934 ? 163.710 169.922 195.871 1.00 14.64  ? 2934 LEU A CD1   1 
ATOM   11100 C  CD2   . LEU A 1 2934 ? 165.643 171.446 195.475 1.00 13.34  ? 2934 LEU A CD2   1 
ATOM   11101 N  N     . LEU A 1 2935 ? 163.658 168.502 199.637 1.00 12.56  ? 2935 LEU A N     1 
ATOM   11102 C  CA    . LEU A 1 2935 ? 164.245 167.291 200.196 1.00 10.99  ? 2935 LEU A CA    1 
ATOM   11103 C  C     . LEU A 1 2935 ? 164.637 166.360 199.057 1.00 10.17  ? 2935 LEU A C     1 
ATOM   11104 O  O     . LEU A 1 2935 ? 163.771 165.852 198.338 1.00 14.37  ? 2935 LEU A O     1 
ATOM   11105 C  CB    . LEU A 1 2935 ? 163.268 166.598 201.143 1.00 10.64  ? 2935 LEU A CB    1 
ATOM   11106 C  CG    . LEU A 1 2935 ? 162.580 167.467 202.194 1.00 12.60  ? 2935 LEU A CG    1 
ATOM   11107 C  CD1   . LEU A 1 2935 ? 161.699 166.612 203.086 1.00 10.49  ? 2935 LEU A CD1   1 
ATOM   11108 C  CD2   . LEU A 1 2935 ? 163.605 168.224 203.020 1.00 12.44  ? 2935 LEU A CD2   1 
ATOM   11109 N  N     . ILE A 1 2936 ? 165.936 166.134 198.898 1.00 12.51  ? 2936 ILE A N     1 
ATOM   11110 C  CA    . ILE A 1 2936 ? 166.463 165.297 197.827 1.00 12.82  ? 2936 ILE A CA    1 
ATOM   11111 C  C     . ILE A 1 2936 ? 166.986 164.013 198.450 1.00 13.74  ? 2936 ILE A C     1 
ATOM   11112 O  O     . ILE A 1 2936 ? 167.903 164.046 199.279 1.00 14.71  ? 2936 ILE A O     1 
ATOM   11113 C  CB    . ILE A 1 2936 ? 167.563 166.019 197.036 1.00 11.19  ? 2936 ILE A CB    1 
ATOM   11114 C  CG1   . ILE A 1 2936 ? 167.033 167.349 196.500 1.00 11.14  ? 2936 ILE A CG1   1 
ATOM   11115 C  CG2   . ILE A 1 2936 ? 168.062 165.143 195.901 1.00 12.04  ? 2936 ILE A CG2   1 
ATOM   11116 C  CD1   . ILE A 1 2936 ? 168.073 168.179 195.808 1.00 17.97  ? 2936 ILE A CD1   1 
ATOM   11117 N  N     . GLY A 1 2937 ? 166.409 162.886 198.052 1.00 11.38  ? 2937 GLY A N     1 
ATOM   11118 C  CA    . GLY A 1 2937 ? 166.816 161.608 198.603 1.00 12.91  ? 2937 GLY A CA    1 
ATOM   11119 C  C     . GLY A 1 2937 ? 166.117 160.478 197.883 1.00 13.57  ? 2937 GLY A C     1 
ATOM   11120 O  O     . GLY A 1 2937 ? 165.229 160.691 197.051 1.00 15.43  ? 2937 GLY A O     1 
ATOM   11121 N  N     . VAL A 1 2938 ? 166.538 159.259 198.222 1.00 14.52  ? 2938 VAL A N     1 
ATOM   11122 C  CA    . VAL A 1 2938 ? 165.977 158.066 197.603 1.00 12.68  ? 2938 VAL A CA    1 
ATOM   11123 C  C     . VAL A 1 2938 ? 164.517 157.904 198.012 1.00 15.93  ? 2938 VAL A C     1 
ATOM   11124 O  O     . VAL A 1 2938 ? 164.105 158.297 199.112 1.00 16.38  ? 2938 VAL A O     1 
ATOM   11125 C  CB    . VAL A 1 2938 ? 166.808 156.829 197.987 1.00 11.63  ? 2938 VAL A CB    1 
ATOM   11126 C  CG1   . VAL A 1 2938 ? 166.439 155.639 197.119 1.00 15.38  ? 2938 VAL A CG1   1 
ATOM   11127 C  CG2   . VAL A 1 2938 ? 168.286 157.136 197.855 1.00 12.18  ? 2938 VAL A CG2   1 
ATOM   11128 N  N     . SER A 1 2939 ? 163.723 157.328 197.112 1.00 12.50  ? 2939 SER A N     1 
ATOM   11129 C  CA    . SER A 1 2939 ? 162.321 157.075 197.405 1.00 10.96  ? 2939 SER A CA    1 
ATOM   11130 C  C     . SER A 1 2939 ? 162.189 156.058 198.531 1.00 13.11  ? 2939 SER A C     1 
ATOM   11131 O  O     . SER A 1 2939 ? 163.007 155.147 198.676 1.00 15.63  ? 2939 SER A O     1 
ATOM   11132 C  CB    . SER A 1 2939 ? 161.597 156.574 196.155 1.00 15.38  ? 2939 SER A CB    1 
ATOM   11133 O  OG    . SER A 1 2939 ? 161.542 157.578 195.158 1.00 24.63  ? 2939 SER A OG    1 
ATOM   11134 N  N     . GLY A 1 2940 ? 161.149 156.228 199.341 1.00 12.59  ? 2940 GLY A N     1 
ATOM   11135 C  CA    . GLY A 1 2940 ? 160.940 155.360 200.478 1.00 10.39  ? 2940 GLY A CA    1 
ATOM   11136 C  C     . GLY A 1 2940 ? 161.836 155.630 201.662 1.00 12.51  ? 2940 GLY A C     1 
ATOM   11137 O  O     . GLY A 1 2940 ? 161.932 154.778 202.553 1.00 15.32  ? 2940 GLY A O     1 
ATOM   11138 N  N     . ALA A 1 2941 ? 162.504 156.780 201.700 1.00 11.91  ? 2941 ALA A N     1 
ATOM   11139 C  CA    . ALA A 1 2941 ? 163.367 157.142 202.815 1.00 11.43  ? 2941 ALA A CA    1 
ATOM   11140 C  C     . ALA A 1 2941 ? 162.625 157.874 203.923 1.00 14.40  ? 2941 ALA A C     1 
ATOM   11141 O  O     . ALA A 1 2941 ? 163.216 158.138 204.975 1.00 14.84  ? 2941 ALA A O     1 
ATOM   11142 C  CB    . ALA A 1 2941 ? 164.532 158.004 202.322 1.00 12.66  ? 2941 ALA A CB    1 
ATOM   11143 N  N     . GLY A 1 2942 ? 161.352 158.200 203.720 1.00 12.62  ? 2942 GLY A N     1 
ATOM   11144 C  CA    . GLY A 1 2942 ? 160.574 158.871 204.738 1.00 11.38  ? 2942 GLY A CA    1 
ATOM   11145 C  C     . GLY A 1 2942 ? 160.467 160.370 204.600 1.00 11.52  ? 2942 GLY A C     1 
ATOM   11146 O  O     . GLY A 1 2942 ? 160.056 161.032 205.559 1.00 13.39  ? 2942 GLY A O     1 
ATOM   11147 N  N     . LYS A 1 2943 ? 160.820 160.932 203.442 1.00 10.05  ? 2943 LYS A N     1 
ATOM   11148 C  CA    . LYS A 1 2943 ? 160.747 162.379 203.267 1.00 8.92   ? 2943 LYS A CA    1 
ATOM   11149 C  C     . LYS A 1 2943 ? 159.318 162.883 203.433 1.00 9.12   ? 2943 LYS A C     1 
ATOM   11150 O  O     . LYS A 1 2943 ? 159.060 163.807 204.214 1.00 11.35  ? 2943 LYS A O     1 
ATOM   11151 C  CB    . LYS A 1 2943 ? 161.296 162.769 201.895 1.00 9.42   ? 2943 LYS A CB    1 
ATOM   11152 C  CG    . LYS A 1 2943 ? 162.702 162.268 201.623 1.00 9.84   ? 2943 LYS A CG    1 
ATOM   11153 C  CD    . LYS A 1 2943 ? 163.281 162.911 200.375 1.00 10.70  ? 2943 LYS A CD    1 
ATOM   11154 C  CE    . LYS A 1 2943 ? 162.519 162.491 199.131 1.00 9.60   ? 2943 LYS A CE    1 
ATOM   11155 N  NZ    . LYS A 1 2943 ? 162.795 161.078 198.762 1.00 12.25  ? 2943 LYS A NZ    1 
ATOM   11156 N  N     . THR A 1 2944 ? 158.373 162.281 202.708 1.00 9.24   ? 2944 THR A N     1 
ATOM   11157 C  CA    . THR A 1 2944 ? 156.981 162.705 202.807 1.00 8.40   ? 2944 THR A CA    1 
ATOM   11158 C  C     . THR A 1 2944 ? 156.418 162.446 204.198 1.00 8.90   ? 2944 THR A C     1 
ATOM   11159 O  O     . THR A 1 2944 ? 155.700 163.289 204.749 1.00 10.23  ? 2944 THR A O     1 
ATOM   11160 C  CB    . THR A 1 2944 ? 156.138 161.993 201.748 1.00 5.92   ? 2944 THR A CB    1 
ATOM   11161 O  OG1   . THR A 1 2944 ? 156.724 162.191 200.457 1.00 7.65   ? 2944 THR A OG1   1 
ATOM   11162 C  CG2   . THR A 1 2944 ? 154.719 162.533 201.741 1.00 6.02   ? 2944 THR A CG2   1 
ATOM   11163 N  N     . THR A 1 2945 ? 156.733 161.290 204.784 1.00 8.30   ? 2945 THR A N     1 
ATOM   11164 C  CA    . THR A 1 2945 ? 156.210 160.962 206.107 1.00 9.42   ? 2945 THR A CA    1 
ATOM   11165 C  C     . THR A 1 2945 ? 156.741 161.925 207.162 1.00 9.86   ? 2945 THR A C     1 
ATOM   11166 O  O     . THR A 1 2945 ? 155.983 162.423 208.002 1.00 16.04  ? 2945 THR A O     1 
ATOM   11167 C  CB    . THR A 1 2945 ? 156.561 159.518 206.465 1.00 16.21  ? 2945 THR A CB    1 
ATOM   11168 O  OG1   . THR A 1 2945 ? 156.051 158.638 205.456 1.00 18.24  ? 2945 THR A OG1   1 
ATOM   11169 C  CG2   . THR A 1 2945 ? 155.958 159.139 207.808 1.00 11.10  ? 2945 THR A CG2   1 
ATOM   11170 N  N     . LEU A 1 2946 ? 158.047 162.202 207.132 1.00 7.92   ? 2946 LEU A N     1 
ATOM   11171 C  CA    . LEU A 1 2946 ? 158.622 163.138 208.093 1.00 6.87   ? 2946 LEU A CA    1 
ATOM   11172 C  C     . LEU A 1 2946 ? 158.079 164.545 207.886 1.00 8.91   ? 2946 LEU A C     1 
ATOM   11173 O  O     . LEU A 1 2946 ? 157.815 165.262 208.858 1.00 11.11  ? 2946 LEU A O     1 
ATOM   11174 C  CB    . LEU A 1 2946 ? 160.147 163.128 207.994 1.00 7.50   ? 2946 LEU A CB    1 
ATOM   11175 C  CG    . LEU A 1 2946 ? 160.873 161.889 208.521 1.00 7.54   ? 2946 LEU A CG    1 
ATOM   11176 C  CD1   . LEU A 1 2946 ? 162.359 162.164 208.655 1.00 11.41  ? 2946 LEU A CD1   1 
ATOM   11177 C  CD2   . LEU A 1 2946 ? 160.288 161.434 209.849 1.00 7.14   ? 2946 LEU A CD2   1 
ATOM   11178 N  N     . SER A 1 2947 ? 157.908 164.959 206.628 1.00 10.12  ? 2947 SER A N     1 
ATOM   11179 C  CA    . SER A 1 2947 ? 157.337 166.274 206.356 1.00 7.57   ? 2947 SER A CA    1 
ATOM   11180 C  C     . SER A 1 2947 ? 155.922 166.385 206.908 1.00 8.38   ? 2947 SER A C     1 
ATOM   11181 O  O     . SER A 1 2947 ? 155.574 167.386 207.544 1.00 12.84  ? 2947 SER A O     1 
ATOM   11182 C  CB    . SER A 1 2947 ? 157.351 166.550 204.854 1.00 7.27   ? 2947 SER A CB    1 
ATOM   11183 O  OG    . SER A 1 2947 ? 158.634 166.313 204.307 1.00 8.97   ? 2947 SER A OG    1 
ATOM   11184 N  N     . ARG A 1 2948 ? 155.096 165.360 206.684 1.00 8.27   ? 2948 ARG A N     1 
ATOM   11185 C  CA    . ARG A 1 2948 ? 153.736 165.370 207.213 1.00 8.53   ? 2948 ARG A CA    1 
ATOM   11186 C  C     . ARG A 1 2948 ? 153.733 165.381 208.735 1.00 9.53   ? 2948 ARG A C     1 
ATOM   11187 O  O     . ARG A 1 2948 ? 152.928 166.083 209.356 1.00 12.61  ? 2948 ARG A O     1 
ATOM   11188 C  CB    . ARG A 1 2948 ? 152.959 164.163 206.688 1.00 6.86   ? 2948 ARG A CB    1 
ATOM   11189 C  CG    . ARG A 1 2948 ? 152.675 164.208 205.202 1.00 9.70   ? 2948 ARG A CG    1 
ATOM   11190 C  CD    . ARG A 1 2948 ? 151.956 162.956 204.742 1.00 15.30  ? 2948 ARG A CD    1 
ATOM   11191 N  NE    . ARG A 1 2948 ? 150.595 162.886 205.255 1.00 23.77  ? 2948 ARG A NE    1 
ATOM   11192 C  CZ    . ARG A 1 2948 ? 149.667 162.055 204.802 1.00 26.36  ? 2948 ARG A CZ    1 
ATOM   11193 N  NH1   . ARG A 1 2948 ? 149.920 161.208 203.817 1.00 24.59  ? 2948 ARG A NH1   1 
ATOM   11194 N  NH2   . ARG A 1 2948 ? 148.457 162.071 205.351 1.00 26.47  ? 2948 ARG A NH2   1 
ATOM   11195 N  N     . PHE A 1 2949 ? 154.626 164.606 209.353 1.00 7.32   ? 2949 PHE A N     1 
ATOM   11196 C  CA    . PHE A 1 2949 ? 154.683 164.549 210.810 1.00 9.78   ? 2949 PHE A CA    1 
ATOM   11197 C  C     . PHE A 1 2949 ? 155.067 165.904 211.396 1.00 12.94  ? 2949 PHE A C     1 
ATOM   11198 O  O     . PHE A 1 2949 ? 154.451 166.377 212.360 1.00 13.02  ? 2949 PHE A O     1 
ATOM   11199 C  CB    . PHE A 1 2949 ? 155.671 163.461 211.234 1.00 10.89  ? 2949 PHE A CB    1 
ATOM   11200 C  CG    . PHE A 1 2949 ? 155.954 163.427 212.706 1.00 11.88  ? 2949 PHE A CG    1 
ATOM   11201 C  CD1   . PHE A 1 2949 ? 154.927 163.275 213.620 1.00 12.74  ? 2949 PHE A CD1   1 
ATOM   11202 C  CD2   . PHE A 1 2949 ? 157.252 163.520 213.176 1.00 11.69  ? 2949 PHE A CD2   1 
ATOM   11203 C  CE1   . PHE A 1 2949 ? 155.185 163.233 214.972 1.00 13.65  ? 2949 PHE A CE1   1 
ATOM   11204 C  CE2   . PHE A 1 2949 ? 157.517 163.476 214.528 1.00 16.07  ? 2949 PHE A CE2   1 
ATOM   11205 C  CZ    . PHE A 1 2949 ? 156.481 163.330 215.427 1.00 16.46  ? 2949 PHE A CZ    1 
ATOM   11206 N  N     . VAL A 1 2950 ? 156.075 166.554 210.811 1.00 12.67  ? 2950 VAL A N     1 
ATOM   11207 C  CA    . VAL A 1 2950 ? 156.508 167.852 211.316 1.00 11.14  ? 2950 VAL A CA    1 
ATOM   11208 C  C     . VAL A 1 2950 ? 155.441 168.910 211.064 1.00 13.03  ? 2950 VAL A C     1 
ATOM   11209 O  O     . VAL A 1 2950 ? 155.213 169.791 211.902 1.00 20.12  ? 2950 VAL A O     1 
ATOM   11210 C  CB    . VAL A 1 2950 ? 157.861 168.245 210.698 1.00 11.43  ? 2950 VAL A CB    1 
ATOM   11211 C  CG1   . VAL A 1 2950 ? 158.270 169.629 211.161 1.00 12.50  ? 2950 VAL A CG1   1 
ATOM   11212 C  CG2   . VAL A 1 2950 ? 158.924 167.231 211.076 1.00 10.63  ? 2950 VAL A CG2   1 
ATOM   11213 N  N     . ALA A 1 2951 ? 154.764 168.842 209.914 1.00 8.81   ? 2951 ALA A N     1 
ATOM   11214 C  CA    . ALA A 1 2951 ? 153.674 169.773 209.647 1.00 9.65   ? 2951 ALA A CA    1 
ATOM   11215 C  C     . ALA A 1 2951 ? 152.544 169.595 210.651 1.00 13.00  ? 2951 ALA A C     1 
ATOM   11216 O  O     . ALA A 1 2951 ? 151.933 170.575 211.093 1.00 16.05  ? 2951 ALA A O     1 
ATOM   11217 C  CB    . ALA A 1 2951 ? 153.160 169.584 208.220 1.00 9.77   ? 2951 ALA A CB    1 
ATOM   11218 N  N     . TRP A 1 2952 ? 152.248 168.347 211.019 1.00 14.75  ? 2952 TRP A N     1 
ATOM   11219 C  CA    . TRP A 1 2952 ? 151.235 168.094 212.036 1.00 13.54  ? 2952 TRP A CA    1 
ATOM   11220 C  C     . TRP A 1 2952 ? 151.666 168.639 213.391 1.00 12.56  ? 2952 TRP A C     1 
ATOM   11221 O  O     . TRP A 1 2952 ? 150.841 169.175 214.141 1.00 16.44  ? 2952 TRP A O     1 
ATOM   11222 C  CB    . TRP A 1 2952 ? 150.944 166.596 212.123 1.00 15.27  ? 2952 TRP A CB    1 
ATOM   11223 C  CG    . TRP A 1 2952 ? 150.124 166.216 213.311 1.00 15.45  ? 2952 TRP A CG    1 
ATOM   11224 C  CD1   . TRP A 1 2952 ? 148.767 166.278 213.424 1.00 17.71  ? 2952 TRP A CD1   1 
ATOM   11225 C  CD2   . TRP A 1 2952 ? 150.609 165.714 214.560 1.00 14.77  ? 2952 TRP A CD2   1 
ATOM   11226 N  NE1   . TRP A 1 2952 ? 148.376 165.846 214.667 1.00 22.05  ? 2952 TRP A NE1   1 
ATOM   11227 C  CE2   . TRP A 1 2952 ? 149.489 165.495 215.384 1.00 17.29  ? 2952 TRP A CE2   1 
ATOM   11228 C  CE3   . TRP A 1 2952 ? 151.881 165.431 215.062 1.00 13.02  ? 2952 TRP A CE3   1 
ATOM   11229 C  CZ2   . TRP A 1 2952 ? 149.603 165.004 216.681 1.00 21.03  ? 2952 TRP A CZ2   1 
ATOM   11230 C  CZ3   . TRP A 1 2952 ? 151.992 164.944 216.348 1.00 17.90  ? 2952 TRP A CZ3   1 
ATOM   11231 C  CH2   . TRP A 1 2952 ? 150.861 164.735 217.143 1.00 21.50  ? 2952 TRP A CH2   1 
ATOM   11232 N  N     . MET A 1 2953 ? 152.951 168.508 213.729 1.00 12.52  ? 2953 MET A N     1 
ATOM   11233 C  CA    . MET A 1 2953 ? 153.424 169.041 215.004 1.00 14.10  ? 2953 MET A CA    1 
ATOM   11234 C  C     . MET A 1 2953 ? 153.344 170.562 215.033 1.00 16.08  ? 2953 MET A C     1 
ATOM   11235 O  O     . MET A 1 2953 ? 153.087 171.158 216.086 1.00 19.32  ? 2953 MET A O     1 
ATOM   11236 C  CB    . MET A 1 2953 ? 154.856 168.587 215.282 1.00 14.41  ? 2953 MET A CB    1 
ATOM   11237 C  CG    . MET A 1 2953 ? 155.011 167.103 215.517 1.00 16.32  ? 2953 MET A CG    1 
ATOM   11238 S  SD    . MET A 1 2953 ? 156.738 166.664 215.757 1.00 36.78  ? 2953 MET A SD    1 
ATOM   11239 C  CE    . MET A 1 2953 ? 157.032 167.387 217.368 1.00 22.85  ? 2953 MET A CE    1 
ATOM   11240 N  N     . ASN A 1 2954 ? 153.573 171.207 213.894 1.00 16.56  ? 2954 ASN A N     1 
ATOM   11241 C  CA    . ASN A 1 2954 ? 153.549 172.660 213.807 1.00 16.21  ? 2954 ASN A CA    1 
ATOM   11242 C  C     . ASN A 1 2954 ? 152.182 173.212 213.431 1.00 17.29  ? 2954 ASN A C     1 
ATOM   11243 O  O     . ASN A 1 2954 ? 152.056 174.422 213.219 1.00 25.69  ? 2954 ASN A O     1 
ATOM   11244 C  CB    . ASN A 1 2954 ? 154.596 173.144 212.801 1.00 14.60  ? 2954 ASN A CB    1 
ATOM   11245 C  CG    . ASN A 1 2954 ? 156.009 173.004 213.324 1.00 18.25  ? 2954 ASN A CG    1 
ATOM   11246 O  OD1   . ASN A 1 2954 ? 156.336 173.503 214.399 1.00 19.79  ? 2954 ASN A OD1   1 
ATOM   11247 N  ND2   . ASN A 1 2954 ? 156.857 172.324 212.564 1.00 20.63  ? 2954 ASN A ND2   1 
ATOM   11248 N  N     . GLY A 1 2955 ? 151.163 172.363 213.331 1.00 16.20  ? 2955 GLY A N     1 
ATOM   11249 C  CA    . GLY A 1 2955 ? 149.823 172.813 213.030 1.00 14.01  ? 2955 GLY A CA    1 
ATOM   11250 C  C     . GLY A 1 2955 ? 149.534 173.064 211.568 1.00 17.25  ? 2955 GLY A C     1 
ATOM   11251 O  O     . GLY A 1 2955 ? 148.416 173.483 211.242 1.00 22.18  ? 2955 GLY A O     1 
ATOM   11252 N  N     . LEU A 1 2956 ? 150.494 172.831 210.678 1.00 15.12  ? 2956 LEU A N     1 
ATOM   11253 C  CA    . LEU A 1 2956 ? 150.254 173.036 209.259 1.00 13.45  ? 2956 LEU A CA    1 
ATOM   11254 C  C     . LEU A 1 2956 ? 149.319 171.964 208.712 1.00 14.77  ? 2956 LEU A C     1 
ATOM   11255 O  O     . LEU A 1 2956 ? 149.327 170.813 209.157 1.00 19.38  ? 2956 LEU A O     1 
ATOM   11256 C  CB    . LEU A 1 2956 ? 151.568 173.022 208.477 1.00 13.16  ? 2956 LEU A CB    1 
ATOM   11257 C  CG    . LEU A 1 2956 ? 152.788 173.765 209.025 1.00 13.79  ? 2956 LEU A CG    1 
ATOM   11258 C  CD1   . LEU A 1 2956 ? 153.884 173.803 207.977 1.00 14.42  ? 2956 LEU A CD1   1 
ATOM   11259 C  CD2   . LEU A 1 2956 ? 152.433 175.170 209.470 1.00 15.29  ? 2956 LEU A CD2   1 
ATOM   11260 N  N     . SER A 1 2957 ? 148.506 172.354 207.737 1.00 14.98  ? 2957 SER A N     1 
ATOM   11261 C  CA    . SER A 1 2957 ? 147.600 171.443 207.052 1.00 14.96  ? 2957 SER A CA    1 
ATOM   11262 C  C     . SER A 1 2957 ? 148.307 170.893 205.821 1.00 14.58  ? 2957 SER A C     1 
ATOM   11263 O  O     . SER A 1 2957 ? 148.764 171.661 204.971 1.00 16.46  ? 2957 SER A O     1 
ATOM   11264 C  CB    . SER A 1 2957 ? 146.306 172.157 206.659 1.00 15.12  ? 2957 SER A CB    1 
ATOM   11265 O  OG    . SER A 1 2957 ? 145.432 171.287 205.963 1.00 24.83  ? 2957 SER A OG    1 
ATOM   11266 N  N     . VAL A 1 2958 ? 148.409 169.573 205.733 1.00 13.53  ? 2958 VAL A N     1 
ATOM   11267 C  CA    . VAL A 1 2958 ? 149.130 168.940 204.635 1.00 13.61  ? 2958 VAL A CA    1 
ATOM   11268 C  C     . VAL A 1 2958 ? 148.232 168.891 203.407 1.00 11.69  ? 2958 VAL A C     1 
ATOM   11269 O  O     . VAL A 1 2958 ? 147.086 168.432 203.478 1.00 14.80  ? 2958 VAL A O     1 
ATOM   11270 C  CB    . VAL A 1 2958 ? 149.605 167.534 205.034 1.00 12.98  ? 2958 VAL A CB    1 
ATOM   11271 C  CG1   . VAL A 1 2958 ? 150.183 166.808 203.832 1.00 11.02  ? 2958 VAL A CG1   1 
ATOM   11272 C  CG2   . VAL A 1 2958 ? 150.633 167.623 206.147 1.00 12.01  ? 2958 VAL A CG2   1 
ATOM   11273 N  N     . TYR A 1 2959 ? 148.747 169.373 202.279 1.00 14.70  ? 2959 TYR A N     1 
ATOM   11274 C  CA    . TYR A 1 2959 ? 148.042 169.320 201.004 1.00 13.38  ? 2959 TYR A CA    1 
ATOM   11275 C  C     . TYR A 1 2959 ? 148.929 168.638 199.975 1.00 16.82  ? 2959 TYR A C     1 
ATOM   11276 O  O     . TYR A 1 2959 ? 150.052 169.085 199.724 1.00 18.25  ? 2959 TYR A O     1 
ATOM   11277 C  CB    . TYR A 1 2959 ? 147.647 170.721 200.529 1.00 14.75  ? 2959 TYR A CB    1 
ATOM   11278 C  CG    . TYR A 1 2959 ? 146.702 170.723 199.347 1.00 19.09  ? 2959 TYR A CG    1 
ATOM   11279 C  CD1   . TYR A 1 2959 ? 147.176 170.549 198.053 1.00 22.83  ? 2959 TYR A CD1   1 
ATOM   11280 C  CD2   . TYR A 1 2959 ? 145.337 170.890 199.525 1.00 20.44  ? 2959 TYR A CD2   1 
ATOM   11281 C  CE1   . TYR A 1 2959 ? 146.318 170.545 196.972 1.00 23.44  ? 2959 TYR A CE1   1 
ATOM   11282 C  CE2   . TYR A 1 2959 ? 144.472 170.890 198.449 1.00 25.79  ? 2959 TYR A CE2   1 
ATOM   11283 C  CZ    . TYR A 1 2959 ? 144.968 170.717 197.175 1.00 25.78  ? 2959 TYR A CZ    1 
ATOM   11284 O  OH    . TYR A 1 2959 ? 144.111 170.714 196.099 1.00 31.32  ? 2959 TYR A OH    1 
ATOM   11285 N  N     . GLN A 1 2960 ? 148.418 167.566 199.375 1.00 19.50  ? 2960 GLN A N     1 
ATOM   11286 C  CA    . GLN A 1 2960 ? 149.093 166.873 198.287 1.00 19.43  ? 2960 GLN A CA    1 
ATOM   11287 C  C     . GLN A 1 2960 ? 148.137 166.776 197.110 1.00 21.59  ? 2960 GLN A C     1 
ATOM   11288 O  O     . GLN A 1 2960 ? 146.978 166.385 197.282 1.00 33.00  ? 2960 GLN A O     1 
ATOM   11289 C  CB    . GLN A 1 2960 ? 149.554 165.475 198.712 1.00 23.66  ? 2960 GLN A CB    1 
ATOM   11290 C  CG    . GLN A 1 2960 ? 150.308 165.436 200.029 1.00 21.54  ? 2960 GLN A CG    1 
ATOM   11291 C  CD    . GLN A 1 2960 ? 150.590 164.023 200.494 1.00 24.79  ? 2960 GLN A CD    1 
ATOM   11292 O  OE1   . GLN A 1 2960 ? 150.175 163.622 201.581 1.00 28.62  ? 2960 GLN A OE1   1 
ATOM   11293 N  NE2   . GLN A 1 2960 ? 151.294 163.258 199.670 1.00 17.09  ? 2960 GLN A NE2   1 
ATOM   11294 N  N     . ILE A 1 2961 ? 148.617 167.138 195.921 1.00 23.96  ? 2961 ILE A N     1 
ATOM   11295 C  CA    . ILE A 1 2961 ? 147.788 167.036 194.727 1.00 30.04  ? 2961 ILE A CA    1 
ATOM   11296 C  C     . ILE A 1 2961 ? 147.641 165.572 194.339 1.00 33.03  ? 2961 ILE A C     1 
ATOM   11297 O  O     . ILE A 1 2961 ? 148.617 164.811 194.329 1.00 29.73  ? 2961 ILE A O     1 
ATOM   11298 C  CB    . ILE A 1 2961 ? 148.379 167.869 193.579 1.00 28.00  ? 2961 ILE A CB    1 
ATOM   11299 C  CG1   . ILE A 1 2961 ? 149.841 167.497 193.329 1.00 23.80  ? 2961 ILE A CG1   1 
ATOM   11300 C  CG2   . ILE A 1 2961 ? 148.244 169.351 193.874 1.00 25.17  ? 2961 ILE A CG2   1 
ATOM   11301 C  CD1   . ILE A 1 2961 ? 150.401 168.075 192.052 1.00 35.31  ? 2961 ILE A CD1   1 
ATOM   11302 N  N     . LYS A 1 2962 ? 146.411 165.166 194.037 1.00 37.29  ? 2962 LYS A N     1 
ATOM   11303 C  CA    . LYS A 1 2962 ? 146.114 163.783 193.668 1.00 37.06  ? 2962 LYS A CA    1 
ATOM   11304 C  C     . LYS A 1 2962 ? 146.210 163.674 192.152 1.00 40.59  ? 2962 LYS A C     1 
ATOM   11305 O  O     . LYS A 1 2962 ? 145.258 163.952 191.423 1.00 42.49  ? 2962 LYS A O     1 
ATOM   11306 C  CB    . LYS A 1 2962 ? 144.743 163.374 194.189 1.00 40.62  ? 2962 LYS A CB    1 
ATOM   11307 C  CG    . LYS A 1 2962 ? 144.655 163.326 195.709 1.00 44.83  ? 2962 LYS A CG    1 
ATOM   11308 C  CD    . LYS A 1 2962 ? 145.960 162.853 196.333 1.00 44.99  ? 2962 LYS A CD    1 
ATOM   11309 C  CE    . LYS A 1 2962 ? 145.805 162.612 197.822 1.00 46.60  ? 2962 LYS A CE    1 
ATOM   11310 N  NZ    . LYS A 1 2962 ? 145.379 163.846 198.538 1.00 43.68  ? 2962 LYS A NZ    1 
ATOM   11311 N  N     . VAL A 1 2963 ? 147.379 163.261 191.676 1.00 41.01  ? 2963 VAL A N     1 
ATOM   11312 C  CA    . VAL A 1 2963 ? 147.652 163.202 190.245 1.00 38.81  ? 2963 VAL A CA    1 
ATOM   11313 C  C     . VAL A 1 2963 ? 147.198 161.854 189.702 1.00 43.89  ? 2963 VAL A C     1 
ATOM   11314 O  O     . VAL A 1 2963 ? 147.449 160.807 190.311 1.00 44.38  ? 2963 VAL A O     1 
ATOM   11315 C  CB    . VAL A 1 2963 ? 149.145 163.438 189.970 1.00 34.86  ? 2963 VAL A CB    1 
ATOM   11316 C  CG1   . VAL A 1 2963 ? 149.450 163.273 188.491 1.00 38.93  ? 2963 VAL A CG1   1 
ATOM   11317 C  CG2   . VAL A 1 2963 ? 149.560 164.815 190.454 1.00 37.11  ? 2963 VAL A CG2   1 
ATOM   11318 N  N     . HIS A 1 2964 ? 146.516 161.877 188.558 1.00 42.21  ? 2964 HIS A N     1 
ATOM   11319 C  CA    . HIS A 1 2964 ? 146.117 160.650 187.881 1.00 44.65  ? 2964 HIS A CA    1 
ATOM   11320 C  C     . HIS A 1 2964 ? 146.491 160.712 186.405 1.00 48.59  ? 2964 HIS A C     1 
ATOM   11321 O  O     . HIS A 1 2964 ? 147.201 161.629 185.978 1.00 46.54  ? 2964 HIS A O     1 
ATOM   11322 C  CB    . HIS A 1 2964 ? 144.616 160.401 188.051 1.00 40.63  ? 2964 HIS A CB    1 
ATOM   11323 C  CG    . HIS A 1 2964 ? 143.769 161.612 187.813 1.00 43.68  ? 2964 HIS A CG    1 
ATOM   11324 N  ND1   . HIS A 1 2964 ? 143.582 162.155 186.561 1.00 40.73  ? 2964 HIS A ND1   1 
ATOM   11325 C  CD2   . HIS A 1 2964 ? 143.054 162.380 188.667 1.00 45.15  ? 2964 HIS A CD2   1 
ATOM   11326 C  CE1   . HIS A 1 2964 ? 142.791 163.209 186.654 1.00 41.88  ? 2964 HIS A CE1   1 
ATOM   11327 N  NE2   . HIS A 1 2964 ? 142.456 163.367 187.922 1.00 46.26  ? 2964 HIS A NE2   1 
ATOM   11328 N  N     . ARG A 1 2965 ? 146.030 159.735 185.622 1.00 48.73  ? 2965 ARG A N     1 
ATOM   11329 C  CA    . ARG A 1 2965 ? 146.375 159.694 184.203 1.00 48.94  ? 2965 ARG A CA    1 
ATOM   11330 C  C     . ARG A 1 2965 ? 145.797 160.885 183.449 1.00 54.94  ? 2965 ARG A C     1 
ATOM   11331 O  O     . ARG A 1 2965 ? 146.460 161.451 182.571 1.00 54.10  ? 2965 ARG A O     1 
ATOM   11332 C  CB    . ARG A 1 2965 ? 145.890 158.386 183.585 1.00 57.79  ? 2965 ARG A CB    1 
ATOM   11333 C  CG    . ARG A 1 2965 ? 146.207 158.247 182.108 1.00 71.79  ? 2965 ARG A CG    1 
ATOM   11334 C  CD    . ARG A 1 2965 ? 145.735 156.906 181.591 1.00 69.22  ? 2965 ARG A CD    1 
ATOM   11335 N  NE    . ARG A 1 2965 ? 146.365 155.819 182.326 1.00 63.60  ? 2965 ARG A NE    1 
ATOM   11336 C  CZ    . ARG A 1 2965 ? 145.783 154.659 182.592 1.00 63.75  ? 2965 ARG A CZ    1 
ATOM   11337 N  NH1   . ARG A 1 2965 ? 144.550 154.397 182.191 1.00 66.08  ? 2965 ARG A NH1   1 
ATOM   11338 N  NH2   . ARG A 1 2965 ? 146.453 153.742 183.282 1.00 62.15  ? 2965 ARG A NH2   1 
ATOM   11339 N  N     . LYS A 1 2966 ? 144.569 161.278 183.771 1.00 54.92  ? 2966 LYS A N     1 
ATOM   11340 C  CA    . LYS A 1 2966 ? 143.902 162.382 183.096 1.00 51.06  ? 2966 LYS A CA    1 
ATOM   11341 C  C     . LYS A 1 2966 ? 144.241 163.736 183.706 1.00 48.51  ? 2966 LYS A C     1 
ATOM   11342 O  O     . LYS A 1 2966 ? 143.633 164.742 183.325 1.00 40.60  ? 2966 LYS A O     1 
ATOM   11343 C  CB    . LYS A 1 2966 ? 142.387 162.168 183.108 1.00 55.51  ? 2966 LYS A CB    1 
ATOM   11344 C  CG    . LYS A 1 2966 ? 141.925 160.984 182.276 1.00 52.03  ? 2966 LYS A CG    1 
ATOM   11345 C  CD    . LYS A 1 2966 ? 140.410 160.921 182.195 1.00 55.73  ? 2966 LYS A CD    1 
ATOM   11346 C  CE    . LYS A 1 2966 ? 139.807 160.451 183.508 1.00 62.10  ? 2966 LYS A CE    1 
ATOM   11347 N  NZ    . LYS A 1 2966 ? 138.332 160.278 183.413 1.00 55.88  ? 2966 LYS A NZ    1 
ATOM   11348 N  N     . TYR A 1 2967 ? 145.179 163.780 184.650 1.00 50.11  ? 2967 TYR A N     1 
ATOM   11349 C  CA    . TYR A 1 2967 ? 145.597 165.044 185.241 1.00 41.49  ? 2967 TYR A CA    1 
ATOM   11350 C  C     . TYR A 1 2967 ? 146.235 165.936 184.185 1.00 41.75  ? 2967 TYR A C     1 
ATOM   11351 O  O     . TYR A 1 2967 ? 147.094 165.494 183.417 1.00 48.64  ? 2967 TYR A O     1 
ATOM   11352 C  CB    . TYR A 1 2967 ? 146.578 164.788 186.383 1.00 43.38  ? 2967 TYR A CB    1 
ATOM   11353 C  CG    . TYR A 1 2967 ? 146.536 165.822 187.483 1.00 43.30  ? 2967 TYR A CG    1 
ATOM   11354 C  CD1   . TYR A 1 2967 ? 145.544 165.792 188.454 1.00 36.64  ? 2967 TYR A CD1   1 
ATOM   11355 C  CD2   . TYR A 1 2967 ? 147.493 166.825 187.555 1.00 42.42  ? 2967 TYR A CD2   1 
ATOM   11356 C  CE1   . TYR A 1 2967 ? 145.506 166.734 189.461 1.00 34.64  ? 2967 TYR A CE1   1 
ATOM   11357 C  CE2   . TYR A 1 2967 ? 147.462 167.769 188.557 1.00 36.88  ? 2967 TYR A CE2   1 
ATOM   11358 C  CZ    . TYR A 1 2967 ? 146.467 167.720 189.508 1.00 36.16  ? 2967 TYR A CZ    1 
ATOM   11359 O  OH    . TYR A 1 2967 ? 146.436 168.661 190.508 1.00 39.36  ? 2967 TYR A OH    1 
ATOM   11360 N  N     . THR A 1 2968 ? 145.815 167.197 184.152 1.00 42.42  ? 2968 THR A N     1 
ATOM   11361 C  CA    . THR A 1 2968 ? 146.281 168.160 183.165 1.00 41.74  ? 2968 THR A CA    1 
ATOM   11362 C  C     . THR A 1 2968 ? 146.712 169.438 183.872 1.00 41.19  ? 2968 THR A C     1 
ATOM   11363 O  O     . THR A 1 2968 ? 146.695 169.534 185.103 1.00 38.52  ? 2968 THR A O     1 
ATOM   11364 C  CB    . THR A 1 2968 ? 145.194 168.460 182.125 1.00 40.77  ? 2968 THR A CB    1 
ATOM   11365 O  OG1   . THR A 1 2968 ? 144.001 168.894 182.790 1.00 38.76  ? 2968 THR A OG1   1 
ATOM   11366 C  CG2   . THR A 1 2968 ? 144.888 167.222 181.295 1.00 45.01  ? 2968 THR A CG2   1 
ATOM   11367 N  N     . GLY A 1 2969 ? 147.109 170.431 183.074 1.00 43.64  ? 2969 GLY A N     1 
ATOM   11368 C  CA    . GLY A 1 2969 ? 147.487 171.717 183.632 1.00 39.88  ? 2969 GLY A CA    1 
ATOM   11369 C  C     . GLY A 1 2969 ? 146.337 172.440 184.299 1.00 33.39  ? 2969 GLY A C     1 
ATOM   11370 O  O     . GLY A 1 2969 ? 146.540 173.163 185.278 1.00 34.27  ? 2969 GLY A O     1 
ATOM   11371 N  N     . GLU A 1 2970 ? 145.119 172.268 183.779 1.00 41.93  ? 2970 GLU A N     1 
ATOM   11372 C  CA    . GLU A 1 2970 ? 143.958 172.915 184.380 1.00 41.03  ? 2970 GLU A CA    1 
ATOM   11373 C  C     . GLU A 1 2970 ? 143.685 172.377 185.780 1.00 36.92  ? 2970 GLU A C     1 
ATOM   11374 O  O     . GLU A 1 2970 ? 143.315 173.138 186.681 1.00 38.14  ? 2970 GLU A O     1 
ATOM   11375 C  CB    . GLU A 1 2970 ? 142.735 172.731 183.483 1.00 41.02  ? 2970 GLU A CB    1 
ATOM   11376 C  CG    . GLU A 1 2970 ? 142.843 173.443 182.147 1.00 55.68  ? 2970 GLU A CG    1 
ATOM   11377 C  CD    . GLU A 1 2970 ? 142.855 174.951 182.289 1.00 72.01  ? 2970 GLU A CD    1 
ATOM   11378 O  OE1   . GLU A 1 2970 ? 142.216 175.466 183.231 1.00 73.10  ? 2970 GLU A OE1   1 
ATOM   11379 O  OE2   . GLU A 1 2970 ? 143.506 175.623 181.462 1.00 77.01  ? 2970 GLU A OE2   1 
ATOM   11380 N  N     . ASP A 1 2971 ? 143.852 171.068 185.978 1.00 35.78  ? 2971 ASP A N     1 
ATOM   11381 C  CA    . ASP A 1 2971 ? 143.674 170.495 187.308 1.00 35.97  ? 2971 ASP A CA    1 
ATOM   11382 C  C     . ASP A 1 2971 ? 144.698 171.054 188.287 1.00 34.65  ? 2971 ASP A C     1 
ATOM   11383 O  O     . ASP A 1 2971 ? 144.368 171.361 189.440 1.00 36.16  ? 2971 ASP A O     1 
ATOM   11384 C  CB    . ASP A 1 2971 ? 143.776 168.972 187.236 1.00 44.70  ? 2971 ASP A CB    1 
ATOM   11385 C  CG    . ASP A 1 2971 ? 142.610 168.344 186.504 1.00 45.69  ? 2971 ASP A CG    1 
ATOM   11386 O  OD1   . ASP A 1 2971 ? 141.506 168.927 186.532 1.00 51.71  ? 2971 ASP A OD1   1 
ATOM   11387 O  OD2   . ASP A 1 2971 ? 142.798 167.268 185.899 1.00 43.30  ? 2971 ASP A OD2   1 
ATOM   11388 N  N     . PHE A 1 2972 ? 145.948 171.195 187.842 1.00 34.49  ? 2972 PHE A N     1 
ATOM   11389 C  CA    . PHE A 1 2972 ? 146.975 171.779 188.695 1.00 33.87  ? 2972 PHE A CA    1 
ATOM   11390 C  C     . PHE A 1 2972 ? 146.664 173.233 189.014 1.00 33.53  ? 2972 PHE A C     1 
ATOM   11391 O  O     . PHE A 1 2972 ? 146.878 173.686 190.143 1.00 33.69  ? 2972 PHE A O     1 
ATOM   11392 C  CB    . PHE A 1 2972 ? 148.341 171.667 188.028 1.00 28.28  ? 2972 PHE A CB    1 
ATOM   11393 C  CG    . PHE A 1 2972 ? 149.470 172.152 188.884 1.00 32.89  ? 2972 PHE A CG    1 
ATOM   11394 C  CD1   . PHE A 1 2972 ? 149.671 171.622 190.146 1.00 28.04  ? 2972 PHE A CD1   1 
ATOM   11395 C  CD2   . PHE A 1 2972 ? 150.332 173.136 188.430 1.00 35.20  ? 2972 PHE A CD2   1 
ATOM   11396 C  CE1   . PHE A 1 2972 ? 150.706 172.064 190.938 1.00 28.91  ? 2972 PHE A CE1   1 
ATOM   11397 C  CE2   . PHE A 1 2972 ? 151.372 173.580 189.218 1.00 29.29  ? 2972 PHE A CE2   1 
ATOM   11398 C  CZ    . PHE A 1 2972 ? 151.559 173.044 190.474 1.00 33.55  ? 2972 PHE A CZ    1 
ATOM   11399 N  N     . ASP A 1 2973 ? 146.171 173.985 188.029 1.00 30.83  ? 2973 ASP A N     1 
ATOM   11400 C  CA    . ASP A 1 2973 ? 145.796 175.372 188.278 1.00 30.59  ? 2973 ASP A CA    1 
ATOM   11401 C  C     . ASP A 1 2973 ? 144.658 175.461 189.286 1.00 30.28  ? 2973 ASP A C     1 
ATOM   11402 O  O     . ASP A 1 2973 ? 144.659 176.335 190.159 1.00 34.20  ? 2973 ASP A O     1 
ATOM   11403 C  CB    . ASP A 1 2973 ? 145.409 176.054 186.966 1.00 34.85  ? 2973 ASP A CB    1 
ATOM   11404 C  CG    . ASP A 1 2973 ? 146.587 176.221 186.027 1.00 41.70  ? 2973 ASP A CG    1 
ATOM   11405 O  OD1   . ASP A 1 2973 ? 147.681 175.712 186.344 1.00 42.91  ? 2973 ASP A OD1   1 
ATOM   11406 O  OD2   . ASP A 1 2973 ? 146.420 176.865 184.970 1.00 43.58  ? 2973 ASP A OD2   1 
ATOM   11407 N  N     . GLU A 1 2974 ? 143.675 174.565 189.179 1.00 28.54  ? 2974 GLU A N     1 
ATOM   11408 C  CA    . GLU A 1 2974 ? 142.569 174.561 190.133 1.00 29.39  ? 2974 GLU A CA    1 
ATOM   11409 C  C     . GLU A 1 2974 ? 143.049 174.216 191.538 1.00 33.84  ? 2974 GLU A C     1 
ATOM   11410 O  O     . GLU A 1 2974 ? 142.626 174.844 192.517 1.00 32.86  ? 2974 GLU A O     1 
ATOM   11411 C  CB    . GLU A 1 2974 ? 141.488 173.583 189.677 1.00 32.49  ? 2974 GLU A CB    1 
ATOM   11412 C  CG    . GLU A 1 2974 ? 140.166 173.741 190.406 1.00 40.77  ? 2974 GLU A CG    1 
ATOM   11413 C  CD    . GLU A 1 2974 ? 139.755 175.192 190.554 1.00 49.05  ? 2974 GLU A CD    1 
ATOM   11414 O  OE1   . GLU A 1 2974 ? 139.550 175.863 189.521 1.00 51.72  ? 2974 GLU A OE1   1 
ATOM   11415 O  OE2   . GLU A 1 2974 ? 139.636 175.662 191.705 1.00 46.43  ? 2974 GLU A OE2   1 
ATOM   11416 N  N     . ASP A 1 2975 ? 143.932 173.222 191.660 1.00 36.20  ? 2975 ASP A N     1 
ATOM   11417 C  CA    . ASP A 1 2975 ? 144.484 172.890 192.971 1.00 30.64  ? 2975 ASP A CA    1 
ATOM   11418 C  C     . ASP A 1 2975 ? 145.297 174.047 193.536 1.00 30.98  ? 2975 ASP A C     1 
ATOM   11419 O  O     . ASP A 1 2975 ? 145.230 174.337 194.737 1.00 30.17  ? 2975 ASP A O     1 
ATOM   11420 C  CB    . ASP A 1 2975 ? 145.337 171.625 192.881 1.00 35.51  ? 2975 ASP A CB    1 
ATOM   11421 C  CG    . ASP A 1 2975 ? 144.510 170.385 192.613 1.00 49.67  ? 2975 ASP A CG    1 
ATOM   11422 O  OD1   . ASP A 1 2975 ? 143.331 170.355 193.024 1.00 54.20  ? 2975 ASP A OD1   1 
ATOM   11423 O  OD2   . ASP A 1 2975 ? 145.039 169.438 191.996 1.00 51.09  ? 2975 ASP A OD2   1 
ATOM   11424 N  N     . LEU A 1 2976 ? 146.077 174.717 192.684 1.00 30.09  ? 2976 LEU A N     1 
ATOM   11425 C  CA    . LEU A 1 2976 ? 146.839 175.880 193.124 1.00 25.92  ? 2976 LEU A CA    1 
ATOM   11426 C  C     . LEU A 1 2976 ? 145.916 176.983 193.616 1.00 25.17  ? 2976 LEU A C     1 
ATOM   11427 O  O     . LEU A 1 2976 ? 146.192 177.624 194.634 1.00 28.60  ? 2976 LEU A O     1 
ATOM   11428 C  CB    . LEU A 1 2976 ? 147.716 176.391 191.982 1.00 25.00  ? 2976 LEU A CB    1 
ATOM   11429 C  CG    . LEU A 1 2976 ? 149.100 175.762 191.833 1.00 25.08  ? 2976 LEU A CG    1 
ATOM   11430 C  CD1   . LEU A 1 2976 ? 149.860 176.434 190.705 1.00 24.33  ? 2976 LEU A CD1   1 
ATOM   11431 C  CD2   . LEU A 1 2976 ? 149.875 175.855 193.135 1.00 29.83  ? 2976 LEU A CD2   1 
ATOM   11432 N  N     . ARG A 1 2977 ? 144.816 177.222 192.899 1.00 26.42  ? 2977 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2977 ? 143.842 178.212 193.342 1.00 30.33  ? 2977 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2977 ? 143.245 177.825 194.686 1.00 28.44  ? 2977 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2977 ? 143.049 178.681 195.554 1.00 30.95  ? 2977 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2977 ? 142.741 178.371 192.295 1.00 29.58  ? 2977 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2977 ? 143.175 179.110 191.046 1.00 24.83  ? 2977 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2977 ? 142.031 179.232 190.062 1.00 29.87  ? 2977 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2977 ? 142.494 179.108 188.686 1.00 35.57  ? 2977 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2977 ? 142.074 178.179 187.839 1.00 37.86  ? 2977 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2977 ? 141.170 177.281 188.192 1.00 37.15  ? 2977 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2977 ? 142.575 178.150 186.607 1.00 42.50  ? 2977 ARG A NH2   1 
ATOM   11443 N  N     . THR A 1 2978 ? 142.951 176.537 194.876 1.00 30.19  ? 2978 THR A N     1 
ATOM   11444 C  CA    . THR A 1 2978 ? 142.413 176.078 196.153 1.00 27.71  ? 2978 THR A CA    1 
ATOM   11445 C  C     . THR A 1 2978 ? 143.389 176.351 197.292 1.00 26.42  ? 2978 THR A C     1 
ATOM   11446 O  O     . THR A 1 2978 ? 143.011 176.905 198.333 1.00 29.13  ? 2978 THR A O     1 
ATOM   11447 C  CB    . THR A 1 2978 ? 142.085 174.586 196.077 1.00 29.29  ? 2978 THR A CB    1 
ATOM   11448 O  OG1   . THR A 1 2978 ? 141.450 174.296 194.826 1.00 32.64  ? 2978 THR A OG1   1 
ATOM   11449 C  CG2   . THR A 1 2978 ? 141.160 174.184 197.215 1.00 33.28  ? 2978 THR A CG2   1 
ATOM   11450 N  N     . VAL A 1 2979 ? 144.657 175.975 197.106 1.00 27.41  ? 2979 VAL A N     1 
ATOM   11451 C  CA    . VAL A 1 2979 ? 145.655 176.177 198.157 1.00 24.76  ? 2979 VAL A CA    1 
ATOM   11452 C  C     . VAL A 1 2979 ? 145.870 177.662 198.423 1.00 25.42  ? 2979 VAL A C     1 
ATOM   11453 O  O     . VAL A 1 2979 ? 145.999 178.086 199.578 1.00 26.99  ? 2979 VAL A O     1 
ATOM   11454 C  CB    . VAL A 1 2979 ? 146.978 175.473 197.802 1.00 25.94  ? 2979 VAL A CB    1 
ATOM   11455 C  CG1   . VAL A 1 2979 ? 147.895 175.447 199.009 1.00 26.51  ? 2979 VAL A CG1   1 
ATOM   11456 C  CG2   . VAL A 1 2979 ? 146.715 174.056 197.354 1.00 26.34  ? 2979 VAL A CG2   1 
ATOM   11457 N  N     . LEU A 1 2980 ? 145.930 178.473 197.365 1.00 26.07  ? 2980 LEU A N     1 
ATOM   11458 C  CA    . LEU A 1 2980 ? 146.133 179.907 197.545 1.00 22.79  ? 2980 LEU A CA    1 
ATOM   11459 C  C     . LEU A 1 2980 ? 144.956 180.546 198.268 1.00 27.44  ? 2980 LEU A C     1 
ATOM   11460 O  O     . LEU A 1 2980 ? 145.149 181.408 199.131 1.00 34.76  ? 2980 LEU A O     1 
ATOM   11461 C  CB    . LEU A 1 2980 ? 146.370 180.582 196.195 1.00 23.14  ? 2980 LEU A CB    1 
ATOM   11462 C  CG    . LEU A 1 2980 ? 147.709 180.296 195.510 1.00 24.50  ? 2980 LEU A CG    1 
ATOM   11463 C  CD1   . LEU A 1 2980 ? 148.039 181.378 194.497 1.00 30.94  ? 2980 LEU A CD1   1 
ATOM   11464 C  CD2   . LEU A 1 2980 ? 148.826 180.156 196.528 1.00 24.68  ? 2980 LEU A CD2   1 
ATOM   11465 N  N     . ARG A 1 2981 ? 143.730 180.141 197.931 1.00 26.65  ? 2981 ARG A N     1 
ATOM   11466 C  CA    . ARG A 1 2981 ? 142.562 180.655 198.636 1.00 27.17  ? 2981 ARG A CA    1 
ATOM   11467 C  C     . ARG A 1 2981 ? 142.589 180.251 200.103 1.00 26.60  ? 2981 ARG A C     1 
ATOM   11468 O  O     . ARG A 1 2981 ? 142.264 181.055 200.984 1.00 30.59  ? 2981 ARG A O     1 
ATOM   11469 C  CB    . ARG A 1 2981 ? 141.282 180.153 197.969 1.00 26.41  ? 2981 ARG A CB    1 
ATOM   11470 C  CG    . ARG A 1 2981 ? 140.752 181.054 196.867 1.00 36.32  ? 2981 ARG A CG    1 
ATOM   11471 C  CD    . ARG A 1 2981 ? 139.415 180.557 196.341 1.00 32.20  ? 2981 ARG A CD    1 
ATOM   11472 N  NE    . ARG A 1 2981 ? 139.535 179.328 195.568 1.00 35.06  ? 2981 ARG A NE    1 
ATOM   11473 C  CZ    . ARG A 1 2981 ? 139.554 179.277 194.243 1.00 43.07  ? 2981 ARG A CZ    1 
ATOM   11474 N  NH1   . ARG A 1 2981 ? 139.474 180.375 193.509 1.00 40.29  ? 2981 ARG A NH1   1 
ATOM   11475 N  NH2   . ARG A 1 2981 ? 139.653 178.096 193.640 1.00 45.07  ? 2981 ARG A NH2   1 
ATOM   11476 N  N     . ARG A 1 2982 ? 142.976 179.007 200.387 1.00 25.26  ? 2982 ARG A N     1 
ATOM   11477 C  CA    . ARG A 1 2982 ? 142.968 178.538 201.767 1.00 24.62  ? 2982 ARG A CA    1 
ATOM   11478 C  C     . ARG A 1 2982 ? 144.046 179.223 202.600 1.00 26.26  ? 2982 ARG A C     1 
ATOM   11479 O  O     . ARG A 1 2982 ? 143.814 179.559 203.767 1.00 29.43  ? 2982 ARG A O     1 
ATOM   11480 C  CB    . ARG A 1 2982 ? 143.140 177.022 201.805 1.00 25.23  ? 2982 ARG A CB    1 
ATOM   11481 C  CG    . ARG A 1 2982 ? 141.900 176.249 201.400 1.00 24.12  ? 2982 ARG A CG    1 
ATOM   11482 C  CD    . ARG A 1 2982 ? 142.155 174.756 201.438 1.00 28.14  ? 2982 ARG A CD    1 
ATOM   11483 N  NE    . ARG A 1 2982 ? 142.618 174.322 202.750 1.00 21.86  ? 2982 ARG A NE    1 
ATOM   11484 C  CZ    . ARG A 1 2982 ? 143.104 173.116 203.010 1.00 23.53  ? 2982 ARG A CZ    1 
ATOM   11485 N  NH1   . ARG A 1 2982 ? 143.210 172.196 202.066 1.00 26.29  ? 2982 ARG A NH1   1 
ATOM   11486 N  NH2   . ARG A 1 2982 ? 143.494 172.827 204.247 1.00 23.72  ? 2982 ARG A NH2   1 
ATOM   11487 N  N     . SER A 1 2983 ? 145.228 179.440 202.025 1.00 27.49  ? 2983 SER A N     1 
ATOM   11488 C  CA    . SER A 1 2983 ? 146.351 179.984 202.778 1.00 25.56  ? 2983 SER A CA    1 
ATOM   11489 C  C     . SER A 1 2983 ? 146.467 181.500 202.693 1.00 27.01  ? 2983 SER A C     1 
ATOM   11490 O  O     . SER A 1 2983 ? 147.294 182.079 203.404 1.00 28.51  ? 2983 SER A O     1 
ATOM   11491 C  CB    . SER A 1 2983 ? 147.662 179.351 202.300 1.00 23.56  ? 2983 SER A CB    1 
ATOM   11492 O  OG    . SER A 1 2983 ? 147.871 179.589 200.919 1.00 27.79  ? 2983 SER A OG    1 
ATOM   11493 N  N     . GLY A 1 2984 ? 145.668 182.156 201.857 1.00 25.41  ? 2984 GLY A N     1 
ATOM   11494 C  CA    . GLY A 1 2984 ? 145.765 183.592 201.705 1.00 24.41  ? 2984 GLY A CA    1 
ATOM   11495 C  C     . GLY A 1 2984 ? 144.504 184.324 202.106 1.00 35.46  ? 2984 GLY A C     1 
ATOM   11496 O  O     . GLY A 1 2984 ? 144.556 185.491 202.506 1.00 42.24  ? 2984 GLY A O     1 
ATOM   11497 N  N     . CYS A 1 2985 ? 143.361 183.650 201.999 1.00 33.64  ? 2985 CYS A N     1 
ATOM   11498 C  CA    . CYS A 1 2985 ? 142.083 184.232 202.384 1.00 30.96  ? 2985 CYS A CA    1 
ATOM   11499 C  C     . CYS A 1 2985 ? 141.583 183.734 203.730 1.00 33.00  ? 2985 CYS A C     1 
ATOM   11500 O  O     . CYS A 1 2985 ? 140.967 184.505 204.473 1.00 38.59  ? 2985 CYS A O     1 
ATOM   11501 C  CB    . CYS A 1 2985 ? 141.022 183.937 201.319 1.00 30.22  ? 2985 CYS A CB    1 
ATOM   11502 S  SG    . CYS A 1 2985 ? 141.468 184.454 199.648 1.00 50.46  ? 2985 CYS A SG    1 
ATOM   11503 N  N     . LYS A 1 2986 ? 141.829 182.469 204.059 1.00 31.65  ? 2986 LYS A N     1 
ATOM   11504 C  CA    . LYS A 1 2986 ? 141.373 181.881 205.310 1.00 29.78  ? 2986 LYS A CA    1 
ATOM   11505 C  C     . LYS A 1 2986 ? 142.445 181.879 206.390 1.00 32.21  ? 2986 LYS A C     1 
ATOM   11506 O  O     . LYS A 1 2986 ? 142.182 181.405 207.500 1.00 34.61  ? 2986 LYS A O     1 
ATOM   11507 C  CB    . LYS A 1 2986 ? 140.877 180.449 205.074 1.00 27.82  ? 2986 LYS A CB    1 
ATOM   11508 C  CG    . LYS A 1 2986 ? 139.986 180.258 203.846 1.00 30.12  ? 2986 LYS A CG    1 
ATOM   11509 C  CD    . LYS A 1 2986 ? 138.959 181.373 203.687 1.00 33.33  ? 2986 LYS A CD    1 
ATOM   11510 C  CE    . LYS A 1 2986 ? 138.385 181.393 202.280 1.00 40.01  ? 2986 LYS A CE    1 
ATOM   11511 N  NZ    . LYS A 1 2986 ? 137.120 182.175 202.201 1.00 40.02  ? 2986 LYS A NZ    1 
ATOM   11512 N  N     . ASN A 1 2987 ? 143.638 182.403 206.095 1.00 30.39  ? 2987 ASN A N     1 
ATOM   11513 C  CA    . ASN A 1 2987 ? 144.743 182.466 207.054 1.00 28.16  ? 2987 ASN A CA    1 
ATOM   11514 C  C     . ASN A 1 2987 ? 145.070 181.088 207.625 1.00 33.70  ? 2987 ASN A C     1 
ATOM   11515 O  O     . ASN A 1 2987 ? 145.256 180.922 208.832 1.00 30.66  ? 2987 ASN A O     1 
ATOM   11516 C  CB    . ASN A 1 2987 ? 144.445 183.462 208.177 1.00 25.53  ? 2987 ASN A CB    1 
ATOM   11517 C  CG    . ASN A 1 2987 ? 145.698 183.923 208.892 1.00 28.33  ? 2987 ASN A CG    1 
ATOM   11518 O  OD1   . ASN A 1 2987 ? 146.669 184.335 208.261 1.00 30.55  ? 2987 ASN A OD1   1 
ATOM   11519 N  ND2   . ASN A 1 2987 ? 145.682 183.854 210.217 1.00 26.37  ? 2987 ASN A ND2   1 
ATOM   11520 N  N     . GLU A 1 2988 ? 145.138 180.089 206.752 1.00 30.57  ? 2988 GLU A N     1 
ATOM   11521 C  CA    . GLU A 1 2988 ? 145.423 178.716 207.146 1.00 25.31  ? 2988 GLU A CA    1 
ATOM   11522 C  C     . GLU A 1 2988 ? 146.833 178.357 206.699 1.00 25.04  ? 2988 GLU A C     1 
ATOM   11523 O  O     . GLU A 1 2988 ? 147.142 178.414 205.505 1.00 25.60  ? 2988 GLU A O     1 
ATOM   11524 C  CB    . GLU A 1 2988 ? 144.403 177.752 206.542 1.00 25.14  ? 2988 GLU A CB    1 
ATOM   11525 C  CG    . GLU A 1 2988 ? 144.695 176.287 206.813 1.00 28.43  ? 2988 GLU A CG    1 
ATOM   11526 C  CD    . GLU A 1 2988 ? 143.725 175.363 206.106 1.00 38.30  ? 2988 GLU A CD    1 
ATOM   11527 O  OE1   . GLU A 1 2988 ? 143.566 174.209 206.554 1.00 36.26  ? 2988 GLU A OE1   1 
ATOM   11528 O  OE2   . GLU A 1 2988 ? 143.120 175.790 205.100 1.00 34.51  ? 2988 GLU A OE2   1 
ATOM   11529 N  N     . LYS A 1 2989 ? 147.681 177.988 207.656 1.00 24.94  ? 2989 LYS A N     1 
ATOM   11530 C  CA    . LYS A 1 2989 ? 149.036 177.563 207.336 1.00 19.21  ? 2989 LYS A CA    1 
ATOM   11531 C  C     . LYS A 1 2989 ? 148.992 176.196 206.666 1.00 18.43  ? 2989 LYS A C     1 
ATOM   11532 O  O     . LYS A 1 2989 ? 148.471 175.234 207.237 1.00 22.74  ? 2989 LYS A O     1 
ATOM   11533 C  CB    . LYS A 1 2989 ? 149.888 177.519 208.600 1.00 15.86  ? 2989 LYS A CB    1 
ATOM   11534 C  CG    . LYS A 1 2989 ? 149.987 178.847 209.327 1.00 20.86  ? 2989 LYS A CG    1 
ATOM   11535 C  CD    . LYS A 1 2989 ? 150.928 178.752 210.514 1.00 24.41  ? 2989 LYS A CD    1 
ATOM   11536 C  CE    . LYS A 1 2989 ? 150.488 177.666 211.481 1.00 32.88  ? 2989 LYS A CE    1 
ATOM   11537 N  NZ    . LYS A 1 2989 ? 151.437 177.521 212.620 1.00 29.68  ? 2989 LYS A NZ    1 
ATOM   11538 N  N     . ILE A 1 2990 ? 149.540 176.109 205.456 1.00 16.58  ? 2990 ILE A N     1 
ATOM   11539 C  CA    . ILE A 1 2990 ? 149.421 174.918 204.626 1.00 13.32  ? 2990 ILE A CA    1 
ATOM   11540 C  C     . ILE A 1 2990 ? 150.807 174.475 204.184 1.00 13.33  ? 2990 ILE A C     1 
ATOM   11541 O  O     . ILE A 1 2990 ? 151.569 175.269 203.620 1.00 14.37  ? 2990 ILE A O     1 
ATOM   11542 C  CB    . ILE A 1 2990 ? 148.523 175.170 203.401 1.00 14.49  ? 2990 ILE A CB    1 
ATOM   11543 C  CG1   . ILE A 1 2990 ? 147.057 175.250 203.825 1.00 17.22  ? 2990 ILE A CG1   1 
ATOM   11544 C  CG2   . ILE A 1 2990 ? 148.726 174.082 202.357 1.00 11.92  ? 2990 ILE A CG2   1 
ATOM   11545 C  CD1   . ILE A 1 2990 ? 146.093 175.259 202.669 1.00 20.88  ? 2990 ILE A CD1   1 
ATOM   11546 N  N     . ALA A 1 2991 ? 151.119 173.204 204.429 1.00 14.16  ? 2991 ALA A N     1 
ATOM   11547 C  CA    . ALA A 1 2991 ? 152.313 172.559 203.892 1.00 12.67  ? 2991 ALA A CA    1 
ATOM   11548 C  C     . ALA A 1 2991 ? 151.910 171.843 202.609 1.00 12.23  ? 2991 ALA A C     1 
ATOM   11549 O  O     . ALA A 1 2991 ? 151.266 170.791 202.641 1.00 10.55  ? 2991 ALA A O     1 
ATOM   11550 C  CB    . ALA A 1 2991 ? 152.916 171.599 204.910 1.00 9.11   ? 2991 ALA A CB    1 
ATOM   11551 N  N     . PHE A 1 2992 ? 152.276 172.430 201.475 1.00 12.45  ? 2992 PHE A N     1 
ATOM   11552 C  CA    . PHE A 1 2992 ? 151.994 171.872 200.156 1.00 11.55  ? 2992 PHE A CA    1 
ATOM   11553 C  C     . PHE A 1 2992 ? 153.144 170.934 199.812 1.00 15.43  ? 2992 PHE A C     1 
ATOM   11554 O  O     . PHE A 1 2992 ? 154.244 171.378 199.481 1.00 17.73  ? 2992 PHE A O     1 
ATOM   11555 C  CB    . PHE A 1 2992 ? 151.842 172.992 199.133 1.00 11.80  ? 2992 PHE A CB    1 
ATOM   11556 C  CG    . PHE A 1 2992 ? 151.398 172.534 197.770 1.00 14.86  ? 2992 PHE A CG    1 
ATOM   11557 C  CD1   . PHE A 1 2992 ? 150.962 171.238 197.555 1.00 20.54  ? 2992 PHE A CD1   1 
ATOM   11558 C  CD2   . PHE A 1 2992 ? 151.424 173.410 196.700 1.00 14.12  ? 2992 PHE A CD2   1 
ATOM   11559 C  CE1   . PHE A 1 2992 ? 150.559 170.829 196.301 1.00 24.86  ? 2992 PHE A CE1   1 
ATOM   11560 C  CE2   . PHE A 1 2992 ? 151.022 173.006 195.446 1.00 16.26  ? 2992 PHE A CE2   1 
ATOM   11561 C  CZ    . PHE A 1 2992 ? 150.589 171.715 195.247 1.00 25.96  ? 2992 PHE A CZ    1 
ATOM   11562 N  N     . ILE A 1 2993 ? 152.894 169.632 199.896 1.00 14.23  ? 2993 ILE A N     1 
ATOM   11563 C  CA    . ILE A 1 2993 ? 153.920 168.628 199.644 1.00 11.04  ? 2993 ILE A CA    1 
ATOM   11564 C  C     . ILE A 1 2993 ? 153.780 168.141 198.209 1.00 15.97  ? 2993 ILE A C     1 
ATOM   11565 O  O     . ILE A 1 2993 ? 152.732 167.615 197.820 1.00 21.66  ? 2993 ILE A O     1 
ATOM   11566 C  CB    . ILE A 1 2993 ? 153.814 167.464 200.640 1.00 11.55  ? 2993 ILE A CB    1 
ATOM   11567 C  CG1   . ILE A 1 2993 ? 153.921 167.988 202.072 1.00 9.87   ? 2993 ILE A CG1   1 
ATOM   11568 C  CG2   . ILE A 1 2993 ? 154.891 166.429 200.365 1.00 17.67  ? 2993 ILE A CG2   1 
ATOM   11569 C  CD1   . ILE A 1 2993 ? 154.037 166.906 203.113 1.00 9.49   ? 2993 ILE A CD1   1 
ATOM   11570 N  N     . MET A 1 2994 ? 154.837 168.315 197.422 1.00 15.84  ? 2994 MET A N     1 
ATOM   11571 C  CA    . MET A 1 2994 ? 154.844 167.959 196.013 1.00 17.05  ? 2994 MET A CA    1 
ATOM   11572 C  C     . MET A 1 2994 ? 156.035 167.058 195.728 1.00 23.64  ? 2994 MET A C     1 
ATOM   11573 O  O     . MET A 1 2994 ? 157.145 167.315 196.203 1.00 28.36  ? 2994 MET A O     1 
ATOM   11574 C  CB    . MET A 1 2994 ? 154.910 169.208 195.132 1.00 17.06  ? 2994 MET A CB    1 
ATOM   11575 C  CG    . MET A 1 2994 ? 154.800 168.935 193.647 1.00 35.57  ? 2994 MET A CG    1 
ATOM   11576 S  SD    . MET A 1 2994 ? 154.877 170.457 192.689 1.00 64.45  ? 2994 MET A SD    1 
ATOM   11577 C  CE    . MET A 1 2994 ? 153.284 171.164 193.077 1.00 32.21  ? 2994 MET A CE    1 
ATOM   11578 N  N     . ASP A 1 2995 ? 155.801 166.009 194.950 1.00 27.81  ? 2995 ASP A N     1 
ATOM   11579 C  CA    . ASP A 1 2995 ? 156.838 165.067 194.567 1.00 26.73  ? 2995 ASP A CA    1 
ATOM   11580 C  C     . ASP A 1 2995 ? 157.169 165.246 193.091 1.00 32.29  ? 2995 ASP A C     1 
ATOM   11581 O  O     . ASP A 1 2995 ? 156.340 165.699 192.297 1.00 38.63  ? 2995 ASP A O     1 
ATOM   11582 C  CB    . ASP A 1 2995 ? 156.398 163.626 194.855 1.00 28.50  ? 2995 ASP A CB    1 
ATOM   11583 C  CG    . ASP A 1 2995 ? 157.411 162.599 194.392 1.00 38.34  ? 2995 ASP A CG    1 
ATOM   11584 O  OD1   . ASP A 1 2995 ? 158.452 162.443 195.064 1.00 35.08  ? 2995 ASP A OD1   1 
ATOM   11585 O  OD2   . ASP A 1 2995 ? 157.166 161.944 193.361 1.00 40.66  ? 2995 ASP A OD2   1 
ATOM   11586 N  N     . GLU A 1 2996 ? 158.408 164.899 192.732 1.00 31.06  ? 2996 GLU A N     1 
ATOM   11587 C  CA    . GLU A 1 2996 ? 158.863 165.090 191.359 1.00 33.17  ? 2996 GLU A CA    1 
ATOM   11588 C  C     . GLU A 1 2996 ? 158.035 164.282 190.368 1.00 32.36  ? 2996 GLU A C     1 
ATOM   11589 O  O     . GLU A 1 2996 ? 157.921 164.667 189.199 1.00 35.98  ? 2996 GLU A O     1 
ATOM   11590 C  CB    . GLU A 1 2996 ? 160.342 164.724 191.243 1.00 40.45  ? 2996 GLU A CB    1 
ATOM   11591 C  CG    . GLU A 1 2996 ? 160.658 163.285 191.616 1.00 39.28  ? 2996 GLU A CG    1 
ATOM   11592 C  CD    . GLU A 1 2996 ? 161.910 162.773 190.938 1.00 35.47  ? 2996 GLU A CD    1 
ATOM   11593 O  OE1   . GLU A 1 2996 ? 162.531 163.542 190.175 1.00 40.90  ? 2996 GLU A OE1   1 
ATOM   11594 O  OE2   . GLU A 1 2996 ? 162.272 161.600 191.164 1.00 32.22  ? 2996 GLU A OE2   1 
ATOM   11595 N  N     . SER A 1 2997 ? 157.450 163.167 190.807 1.00 37.72  ? 2997 SER A N     1 
ATOM   11596 C  CA    . SER A 1 2997 ? 156.603 162.371 189.928 1.00 41.02  ? 2997 SER A CA    1 
ATOM   11597 C  C     . SER A 1 2997 ? 155.238 163.004 189.695 1.00 41.76  ? 2997 SER A C     1 
ATOM   11598 O  O     . SER A 1 2997 ? 154.552 162.625 188.740 1.00 49.10  ? 2997 SER A O     1 
ATOM   11599 C  CB    . SER A 1 2997 ? 156.425 160.963 190.495 1.00 40.12  ? 2997 SER A CB    1 
ATOM   11600 O  OG    . SER A 1 2997 ? 155.819 161.002 191.775 1.00 43.90  ? 2997 SER A OG    1 
ATOM   11601 N  N     . ASN A 1 2998 ? 154.831 163.954 190.537 1.00 38.07  ? 2998 ASN A N     1 
ATOM   11602 C  CA    . ASN A 1 2998 ? 153.577 164.666 190.335 1.00 36.93  ? 2998 ASN A CA    1 
ATOM   11603 C  C     . ASN A 1 2998 ? 153.628 165.629 189.158 1.00 40.76  ? 2998 ASN A C     1 
ATOM   11604 O  O     . ASN A 1 2998 ? 152.583 166.158 188.766 1.00 48.45  ? 2998 ASN A O     1 
ATOM   11605 C  CB    . ASN A 1 2998 ? 153.195 165.437 191.601 1.00 35.12  ? 2998 ASN A CB    1 
ATOM   11606 C  CG    . ASN A 1 2998 ? 152.900 164.525 192.770 1.00 40.12  ? 2998 ASN A CG    1 
ATOM   11607 O  OD1   . ASN A 1 2998 ? 152.962 163.302 192.650 1.00 40.40  ? 2998 ASN A OD1   1 
ATOM   11608 N  ND2   . ASN A 1 2998 ? 152.576 165.117 193.913 1.00 31.02  ? 2998 ASN A ND2   1 
ATOM   11609 N  N     . VAL A 1 2999 ? 154.808 165.865 188.590 1.00 41.94  ? 2999 VAL A N     1 
ATOM   11610 C  CA    . VAL A 1 2999 ? 154.981 166.811 187.490 1.00 43.00  ? 2999 VAL A CA    1 
ATOM   11611 C  C     . VAL A 1 2999 ? 154.756 166.055 186.183 1.00 51.01  ? 2999 VAL A C     1 
ATOM   11612 O  O     . VAL A 1 2999 ? 155.369 165.015 185.938 1.00 55.57  ? 2999 VAL A O     1 
ATOM   11613 C  CB    . VAL A 1 2999 ? 156.358 167.474 187.525 1.00 43.83  ? 2999 VAL A CB    1 
ATOM   11614 C  CG1   . VAL A 1 2999 ? 156.664 168.107 186.181 1.00 48.89  ? 2999 VAL A CG1   1 
ATOM   11615 C  CG2   . VAL A 1 2999 ? 156.414 168.506 188.640 1.00 36.77  ? 2999 VAL A CG2   1 
ATOM   11616 N  N     . LEU A 1 3000 ? 153.874 166.582 185.337 1.00 47.31  ? 3000 LEU A N     1 
ATOM   11617 C  CA    . LEU A 1 3000 ? 153.595 166.005 184.030 1.00 50.45  ? 3000 LEU A CA    1 
ATOM   11618 C  C     . LEU A 1 3000 ? 153.913 166.956 182.884 1.00 58.51  ? 3000 LEU A C     1 
ATOM   11619 O  O     . LEU A 1 3000 ? 153.801 166.561 181.719 1.00 63.83  ? 3000 LEU A O     1 
ATOM   11620 C  CB    . LEU A 1 3000 ? 152.128 165.575 183.952 1.00 48.96  ? 3000 LEU A CB    1 
ATOM   11621 C  CG    . LEU A 1 3000 ? 151.597 164.805 185.162 1.00 56.02  ? 3000 LEU A CG    1 
ATOM   11622 C  CD1   . LEU A 1 3000 ? 150.080 164.719 185.120 1.00 54.72  ? 3000 LEU A CD1   1 
ATOM   11623 C  CD2   . LEU A 1 3000 ? 152.213 163.417 185.228 1.00 53.14  ? 3000 LEU A CD2   1 
ATOM   11624 N  N     . ASP A 1 3001 ? 154.308 168.191 183.183 1.00 54.90  ? 3001 ASP A N     1 
ATOM   11625 C  CA    . ASP A 1 3001 ? 154.541 169.204 182.164 1.00 56.49  ? 3001 ASP A CA    1 
ATOM   11626 C  C     . ASP A 1 3001 ? 155.419 170.294 182.762 1.00 50.85  ? 3001 ASP A C     1 
ATOM   11627 O  O     . ASP A 1 3001 ? 155.573 170.393 183.982 1.00 44.20  ? 3001 ASP A O     1 
ATOM   11628 C  CB    . ASP A 1 3001 ? 153.219 169.786 181.646 1.00 54.10  ? 3001 ASP A CB    1 
ATOM   11629 C  CG    . ASP A 1 3001 ? 153.401 170.673 180.426 1.00 61.66  ? 3001 ASP A CG    1 
ATOM   11630 O  OD1   . ASP A 1 3001 ? 154.555 170.867 179.988 1.00 65.75  ? 3001 ASP A OD1   1 
ATOM   11631 O  OD2   . ASP A 1 3001 ? 152.385 171.179 179.907 1.00 65.56  ? 3001 ASP A OD2   1 
ATOM   11632 N  N     . SER A 1 3002 ? 156.002 171.110 181.880 1.00 48.70  ? 3002 SER A N     1 
ATOM   11633 C  CA    . SER A 1 3002 ? 156.818 172.231 182.331 1.00 50.85  ? 3002 SER A CA    1 
ATOM   11634 C  C     . SER A 1 3002 ? 155.980 173.362 182.915 1.00 45.14  ? 3002 SER A C     1 
ATOM   11635 O  O     . SER A 1 3002 ? 156.516 174.191 183.658 1.00 48.19  ? 3002 SER A O     1 
ATOM   11636 C  CB    . SER A 1 3002 ? 157.673 172.758 181.178 1.00 48.85  ? 3002 SER A CB    1 
ATOM   11637 O  OG    . SER A 1 3002 ? 158.483 173.841 181.601 1.00 43.27  ? 3002 SER A OG    1 
ATOM   11638 N  N     . GLY A 1 3003 ? 154.687 173.420 182.589 1.00 37.37  ? 3003 GLY A N     1 
ATOM   11639 C  CA    . GLY A 1 3003 ? 153.830 174.433 183.183 1.00 33.61  ? 3003 GLY A CA    1 
ATOM   11640 C  C     . GLY A 1 3003 ? 153.707 174.275 184.685 1.00 36.84  ? 3003 GLY A C     1 
ATOM   11641 O  O     . GLY A 1 3003 ? 153.573 175.262 185.416 1.00 43.07  ? 3003 GLY A O     1 
ATOM   11642 N  N     . PHE A 1 3004 ? 153.742 173.029 185.164 1.00 34.94  ? 3004 PHE A N     1 
ATOM   11643 C  CA    . PHE A 1 3004 ? 153.831 172.771 186.596 1.00 35.97  ? 3004 PHE A CA    1 
ATOM   11644 C  C     . PHE A 1 3004 ? 154.996 173.536 187.206 1.00 34.64  ? 3004 PHE A C     1 
ATOM   11645 O  O     . PHE A 1 3004 ? 154.831 174.278 188.181 1.00 35.12  ? 3004 PHE A O     1 
ATOM   11646 C  CB    . PHE A 1 3004 ? 154.007 171.270 186.838 1.00 43.59  ? 3004 PHE A CB    1 
ATOM   11647 C  CG    . PHE A 1 3004 ? 152.813 170.439 186.462 1.00 41.89  ? 3004 PHE A CG    1 
ATOM   11648 C  CD1   . PHE A 1 3004 ? 151.746 170.295 187.326 1.00 36.49  ? 3004 PHE A CD1   1 
ATOM   11649 C  CD2   . PHE A 1 3004 ? 152.749 169.825 185.227 1.00 49.96  ? 3004 PHE A CD2   1 
ATOM   11650 C  CE1   . PHE A 1 3004 ? 150.655 169.524 186.975 1.00 40.46  ? 3004 PHE A CE1   1 
ATOM   11651 C  CE2   . PHE A 1 3004 ? 151.656 169.063 184.869 1.00 52.88  ? 3004 PHE A CE2   1 
ATOM   11652 C  CZ    . PHE A 1 3004 ? 150.607 168.914 185.744 1.00 48.69  ? 3004 PHE A CZ    1 
ATOM   11653 N  N     . LEU A 1 3005 ? 156.186 173.380 186.619 1.00 37.97  ? 3005 LEU A N     1 
ATOM   11654 C  CA    . LEU A 1 3005 ? 157.369 174.049 187.144 1.00 34.82  ? 3005 LEU A CA    1 
ATOM   11655 C  C     . LEU A 1 3005 ? 157.286 175.557 186.983 1.00 31.56  ? 3005 LEU A C     1 
ATOM   11656 O  O     . LEU A 1 3005 ? 157.762 176.285 187.852 1.00 35.31  ? 3005 LEU A O     1 
ATOM   11657 C  CB    . LEU A 1 3005 ? 158.637 173.521 186.474 1.00 42.05  ? 3005 LEU A CB    1 
ATOM   11658 C  CG    . LEU A 1 3005 ? 159.265 172.236 187.023 1.00 42.29  ? 3005 LEU A CG    1 
ATOM   11659 C  CD1   . LEU A 1 3005 ? 159.730 172.430 188.458 1.00 36.10  ? 3005 LEU A CD1   1 
ATOM   11660 C  CD2   . LEU A 1 3005 ? 158.322 171.066 186.926 1.00 38.79  ? 3005 LEU A CD2   1 
ATOM   11661 N  N     . GLU A 1 3006 ? 156.697 176.047 185.891 1.00 29.58  ? 3006 GLU A N     1 
ATOM   11662 C  CA    . GLU A 1 3006 ? 156.548 177.492 185.724 1.00 26.12  ? 3006 GLU A CA    1 
ATOM   11663 C  C     . GLU A 1 3006 ? 155.691 178.091 186.831 1.00 28.05  ? 3006 GLU A C     1 
ATOM   11664 O  O     . GLU A 1 3006 ? 156.086 179.069 187.486 1.00 28.50  ? 3006 GLU A O     1 
ATOM   11665 C  CB    . GLU A 1 3006 ? 155.947 177.799 184.352 1.00 25.41  ? 3006 GLU A CB    1 
ATOM   11666 C  CG    . GLU A 1 3006 ? 156.853 177.437 183.196 1.00 36.58  ? 3006 GLU A CG    1 
ATOM   11667 C  CD    . GLU A 1 3006 ? 158.095 178.300 183.160 1.00 43.25  ? 3006 GLU A CD    1 
ATOM   11668 O  OE1   . GLU A 1 3006 ? 158.013 179.477 183.569 1.00 36.67  ? 3006 GLU A OE1   1 
ATOM   11669 O  OE2   . GLU A 1 3006 ? 159.162 177.800 182.750 1.00 39.56  ? 3006 GLU A OE2   1 
ATOM   11670 N  N     . ARG A 1 3007 ? 154.512 177.509 187.061 1.00 27.43  ? 3007 ARG A N     1 
ATOM   11671 C  CA    . ARG A 1 3007 ? 153.623 178.032 188.090 1.00 26.51  ? 3007 ARG A CA    1 
ATOM   11672 C  C     . ARG A 1 3007 ? 154.244 177.891 189.474 1.00 25.78  ? 3007 ARG A C     1 
ATOM   11673 O  O     . ARG A 1 3007 ? 154.154 178.810 190.299 1.00 25.08  ? 3007 ARG A O     1 
ATOM   11674 C  CB    . ARG A 1 3007 ? 152.270 177.326 188.018 1.00 27.61  ? 3007 ARG A CB    1 
ATOM   11675 C  CG    . ARG A 1 3007 ? 151.568 177.524 186.684 1.00 22.49  ? 3007 ARG A CG    1 
ATOM   11676 C  CD    . ARG A 1 3007 ? 151.133 178.968 186.509 1.00 32.80  ? 3007 ARG A CD    1 
ATOM   11677 N  NE    . ARG A 1 3007 ? 150.471 179.199 185.231 1.00 48.69  ? 3007 ARG A NE    1 
ATOM   11678 C  CZ    . ARG A 1 3007 ? 149.166 179.085 185.029 1.00 45.32  ? 3007 ARG A CZ    1 
ATOM   11679 N  NH1   . ARG A 1 3007 ? 148.342 178.757 186.008 1.00 37.35  ? 3007 ARG A NH1   1 
ATOM   11680 N  NH2   . ARG A 1 3007 ? 148.676 179.312 183.814 1.00 48.51  ? 3007 ARG A NH2   1 
ATOM   11681 N  N     . MET A 1 3008 ? 154.898 176.757 189.740 1.00 28.29  ? 3008 MET A N     1 
ATOM   11682 C  CA    . MET A 1 3008 ? 155.528 176.563 191.041 1.00 23.77  ? 3008 MET A CA    1 
ATOM   11683 C  C     . MET A 1 3008 ? 156.687 177.529 191.244 1.00 24.52  ? 3008 MET A C     1 
ATOM   11684 O  O     . MET A 1 3008 ? 156.893 178.029 192.351 1.00 28.68  ? 3008 MET A O     1 
ATOM   11685 C  CB    . MET A 1 3008 ? 155.995 175.117 191.189 1.00 24.35  ? 3008 MET A CB    1 
ATOM   11686 C  CG    . MET A 1 3008 ? 154.868 174.141 191.468 1.00 27.21  ? 3008 MET A CG    1 
ATOM   11687 S  SD    . MET A 1 3008 ? 153.722 174.739 192.725 1.00 39.35  ? 3008 MET A SD    1 
ATOM   11688 C  CE    . MET A 1 3008 ? 154.784 174.781 194.165 1.00 26.50  ? 3008 MET A CE    1 
ATOM   11689 N  N     . ASN A 1 3009 ? 157.453 177.804 190.187 1.00 26.98  ? 3009 ASN A N     1 
ATOM   11690 C  CA    . ASN A 1 3009 ? 158.555 178.755 190.274 1.00 20.98  ? 3009 ASN A CA    1 
ATOM   11691 C  C     . ASN A 1 3009 ? 158.040 180.146 190.612 1.00 21.20  ? 3009 ASN A C     1 
ATOM   11692 O  O     . ASN A 1 3009 ? 158.569 180.822 191.505 1.00 21.72  ? 3009 ASN A O     1 
ATOM   11693 C  CB    . ASN A 1 3009 ? 159.318 178.761 188.946 1.00 20.65  ? 3009 ASN A CB    1 
ATOM   11694 C  CG    . ASN A 1 3009 ? 160.565 179.617 188.983 1.00 28.14  ? 3009 ASN A CG    1 
ATOM   11695 O  OD1   . ASN A 1 3009 ? 161.554 179.263 189.621 1.00 24.14  ? 3009 ASN A OD1   1 
ATOM   11696 N  ND2   . ASN A 1 3009 ? 160.531 180.745 188.285 1.00 24.52  ? 3009 ASN A ND2   1 
ATOM   11697 N  N     . THR A 1 3010 ? 156.986 180.580 189.915 1.00 29.79  ? 3010 THR A N     1 
ATOM   11698 C  CA    . THR A 1 3010 ? 156.408 181.889 190.203 1.00 25.71  ? 3010 THR A CA    1 
ATOM   11699 C  C     . THR A 1 3010 ? 155.873 181.956 191.629 1.00 22.40  ? 3010 THR A C     1 
ATOM   11700 O  O     . THR A 1 3010 ? 156.089 182.950 192.334 1.00 25.16  ? 3010 THR A O     1 
ATOM   11701 C  CB    . THR A 1 3010 ? 155.301 182.210 189.199 1.00 27.28  ? 3010 THR A CB    1 
ATOM   11702 O  OG1   . THR A 1 3010 ? 155.732 181.856 187.880 1.00 25.10  ? 3010 THR A OG1   1 
ATOM   11703 C  CG2   . THR A 1 3010 ? 154.970 183.691 189.234 1.00 25.33  ? 3010 THR A CG2   1 
ATOM   11704 N  N     . LEU A 1 3011 ? 155.183 180.903 192.078 1.00 21.64  ? 3011 LEU A N     1 
ATOM   11705 C  CA    . LEU A 1 3011 ? 154.627 180.904 193.428 1.00 20.39  ? 3011 LEU A CA    1 
ATOM   11706 C  C     . LEU A 1 3011 ? 155.724 180.900 194.487 1.00 20.87  ? 3011 LEU A C     1 
ATOM   11707 O  O     . LEU A 1 3011 ? 155.611 181.588 195.508 1.00 20.47  ? 3011 LEU A O     1 
ATOM   11708 C  CB    . LEU A 1 3011 ? 153.696 179.707 193.613 1.00 19.67  ? 3011 LEU A CB    1 
ATOM   11709 C  CG    . LEU A 1 3011 ? 153.227 179.417 195.040 1.00 20.61  ? 3011 LEU A CG    1 
ATOM   11710 C  CD1   . LEU A 1 3011 ? 152.371 180.558 195.560 1.00 19.33  ? 3011 LEU A CD1   1 
ATOM   11711 C  CD2   . LEU A 1 3011 ? 152.463 178.106 195.097 1.00 24.39  ? 3011 LEU A CD2   1 
ATOM   11712 N  N     . LEU A 1 3012 ? 156.787 180.123 194.271 1.00 19.38  ? 3012 LEU A N     1 
ATOM   11713 C  CA    . LEU A 1 3012 ? 157.882 180.075 195.233 1.00 16.89  ? 3012 LEU A CA    1 
ATOM   11714 C  C     . LEU A 1 3012 ? 158.597 181.414 195.324 1.00 20.97  ? 3012 LEU A C     1 
ATOM   11715 O  O     . LEU A 1 3012 ? 158.956 181.860 196.420 1.00 20.91  ? 3012 LEU A O     1 
ATOM   11716 C  CB    . LEU A 1 3012 ? 158.871 178.973 194.852 1.00 16.32  ? 3012 LEU A CB    1 
ATOM   11717 C  CG    . LEU A 1 3012 ? 158.414 177.524 195.018 1.00 13.19  ? 3012 LEU A CG    1 
ATOM   11718 C  CD1   . LEU A 1 3012 ? 159.453 176.568 194.461 1.00 14.27  ? 3012 LEU A CD1   1 
ATOM   11719 C  CD2   . LEU A 1 3012 ? 158.133 177.221 196.468 1.00 17.12  ? 3012 LEU A CD2   1 
ATOM   11720 N  N     . ALA A 1 3013 ? 158.822 182.069 194.185 1.00 18.47  ? 3013 ALA A N     1 
ATOM   11721 C  CA    . ALA A 1 3013 ? 159.615 183.291 194.204 1.00 16.69  ? 3013 ALA A CA    1 
ATOM   11722 C  C     . ALA A 1 3013 ? 158.805 184.492 194.683 1.00 22.54  ? 3013 ALA A C     1 
ATOM   11723 O  O     . ALA A 1 3013 ? 159.272 185.261 195.530 1.00 24.83  ? 3013 ALA A O     1 
ATOM   11724 C  CB    . ALA A 1 3013 ? 160.203 183.551 192.821 1.00 19.48  ? 3013 ALA A CB    1 
ATOM   11725 N  N     . ASN A 1 3014 ? 157.589 184.672 194.163 1.00 25.34  ? 3014 ASN A N     1 
ATOM   11726 C  CA    . ASN A 1 3014 ? 156.807 185.859 194.486 1.00 22.81  ? 3014 ASN A CA    1 
ATOM   11727 C  C     . ASN A 1 3014 ? 155.686 185.609 195.483 1.00 27.87  ? 3014 ASN A C     1 
ATOM   11728 O  O     . ASN A 1 3014 ? 155.248 186.557 196.142 1.00 29.99  ? 3014 ASN A O     1 
ATOM   11729 C  CB    . ASN A 1 3014 ? 156.202 186.469 193.215 1.00 22.63  ? 3014 ASN A CB    1 
ATOM   11730 C  CG    . ASN A 1 3014 ? 157.254 186.966 192.248 1.00 28.79  ? 3014 ASN A CG    1 
ATOM   11731 O  OD1   . ASN A 1 3014 ? 157.396 186.442 191.144 1.00 29.16  ? 3014 ASN A OD1   1 
ATOM   11732 N  ND2   . ASN A 1 3014 ? 158.001 187.984 192.659 1.00 22.33  ? 3014 ASN A ND2   1 
ATOM   11733 N  N     . GLY A 1 3015 ? 155.212 184.374 195.613 1.00 26.42  ? 3015 GLY A N     1 
ATOM   11734 C  CA    . GLY A 1 3015 ? 154.054 184.117 196.440 1.00 24.19  ? 3015 GLY A CA    1 
ATOM   11735 C  C     . GLY A 1 3015 ? 152.728 184.294 195.741 1.00 25.61  ? 3015 GLY A C     1 
ATOM   11736 O  O     . GLY A 1 3015 ? 151.686 184.250 196.402 1.00 29.05  ? 3015 GLY A O     1 
ATOM   11737 N  N     . GLU A 1 3016 ? 152.735 184.500 194.427 1.00 28.77  ? 3016 GLU A N     1 
ATOM   11738 C  CA    . GLU A 1 3016 ? 151.517 184.671 193.648 1.00 29.63  ? 3016 GLU A CA    1 
ATOM   11739 C  C     . GLU A 1 3016 ? 151.811 184.348 192.192 1.00 34.16  ? 3016 GLU A C     1 
ATOM   11740 O  O     . GLU A 1 3016 ? 152.941 184.521 191.730 1.00 36.75  ? 3016 GLU A O     1 
ATOM   11741 C  CB    . GLU A 1 3016 ? 150.970 186.099 193.788 1.00 29.23  ? 3016 GLU A CB    1 
ATOM   11742 C  CG    . GLU A 1 3016 ? 151.914 187.196 193.299 1.00 29.63  ? 3016 GLU A CG    1 
ATOM   11743 C  CD    . GLU A 1 3016 ? 151.805 187.469 191.813 1.00 44.33  ? 3016 GLU A CD    1 
ATOM   11744 O  OE1   . GLU A 1 3016 ? 150.775 187.104 191.211 1.00 48.91  ? 3016 GLU A OE1   1 
ATOM   11745 O  OE2   . GLU A 1 3016 ? 152.755 188.046 191.245 1.00 43.62  ? 3016 GLU A OE2   1 
ATOM   11746 N  N     . VAL A 1 3017 ? 150.794 183.876 191.484 1.00 34.38  ? 3017 VAL A N     1 
ATOM   11747 C  CA    . VAL A 1 3017 ? 150.863 183.648 190.043 1.00 35.79  ? 3017 VAL A CA    1 
ATOM   11748 C  C     . VAL A 1 3017 ? 150.042 184.739 189.363 1.00 39.78  ? 3017 VAL A C     1 
ATOM   11749 O  O     . VAL A 1 3017 ? 148.839 184.853 189.644 1.00 39.08  ? 3017 VAL A O     1 
ATOM   11750 C  CB    . VAL A 1 3017 ? 150.351 182.252 189.664 1.00 33.63  ? 3017 VAL A CB    1 
ATOM   11751 C  CG1   . VAL A 1 3017 ? 150.336 182.090 188.154 1.00 33.79  ? 3017 VAL A CG1   1 
ATOM   11752 C  CG2   . VAL A 1 3017 ? 151.211 181.179 190.311 1.00 25.11  ? 3017 VAL A CG2   1 
ATOM   11753 N  N     . PRO A 1 3018 ? 150.638 185.557 188.490 1.00 38.34  ? 3018 PRO A N     1 
ATOM   11754 C  CA    . PRO A 1 3018 ? 149.900 186.714 187.952 1.00 43.42  ? 3018 PRO A CA    1 
ATOM   11755 C  C     . PRO A 1 3018 ? 148.655 186.346 187.161 1.00 45.02  ? 3018 PRO A C     1 
ATOM   11756 O  O     . PRO A 1 3018 ? 147.663 187.083 187.205 1.00 50.15  ? 3018 PRO A O     1 
ATOM   11757 C  CB    . PRO A 1 3018 ? 150.949 187.411 187.076 1.00 41.20  ? 3018 PRO A CB    1 
ATOM   11758 C  CG    . PRO A 1 3018 ? 151.885 186.322 186.675 1.00 36.48  ? 3018 PRO A CG    1 
ATOM   11759 C  CD    . PRO A 1 3018 ? 151.951 185.383 187.845 1.00 36.54  ? 3018 PRO A CD    1 
ATOM   11760 N  N     . GLY A 1 3019 ? 148.674 185.231 186.437 1.00 33.51  ? 3019 GLY A N     1 
ATOM   11761 C  CA    . GLY A 1 3019 ? 147.547 184.814 185.631 1.00 35.22  ? 3019 GLY A CA    1 
ATOM   11762 C  C     . GLY A 1 3019 ? 146.699 183.699 186.205 1.00 41.97  ? 3019 GLY A C     1 
ATOM   11763 O  O     . GLY A 1 3019 ? 145.826 183.184 185.497 1.00 43.25  ? 3019 GLY A O     1 
ATOM   11764 N  N     . LEU A 1 3020 ? 146.923 183.305 187.460 1.00 34.19  ? 3020 LEU A N     1 
ATOM   11765 C  CA    . LEU A 1 3020 ? 146.168 182.194 188.031 1.00 33.02  ? 3020 LEU A CA    1 
ATOM   11766 C  C     . LEU A 1 3020 ? 144.704 182.564 188.233 1.00 37.67  ? 3020 LEU A C     1 
ATOM   11767 O  O     . LEU A 1 3020 ? 143.803 181.784 187.903 1.00 35.02  ? 3020 LEU A O     1 
ATOM   11768 C  CB    . LEU A 1 3020 ? 146.800 181.754 189.350 1.00 28.54  ? 3020 LEU A CB    1 
ATOM   11769 C  CG    . LEU A 1 3020 ? 146.415 180.360 189.843 1.00 28.96  ? 3020 LEU A CG    1 
ATOM   11770 C  CD1   . LEU A 1 3020 ? 146.971 179.296 188.919 1.00 31.80  ? 3020 LEU A CD1   1 
ATOM   11771 C  CD2   . LEU A 1 3020 ? 146.899 180.141 191.264 1.00 22.19  ? 3020 LEU A CD2   1 
ATOM   11772 N  N     . PHE A 1 3021 ? 144.447 183.749 188.775 1.00 38.62  ? 3021 PHE A N     1 
ATOM   11773 C  CA    . PHE A 1 3021 ? 143.090 184.220 189.036 1.00 36.93  ? 3021 PHE A CA    1 
ATOM   11774 C  C     . PHE A 1 3021 ? 142.729 185.242 187.964 1.00 48.99  ? 3021 PHE A C     1 
ATOM   11775 O  O     . PHE A 1 3021 ? 143.110 186.412 188.053 1.00 47.94  ? 3021 PHE A O     1 
ATOM   11776 C  CB    . PHE A 1 3021 ? 142.982 184.816 190.434 1.00 34.83  ? 3021 PHE A CB    1 
ATOM   11777 C  CG    . PHE A 1 3021 ? 143.321 183.852 191.534 1.00 34.70  ? 3021 PHE A CG    1 
ATOM   11778 C  CD1   . PHE A 1 3021 ? 144.628 183.700 191.962 1.00 29.82  ? 3021 PHE A CD1   1 
ATOM   11779 C  CD2   . PHE A 1 3021 ? 142.331 183.106 192.148 1.00 36.83  ? 3021 PHE A CD2   1 
ATOM   11780 C  CE1   . PHE A 1 3021 ? 144.941 182.819 192.976 1.00 27.02  ? 3021 PHE A CE1   1 
ATOM   11781 C  CE2   . PHE A 1 3021 ? 142.639 182.223 193.164 1.00 34.61  ? 3021 PHE A CE2   1 
ATOM   11782 C  CZ    . PHE A 1 3021 ? 143.946 182.081 193.578 1.00 29.30  ? 3021 PHE A CZ    1 
ATOM   11783 N  N     . GLU A 1 3022 ? 141.995 184.798 186.947 1.00 52.23  ? 3022 GLU A N     1 
ATOM   11784 C  CA    . GLU A 1 3022 ? 141.551 185.674 185.873 1.00 54.20  ? 3022 GLU A CA    1 
ATOM   11785 C  C     . GLU A 1 3022 ? 140.107 185.349 185.528 1.00 52.72  ? 3022 GLU A C     1 
ATOM   11786 O  O     . GLU A 1 3022 ? 139.759 184.179 185.348 1.00 47.82  ? 3022 GLU A O     1 
ATOM   11787 C  CB    . GLU A 1 3022 ? 142.442 185.531 184.633 1.00 54.63  ? 3022 GLU A CB    1 
ATOM   11788 C  CG    . GLU A 1 3022 ? 142.061 186.452 183.483 1.00 68.71  ? 3022 GLU A CG    1 
ATOM   11789 C  CD    . GLU A 1 3022 ? 142.248 187.920 183.817 1.00 69.52  ? 3022 GLU A CD    1 
ATOM   11790 O  OE1   . GLU A 1 3022 ? 143.089 188.235 184.684 1.00 77.75  ? 3022 GLU A OE1   1 
ATOM   11791 O  OE2   . GLU A 1 3022 ? 141.550 188.760 183.212 1.00 70.05  ? 3022 GLU A OE2   1 
ATOM   11792 N  N     . GLY A 1 3023 ? 139.276 186.383 185.434 1.00 51.49  ? 3023 GLY A N     1 
ATOM   11793 C  CA    . GLY A 1 3023 ? 137.871 186.204 185.125 1.00 48.31  ? 3023 GLY A CA    1 
ATOM   11794 C  C     . GLY A 1 3023 ? 136.991 186.229 186.356 1.00 43.70  ? 3023 GLY A C     1 
ATOM   11795 O  O     . GLY A 1 3023 ? 137.229 187.012 187.280 1.00 42.51  ? 3023 GLY A O     1 
ATOM   11796 N  N     . ASP A 1 3024 ? 135.961 185.379 186.377 1.00 52.11  ? 3024 ASP A N     1 
ATOM   11797 C  CA    . ASP A 1 3024 ? 135.111 185.274 187.559 1.00 54.66  ? 3024 ASP A CA    1 
ATOM   11798 C  C     . ASP A 1 3024 ? 135.896 184.772 188.761 1.00 48.92  ? 3024 ASP A C     1 
ATOM   11799 O  O     . ASP A 1 3024 ? 135.554 185.092 189.907 1.00 48.06  ? 3024 ASP A O     1 
ATOM   11800 C  CB    . ASP A 1 3024 ? 133.928 184.351 187.274 1.00 59.99  ? 3024 ASP A CB    1 
ATOM   11801 C  CG    . ASP A 1 3024 ? 134.335 183.095 186.530 1.00 63.90  ? 3024 ASP A CG    1 
ATOM   11802 O  OD1   . ASP A 1 3024 ? 135.506 183.009 186.104 1.00 60.02  ? 3024 ASP A OD1   1 
ATOM   11803 O  OD2   . ASP A 1 3024 ? 133.486 182.193 186.372 1.00 73.16  ? 3024 ASP A OD2   1 
ATOM   11804 N  N     . GLU A 1 3025 ? 136.946 183.984 188.518 1.00 47.63  ? 3025 GLU A N     1 
ATOM   11805 C  CA    . GLU A 1 3025 ? 137.794 183.518 189.608 1.00 47.84  ? 3025 GLU A CA    1 
ATOM   11806 C  C     . GLU A 1 3025 ? 138.461 184.685 190.323 1.00 43.98  ? 3025 GLU A C     1 
ATOM   11807 O  O     . GLU A 1 3025 ? 138.570 184.684 191.553 1.00 45.78  ? 3025 GLU A O     1 
ATOM   11808 C  CB    . GLU A 1 3025 ? 138.843 182.540 189.077 1.00 50.35  ? 3025 GLU A CB    1 
ATOM   11809 C  CG    . GLU A 1 3025 ? 138.265 181.321 188.375 1.00 51.15  ? 3025 GLU A CG    1 
ATOM   11810 C  CD    . GLU A 1 3025 ? 137.750 180.273 189.345 1.00 59.65  ? 3025 GLU A CD    1 
ATOM   11811 O  OE1   . GLU A 1 3025 ? 137.986 180.417 190.564 1.00 57.63  ? 3025 GLU A OE1   1 
ATOM   11812 O  OE2   . GLU A 1 3025 ? 137.109 179.303 188.889 1.00 49.88  ? 3025 GLU A OE2   1 
ATOM   11813 N  N     . TYR A 1 3026 ? 138.917 185.690 189.570 1.00 38.77  ? 3026 TYR A N     1 
ATOM   11814 C  CA    . TYR A 1 3026 ? 139.537 186.853 190.200 1.00 36.79  ? 3026 TYR A CA    1 
ATOM   11815 C  C     . TYR A 1 3026 ? 138.536 187.618 191.056 1.00 39.90  ? 3026 TYR A C     1 
ATOM   11816 O  O     . TYR A 1 3026 ? 138.877 188.093 192.144 1.00 38.75  ? 3026 TYR A O     1 
ATOM   11817 C  CB    . TYR A 1 3026 ? 140.146 187.772 189.143 1.00 36.14  ? 3026 TYR A CB    1 
ATOM   11818 C  CG    . TYR A 1 3026 ? 141.011 188.865 189.732 1.00 32.78  ? 3026 TYR A CG    1 
ATOM   11819 C  CD1   . TYR A 1 3026 ? 142.186 188.557 190.404 1.00 33.16  ? 3026 TYR A CD1   1 
ATOM   11820 C  CD2   . TYR A 1 3026 ? 140.648 190.201 189.626 1.00 35.47  ? 3026 TYR A CD2   1 
ATOM   11821 C  CE1   . TYR A 1 3026 ? 142.979 189.547 190.948 1.00 31.96  ? 3026 TYR A CE1   1 
ATOM   11822 C  CE2   . TYR A 1 3026 ? 141.436 191.199 190.169 1.00 35.56  ? 3026 TYR A CE2   1 
ATOM   11823 C  CZ    . TYR A 1 3026 ? 142.600 190.865 190.829 1.00 34.11  ? 3026 TYR A CZ    1 
ATOM   11824 O  OH    . TYR A 1 3026 ? 143.390 191.851 191.371 1.00 38.99  ? 3026 TYR A OH    1 
ATOM   11825 N  N     . ALA A 1 3027 ? 137.297 187.758 190.578 1.00 42.80  ? 3027 ALA A N     1 
ATOM   11826 C  CA    . ALA A 1 3027 ? 136.276 188.444 191.365 1.00 38.36  ? 3027 ALA A CA    1 
ATOM   11827 C  C     . ALA A 1 3027 ? 135.949 187.677 192.642 1.00 38.29  ? 3027 ALA A C     1 
ATOM   11828 O  O     . ALA A 1 3027 ? 135.805 188.275 193.716 1.00 45.09  ? 3027 ALA A O     1 
ATOM   11829 C  CB    . ALA A 1 3027 ? 135.018 188.652 190.523 1.00 42.39  ? 3027 ALA A CB    1 
ATOM   11830 N  N     . THR A 1 3028 ? 135.828 186.351 192.545 1.00 37.00  ? 3028 THR A N     1 
ATOM   11831 C  CA    . THR A 1 3028 ? 135.590 185.542 193.738 1.00 39.94  ? 3028 THR A CA    1 
ATOM   11832 C  C     . THR A 1 3028 ? 136.755 185.650 194.715 1.00 42.25  ? 3028 THR A C     1 
ATOM   11833 O  O     . THR A 1 3028 ? 136.554 185.738 195.935 1.00 43.67  ? 3028 THR A O     1 
ATOM   11834 C  CB    . THR A 1 3028 ? 135.351 184.085 193.342 1.00 40.52  ? 3028 THR A CB    1 
ATOM   11835 O  OG1   . THR A 1 3028 ? 134.207 184.002 192.483 1.00 40.82  ? 3028 THR A OG1   1 
ATOM   11836 C  CG2   . THR A 1 3028 ? 135.107 183.228 194.575 1.00 44.75  ? 3028 THR A CG2   1 
ATOM   11837 N  N     . LEU A 1 3029 ? 137.984 185.643 194.192 1.00 40.31  ? 3029 LEU A N     1 
ATOM   11838 C  CA    . LEU A 1 3029 ? 139.161 185.797 195.038 1.00 41.65  ? 3029 LEU A CA    1 
ATOM   11839 C  C     . LEU A 1 3029 ? 139.165 187.150 195.732 1.00 42.02  ? 3029 LEU A C     1 
ATOM   11840 O  O     . LEU A 1 3029 ? 139.502 187.244 196.914 1.00 45.33  ? 3029 LEU A O     1 
ATOM   11841 C  CB    . LEU A 1 3029 ? 140.431 185.618 194.206 1.00 39.61  ? 3029 LEU A CB    1 
ATOM   11842 C  CG    . LEU A 1 3029 ? 141.757 185.959 194.892 1.00 33.87  ? 3029 LEU A CG    1 
ATOM   11843 C  CD1   . LEU A 1 3029 ? 142.197 184.831 195.810 1.00 31.31  ? 3029 LEU A CD1   1 
ATOM   11844 C  CD2   . LEU A 1 3029 ? 142.835 186.281 193.872 1.00 28.93  ? 3029 LEU A CD2   1 
ATOM   11845 N  N     . MET A 1 3030 ? 138.795 188.211 195.011 1.00 41.41  ? 3030 MET A N     1 
ATOM   11846 C  CA    . MET A 1 3030 ? 138.722 189.535 195.621 1.00 40.26  ? 3030 MET A CA    1 
ATOM   11847 C  C     . MET A 1 3030 ? 137.667 189.577 196.718 1.00 37.87  ? 3030 MET A C     1 
ATOM   11848 O  O     . MET A 1 3030 ? 137.886 190.174 197.778 1.00 42.11  ? 3030 MET A O     1 
ATOM   11849 C  CB    . MET A 1 3030 ? 138.430 190.589 194.553 1.00 40.14  ? 3030 MET A CB    1 
ATOM   11850 C  CG    . MET A 1 3030 ? 139.639 191.072 193.749 1.00 37.55  ? 3030 MET A CG    1 
ATOM   11851 S  SD    . MET A 1 3030 ? 141.149 191.361 194.697 1.00 50.27  ? 3030 MET A SD    1 
ATOM   11852 C  CE    . MET A 1 3030 ? 142.016 189.804 194.500 1.00 40.51  ? 3030 MET A CE    1 
ATOM   11853 N  N     . THR A 1 3031 ? 136.516 188.944 196.482 1.00 38.66  ? 3031 THR A N     1 
ATOM   11854 C  CA    . THR A 1 3031 ? 135.471 188.904 197.502 1.00 43.30  ? 3031 THR A CA    1 
ATOM   11855 C  C     . THR A 1 3031 ? 135.963 188.200 198.762 1.00 41.68  ? 3031 THR A C     1 
ATOM   11856 O  O     . THR A 1 3031 ? 135.817 188.716 199.879 1.00 41.23  ? 3031 THR A O     1 
ATOM   11857 C  CB    . THR A 1 3031 ? 134.229 188.209 196.947 1.00 43.51  ? 3031 THR A CB    1 
ATOM   11858 O  OG1   . THR A 1 3031 ? 133.943 188.710 195.636 1.00 42.62  ? 3031 THR A OG1   1 
ATOM   11859 C  CG2   . THR A 1 3031 ? 133.032 188.457 197.850 1.00 40.45  ? 3031 THR A CG2   1 
ATOM   11860 N  N     . GLN A 1 3032 ? 136.563 187.018 198.597 1.00 42.68  ? 3032 GLN A N     1 
ATOM   11861 C  CA    . GLN A 1 3032 ? 137.059 186.287 199.758 1.00 39.97  ? 3032 GLN A CA    1 
ATOM   11862 C  C     . GLN A 1 3032 ? 138.201 187.024 200.446 1.00 40.72  ? 3032 GLN A C     1 
ATOM   11863 O  O     . GLN A 1 3032 ? 138.321 186.966 201.673 1.00 41.81  ? 3032 GLN A O     1 
ATOM   11864 C  CB    . GLN A 1 3032 ? 137.505 184.882 199.362 1.00 41.21  ? 3032 GLN A CB    1 
ATOM   11865 C  CG    . GLN A 1 3032 ? 136.382 183.973 198.905 1.00 49.47  ? 3032 GLN A CG    1 
ATOM   11866 C  CD    . GLN A 1 3032 ? 136.885 182.602 198.513 1.00 59.86  ? 3032 GLN A CD    1 
ATOM   11867 O  OE1   . GLN A 1 3032 ? 138.088 182.350 198.520 1.00 58.19  ? 3032 GLN A OE1   1 
ATOM   11868 N  NE2   . GLN A 1 3032 ? 135.967 181.706 198.174 1.00 63.29  ? 3032 GLN A NE2   1 
ATOM   11869 N  N     . CYS A 1 3033 ? 139.049 187.715 199.682 1.00 39.24  ? 3033 CYS A N     1 
ATOM   11870 C  CA    . CYS A 1 3033 ? 140.138 188.477 200.281 1.00 40.50  ? 3033 CYS A CA    1 
ATOM   11871 C  C     . CYS A 1 3033 ? 139.608 189.644 201.101 1.00 40.29  ? 3033 CYS A C     1 
ATOM   11872 O  O     . CYS A 1 3033 ? 140.134 189.939 202.180 1.00 42.43  ? 3033 CYS A O     1 
ATOM   11873 C  CB    . CYS A 1 3033 ? 141.091 188.974 199.195 1.00 46.27  ? 3033 CYS A CB    1 
ATOM   11874 S  SG    . CYS A 1 3033 ? 142.144 187.702 198.472 1.00 65.58  ? 3033 CYS A SG    1 
ATOM   11875 N  N     . LYS A 1 3034 ? 138.580 190.330 200.599 1.00 40.23  ? 3034 LYS A N     1 
ATOM   11876 C  CA    . LYS A 1 3034 ? 137.961 191.396 201.378 1.00 42.79  ? 3034 LYS A CA    1 
ATOM   11877 C  C     . LYS A 1 3034 ? 137.343 190.845 202.655 1.00 50.55  ? 3034 LYS A C     1 
ATOM   11878 O  O     . LYS A 1 3034 ? 137.468 191.451 203.727 1.00 48.29  ? 3034 LYS A O     1 
ATOM   11879 C  CB    . LYS A 1 3034 ? 136.909 192.121 200.542 1.00 43.47  ? 3034 LYS A CB    1 
ATOM   11880 C  CG    . LYS A 1 3034 ? 136.635 193.544 200.998 1.00 42.77  ? 3034 LYS A CG    1 
ATOM   11881 C  CD    . LYS A 1 3034 ? 135.309 194.055 200.460 1.00 38.91  ? 3034 LYS A CD    1 
ATOM   11882 C  CE    . LYS A 1 3034 ? 134.948 195.399 201.068 1.00 44.20  ? 3034 LYS A CE    1 
ATOM   11883 N  NZ    . LYS A 1 3034 ? 135.797 196.494 200.519 1.00 50.09  ? 3034 LYS A NZ    1 
ATOM   11884 N  N     . GLU A 1 3035 ? 136.679 189.689 202.562 1.00 46.78  ? 3035 GLU A N     1 
ATOM   11885 C  CA    . GLU A 1 3035 ? 136.120 189.070 203.760 1.00 49.90  ? 3035 GLU A CA    1 
ATOM   11886 C  C     . GLU A 1 3035 ? 137.214 188.717 204.764 1.00 53.40  ? 3035 GLU A C     1 
ATOM   11887 O  O     . GLU A 1 3035 ? 137.066 188.958 205.969 1.00 59.17  ? 3035 GLU A O     1 
ATOM   11888 C  CB    . GLU A 1 3035 ? 135.316 187.827 203.379 1.00 52.30  ? 3035 GLU A CB    1 
ATOM   11889 C  CG    . GLU A 1 3035 ? 134.655 187.130 204.554 1.00 64.41  ? 3035 GLU A CG    1 
ATOM   11890 C  CD    . GLU A 1 3035 ? 133.590 187.985 205.217 1.00 75.36  ? 3035 GLU A CD    1 
ATOM   11891 O  OE1   . GLU A 1 3035 ? 133.016 188.863 204.540 1.00 73.60  ? 3035 GLU A OE1   1 
ATOM   11892 O  OE2   . GLU A 1 3035 ? 133.328 187.778 206.420 1.00 76.56  ? 3035 GLU A OE2   1 
ATOM   11893 N  N     . GLY A 1 3036 ? 138.325 188.155 204.285 1.00 44.61  ? 3036 GLY A N     1 
ATOM   11894 C  CA    . GLY A 1 3036 ? 139.411 187.797 205.181 1.00 44.69  ? 3036 GLY A CA    1 
ATOM   11895 C  C     . GLY A 1 3036 ? 140.072 189.004 205.819 1.00 49.71  ? 3036 GLY A C     1 
ATOM   11896 O  O     . GLY A 1 3036 ? 140.439 188.970 206.997 1.00 48.47  ? 3036 GLY A O     1 
ATOM   11897 N  N     . ALA A 1 3037 ? 140.247 190.080 205.050 1.00 49.89  ? 3037 ALA A N     1 
ATOM   11898 C  CA    . ALA A 1 3037 ? 140.814 191.304 205.605 1.00 51.04  ? 3037 ALA A CA    1 
ATOM   11899 C  C     . ALA A 1 3037 ? 139.887 191.914 206.647 1.00 60.00  ? 3037 ALA A C     1 
ATOM   11900 O  O     . ALA A 1 3037 ? 140.347 192.429 207.673 1.00 61.41  ? 3037 ALA A O     1 
ATOM   11901 C  CB    . ALA A 1 3037 ? 141.107 192.304 204.487 1.00 51.35  ? 3037 ALA A CB    1 
ATOM   11902 N  N     . GLN A 1 3038 ? 138.575 191.871 206.399 1.00 61.13  ? 3038 GLN A N     1 
ATOM   11903 C  CA    . GLN A 1 3038 ? 137.622 192.328 207.406 1.00 62.97  ? 3038 GLN A CA    1 
ATOM   11904 C  C     . GLN A 1 3038 ? 137.714 191.479 208.667 1.00 62.74  ? 3038 GLN A C     1 
ATOM   11905 O  O     . GLN A 1 3038 ? 137.635 192.002 209.784 1.00 66.41  ? 3038 GLN A O     1 
ATOM   11906 C  CB    . GLN A 1 3038 ? 136.203 192.296 206.838 1.00 66.01  ? 3038 GLN A CB    1 
ATOM   11907 C  CG    . GLN A 1 3038 ? 135.803 193.553 206.087 1.00 71.83  ? 3038 GLN A CG    1 
ATOM   11908 C  CD    . GLN A 1 3038 ? 134.545 193.359 205.264 1.00 73.52  ? 3038 GLN A CD    1 
ATOM   11909 O  OE1   . GLN A 1 3038 ? 133.771 192.431 205.502 1.00 73.00  ? 3038 GLN A OE1   1 
ATOM   11910 N  NE2   . GLN A 1 3038 ? 134.333 194.236 204.289 1.00 66.18  ? 3038 GLN A NE2   1 
ATOM   11911 N  N     . LYS A 1 3039 ? 137.874 190.163 208.504 1.00 59.73  ? 3039 LYS A N     1 
ATOM   11912 C  CA    . LYS A 1 3039 ? 138.060 189.287 209.657 1.00 56.82  ? 3039 LYS A CA    1 
ATOM   11913 C  C     . LYS A 1 3039 ? 139.320 189.652 210.432 1.00 59.66  ? 3039 LYS A C     1 
ATOM   11914 O  O     . LYS A 1 3039 ? 139.312 189.683 211.669 1.00 60.97  ? 3039 LYS A O     1 
ATOM   11915 C  CB    . LYS A 1 3039 ? 138.118 187.830 209.199 1.00 52.84  ? 3039 LYS A CB    1 
ATOM   11916 C  CG    . LYS A 1 3039 ? 138.308 186.827 210.322 1.00 50.99  ? 3039 LYS A CG    1 
ATOM   11917 C  CD    . LYS A 1 3039 ? 137.368 185.643 210.172 1.00 54.68  ? 3039 LYS A CD    1 
ATOM   11918 C  CE    . LYS A 1 3039 ? 137.562 184.640 211.298 1.00 57.12  ? 3039 LYS A CE    1 
ATOM   11919 N  NZ    . LYS A 1 3039 ? 136.547 183.552 211.255 1.00 54.55  ? 3039 LYS A NZ    1 
ATOM   11920 N  N     . GLU A 1 3040 ? 140.415 189.932 209.722 1.00 65.71  ? 3040 GLU A N     1 
ATOM   11921 C  CA    . GLU A 1 3040 ? 141.667 190.284 210.383 1.00 62.10  ? 3040 GLU A CA    1 
ATOM   11922 C  C     . GLU A 1 3040 ? 141.574 191.635 211.083 1.00 66.92  ? 3040 GLU A C     1 
ATOM   11923 O  O     . GLU A 1 3040 ? 142.242 191.854 212.099 1.00 70.80  ? 3040 GLU A O     1 
ATOM   11924 C  CB    . GLU A 1 3040 ? 142.808 190.286 209.364 1.00 58.76  ? 3040 GLU A CB    1 
ATOM   11925 C  CG    . GLU A 1 3040 ? 144.155 190.733 209.914 1.00 60.80  ? 3040 GLU A CG    1 
ATOM   11926 C  CD    . GLU A 1 3040 ? 145.307 190.390 208.989 1.00 63.29  ? 3040 GLU A CD    1 
ATOM   11927 O  OE1   . GLU A 1 3040 ? 145.390 189.226 208.544 1.00 50.34  ? 3040 GLU A OE1   1 
ATOM   11928 O  OE2   . GLU A 1 3040 ? 146.131 191.285 208.708 1.00 62.52  ? 3040 GLU A OE2   1 
ATOM   11929 N  N     . GLY A 1 3041 ? 140.746 192.540 210.570 1.00 64.09  ? 3041 GLY A N     1 
ATOM   11930 C  CA    . GLY A 1 3041 ? 140.621 193.871 211.122 1.00 61.48  ? 3041 GLY A CA    1 
ATOM   11931 C  C     . GLY A 1 3041 ? 141.140 194.989 210.244 1.00 65.14  ? 3041 GLY A C     1 
ATOM   11932 O  O     . GLY A 1 3041 ? 141.316 196.108 210.739 1.00 69.84  ? 3041 GLY A O     1 
ATOM   11933 N  N     . LEU A 1 3042 ? 141.392 194.727 208.965 1.00 65.35  ? 3042 LEU A N     1 
ATOM   11934 C  CA    . LEU A 1 3042 ? 141.908 195.723 208.036 1.00 64.97  ? 3042 LEU A CA    1 
ATOM   11935 C  C     . LEU A 1 3042 ? 140.842 196.046 207.000 1.00 68.45  ? 3042 LEU A C     1 
ATOM   11936 O  O     . LEU A 1 3042 ? 140.302 195.140 206.356 1.00 68.09  ? 3042 LEU A O     1 
ATOM   11937 C  CB    . LEU A 1 3042 ? 143.179 195.223 207.348 1.00 61.27  ? 3042 LEU A CB    1 
ATOM   11938 C  CG    . LEU A 1 3042 ? 144.294 194.732 208.270 1.00 66.00  ? 3042 LEU A CG    1 
ATOM   11939 C  CD1   . LEU A 1 3042 ? 145.510 194.303 207.463 1.00 55.83  ? 3042 LEU A CD1   1 
ATOM   11940 C  CD2   . LEU A 1 3042 ? 144.667 195.804 209.282 1.00 67.60  ? 3042 LEU A CD2   1 
ATOM   11941 N  N     . MET A 1 3043 ? 140.545 197.332 206.841 1.00 71.41  ? 3043 MET A N     1 
ATOM   11942 C  CA    . MET A 1 3043 ? 139.548 197.797 205.881 1.00 69.52  ? 3043 MET A CA    1 
ATOM   11943 C  C     . MET A 1 3043 ? 140.279 198.218 204.612 1.00 67.86  ? 3043 MET A C     1 
ATOM   11944 O  O     . MET A 1 3043 ? 140.894 199.286 204.560 1.00 65.12  ? 3043 MET A O     1 
ATOM   11945 C  CB    . MET A 1 3043 ? 138.724 198.941 206.462 1.00 75.40  ? 3043 MET A CB    1 
ATOM   11946 C  CG    . MET A 1 3043 ? 137.781 198.517 207.574 1.00 83.92  ? 3043 MET A CG    1 
ATOM   11947 S  SD    . MET A 1 3043 ? 136.696 197.166 207.076 1.00 97.46  ? 3043 MET A SD    1 
ATOM   11948 C  CE    . MET A 1 3043 ? 135.597 198.015 205.945 1.00 86.18  ? 3043 MET A CE    1 
ATOM   11949 N  N     . LEU A 1 3044 ? 140.213 197.372 203.589 1.00 61.63  ? 3044 LEU A N     1 
ATOM   11950 C  CA    . LEU A 1 3044 ? 140.859 197.625 202.311 1.00 61.44  ? 3044 LEU A CA    1 
ATOM   11951 C  C     . LEU A 1 3044 ? 139.796 197.747 201.228 1.00 63.50  ? 3044 LEU A C     1 
ATOM   11952 O  O     . LEU A 1 3044 ? 138.853 196.952 201.180 1.00 58.40  ? 3044 LEU A O     1 
ATOM   11953 C  CB    . LEU A 1 3044 ? 141.846 196.507 201.968 1.00 56.28  ? 3044 LEU A CB    1 
ATOM   11954 C  CG    . LEU A 1 3044 ? 143.077 196.423 202.874 1.00 53.73  ? 3044 LEU A CG    1 
ATOM   11955 C  CD1   . LEU A 1 3044 ? 143.511 194.977 203.051 1.00 56.62  ? 3044 LEU A CD1   1 
ATOM   11956 C  CD2   . LEU A 1 3044 ? 144.222 197.274 202.347 1.00 50.07  ? 3044 LEU A CD2   1 
ATOM   11957 N  N     . ASP A 1 3045 ? 139.946 198.750 200.362 1.00 67.28  ? 3045 ASP A N     1 
ATOM   11958 C  CA    . ASP A 1 3045 ? 138.928 199.073 199.369 1.00 68.52  ? 3045 ASP A CA    1 
ATOM   11959 C  C     . ASP A 1 3045 ? 139.330 198.679 197.952 1.00 64.10  ? 3045 ASP A C     1 
ATOM   11960 O  O     . ASP A 1 3045 ? 138.567 197.992 197.266 1.00 57.17  ? 3045 ASP A O     1 
ATOM   11961 C  CB    . ASP A 1 3045 ? 138.579 200.570 199.447 1.00 68.42  ? 3045 ASP A CB    1 
ATOM   11962 C  CG    . ASP A 1 3045 ? 139.758 201.476 199.124 1.00 75.80  ? 3045 ASP A CG    1 
ATOM   11963 O  OD1   . ASP A 1 3045 ? 140.869 200.964 198.876 1.00 76.86  ? 3045 ASP A OD1   1 
ATOM   11964 O  OD2   . ASP A 1 3045 ? 139.567 202.709 199.114 1.00 76.69  ? 3045 ASP A OD2   1 
ATOM   11965 N  N     . SER A 1 3046 ? 140.507 199.089 197.490 1.00 65.14  ? 3046 SER A N     1 
ATOM   11966 C  CA    . SER A 1 3046 ? 140.883 198.842 196.108 1.00 57.50  ? 3046 SER A CA    1 
ATOM   11967 C  C     . SER A 1 3046 ? 141.398 197.417 195.932 1.00 54.56  ? 3046 SER A C     1 
ATOM   11968 O  O     . SER A 1 3046 ? 141.788 196.741 196.888 1.00 59.22  ? 3046 SER A O     1 
ATOM   11969 C  CB    . SER A 1 3046 ? 141.939 199.845 195.643 1.00 60.43  ? 3046 SER A CB    1 
ATOM   11970 O  OG    . SER A 1 3046 ? 143.146 199.698 196.366 1.00 59.63  ? 3046 SER A OG    1 
ATOM   11971 N  N     . HIS A 1 3047 ? 141.388 196.961 194.678 1.00 52.52  ? 3047 HIS A N     1 
ATOM   11972 C  CA    . HIS A 1 3047 ? 141.804 195.596 194.384 1.00 44.25  ? 3047 HIS A CA    1 
ATOM   11973 C  C     . HIS A 1 3047 ? 143.318 195.435 194.452 1.00 49.51  ? 3047 HIS A C     1 
ATOM   11974 O  O     . HIS A 1 3047 ? 143.806 194.335 194.728 1.00 51.84  ? 3047 HIS A O     1 
ATOM   11975 C  CB    . HIS A 1 3047 ? 141.284 195.174 193.010 1.00 44.37  ? 3047 HIS A CB    1 
ATOM   11976 C  CG    . HIS A 1 3047 ? 139.825 194.841 192.992 1.00 49.28  ? 3047 HIS A CG    1 
ATOM   11977 N  ND1   . HIS A 1 3047 ? 139.162 194.460 191.846 1.00 46.00  ? 3047 HIS A ND1   1 
ATOM   11978 C  CD2   . HIS A 1 3047 ? 138.900 194.830 193.982 1.00 48.99  ? 3047 HIS A CD2   1 
ATOM   11979 C  CE1   . HIS A 1 3047 ? 137.893 194.227 192.129 1.00 47.93  ? 3047 HIS A CE1   1 
ATOM   11980 N  NE2   . HIS A 1 3047 ? 137.707 194.445 193.418 1.00 47.32  ? 3047 HIS A NE2   1 
ATOM   11981 N  N     . GLU A 1 3048 ? 144.075 196.506 194.203 1.00 54.67  ? 3048 GLU A N     1 
ATOM   11982 C  CA    . GLU A 1 3048 ? 145.532 196.402 194.227 1.00 49.19  ? 3048 GLU A CA    1 
ATOM   11983 C  C     . GLU A 1 3048 ? 146.048 196.130 195.637 1.00 46.84  ? 3048 GLU A C     1 
ATOM   11984 O  O     . GLU A 1 3048 ? 146.828 195.195 195.855 1.00 45.68  ? 3048 GLU A O     1 
ATOM   11985 C  CB    . GLU A 1 3048 ? 146.157 197.677 193.660 1.00 53.14  ? 3048 GLU A CB    1 
ATOM   11986 C  CG    . GLU A 1 3048 ? 145.899 197.894 192.176 1.00 63.54  ? 3048 GLU A CG    1 
ATOM   11987 C  CD    . GLU A 1 3048 ? 144.550 198.529 191.902 1.00 75.06  ? 3048 GLU A CD    1 
ATOM   11988 O  OE1   . GLU A 1 3048 ? 143.837 198.861 192.871 1.00 65.79  ? 3048 GLU A OE1   1 
ATOM   11989 O  OE2   . GLU A 1 3048 ? 144.199 198.692 190.715 1.00 90.46  ? 3048 GLU A OE2   1 
ATOM   11990 N  N     . GLU A 1 3049 ? 145.613 196.931 196.613 1.00 47.67  ? 3049 GLU A N     1 
ATOM   11991 C  CA    . GLU A 1 3049 ? 146.070 196.730 197.985 1.00 46.98  ? 3049 GLU A CA    1 
ATOM   11992 C  C     . GLU A 1 3049 ? 145.530 195.426 198.558 1.00 43.19  ? 3049 GLU A C     1 
ATOM   11993 O  O     . GLU A 1 3049 ? 146.209 194.754 199.344 1.00 38.85  ? 3049 GLU A O     1 
ATOM   11994 C  CB    . GLU A 1 3049 ? 145.659 197.917 198.858 1.00 46.73  ? 3049 GLU A CB    1 
ATOM   11995 C  CG    . GLU A 1 3049 ? 144.161 198.173 198.898 1.00 55.62  ? 3049 GLU A CG    1 
ATOM   11996 C  CD    . GLU A 1 3049 ? 143.811 199.525 199.491 1.00 65.45  ? 3049 GLU A CD    1 
ATOM   11997 O  OE1   . GLU A 1 3049 ? 142.943 199.575 200.389 1.00 66.90  ? 3049 GLU A OE1   1 
ATOM   11998 O  OE2   . GLU A 1 3049 ? 144.401 200.537 199.060 1.00 71.02  ? 3049 GLU A OE2   1 
ATOM   11999 N  N     . LEU A 1 3050 ? 144.308 195.054 198.175 1.00 39.89  ? 3050 LEU A N     1 
ATOM   12000 C  CA    . LEU A 1 3050 ? 143.740 193.791 198.628 1.00 41.49  ? 3050 LEU A CA    1 
ATOM   12001 C  C     . LEU A 1 3050 ? 144.529 192.609 198.074 1.00 35.41  ? 3050 LEU A C     1 
ATOM   12002 O  O     . LEU A 1 3050 ? 144.778 191.627 198.784 1.00 35.79  ? 3050 LEU A O     1 
ATOM   12003 C  CB    . LEU A 1 3050 ? 142.272 193.717 198.212 1.00 44.88  ? 3050 LEU A CB    1 
ATOM   12004 C  CG    . LEU A 1 3050 ? 141.448 192.509 198.641 1.00 45.39  ? 3050 LEU A CG    1 
ATOM   12005 C  CD1   . LEU A 1 3050 ? 141.363 192.458 200.155 1.00 43.95  ? 3050 LEU A CD1   1 
ATOM   12006 C  CD2   . LEU A 1 3050 ? 140.064 192.581 198.025 1.00 43.94  ? 3050 LEU A CD2   1 
ATOM   12007 N  N     . TYR A 1 3051 ? 144.944 192.694 196.808 1.00 35.62  ? 3051 TYR A N     1 
ATOM   12008 C  CA    . TYR A 1 3051 ? 145.780 191.651 196.224 1.00 32.71  ? 3051 TYR A CA    1 
ATOM   12009 C  C     . TYR A 1 3051 ? 147.151 191.613 196.886 1.00 31.07  ? 3051 TYR A C     1 
ATOM   12010 O  O     . TYR A 1 3051 ? 147.738 190.539 197.050 1.00 33.35  ? 3051 TYR A O     1 
ATOM   12011 C  CB    . TYR A 1 3051 ? 145.912 191.876 194.718 1.00 36.03  ? 3051 TYR A CB    1 
ATOM   12012 C  CG    . TYR A 1 3051 ? 146.679 190.798 193.990 1.00 35.15  ? 3051 TYR A CG    1 
ATOM   12013 C  CD1   . TYR A 1 3051 ? 148.014 190.975 193.652 1.00 35.09  ? 3051 TYR A CD1   1 
ATOM   12014 C  CD2   . TYR A 1 3051 ? 146.063 189.608 193.628 1.00 26.99  ? 3051 TYR A CD2   1 
ATOM   12015 C  CE1   . TYR A 1 3051 ? 148.716 189.992 192.983 1.00 31.97  ? 3051 TYR A CE1   1 
ATOM   12016 C  CE2   . TYR A 1 3051 ? 146.756 188.621 192.960 1.00 29.39  ? 3051 TYR A CE2   1 
ATOM   12017 C  CZ    . TYR A 1 3051 ? 148.081 188.818 192.639 1.00 35.51  ? 3051 TYR A CZ    1 
ATOM   12018 O  OH    . TYR A 1 3051 ? 148.771 187.835 191.971 1.00 42.35  ? 3051 TYR A OH    1 
ATOM   12019 N  N     . LYS A 1 3052 ? 147.679 192.778 197.271 1.00 31.82  ? 3052 LYS A N     1 
ATOM   12020 C  CA    . LYS A 1 3052 ? 148.927 192.804 198.030 1.00 30.03  ? 3052 LYS A CA    1 
ATOM   12021 C  C     . LYS A 1 3052 ? 148.772 192.098 199.372 1.00 28.44  ? 3052 LYS A C     1 
ATOM   12022 O  O     . LYS A 1 3052 ? 149.662 191.352 199.798 1.00 28.82  ? 3052 LYS A O     1 
ATOM   12023 C  CB    . LYS A 1 3052 ? 149.390 194.245 198.236 1.00 31.19  ? 3052 LYS A CB    1 
ATOM   12024 C  CG    . LYS A 1 3052 ? 149.786 194.964 196.962 1.00 34.03  ? 3052 LYS A CG    1 
ATOM   12025 C  CD    . LYS A 1 3052 ? 150.322 196.351 197.262 1.00 38.25  ? 3052 LYS A CD    1 
ATOM   12026 C  CE    . LYS A 1 3052 ? 151.839 196.351 197.318 1.00 41.08  ? 3052 LYS A CE    1 
ATOM   12027 N  NZ    . LYS A 1 3052 ? 152.440 196.687 196.000 1.00 37.77  ? 3052 LYS A NZ    1 
ATOM   12028 N  N     . TRP A 1 3053 ? 147.652 192.333 200.059 1.00 28.68  ? 3053 TRP A N     1 
ATOM   12029 C  CA    . TRP A 1 3053 ? 147.394 191.641 201.319 1.00 26.22  ? 3053 TRP A CA    1 
ATOM   12030 C  C     . TRP A 1 3053 ? 147.273 190.137 201.105 1.00 26.07  ? 3053 TRP A C     1 
ATOM   12031 O  O     . TRP A 1 3053 ? 147.763 189.342 201.916 1.00 30.18  ? 3053 TRP A O     1 
ATOM   12032 C  CB    . TRP A 1 3053 ? 146.129 192.192 201.976 1.00 31.62  ? 3053 TRP A CB    1 
ATOM   12033 C  CG    . TRP A 1 3053 ? 145.749 191.481 203.241 1.00 31.09  ? 3053 TRP A CG    1 
ATOM   12034 C  CD1   . TRP A 1 3053 ? 146.228 191.725 204.494 1.00 30.25  ? 3053 TRP A CD1   1 
ATOM   12035 C  CD2   . TRP A 1 3053 ? 144.810 190.408 203.373 1.00 29.60  ? 3053 TRP A CD2   1 
ATOM   12036 N  NE1   . TRP A 1 3053 ? 145.646 190.872 205.398 1.00 27.27  ? 3053 TRP A NE1   1 
ATOM   12037 C  CE2   . TRP A 1 3053 ? 144.770 190.053 204.735 1.00 30.63  ? 3053 TRP A CE2   1 
ATOM   12038 C  CE3   . TRP A 1 3053 ? 143.998 189.713 202.472 1.00 31.70  ? 3053 TRP A CE3   1 
ATOM   12039 C  CZ2   . TRP A 1 3053 ? 143.952 189.036 205.217 1.00 35.54  ? 3053 TRP A CZ2   1 
ATOM   12040 C  CZ3   . TRP A 1 3053 ? 143.188 188.704 202.953 1.00 35.63  ? 3053 TRP A CZ3   1 
ATOM   12041 C  CH2   . TRP A 1 3053 ? 143.170 188.374 204.312 1.00 37.54  ? 3053 TRP A CH2   1 
ATOM   12042 N  N     . PHE A 1 3054 ? 146.612 189.731 200.019 1.00 26.07  ? 3054 PHE A N     1 
ATOM   12043 C  CA    . PHE A 1 3054 ? 146.515 188.312 199.692 1.00 25.79  ? 3054 PHE A CA    1 
ATOM   12044 C  C     . PHE A 1 3054 ? 147.892 187.704 199.451 1.00 22.48  ? 3054 PHE A C     1 
ATOM   12045 O  O     . PHE A 1 3054 ? 148.183 186.597 199.920 1.00 26.50  ? 3054 PHE A O     1 
ATOM   12046 C  CB    . PHE A 1 3054 ? 145.622 188.126 198.466 1.00 26.22  ? 3054 PHE A CB    1 
ATOM   12047 C  CG    . PHE A 1 3054 ? 145.632 186.733 197.909 1.00 28.11  ? 3054 PHE A CG    1 
ATOM   12048 C  CD1   . PHE A 1 3054 ? 145.035 185.692 198.597 1.00 26.72  ? 3054 PHE A CD1   1 
ATOM   12049 C  CD2   . PHE A 1 3054 ? 146.223 186.467 196.686 1.00 28.34  ? 3054 PHE A CD2   1 
ATOM   12050 C  CE1   . PHE A 1 3054 ? 145.039 184.413 198.083 1.00 22.36  ? 3054 PHE A CE1   1 
ATOM   12051 C  CE2   . PHE A 1 3054 ? 146.229 185.189 196.167 1.00 23.15  ? 3054 PHE A CE2   1 
ATOM   12052 C  CZ    . PHE A 1 3054 ? 145.636 184.161 196.867 1.00 21.87  ? 3054 PHE A CZ    1 
ATOM   12053 N  N     . THR A 1 3055 ? 148.751 188.416 198.720 1.00 25.67  ? 3055 THR A N     1 
ATOM   12054 C  CA    . THR A 1 3055 ? 150.103 187.926 198.469 1.00 25.15  ? 3055 THR A CA    1 
ATOM   12055 C  C     . THR A 1 3055 ? 150.891 187.805 199.766 1.00 21.74  ? 3055 THR A C     1 
ATOM   12056 O  O     . THR A 1 3055 ? 151.615 186.824 199.973 1.00 20.21  ? 3055 THR A O     1 
ATOM   12057 C  CB    . THR A 1 3055 ? 150.822 188.850 197.485 1.00 24.04  ? 3055 THR A CB    1 
ATOM   12058 O  OG1   . THR A 1 3055 ? 150.147 188.822 196.223 1.00 31.18  ? 3055 THR A OG1   1 
ATOM   12059 C  CG2   . THR A 1 3055 ? 152.262 188.407 197.284 1.00 22.00  ? 3055 THR A CG2   1 
ATOM   12060 N  N     . SER A 1 3056 ? 150.761 188.793 200.655 1.00 19.11  ? 3056 SER A N     1 
ATOM   12061 C  CA    . SER A 1 3056 ? 151.452 188.727 201.938 1.00 18.86  ? 3056 SER A CA    1 
ATOM   12062 C  C     . SER A 1 3056 ? 150.966 187.543 202.764 1.00 19.88  ? 3056 SER A C     1 
ATOM   12063 O  O     . SER A 1 3056 ? 151.767 186.849 203.402 1.00 21.47  ? 3056 SER A O     1 
ATOM   12064 C  CB    . SER A 1 3056 ? 151.261 190.034 202.706 1.00 18.33  ? 3056 SER A CB    1 
ATOM   12065 O  OG    . SER A 1 3056 ? 149.929 190.167 203.168 1.00 26.22  ? 3056 SER A OG    1 
ATOM   12066 N  N     . GLN A 1 3057 ? 149.654 187.295 202.762 1.00 22.53  ? 3057 GLN A N     1 
ATOM   12067 C  CA    . GLN A 1 3057 ? 149.114 186.153 203.492 1.00 23.44  ? 3057 GLN A CA    1 
ATOM   12068 C  C     . GLN A 1 3057 ? 149.635 184.837 202.928 1.00 21.80  ? 3057 GLN A C     1 
ATOM   12069 O  O     . GLN A 1 3057 ? 150.015 183.934 203.685 1.00 24.91  ? 3057 GLN A O     1 
ATOM   12070 C  CB    . GLN A 1 3057 ? 147.587 186.185 203.454 1.00 26.47  ? 3057 GLN A CB    1 
ATOM   12071 C  CG    . GLN A 1 3057 ? 146.965 187.215 204.379 1.00 28.23  ? 3057 GLN A CG    1 
ATOM   12072 C  CD    . GLN A 1 3057 ? 147.137 186.860 205.839 1.00 28.35  ? 3057 GLN A CD    1 
ATOM   12073 O  OE1   . GLN A 1 3057 ? 147.962 187.444 206.539 1.00 31.46  ? 3057 GLN A OE1   1 
ATOM   12074 N  NE2   . GLN A 1 3057 ? 146.358 185.894 206.307 1.00 33.11  ? 3057 GLN A NE2   1 
ATOM   12075 N  N     . VAL A 1 3058 ? 149.668 184.711 201.599 1.00 20.15  ? 3058 VAL A N     1 
ATOM   12076 C  CA    . VAL A 1 3058 ? 150.190 183.494 200.982 1.00 19.31  ? 3058 VAL A CA    1 
ATOM   12077 C  C     . VAL A 1 3058 ? 151.659 183.303 201.338 1.00 21.94  ? 3058 VAL A C     1 
ATOM   12078 O  O     . VAL A 1 3058 ? 152.099 182.189 201.646 1.00 25.01  ? 3058 VAL A O     1 
ATOM   12079 C  CB    . VAL A 1 3058 ? 149.980 183.529 199.457 1.00 18.81  ? 3058 VAL A CB    1 
ATOM   12080 C  CG1   . VAL A 1 3058 ? 150.622 182.316 198.814 1.00 21.28  ? 3058 VAL A CG1   1 
ATOM   12081 C  CG2   . VAL A 1 3058 ? 148.501 183.569 199.130 1.00 20.80  ? 3058 VAL A CG2   1 
ATOM   12082 N  N     . ILE A 1 3059 ? 152.439 184.385 201.299 1.00 25.44  ? 3059 ILE A N     1 
ATOM   12083 C  CA    . ILE A 1 3059 ? 153.859 184.296 201.622 1.00 19.28  ? 3059 ILE A CA    1 
ATOM   12084 C  C     . ILE A 1 3059 ? 154.048 183.852 203.066 1.00 21.03  ? 3059 ILE A C     1 
ATOM   12085 O  O     . ILE A 1 3059 ? 154.897 183.005 203.367 1.00 30.02  ? 3059 ILE A O     1 
ATOM   12086 C  CB    . ILE A 1 3059 ? 154.550 185.645 201.345 1.00 19.63  ? 3059 ILE A CB    1 
ATOM   12087 C  CG1   . ILE A 1 3059 ? 154.870 185.782 199.856 1.00 22.73  ? 3059 ILE A CG1   1 
ATOM   12088 C  CG2   . ILE A 1 3059 ? 155.814 185.788 202.177 1.00 14.50  ? 3059 ILE A CG2   1 
ATOM   12089 C  CD1   . ILE A 1 3059 ? 155.590 187.060 199.502 1.00 18.37  ? 3059 ILE A CD1   1 
ATOM   12090 N  N     . ARG A 1 3060 ? 153.250 184.406 203.979 1.00 24.42  ? 3060 ARG A N     1 
ATOM   12091 C  CA    . ARG A 1 3060 ? 153.415 184.089 205.393 1.00 21.18  ? 3060 ARG A CA    1 
ATOM   12092 C  C     . ARG A 1 3060 ? 152.930 182.682 205.727 1.00 21.56  ? 3060 ARG A C     1 
ATOM   12093 O  O     . ARG A 1 3060 ? 153.466 182.050 206.644 1.00 27.16  ? 3060 ARG A O     1 
ATOM   12094 C  CB    . ARG A 1 3060 ? 152.680 185.126 206.240 1.00 21.40  ? 3060 ARG A CB    1 
ATOM   12095 C  CG    . ARG A 1 3060 ? 152.857 184.965 207.736 1.00 24.16  ? 3060 ARG A CG    1 
ATOM   12096 C  CD    . ARG A 1 3060 ? 152.517 186.262 208.467 1.00 31.84  ? 3060 ARG A CD    1 
ATOM   12097 N  NE    . ARG A 1 3060 ? 151.096 186.599 208.452 1.00 36.37  ? 3060 ARG A NE    1 
ATOM   12098 C  CZ    . ARG A 1 3060 ? 150.103 185.800 208.827 1.00 39.51  ? 3060 ARG A CZ    1 
ATOM   12099 N  NH1   . ARG A 1 3060 ? 150.328 184.602 209.343 1.00 36.87  ? 3060 ARG A NH1   1 
ATOM   12100 N  NH2   . ARG A 1 3060 ? 148.849 186.224 208.701 1.00 42.64  ? 3060 ARG A NH2   1 
ATOM   12101 N  N     . ASN A 1 3061 ? 151.939 182.167 205.000 1.00 21.42  ? 3061 ASN A N     1 
ATOM   12102 C  CA    . ASN A 1 3061 ? 151.299 180.909 205.372 1.00 16.71  ? 3061 ASN A CA    1 
ATOM   12103 C  C     . ASN A 1 3061 ? 151.827 179.699 204.608 1.00 18.44  ? 3061 ASN A C     1 
ATOM   12104 O  O     . ASN A 1 3061 ? 152.167 178.685 205.223 1.00 24.25  ? 3061 ASN A O     1 
ATOM   12105 C  CB    . ASN A 1 3061 ? 149.783 181.019 205.174 1.00 21.38  ? 3061 ASN A CB    1 
ATOM   12106 C  CG    . ASN A 1 3061 ? 149.115 181.857 206.243 1.00 24.09  ? 3061 ASN A CG    1 
ATOM   12107 O  OD1   . ASN A 1 3061 ? 149.468 181.781 207.419 1.00 24.89  ? 3061 ASN A OD1   1 
ATOM   12108 N  ND2   . ASN A 1 3061 ? 148.141 182.662 205.838 1.00 26.91  ? 3061 ASN A ND2   1 
ATOM   12109 N  N     . LEU A 1 3062 ? 151.899 179.778 203.282 1.00 14.68  ? 3062 LEU A N     1 
ATOM   12110 C  CA    . LEU A 1 3062 ? 152.162 178.600 202.463 1.00 12.64  ? 3062 LEU A CA    1 
ATOM   12111 C  C     . LEU A 1 3062 ? 153.626 178.183 202.549 1.00 18.65  ? 3062 LEU A C     1 
ATOM   12112 O  O     . LEU A 1 3062 ? 154.527 179.003 202.344 1.00 22.97  ? 3062 LEU A O     1 
ATOM   12113 C  CB    . LEU A 1 3062 ? 151.780 178.877 201.010 1.00 15.03  ? 3062 LEU A CB    1 
ATOM   12114 C  CG    . LEU A 1 3062 ? 151.869 177.710 200.026 1.00 15.28  ? 3062 LEU A CG    1 
ATOM   12115 C  CD1   . LEU A 1 3062 ? 151.148 176.494 200.575 1.00 16.06  ? 3062 LEU A CD1   1 
ATOM   12116 C  CD2   . LEU A 1 3062 ? 151.300 178.105 198.677 1.00 13.11  ? 3062 LEU A CD2   1 
ATOM   12117 N  N     . HIS A 1 3063 ? 153.860 176.905 202.845 1.00 13.45  ? 3063 HIS A N     1 
ATOM   12118 C  CA    . HIS A 1 3063 ? 155.194 176.315 202.844 1.00 10.99  ? 3063 HIS A CA    1 
ATOM   12119 C  C     . HIS A 1 3063 ? 155.201 175.154 201.862 1.00 10.12  ? 3063 HIS A C     1 
ATOM   12120 O  O     . HIS A 1 3063 ? 154.457 174.188 202.042 1.00 13.67  ? 3063 HIS A O     1 
ATOM   12121 C  CB    . HIS A 1 3063 ? 155.589 175.828 204.241 1.00 8.88   ? 3063 HIS A CB    1 
ATOM   12122 C  CG    . HIS A 1 3063 ? 155.559 176.894 205.289 1.00 9.76   ? 3063 HIS A CG    1 
ATOM   12123 N  ND1   . HIS A 1 3063 ? 154.474 177.098 206.113 1.00 11.46  ? 3063 HIS A ND1   1 
ATOM   12124 C  CD2   . HIS A 1 3063 ? 156.491 177.802 205.664 1.00 12.46  ? 3063 HIS A CD2   1 
ATOM   12125 C  CE1   . HIS A 1 3063 ? 154.733 178.093 206.942 1.00 13.88  ? 3063 HIS A CE1   1 
ATOM   12126 N  NE2   . HIS A 1 3063 ? 155.951 178.537 206.691 1.00 15.32  ? 3063 HIS A NE2   1 
ATOM   12127 N  N     . VAL A 1 3064 ? 156.049 175.234 200.843 1.00 9.24   ? 3064 VAL A N     1 
ATOM   12128 C  CA    . VAL A 1 3064 ? 156.108 174.225 199.790 1.00 8.68   ? 3064 VAL A CA    1 
ATOM   12129 C  C     . VAL A 1 3064 ? 157.275 173.288 200.066 1.00 10.86  ? 3064 VAL A C     1 
ATOM   12130 O  O     . VAL A 1 3064 ? 158.418 173.734 200.218 1.00 13.75  ? 3064 VAL A O     1 
ATOM   12131 C  CB    . VAL A 1 3064 ? 156.241 174.875 198.403 1.00 8.79   ? 3064 VAL A CB    1 
ATOM   12132 C  CG1   . VAL A 1 3064 ? 156.417 173.811 197.333 1.00 9.74   ? 3064 VAL A CG1   1 
ATOM   12133 C  CG2   . VAL A 1 3064 ? 155.030 175.740 198.107 1.00 11.45  ? 3064 VAL A CG2   1 
ATOM   12134 N  N     . VAL A 1 3065 ? 156.990 171.991 200.127 1.00 11.40  ? 3065 VAL A N     1 
ATOM   12135 C  CA    . VAL A 1 3065 ? 157.999 170.961 200.347 1.00 9.60   ? 3065 VAL A CA    1 
ATOM   12136 C  C     . VAL A 1 3065 ? 158.094 170.136 199.073 1.00 10.76  ? 3065 VAL A C     1 
ATOM   12137 O  O     . VAL A 1 3065 ? 157.176 169.374 198.747 1.00 15.68  ? 3065 VAL A O     1 
ATOM   12138 C  CB    . VAL A 1 3065 ? 157.663 170.076 201.553 1.00 10.49  ? 3065 VAL A CB    1 
ATOM   12139 C  CG1   . VAL A 1 3065 ? 158.842 169.185 201.895 1.00 11.07  ? 3065 VAL A CG1   1 
ATOM   12140 C  CG2   . VAL A 1 3065 ? 157.270 170.928 202.744 1.00 9.83   ? 3065 VAL A CG2   1 
ATOM   12141 N  N     . PHE A 1 3066 ? 159.209 170.267 198.364 1.00 11.89  ? 3066 PHE A N     1 
ATOM   12142 C  CA    . PHE A 1 3066 ? 159.441 169.550 197.118 1.00 10.43  ? 3066 PHE A CA    1 
ATOM   12143 C  C     . PHE A 1 3066 ? 160.367 168.372 197.389 1.00 14.14  ? 3066 PHE A C     1 
ATOM   12144 O  O     . PHE A 1 3066 ? 161.455 168.548 197.945 1.00 16.98  ? 3066 PHE A O     1 
ATOM   12145 C  CB    . PHE A 1 3066 ? 160.040 170.482 196.065 1.00 15.05  ? 3066 PHE A CB    1 
ATOM   12146 C  CG    . PHE A 1 3066 ? 159.748 170.069 194.653 1.00 22.57  ? 3066 PHE A CG    1 
ATOM   12147 C  CD1   . PHE A 1 3066 ? 160.585 169.189 193.988 1.00 25.44  ? 3066 PHE A CD1   1 
ATOM   12148 C  CD2   . PHE A 1 3066 ? 158.635 170.557 193.992 1.00 19.37  ? 3066 PHE A CD2   1 
ATOM   12149 C  CE1   . PHE A 1 3066 ? 160.319 168.806 192.689 1.00 28.10  ? 3066 PHE A CE1   1 
ATOM   12150 C  CE2   . PHE A 1 3066 ? 158.364 170.176 192.694 1.00 30.27  ? 3066 PHE A CE2   1 
ATOM   12151 C  CZ    . PHE A 1 3066 ? 159.207 169.300 192.041 1.00 35.39  ? 3066 PHE A CZ    1 
ATOM   12152 N  N     . THR A 1 3067 ? 159.933 167.176 197.003 1.00 14.07  ? 3067 THR A N     1 
ATOM   12153 C  CA    . THR A 1 3067 ? 160.702 165.954 197.197 1.00 15.26  ? 3067 THR A CA    1 
ATOM   12154 C  C     . THR A 1 3067 ? 161.061 165.361 195.843 1.00 21.26  ? 3067 THR A C     1 
ATOM   12155 O  O     . THR A 1 3067 ? 160.205 165.269 194.956 1.00 29.76  ? 3067 THR A O     1 
ATOM   12156 C  CB    . THR A 1 3067 ? 159.921 164.935 198.030 1.00 14.80  ? 3067 THR A CB    1 
ATOM   12157 O  OG1   . THR A 1 3067 ? 158.751 164.525 197.313 1.00 22.03  ? 3067 THR A OG1   1 
ATOM   12158 C  CG2   . THR A 1 3067 ? 159.510 165.538 199.363 1.00 12.40  ? 3067 THR A CG2   1 
ATOM   12159 N  N     . MET A 1 3068 ? 162.322 164.963 195.683 1.00 16.66  ? 3068 MET A N     1 
ATOM   12160 C  CA    . MET A 1 3068 ? 162.781 164.401 194.423 1.00 22.26  ? 3068 MET A CA    1 
ATOM   12161 C  C     . MET A 1 3068 ? 163.915 163.418 194.676 1.00 20.11  ? 3068 MET A C     1 
ATOM   12162 O  O     . MET A 1 3068 ? 164.657 163.538 195.654 1.00 17.37  ? 3068 MET A O     1 
ATOM   12163 C  CB    . MET A 1 3068 ? 163.235 165.500 193.455 1.00 23.94  ? 3068 MET A CB    1 
ATOM   12164 C  CG    . MET A 1 3068 ? 164.498 166.224 193.881 1.00 21.71  ? 3068 MET A CG    1 
ATOM   12165 S  SD    . MET A 1 3068 ? 164.745 167.762 192.978 1.00 48.94  ? 3068 MET A SD    1 
ATOM   12166 C  CE    . MET A 1 3068 ? 164.667 167.171 191.292 1.00 30.75  ? 3068 MET A CE    1 
ATOM   12167 N  N     . ASN A 1 3069 ? 164.035 162.440 193.780 1.00 20.37  ? 3069 ASN A N     1 
ATOM   12168 C  CA    . ASN A 1 3069 ? 165.132 161.491 193.850 1.00 18.40  ? 3069 ASN A CA    1 
ATOM   12169 C  C     . ASN A 1 3069 ? 166.432 162.148 193.389 1.00 25.59  ? 3069 ASN A C     1 
ATOM   12170 O  O     . ASN A 1 3069 ? 166.417 163.054 192.552 1.00 29.92  ? 3069 ASN A O     1 
ATOM   12171 C  CB    . ASN A 1 3069 ? 164.836 160.263 192.992 1.00 19.75  ? 3069 ASN A CB    1 
ATOM   12172 C  CG    . ASN A 1 3069 ? 163.637 159.482 193.486 1.00 24.07  ? 3069 ASN A CG    1 
ATOM   12173 O  OD1   . ASN A 1 3069 ? 163.651 158.915 194.577 1.00 28.13  ? 3069 ASN A OD1   1 
ATOM   12174 N  ND2   . ASN A 1 3069 ? 162.585 159.455 192.682 1.00 28.10  ? 3069 ASN A ND2   1 
ATOM   12175 N  N     . PRO A 1 3070 ? 167.576 161.701 193.916 1.00 26.44  ? 3070 PRO A N     1 
ATOM   12176 C  CA    . PRO A 1 3070 ? 168.865 162.337 193.576 1.00 24.03  ? 3070 PRO A CA    1 
ATOM   12177 C  C     . PRO A 1 3070 ? 169.434 161.887 192.232 1.00 30.02  ? 3070 PRO A C     1 
ATOM   12178 O  O     . PRO A 1 3070 ? 170.266 160.988 192.120 1.00 38.55  ? 3070 PRO A O     1 
ATOM   12179 C  CB    . PRO A 1 3070 ? 169.758 161.918 194.745 1.00 20.56  ? 3070 PRO A CB    1 
ATOM   12180 C  CG    . PRO A 1 3070 ? 169.229 160.590 195.151 1.00 20.79  ? 3070 PRO A CG    1 
ATOM   12181 C  CD    . PRO A 1 3070 ? 167.746 160.597 194.877 1.00 23.04  ? 3070 PRO A CD    1 
ATOM   12182 N  N     . SER A 1 3071 ? 168.965 162.531 191.170 1.00 34.14  ? 3071 SER A N     1 
ATOM   12183 C  CA    . SER A 1 3071 ? 169.489 162.295 189.834 1.00 42.86  ? 3071 SER A CA    1 
ATOM   12184 C  C     . SER A 1 3071 ? 170.591 163.297 189.514 1.00 48.82  ? 3071 SER A C     1 
ATOM   12185 O  O     . SER A 1 3071 ? 170.521 164.470 189.891 1.00 46.05  ? 3071 SER A O     1 
ATOM   12186 C  CB    . SER A 1 3071 ? 168.378 162.390 188.788 1.00 40.79  ? 3071 SER A CB    1 
ATOM   12187 O  OG    . SER A 1 3071 ? 168.893 162.201 187.482 1.00 36.95  ? 3071 SER A OG    1 
ATOM   12188 N  N     . SER A 1 3072 ? 171.617 162.819 188.810 1.00 50.95  ? 3072 SER A N     1 
ATOM   12189 C  CA    . SER A 1 3072 ? 172.738 163.682 188.450 1.00 53.23  ? 3072 SER A CA    1 
ATOM   12190 C  C     . SER A 1 3072 ? 172.310 164.744 187.444 1.00 51.57  ? 3072 SER A C     1 
ATOM   12191 O  O     . SER A 1 3072 ? 172.427 165.947 187.701 1.00 53.03  ? 3072 SER A O     1 
ATOM   12192 C  CB    . SER A 1 3072 ? 173.889 162.841 187.897 1.00 55.88  ? 3072 SER A CB    1 
ATOM   12193 O  OG    . SER A 1 3072 ? 174.279 161.841 188.821 1.00 53.01  ? 3072 SER A OG    1 
ATOM   12194 N  N     . GLU A 1 3073 ? 171.812 164.314 186.284 1.00 47.55  ? 3073 GLU A N     1 
ATOM   12195 C  CA    . GLU A 1 3073 ? 171.364 165.259 185.268 1.00 49.00  ? 3073 GLU A CA    1 
ATOM   12196 C  C     . GLU A 1 3073 ? 170.007 165.866 185.603 1.00 45.75  ? 3073 GLU A C     1 
ATOM   12197 O  O     . GLU A 1 3073 ? 169.695 166.969 185.139 1.00 49.34  ? 3073 GLU A O     1 
ATOM   12198 C  CB    . GLU A 1 3073 ? 171.316 164.575 183.900 1.00 56.89  ? 3073 GLU A CB    1 
ATOM   12199 C  CG    . GLU A 1 3073 ? 170.115 163.666 183.694 1.00 58.26  ? 3073 GLU A CG    1 
ATOM   12200 C  CD    . GLU A 1 3073 ? 170.410 162.224 184.055 1.00 63.44  ? 3073 GLU A CD    1 
ATOM   12201 O  OE1   . GLU A 1 3073 ? 171.510 161.954 184.583 1.00 55.25  ? 3073 GLU A OE1   1 
ATOM   12202 O  OE2   . GLU A 1 3073 ? 169.542 161.359 183.812 1.00 71.15  ? 3073 GLU A OE2   1 
ATOM   12203 N  N     . GLY A 1 3074 ? 169.190 165.167 186.394 1.00 43.32  ? 3074 GLY A N     1 
ATOM   12204 C  CA    . GLY A 1 3074 ? 167.885 165.700 186.747 1.00 42.12  ? 3074 GLY A CA    1 
ATOM   12205 C  C     . GLY A 1 3074 ? 167.976 166.971 187.567 1.00 41.23  ? 3074 GLY A C     1 
ATOM   12206 O  O     . GLY A 1 3074 ? 167.223 167.922 187.345 1.00 42.66  ? 3074 GLY A O     1 
ATOM   12207 N  N     . LEU A 1 3075 ? 168.903 167.007 188.527 1.00 36.20  ? 3075 LEU A N     1 
ATOM   12208 C  CA    . LEU A 1 3075 ? 169.089 168.211 189.328 1.00 36.23  ? 3075 LEU A CA    1 
ATOM   12209 C  C     . LEU A 1 3075 ? 169.596 169.367 188.476 1.00 41.20  ? 3075 LEU A C     1 
ATOM   12210 O  O     . LEU A 1 3075 ? 169.170 170.514 188.659 1.00 42.26  ? 3075 LEU A O     1 
ATOM   12211 C  CB    . LEU A 1 3075 ? 170.048 167.928 190.481 1.00 34.72  ? 3075 LEU A CB    1 
ATOM   12212 C  CG    . LEU A 1 3075 ? 169.725 168.680 191.768 1.00 31.25  ? 3075 LEU A CG    1 
ATOM   12213 C  CD1   . LEU A 1 3075 ? 168.336 168.306 192.243 1.00 27.66  ? 3075 LEU A CD1   1 
ATOM   12214 C  CD2   . LEU A 1 3075 ? 170.758 168.375 192.833 1.00 26.91  ? 3075 LEU A CD2   1 
ATOM   12215 N  N     . LYS A 1 3076 ? 170.505 169.087 187.539 1.00 39.20  ? 3076 LYS A N     1 
ATOM   12216 C  CA    . LYS A 1 3076 ? 170.981 170.130 186.638 1.00 33.90  ? 3076 LYS A CA    1 
ATOM   12217 C  C     . LYS A 1 3076 ? 169.847 170.673 185.778 1.00 35.92  ? 3076 LYS A C     1 
ATOM   12218 O  O     . LYS A 1 3076 ? 169.758 171.884 185.545 1.00 44.86  ? 3076 LYS A O     1 
ATOM   12219 C  CB    . LYS A 1 3076 ? 172.111 169.591 185.761 1.00 29.87  ? 3076 LYS A CB    1 
ATOM   12220 C  CG    . LYS A 1 3076 ? 173.297 169.046 186.539 1.00 31.78  ? 3076 LYS A CG    1 
ATOM   12221 C  CD    . LYS A 1 3076 ? 174.564 169.064 185.700 1.00 31.73  ? 3076 LYS A CD    1 
ATOM   12222 C  CE    . LYS A 1 3076 ? 175.487 167.917 186.072 1.00 32.19  ? 3076 LYS A CE    1 
ATOM   12223 N  NZ    . LYS A 1 3076 ? 176.389 168.270 187.201 1.00 41.23  ? 3076 LYS A NZ    1 
ATOM   12224 N  N     . ASP A 1 3077 ? 168.974 169.789 185.290 1.00 31.08  ? 3077 ASP A N     1 
ATOM   12225 C  CA    . ASP A 1 3077 ? 167.835 170.237 184.495 1.00 38.78  ? 3077 ASP A CA    1 
ATOM   12226 C  C     . ASP A 1 3077 ? 166.871 171.076 185.327 1.00 40.16  ? 3077 ASP A C     1 
ATOM   12227 O  O     . ASP A 1 3077 ? 166.354 172.094 184.851 1.00 39.36  ? 3077 ASP A O     1 
ATOM   12228 C  CB    . ASP A 1 3077 ? 167.115 169.033 183.888 1.00 48.90  ? 3077 ASP A CB    1 
ATOM   12229 C  CG    . ASP A 1 3077 ? 167.939 168.337 182.823 1.00 59.42  ? 3077 ASP A CG    1 
ATOM   12230 O  OD1   . ASP A 1 3077 ? 168.754 169.014 182.162 1.00 57.15  ? 3077 ASP A OD1   1 
ATOM   12231 O  OD2   . ASP A 1 3077 ? 167.772 167.112 182.646 1.00 57.08  ? 3077 ASP A OD2   1 
ATOM   12232 N  N     . ARG A 1 3078 ? 166.615 170.661 186.571 1.00 43.71  ? 3078 ARG A N     1 
ATOM   12233 C  CA    . ARG A 1 3078 ? 165.728 171.430 187.439 1.00 39.62  ? 3078 ARG A CA    1 
ATOM   12234 C  C     . ARG A 1 3078 ? 166.329 172.779 187.812 1.00 37.12  ? 3078 ARG A C     1 
ATOM   12235 O  O     . ARG A 1 3078 ? 165.589 173.741 188.043 1.00 32.40  ? 3078 ARG A O     1 
ATOM   12236 C  CB    . ARG A 1 3078 ? 165.402 170.636 188.703 1.00 39.26  ? 3078 ARG A CB    1 
ATOM   12237 C  CG    . ARG A 1 3078 ? 164.629 169.356 188.461 1.00 37.55  ? 3078 ARG A CG    1 
ATOM   12238 C  CD    . ARG A 1 3078 ? 163.212 169.636 188.000 1.00 34.71  ? 3078 ARG A CD    1 
ATOM   12239 N  NE    . ARG A 1 3078 ? 162.437 168.407 187.877 1.00 51.80  ? 3078 ARG A NE    1 
ATOM   12240 C  CZ    . ARG A 1 3078 ? 162.343 167.689 186.766 1.00 58.27  ? 3078 ARG A CZ    1 
ATOM   12241 N  NH1   . ARG A 1 3078 ? 162.965 168.049 185.655 1.00 52.60  ? 3078 ARG A NH1   1 
ATOM   12242 N  NH2   . ARG A 1 3078 ? 161.608 166.581 186.770 1.00 53.82  ? 3078 ARG A NH2   1 
ATOM   12243 N  N     . ALA A 1 3079 ? 167.660 172.868 187.883 1.00 36.52  ? 3079 ALA A N     1 
ATOM   12244 C  CA    . ALA A 1 3079 ? 168.303 174.136 188.204 1.00 33.33  ? 3079 ALA A CA    1 
ATOM   12245 C  C     . ALA A 1 3079 ? 168.018 175.209 187.163 1.00 38.88  ? 3079 ALA A C     1 
ATOM   12246 O  O     . ALA A 1 3079 ? 168.077 176.401 187.486 1.00 33.84  ? 3079 ALA A O     1 
ATOM   12247 C  CB    . ALA A 1 3079 ? 169.812 173.938 188.352 1.00 28.78  ? 3079 ALA A CB    1 
ATOM   12248 N  N     . ALA A 1 3080 ? 167.706 174.819 185.930 1.00 37.02  ? 3080 ALA A N     1 
ATOM   12249 C  CA    . ALA A 1 3080 ? 167.318 175.752 184.881 1.00 34.96  ? 3080 ALA A CA    1 
ATOM   12250 C  C     . ALA A 1 3080 ? 165.815 175.852 184.695 1.00 29.35  ? 3080 ALA A C     1 
ATOM   12251 O  O     . ALA A 1 3080 ? 165.300 176.946 184.458 1.00 28.59  ? 3080 ALA A O     1 
ATOM   12252 C  CB    . ALA A 1 3080 ? 167.964 175.351 183.550 1.00 33.02  ? 3080 ALA A CB    1 
ATOM   12253 N  N     . THR A 1 3081 ? 165.094 174.733 184.795 1.00 30.81  ? 3081 THR A N     1 
ATOM   12254 C  CA    . THR A 1 3081 ? 163.644 174.775 184.638 1.00 31.69  ? 3081 THR A CA    1 
ATOM   12255 C  C     . THR A 1 3081 ? 162.982 175.544 185.776 1.00 34.89  ? 3081 THR A C     1 
ATOM   12256 O  O     . THR A 1 3081 ? 162.032 176.302 185.549 1.00 40.10  ? 3081 THR A O     1 
ATOM   12257 C  CB    . THR A 1 3081 ? 163.085 173.355 184.549 1.00 36.63  ? 3081 THR A CB    1 
ATOM   12258 O  OG1   . THR A 1 3081 ? 163.714 172.660 183.465 1.00 33.92  ? 3081 THR A OG1   1 
ATOM   12259 C  CG2   . THR A 1 3081 ? 161.585 173.386 184.312 1.00 34.70  ? 3081 THR A CG2   1 
ATOM   12260 N  N     . SER A 1 3082 ? 163.460 175.359 187.005 1.00 31.96  ? 3082 SER A N     1 
ATOM   12261 C  CA    . SER A 1 3082 ? 162.922 176.043 188.182 1.00 26.64  ? 3082 SER A CA    1 
ATOM   12262 C  C     . SER A 1 3082 ? 164.075 176.614 188.995 1.00 26.09  ? 3082 SER A C     1 
ATOM   12263 O  O     . SER A 1 3082 ? 164.573 175.969 189.928 1.00 25.04  ? 3082 SER A O     1 
ATOM   12264 C  CB    . SER A 1 3082 ? 162.067 175.101 189.029 1.00 28.66  ? 3082 SER A CB    1 
ATOM   12265 O  OG    . SER A 1 3082 ? 161.393 175.810 190.053 1.00 24.81  ? 3082 SER A OG    1 
ATOM   12266 N  N     . PRO A 1 3083 ? 164.537 177.821 188.659 1.00 20.95  ? 3083 PRO A N     1 
ATOM   12267 C  CA    . PRO A 1 3083 ? 165.617 178.431 189.454 1.00 20.16  ? 3083 PRO A CA    1 
ATOM   12268 C  C     . PRO A 1 3083 ? 165.249 178.658 190.911 1.00 17.15  ? 3083 PRO A C     1 
ATOM   12269 O  O     . PRO A 1 3083 ? 166.113 178.527 191.787 1.00 23.09  ? 3083 PRO A O     1 
ATOM   12270 C  CB    . PRO A 1 3083 ? 165.884 179.751 188.715 1.00 17.50  ? 3083 PRO A CB    1 
ATOM   12271 C  CG    . PRO A 1 3083 ? 164.617 180.037 187.983 1.00 20.59  ? 3083 PRO A CG    1 
ATOM   12272 C  CD    . PRO A 1 3083 ? 164.085 178.701 187.570 1.00 17.40  ? 3083 PRO A CD    1 
ATOM   12273 N  N     . ALA A 1 3084 ? 163.986 178.985 191.200 1.00 14.40  ? 3084 ALA A N     1 
ATOM   12274 C  CA    . ALA A 1 3084 ? 163.582 179.242 192.577 1.00 15.91  ? 3084 ALA A CA    1 
ATOM   12275 C  C     . ALA A 1 3084 ? 163.693 178.006 193.457 1.00 19.83  ? 3084 ALA A C     1 
ATOM   12276 O  O     . ALA A 1 3084 ? 163.773 178.138 194.683 1.00 18.93  ? 3084 ALA A O     1 
ATOM   12277 C  CB    . ALA A 1 3084 ? 162.153 179.781 192.623 1.00 17.85  ? 3084 ALA A CB    1 
ATOM   12278 N  N     . LEU A 1 3085 ? 163.703 176.810 192.866 1.00 20.00  ? 3085 LEU A N     1 
ATOM   12279 C  CA    . LEU A 1 3085 ? 163.918 175.602 193.650 1.00 15.91  ? 3085 LEU A CA    1 
ATOM   12280 C  C     . LEU A 1 3085 ? 165.316 175.548 194.248 1.00 15.54  ? 3085 LEU A C     1 
ATOM   12281 O  O     . LEU A 1 3085 ? 165.566 174.722 195.131 1.00 23.16  ? 3085 LEU A O     1 
ATOM   12282 C  CB    . LEU A 1 3085 ? 163.675 174.363 192.788 1.00 18.44  ? 3085 LEU A CB    1 
ATOM   12283 C  CG    . LEU A 1 3085 ? 162.282 173.737 192.847 1.00 14.92  ? 3085 LEU A CG    1 
ATOM   12284 C  CD1   . LEU A 1 3085 ? 162.240 172.462 192.024 1.00 14.29  ? 3085 LEU A CD1   1 
ATOM   12285 C  CD2   . LEU A 1 3085 ? 161.876 173.461 194.283 1.00 14.58  ? 3085 LEU A CD2   1 
ATOM   12286 N  N     . PHE A 1 3086 ? 166.231 176.403 193.789 1.00 15.99  ? 3086 PHE A N     1 
ATOM   12287 C  CA    . PHE A 1 3086 ? 167.601 176.390 194.271 1.00 20.77  ? 3086 PHE A CA    1 
ATOM   12288 C  C     . PHE A 1 3086 ? 168.055 177.707 194.883 1.00 20.31  ? 3086 PHE A C     1 
ATOM   12289 O  O     . PHE A 1 3086 ? 169.155 177.756 195.444 1.00 24.06  ? 3086 PHE A O     1 
ATOM   12290 C  CB    . PHE A 1 3086 ? 168.557 175.999 193.135 1.00 15.44  ? 3086 PHE A CB    1 
ATOM   12291 C  CG    . PHE A 1 3086 ? 168.416 174.569 192.702 1.00 20.01  ? 3086 PHE A CG    1 
ATOM   12292 C  CD1   . PHE A 1 3086 ? 167.410 174.193 191.830 1.00 22.13  ? 3086 PHE A CD1   1 
ATOM   12293 C  CD2   . PHE A 1 3086 ? 169.277 173.599 193.182 1.00 25.22  ? 3086 PHE A CD2   1 
ATOM   12294 C  CE1   . PHE A 1 3086 ? 167.271 172.878 191.438 1.00 27.30  ? 3086 PHE A CE1   1 
ATOM   12295 C  CE2   . PHE A 1 3086 ? 169.143 172.283 192.792 1.00 25.37  ? 3086 PHE A CE2   1 
ATOM   12296 C  CZ    . PHE A 1 3086 ? 168.138 171.923 191.919 1.00 28.05  ? 3086 PHE A CZ    1 
ATOM   12297 N  N     . ASN A 1 3087 ? 167.252 178.767 194.798 1.00 17.65  ? 3087 ASN A N     1 
ATOM   12298 C  CA    . ASN A 1 3087 ? 167.566 180.022 195.461 1.00 19.31  ? 3087 ASN A CA    1 
ATOM   12299 C  C     . ASN A 1 3087 ? 166.463 180.506 196.389 1.00 17.82  ? 3087 ASN A C     1 
ATOM   12300 O  O     . ASN A 1 3087 ? 166.708 181.421 197.184 1.00 22.96  ? 3087 ASN A O     1 
ATOM   12301 C  CB    . ASN A 1 3087 ? 167.889 181.114 194.426 1.00 22.48  ? 3087 ASN A CB    1 
ATOM   12302 C  CG    . ASN A 1 3087 ? 166.649 181.778 193.859 1.00 24.65  ? 3087 ASN A CG    1 
ATOM   12303 O  OD1   . ASN A 1 3087 ? 166.082 182.688 194.464 1.00 25.32  ? 3087 ASN A OD1   1 
ATOM   12304 N  ND2   . ASN A 1 3087 ? 166.226 181.330 192.684 1.00 27.56  ? 3087 ASN A ND2   1 
ATOM   12305 N  N     . ARG A 1 3088 ? 165.264 179.925 196.317 1.00 13.94  ? 3088 ARG A N     1 
ATOM   12306 C  CA    . ARG A 1 3088 ? 164.186 180.244 197.240 1.00 15.40  ? 3088 ARG A CA    1 
ATOM   12307 C  C     . ARG A 1 3088 ? 163.852 179.110 198.196 1.00 12.73  ? 3088 ARG A C     1 
ATOM   12308 O  O     . ARG A 1 3088 ? 163.150 179.345 199.183 1.00 14.16  ? 3088 ARG A O     1 
ATOM   12309 C  CB    . ARG A 1 3088 ? 162.914 180.628 196.470 1.00 19.32  ? 3088 ARG A CB    1 
ATOM   12310 C  CG    . ARG A 1 3088 ? 163.021 181.909 195.664 1.00 17.76  ? 3088 ARG A CG    1 
ATOM   12311 C  CD    . ARG A 1 3088 ? 163.348 183.097 196.549 1.00 18.58  ? 3088 ARG A CD    1 
ATOM   12312 N  NE    . ARG A 1 3088 ? 162.890 184.355 195.969 1.00 35.48  ? 3088 ARG A NE    1 
ATOM   12313 C  CZ    . ARG A 1 3088 ? 163.465 184.964 194.941 1.00 39.57  ? 3088 ARG A CZ    1 
ATOM   12314 N  NH1   . ARG A 1 3088 ? 164.539 184.465 194.352 1.00 28.71  ? 3088 ARG A NH1   1 
ATOM   12315 N  NH2   . ARG A 1 3088 ? 162.948 186.104 194.492 1.00 30.39  ? 3088 ARG A NH2   1 
ATOM   12316 N  N     . CYS A 1 3089 ? 164.332 177.900 197.931 1.00 16.18  ? 3089 CYS A N     1 
ATOM   12317 C  CA    . CYS A 1 3089 ? 164.062 176.742 198.770 1.00 12.93  ? 3089 CYS A CA    1 
ATOM   12318 C  C     . CYS A 1 3089 ? 165.325 176.336 199.516 1.00 11.62  ? 3089 CYS A C     1 
ATOM   12319 O  O     . CYS A 1 3089 ? 166.433 176.432 198.980 1.00 15.94  ? 3089 CYS A O     1 
ATOM   12320 C  CB    . CYS A 1 3089 ? 163.559 175.563 197.934 1.00 8.40   ? 3089 CYS A CB    1 
ATOM   12321 S  SG    . CYS A 1 3089 ? 161.972 175.825 197.120 1.00 22.01  ? 3089 CYS A SG    1 
ATOM   12322 N  N     . VAL A 1 3090 ? 165.153 175.890 200.755 1.00 12.96  ? 3090 VAL A N     1 
ATOM   12323 C  CA    . VAL A 1 3090 ? 166.251 175.318 201.524 1.00 10.35  ? 3090 VAL A CA    1 
ATOM   12324 C  C     . VAL A 1 3090 ? 166.425 173.870 201.087 1.00 12.37  ? 3090 VAL A C     1 
ATOM   12325 O  O     . VAL A 1 3090 ? 165.481 173.076 201.149 1.00 17.66  ? 3090 VAL A O     1 
ATOM   12326 C  CB    . VAL A 1 3090 ? 165.984 175.416 203.031 1.00 8.00   ? 3090 VAL A CB    1 
ATOM   12327 C  CG1   . VAL A 1 3090 ? 167.003 174.598 203.804 1.00 9.95   ? 3090 VAL A CG1   1 
ATOM   12328 C  CG2   . VAL A 1 3090 ? 166.008 176.865 203.477 1.00 15.05  ? 3090 VAL A CG2   1 
ATOM   12329 N  N     . LEU A 1 3091 ? 167.627 173.526 200.636 1.00 9.36   ? 3091 LEU A N     1 
ATOM   12330 C  CA    . LEU A 1 3091 ? 167.903 172.202 200.097 1.00 8.44   ? 3091 LEU A CA    1 
ATOM   12331 C  C     . LEU A 1 3091 ? 168.442 171.306 201.205 1.00 15.54  ? 3091 LEU A C     1 
ATOM   12332 O  O     . LEU A 1 3091 ? 169.428 171.651 201.865 1.00 16.84  ? 3091 LEU A O     1 
ATOM   12333 C  CB    . LEU A 1 3091 ? 168.896 172.291 198.939 1.00 9.00   ? 3091 LEU A CB    1 
ATOM   12334 C  CG    . LEU A 1 3091 ? 169.008 171.091 197.997 1.00 9.79   ? 3091 LEU A CG    1 
ATOM   12335 C  CD1   . LEU A 1 3091 ? 169.340 171.561 196.593 1.00 11.67  ? 3091 LEU A CD1   1 
ATOM   12336 C  CD2   . LEU A 1 3091 ? 170.055 170.104 198.483 1.00 13.53  ? 3091 LEU A CD2   1 
ATOM   12337 N  N     . ASN A 1 3092 ? 167.796 170.160 201.406 1.00 18.04  ? 3092 ASN A N     1 
ATOM   12338 C  CA    . ASN A 1 3092 ? 168.231 169.164 202.376 1.00 12.65  ? 3092 ASN A CA    1 
ATOM   12339 C  C     . ASN A 1 3092 ? 168.489 167.858 201.642 1.00 16.00  ? 3092 ASN A C     1 
ATOM   12340 O  O     . ASN A 1 3092 ? 167.570 167.286 201.042 1.00 16.44  ? 3092 ASN A O     1 
ATOM   12341 C  CB    . ASN A 1 3092 ? 167.188 168.971 203.478 1.00 13.37  ? 3092 ASN A CB    1 
ATOM   12342 C  CG    . ASN A 1 3092 ? 167.239 170.062 204.525 1.00 23.72  ? 3092 ASN A CG    1 
ATOM   12343 O  OD1   . ASN A 1 3092 ? 168.247 170.753 204.668 1.00 27.12  ? 3092 ASN A OD1   1 
ATOM   12344 N  ND2   . ASN A 1 3092 ? 166.150 170.224 205.264 1.00 25.12  ? 3092 ASN A ND2   1 
ATOM   12345 N  N     . TRP A 1 3093 ? 169.732 167.386 201.698 1.00 15.72  ? 3093 TRP A N     1 
ATOM   12346 C  CA    . TRP A 1 3093 ? 170.131 166.150 201.029 1.00 13.35  ? 3093 TRP A CA    1 
ATOM   12347 C  C     . TRP A 1 3093 ? 170.000 165.002 202.019 1.00 16.71  ? 3093 TRP A C     1 
ATOM   12348 O  O     . TRP A 1 3093 ? 170.908 164.715 202.799 1.00 22.30  ? 3093 TRP A O     1 
ATOM   12349 C  CB    . TRP A 1 3093 ? 171.547 166.261 200.484 1.00 12.50  ? 3093 TRP A CB    1 
ATOM   12350 C  CG    . TRP A 1 3093 ? 171.822 165.309 199.370 1.00 13.13  ? 3093 TRP A CG    1 
ATOM   12351 C  CD1   . TRP A 1 3093 ? 172.198 164.004 199.482 1.00 11.89  ? 3093 TRP A CD1   1 
ATOM   12352 C  CD2   . TRP A 1 3093 ? 171.726 165.581 197.969 1.00 13.74  ? 3093 TRP A CD2   1 
ATOM   12353 N  NE1   . TRP A 1 3093 ? 172.351 163.448 198.236 1.00 10.57  ? 3093 TRP A NE1   1 
ATOM   12354 C  CE2   . TRP A 1 3093 ? 172.067 164.397 197.290 1.00 10.31  ? 3093 TRP A CE2   1 
ATOM   12355 C  CE3   . TRP A 1 3093 ? 171.392 166.714 197.222 1.00 12.95  ? 3093 TRP A CE3   1 
ATOM   12356 C  CZ2   . TRP A 1 3093 ? 172.081 164.312 195.902 1.00 12.98  ? 3093 TRP A CZ2   1 
ATOM   12357 C  CZ3   . TRP A 1 3093 ? 171.404 166.627 195.846 1.00 12.33  ? 3093 TRP A CZ3   1 
ATOM   12358 C  CH2   . TRP A 1 3093 ? 171.746 165.435 195.199 1.00 14.40  ? 3093 TRP A CH2   1 
ATOM   12359 N  N     . PHE A 1 3094 ? 168.845 164.338 201.988 1.00 14.65  ? 3094 PHE A N     1 
ATOM   12360 C  CA    . PHE A 1 3094 ? 168.657 163.158 202.821 1.00 11.76  ? 3094 PHE A CA    1 
ATOM   12361 C  C     . PHE A 1 3094 ? 169.415 161.968 202.247 1.00 14.97  ? 3094 PHE A C     1 
ATOM   12362 O  O     . PHE A 1 3094 ? 170.027 161.194 202.992 1.00 21.67  ? 3094 PHE A O     1 
ATOM   12363 C  CB    . PHE A 1 3094 ? 167.167 162.837 202.949 1.00 16.44  ? 3094 PHE A CB    1 
ATOM   12364 C  CG    . PHE A 1 3094 ? 166.399 163.809 203.805 1.00 17.48  ? 3094 PHE A CG    1 
ATOM   12365 C  CD1   . PHE A 1 3094 ? 167.024 164.901 204.384 1.00 20.11  ? 3094 PHE A CD1   1 
ATOM   12366 C  CD2   . PHE A 1 3094 ? 165.045 163.630 204.023 1.00 17.48  ? 3094 PHE A CD2   1 
ATOM   12367 C  CE1   . PHE A 1 3094 ? 166.312 165.792 205.163 1.00 18.14  ? 3094 PHE A CE1   1 
ATOM   12368 C  CE2   . PHE A 1 3094 ? 164.329 164.516 204.802 1.00 19.63  ? 3094 PHE A CE2   1 
ATOM   12369 C  CZ    . PHE A 1 3094 ? 164.964 165.598 205.373 1.00 19.62  ? 3094 PHE A CZ    1 
ATOM   12370 N  N     . GLY A 1 3095 ? 169.393 161.814 200.925 1.00 11.35  ? 3095 GLY A N     1 
ATOM   12371 C  CA    . GLY A 1 3095 ? 170.066 160.725 200.250 1.00 9.17   ? 3095 GLY A CA    1 
ATOM   12372 C  C     . GLY A 1 3095 ? 169.465 159.382 200.613 1.00 16.67  ? 3095 GLY A C     1 
ATOM   12373 O  O     . GLY A 1 3095 ? 168.264 159.247 200.870 1.00 18.98  ? 3095 GLY A O     1 
ATOM   12374 N  N     . ASP A 1 3096 ? 170.318 158.365 200.622 1.00 18.13  ? 3096 ASP A N     1 
ATOM   12375 C  CA    . ASP A 1 3096 ? 169.946 157.049 201.114 1.00 13.03  ? 3096 ASP A CA    1 
ATOM   12376 C  C     . ASP A 1 3096 ? 170.272 156.942 202.599 1.00 13.01  ? 3096 ASP A C     1 
ATOM   12377 O  O     . ASP A 1 3096 ? 171.025 157.744 203.154 1.00 17.82  ? 3096 ASP A O     1 
ATOM   12378 C  CB    . ASP A 1 3096 ? 170.671 155.951 200.333 1.00 19.31  ? 3096 ASP A CB    1 
ATOM   12379 C  CG    . ASP A 1 3096 ? 169.948 154.617 200.390 1.00 27.18  ? 3096 ASP A CG    1 
ATOM   12380 O  OD1   . ASP A 1 3096 ? 169.599 154.170 201.503 1.00 23.46  ? 3096 ASP A OD1   1 
ATOM   12381 O  OD2   . ASP A 1 3096 ? 169.730 154.011 199.320 1.00 33.94  ? 3096 ASP A OD2   1 
ATOM   12382 N  N     . TRP A 1 3097 ? 169.683 155.939 203.243 1.00 13.11  ? 3097 TRP A N     1 
ATOM   12383 C  CA    . TRP A 1 3097 ? 169.993 155.677 204.640 1.00 11.14  ? 3097 TRP A CA    1 
ATOM   12384 C  C     . TRP A 1 3097 ? 171.450 155.260 204.771 1.00 19.27  ? 3097 TRP A C     1 
ATOM   12385 O  O     . TRP A 1 3097 ? 171.934 154.407 204.020 1.00 19.11  ? 3097 TRP A O     1 
ATOM   12386 C  CB    . TRP A 1 3097 ? 169.075 154.594 205.199 1.00 8.71   ? 3097 TRP A CB    1 
ATOM   12387 C  CG    . TRP A 1 3097 ? 167.679 155.063 205.443 1.00 10.32  ? 3097 TRP A CG    1 
ATOM   12388 C  CD1   . TRP A 1 3097 ? 167.151 156.271 205.102 1.00 8.65   ? 3097 TRP A CD1   1 
ATOM   12389 C  CD2   . TRP A 1 3097 ? 166.630 154.332 206.086 1.00 10.40  ? 3097 TRP A CD2   1 
ATOM   12390 N  NE1   . TRP A 1 3097 ? 165.837 156.338 205.490 1.00 9.80   ? 3097 TRP A NE1   1 
ATOM   12391 C  CE2   . TRP A 1 3097 ? 165.492 155.160 206.096 1.00 9.84   ? 3097 TRP A CE2   1 
ATOM   12392 C  CE3   . TRP A 1 3097 ? 166.541 153.057 206.650 1.00 9.76   ? 3097 TRP A CE3   1 
ATOM   12393 C  CZ2   . TRP A 1 3097 ? 164.282 154.755 206.649 1.00 11.12  ? 3097 TRP A CZ2   1 
ATOM   12394 C  CZ3   . TRP A 1 3097 ? 165.340 152.658 207.198 1.00 10.80  ? 3097 TRP A CZ3   1 
ATOM   12395 C  CH2   . TRP A 1 3097 ? 164.226 153.503 207.194 1.00 11.79  ? 3097 TRP A CH2   1 
ATOM   12396 N  N     . SER A 1 3098 ? 172.151 155.864 205.725 1.00 22.57  ? 3098 SER A N     1 
ATOM   12397 C  CA    . SER A 1 3098 ? 173.558 155.565 205.917 1.00 15.98  ? 3098 SER A CA    1 
ATOM   12398 C  C     . SER A 1 3098 ? 173.730 154.171 206.516 1.00 17.66  ? 3098 SER A C     1 
ATOM   12399 O  O     . SER A 1 3098 ? 172.767 153.497 206.892 1.00 19.18  ? 3098 SER A O     1 
ATOM   12400 C  CB    . SER A 1 3098 ? 174.209 156.612 206.818 1.00 17.54  ? 3098 SER A CB    1 
ATOM   12401 O  OG    . SER A 1 3098 ? 173.549 156.688 208.068 1.00 15.36  ? 3098 SER A OG    1 
ATOM   12402 N  N     . THR A 1 3099 ? 174.989 153.737 206.595 1.00 16.38  ? 3099 THR A N     1 
ATOM   12403 C  CA    . THR A 1 3099 ? 175.291 152.480 207.268 1.00 15.76  ? 3099 THR A CA    1 
ATOM   12404 C  C     . THR A 1 3099 ? 174.869 152.535 208.730 1.00 16.82  ? 3099 THR A C     1 
ATOM   12405 O  O     . THR A 1 3099 ? 174.325 151.563 209.266 1.00 19.69  ? 3099 THR A O     1 
ATOM   12406 C  CB    . THR A 1 3099 ? 176.782 152.167 207.149 1.00 20.20  ? 3099 THR A CB    1 
ATOM   12407 O  OG1   . THR A 1 3099 ? 177.180 152.256 205.776 1.00 26.47  ? 3099 THR A OG1   1 
ATOM   12408 C  CG2   . THR A 1 3099 ? 177.079 150.771 207.666 1.00 19.17  ? 3099 THR A CG2   1 
ATOM   12409 N  N     . GLU A 1 3100 ? 175.107 153.672 209.387 1.00 17.11  ? 3100 GLU A N     1 
ATOM   12410 C  CA    . GLU A 1 3100 ? 174.658 153.843 210.764 1.00 16.10  ? 3100 GLU A CA    1 
ATOM   12411 C  C     . GLU A 1 3100 ? 173.140 153.782 210.861 1.00 13.70  ? 3100 GLU A C     1 
ATOM   12412 O  O     . GLU A 1 3100 ? 172.596 153.186 211.796 1.00 13.35  ? 3100 GLU A O     1 
ATOM   12413 C  CB    . GLU A 1 3100 ? 175.177 155.167 211.324 1.00 22.57  ? 3100 GLU A CB    1 
ATOM   12414 C  CG    . GLU A 1 3100 ? 174.728 155.458 212.745 1.00 28.07  ? 3100 GLU A CG    1 
ATOM   12415 C  CD    . GLU A 1 3100 ? 174.724 156.939 213.061 1.00 37.41  ? 3100 GLU A CD    1 
ATOM   12416 O  OE1   . GLU A 1 3100 ? 174.701 157.749 212.111 1.00 40.01  ? 3100 GLU A OE1   1 
ATOM   12417 O  OE2   . GLU A 1 3100 ? 174.741 157.294 214.259 1.00 35.26  ? 3100 GLU A OE2   1 
ATOM   12418 N  N     . ALA A 1 3101 ? 172.439 154.402 209.908 1.00 15.24  ? 3101 ALA A N     1 
ATOM   12419 C  CA    . ALA A 1 3101 ? 170.980 154.372 209.925 1.00 13.25  ? 3101 ALA A CA    1 
ATOM   12420 C  C     . ALA A 1 3101 ? 170.453 152.953 209.762 1.00 14.71  ? 3101 ALA A C     1 
ATOM   12421 O  O     . ALA A 1 3101 ? 169.537 152.536 210.482 1.00 15.97  ? 3101 ALA A O     1 
ATOM   12422 C  CB    . ALA A 1 3101 ? 170.425 155.279 208.829 1.00 16.09  ? 3101 ALA A CB    1 
ATOM   12423 N  N     . LEU A 1 3102 ? 171.021 152.195 208.820 1.00 15.60  ? 3102 LEU A N     1 
ATOM   12424 C  CA    . LEU A 1 3102 ? 170.613 150.806 208.637 1.00 9.77   ? 3102 LEU A CA    1 
ATOM   12425 C  C     . LEU A 1 3102 ? 170.903 149.982 209.882 1.00 10.03  ? 3102 LEU A C     1 
ATOM   12426 O  O     . LEU A 1 3102 ? 170.078 149.161 210.300 1.00 13.47  ? 3102 LEU A O     1 
ATOM   12427 C  CB    . LEU A 1 3102 ? 171.326 150.205 207.426 1.00 11.72  ? 3102 LEU A CB    1 
ATOM   12428 C  CG    . LEU A 1 3102 ? 171.032 150.805 206.052 1.00 11.55  ? 3102 LEU A CG    1 
ATOM   12429 C  CD1   . LEU A 1 3102 ? 171.938 150.180 205.009 1.00 12.44  ? 3102 LEU A CD1   1 
ATOM   12430 C  CD2   . LEU A 1 3102 ? 169.573 150.603 205.680 1.00 9.65   ? 3102 LEU A CD2   1 
ATOM   12431 N  N     . TYR A 1 3103 ? 172.073 150.189 210.489 1.00 10.55  ? 3103 TYR A N     1 
ATOM   12432 C  CA    . TYR A 1 3103 ? 172.426 149.448 211.694 1.00 14.38  ? 3103 TYR A CA    1 
ATOM   12433 C  C     . TYR A 1 3103 ? 171.463 149.756 212.833 1.00 12.92  ? 3103 TYR A C     1 
ATOM   12434 O  O     . TYR A 1 3103 ? 171.024 148.848 213.548 1.00 19.36  ? 3103 TYR A O     1 
ATOM   12435 C  CB    . TYR A 1 3103 ? 173.864 149.773 212.096 1.00 17.08  ? 3103 TYR A CB    1 
ATOM   12436 C  CG    . TYR A 1 3103 ? 174.377 148.970 213.267 1.00 22.64  ? 3103 TYR A CG    1 
ATOM   12437 C  CD1   . TYR A 1 3103 ? 174.986 147.739 213.073 1.00 23.62  ? 3103 TYR A CD1   1 
ATOM   12438 C  CD2   . TYR A 1 3103 ? 174.262 149.446 214.564 1.00 23.22  ? 3103 TYR A CD2   1 
ATOM   12439 C  CE1   . TYR A 1 3103 ? 175.456 147.000 214.138 1.00 23.56  ? 3103 TYR A CE1   1 
ATOM   12440 C  CE2   . TYR A 1 3103 ? 174.731 148.717 215.633 1.00 27.27  ? 3103 TYR A CE2   1 
ATOM   12441 C  CZ    . TYR A 1 3103 ? 175.327 147.495 215.416 1.00 30.68  ? 3103 TYR A CZ    1 
ATOM   12442 O  OH    . TYR A 1 3103 ? 175.796 146.765 216.483 1.00 44.43  ? 3103 TYR A OH    1 
ATOM   12443 N  N     . GLN A 1 3104 ? 171.123 151.033 213.018 1.00 12.46  ? 3104 GLN A N     1 
ATOM   12444 C  CA    . GLN A 1 3104 ? 170.196 151.410 214.079 1.00 14.27  ? 3104 GLN A CA    1 
ATOM   12445 C  C     . GLN A 1 3104 ? 168.805 150.847 213.827 1.00 13.48  ? 3104 GLN A C     1 
ATOM   12446 O  O     . GLN A 1 3104 ? 168.151 150.361 214.758 1.00 15.22  ? 3104 GLN A O     1 
ATOM   12447 C  CB    . GLN A 1 3104 ? 170.146 152.930 214.213 1.00 14.40  ? 3104 GLN A CB    1 
ATOM   12448 C  CG    . GLN A 1 3104 ? 171.434 153.543 214.727 1.00 16.13  ? 3104 GLN A CG    1 
ATOM   12449 C  CD    . GLN A 1 3104 ? 171.277 155.000 215.095 1.00 22.30  ? 3104 GLN A CD    1 
ATOM   12450 O  OE1   . GLN A 1 3104 ? 171.917 155.871 214.508 1.00 24.40  ? 3104 GLN A OE1   1 
ATOM   12451 N  NE2   . GLN A 1 3104 ? 170.421 155.276 216.071 1.00 21.59  ? 3104 GLN A NE2   1 
ATOM   12452 N  N     . VAL A 1 3105 ? 168.336 150.901 212.578 1.00 12.62  ? 3105 VAL A N     1 
ATOM   12453 C  CA    . VAL A 1 3105 ? 167.024 150.347 212.251 1.00 10.95  ? 3105 VAL A CA    1 
ATOM   12454 C  C     . VAL A 1 3105 ? 167.002 148.851 212.529 1.00 16.34  ? 3105 VAL A C     1 
ATOM   12455 O  O     . VAL A 1 3105 ? 166.049 148.323 213.115 1.00 21.39  ? 3105 VAL A O     1 
ATOM   12456 C  CB    . VAL A 1 3105 ? 166.661 150.655 210.787 1.00 10.26  ? 3105 VAL A CB    1 
ATOM   12457 C  CG1   . VAL A 1 3105 ? 165.534 149.754 210.316 1.00 14.61  ? 3105 VAL A CG1   1 
ATOM   12458 C  CG2   . VAL A 1 3105 ? 166.272 152.106 210.638 1.00 11.84  ? 3105 VAL A CG2   1 
ATOM   12459 N  N     . GLY A 1 3106 ? 168.057 148.147 212.115 1.00 15.22  ? 3106 GLY A N     1 
ATOM   12460 C  CA    . GLY A 1 3106 ? 168.123 146.719 212.365 1.00 15.63  ? 3106 GLY A CA    1 
ATOM   12461 C  C     . GLY A 1 3106 ? 168.148 146.386 213.843 1.00 19.90  ? 3106 GLY A C     1 
ATOM   12462 O  O     . GLY A 1 3106 ? 167.428 145.497 214.299 1.00 22.81  ? 3106 GLY A O     1 
ATOM   12463 N  N     . LYS A 1 3107 ? 168.968 147.100 214.617 1.00 17.39  ? 3107 LYS A N     1 
ATOM   12464 C  CA    . LYS A 1 3107 ? 169.044 146.824 216.047 1.00 18.08  ? 3107 LYS A CA    1 
ATOM   12465 C  C     . LYS A 1 3107 ? 167.712 147.103 216.732 1.00 20.70  ? 3107 LYS A C     1 
ATOM   12466 O  O     . LYS A 1 3107 ? 167.286 146.350 217.615 1.00 26.40  ? 3107 LYS A O     1 
ATOM   12467 C  CB    . LYS A 1 3107 ? 170.167 147.639 216.689 1.00 18.24  ? 3107 LYS A CB    1 
ATOM   12468 C  CG    . LYS A 1 3107 ? 170.386 147.301 218.157 1.00 24.79  ? 3107 LYS A CG    1 
ATOM   12469 C  CD    . LYS A 1 3107 ? 171.460 148.167 218.786 1.00 29.23  ? 3107 LYS A CD    1 
ATOM   12470 C  CE    . LYS A 1 3107 ? 172.841 147.754 218.313 1.00 32.95  ? 3107 LYS A CE    1 
ATOM   12471 N  NZ    . LYS A 1 3107 ? 173.920 148.512 219.005 1.00 25.13  ? 3107 LYS A NZ    1 
ATOM   12472 N  N     . GLU A 1 3108 ? 167.037 148.186 216.339 1.00 19.99  ? 3108 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3108 ? 165.755 148.512 216.954 1.00 25.69  ? 3108 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3108 ? 164.685 147.487 216.597 1.00 29.49  ? 3108 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3108 ? 163.912 147.061 217.463 1.00 28.86  ? 3108 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3108 ? 165.313 149.913 216.534 1.00 26.10  ? 3108 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3108 ? 163.979 150.338 217.122 1.00 32.72  ? 3108 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3108 ? 164.063 150.602 218.611 1.00 39.44  ? 3108 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3108 ? 164.908 151.424 219.022 1.00 34.43  ? 3108 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3108 ? 163.285 149.986 219.370 1.00 34.14  ? 3108 GLU A OE2   1 
ATOM   12481 N  N     . PHE A 1 3109 ? 164.624 147.075 215.329 1.00 29.63  ? 3109 PHE A N     1 
ATOM   12482 C  CA    . PHE A 1 3109 ? 163.547 146.195 214.891 1.00 29.74  ? 3109 PHE A CA    1 
ATOM   12483 C  C     . PHE A 1 3109 ? 163.773 144.758 215.353 1.00 32.00  ? 3109 PHE A C     1 
ATOM   12484 O  O     . PHE A 1 3109 ? 162.818 144.084 215.754 1.00 35.53  ? 3109 PHE A O     1 
ATOM   12485 C  CB    . PHE A 1 3109 ? 163.415 146.283 213.365 1.00 24.85  ? 3109 PHE A CB    1 
ATOM   12486 C  CG    . PHE A 1 3109 ? 162.141 145.690 212.807 1.00 30.50  ? 3109 PHE A CG    1 
ATOM   12487 C  CD1   . PHE A 1 3109 ? 161.831 144.348 212.960 1.00 33.15  ? 3109 PHE A CD1   1 
ATOM   12488 C  CD2   . PHE A 1 3109 ? 161.251 146.497 212.120 1.00 22.40  ? 3109 PHE A CD2   1 
ATOM   12489 C  CE1   . PHE A 1 3109 ? 160.664 143.827 212.440 1.00 32.50  ? 3109 PHE A CE1   1 
ATOM   12490 C  CE2   . PHE A 1 3109 ? 160.083 145.979 211.598 1.00 24.05  ? 3109 PHE A CE2   1 
ATOM   12491 C  CZ    . PHE A 1 3109 ? 159.790 144.643 211.759 1.00 28.89  ? 3109 PHE A CZ    1 
ATOM   12492 N  N     . THR A 1 3110 ? 165.017 144.284 215.332 1.00 26.59  ? 3110 THR A N     1 
ATOM   12493 C  CA    . THR A 1 3110 ? 165.348 142.919 215.718 1.00 24.92  ? 3110 THR A CA    1 
ATOM   12494 C  C     . THR A 1 3110 ? 165.563 142.750 217.215 1.00 30.49  ? 3110 THR A C     1 
ATOM   12495 O  O     . THR A 1 3110 ? 165.896 141.646 217.657 1.00 36.63  ? 3110 THR A O     1 
ATOM   12496 C  CB    . THR A 1 3110 ? 166.599 142.442 214.969 1.00 28.70  ? 3110 THR A CB    1 
ATOM   12497 O  OG1   . THR A 1 3110 ? 167.760 143.104 215.488 1.00 25.87  ? 3110 THR A OG1   1 
ATOM   12498 C  CG2   . THR A 1 3110 ? 166.472 142.700 213.475 1.00 25.50  ? 3110 THR A CG2   1 
ATOM   12499 N  N     . SER A 1 3111 ? 165.391 143.812 218.005 1.00 31.94  ? 3111 SER A N     1 
ATOM   12500 C  CA    . SER A 1 3111 ? 165.537 143.689 219.451 1.00 37.44  ? 3111 SER A CA    1 
ATOM   12501 C  C     . SER A 1 3111 ? 164.478 142.782 220.063 1.00 39.70  ? 3111 SER A C     1 
ATOM   12502 O  O     . SER A 1 3111 ? 164.692 142.243 221.153 1.00 34.71  ? 3111 SER A O     1 
ATOM   12503 C  CB    . SER A 1 3111 ? 165.474 145.069 220.103 1.00 33.19  ? 3111 SER A CB    1 
ATOM   12504 O  OG    . SER A 1 3111 ? 164.315 145.771 219.689 1.00 32.71  ? 3111 SER A OG    1 
ATOM   12505 N  N     . LYS A 1 3112 ? 163.341 142.605 219.388 1.00 42.41  ? 3112 LYS A N     1 
ATOM   12506 C  CA    . LYS A 1 3112 ? 162.267 141.779 219.927 1.00 37.10  ? 3112 LYS A CA    1 
ATOM   12507 C  C     . LYS A 1 3112 ? 162.575 140.291 219.820 1.00 41.33  ? 3112 LYS A C     1 
ATOM   12508 O  O     . LYS A 1 3112 ? 162.026 139.496 220.590 1.00 42.31  ? 3112 LYS A O     1 
ATOM   12509 C  CB    . LYS A 1 3112 ? 160.942 142.089 219.220 1.00 42.20  ? 3112 LYS A CB    1 
ATOM   12510 C  CG    . LYS A 1 3112 ? 160.676 143.561 218.872 1.00 47.01  ? 3112 LYS A CG    1 
ATOM   12511 C  CD    . LYS A 1 3112 ? 161.099 144.532 219.974 1.00 46.47  ? 3112 LYS A CD    1 
ATOM   12512 C  CE    . LYS A 1 3112 ? 160.387 145.869 219.841 1.00 49.63  ? 3112 LYS A CE    1 
ATOM   12513 N  NZ    . LYS A 1 3112 ? 160.427 146.385 218.444 1.00 47.86  ? 3112 LYS A NZ    1 
ATOM   12514 N  N     . MET A 1 3113 ? 163.433 139.895 218.883 1.00 39.68  ? 3113 MET A N     1 
ATOM   12515 C  CA    . MET A 1 3113 ? 163.759 138.489 218.719 1.00 35.09  ? 3113 MET A CA    1 
ATOM   12516 C  C     . MET A 1 3113 ? 164.789 138.043 219.754 1.00 47.44  ? 3113 MET A C     1 
ATOM   12517 O  O     . MET A 1 3113 ? 165.407 138.849 220.455 1.00 53.22  ? 3113 MET A O     1 
ATOM   12518 C  CB    . MET A 1 3113 ? 164.284 138.211 217.313 1.00 36.32  ? 3113 MET A CB    1 
ATOM   12519 C  CG    . MET A 1 3113 ? 163.263 138.401 216.212 1.00 44.94  ? 3113 MET A CG    1 
ATOM   12520 S  SD    . MET A 1 3113 ? 163.947 137.986 214.600 1.00 58.52  ? 3113 MET A SD    1 
ATOM   12521 C  CE    . MET A 1 3113 ? 165.007 139.386 214.297 1.00 23.20  ? 3113 MET A CE    1 
ATOM   12522 N  N     . ASP A 1 3114 ? 164.971 136.727 219.838 1.00 47.21  ? 3114 ASP A N     1 
ATOM   12523 C  CA    . ASP A 1 3114 ? 165.935 136.111 220.747 1.00 46.23  ? 3114 ASP A CA    1 
ATOM   12524 C  C     . ASP A 1 3114 ? 167.199 135.816 219.946 1.00 46.21  ? 3114 ASP A C     1 
ATOM   12525 O  O     . ASP A 1 3114 ? 167.420 134.697 219.485 1.00 48.83  ? 3114 ASP A O     1 
ATOM   12526 C  CB    . ASP A 1 3114 ? 165.354 134.850 221.376 1.00 55.23  ? 3114 ASP A CB    1 
ATOM   12527 C  CG    . ASP A 1 3114 ? 166.225 134.292 222.488 1.00 60.50  ? 3114 ASP A CG    1 
ATOM   12528 O  OD1   . ASP A 1 3114 ? 167.301 134.868 222.756 1.00 55.74  ? 3114 ASP A OD1   1 
ATOM   12529 O  OD2   . ASP A 1 3114 ? 165.830 133.275 223.095 1.00 61.91  ? 3114 ASP A OD2   1 
ATOM   12530 N  N     . LEU A 1 3115 ? 168.036 136.838 219.782 1.00 46.76  ? 3115 LEU A N     1 
ATOM   12531 C  CA    . LEU A 1 3115 ? 169.305 136.709 219.083 1.00 43.89  ? 3115 LEU A CA    1 
ATOM   12532 C  C     . LEU A 1 3115 ? 170.480 136.535 220.036 1.00 44.43  ? 3115 LEU A C     1 
ATOM   12533 O  O     . LEU A 1 3115 ? 171.633 136.589 219.599 1.00 41.64  ? 3115 LEU A O     1 
ATOM   12534 C  CB    . LEU A 1 3115 ? 169.541 137.924 218.185 1.00 42.20  ? 3115 LEU A CB    1 
ATOM   12535 C  CG    . LEU A 1 3115 ? 168.581 138.101 217.009 1.00 40.58  ? 3115 LEU A CG    1 
ATOM   12536 C  CD1   . LEU A 1 3115 ? 168.848 139.414 216.295 1.00 31.19  ? 3115 LEU A CD1   1 
ATOM   12537 C  CD2   . LEU A 1 3115 ? 168.701 136.933 216.047 1.00 36.18  ? 3115 LEU A CD2   1 
ATOM   12538 N  N     . GLU A 1 3116 ? 170.215 136.326 221.322 1.00 52.42  ? 3116 GLU A N     1 
ATOM   12539 C  CA    . GLU A 1 3116 ? 171.274 136.204 222.317 1.00 55.19  ? 3116 GLU A CA    1 
ATOM   12540 C  C     . GLU A 1 3116 ? 171.853 134.796 222.256 1.00 54.64  ? 3116 GLU A C     1 
ATOM   12541 O  O     . GLU A 1 3116 ? 171.172 133.819 222.584 1.00 56.85  ? 3116 GLU A O     1 
ATOM   12542 C  CB    . GLU A 1 3116 ? 170.732 136.519 223.708 1.00 54.06  ? 3116 GLU A CB    1 
ATOM   12543 C  CG    . GLU A 1 3116 ? 169.885 137.780 223.767 1.00 54.67  ? 3116 GLU A CG    1 
ATOM   12544 C  CD    . GLU A 1 3116 ? 170.719 139.047 223.801 1.00 60.77  ? 3116 GLU A CD    1 
ATOM   12545 O  OE1   . GLU A 1 3116 ? 171.952 138.946 223.968 1.00 68.89  ? 3116 GLU A OE1   1 
ATOM   12546 O  OE2   . GLU A 1 3116 ? 170.141 140.144 223.661 1.00 60.95  ? 3116 GLU A OE2   1 
ATOM   12547 N  N     . LYS A 1 3117 ? 173.110 134.692 221.834 1.00 53.15  ? 3117 LYS A N     1 
ATOM   12548 C  CA    . LYS A 1 3117 ? 173.816 133.414 221.756 1.00 54.25  ? 3117 LYS A CA    1 
ATOM   12549 C  C     . LYS A 1 3117 ? 175.057 133.484 222.634 1.00 57.62  ? 3117 LYS A C     1 
ATOM   12550 O  O     . LYS A 1 3117 ? 176.108 133.979 222.189 1.00 53.24  ? 3117 LYS A O     1 
ATOM   12551 C  CB    . LYS A 1 3117 ? 174.190 133.085 220.312 1.00 47.90  ? 3117 LYS A CB    1 
ATOM   12552 C  CG    . LYS A 1 3117 ? 174.811 131.713 220.129 1.00 54.37  ? 3117 LYS A CG    1 
ATOM   12553 C  CD    . LYS A 1 3117 ? 175.212 131.476 218.685 1.00 49.27  ? 3117 LYS A CD    1 
ATOM   12554 C  CE    . LYS A 1 3117 ? 173.994 131.231 217.810 1.00 48.36  ? 3117 LYS A CE    1 
ATOM   12555 N  NZ    . LYS A 1 3117 ? 174.376 130.880 216.415 1.00 41.94  ? 3117 LYS A NZ    1 
ATOM   12556 N  N     . PRO A 1 3118 ? 174.985 133.024 223.885 1.00 60.54  ? 3118 PRO A N     1 
ATOM   12557 C  CA    . PRO A 1 3118 ? 176.167 133.086 224.761 1.00 61.01  ? 3118 PRO A CA    1 
ATOM   12558 C  C     . PRO A 1 3118 ? 177.351 132.284 224.250 1.00 64.23  ? 3118 PRO A C     1 
ATOM   12559 O  O     . PRO A 1 3118 ? 178.495 132.615 224.586 1.00 62.82  ? 3118 PRO A O     1 
ATOM   12560 C  CB    . PRO A 1 3118 ? 175.648 132.529 226.094 1.00 56.97  ? 3118 PRO A CB    1 
ATOM   12561 C  CG    . PRO A 1 3118 ? 174.164 132.686 226.027 1.00 50.80  ? 3118 PRO A CG    1 
ATOM   12562 C  CD    . PRO A 1 3118 ? 173.802 132.502 224.587 1.00 54.91  ? 3118 PRO A CD    1 
ATOM   12563 N  N     . ASN A 1 3119 ? 177.119 131.251 223.446 1.00 65.48  ? 3119 ASN A N     1 
ATOM   12564 C  CA    . ASN A 1 3119 ? 178.190 130.423 222.912 1.00 69.13  ? 3119 ASN A CA    1 
ATOM   12565 C  C     . ASN A 1 3119 ? 178.818 131.004 221.654 1.00 67.52  ? 3119 ASN A C     1 
ATOM   12566 O  O     . ASN A 1 3119 ? 179.695 130.364 221.065 1.00 71.84  ? 3119 ASN A O     1 
ATOM   12567 C  CB    . ASN A 1 3119 ? 177.671 129.011 222.621 1.00 70.03  ? 3119 ASN A CB    1 
ATOM   12568 C  CG    . ASN A 1 3119 ? 177.395 128.220 223.883 1.00 77.03  ? 3119 ASN A CG    1 
ATOM   12569 O  OD1   . ASN A 1 3119 ? 178.181 128.248 224.830 1.00 82.56  ? 3119 ASN A OD1   1 
ATOM   12570 N  ND2   . ASN A 1 3119 ? 176.274 127.508 223.902 1.00 78.87  ? 3119 ASN A ND2   1 
ATOM   12571 N  N     . TYR A 1 3120 ? 178.384 132.187 221.222 1.00 62.92  ? 3120 TYR A N     1 
ATOM   12572 C  CA    . TYR A 1 3120 ? 178.951 132.805 220.032 1.00 62.80  ? 3120 TYR A CA    1 
ATOM   12573 C  C     . TYR A 1 3120 ? 180.423 133.127 220.248 1.00 57.23  ? 3120 TYR A C     1 
ATOM   12574 O  O     . TYR A 1 3120 ? 180.810 133.656 221.294 1.00 60.15  ? 3120 TYR A O     1 
ATOM   12575 C  CB    . TYR A 1 3120 ? 178.178 134.075 219.678 1.00 50.38  ? 3120 TYR A CB    1 
ATOM   12576 C  CG    . TYR A 1 3120 ? 178.746 134.824 218.496 1.00 44.28  ? 3120 TYR A CG    1 
ATOM   12577 C  CD1   . TYR A 1 3120 ? 178.695 134.282 217.219 1.00 44.21  ? 3120 TYR A CD1   1 
ATOM   12578 C  CD2   . TYR A 1 3120 ? 179.339 136.069 218.656 1.00 46.36  ? 3120 TYR A CD2   1 
ATOM   12579 C  CE1   . TYR A 1 3120 ? 179.214 134.959 216.136 1.00 39.87  ? 3120 TYR A CE1   1 
ATOM   12580 C  CE2   . TYR A 1 3120 ? 179.862 136.754 217.577 1.00 46.09  ? 3120 TYR A CE2   1 
ATOM   12581 C  CZ    . TYR A 1 3120 ? 179.796 136.193 216.319 1.00 44.86  ? 3120 TYR A CZ    1 
ATOM   12582 O  OH    . TYR A 1 3120 ? 180.312 136.866 215.239 1.00 45.96  ? 3120 TYR A OH    1 
ATOM   12583 N  N     . ILE A 1 3121 ? 181.245 132.805 219.254 1.00 51.31  ? 3121 ILE A N     1 
ATOM   12584 C  CA    . ILE A 1 3121 ? 182.679 133.065 219.290 1.00 54.09  ? 3121 ILE A CA    1 
ATOM   12585 C  C     . ILE A 1 3121 ? 183.004 134.039 218.169 1.00 54.25  ? 3121 ILE A C     1 
ATOM   12586 O  O     . ILE A 1 3121 ? 182.787 133.731 216.991 1.00 59.54  ? 3121 ILE A O     1 
ATOM   12587 C  CB    . ILE A 1 3121 ? 183.500 131.773 219.151 1.00 60.09  ? 3121 ILE A CB    1 
ATOM   12588 C  CG1   . ILE A 1 3121 ? 183.301 130.880 220.376 1.00 59.11  ? 3121 ILE A CG1   1 
ATOM   12589 C  CG2   . ILE A 1 3121 ? 184.973 132.093 218.948 1.00 60.97  ? 3121 ILE A CG2   1 
ATOM   12590 C  CD1   . ILE A 1 3121 ? 183.681 131.544 221.680 1.00 60.35  ? 3121 ILE A CD1   1 
ATOM   12591 N  N     . VAL A 1 3122 ? 183.523 135.203 218.533 1.00 49.89  ? 3122 VAL A N     1 
ATOM   12592 C  CA    . VAL A 1 3122 ? 183.867 136.218 217.531 1.00 49.53  ? 3122 VAL A CA    1 
ATOM   12593 C  C     . VAL A 1 3122 ? 185.034 135.714 216.689 1.00 56.98  ? 3122 VAL A C     1 
ATOM   12594 O  O     . VAL A 1 3122 ? 186.046 135.257 217.250 1.00 64.21  ? 3122 VAL A O     1 
ATOM   12595 C  CB    . VAL A 1 3122 ? 184.211 137.543 218.212 1.00 54.62  ? 3122 VAL A CB    1 
ATOM   12596 C  CG1   . VAL A 1 3122 ? 184.563 138.600 217.177 1.00 50.69  ? 3122 VAL A CG1   1 
ATOM   12597 C  CG2   . VAL A 1 3122 ? 183.050 138.008 219.078 1.00 50.66  ? 3122 VAL A CG2   1 
ATOM   12598 N  N     . PRO A 1 3123 ? 184.948 135.768 215.363 1.00 56.54  ? 3123 PRO A N     1 
ATOM   12599 C  CA    . PRO A 1 3123 ? 186.068 135.321 214.533 1.00 63.31  ? 3123 PRO A CA    1 
ATOM   12600 C  C     . PRO A 1 3123 ? 187.278 136.229 214.691 1.00 64.30  ? 3123 PRO A C     1 
ATOM   12601 O  O     . PRO A 1 3123 ? 187.198 137.339 215.222 1.00 62.00  ? 3123 PRO A O     1 
ATOM   12602 C  CB    . PRO A 1 3123 ? 185.506 135.390 213.108 1.00 59.66  ? 3123 PRO A CB    1 
ATOM   12603 C  CG    . PRO A 1 3123 ? 184.399 136.386 213.191 1.00 53.89  ? 3123 PRO A CG    1 
ATOM   12604 C  CD    . PRO A 1 3123 ? 183.797 136.197 214.552 1.00 52.20  ? 3123 PRO A CD    1 
ATOM   12605 N  N     . ASP A 1 3124 ? 188.421 135.724 214.222 1.00 71.67  ? 3124 ASP A N     1 
ATOM   12606 C  CA    . ASP A 1 3124 ? 189.659 136.492 214.307 1.00 71.26  ? 3124 ASP A CA    1 
ATOM   12607 C  C     . ASP A 1 3124 ? 189.558 137.795 213.523 1.00 72.71  ? 3124 ASP A C     1 
ATOM   12608 O  O     . ASP A 1 3124 ? 190.053 138.837 213.969 1.00 71.60  ? 3124 ASP A O     1 
ATOM   12609 C  CB    . ASP A 1 3124 ? 190.835 135.640 213.825 1.00 75.77  ? 3124 ASP A CB    1 
ATOM   12610 C  CG    . ASP A 1 3124 ? 190.697 135.204 212.376 1.00 79.07  ? 3124 ASP A CG    1 
ATOM   12611 O  OD1   . ASP A 1 3124 ? 189.666 135.513 211.744 1.00 72.34  ? 3124 ASP A OD1   1 
ATOM   12612 O  OD2   . ASP A 1 3124 ? 191.628 134.544 211.869 1.00 88.93  ? 3124 ASP A OD2   1 
ATOM   12613 N  N     . TYR A 1 3125 ? 188.923 137.758 212.355 1.00 74.04  ? 3125 TYR A N     1 
ATOM   12614 C  CA    . TYR A 1 3125 ? 188.630 138.956 211.581 1.00 72.09  ? 3125 TYR A CA    1 
ATOM   12615 C  C     . TYR A 1 3125 ? 187.123 139.047 211.380 1.00 73.29  ? 3125 TYR A C     1 
ATOM   12616 O  O     . TYR A 1 3125 ? 186.502 138.098 210.890 1.00 67.86  ? 3125 TYR A O     1 
ATOM   12617 C  CB    . TYR A 1 3125 ? 189.347 138.940 210.232 1.00 65.77  ? 3125 TYR A CB    1 
ATOM   12618 C  CG    . TYR A 1 3125 ? 188.697 139.838 209.205 1.00 72.69  ? 3125 TYR A CG    1 
ATOM   12619 C  CD1   . TYR A 1 3125 ? 188.778 141.220 209.315 1.00 69.56  ? 3125 TYR A CD1   1 
ATOM   12620 C  CD2   . TYR A 1 3125 ? 187.991 139.307 208.134 1.00 74.54  ? 3125 TYR A CD2   1 
ATOM   12621 C  CE1   . TYR A 1 3125 ? 188.182 142.048 208.384 1.00 73.32  ? 3125 TYR A CE1   1 
ATOM   12622 C  CE2   . TYR A 1 3125 ? 187.390 140.128 207.198 1.00 73.72  ? 3125 TYR A CE2   1 
ATOM   12623 C  CZ    . TYR A 1 3125 ? 187.489 141.496 207.327 1.00 77.97  ? 3125 TYR A CZ    1 
ATOM   12624 O  OH    . TYR A 1 3125 ? 186.892 142.315 206.395 1.00 73.94  ? 3125 TYR A OH    1 
ATOM   12625 N  N     . MET A 1 3126 ? 186.542 140.184 211.759 1.00 74.72  ? 3126 MET A N     1 
ATOM   12626 C  CA    . MET A 1 3126 ? 185.119 140.419 211.573 1.00 66.83  ? 3126 MET A CA    1 
ATOM   12627 C  C     . MET A 1 3126 ? 184.896 141.247 210.321 1.00 62.07  ? 3126 MET A C     1 
ATOM   12628 O  O     . MET A 1 3126 ? 185.528 142.304 210.171 1.00 60.50  ? 3126 MET A O     1 
ATOM   12629 C  CB    . MET A 1 3126 ? 184.526 141.130 212.784 1.00 60.96  ? 3126 MET A CB    1 
ATOM   12630 C  CG    . MET A 1 3126 ? 183.019 141.318 212.707 1.00 58.81  ? 3126 MET A CG    1 
ATOM   12631 S  SD    . MET A 1 3126 ? 182.107 139.764 212.743 1.00 66.56  ? 3126 MET A SD    1 
ATOM   12632 C  CE    . MET A 1 3126 ? 182.104 139.416 214.496 1.00 48.75  ? 3126 MET A CE    1 
ATOM   12633 N  N     . PRO A 1 3127 ? 184.028 140.819 209.402 1.00 58.70  ? 3127 PRO A N     1 
ATOM   12634 C  CA    . PRO A 1 3127 ? 183.732 141.650 208.228 1.00 59.47  ? 3127 PRO A CA    1 
ATOM   12635 C  C     . PRO A 1 3127 ? 182.927 142.875 208.622 1.00 57.31  ? 3127 PRO A C     1 
ATOM   12636 O  O     . PRO A 1 3127 ? 181.717 142.943 208.381 1.00 55.20  ? 3127 PRO A O     1 
ATOM   12637 C  CB    . PRO A 1 3127 ? 182.927 140.715 207.314 1.00 53.41  ? 3127 PRO A CB    1 
ATOM   12638 C  CG    . PRO A 1 3127 ? 183.060 139.345 207.904 1.00 52.95  ? 3127 PRO A CG    1 
ATOM   12639 C  CD    . PRO A 1 3127 ? 183.334 139.523 209.358 1.00 49.21  ? 3127 PRO A CD    1 
ATOM   12640 N  N     . VAL A 1 3128 ? 183.597 143.849 209.232 1.00 56.85  ? 3128 VAL A N     1 
ATOM   12641 C  CA    . VAL A 1 3128 ? 182.913 144.995 209.818 1.00 48.01  ? 3128 VAL A CA    1 
ATOM   12642 C  C     . VAL A 1 3128 ? 182.362 145.877 208.706 1.00 47.31  ? 3128 VAL A C     1 
ATOM   12643 O  O     . VAL A 1 3128 ? 183.102 146.332 207.826 1.00 45.47  ? 3128 VAL A O     1 
ATOM   12644 C  CB    . VAL A 1 3128 ? 183.858 145.781 210.736 1.00 55.87  ? 3128 VAL A CB    1 
ATOM   12645 C  CG1   . VAL A 1 3128 ? 183.214 147.085 211.170 1.00 48.63  ? 3128 VAL A CG1   1 
ATOM   12646 C  CG2   . VAL A 1 3128 ? 184.241 144.939 211.945 1.00 51.00  ? 3128 VAL A CG2   1 
ATOM   12647 N  N     . VAL A 1 3129 ? 181.055 146.118 208.741 1.00 46.31  ? 3129 VAL A N     1 
ATOM   12648 C  CA    . VAL A 1 3129 ? 180.400 147.013 207.799 1.00 39.99  ? 3129 VAL A CA    1 
ATOM   12649 C  C     . VAL A 1 3129 ? 180.090 148.361 208.436 1.00 33.29  ? 3129 VAL A C     1 
ATOM   12650 O  O     . VAL A 1 3129 ? 180.320 149.406 207.828 1.00 36.79  ? 3129 VAL A O     1 
ATOM   12651 C  CB    . VAL A 1 3129 ? 179.122 146.353 207.239 1.00 29.03  ? 3129 VAL A CB    1 
ATOM   12652 C  CG1   . VAL A 1 3129 ? 178.492 147.230 206.173 1.00 30.99  ? 3129 VAL A CG1   1 
ATOM   12653 C  CG2   . VAL A 1 3129 ? 179.444 144.980 206.682 1.00 29.57  ? 3129 VAL A CG2   1 
ATOM   12654 N  N     . TYR A 1 3130 ? 179.572 148.351 209.660 1.00 30.29  ? 3130 TYR A N     1 
ATOM   12655 C  CA    . TYR A 1 3130 ? 179.320 149.571 210.416 1.00 36.28  ? 3130 TYR A CA    1 
ATOM   12656 C  C     . TYR A 1 3130 ? 180.603 149.936 211.153 1.00 49.00  ? 3130 TYR A C     1 
ATOM   12657 O  O     . TYR A 1 3130 ? 181.044 149.202 212.043 1.00 54.06  ? 3130 TYR A O     1 
ATOM   12658 C  CB    . TYR A 1 3130 ? 178.158 149.373 211.385 1.00 31.89  ? 3130 TYR A CB    1 
ATOM   12659 C  CG    . TYR A 1 3130 ? 177.850 150.576 212.244 1.00 31.18  ? 3130 TYR A CG    1 
ATOM   12660 C  CD1   . TYR A 1 3130 ? 177.945 151.862 211.733 1.00 28.12  ? 3130 TYR A CD1   1 
ATOM   12661 C  CD2   . TYR A 1 3130 ? 177.459 150.424 213.566 1.00 39.80  ? 3130 TYR A CD2   1 
ATOM   12662 C  CE1   . TYR A 1 3130 ? 177.662 152.962 212.515 1.00 32.50  ? 3130 TYR A CE1   1 
ATOM   12663 C  CE2   . TYR A 1 3130 ? 177.172 151.520 214.356 1.00 37.46  ? 3130 TYR A CE2   1 
ATOM   12664 C  CZ    . TYR A 1 3130 ? 177.274 152.786 213.824 1.00 34.35  ? 3130 TYR A CZ    1 
ATOM   12665 O  OH    . TYR A 1 3130 ? 176.991 153.880 214.607 1.00 44.23  ? 3130 TYR A OH    1 
ATOM   12666 N  N     . ASP A 1 3131 ? 181.197 151.076 210.787 1.00 47.51  ? 3131 ASP A N     1 
ATOM   12667 C  CA    . ASP A 1 3131 ? 182.510 151.433 211.313 1.00 45.20  ? 3131 ASP A CA    1 
ATOM   12668 C  C     . ASP A 1 3131 ? 182.498 151.591 212.827 1.00 42.09  ? 3131 ASP A C     1 
ATOM   12669 O  O     . ASP A 1 3131 ? 183.515 151.343 213.484 1.00 45.25  ? 3131 ASP A O     1 
ATOM   12670 C  CB    . ASP A 1 3131 ? 183.005 152.718 210.650 1.00 52.19  ? 3131 ASP A CB    1 
ATOM   12671 C  CG    . ASP A 1 3131 ? 183.334 152.526 209.183 1.00 60.48  ? 3131 ASP A CG    1 
ATOM   12672 O  OD1   . ASP A 1 3131 ? 183.718 151.401 208.802 1.00 60.60  ? 3131 ASP A OD1   1 
ATOM   12673 O  OD2   . ASP A 1 3131 ? 183.212 153.501 208.413 1.00 68.15  ? 3131 ASP A OD2   1 
ATOM   12674 N  N     . LYS A 1 3132 ? 181.366 151.996 213.400 1.00 40.52  ? 3132 LYS A N     1 
ATOM   12675 C  CA    . LYS A 1 3132 ? 181.243 152.169 214.840 1.00 44.83  ? 3132 LYS A CA    1 
ATOM   12676 C  C     . LYS A 1 3132 ? 180.702 150.924 215.537 1.00 43.08  ? 3132 LYS A C     1 
ATOM   12677 O  O     . LYS A 1 3132 ? 180.136 151.034 216.631 1.00 45.22  ? 3132 LYS A O     1 
ATOM   12678 C  CB    . LYS A 1 3132 ? 180.358 153.377 215.152 1.00 41.14  ? 3132 LYS A CB    1 
ATOM   12679 C  CG    . LYS A 1 3132 ? 180.889 154.687 214.599 1.00 49.78  ? 3132 LYS A CG    1 
ATOM   12680 C  CD    . LYS A 1 3132 ? 182.196 155.076 215.269 1.00 63.81  ? 3132 LYS A CD    1 
ATOM   12681 C  CE    . LYS A 1 3132 ? 182.644 156.465 214.842 1.00 68.88  ? 3132 LYS A CE    1 
ATOM   12682 N  NZ    . LYS A 1 3132 ? 183.062 156.497 213.414 1.00 67.35  ? 3132 LYS A NZ    1 
ATOM   12683 N  N     . LEU A 1 3133 ? 180.855 149.754 214.928 1.00 39.04  ? 3133 LEU A N     1 
ATOM   12684 C  CA    . LEU A 1 3133 ? 180.453 148.520 215.583 1.00 44.54  ? 3133 LEU A CA    1 
ATOM   12685 C  C     . LEU A 1 3133 ? 181.344 148.263 216.797 1.00 49.88  ? 3133 LEU A C     1 
ATOM   12686 O  O     . LEU A 1 3133 ? 182.556 148.498 216.737 1.00 54.30  ? 3133 LEU A O     1 
ATOM   12687 C  CB    . LEU A 1 3133 ? 180.539 147.346 214.607 1.00 41.84  ? 3133 LEU A CB    1 
ATOM   12688 C  CG    . LEU A 1 3133 ? 180.185 145.947 215.113 1.00 43.27  ? 3133 LEU A CG    1 
ATOM   12689 C  CD1   . LEU A 1 3133 ? 178.681 145.744 215.141 1.00 36.12  ? 3133 LEU A CD1   1 
ATOM   12690 C  CD2   . LEU A 1 3133 ? 180.851 144.889 214.249 1.00 48.11  ? 3133 LEU A CD2   1 
ATOM   12691 N  N     . PRO A 1 3134 ? 180.776 147.805 217.912 1.00 44.64  ? 3134 PRO A N     1 
ATOM   12692 C  CA    . PRO A 1 3134 ? 181.596 147.532 219.099 1.00 52.47  ? 3134 PRO A CA    1 
ATOM   12693 C  C     . PRO A 1 3134 ? 182.683 146.506 218.808 1.00 60.61  ? 3134 PRO A C     1 
ATOM   12694 O  O     . PRO A 1 3134 ? 182.469 145.533 218.082 1.00 54.58  ? 3134 PRO A O     1 
ATOM   12695 C  CB    . PRO A 1 3134 ? 180.578 147.005 220.115 1.00 50.67  ? 3134 PRO A CB    1 
ATOM   12696 C  CG    . PRO A 1 3134 ? 179.290 147.633 219.700 1.00 48.98  ? 3134 PRO A CG    1 
ATOM   12697 C  CD    . PRO A 1 3134 ? 179.335 147.693 218.199 1.00 43.24  ? 3134 PRO A CD    1 
ATOM   12698 N  N     . GLN A 1 3135 ? 183.862 146.743 219.387 1.00 68.03  ? 3135 GLN A N     1 
ATOM   12699 C  CA    . GLN A 1 3135 ? 185.017 145.891 219.107 1.00 65.73  ? 3135 GLN A CA    1 
ATOM   12700 C  C     . GLN A 1 3135 ? 184.812 144.442 219.535 1.00 67.53  ? 3135 GLN A C     1 
ATOM   12701 O  O     . GLN A 1 3135 ? 185.201 143.543 218.770 1.00 74.87  ? 3135 GLN A O     1 
ATOM   12702 C  CB    . GLN A 1 3135 ? 186.272 146.497 219.746 1.00 77.10  ? 3135 GLN A CB    1 
ATOM   12703 C  CG    . GLN A 1 3135 ? 186.393 148.007 219.590 1.00 84.00  ? 3135 GLN A CG    1 
ATOM   12704 C  CD    . GLN A 1 3135 ? 186.304 148.458 218.145 1.00 88.78  ? 3135 GLN A CD    1 
ATOM   12705 O  OE1   . GLN A 1 3135 ? 186.899 147.853 217.254 1.00 89.58  ? 3135 GLN A OE1   1 
ATOM   12706 N  NE2   . GLN A 1 3135 ? 185.561 149.533 217.908 1.00 82.01  ? 3135 GLN A NE2   1 
ATOM   12707 N  N     . PRO A 1 3136 ? 184.306 144.135 220.730 1.00 68.72  ? 3136 PRO A N     1 
ATOM   12708 C  CA    . PRO A 1 3136 ? 183.876 142.762 221.022 1.00 63.83  ? 3136 PRO A CA    1 
ATOM   12709 C  C     . PRO A 1 3136 ? 182.399 142.573 220.723 1.00 64.78  ? 3136 PRO A C     1 
ATOM   12710 O  O     . PRO A 1 3136 ? 181.568 142.609 221.643 1.00 67.93  ? 3136 PRO A O     1 
ATOM   12711 C  CB    . PRO A 1 3136 ? 184.167 142.616 222.521 1.00 66.43  ? 3136 PRO A CB    1 
ATOM   12712 C  CG    . PRO A 1 3136 ? 184.031 144.009 223.066 1.00 68.70  ? 3136 PRO A CG    1 
ATOM   12713 C  CD    . PRO A 1 3136 ? 184.177 144.994 221.924 1.00 69.58  ? 3136 PRO A CD    1 
ATOM   12714 N  N     . PRO A 1 3137 ? 182.022 142.371 219.459 1.00 61.87  ? 3137 PRO A N     1 
ATOM   12715 C  CA    . PRO A 1 3137 ? 180.597 142.373 219.120 1.00 50.22  ? 3137 PRO A CA    1 
ATOM   12716 C  C     . PRO A 1 3137 ? 179.895 141.126 219.629 1.00 43.73  ? 3137 PRO A C     1 
ATOM   12717 O  O     . PRO A 1 3137 ? 180.472 140.038 219.675 1.00 51.46  ? 3137 PRO A O     1 
ATOM   12718 C  CB    . PRO A 1 3137 ? 180.602 142.426 217.591 1.00 46.72  ? 3137 PRO A CB    1 
ATOM   12719 C  CG    . PRO A 1 3137 ? 181.841 141.701 217.216 1.00 50.29  ? 3137 PRO A CG    1 
ATOM   12720 C  CD    . PRO A 1 3137 ? 182.832 141.832 218.354 1.00 60.28  ? 3137 PRO A CD    1 
ATOM   12721 N  N     . SER A 1 3138 ? 178.633 141.296 220.012 1.00 39.85  ? 3138 SER A N     1 
ATOM   12722 C  CA    . SER A 1 3138 ? 177.810 140.173 220.425 1.00 39.13  ? 3138 SER A CA    1 
ATOM   12723 C  C     . SER A 1 3138 ? 177.206 139.494 219.198 1.00 42.02  ? 3138 SER A C     1 
ATOM   12724 O  O     . SER A 1 3138 ? 177.454 139.880 218.053 1.00 44.59  ? 3138 SER A O     1 
ATOM   12725 C  CB    . SER A 1 3138 ? 176.724 140.639 221.391 1.00 37.00  ? 3138 SER A CB    1 
ATOM   12726 O  OG    . SER A 1 3138 ? 175.937 141.665 220.813 1.00 37.52  ? 3138 SER A OG    1 
ATOM   12727 N  N     . HIS A 1 3139 ? 176.405 138.455 219.442 1.00 39.63  ? 3139 HIS A N     1 
ATOM   12728 C  CA    . HIS A 1 3139 ? 175.732 137.773 218.341 1.00 36.85  ? 3139 HIS A CA    1 
ATOM   12729 C  C     . HIS A 1 3139 ? 174.731 138.691 217.651 1.00 35.33  ? 3139 HIS A C     1 
ATOM   12730 O  O     . HIS A 1 3139 ? 174.646 138.711 216.418 1.00 31.51  ? 3139 HIS A O     1 
ATOM   12731 C  CB    . HIS A 1 3139 ? 175.040 136.510 218.853 1.00 37.23  ? 3139 HIS A CB    1 
ATOM   12732 C  CG    . HIS A 1 3139 ? 174.542 135.613 217.764 1.00 38.40  ? 3139 HIS A CG    1 
ATOM   12733 N  ND1   . HIS A 1 3139 ? 173.228 135.206 217.678 1.00 37.38  ? 3139 HIS A ND1   1 
ATOM   12734 C  CD2   . HIS A 1 3139 ? 175.181 135.045 216.715 1.00 36.46  ? 3139 HIS A CD2   1 
ATOM   12735 C  CE1   . HIS A 1 3139 ? 173.079 134.426 216.623 1.00 39.66  ? 3139 HIS A CE1   1 
ATOM   12736 N  NE2   . HIS A 1 3139 ? 174.249 134.312 216.021 1.00 38.01  ? 3139 HIS A NE2   1 
ATOM   12737 N  N     . ARG A 1 3140 ? 173.966 139.458 218.431 1.00 33.19  ? 3140 ARG A N     1 
ATOM   12738 C  CA    . ARG A 1 3140 ? 172.960 140.346 217.856 1.00 27.62  ? 3140 ARG A CA    1 
ATOM   12739 C  C     . ARG A 1 3140 ? 173.599 141.414 216.977 1.00 28.95  ? 3140 ARG A C     1 
ATOM   12740 O  O     . ARG A 1 3140 ? 173.100 141.714 215.884 1.00 31.20  ? 3140 ARG A O     1 
ATOM   12741 C  CB    . ARG A 1 3140 ? 172.142 140.987 218.977 1.00 27.01  ? 3140 ARG A CB    1 
ATOM   12742 C  CG    . ARG A 1 3140 ? 170.857 141.651 218.526 1.00 33.31  ? 3140 ARG A CG    1 
ATOM   12743 C  CD    . ARG A 1 3140 ? 170.150 142.309 219.699 1.00 31.86  ? 3140 ARG A CD    1 
ATOM   12744 N  NE    . ARG A 1 3140 ? 169.591 141.326 220.617 1.00 29.03  ? 3140 ARG A NE    1 
ATOM   12745 C  CZ    . ARG A 1 3140 ? 168.422 140.723 220.449 1.00 38.21  ? 3140 ARG A CZ    1 
ATOM   12746 N  NH1   . ARG A 1 3140 ? 167.653 140.985 219.405 1.00 41.16  ? 3140 ARG A NH1   1 
ATOM   12747 N  NH2   . ARG A 1 3140 ? 168.013 139.835 221.350 1.00 47.27  ? 3140 ARG A NH2   1 
ATOM   12748 N  N     . GLU A 1 3141 ? 174.706 141.999 217.438 1.00 29.55  ? 3141 GLU A N     1 
ATOM   12749 C  CA    . GLU A 1 3141 ? 175.393 143.010 216.643 1.00 28.15  ? 3141 GLU A CA    1 
ATOM   12750 C  C     . GLU A 1 3141 ? 175.957 142.412 215.362 1.00 26.07  ? 3141 GLU A C     1 
ATOM   12751 O  O     . GLU A 1 3141 ? 175.928 143.055 214.307 1.00 27.08  ? 3141 GLU A O     1 
ATOM   12752 C  CB    . GLU A 1 3141 ? 176.496 143.665 217.470 1.00 35.18  ? 3141 GLU A CB    1 
ATOM   12753 C  CG    . GLU A 1 3141 ? 175.987 144.354 218.724 1.00 43.45  ? 3141 GLU A CG    1 
ATOM   12754 C  CD    . GLU A 1 3141 ? 177.107 144.818 219.629 1.00 49.16  ? 3141 GLU A CD    1 
ATOM   12755 O  OE1   . GLU A 1 3141 ? 178.283 144.592 219.281 1.00 49.80  ? 3141 GLU A OE1   1 
ATOM   12756 O  OE2   . GLU A 1 3141 ? 176.810 145.408 220.689 1.00 48.86  ? 3141 GLU A OE2   1 
ATOM   12757 N  N     . ALA A 1 3142 ? 176.470 141.182 215.431 1.00 28.86  ? 3142 ALA A N     1 
ATOM   12758 C  CA    . ALA A 1 3142 ? 176.934 140.505 214.225 1.00 27.00  ? 3142 ALA A CA    1 
ATOM   12759 C  C     . ALA A 1 3142 ? 175.787 140.270 213.249 1.00 21.40  ? 3142 ALA A C     1 
ATOM   12760 O  O     . ALA A 1 3142 ? 175.952 140.435 212.035 1.00 19.35  ? 3142 ALA A O     1 
ATOM   12761 C  CB    . ALA A 1 3142 ? 177.609 139.184 214.591 1.00 30.26  ? 3142 ALA A CB    1 
ATOM   12762 N  N     . ILE A 1 3143 ? 174.616 139.887 213.763 1.00 21.56  ? 3143 ILE A N     1 
ATOM   12763 C  CA    . ILE A 1 3143 ? 173.449 139.684 212.907 1.00 18.04  ? 3143 ILE A CA    1 
ATOM   12764 C  C     . ILE A 1 3143 ? 173.061 140.984 212.215 1.00 19.06  ? 3143 ILE A C     1 
ATOM   12765 O  O     . ILE A 1 3143 ? 172.773 141.005 211.010 1.00 17.09  ? 3143 ILE A O     1 
ATOM   12766 C  CB    . ILE A 1 3143 ? 172.277 139.114 213.729 1.00 21.79  ? 3143 ILE A CB    1 
ATOM   12767 C  CG1   . ILE A 1 3143 ? 172.596 137.703 214.229 1.00 24.50  ? 3143 ILE A CG1   1 
ATOM   12768 C  CG2   . ILE A 1 3143 ? 171.002 139.106 212.907 1.00 22.48  ? 3143 ILE A CG2   1 
ATOM   12769 C  CD1   . ILE A 1 3143 ? 172.986 136.739 213.139 1.00 21.78  ? 3143 ILE A CD1   1 
ATOM   12770 N  N     . VAL A 1 3144 ? 173.048 142.089 212.961 1.00 19.60  ? 3144 VAL A N     1 
ATOM   12771 C  CA    . VAL A 1 3144 ? 172.661 143.370 212.373 1.00 16.46  ? 3144 VAL A CA    1 
ATOM   12772 C  C     . VAL A 1 3144 ? 173.694 143.823 211.345 1.00 18.38  ? 3144 VAL A C     1 
ATOM   12773 O  O     . VAL A 1 3144 ? 173.344 144.370 210.290 1.00 22.73  ? 3144 VAL A O     1 
ATOM   12774 C  CB    . VAL A 1 3144 ? 172.448 144.422 213.475 1.00 18.05  ? 3144 VAL A CB    1 
ATOM   12775 C  CG1   . VAL A 1 3144 ? 172.112 145.771 212.864 1.00 20.35  ? 3144 VAL A CG1   1 
ATOM   12776 C  CG2   . VAL A 1 3144 ? 171.346 143.979 214.421 1.00 15.44  ? 3144 VAL A CG2   1 
ATOM   12777 N  N     . ASN A 1 3145 ? 174.979 143.603 211.632 1.00 18.21  ? 3145 ASN A N     1 
ATOM   12778 C  CA    . ASN A 1 3145 ? 176.025 143.931 210.669 1.00 16.52  ? 3145 ASN A CA    1 
ATOM   12779 C  C     . ASN A 1 3145 ? 175.868 143.113 209.394 1.00 19.17  ? 3145 ASN A C     1 
ATOM   12780 O  O     . ASN A 1 3145 ? 176.061 143.628 208.285 1.00 20.70  ? 3145 ASN A O     1 
ATOM   12781 C  CB    . ASN A 1 3145 ? 177.398 143.695 211.298 1.00 25.51  ? 3145 ASN A CB    1 
ATOM   12782 C  CG    . ASN A 1 3145 ? 178.528 144.288 210.481 1.00 34.13  ? 3145 ASN A CG    1 
ATOM   12783 O  OD1   . ASN A 1 3145 ? 178.636 145.505 210.342 1.00 39.34  ? 3145 ASN A OD1   1 
ATOM   12784 N  ND2   . ASN A 1 3145 ? 179.378 143.428 209.937 1.00 30.05  ? 3145 ASN A ND2   1 
ATOM   12785 N  N     . SER A 1 3146 ? 175.518 141.833 209.534 1.00 22.27  ? 3146 SER A N     1 
ATOM   12786 C  CA    . SER A 1 3146 ? 175.274 140.997 208.364 1.00 17.55  ? 3146 SER A CA    1 
ATOM   12787 C  C     . SER A 1 3146 ? 174.073 141.494 207.571 1.00 19.48  ? 3146 SER A C     1 
ATOM   12788 O  O     . SER A 1 3146 ? 174.080 141.457 206.337 1.00 21.29  ? 3146 SER A O     1 
ATOM   12789 C  CB    . SER A 1 3146 ? 175.073 139.547 208.795 1.00 19.49  ? 3146 SER A CB    1 
ATOM   12790 O  OG    . SER A 1 3146 ? 176.253 139.036 209.388 1.00 25.92  ? 3146 SER A OG    1 
ATOM   12791 N  N     . CYS A 1 3147 ? 173.027 141.953 208.261 1.00 14.93  ? 3147 CYS A N     1 
ATOM   12792 C  CA    . CYS A 1 3147 ? 171.876 142.525 207.565 1.00 9.75   ? 3147 CYS A CA    1 
ATOM   12793 C  C     . CYS A 1 3147 ? 172.271 143.768 206.773 1.00 12.65  ? 3147 CYS A C     1 
ATOM   12794 O  O     . CYS A 1 3147 ? 171.840 143.954 205.626 1.00 15.94  ? 3147 CYS A O     1 
ATOM   12795 C  CB    . CYS A 1 3147 ? 170.771 142.861 208.567 1.00 13.57  ? 3147 CYS A CB    1 
ATOM   12796 S  SG    . CYS A 1 3147 ? 170.019 141.435 209.381 1.00 18.28  ? 3147 CYS A SG    1 
ATOM   12797 N  N     . VAL A 1 3148 ? 173.092 144.633 207.373 1.00 13.34  ? 3148 VAL A N     1 
ATOM   12798 C  CA    . VAL A 1 3148 ? 173.553 145.830 206.673 1.00 12.49  ? 3148 VAL A CA    1 
ATOM   12799 C  C     . VAL A 1 3148 ? 174.385 145.448 205.454 1.00 11.54  ? 3148 VAL A C     1 
ATOM   12800 O  O     . VAL A 1 3148 ? 174.245 146.040 204.372 1.00 15.44  ? 3148 VAL A O     1 
ATOM   12801 C  CB    . VAL A 1 3148 ? 174.335 146.745 207.633 1.00 12.21  ? 3148 VAL A CB    1 
ATOM   12802 C  CG1   . VAL A 1 3148 ? 174.911 147.932 206.883 1.00 15.73  ? 3148 VAL A CG1   1 
ATOM   12803 C  CG2   . VAL A 1 3148 ? 173.435 147.220 208.758 1.00 11.78  ? 3148 VAL A CG2   1 
ATOM   12804 N  N     . PHE A 1 3149 ? 175.263 144.453 205.606 1.00 11.89  ? 3149 PHE A N     1 
ATOM   12805 C  CA    . PHE A 1 3149 ? 176.048 143.991 204.467 1.00 15.09  ? 3149 PHE A CA    1 
ATOM   12806 C  C     . PHE A 1 3149 ? 175.149 143.428 203.376 1.00 12.19  ? 3149 PHE A C     1 
ATOM   12807 O  O     . PHE A 1 3149 ? 175.412 143.621 202.185 1.00 12.52  ? 3149 PHE A O     1 
ATOM   12808 C  CB    . PHE A 1 3149 ? 177.063 142.934 204.896 1.00 13.73  ? 3149 PHE A CB    1 
ATOM   12809 C  CG    . PHE A 1 3149 ? 177.763 142.278 203.739 1.00 12.59  ? 3149 PHE A CG    1 
ATOM   12810 C  CD1   . PHE A 1 3149 ? 178.811 142.916 203.101 1.00 14.59  ? 3149 PHE A CD1   1 
ATOM   12811 C  CD2   . PHE A 1 3149 ? 177.349 141.045 203.264 1.00 12.90  ? 3149 PHE A CD2   1 
ATOM   12812 C  CE1   . PHE A 1 3149 ? 179.448 142.328 202.028 1.00 17.21  ? 3149 PHE A CE1   1 
ATOM   12813 C  CE2   . PHE A 1 3149 ? 177.982 140.455 202.190 1.00 15.28  ? 3149 PHE A CE2   1 
ATOM   12814 C  CZ    . PHE A 1 3149 ? 179.033 141.096 201.573 1.00 17.32  ? 3149 PHE A CZ    1 
ATOM   12815 N  N     . VAL A 1 3150 ? 174.096 142.708 203.765 1.00 10.67  ? 3150 VAL A N     1 
ATOM   12816 C  CA    . VAL A 1 3150 ? 173.157 142.167 202.788 1.00 10.65  ? 3150 VAL A CA    1 
ATOM   12817 C  C     . VAL A 1 3150 ? 172.505 143.296 202.006 1.00 13.95  ? 3150 VAL A C     1 
ATOM   12818 O  O     . VAL A 1 3150 ? 172.356 143.219 200.780 1.00 16.56  ? 3150 VAL A O     1 
ATOM   12819 C  CB    . VAL A 1 3150 ? 172.110 141.280 203.488 1.00 10.95  ? 3150 VAL A CB    1 
ATOM   12820 C  CG1   . VAL A 1 3150 ? 170.879 141.108 202.612 1.00 9.47   ? 3150 VAL A CG1   1 
ATOM   12821 C  CG2   . VAL A 1 3150 ? 172.707 139.929 203.841 1.00 14.35  ? 3150 VAL A CG2   1 
ATOM   12822 N  N     . HIS A 1 3151 ? 172.112 144.366 202.700 1.00 12.57  ? 3151 HIS A N     1 
ATOM   12823 C  CA    . HIS A 1 3151 ? 171.518 145.503 202.001 1.00 10.15  ? 3151 HIS A CA    1 
ATOM   12824 C  C     . HIS A 1 3151 ? 172.504 146.138 201.025 1.00 12.02  ? 3151 HIS A C     1 
ATOM   12825 O  O     . HIS A 1 3151 ? 172.142 146.450 199.884 1.00 14.78  ? 3151 HIS A O     1 
ATOM   12826 C  CB    . HIS A 1 3151 ? 171.016 146.547 202.996 1.00 8.13   ? 3151 HIS A CB    1 
ATOM   12827 C  CG    . HIS A 1 3151 ? 170.268 147.672 202.351 1.00 8.19   ? 3151 HIS A CG    1 
ATOM   12828 N  ND1   . HIS A 1 3151 ? 168.963 147.552 201.928 1.00 8.80   ? 3151 HIS A ND1   1 
ATOM   12829 C  CD2   . HIS A 1 3151 ? 170.649 148.933 202.039 1.00 10.13  ? 3151 HIS A CD2   1 
ATOM   12830 C  CE1   . HIS A 1 3151 ? 168.569 148.692 201.392 1.00 8.31   ? 3151 HIS A CE1   1 
ATOM   12831 N  NE2   . HIS A 1 3151 ? 169.574 149.547 201.447 1.00 11.32  ? 3151 HIS A NE2   1 
ATOM   12832 N  N     . GLN A 1 3152 ? 173.754 146.338 201.450 1.00 14.56  ? 3152 GLN A N     1 
ATOM   12833 C  CA    . GLN A 1 3152 ? 174.728 146.975 200.562 1.00 15.24  ? 3152 GLN A CA    1 
ATOM   12834 C  C     . GLN A 1 3152 ? 175.130 146.060 199.409 1.00 18.00  ? 3152 GLN A C     1 
ATOM   12835 O  O     . GLN A 1 3152 ? 175.575 146.539 198.352 1.00 19.11  ? 3152 GLN A O     1 
ATOM   12836 C  CB    . GLN A 1 3152 ? 175.955 147.411 201.360 1.00 18.28  ? 3152 GLN A CB    1 
ATOM   12837 C  CG    . GLN A 1 3152 ? 175.618 148.228 202.595 1.00 15.65  ? 3152 GLN A CG    1 
ATOM   12838 C  CD    . GLN A 1 3152 ? 176.794 149.032 203.103 1.00 22.46  ? 3152 GLN A CD    1 
ATOM   12839 O  OE1   . GLN A 1 3152 ? 177.919 148.537 203.164 1.00 35.23  ? 3152 GLN A OE1   1 
ATOM   12840 N  NE2   . GLN A 1 3152 ? 176.540 150.280 203.478 1.00 20.24  ? 3152 GLN A NE2   1 
ATOM   12841 N  N     . THR A 1 3153 ? 174.978 144.748 199.591 1.00 19.29  ? 3153 THR A N     1 
ATOM   12842 C  CA    . THR A 1 3153 ? 175.255 143.808 198.514 1.00 14.51  ? 3153 THR A CA    1 
ATOM   12843 C  C     . THR A 1 3153 ? 174.329 144.038 197.331 1.00 14.75  ? 3153 THR A C     1 
ATOM   12844 O  O     . THR A 1 3153 ? 174.735 143.844 196.184 1.00 21.19  ? 3153 THR A O     1 
ATOM   12845 C  CB    . THR A 1 3153 ? 175.124 142.374 199.025 1.00 15.27  ? 3153 THR A CB    1 
ATOM   12846 O  OG1   . THR A 1 3153 ? 175.932 142.211 200.196 1.00 18.82  ? 3153 THR A OG1   1 
ATOM   12847 C  CG2   . THR A 1 3153 ? 175.583 141.383 197.969 1.00 23.12  ? 3153 THR A CG2   1 
ATOM   12848 N  N     . LEU A 1 3154 ? 173.091 144.461 197.585 1.00 15.90  ? 3154 LEU A N     1 
ATOM   12849 C  CA    . LEU A 1 3154 ? 172.177 144.753 196.485 1.00 14.11  ? 3154 LEU A CA    1 
ATOM   12850 C  C     . LEU A 1 3154 ? 172.614 145.991 195.714 1.00 17.59  ? 3154 LEU A C     1 
ATOM   12851 O  O     . LEU A 1 3154 ? 172.457 146.048 194.491 1.00 23.54  ? 3154 LEU A O     1 
ATOM   12852 C  CB    . LEU A 1 3154 ? 170.749 144.914 197.002 1.00 10.11  ? 3154 LEU A CB    1 
ATOM   12853 C  CG    . LEU A 1 3154 ? 169.934 143.629 197.173 1.00 8.68   ? 3154 LEU A CG    1 
ATOM   12854 C  CD1   . LEU A 1 3154 ? 169.728 142.965 195.826 1.00 9.11   ? 3154 LEU A CD1   1 
ATOM   12855 C  CD2   . LEU A 1 3154 ? 170.567 142.659 198.156 1.00 10.44  ? 3154 LEU A CD2   1 
ATOM   12856 N  N     . HIS A 1 3155 ? 173.154 146.996 196.406 1.00 20.59  ? 3155 HIS A N     1 
ATOM   12857 C  CA    . HIS A 1 3155 ? 173.714 148.144 195.699 1.00 21.18  ? 3155 HIS A CA    1 
ATOM   12858 C  C     . HIS A 1 3155 ? 174.891 147.728 194.829 1.00 18.77  ? 3155 HIS A C     1 
ATOM   12859 O  O     . HIS A 1 3155 ? 174.995 148.142 193.667 1.00 20.56  ? 3155 HIS A O     1 
ATOM   12860 C  CB    . HIS A 1 3155 ? 174.137 149.222 196.697 1.00 17.26  ? 3155 HIS A CB    1 
ATOM   12861 C  CG    . HIS A 1 3155 ? 172.988 149.953 197.317 1.00 21.46  ? 3155 HIS A CG    1 
ATOM   12862 N  ND1   . HIS A 1 3155 ? 172.730 149.922 198.670 1.00 23.49  ? 3155 HIS A ND1   1 
ATOM   12863 C  CD2   . HIS A 1 3155 ? 172.029 150.735 196.769 1.00 21.11  ? 3155 HIS A CD2   1 
ATOM   12864 C  CE1   . HIS A 1 3155 ? 171.661 150.654 198.929 1.00 25.78  ? 3155 HIS A CE1   1 
ATOM   12865 N  NE2   . HIS A 1 3155 ? 171.216 151.158 197.792 1.00 20.85  ? 3155 HIS A NE2   1 
ATOM   12866 N  N     . GLN A 1 3156 ? 175.783 146.896 195.373 1.00 25.78  ? 3156 GLN A N     1 
ATOM   12867 C  CA    . GLN A 1 3156 ? 176.901 146.395 194.574 1.00 23.92  ? 3156 GLN A CA    1 
ATOM   12868 C  C     . GLN A 1 3156 ? 176.403 145.596 193.374 1.00 23.58  ? 3156 GLN A C     1 
ATOM   12869 O  O     . GLN A 1 3156 ? 176.934 145.722 192.263 1.00 26.56  ? 3156 GLN A O     1 
ATOM   12870 C  CB    . GLN A 1 3156 ? 177.825 145.540 195.440 1.00 23.91  ? 3156 GLN A CB    1 
ATOM   12871 C  CG    . GLN A 1 3156 ? 178.431 146.275 196.621 1.00 26.70  ? 3156 GLN A CG    1 
ATOM   12872 C  CD    . GLN A 1 3156 ? 178.899 145.333 197.713 1.00 39.52  ? 3156 GLN A CD    1 
ATOM   12873 O  OE1   . GLN A 1 3156 ? 178.901 145.683 198.893 1.00 38.19  ? 3156 GLN A OE1   1 
ATOM   12874 N  NE2   . GLN A 1 3156 ? 179.298 144.127 197.324 1.00 33.78  ? 3156 GLN A NE2   1 
ATOM   12875 N  N     . ALA A 1 3157 ? 175.376 144.773 193.584 1.00 25.17  ? 3157 ALA A N     1 
ATOM   12876 C  CA    . ALA A 1 3157 ? 174.799 143.973 192.511 1.00 23.44  ? 3157 ALA A CA    1 
ATOM   12877 C  C     . ALA A 1 3157 ? 174.200 144.849 191.421 1.00 27.63  ? 3157 ALA A C     1 
ATOM   12878 O  O     . ALA A 1 3157 ? 174.402 144.592 190.229 1.00 33.99  ? 3157 ALA A O     1 
ATOM   12879 C  CB    . ALA A 1 3157 ? 173.735 143.043 193.087 1.00 18.15  ? 3157 ALA A CB    1 
ATOM   12880 N  N     . ASN A 1 3158 ? 173.446 145.876 191.811 1.00 25.72  ? 3158 ASN A N     1 
ATOM   12881 C  CA    . ASN A 1 3158 ? 172.852 146.770 190.827 1.00 23.85  ? 3158 ASN A CA    1 
ATOM   12882 C  C     . ASN A 1 3158 ? 173.927 147.521 190.060 1.00 30.83  ? 3158 ASN A C     1 
ATOM   12883 O  O     . ASN A 1 3158 ? 173.788 147.748 188.855 1.00 36.28  ? 3158 ASN A O     1 
ATOM   12884 C  CB    . ASN A 1 3158 ? 171.892 147.740 191.511 1.00 24.71  ? 3158 ASN A CB    1 
ATOM   12885 C  CG    . ASN A 1 3158 ? 170.498 147.173 191.642 1.00 23.06  ? 3158 ASN A CG    1 
ATOM   12886 O  OD1   . ASN A 1 3158 ? 169.610 147.494 190.857 1.00 23.45  ? 3158 ASN A OD1   1 
ATOM   12887 N  ND2   . ASN A 1 3158 ? 170.300 146.316 192.635 1.00 19.87  ? 3158 ASN A ND2   1 
ATOM   12888 N  N     . ALA A 1 3159 ? 175.015 147.901 190.735 1.00 35.82  ? 3159 ALA A N     1 
ATOM   12889 C  CA    . ALA A 1 3159 ? 176.142 148.496 190.026 1.00 29.99  ? 3159 ALA A CA    1 
ATOM   12890 C  C     . ALA A 1 3159 ? 176.723 147.525 189.004 1.00 31.65  ? 3159 ALA A C     1 
ATOM   12891 O  O     . ALA A 1 3159 ? 177.043 147.916 187.875 1.00 37.33  ? 3159 ALA A O     1 
ATOM   12892 C  CB    . ALA A 1 3159 ? 177.217 148.937 191.019 1.00 22.38  ? 3159 ALA A CB    1 
ATOM   12893 N  N     . ARG A 1 3160 ? 176.865 146.253 189.384 1.00 29.46  ? 3160 ARG A N     1 
ATOM   12894 C  CA    . ARG A 1 3160 ? 177.423 145.265 188.463 1.00 33.51  ? 3160 ARG A CA    1 
ATOM   12895 C  C     . ARG A 1 3160 ? 176.524 145.054 187.247 1.00 41.21  ? 3160 ARG A C     1 
ATOM   12896 O  O     . ARG A 1 3160 ? 177.014 144.967 186.115 1.00 45.51  ? 3160 ARG A O     1 
ATOM   12897 C  CB    . ARG A 1 3160 ? 177.681 143.950 189.198 1.00 37.43  ? 3160 ARG A CB    1 
ATOM   12898 C  CG    . ARG A 1 3160 ? 178.078 142.795 188.293 1.00 42.05  ? 3160 ARG A CG    1 
ATOM   12899 C  CD    . ARG A 1 3160 ? 178.208 141.497 189.075 1.00 51.14  ? 3160 ARG A CD    1 
ATOM   12900 N  NE    . ARG A 1 3160 ? 177.345 141.468 190.250 1.00 49.23  ? 3160 ARG A NE    1 
ATOM   12901 C  CZ    . ARG A 1 3160 ? 177.709 140.979 191.428 1.00 50.51  ? 3160 ARG A CZ    1 
ATOM   12902 N  NH1   . ARG A 1 3160 ? 178.910 140.458 191.618 1.00 62.11  ? 3160 ARG A NH1   1 
ATOM   12903 N  NH2   . ARG A 1 3160 ? 176.850 141.018 192.441 1.00 37.40  ? 3160 ARG A NH2   1 
ATOM   12904 N  N     . LEU A 1 3161 ? 175.207 144.961 187.455 1.00 39.32  ? 3161 LEU A N     1 
ATOM   12905 C  CA    . LEU A 1 3161 ? 174.294 144.888 186.311 1.00 37.24  ? 3161 LEU A CA    1 
ATOM   12906 C  C     . LEU A 1 3161 ? 174.331 146.164 185.477 1.00 39.10  ? 3161 LEU A C     1 
ATOM   12907 O  O     . LEU A 1 3161 ? 174.173 146.113 184.252 1.00 43.23  ? 3161 LEU A O     1 
ATOM   12908 C  CB    . LEU A 1 3161 ? 172.859 144.587 186.753 1.00 38.56  ? 3161 LEU A CB    1 
ATOM   12909 C  CG    . LEU A 1 3161 ? 172.413 143.168 187.135 1.00 42.07  ? 3161 LEU A CG    1 
ATOM   12910 C  CD1   . LEU A 1 3161 ? 172.966 142.665 188.450 1.00 41.00  ? 3161 LEU A CD1   1 
ATOM   12911 C  CD2   . LEU A 1 3161 ? 170.891 143.097 187.134 1.00 40.96  ? 3161 LEU A CD2   1 
ATOM   12912 N  N     . ALA A 1 3162 ? 174.520 147.319 186.119 1.00 35.39  ? 3162 ALA A N     1 
ATOM   12913 C  CA    . ALA A 1 3162 ? 174.621 148.568 185.371 1.00 39.07  ? 3162 ALA A CA    1 
ATOM   12914 C  C     . ALA A 1 3162 ? 175.841 148.565 184.461 1.00 48.21  ? 3162 ALA A C     1 
ATOM   12915 O  O     . ALA A 1 3162 ? 175.771 149.015 183.311 1.00 47.00  ? 3162 ALA A O     1 
ATOM   12916 C  CB    . ALA A 1 3162 ? 174.671 149.753 186.334 1.00 32.50  ? 3162 ALA A CB    1 
ATOM   12917 N  N     . LYS A 1 3163 ? 176.972 148.060 184.958 1.00 48.18  ? 3163 LYS A N     1 
ATOM   12918 C  CA    . LYS A 1 3163 ? 178.179 148.008 184.144 1.00 44.33  ? 3163 LYS A CA    1 
ATOM   12919 C  C     . LYS A 1 3163 ? 178.075 146.983 183.022 1.00 47.62  ? 3163 LYS A C     1 
ATOM   12920 O  O     . LYS A 1 3163 ? 178.827 147.076 182.046 1.00 54.27  ? 3163 LYS A O     1 
ATOM   12921 C  CB    . LYS A 1 3163 ? 179.398 147.707 185.018 1.00 43.80  ? 3163 LYS A CB    1 
ATOM   12922 C  CG    . LYS A 1 3163 ? 179.578 148.658 186.193 1.00 44.95  ? 3163 LYS A CG    1 
ATOM   12923 C  CD    . LYS A 1 3163 ? 179.343 150.106 185.788 1.00 43.96  ? 3163 LYS A CD    1 
ATOM   12924 C  CE    . LYS A 1 3163 ? 178.853 150.936 186.964 1.00 41.47  ? 3163 LYS A CE    1 
ATOM   12925 N  NZ    . LYS A 1 3163 ? 179.727 150.789 188.161 1.00 33.92  ? 3163 LYS A NZ    1 
ATOM   12926 N  N     . ARG A 1 3164 ? 177.172 146.011 183.137 1.00 47.65  ? 3164 ARG A N     1 
ATOM   12927 C  CA    . ARG A 1 3164 ? 176.948 145.032 182.083 1.00 45.87  ? 3164 ARG A CA    1 
ATOM   12928 C  C     . ARG A 1 3164 ? 175.796 145.407 181.159 1.00 48.04  ? 3164 ARG A C     1 
ATOM   12929 O  O     . ARG A 1 3164 ? 175.473 144.635 180.251 1.00 44.62  ? 3164 ARG A O     1 
ATOM   12930 C  CB    . ARG A 1 3164 ? 176.697 143.644 182.684 1.00 46.71  ? 3164 ARG A CB    1 
ATOM   12931 C  CG    . ARG A 1 3164 ? 177.913 143.034 183.363 1.00 46.07  ? 3164 ARG A CG    1 
ATOM   12932 C  CD    . ARG A 1 3164 ? 177.628 141.627 183.869 1.00 53.35  ? 3164 ARG A CD    1 
ATOM   12933 N  NE    . ARG A 1 3164 ? 176.693 141.601 184.987 1.00 61.45  ? 3164 ARG A NE    1 
ATOM   12934 C  CZ    . ARG A 1 3164 ? 175.473 141.085 184.927 1.00 59.96  ? 3164 ARG A CZ    1 
ATOM   12935 N  NH1   . ARG A 1 3164 ? 174.996 140.564 183.808 1.00 58.02  ? 3164 ARG A NH1   1 
ATOM   12936 N  NH2   . ARG A 1 3164 ? 174.712 141.089 186.018 1.00 59.90  ? 3164 ARG A NH2   1 
ATOM   12937 N  N     . GLY A 1 3165 ? 175.165 146.560 181.371 1.00 46.85  ? 3165 GLY A N     1 
ATOM   12938 C  CA    . GLY A 1 3165 ? 174.128 147.018 180.470 1.00 45.80  ? 3165 GLY A CA    1 
ATOM   12939 C  C     . GLY A 1 3165 ? 172.757 146.422 180.687 1.00 53.02  ? 3165 GLY A C     1 
ATOM   12940 O  O     . GLY A 1 3165 ? 171.927 146.465 179.774 1.00 52.40  ? 3165 GLY A O     1 
ATOM   12941 N  N     . GLY A 1 3166 ? 172.490 145.861 181.866 1.00 57.54  ? 3166 GLY A N     1 
ATOM   12942 C  CA    . GLY A 1 3166 ? 171.195 145.298 182.171 1.00 47.65  ? 3166 GLY A CA    1 
ATOM   12943 C  C     . GLY A 1 3166 ? 170.313 146.258 182.948 1.00 38.33  ? 3166 GLY A C     1 
ATOM   12944 O  O     . GLY A 1 3166 ? 170.787 147.212 183.559 1.00 39.20  ? 3166 GLY A O     1 
ATOM   12945 N  N     . ARG A 1 3167 ? 169.009 145.991 182.913 1.00 40.14  ? 3167 ARG A N     1 
ATOM   12946 C  CA    . ARG A 1 3167 ? 168.058 146.809 183.655 1.00 39.23  ? 3167 ARG A CA    1 
ATOM   12947 C  C     . ARG A 1 3167 ? 168.252 146.609 185.152 1.00 38.07  ? 3167 ARG A C     1 
ATOM   12948 O  O     . ARG A 1 3167 ? 168.406 145.479 185.624 1.00 39.21  ? 3167 ARG A O     1 
ATOM   12949 C  CB    . ARG A 1 3167 ? 166.622 146.463 183.262 1.00 41.52  ? 3167 ARG A CB    1 
ATOM   12950 C  CG    . ARG A 1 3167 ? 166.172 147.017 181.918 1.00 51.08  ? 3167 ARG A CG    1 
ATOM   12951 C  CD    . ARG A 1 3167 ? 166.574 146.109 180.766 1.00 55.42  ? 3167 ARG A CD    1 
ATOM   12952 N  NE    . ARG A 1 3167 ? 165.950 146.517 179.513 1.00 59.62  ? 3167 ARG A NE    1 
ATOM   12953 C  CZ    . ARG A 1 3167 ? 166.512 147.326 178.626 1.00 61.68  ? 3167 ARG A CZ    1 
ATOM   12954 N  NH1   . ARG A 1 3167 ? 167.715 147.839 178.824 1.00 62.96  ? 3167 ARG A NH1   1 
ATOM   12955 N  NH2   . ARG A 1 3167 ? 165.851 147.627 177.512 1.00 55.97  ? 3167 ARG A NH2   1 
ATOM   12956 N  N     . THR A 1 3168 ? 168.244 147.710 185.897 1.00 33.80  ? 3168 THR A N     1 
ATOM   12957 C  CA    . THR A 1 3168 ? 168.419 147.688 187.341 1.00 25.49  ? 3168 THR A CA    1 
ATOM   12958 C  C     . THR A 1 3168 ? 167.257 148.407 188.010 1.00 21.92  ? 3168 THR A C     1 
ATOM   12959 O  O     . THR A 1 3168 ? 166.819 149.464 187.546 1.00 26.10  ? 3168 THR A O     1 
ATOM   12960 C  CB    . THR A 1 3168 ? 169.740 148.345 187.755 1.00 28.22  ? 3168 THR A CB    1 
ATOM   12961 O  OG1   . THR A 1 3168 ? 169.743 149.718 187.349 1.00 40.95  ? 3168 THR A OG1   1 
ATOM   12962 C  CG2   . THR A 1 3168 ? 170.914 147.632 187.112 1.00 33.69  ? 3168 THR A CG2   1 
ATOM   12963 N  N     . MET A 1 3169 ? 166.763 147.828 189.099 1.00 21.09  ? 3169 MET A N     1 
ATOM   12964 C  CA    . MET A 1 3169 ? 165.707 148.431 189.897 1.00 19.36  ? 3169 MET A CA    1 
ATOM   12965 C  C     . MET A 1 3169 ? 166.302 149.039 191.159 1.00 15.40  ? 3169 MET A C     1 
ATOM   12966 O  O     . MET A 1 3169 ? 167.194 148.457 191.782 1.00 14.87  ? 3169 MET A O     1 
ATOM   12967 C  CB    . MET A 1 3169 ? 164.636 147.400 190.260 1.00 20.68  ? 3169 MET A CB    1 
ATOM   12968 C  CG    . MET A 1 3169 ? 163.892 146.841 189.060 1.00 22.73  ? 3169 MET A CG    1 
ATOM   12969 S  SD    . MET A 1 3169 ? 163.044 148.131 188.129 1.00 35.08  ? 3169 MET A SD    1 
ATOM   12970 C  CE    . MET A 1 3169 ? 163.008 147.415 186.491 1.00 18.53  ? 3169 MET A CE    1 
ATOM   12971 N  N     . ALA A 1 3170 ? 165.804 150.216 191.528 1.00 14.84  ? 3170 ALA A N     1 
ATOM   12972 C  CA    . ALA A 1 3170 ? 166.353 150.943 192.662 1.00 13.99  ? 3170 ALA A CA    1 
ATOM   12973 C  C     . ALA A 1 3170 ? 166.146 150.173 193.959 1.00 15.41  ? 3170 ALA A C     1 
ATOM   12974 O  O     . ALA A 1 3170 ? 165.083 149.593 194.196 1.00 19.63  ? 3170 ALA A O     1 
ATOM   12975 C  CB    . ALA A 1 3170 ? 165.708 152.324 192.765 1.00 12.88  ? 3170 ALA A CB    1 
ATOM   12976 N  N     . ILE A 1 3171 ? 167.174 150.169 194.802 1.00 10.63  ? 3171 ILE A N     1 
ATOM   12977 C  CA    . ILE A 1 3171 ? 167.119 149.540 196.115 1.00 10.70  ? 3171 ILE A CA    1 
ATOM   12978 C  C     . ILE A 1 3171 ? 166.913 150.638 197.147 1.00 11.24  ? 3171 ILE A C     1 
ATOM   12979 O  O     . ILE A 1 3171 ? 167.770 151.512 197.317 1.00 17.30  ? 3171 ILE A O     1 
ATOM   12980 C  CB    . ILE A 1 3171 ? 168.393 148.733 196.407 1.00 12.72  ? 3171 ILE A CB    1 
ATOM   12981 C  CG1   . ILE A 1 3171 ? 168.654 147.724 195.288 1.00 11.30  ? 3171 ILE A CG1   1 
ATOM   12982 C  CG2   . ILE A 1 3171 ? 168.277 148.029 197.748 1.00 12.71  ? 3171 ILE A CG2   1 
ATOM   12983 C  CD1   . ILE A 1 3171 ? 167.582 146.670 195.149 1.00 7.74   ? 3171 ILE A CD1   1 
ATOM   12984 N  N     . THR A 1 3172 ? 165.784 150.592 197.833 1.00 12.84  ? 3172 THR A N     1 
ATOM   12985 C  CA    . THR A 1 3172 ? 165.339 151.627 198.746 1.00 11.62  ? 3172 THR A CA    1 
ATOM   12986 C  C     . THR A 1 3172 ? 165.411 151.152 200.191 1.00 8.63   ? 3172 THR A C     1 
ATOM   12987 O  O     . THR A 1 3172 ? 165.563 149.957 200.461 1.00 10.01  ? 3172 THR A O     1 
ATOM   12988 C  CB    . THR A 1 3172 ? 163.904 152.042 198.402 1.00 11.34  ? 3172 THR A CB    1 
ATOM   12989 O  OG1   . THR A 1 3172 ? 162.995 151.013 198.810 1.00 13.74  ? 3172 THR A OG1   1 
ATOM   12990 C  CG2   . THR A 1 3172 ? 163.763 152.269 196.906 1.00 11.58  ? 3172 THR A CG2   1 
ATOM   12991 N  N     . PRO A 1 3173 ? 165.325 152.073 201.156 1.00 8.86   ? 3173 PRO A N     1 
ATOM   12992 C  CA    . PRO A 1 3173 ? 165.200 151.646 202.558 1.00 7.84   ? 3173 PRO A CA    1 
ATOM   12993 C  C     . PRO A 1 3173 ? 163.963 150.807 202.824 1.00 7.31   ? 3173 PRO A C     1 
ATOM   12994 O  O     . PRO A 1 3173 ? 163.942 150.054 203.806 1.00 9.51   ? 3173 PRO A O     1 
ATOM   12995 C  CB    . PRO A 1 3173 ? 165.154 152.974 203.323 1.00 8.85   ? 3173 PRO A CB    1 
ATOM   12996 C  CG    . PRO A 1 3173 ? 165.890 153.924 202.451 1.00 7.54   ? 3173 PRO A CG    1 
ATOM   12997 C  CD    . PRO A 1 3173 ? 165.562 153.524 201.045 1.00 11.11  ? 3173 PRO A CD    1 
ATOM   12998 N  N     . ARG A 1 3174 ? 162.930 150.917 201.986 1.00 8.68   ? 3174 ARG A N     1 
ATOM   12999 C  CA    . ARG A 1 3174 ? 161.778 150.033 202.111 1.00 8.83   ? 3174 ARG A CA    1 
ATOM   13000 C  C     . ARG A 1 3174 ? 162.166 148.580 201.877 1.00 8.20   ? 3174 ARG A C     1 
ATOM   13001 O  O     . ARG A 1 3174 ? 161.585 147.677 202.488 1.00 10.77  ? 3174 ARG A O     1 
ATOM   13002 C  CB    . ARG A 1 3174 ? 160.683 150.462 201.134 1.00 10.52  ? 3174 ARG A CB    1 
ATOM   13003 C  CG    . ARG A 1 3174 ? 160.047 151.797 201.474 1.00 10.32  ? 3174 ARG A CG    1 
ATOM   13004 C  CD    . ARG A 1 3174 ? 158.684 151.943 200.827 1.00 11.21  ? 3174 ARG A CD    1 
ATOM   13005 N  NE    . ARG A 1 3174 ? 157.671 151.132 201.488 1.00 11.54  ? 3174 ARG A NE    1 
ATOM   13006 C  CZ    . ARG A 1 3174 ? 156.380 151.159 201.189 1.00 14.67  ? 3174 ARG A CZ    1 
ATOM   13007 N  NH1   . ARG A 1 3174 ? 155.908 151.948 200.238 1.00 14.05  ? 3174 ARG A NH1   1 
ATOM   13008 N  NH2   . ARG A 1 3174 ? 155.542 150.373 201.858 1.00 16.71  ? 3174 ARG A NH2   1 
ATOM   13009 N  N     . HIS A 1 3175 ? 163.148 148.337 201.005 1.00 8.11   ? 3175 HIS A N     1 
ATOM   13010 C  CA    . HIS A 1 3175 ? 163.676 146.986 200.842 1.00 8.96   ? 3175 HIS A CA    1 
ATOM   13011 C  C     . HIS A 1 3175 ? 164.268 146.474 202.148 1.00 8.87   ? 3175 HIS A C     1 
ATOM   13012 O  O     . HIS A 1 3175 ? 164.032 145.326 202.540 1.00 11.45  ? 3175 HIS A O     1 
ATOM   13013 C  CB    . HIS A 1 3175 ? 164.737 146.964 199.742 1.00 9.37   ? 3175 HIS A CB    1 
ATOM   13014 C  CG    . HIS A 1 3175 ? 164.189 147.147 198.363 1.00 8.27   ? 3175 HIS A CG    1 
ATOM   13015 N  ND1   . HIS A 1 3175 ? 163.515 148.284 197.975 1.00 10.98  ? 3175 HIS A ND1   1 
ATOM   13016 C  CD2   . HIS A 1 3175 ? 164.226 146.342 197.276 1.00 9.62   ? 3175 HIS A CD2   1 
ATOM   13017 C  CE1   . HIS A 1 3175 ? 163.156 148.169 196.709 1.00 12.56  ? 3175 HIS A CE1   1 
ATOM   13018 N  NE2   . HIS A 1 3175 ? 163.575 147.000 196.262 1.00 12.04  ? 3175 HIS A NE2   1 
ATOM   13019 N  N     . TYR A 1 3176 ? 165.043 147.318 202.834 1.00 7.23   ? 3176 TYR A N     1 
ATOM   13020 C  CA    . TYR A 1 3176 ? 165.620 146.928 204.115 1.00 7.09   ? 3176 TYR A CA    1 
ATOM   13021 C  C     . TYR A 1 3176 ? 164.535 146.668 205.150 1.00 8.19   ? 3176 TYR A C     1 
ATOM   13022 O  O     . TYR A 1 3176 ? 164.626 145.713 205.932 1.00 10.33  ? 3176 TYR A O     1 
ATOM   13023 C  CB    . TYR A 1 3176 ? 166.578 148.014 204.602 1.00 8.14   ? 3176 TYR A CB    1 
ATOM   13024 C  CG    . TYR A 1 3176 ? 167.419 147.611 205.791 1.00 8.57   ? 3176 TYR A CG    1 
ATOM   13025 C  CD1   . TYR A 1 3176 ? 168.476 146.726 205.646 1.00 8.75   ? 3176 TYR A CD1   1 
ATOM   13026 C  CD2   . TYR A 1 3176 ? 167.154 148.114 207.057 1.00 7.37   ? 3176 TYR A CD2   1 
ATOM   13027 C  CE1   . TYR A 1 3176 ? 169.248 146.355 206.726 1.00 10.67  ? 3176 TYR A CE1   1 
ATOM   13028 C  CE2   . TYR A 1 3176 ? 167.920 147.748 208.143 1.00 7.80   ? 3176 TYR A CE2   1 
ATOM   13029 C  CZ    . TYR A 1 3176 ? 168.965 146.869 207.972 1.00 12.05  ? 3176 TYR A CZ    1 
ATOM   13030 O  OH    . TYR A 1 3176 ? 169.734 146.498 209.050 1.00 17.28  ? 3176 TYR A OH    1 
ATOM   13031 N  N     . LEU A 1 3177 ? 163.506 147.517 205.180 1.00 7.33   ? 3177 LEU A N     1 
ATOM   13032 C  CA    . LEU A 1 3177 ? 162.418 147.321 206.132 1.00 8.98   ? 3177 LEU A CA    1 
ATOM   13033 C  C     . LEU A 1 3177 ? 161.686 146.010 205.870 1.00 10.02  ? 3177 LEU A C     1 
ATOM   13034 O  O     . LEU A 1 3177 ? 161.354 145.278 206.810 1.00 17.08  ? 3177 LEU A O     1 
ATOM   13035 C  CB    . LEU A 1 3177 ? 161.454 148.505 206.078 1.00 8.99   ? 3177 LEU A CB    1 
ATOM   13036 C  CG    . LEU A 1 3177 ? 162.055 149.852 206.483 1.00 10.30  ? 3177 LEU A CG    1 
ATOM   13037 C  CD1   . LEU A 1 3177 ? 161.183 151.002 206.008 1.00 11.72  ? 3177 LEU A CD1   1 
ATOM   13038 C  CD2   . LEU A 1 3177 ? 162.257 149.917 207.986 1.00 8.32   ? 3177 LEU A CD2   1 
ATOM   13039 N  N     . ASP A 1 3178 ? 161.436 145.691 204.596 1.00 9.45   ? 3178 ASP A N     1 
ATOM   13040 C  CA    . ASP A 1 3178 ? 160.829 144.406 204.263 1.00 10.00  ? 3178 ASP A CA    1 
ATOM   13041 C  C     . ASP A 1 3178 ? 161.728 143.251 204.672 1.00 11.21  ? 3178 ASP A C     1 
ATOM   13042 O  O     . ASP A 1 3178 ? 161.246 142.224 205.159 1.00 13.56  ? 3178 ASP A O     1 
ATOM   13043 C  CB    . ASP A 1 3178 ? 160.533 144.321 202.769 1.00 11.16  ? 3178 ASP A CB    1 
ATOM   13044 C  CG    . ASP A 1 3178 ? 159.431 145.251 202.339 1.00 26.92  ? 3178 ASP A CG    1 
ATOM   13045 O  OD1   . ASP A 1 3178 ? 158.538 145.548 203.159 1.00 34.14  ? 3178 ASP A OD1   1 
ATOM   13046 O  OD2   . ASP A 1 3178 ? 159.457 145.673 201.169 1.00 35.31  ? 3178 ASP A OD2   1 
ATOM   13047 N  N     . PHE A 1 3179 ? 163.037 143.390 204.455 1.00 9.45   ? 3179 PHE A N     1 
ATOM   13048 C  CA    . PHE A 1 3179 ? 163.962 142.322 204.815 1.00 7.19   ? 3179 PHE A CA    1 
ATOM   13049 C  C     . PHE A 1 3179 ? 163.927 142.058 206.314 1.00 11.72  ? 3179 PHE A C     1 
ATOM   13050 O  O     . PHE A 1 3179 ? 163.859 140.903 206.747 1.00 16.01  ? 3179 PHE A O     1 
ATOM   13051 C  CB    . PHE A 1 3179 ? 165.373 142.687 204.346 1.00 8.22   ? 3179 PHE A CB    1 
ATOM   13052 C  CG    . PHE A 1 3179 ? 166.469 141.865 204.969 1.00 9.32   ? 3179 PHE A CG    1 
ATOM   13053 C  CD1   . PHE A 1 3179 ? 166.383 140.485 205.020 1.00 11.48  ? 3179 PHE A CD1   1 
ATOM   13054 C  CD2   . PHE A 1 3179 ? 167.603 142.475 205.476 1.00 9.88   ? 3179 PHE A CD2   1 
ATOM   13055 C  CE1   . PHE A 1 3179 ? 167.393 139.733 205.584 1.00 12.78  ? 3179 PHE A CE1   1 
ATOM   13056 C  CE2   . PHE A 1 3179 ? 168.616 141.726 206.037 1.00 12.31  ? 3179 PHE A CE2   1 
ATOM   13057 C  CZ    . PHE A 1 3179 ? 168.510 140.353 206.091 1.00 12.53  ? 3179 PHE A CZ    1 
ATOM   13058 N  N     . ILE A 1 3180 ? 163.933 143.119 207.122 1.00 13.30  ? 3180 ILE A N     1 
ATOM   13059 C  CA    . ILE A 1 3180 ? 163.916 142.939 208.572 1.00 11.63  ? 3180 ILE A CA    1 
ATOM   13060 C  C     . ILE A 1 3180 ? 162.569 142.390 209.036 1.00 11.69  ? 3180 ILE A C     1 
ATOM   13061 O  O     . ILE A 1 3180 ? 162.506 141.550 209.944 1.00 16.11  ? 3180 ILE A O     1 
ATOM   13062 C  CB    . ILE A 1 3180 ? 164.276 144.255 209.284 1.00 14.41  ? 3180 ILE A CB    1 
ATOM   13063 C  CG1   . ILE A 1 3180 ? 165.568 144.835 208.712 1.00 10.76  ? 3180 ILE A CG1   1 
ATOM   13064 C  CG2   . ILE A 1 3180 ? 164.460 144.018 210.763 1.00 19.45  ? 3180 ILE A CG2   1 
ATOM   13065 C  CD1   . ILE A 1 3180 ? 166.767 143.931 208.872 1.00 11.07  ? 3180 ILE A CD1   1 
ATOM   13066 N  N     . ASN A 1 3181 ? 161.471 142.854 208.431 1.00 13.65  ? 3181 ASN A N     1 
ATOM   13067 C  CA    . ASN A 1 3181 ? 160.155 142.331 208.790 1.00 16.93  ? 3181 ASN A CA    1 
ATOM   13068 C  C     . ASN A 1 3181 ? 160.044 140.846 208.465 1.00 16.95  ? 3181 ASN A C     1 
ATOM   13069 O  O     . ASN A 1 3181 ? 159.543 140.057 209.278 1.00 19.18  ? 3181 ASN A O     1 
ATOM   13070 C  CB    . ASN A 1 3181 ? 159.065 143.123 208.066 1.00 17.37  ? 3181 ASN A CB    1 
ATOM   13071 C  CG    . ASN A 1 3181 ? 157.754 143.144 208.825 1.00 27.75  ? 3181 ASN A CG    1 
ATOM   13072 O  OD1   . ASN A 1 3181 ? 156.979 142.189 208.779 1.00 30.75  ? 3181 ASN A OD1   1 
ATOM   13073 N  ND2   . ASN A 1 3181 ? 157.493 144.244 209.523 1.00 28.31  ? 3181 ASN A ND2   1 
ATOM   13074 N  N     . HIS A 1 3182 ? 160.518 140.447 207.281 1.00 15.02  ? 3182 HIS A N     1 
ATOM   13075 C  CA    . HIS A 1 3182 ? 160.535 139.036 206.916 1.00 11.69  ? 3182 HIS A CA    1 
ATOM   13076 C  C     . HIS A 1 3182 ? 161.423 138.241 207.860 1.00 15.20  ? 3182 HIS A C     1 
ATOM   13077 O  O     . HIS A 1 3182 ? 161.094 137.108 208.220 1.00 23.40  ? 3182 HIS A O     1 
ATOM   13078 C  CB    . HIS A 1 3182 ? 161.012 138.866 205.474 1.00 10.94  ? 3182 HIS A CB    1 
ATOM   13079 C  CG    . HIS A 1 3182 ? 159.980 139.204 204.445 1.00 11.44  ? 3182 HIS A CG    1 
ATOM   13080 N  ND1   . HIS A 1 3182 ? 160.273 139.919 203.305 1.00 9.21   ? 3182 HIS A ND1   1 
ATOM   13081 C  CD2   . HIS A 1 3182 ? 158.659 138.916 204.379 1.00 14.93  ? 3182 HIS A CD2   1 
ATOM   13082 C  CE1   . HIS A 1 3182 ? 159.176 140.062 202.583 1.00 12.53  ? 3182 HIS A CE1   1 
ATOM   13083 N  NE2   . HIS A 1 3182 ? 158.183 139.463 203.213 1.00 15.37  ? 3182 HIS A NE2   1 
ATOM   13084 N  N     . TYR A 1 3183 ? 162.557 138.815 208.263 1.00 12.18  ? 3183 TYR A N     1 
ATOM   13085 C  CA    . TYR A 1 3183 ? 163.442 138.132 209.198 1.00 14.02  ? 3183 TYR A CA    1 
ATOM   13086 C  C     . TYR A 1 3183 ? 162.724 137.852 210.511 1.00 19.07  ? 3183 TYR A C     1 
ATOM   13087 O  O     . TYR A 1 3183 ? 162.753 136.726 211.020 1.00 27.27  ? 3183 TYR A O     1 
ATOM   13088 C  CB    . TYR A 1 3183 ? 164.692 138.981 209.432 1.00 15.38  ? 3183 TYR A CB    1 
ATOM   13089 C  CG    . TYR A 1 3183 ? 165.809 138.303 210.197 1.00 18.16  ? 3183 TYR A CG    1 
ATOM   13090 C  CD1   . TYR A 1 3183 ? 165.762 136.948 210.497 1.00 19.06  ? 3183 TYR A CD1   1 
ATOM   13091 C  CD2   . TYR A 1 3183 ? 166.908 139.027 210.630 1.00 20.71  ? 3183 TYR A CD2   1 
ATOM   13092 C  CE1   . TYR A 1 3183 ? 166.780 136.337 211.196 1.00 22.23  ? 3183 TYR A CE1   1 
ATOM   13093 C  CE2   . TYR A 1 3183 ? 167.929 138.424 211.329 1.00 23.09  ? 3183 TYR A CE2   1 
ATOM   13094 C  CZ    . TYR A 1 3183 ? 167.862 137.080 211.609 1.00 24.40  ? 3183 TYR A CZ    1 
ATOM   13095 O  OH    . TYR A 1 3183 ? 168.881 136.478 212.307 1.00 30.36  ? 3183 TYR A OH    1 
ATOM   13096 N  N     . ALA A 1 3184 ? 162.053 138.864 211.061 1.00 18.09  ? 3184 ALA A N     1 
ATOM   13097 C  CA    . ALA A 1 3184 ? 161.344 138.681 212.324 1.00 20.25  ? 3184 ALA A CA    1 
ATOM   13098 C  C     . ALA A 1 3184 ? 160.235 137.644 212.187 1.00 20.98  ? 3184 ALA A C     1 
ATOM   13099 O  O     . ALA A 1 3184 ? 160.101 136.740 213.026 1.00 28.73  ? 3184 ALA A O     1 
ATOM   13100 C  CB    . ALA A 1 3184 ? 160.780 140.016 212.806 1.00 23.04  ? 3184 ALA A CB    1 
ATOM   13101 N  N     . ASN A 1 3185 ? 159.436 137.751 211.120 1.00 21.45  ? 3185 ASN A N     1 
ATOM   13102 C  CA    . ASN A 1 3185 ? 158.321 136.829 210.933 1.00 19.17  ? 3185 ASN A CA    1 
ATOM   13103 C  C     . ASN A 1 3185 ? 158.812 135.396 210.767 1.00 23.47  ? 3185 ASN A C     1 
ATOM   13104 O  O     . ASN A 1 3185 ? 158.279 134.469 211.389 1.00 28.47  ? 3185 ASN A O     1 
ATOM   13105 C  CB    . ASN A 1 3185 ? 157.489 137.254 209.724 1.00 14.57  ? 3185 ASN A CB    1 
ATOM   13106 C  CG    . ASN A 1 3185 ? 156.848 138.611 209.906 1.00 18.71  ? 3185 ASN A CG    1 
ATOM   13107 O  OD1   . ASN A 1 3185 ? 156.835 139.162 211.006 1.00 25.15  ? 3185 ASN A OD1   1 
ATOM   13108 N  ND2   . ASN A 1 3185 ? 156.313 139.161 208.824 1.00 19.42  ? 3185 ASN A ND2   1 
ATOM   13109 N  N     . LEU A 1 3186 ? 159.830 135.197 209.927 1.00 23.11  ? 3186 LEU A N     1 
ATOM   13110 C  CA    . LEU A 1 3186 ? 160.353 133.858 209.690 1.00 25.67  ? 3186 LEU A CA    1 
ATOM   13111 C  C     . LEU A 1 3186 ? 160.980 133.281 210.948 1.00 27.37  ? 3186 LEU A C     1 
ATOM   13112 O  O     . LEU A 1 3186 ? 160.799 132.096 211.246 1.00 32.09  ? 3186 LEU A O     1 
ATOM   13113 C  CB    . LEU A 1 3186 ? 161.367 133.886 208.549 1.00 19.03  ? 3186 LEU A CB    1 
ATOM   13114 C  CG    . LEU A 1 3186 ? 160.776 133.866 207.140 1.00 19.40  ? 3186 LEU A CG    1 
ATOM   13115 C  CD1   . LEU A 1 3186 ? 161.867 134.060 206.103 1.00 21.21  ? 3186 LEU A CD1   1 
ATOM   13116 C  CD2   . LEU A 1 3186 ? 160.018 132.573 206.896 1.00 24.94  ? 3186 LEU A CD2   1 
ATOM   13117 N  N     . PHE A 1 3187 ? 161.722 134.098 211.699 1.00 26.62  ? 3187 PHE A N     1 
ATOM   13118 C  CA    . PHE A 1 3187 ? 162.305 133.630 212.950 1.00 27.45  ? 3187 PHE A CA    1 
ATOM   13119 C  C     . PHE A 1 3187 ? 161.223 133.141 213.901 1.00 29.23  ? 3187 PHE A C     1 
ATOM   13120 O  O     . PHE A 1 3187 ? 161.307 132.028 214.435 1.00 35.37  ? 3187 PHE A O     1 
ATOM   13121 C  CB    . PHE A 1 3187 ? 163.120 134.754 213.589 1.00 30.04  ? 3187 PHE A CB    1 
ATOM   13122 C  CG    . PHE A 1 3187 ? 164.125 134.283 214.599 1.00 31.05  ? 3187 PHE A CG    1 
ATOM   13123 C  CD1   . PHE A 1 3187 ? 165.376 133.846 214.200 1.00 31.54  ? 3187 PHE A CD1   1 
ATOM   13124 C  CD2   . PHE A 1 3187 ? 163.823 134.290 215.949 1.00 28.77  ? 3187 PHE A CD2   1 
ATOM   13125 C  CE1   . PHE A 1 3187 ? 166.302 133.418 215.128 1.00 31.38  ? 3187 PHE A CE1   1 
ATOM   13126 C  CE2   . PHE A 1 3187 ? 164.745 133.864 216.881 1.00 33.86  ? 3187 PHE A CE2   1 
ATOM   13127 C  CZ    . PHE A 1 3187 ? 165.986 133.427 216.470 1.00 36.32  ? 3187 PHE A CZ    1 
ATOM   13128 N  N     . HIS A 1 3188 ? 160.184 133.956 214.108 1.00 30.71  ? 3188 HIS A N     1 
ATOM   13129 C  CA    . HIS A 1 3188 ? 159.122 133.563 215.029 1.00 37.15  ? 3188 HIS A CA    1 
ATOM   13130 C  C     . HIS A 1 3188 ? 158.412 132.301 214.552 1.00 39.03  ? 3188 HIS A C     1 
ATOM   13131 O  O     . HIS A 1 3188 ? 158.164 131.381 215.343 1.00 43.23  ? 3188 HIS A O     1 
ATOM   13132 C  CB    . HIS A 1 3188 ? 158.126 134.708 215.202 1.00 35.68  ? 3188 HIS A CB    1 
ATOM   13133 C  CG    . HIS A 1 3188 ? 157.146 134.491 216.311 1.00 56.35  ? 3188 HIS A CG    1 
ATOM   13134 N  ND1   . HIS A 1 3188 ? 157.441 134.766 217.629 1.00 61.39  ? 3188 HIS A ND1   1 
ATOM   13135 C  CD2   . HIS A 1 3188 ? 155.876 134.021 216.301 1.00 60.66  ? 3188 HIS A CD2   1 
ATOM   13136 C  CE1   . HIS A 1 3188 ? 156.395 134.477 218.382 1.00 63.68  ? 3188 HIS A CE1   1 
ATOM   13137 N  NE2   . HIS A 1 3188 ? 155.432 134.023 217.601 1.00 66.85  ? 3188 HIS A NE2   1 
ATOM   13138 N  N     . GLU A 1 3189 ? 158.092 132.233 213.257 1.00 38.31  ? 3189 GLU A N     1 
ATOM   13139 C  CA    . GLU A 1 3189 ? 157.372 131.081 212.724 1.00 36.88  ? 3189 GLU A CA    1 
ATOM   13140 C  C     . GLU A 1 3189 ? 158.193 129.803 212.859 1.00 39.45  ? 3189 GLU A C     1 
ATOM   13141 O  O     . GLU A 1 3189 ? 157.674 128.757 213.272 1.00 44.19  ? 3189 GLU A O     1 
ATOM   13142 C  CB    . GLU A 1 3189 ? 157.000 131.338 211.263 1.00 32.08  ? 3189 GLU A CB    1 
ATOM   13143 C  CG    . GLU A 1 3189 ? 156.674 130.090 210.465 1.00 44.83  ? 3189 GLU A CG    1 
ATOM   13144 C  CD    . GLU A 1 3189 ? 156.671 130.338 208.969 1.00 47.05  ? 3189 GLU A CD    1 
ATOM   13145 O  OE1   . GLU A 1 3189 ? 155.882 131.189 208.506 1.00 41.19  ? 3189 GLU A OE1   1 
ATOM   13146 O  OE2   . GLU A 1 3189 ? 157.457 129.683 208.254 1.00 48.64  ? 3189 GLU A OE2   1 
ATOM   13147 N  N     . LYS A 1 3190 ? 159.484 129.869 212.520 1.00 36.85  ? 3190 LYS A N     1 
ATOM   13148 C  CA    . LYS A 1 3190 ? 160.332 128.686 212.597 1.00 35.16  ? 3190 LYS A CA    1 
ATOM   13149 C  C     . LYS A 1 3190 ? 160.509 128.230 214.038 1.00 39.96  ? 3190 LYS A C     1 
ATOM   13150 O  O     . LYS A 1 3190 ? 160.397 127.031 214.330 1.00 52.83  ? 3190 LYS A O     1 
ATOM   13151 C  CB    . LYS A 1 3190 ? 161.688 128.972 211.951 1.00 35.85  ? 3190 LYS A CB    1 
ATOM   13152 C  CG    . LYS A 1 3190 ? 161.621 129.200 210.450 1.00 36.53  ? 3190 LYS A CG    1 
ATOM   13153 C  CD    . LYS A 1 3190 ? 161.044 128.005 209.725 1.00 36.12  ? 3190 LYS A CD    1 
ATOM   13154 C  CE    . LYS A 1 3190 ? 160.998 128.230 208.223 1.00 35.11  ? 3190 LYS A CE    1 
ATOM   13155 N  NZ    . LYS A 1 3190 ? 160.625 126.991 207.490 1.00 31.53  ? 3190 LYS A NZ    1 
ATOM   13156 N  N     . ARG A 1 3191 ? 160.772 129.169 214.953 1.00 41.32  ? 3191 ARG A N     1 
ATOM   13157 C  CA    . ARG A 1 3191 ? 160.875 128.814 216.365 1.00 46.60  ? 3191 ARG A CA    1 
ATOM   13158 C  C     . ARG A 1 3191 ? 159.607 128.127 216.850 1.00 47.51  ? 3191 ARG A C     1 
ATOM   13159 O  O     . ARG A 1 3191 ? 159.667 127.058 217.470 1.00 54.49  ? 3191 ARG A O     1 
ATOM   13160 C  CB    . ARG A 1 3191 ? 161.161 130.058 217.210 1.00 49.18  ? 3191 ARG A CB    1 
ATOM   13161 C  CG    . ARG A 1 3191 ? 162.500 130.721 216.952 1.00 41.01  ? 3191 ARG A CG    1 
ATOM   13162 C  CD    . ARG A 1 3191 ? 163.642 129.850 217.436 1.00 46.95  ? 3191 ARG A CD    1 
ATOM   13163 N  NE    . ARG A 1 3191 ? 163.560 129.605 218.872 1.00 50.49  ? 3191 ARG A NE    1 
ATOM   13164 C  CZ    . ARG A 1 3191 ? 164.054 130.414 219.799 1.00 48.87  ? 3191 ARG A CZ    1 
ATOM   13165 N  NH1   . ARG A 1 3191 ? 164.673 131.538 219.478 1.00 49.81  ? 3191 ARG A NH1   1 
ATOM   13166 N  NH2   . ARG A 1 3191 ? 163.921 130.087 221.081 1.00 42.12  ? 3191 ARG A NH2   1 
ATOM   13167 N  N     . SER A 1 3192 ? 158.445 128.715 216.557 1.00 43.59  ? 3192 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3192 ? 157.190 128.155 217.046 1.00 48.64  ? 3192 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3192 ? 156.954 126.755 216.491 1.00 51.05  ? 3192 SER A C     1 
ATOM   13170 O  O     . SER A 1 3192 ? 156.657 125.815 217.245 1.00 60.10  ? 3192 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3192 ? 156.030 129.081 216.682 1.00 51.58  ? 3192 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3192 ? 156.168 130.345 217.307 1.00 54.99  ? 3192 SER A OG    1 
ATOM   13173 N  N     . GLU A 1 3193 ? 157.086 126.593 215.170 1.00 48.46  ? 3193 GLU A N     1 
ATOM   13174 C  CA    . GLU A 1 3193 ? 156.761 125.303 214.575 1.00 53.10  ? 3193 GLU A CA    1 
ATOM   13175 C  C     . GLU A 1 3193 ? 157.732 124.225 215.036 1.00 56.39  ? 3193 GLU A C     1 
ATOM   13176 O  O     . GLU A 1 3193 ? 157.322 123.090 215.309 1.00 62.53  ? 3193 GLU A O     1 
ATOM   13177 C  CB    . GLU A 1 3193 ? 156.737 125.387 213.047 1.00 50.11  ? 3193 GLU A CB    1 
ATOM   13178 C  CG    . GLU A 1 3193 ? 158.073 125.625 212.372 1.00 48.36  ? 3193 GLU A CG    1 
ATOM   13179 C  CD    . GLU A 1 3193 ? 157.939 125.714 210.866 1.00 55.32  ? 3193 GLU A CD    1 
ATOM   13180 O  OE1   . GLU A 1 3193 ? 156.799 125.637 210.363 1.00 61.15  ? 3193 GLU A OE1   1 
ATOM   13181 O  OE2   . GLU A 1 3193 ? 158.974 125.820 210.180 1.00 50.23  ? 3193 GLU A OE2   1 
ATOM   13182 N  N     . LEU A 1 3194 ? 159.021 124.557 215.159 1.00 50.89  ? 3194 LEU A N     1 
ATOM   13183 C  CA    . LEU A 1 3194 ? 159.973 123.517 215.524 1.00 56.07  ? 3194 LEU A CA    1 
ATOM   13184 C  C     . LEU A 1 3194 ? 159.868 123.192 217.009 1.00 58.72  ? 3194 LEU A C     1 
ATOM   13185 O  O     . LEU A 1 3194 ? 160.108 122.051 217.415 1.00 70.61  ? 3194 LEU A O     1 
ATOM   13186 C  CB    . LEU A 1 3194 ? 161.391 123.941 215.140 1.00 57.11  ? 3194 LEU A CB    1 
ATOM   13187 C  CG    . LEU A 1 3194 ? 162.480 122.860 215.165 1.00 61.21  ? 3194 LEU A CG    1 
ATOM   13188 C  CD1   . LEU A 1 3194 ? 163.581 123.233 214.186 1.00 67.38  ? 3194 LEU A CD1   1 
ATOM   13189 C  CD2   . LEU A 1 3194 ? 163.060 122.588 216.535 1.00 61.31  ? 3194 LEU A CD2   1 
ATOM   13190 N  N     . GLU A 1 3195 ? 159.489 124.172 217.837 1.00 56.55  ? 3195 GLU A N     1 
ATOM   13191 C  CA    . GLU A 1 3195 ? 159.214 123.876 219.238 1.00 63.21  ? 3195 GLU A CA    1 
ATOM   13192 C  C     . GLU A 1 3195 ? 158.026 122.932 219.376 1.00 66.91  ? 3195 GLU A C     1 
ATOM   13193 O  O     . GLU A 1 3195 ? 158.068 121.979 220.165 1.00 67.82  ? 3195 GLU A O     1 
ATOM   13194 C  CB    . GLU A 1 3195 ? 158.959 125.173 220.007 1.00 65.57  ? 3195 GLU A CB    1 
ATOM   13195 C  CG    . GLU A 1 3195 ? 160.222 125.905 220.428 1.00 70.09  ? 3195 GLU A CG    1 
ATOM   13196 C  CD    . GLU A 1 3195 ? 159.934 127.291 220.972 1.00 73.75  ? 3195 GLU A CD    1 
ATOM   13197 O  OE1   . GLU A 1 3195 ? 158.746 127.612 221.185 1.00 80.47  ? 3195 GLU A OE1   1 
ATOM   13198 O  OE2   . GLU A 1 3195 ? 160.894 128.061 221.184 1.00 70.27  ? 3195 GLU A OE2   1 
ATOM   13199 N  N     . GLU A 1 3196 ? 156.959 123.174 218.607 1.00 66.45  ? 3196 GLU A N     1 
ATOM   13200 C  CA    . GLU A 1 3196 ? 155.823 122.254 218.627 1.00 67.62  ? 3196 GLU A CA    1 
ATOM   13201 C  C     . GLU A 1 3196 ? 156.235 120.867 218.147 1.00 67.79  ? 3196 GLU A C     1 
ATOM   13202 O  O     . GLU A 1 3196 ? 155.822 119.848 218.719 1.00 73.00  ? 3196 GLU A O     1 
ATOM   13203 C  CB    . GLU A 1 3196 ? 154.684 122.804 217.767 1.00 68.44  ? 3196 GLU A CB    1 
ATOM   13204 C  CG    . GLU A 1 3196 ? 154.063 124.087 218.297 1.00 73.76  ? 3196 GLU A CG    1 
ATOM   13205 C  CD    . GLU A 1 3196 ? 153.334 123.886 219.611 1.00 86.00  ? 3196 GLU A CD    1 
ATOM   13206 O  OE1   . GLU A 1 3196 ? 152.787 122.784 219.829 1.00 87.06  ? 3196 GLU A OE1   1 
ATOM   13207 O  OE2   . GLU A 1 3196 ? 153.308 124.830 220.428 1.00 86.03  ? 3196 GLU A OE2   1 
ATOM   13208 N  N     . GLN A 1 3197 ? 157.057 120.814 217.096 1.00 68.40  ? 3197 GLN A N     1 
ATOM   13209 C  CA    . GLN A 1 3197 ? 157.562 119.538 216.602 1.00 65.57  ? 3197 GLN A CA    1 
ATOM   13210 C  C     . GLN A 1 3197 ? 158.326 118.789 217.686 1.00 69.55  ? 3197 GLN A C     1 
ATOM   13211 O  O     . GLN A 1 3197 ? 158.058 117.609 217.939 1.00 81.56  ? 3197 GLN A O     1 
ATOM   13212 C  CB    . GLN A 1 3197 ? 158.454 119.773 215.384 1.00 67.00  ? 3197 GLN A CB    1 
ATOM   13213 C  CG    . GLN A 1 3197 ? 159.034 118.510 214.776 1.00 74.22  ? 3197 GLN A CG    1 
ATOM   13214 C  CD    . GLN A 1 3197 ? 159.902 118.792 213.568 1.00 70.66  ? 3197 GLN A CD    1 
ATOM   13215 O  OE1   . GLN A 1 3197 ? 160.073 119.943 213.168 1.00 71.86  ? 3197 GLN A OE1   1 
ATOM   13216 N  NE2   . GLN A 1 3197 ? 160.457 117.740 212.979 1.00 63.00  ? 3197 GLN A NE2   1 
ATOM   13217 N  N     . GLN A 1 3198 ? 159.270 119.462 218.344 1.00 66.58  ? 3198 GLN A N     1 
ATOM   13218 C  CA    . GLN A 1 3198 ? 160.055 118.809 219.385 1.00 71.25  ? 3198 GLN A CA    1 
ATOM   13219 C  C     . GLN A 1 3198 ? 159.174 118.352 220.540 1.00 72.46  ? 3198 GLN A C     1 
ATOM   13220 O  O     . GLN A 1 3198 ? 159.406 117.283 221.111 1.00 75.99  ? 3198 GLN A O     1 
ATOM   13221 C  CB    . GLN A 1 3198 ? 161.161 119.739 219.883 1.00 71.38  ? 3198 GLN A CB    1 
ATOM   13222 C  CG    . GLN A 1 3198 ? 162.050 119.107 220.943 1.00 72.36  ? 3198 GLN A CG    1 
ATOM   13223 C  CD    . GLN A 1 3198 ? 163.282 118.434 220.370 1.00 71.60  ? 3198 GLN A CD    1 
ATOM   13224 O  OE1   . GLN A 1 3198 ? 163.331 118.104 219.187 1.00 74.51  ? 3198 GLN A OE1   1 
ATOM   13225 N  NE2   . GLN A 1 3198 ? 164.277 118.208 221.217 1.00 62.75  ? 3198 GLN A NE2   1 
ATOM   13226 N  N     . MET A 1 3199 ? 158.160 119.143 220.898 1.00 75.12  ? 3199 MET A N     1 
ATOM   13227 C  CA    . MET A 1 3199 ? 157.230 118.711 221.937 1.00 75.62  ? 3199 MET A CA    1 
ATOM   13228 C  C     . MET A 1 3199 ? 156.537 117.413 221.540 1.00 82.29  ? 3199 MET A C     1 
ATOM   13229 O  O     . MET A 1 3199 ? 156.424 116.476 222.346 1.00 86.24  ? 3199 MET A O     1 
ATOM   13230 C  CB    . MET A 1 3199 ? 156.202 119.808 222.210 1.00 71.53  ? 3199 MET A CB    1 
ATOM   13231 C  CG    . MET A 1 3199 ? 155.234 119.483 223.335 1.00 78.86  ? 3199 MET A CG    1 
ATOM   13232 S  SD    . MET A 1 3199 ? 154.096 120.835 223.692 1.00 110.59 ? 3199 MET A SD    1 
ATOM   13233 C  CE    . MET A 1 3199 ? 153.067 120.084 224.951 1.00 79.91  ? 3199 MET A CE    1 
ATOM   13234 N  N     . HIS A 1 3200 ? 156.074 117.337 220.288 1.00 76.23  ? 3200 HIS A N     1 
ATOM   13235 C  CA    . HIS A 1 3200 ? 155.408 116.125 219.821 1.00 74.51  ? 3200 HIS A CA    1 
ATOM   13236 C  C     . HIS A 1 3200 ? 156.351 114.927 219.850 1.00 75.00  ? 3200 HIS A C     1 
ATOM   13237 O  O     . HIS A 1 3200 ? 155.971 113.838 220.298 1.00 79.91  ? 3200 HIS A O     1 
ATOM   13238 C  CB    . HIS A 1 3200 ? 154.852 116.340 218.415 1.00 68.39  ? 3200 HIS A CB    1 
ATOM   13239 C  CG    . HIS A 1 3200 ? 153.738 117.337 218.353 1.00 66.81  ? 3200 HIS A CG    1 
ATOM   13240 N  ND1   . HIS A 1 3200 ? 153.156 117.872 219.482 1.00 72.48  ? 3200 HIS A ND1   1 
ATOM   13241 C  CD2   . HIS A 1 3200 ? 153.103 117.900 217.299 1.00 65.27  ? 3200 HIS A CD2   1 
ATOM   13242 C  CE1   . HIS A 1 3200 ? 152.207 118.719 219.126 1.00 71.81  ? 3200 HIS A CE1   1 
ATOM   13243 N  NE2   . HIS A 1 3200 ? 152.155 118.755 217.806 1.00 71.59  ? 3200 HIS A NE2   1 
ATOM   13244 N  N     . LEU A 1 3201 ? 157.587 115.108 219.381 1.00 72.78  ? 3201 LEU A N     1 
ATOM   13245 C  CA    . LEU A 1 3201 ? 158.547 114.004 219.409 1.00 77.29  ? 3201 LEU A CA    1 
ATOM   13246 C  C     . LEU A 1 3201 ? 158.871 113.559 220.831 1.00 81.10  ? 3201 LEU A C     1 
ATOM   13247 O  O     . LEU A 1 3201 ? 158.956 112.355 221.097 1.00 86.10  ? 3201 LEU A O     1 
ATOM   13248 C  CB    . LEU A 1 3201 ? 159.823 114.366 218.651 1.00 75.86  ? 3201 LEU A CB    1 
ATOM   13249 C  CG    . LEU A 1 3201 ? 159.816 114.262 217.120 1.00 79.95  ? 3201 LEU A CG    1 
ATOM   13250 C  CD1   . LEU A 1 3201 ? 158.996 115.304 216.405 1.00 71.28  ? 3201 LEU A CD1   1 
ATOM   13251 C  CD2   . LEU A 1 3201 ? 161.248 114.331 216.645 1.00 81.31  ? 3201 LEU A CD2   1 
ATOM   13252 N  N     . ASN A 1 3202 ? 159.065 114.500 221.758 1.00 80.65  ? 3202 ASN A N     1 
ATOM   13253 C  CA    . ASN A 1 3202 ? 159.363 114.100 223.131 1.00 84.43  ? 3202 ASN A CA    1 
ATOM   13254 C  C     . ASN A 1 3202 ? 158.202 113.340 223.757 1.00 86.21  ? 3202 ASN A C     1 
ATOM   13255 O  O     . ASN A 1 3202 ? 158.413 112.313 224.416 1.00 91.80  ? 3202 ASN A O     1 
ATOM   13256 C  CB    . ASN A 1 3202 ? 159.739 115.306 223.995 1.00 86.40  ? 3202 ASN A CB    1 
ATOM   13257 C  CG    . ASN A 1 3202 ? 161.044 115.948 223.569 1.00 84.46  ? 3202 ASN A CG    1 
ATOM   13258 O  OD1   . ASN A 1 3202 ? 161.076 117.096 223.136 1.00 82.82  ? 3202 ASN A OD1   1 
ATOM   13259 N  ND2   . ASN A 1 3202 ? 162.134 115.201 223.695 1.00 80.87  ? 3202 ASN A ND2   1 
ATOM   13260 N  N     . VAL A 1 3203 ? 156.967 113.810 223.560 1.00 83.18  ? 3203 VAL A N     1 
ATOM   13261 C  CA    . VAL A 1 3203 ? 155.835 113.116 224.172 1.00 83.04  ? 3203 VAL A CA    1 
ATOM   13262 C  C     . VAL A 1 3203 ? 155.648 111.740 223.537 1.00 86.14  ? 3203 VAL A C     1 
ATOM   13263 O  O     . VAL A 1 3203 ? 155.342 110.758 224.225 1.00 93.59  ? 3203 VAL A O     1 
ATOM   13264 C  CB    . VAL A 1 3203 ? 154.557 113.976 224.105 1.00 77.77  ? 3203 VAL A CB    1 
ATOM   13265 C  CG1   . VAL A 1 3203 ? 154.075 114.167 222.683 1.00 78.60  ? 3203 VAL A CG1   1 
ATOM   13266 C  CG2   . VAL A 1 3203 ? 153.459 113.358 224.958 1.00 76.89  ? 3203 VAL A CG2   1 
ATOM   13267 N  N     . GLY A 1 3204 ? 155.874 111.634 222.223 1.00 87.28  ? 3204 GLY A N     1 
ATOM   13268 C  CA    . GLY A 1 3204 ? 155.768 110.337 221.571 1.00 92.56  ? 3204 GLY A CA    1 
ATOM   13269 C  C     . GLY A 1 3204 ? 156.824 109.354 222.040 1.00 93.15  ? 3204 GLY A C     1 
ATOM   13270 O  O     . GLY A 1 3204 ? 156.527 108.180 222.291 1.00 98.78  ? 3204 GLY A O     1 
ATOM   13271 N  N     . LEU A 1 3205 ? 158.072 109.815 222.161 1.00 85.65  ? 3205 LEU A N     1 
ATOM   13272 C  CA    . LEU A 1 3205 ? 159.133 108.945 222.657 1.00 89.93  ? 3205 LEU A CA    1 
ATOM   13273 C  C     . LEU A 1 3205 ? 158.864 108.523 224.095 1.00 94.86  ? 3205 LEU A C     1 
ATOM   13274 O  O     . LEU A 1 3205 ? 159.125 107.375 224.469 1.00 95.84  ? 3205 LEU A O     1 
ATOM   13275 C  CB    . LEU A 1 3205 ? 160.490 109.641 222.546 1.00 88.60  ? 3205 LEU A CB    1 
ATOM   13276 C  CG    . LEU A 1 3205 ? 161.021 109.939 221.141 1.00 84.34  ? 3205 LEU A CG    1 
ATOM   13277 C  CD1   . LEU A 1 3205 ? 162.303 110.754 221.214 1.00 80.49  ? 3205 LEU A CD1   1 
ATOM   13278 C  CD2   . LEU A 1 3205 ? 161.240 108.662 220.348 1.00 87.52  ? 3205 LEU A CD2   1 
ATOM   13279 N  N     . ARG A 1 3206 ? 158.343 109.438 224.917 1.00 98.81  ? 3206 ARG A N     1 
ATOM   13280 C  CA    . ARG A 1 3206 ? 157.995 109.082 226.288 1.00 99.81  ? 3206 ARG A CA    1 
ATOM   13281 C  C     . ARG A 1 3206 ? 156.910 108.012 226.319 1.00 102.89 ? 3206 ARG A C     1 
ATOM   13282 O  O     . ARG A 1 3206 ? 156.994 107.053 227.097 1.00 107.83 ? 3206 ARG A O     1 
ATOM   13283 C  CB    . ARG A 1 3206 ? 157.549 110.330 227.051 1.00 98.69  ? 3206 ARG A CB    1 
ATOM   13284 C  CG    . ARG A 1 3206 ? 156.593 110.064 228.201 1.00 98.44  ? 3206 ARG A CG    1 
ATOM   13285 C  CD    . ARG A 1 3206 ? 156.530 111.257 229.138 1.00 90.64  ? 3206 ARG A CD    1 
ATOM   13286 N  NE    . ARG A 1 3206 ? 155.795 112.369 228.548 1.00 90.83  ? 3206 ARG A NE    1 
ATOM   13287 C  CZ    . ARG A 1 3206 ? 156.348 113.508 228.155 1.00 88.73  ? 3206 ARG A CZ    1 
ATOM   13288 N  NH1   . ARG A 1 3206 ? 157.649 113.721 228.268 1.00 87.64  ? 3206 ARG A NH1   1 
ATOM   13289 N  NH2   . ARG A 1 3206 ? 155.577 114.457 227.632 1.00 85.14  ? 3206 ARG A NH2   1 
ATOM   13290 N  N     . LYS A 1 3207 ? 155.889 108.153 225.469 1.00 100.19 ? 3207 LYS A N     1 
ATOM   13291 C  CA    . LYS A 1 3207 ? 154.825 107.154 225.426 1.00 101.06 ? 3207 LYS A CA    1 
ATOM   13292 C  C     . LYS A 1 3207 ? 155.355 105.796 224.981 1.00 102.58 ? 3207 LYS A C     1 
ATOM   13293 O  O     . LYS A 1 3207 ? 154.992 104.760 225.553 1.00 105.96 ? 3207 LYS A O     1 
ATOM   13294 C  CB    . LYS A 1 3207 ? 153.701 107.623 224.504 1.00 97.79  ? 3207 LYS A CB    1 
ATOM   13295 C  CG    . LYS A 1 3207 ? 152.966 108.855 225.008 1.00 97.70  ? 3207 LYS A CG    1 
ATOM   13296 C  CD    . LYS A 1 3207 ? 151.887 108.489 226.008 1.00 94.21  ? 3207 LYS A CD    1 
ATOM   13297 C  CE    . LYS A 1 3207 ? 151.086 109.710 226.428 1.00 95.92  ? 3207 LYS A CE    1 
ATOM   13298 N  NZ    . LYS A 1 3207 ? 150.319 110.296 225.295 1.00 99.67  ? 3207 LYS A NZ    1 
ATOM   13299 N  N     . ILE A 1 3208 ? 156.222 105.777 223.966 1.00 102.98 ? 3208 ILE A N     1 
ATOM   13300 C  CA    . ILE A 1 3208 ? 156.740 104.502 223.475 1.00 103.33 ? 3208 ILE A CA    1 
ATOM   13301 C  C     . ILE A 1 3208 ? 157.670 103.863 224.507 1.00 108.47 ? 3208 ILE A C     1 
ATOM   13302 O  O     . ILE A 1 3208 ? 157.694 102.636 224.664 1.00 112.91 ? 3208 ILE A O     1 
ATOM   13303 C  CB    . ILE A 1 3208 ? 157.428 104.688 222.110 1.00 99.76  ? 3208 ILE A CB    1 
ATOM   13304 C  CG1   . ILE A 1 3208 ? 156.424 105.217 221.085 1.00 98.99  ? 3208 ILE A CG1   1 
ATOM   13305 C  CG2   . ILE A 1 3208 ? 157.978 103.365 221.606 1.00 99.80  ? 3208 ILE A CG2   1 
ATOM   13306 C  CD1   . ILE A 1 3208 ? 156.951 105.245 219.668 1.00 93.03  ? 3208 ILE A CD1   1 
ATOM   13307 N  N     . LYS A 1 3209 ? 158.446 104.677 225.228 1.00 106.96 ? 3209 LYS A N     1 
ATOM   13308 C  CA    . LYS A 1 3209 ? 159.287 104.145 226.299 1.00 105.14 ? 3209 LYS A CA    1 
ATOM   13309 C  C     . LYS A 1 3209 ? 158.441 103.555 227.421 1.00 109.25 ? 3209 LYS A C     1 
ATOM   13310 O  O     . LYS A 1 3209 ? 158.776 102.499 227.979 1.00 109.13 ? 3209 LYS A O     1 
ATOM   13311 C  CB    . LYS A 1 3209 ? 160.202 105.244 226.839 1.00 102.62 ? 3209 LYS A CB    1 
ATOM   13312 C  CG    . LYS A 1 3209 ? 161.394 104.737 227.630 1.00 98.18  ? 3209 LYS A CG    1 
ATOM   13313 C  CD    . LYS A 1 3209 ? 162.618 104.584 226.743 1.00 94.43  ? 3209 LYS A CD    1 
ATOM   13314 C  CE    . LYS A 1 3209 ? 163.896 104.575 227.565 1.00 84.49  ? 3209 LYS A CE    1 
ATOM   13315 N  NZ    . LYS A 1 3209 ? 164.986 103.821 226.888 1.00 74.17  ? 3209 LYS A NZ    1 
ATOM   13316 N  N     . GLU A 1 3210 ? 157.344 104.231 227.772 1.00 109.34 ? 3210 GLU A N     1 
ATOM   13317 C  CA    . GLU A 1 3210 ? 156.413 103.672 228.745 1.00 111.10 ? 3210 GLU A CA    1 
ATOM   13318 C  C     . GLU A 1 3210 ? 155.850 102.345 228.256 1.00 116.00 ? 3210 GLU A C     1 
ATOM   13319 O  O     . GLU A 1 3210 ? 155.710 101.396 229.035 1.00 117.08 ? 3210 GLU A O     1 
ATOM   13320 C  CB    . GLU A 1 3210 ? 155.285 104.666 229.023 1.00 106.35 ? 3210 GLU A CB    1 
ATOM   13321 C  CG    . GLU A 1 3210 ? 154.671 104.544 230.407 1.00 110.83 ? 3210 GLU A CG    1 
ATOM   13322 C  CD    . GLU A 1 3210 ? 153.879 105.776 230.803 1.00 118.70 ? 3210 GLU A CD    1 
ATOM   13323 O  OE1   . GLU A 1 3210 ? 153.615 106.624 229.924 1.00 113.15 ? 3210 GLU A OE1   1 
ATOM   13324 O  OE2   . GLU A 1 3210 ? 153.519 105.896 231.992 1.00 119.93 ? 3210 GLU A OE2   1 
ATOM   13325 N  N     . THR A 1 3211 ? 155.529 102.261 226.962 1.00 115.66 ? 3211 THR A N     1 
ATOM   13326 C  CA    . THR A 1 3211 ? 155.046 101.006 226.392 1.00 113.84 ? 3211 THR A CA    1 
ATOM   13327 C  C     . THR A 1 3211 ? 156.094 99.903  226.508 1.00 114.42 ? 3211 THR A C     1 
ATOM   13328 O  O     . THR A 1 3211 ? 155.764 98.752  226.814 1.00 118.20 ? 3211 THR A O     1 
ATOM   13329 C  CB    . THR A 1 3211 ? 154.646 101.217 224.931 1.00 110.31 ? 3211 THR A CB    1 
ATOM   13330 O  OG1   . THR A 1 3211 ? 153.597 102.191 224.857 1.00 107.60 ? 3211 THR A OG1   1 
ATOM   13331 C  CG2   . THR A 1 3211 ? 154.172 99.916  224.303 1.00 105.66 ? 3211 THR A CG2   1 
ATOM   13332 N  N     . VAL A 1 3212 ? 157.362 100.235 226.258 1.00 112.34 ? 3212 VAL A N     1 
ATOM   13333 C  CA    . VAL A 1 3212 ? 158.432 99.244  226.367 1.00 110.88 ? 3212 VAL A CA    1 
ATOM   13334 C  C     . VAL A 1 3212 ? 158.555 98.740  227.802 1.00 113.71 ? 3212 VAL A C     1 
ATOM   13335 O  O     . VAL A 1 3212 ? 158.679 97.531  228.047 1.00 112.82 ? 3212 VAL A O     1 
ATOM   13336 C  CB    . VAL A 1 3212 ? 159.758 99.836  225.857 1.00 102.23 ? 3212 VAL A CB    1 
ATOM   13337 C  CG1   . VAL A 1 3212 ? 160.940 99.024  226.368 1.00 93.23  ? 3212 VAL A CG1   1 
ATOM   13338 C  CG2   . VAL A 1 3212 ? 159.765 99.898  224.338 1.00 100.86 ? 3212 VAL A CG2   1 
ATOM   13339 N  N     . ASP A 1 3213 ? 158.523 99.654  228.774 1.00 117.84 ? 3213 ASP A N     1 
ATOM   13340 C  CA    . ASP A 1 3213 ? 158.562 99.230  230.172 1.00 118.75 ? 3213 ASP A CA    1 
ATOM   13341 C  C     . ASP A 1 3213 ? 157.360 98.360  230.519 1.00 118.80 ? 3213 ASP A C     1 
ATOM   13342 O  O     . ASP A 1 3213 ? 157.494 97.364  231.248 1.00 120.93 ? 3213 ASP A O     1 
ATOM   13343 C  CB    . ASP A 1 3213 ? 158.623 100.450 231.091 1.00 122.17 ? 3213 ASP A CB    1 
ATOM   13344 C  CG    . ASP A 1 3213 ? 160.041 100.927 231.333 1.00 124.61 ? 3213 ASP A CG    1 
ATOM   13345 O  OD1   . ASP A 1 3213 ? 160.957 100.079 231.367 1.00 120.66 ? 3213 ASP A OD1   1 
ATOM   13346 O  OD2   . ASP A 1 3213 ? 160.240 102.150 231.489 1.00 122.48 ? 3213 ASP A OD2   1 
ATOM   13347 N  N     . GLN A 1 3214 ? 156.183 98.720  230.002 1.00 119.17 ? 3214 GLN A N     1 
ATOM   13348 C  CA    . GLN A 1 3214 ? 154.983 97.930  230.243 1.00 119.85 ? 3214 GLN A CA    1 
ATOM   13349 C  C     . GLN A 1 3214 ? 155.133 96.518  229.695 1.00 119.71 ? 3214 GLN A C     1 
ATOM   13350 O  O     . GLN A 1 3214 ? 154.785 95.548  230.373 1.00 122.16 ? 3214 GLN A O     1 
ATOM   13351 C  CB    . GLN A 1 3214 ? 153.770 98.620  229.618 1.00 117.04 ? 3214 GLN A CB    1 
ATOM   13352 C  CG    . GLN A 1 3214 ? 153.292 99.847  230.376 1.00 115.05 ? 3214 GLN A CG    1 
ATOM   13353 C  CD    . GLN A 1 3214 ? 153.143 99.594  231.861 1.00 118.63 ? 3214 GLN A CD    1 
ATOM   13354 O  OE1   . GLN A 1 3214 ? 152.426 98.684  232.275 1.00 122.80 ? 3214 GLN A OE1   1 
ATOM   13355 N  NE2   . GLN A 1 3214 ? 153.825 100.395 232.671 1.00 109.95 ? 3214 GLN A NE2   1 
ATOM   13356 N  N     . VAL A 1 3215 ? 155.653 96.379  228.474 1.00 118.30 ? 3215 VAL A N     1 
ATOM   13357 C  CA    . VAL A 1 3215 ? 155.783 95.038  227.910 1.00 115.92 ? 3215 VAL A CA    1 
ATOM   13358 C  C     . VAL A 1 3215 ? 156.837 94.241  228.666 1.00 118.36 ? 3215 VAL A C     1 
ATOM   13359 O  O     . VAL A 1 3215 ? 156.707 93.021  228.815 1.00 116.09 ? 3215 VAL A O     1 
ATOM   13360 C  CB    . VAL A 1 3215 ? 156.080 95.080  226.397 1.00 112.86 ? 3215 VAL A CB    1 
ATOM   13361 C  CG1   . VAL A 1 3215 ? 155.078 95.964  225.681 1.00 110.22 ? 3215 VAL A CG1   1 
ATOM   13362 C  CG2   . VAL A 1 3215 ? 157.505 95.511  226.115 1.00 109.89 ? 3215 VAL A CG2   1 
ATOM   13363 N  N     . GLU A 1 3216 ? 157.886 94.901  229.168 1.00 120.32 ? 3216 GLU A N     1 
ATOM   13364 C  CA    . GLU A 1 3216 ? 158.872 94.189  229.978 1.00 120.49 ? 3216 GLU A CA    1 
ATOM   13365 C  C     . GLU A 1 3216 ? 158.237 93.636  231.251 1.00 123.85 ? 3216 GLU A C     1 
ATOM   13366 O  O     . GLU A 1 3216 ? 158.429 92.461  231.605 1.00 125.05 ? 3216 GLU A O     1 
ATOM   13367 C  CB    . GLU A 1 3216 ? 160.041 95.117  230.313 1.00 121.66 ? 3216 GLU A CB    1 
ATOM   13368 C  CG    . GLU A 1 3216 ? 161.250 94.416  230.919 1.00 121.85 ? 3216 GLU A CG    1 
ATOM   13369 C  CD    . GLU A 1 3216 ? 161.172 94.310  232.430 1.00 122.22 ? 3216 GLU A CD    1 
ATOM   13370 O  OE1   . GLU A 1 3216 ? 160.533 95.180  233.057 1.00 123.70 ? 3216 GLU A OE1   1 
ATOM   13371 O  OE2   . GLU A 1 3216 ? 161.750 93.355  232.991 1.00 112.47 ? 3216 GLU A OE2   1 
ATOM   13372 N  N     . GLU A 1 3217 ? 157.456 94.467  231.949 1.00 124.21 ? 3217 GLU A N     1 
ATOM   13373 C  CA    . GLU A 1 3217 ? 156.851 93.984  233.186 1.00 124.06 ? 3217 GLU A CA    1 
ATOM   13374 C  C     . GLU A 1 3217 ? 155.759 92.954  232.911 1.00 124.65 ? 3217 GLU A C     1 
ATOM   13375 O  O     . GLU A 1 3217 ? 155.549 92.049  233.724 1.00 124.30 ? 3217 GLU A O     1 
ATOM   13376 C  CB    . GLU A 1 3217 ? 156.307 95.145  234.023 1.00 121.26 ? 3217 GLU A CB    1 
ATOM   13377 C  CG    . GLU A 1 3217 ? 154.972 95.706  233.583 1.00 119.69 ? 3217 GLU A CG    1 
ATOM   13378 C  CD    . GLU A 1 3217 ? 154.512 96.839  234.475 1.00 118.34 ? 3217 GLU A CD    1 
ATOM   13379 O  OE1   . GLU A 1 3217 ? 155.321 97.311  235.302 1.00 118.56 ? 3217 GLU A OE1   1 
ATOM   13380 O  OE2   . GLU A 1 3217 ? 153.336 97.244  234.371 1.00 117.58 ? 3217 GLU A OE2   1 
ATOM   13381 N  N     . LEU A 1 3218 ? 155.079 93.048  231.765 1.00 124.94 ? 3218 LEU A N     1 
ATOM   13382 C  CA    . LEU A 1 3218 ? 154.115 92.013  231.397 1.00 123.53 ? 3218 LEU A CA    1 
ATOM   13383 C  C     . LEU A 1 3218 ? 154.803 90.706  231.022 1.00 123.39 ? 3218 LEU A C     1 
ATOM   13384 O  O     . LEU A 1 3218 ? 154.249 89.631  231.254 1.00 124.16 ? 3218 LEU A O     1 
ATOM   13385 C  CB    . LEU A 1 3218 ? 153.203 92.492  230.265 1.00 118.70 ? 3218 LEU A CB    1 
ATOM   13386 C  CG    . LEU A 1 3218 ? 151.920 93.255  230.626 1.00 112.63 ? 3218 LEU A CG    1 
ATOM   13387 C  CD1   . LEU A 1 3218 ? 150.981 92.329  231.380 1.00 104.09 ? 3218 LEU A CD1   1 
ATOM   13388 C  CD2   . LEU A 1 3218 ? 152.170 94.503  231.451 1.00 113.96 ? 3218 LEU A CD2   1 
ATOM   13389 N  N     . ARG A 1 3219 ? 156.004 90.766  230.441 1.00 122.47 ? 3219 ARG A N     1 
ATOM   13390 C  CA    . ARG A 1 3219 ? 156.759 89.535  230.214 1.00 122.60 ? 3219 ARG A CA    1 
ATOM   13391 C  C     . ARG A 1 3219 ? 157.158 88.889  231.536 1.00 123.12 ? 3219 ARG A C     1 
ATOM   13392 O  O     . ARG A 1 3219 ? 157.061 87.662  231.699 1.00 121.10 ? 3219 ARG A O     1 
ATOM   13393 C  CB    . ARG A 1 3219 ? 157.995 89.816  229.359 1.00 117.67 ? 3219 ARG A CB    1 
ATOM   13394 C  CG    . ARG A 1 3219 ? 157.756 89.697  227.863 1.00 114.20 ? 3219 ARG A CG    1 
ATOM   13395 C  CD    . ARG A 1 3219 ? 159.049 89.403  227.116 1.00 112.08 ? 3219 ARG A CD    1 
ATOM   13396 N  NE    . ARG A 1 3219 ? 160.137 90.286  227.516 1.00 115.13 ? 3219 ARG A NE    1 
ATOM   13397 C  CZ    . ARG A 1 3219 ? 160.675 91.213  226.734 1.00 110.60 ? 3219 ARG A CZ    1 
ATOM   13398 N  NH1   . ARG A 1 3219 ? 160.251 91.404  225.496 1.00 103.58 ? 3219 ARG A NH1   1 
ATOM   13399 N  NH2   . ARG A 1 3219 ? 161.666 91.965  227.206 1.00 108.16 ? 3219 ARG A NH2   1 
ATOM   13400 N  N     . ARG A 1 3220 ? 157.607 89.703  232.495 1.00 123.25 ? 3220 ARG A N     1 
ATOM   13401 C  CA    . ARG A 1 3220 ? 157.913 89.166  233.819 1.00 124.10 ? 3220 ARG A CA    1 
ATOM   13402 C  C     . ARG A 1 3220 ? 156.672 88.554  234.464 1.00 126.32 ? 3220 ARG A C     1 
ATOM   13403 O  O     . ARG A 1 3220 ? 156.733 87.464  235.050 1.00 128.31 ? 3220 ARG A O     1 
ATOM   13404 C  CB    . ARG A 1 3220 ? 158.503 90.263  234.707 1.00 122.98 ? 3220 ARG A CB    1 
ATOM   13405 C  CG    . ARG A 1 3220 ? 158.523 89.926  236.189 1.00 120.29 ? 3220 ARG A CG    1 
ATOM   13406 C  CD    . ARG A 1 3220 ? 158.360 91.175  237.038 1.00 118.64 ? 3220 ARG A CD    1 
ATOM   13407 N  NE    . ARG A 1 3220 ? 157.212 91.972  236.621 1.00 124.39 ? 3220 ARG A NE    1 
ATOM   13408 C  CZ    . ARG A 1 3220 ? 155.962 91.740  236.998 1.00 125.31 ? 3220 ARG A CZ    1 
ATOM   13409 N  NH1   . ARG A 1 3220 ? 155.658 90.738  237.805 1.00 124.22 ? 3220 ARG A NH1   1 
ATOM   13410 N  NH2   . ARG A 1 3220 ? 154.993 92.535  236.553 1.00 123.88 ? 3220 ARG A NH2   1 
ATOM   13411 N  N     . ASP A 1 3221 ? 155.530 89.236  234.346 1.00 125.59 ? 3221 ASP A N     1 
ATOM   13412 C  CA    . ASP A 1 3221 ? 154.281 88.703  234.877 1.00 126.13 ? 3221 ASP A CA    1 
ATOM   13413 C  C     . ASP A 1 3221 ? 153.863 87.426  234.160 1.00 128.37 ? 3221 ASP A C     1 
ATOM   13414 O  O     . ASP A 1 3221 ? 153.284 86.535  234.783 1.00 125.52 ? 3221 ASP A O     1 
ATOM   13415 C  CB    . ASP A 1 3221 ? 153.176 89.755  234.777 1.00 122.46 ? 3221 ASP A CB    1 
ATOM   13416 C  CG    . ASP A 1 3221 ? 151.918 89.351  235.524 1.00 124.13 ? 3221 ASP A CG    1 
ATOM   13417 O  OD1   . ASP A 1 3221 ? 151.061 88.669  234.925 1.00 128.46 ? 3221 ASP A OD1   1 
ATOM   13418 O  OD2   . ASP A 1 3221 ? 151.788 89.716  236.711 1.00 117.28 ? 3221 ASP A OD2   1 
ATOM   13419 N  N     . LEU A 1 3222 ? 154.131 87.324  232.857 1.00 129.58 ? 3222 LEU A N     1 
ATOM   13420 C  CA    . LEU A 1 3222 ? 153.833 86.099  232.123 1.00 126.79 ? 3222 LEU A CA    1 
ATOM   13421 C  C     . LEU A 1 3222 ? 154.662 84.934  232.643 1.00 129.61 ? 3222 LEU A C     1 
ATOM   13422 O  O     . LEU A 1 3222 ? 154.152 83.819  232.800 1.00 130.64 ? 3222 LEU A O     1 
ATOM   13423 C  CB    . LEU A 1 3222 ? 154.084 86.309  230.630 1.00 122.98 ? 3222 LEU A CB    1 
ATOM   13424 C  CG    . LEU A 1 3222 ? 153.905 85.092  229.720 1.00 117.70 ? 3222 LEU A CG    1 
ATOM   13425 C  CD1   . LEU A 1 3222 ? 152.441 84.700  229.621 1.00 118.23 ? 3222 LEU A CD1   1 
ATOM   13426 C  CD2   . LEU A 1 3222 ? 154.486 85.360  228.340 1.00 110.87 ? 3222 LEU A CD2   1 
ATOM   13427 N  N     . ARG A 1 3223 ? 155.947 85.175  232.915 1.00 129.21 ? 3223 ARG A N     1 
ATOM   13428 C  CA    . ARG A 1 3223 ? 156.770 84.125  233.511 1.00 126.53 ? 3223 ARG A CA    1 
ATOM   13429 C  C     . ARG A 1 3223 ? 156.239 83.728  234.886 1.00 127.34 ? 3223 ARG A C     1 
ATOM   13430 O  O     . ARG A 1 3223 ? 156.189 82.536  235.228 1.00 126.64 ? 3223 ARG A O     1 
ATOM   13431 C  CB    . ARG A 1 3223 ? 158.225 84.585  233.608 1.00 123.49 ? 3223 ARG A CB    1 
ATOM   13432 C  CG    . ARG A 1 3223 ? 159.172 83.526  234.150 1.00 122.09 ? 3223 ARG A CG    1 
ATOM   13433 C  CD    . ARG A 1 3223 ? 160.458 84.145  234.675 1.00 120.56 ? 3223 ARG A CD    1 
ATOM   13434 N  NE    . ARG A 1 3223 ? 160.213 85.391  235.390 1.00 126.37 ? 3223 ARG A NE    1 
ATOM   13435 C  CZ    . ARG A 1 3223 ? 159.835 85.464  236.659 1.00 125.14 ? 3223 ARG A CZ    1 
ATOM   13436 N  NH1   . ARG A 1 3223 ? 159.648 84.376  237.388 1.00 118.77 ? 3223 ARG A NH1   1 
ATOM   13437 N  NH2   . ARG A 1 3223 ? 159.640 86.659  237.211 1.00 123.28 ? 3223 ARG A NH2   1 
ATOM   13438 N  N     . ILE A 1 3224 ? 155.828 84.717  235.684 1.00 127.10 ? 3224 ILE A N     1 
ATOM   13439 C  CA    . ILE A 1 3224 ? 155.280 84.428  237.009 1.00 126.29 ? 3224 ILE A CA    1 
ATOM   13440 C  C     . ILE A 1 3224 ? 154.004 83.599  236.895 1.00 127.82 ? 3224 ILE A C     1 
ATOM   13441 O  O     . ILE A 1 3224 ? 153.800 82.638  237.649 1.00 127.08 ? 3224 ILE A O     1 
ATOM   13442 C  CB    . ILE A 1 3224 ? 155.040 85.738  237.784 1.00 122.26 ? 3224 ILE A CB    1 
ATOM   13443 C  CG1   . ILE A 1 3224 ? 156.373 86.347  238.223 1.00 118.35 ? 3224 ILE A CG1   1 
ATOM   13444 C  CG2   . ILE A 1 3224 ? 154.142 85.497  238.988 1.00 113.49 ? 3224 ILE A CG2   1 
ATOM   13445 C  CD1   . ILE A 1 3224 ? 156.228 87.627  239.014 1.00 112.58 ? 3224 ILE A CD1   1 
ATOM   13446 N  N     . LYS A 1 3225 ? 153.126 83.958  235.956 1.00 128.44 ? 3225 LYS A N     1 
ATOM   13447 C  CA    . LYS A 1 3225 ? 151.888 83.209  235.759 1.00 127.59 ? 3225 LYS A CA    1 
ATOM   13448 C  C     . LYS A 1 3225 ? 152.166 81.796  235.264 1.00 130.39 ? 3225 LYS A C     1 
ATOM   13449 O  O     . LYS A 1 3225 ? 151.449 80.860  235.627 1.00 131.23 ? 3225 LYS A O     1 
ATOM   13450 C  CB    . LYS A 1 3225 ? 150.966 83.945  234.786 1.00 124.59 ? 3225 LYS A CB    1 
ATOM   13451 C  CG    . LYS A 1 3225 ? 150.507 85.314  235.260 1.00 127.16 ? 3225 LYS A CG    1 
ATOM   13452 C  CD    . LYS A 1 3225 ? 149.697 85.217  236.541 1.00 128.98 ? 3225 LYS A CD    1 
ATOM   13453 C  CE    . LYS A 1 3225 ? 148.373 84.509  236.300 1.00 128.29 ? 3225 LYS A CE    1 
ATOM   13454 N  NZ    . LYS A 1 3225 ? 147.489 85.281  235.384 1.00 126.95 ? 3225 LYS A NZ    1 
ATOM   13455 N  N     . SER A 1 3226 ? 153.187 81.622  234.422 1.00 130.15 ? 3226 SER A N     1 
ATOM   13456 C  CA    . SER A 1 3226 ? 153.556 80.277  233.991 1.00 129.37 ? 3226 SER A CA    1 
ATOM   13457 C  C     . SER A 1 3226 ? 154.017 79.431  235.172 1.00 131.36 ? 3226 SER A C     1 
ATOM   13458 O  O     . SER A 1 3226 ? 153.630 78.261  235.301 1.00 128.65 ? 3226 SER A O     1 
ATOM   13459 C  CB    . SER A 1 3226 ? 154.647 80.347  232.922 1.00 123.18 ? 3226 SER A CB    1 
ATOM   13460 O  OG    . SER A 1 3226 ? 155.867 80.814  233.470 1.00 122.61 ? 3226 SER A OG    1 
ATOM   13461 N  N     . GLN A 1 3227 ? 154.841 80.011  236.050 1.00 130.45 ? 3227 GLN A N     1 
ATOM   13462 C  CA    . GLN A 1 3227 ? 155.267 79.286  237.245 1.00 126.33 ? 3227 GLN A CA    1 
ATOM   13463 C  C     . GLN A 1 3227 ? 154.075 78.938  238.132 1.00 130.07 ? 3227 GLN A C     1 
ATOM   13464 O  O     . GLN A 1 3227 ? 153.982 77.819  238.656 1.00 129.90 ? 3227 GLN A O     1 
ATOM   13465 C  CB    . GLN A 1 3227 ? 156.294 80.111  238.021 1.00 122.73 ? 3227 GLN A CB    1 
ATOM   13466 C  CG    . GLN A 1 3227 ? 156.811 79.441  239.285 1.00 118.84 ? 3227 GLN A CG    1 
ATOM   13467 C  CD    . GLN A 1 3227 ? 156.073 79.893  240.530 1.00 118.23 ? 3227 GLN A CD    1 
ATOM   13468 O  OE1   . GLN A 1 3227 ? 155.249 80.806  240.480 1.00 121.74 ? 3227 GLN A OE1   1 
ATOM   13469 N  NE2   . GLN A 1 3227 ? 156.365 79.253  241.657 1.00 111.92 ? 3227 GLN A NE2   1 
ATOM   13470 N  N     . GLU A 1 3228 ? 153.153 79.888  238.310 1.00 129.42 ? 3228 GLU A N     1 
ATOM   13471 C  CA    . GLU A 1 3228 ? 151.971 79.637  239.129 1.00 128.25 ? 3228 GLU A CA    1 
ATOM   13472 C  C     . GLU A 1 3228 ? 151.102 78.541  238.525 1.00 131.31 ? 3228 GLU A C     1 
ATOM   13473 O  O     . GLU A 1 3228 ? 150.566 77.695  239.249 1.00 130.32 ? 3228 GLU A O     1 
ATOM   13474 C  CB    . GLU A 1 3228 ? 151.171 80.928  239.301 1.00 125.79 ? 3228 GLU A CB    1 
ATOM   13475 C  CG    . GLU A 1 3228 ? 149.836 80.746  240.005 1.00 127.47 ? 3228 GLU A CG    1 
ATOM   13476 C  CD    . GLU A 1 3228 ? 148.885 81.901  239.757 1.00 130.78 ? 3228 GLU A CD    1 
ATOM   13477 O  OE1   . GLU A 1 3228 ? 149.224 82.786  238.945 1.00 129.33 ? 3228 GLU A OE1   1 
ATOM   13478 O  OE2   . GLU A 1 3228 ? 147.800 81.923  240.375 1.00 132.41 ? 3228 GLU A OE2   1 
ATOM   13479 N  N     . LEU A 1 3229 ? 150.943 78.548  237.200 1.00 132.74 ? 3229 LEU A N     1 
ATOM   13480 C  CA    . LEU A 1 3229 ? 150.167 77.509  236.532 1.00 131.90 ? 3229 LEU A CA    1 
ATOM   13481 C  C     . LEU A 1 3229 ? 150.810 76.142  236.708 1.00 132.93 ? 3229 LEU A C     1 
ATOM   13482 O  O     . LEU A 1 3229 ? 150.114 75.145  236.937 1.00 132.50 ? 3229 LEU A O     1 
ATOM   13483 C  CB    . LEU A 1 3229 ? 150.018 77.841  235.048 1.00 129.05 ? 3229 LEU A CB    1 
ATOM   13484 C  CG    . LEU A 1 3229 ? 149.314 76.793  234.185 1.00 126.70 ? 3229 LEU A CG    1 
ATOM   13485 C  CD1   . LEU A 1 3229 ? 147.947 76.453  234.758 1.00 128.33 ? 3229 LEU A CD1   1 
ATOM   13486 C  CD2   . LEU A 1 3229 ? 149.200 77.275  232.747 1.00 123.48 ? 3229 LEU A CD2   1 
ATOM   13487 N  N     . GLU A 1 3230 ? 152.139 76.070  236.591 1.00 132.21 ? 3230 GLU A N     1 
ATOM   13488 C  CA    . GLU A 1 3230 ? 152.822 74.801  236.824 1.00 129.55 ? 3230 GLU A CA    1 
ATOM   13489 C  C     . GLU A 1 3230 ? 152.605 74.317  238.251 1.00 132.96 ? 3230 GLU A C     1 
ATOM   13490 O  O     . GLU A 1 3230 ? 152.322 73.134  238.479 1.00 132.02 ? 3230 GLU A O     1 
ATOM   13491 C  CB    . GLU A 1 3230 ? 154.314 74.936  236.523 1.00 122.56 ? 3230 GLU A CB    1 
ATOM   13492 C  CG    . GLU A 1 3230 ? 154.649 74.949  235.043 1.00 118.25 ? 3230 GLU A CG    1 
ATOM   13493 C  CD    . GLU A 1 3230 ? 156.131 75.120  234.785 1.00 116.00 ? 3230 GLU A CD    1 
ATOM   13494 O  OE1   . GLU A 1 3230 ? 156.904 75.166  235.765 1.00 114.42 ? 3230 GLU A OE1   1 
ATOM   13495 O  OE2   . GLU A 1 3230 ? 156.524 75.205  233.603 1.00 114.71 ? 3230 GLU A OE2   1 
ATOM   13496 N  N     . VAL A 1 3231 ? 152.713 75.222  239.226 1.00 133.87 ? 3231 VAL A N     1 
ATOM   13497 C  CA    . VAL A 1 3231 ? 152.492 74.837  240.619 1.00 132.90 ? 3231 VAL A CA    1 
ATOM   13498 C  C     . VAL A 1 3231 ? 151.070 74.320  240.808 1.00 134.36 ? 3231 VAL A C     1 
ATOM   13499 O  O     . VAL A 1 3231 ? 150.845 73.273  241.428 1.00 133.28 ? 3231 VAL A O     1 
ATOM   13500 C  CB    . VAL A 1 3231 ? 152.793 76.021  241.557 1.00 125.40 ? 3231 VAL A CB    1 
ATOM   13501 C  CG1   . VAL A 1 3231 ? 152.221 75.764  242.943 1.00 119.53 ? 3231 VAL A CG1   1 
ATOM   13502 C  CG2   . VAL A 1 3231 ? 154.291 76.271  241.631 1.00 115.57 ? 3231 VAL A CG2   1 
ATOM   13503 N  N     . LYS A 1 3232 ? 150.091 75.041  240.256 1.00 135.04 ? 3232 LYS A N     1 
ATOM   13504 C  CA    . LYS A 1 3232 ? 148.691 74.668  240.429 1.00 130.80 ? 3232 LYS A CA    1 
ATOM   13505 C  C     . LYS A 1 3232 ? 148.392 73.315  239.795 1.00 132.00 ? 3232 LYS A C     1 
ATOM   13506 O  O     . LYS A 1 3232 ? 147.721 72.470  240.399 1.00 131.27 ? 3232 LYS A O     1 
ATOM   13507 C  CB    . LYS A 1 3232 ? 147.784 75.749  239.840 1.00 126.98 ? 3232 LYS A CB    1 
ATOM   13508 C  CG    . LYS A 1 3232 ? 147.745 77.040  240.641 1.00 123.59 ? 3232 LYS A CG    1 
ATOM   13509 C  CD    . LYS A 1 3232 ? 146.730 76.960  241.770 1.00 117.74 ? 3232 LYS A CD    1 
ATOM   13510 C  CE    . LYS A 1 3232 ? 146.364 78.343  242.282 1.00 114.44 ? 3232 LYS A CE    1 
ATOM   13511 N  NZ    . LYS A 1 3232 ? 145.203 78.303  243.214 1.00 114.25 ? 3232 LYS A NZ    1 
ATOM   13512 N  N     . ASN A 1 3233 ? 148.882 73.087  238.572 1.00 134.02 ? 3233 ASN A N     1 
ATOM   13513 C  CA    . ASN A 1 3233 ? 148.560 71.834  237.896 1.00 134.59 ? 3233 ASN A CA    1 
ATOM   13514 C  C     . ASN A 1 3233 ? 149.284 70.659  238.543 1.00 137.15 ? 3233 ASN A C     1 
ATOM   13515 O  O     . ASN A 1 3233 ? 148.724 69.561  238.644 1.00 136.50 ? 3233 ASN A O     1 
ATOM   13516 C  CB    . ASN A 1 3233 ? 148.854 71.940  236.391 1.00 133.35 ? 3233 ASN A CB    1 
ATOM   13517 C  CG    . ASN A 1 3233 ? 150.342 72.033  236.056 1.00 132.73 ? 3233 ASN A CG    1 
ATOM   13518 O  OD1   . ASN A 1 3233 ? 151.200 71.505  236.759 1.00 135.27 ? 3233 ASN A OD1   1 
ATOM   13519 N  ND2   . ASN A 1 3233 ? 150.645 72.719  234.960 1.00 124.29 ? 3233 ASN A ND2   1 
ATOM   13520 N  N     . ALA A 1 3234 ? 150.522 70.870  239.006 1.00 137.86 ? 3234 ALA A N     1 
ATOM   13521 C  CA    . ALA A 1 3234 ? 151.215 69.815  239.737 1.00 133.67 ? 3234 ALA A CA    1 
ATOM   13522 C  C     . ALA A 1 3234 ? 150.483 69.469  241.027 1.00 135.49 ? 3234 ALA A C     1 
ATOM   13523 O  O     . ALA A 1 3234 ? 150.325 68.288  241.363 1.00 133.65 ? 3234 ALA A O     1 
ATOM   13524 C  CB    . ALA A 1 3234 ? 152.655 70.237  240.031 1.00 123.38 ? 3234 ALA A CB    1 
ATOM   13525 N  N     . ALA A 1 3235 ? 150.018 70.486  241.760 1.00 136.20 ? 3235 ALA A N     1 
ATOM   13526 C  CA    . ALA A 1 3235 ? 149.271 70.229  242.987 1.00 130.93 ? 3235 ALA A CA    1 
ATOM   13527 C  C     . ALA A 1 3235 ? 147.971 69.488  242.699 1.00 133.92 ? 3235 ALA A C     1 
ATOM   13528 O  O     . ALA A 1 3235 ? 147.603 68.559  243.428 1.00 132.21 ? 3235 ALA A O     1 
ATOM   13529 C  CB    . ALA A 1 3235 ? 148.991 71.542  243.717 1.00 119.30 ? 3235 ALA A CB    1 
ATOM   13530 N  N     . ALA A 1 3236 ? 147.259 69.888  241.642 1.00 136.27 ? 3236 ALA A N     1 
ATOM   13531 C  CA    . ALA A 1 3236 ? 146.012 69.216  241.292 1.00 134.73 ? 3236 ALA A CA    1 
ATOM   13532 C  C     . ALA A 1 3236 ? 146.255 67.762  240.907 1.00 134.58 ? 3236 ALA A C     1 
ATOM   13533 O  O     . ALA A 1 3236 ? 145.503 66.869  241.319 1.00 131.13 ? 3236 ALA A O     1 
ATOM   13534 C  CB    . ALA A 1 3236 ? 145.313 69.964  240.156 1.00 129.07 ? 3236 ALA A CB    1 
ATOM   13535 N  N     . ASN A 1 3237 ? 147.302 67.503  240.119 1.00 135.76 ? 3237 ASN A N     1 
ATOM   13536 C  CA    . ASN A 1 3237 ? 147.614 66.131  239.731 1.00 134.09 ? 3237 ASN A CA    1 
ATOM   13537 C  C     . ASN A 1 3237 ? 148.003 65.290  240.939 1.00 134.58 ? 3237 ASN A C     1 
ATOM   13538 O  O     . ASN A 1 3237 ? 147.615 64.120  241.041 1.00 130.90 ? 3237 ASN A O     1 
ATOM   13539 C  CB    . ASN A 1 3237 ? 148.729 66.122  238.685 1.00 128.53 ? 3237 ASN A CB    1 
ATOM   13540 C  CG    . ASN A 1 3237 ? 148.304 66.758  237.376 1.00 125.84 ? 3237 ASN A CG    1 
ATOM   13541 O  OD1   . ASN A 1 3237 ? 147.250 67.389  237.292 1.00 127.05 ? 3237 ASN A OD1   1 
ATOM   13542 N  ND2   . ASN A 1 3237 ? 149.124 66.594  236.344 1.00 119.26 ? 3237 ASN A ND2   1 
ATOM   13543 N  N     . ASP A 1 3238 ? 148.778 65.864  241.864 1.00 136.96 ? 3238 ASP A N     1 
ATOM   13544 C  CA    . ASP A 1 3238 ? 149.147 65.133  243.072 1.00 134.78 ? 3238 ASP A CA    1 
ATOM   13545 C  C     . ASP A 1 3238 ? 147.927 64.832  243.935 1.00 134.80 ? 3238 ASP A C     1 
ATOM   13546 O  O     . ASP A 1 3238 ? 147.809 63.733  244.491 1.00 131.32 ? 3238 ASP A O     1 
ATOM   13547 C  CB    . ASP A 1 3238 ? 150.186 65.923  243.866 1.00 131.62 ? 3238 ASP A CB    1 
ATOM   13548 C  CG    . ASP A 1 3238 ? 151.587 65.767  243.308 1.00 129.89 ? 3238 ASP A CG    1 
ATOM   13549 O  OD1   . ASP A 1 3238 ? 151.764 64.982  242.353 1.00 130.61 ? 3238 ASP A OD1   1 
ATOM   13550 O  OD2   . ASP A 1 3238 ? 152.511 66.430  243.824 1.00 125.15 ? 3238 ASP A OD2   1 
ATOM   13551 N  N     . LYS A 1 3239 ? 147.010 65.795  244.061 1.00 136.26 ? 3239 LYS A N     1 
ATOM   13552 C  CA    . LYS A 1 3239 ? 145.820 65.583  244.878 1.00 134.50 ? 3239 LYS A CA    1 
ATOM   13553 C  C     . LYS A 1 3239 ? 144.867 64.577  244.245 1.00 134.35 ? 3239 LYS A C     1 
ATOM   13554 O  O     . LYS A 1 3239 ? 144.184 63.839  244.963 1.00 133.51 ? 3239 LYS A O     1 
ATOM   13555 C  CB    . LYS A 1 3239 ? 145.104 66.912  245.119 1.00 131.55 ? 3239 LYS A CB    1 
ATOM   13556 C  CG    . LYS A 1 3239 ? 145.715 67.753  246.229 1.00 125.62 ? 3239 LYS A CG    1 
ATOM   13557 C  CD    . LYS A 1 3239 ? 144.730 68.792  246.741 1.00 120.99 ? 3239 LYS A CD    1 
ATOM   13558 C  CE    . LYS A 1 3239 ? 145.364 69.676  247.803 1.00 114.78 ? 3239 LYS A CE    1 
ATOM   13559 N  NZ    . LYS A 1 3239 ? 144.417 70.712  248.301 1.00 113.89 ? 3239 LYS A NZ    1 
ATOM   13560 N  N     . LEU A 1 3240 ? 144.800 64.538  242.911 1.00 134.09 ? 3240 LEU A N     1 
ATOM   13561 C  CA    . LEU A 1 3240 ? 143.907 63.595  242.243 1.00 132.17 ? 3240 LEU A CA    1 
ATOM   13562 C  C     . LEU A 1 3240 ? 144.303 62.149  242.515 1.00 132.60 ? 3240 LEU A C     1 
ATOM   13563 O  O     . LEU A 1 3240 ? 143.444 61.260  242.507 1.00 128.82 ? 3240 LEU A O     1 
ATOM   13564 C  CB    . LEU A 1 3240 ? 143.887 63.864  240.739 1.00 128.13 ? 3240 LEU A CB    1 
ATOM   13565 C  CG    . LEU A 1 3240 ? 143.009 65.024  240.266 1.00 126.70 ? 3240 LEU A CG    1 
ATOM   13566 C  CD1   . LEU A 1 3240 ? 143.335 65.392  238.828 1.00 120.02 ? 3240 LEU A CD1   1 
ATOM   13567 C  CD2   . LEU A 1 3240 ? 141.537 64.671  240.410 1.00 124.01 ? 3240 LEU A CD2   1 
ATOM   13568 N  N     . LYS A 1 3241 ? 145.591 61.894  242.755 1.00 135.40 ? 3241 LYS A N     1 
ATOM   13569 C  CA    . LYS A 1 3241 ? 146.050 60.532  243.007 1.00 133.80 ? 3241 LYS A CA    1 
ATOM   13570 C  C     . LYS A 1 3241 ? 145.566 59.989  244.346 1.00 131.10 ? 3241 LYS A C     1 
ATOM   13571 O  O     . LYS A 1 3241 ? 145.609 58.773  244.557 1.00 121.46 ? 3241 LYS A O     1 
ATOM   13572 C  CB    . LYS A 1 3241 ? 147.577 60.473  242.943 1.00 127.73 ? 3241 LYS A CB    1 
ATOM   13573 C  CG    . LYS A 1 3241 ? 148.139 60.552  241.533 1.00 120.44 ? 3241 LYS A CG    1 
ATOM   13574 C  CD    . LYS A 1 3241 ? 149.533 61.158  241.527 1.00 120.33 ? 3241 LYS A CD    1 
ATOM   13575 C  CE    . LYS A 1 3241 ? 149.919 61.636  240.137 1.00 119.29 ? 3241 LYS A CE    1 
ATOM   13576 N  NZ    . LYS A 1 3241 ? 151.194 62.405  240.148 1.00 113.24 ? 3241 LYS A NZ    1 
ATOM   13577 N  N     . LYS A 1 3242 ? 145.113 60.854  245.248 1.00 131.91 ? 3242 LYS A N     1 
ATOM   13578 C  CA    . LYS A 1 3242 ? 144.621 60.415  246.550 1.00 124.42 ? 3242 LYS A CA    1 
ATOM   13579 C  C     . LYS A 1 3242 ? 143.307 59.652  246.414 1.00 118.56 ? 3242 LYS A C     1 
ATOM   13580 O  O     . LYS A 1 3242 ? 142.602 59.777  245.412 0.00 121.88 ? 3242 LYS A O     1 
ATOM   13581 C  CB    . LYS A 1 3242 ? 144.438 61.612  247.486 1.00 120.85 ? 3242 LYS A CB    1 
ATOM   13582 C  CG    . LYS A 1 3242 ? 145.724 62.098  248.134 1.00 119.67 ? 3242 LYS A CG    1 
ATOM   13583 C  CD    . LYS A 1 3242 ? 145.469 63.304  249.023 1.00 116.17 ? 3242 LYS A CD    1 
ATOM   13584 C  CE    . LYS A 1 3242 ? 146.755 63.800  249.664 1.00 107.31 ? 3242 LYS A CE    1 
ATOM   13585 N  NZ    . LYS A 1 3242 ? 146.571 65.121  250.326 1.00 99.26  ? 3242 LYS A NZ    1 
ATOM   13586 N  N     . GLU A 1 3449 ? 134.804 67.052  244.694 1.00 126.46 ? 3449 GLU A N     1 
ATOM   13587 C  CA    . GLU A 1 3449 ? 134.360 68.439  244.769 1.00 132.27 ? 3449 GLU A CA    1 
ATOM   13588 C  C     . GLU A 1 3449 ? 135.548 69.394  244.790 1.00 138.46 ? 3449 GLU A C     1 
ATOM   13589 O  O     . GLU A 1 3449 ? 135.626 70.319  243.981 1.00 136.85 ? 3449 GLU A O     1 
ATOM   13590 C  CB    . GLU A 1 3449 ? 133.489 68.658  246.007 1.00 128.60 ? 3449 GLU A CB    1 
ATOM   13591 C  CG    . GLU A 1 3449 ? 132.411 67.605  246.204 1.00 125.47 ? 3449 GLU A CG    1 
ATOM   13592 C  CD    . GLU A 1 3449 ? 131.647 67.790  247.499 1.00 120.92 ? 3449 GLU A CD    1 
ATOM   13593 O  OE1   . GLU A 1 3449 ? 131.879 68.806  248.187 1.00 120.59 ? 3449 GLU A OE1   1 
ATOM   13594 O  OE2   . GLU A 1 3449 ? 130.814 66.920  247.829 1.00 117.80 ? 3449 GLU A OE2   1 
ATOM   13595 N  N     . GLU A 1 3450 ? 136.469 69.166  245.729 1.00 141.25 ? 3450 GLU A N     1 
ATOM   13596 C  CA    . GLU A 1 3450 ? 137.647 70.021  245.834 1.00 138.37 ? 3450 GLU A CA    1 
ATOM   13597 C  C     . GLU A 1 3450 ? 138.517 69.919  244.587 1.00 139.36 ? 3450 GLU A C     1 
ATOM   13598 O  O     . GLU A 1 3450 ? 138.886 70.940  243.993 1.00 136.08 ? 3450 GLU A O     1 
ATOM   13599 C  CB    . GLU A 1 3450 ? 138.449 69.653  247.083 1.00 132.71 ? 3450 GLU A CB    1 
ATOM   13600 C  CG    . GLU A 1 3450 ? 139.542 70.647  247.441 1.00 132.02 ? 3450 GLU A CG    1 
ATOM   13601 C  CD    . GLU A 1 3450 ? 140.191 70.341  248.776 1.00 126.55 ? 3450 GLU A CD    1 
ATOM   13602 O  OE1   . GLU A 1 3450 ? 139.771 69.365  249.434 1.00 123.31 ? 3450 GLU A OE1   1 
ATOM   13603 O  OE2   . GLU A 1 3450 ? 141.121 71.076  249.169 1.00 121.09 ? 3450 GLU A OE2   1 
ATOM   13604 N  N     . TYR A 1 3451 ? 138.842 68.693  244.166 1.00 141.53 ? 3451 TYR A N     1 
ATOM   13605 C  CA    . TYR A 1 3451 ? 139.670 68.508  242.979 1.00 139.26 ? 3451 TYR A CA    1 
ATOM   13606 C  C     . TYR A 1 3451 ? 139.029 69.128  241.745 1.00 139.80 ? 3451 TYR A C     1 
ATOM   13607 O  O     . TYR A 1 3451 ? 139.739 69.620  240.860 1.00 138.53 ? 3451 TYR A O     1 
ATOM   13608 C  CB    . TYR A 1 3451 ? 139.939 67.020  242.753 1.00 135.20 ? 3451 TYR A CB    1 
ATOM   13609 C  CG    . TYR A 1 3451 ? 140.336 66.269  244.005 1.00 134.81 ? 3451 TYR A CG    1 
ATOM   13610 C  CD1   . TYR A 1 3451 ? 141.343 66.747  244.834 1.00 133.17 ? 3451 TYR A CD1   1 
ATOM   13611 C  CD2   . TYR A 1 3451 ? 139.705 65.083  244.357 1.00 130.38 ? 3451 TYR A CD2   1 
ATOM   13612 C  CE1   . TYR A 1 3451 ? 141.709 66.064  245.980 1.00 132.01 ? 3451 TYR A CE1   1 
ATOM   13613 C  CE2   . TYR A 1 3451 ? 140.065 64.393  245.501 1.00 125.86 ? 3451 TYR A CE2   1 
ATOM   13614 C  CZ    . TYR A 1 3451 ? 141.068 64.889  246.308 1.00 128.76 ? 3451 TYR A CZ    1 
ATOM   13615 O  OH    . TYR A 1 3451 ? 141.430 64.207  247.447 1.00 118.86 ? 3451 TYR A OH    1 
ATOM   13616 N  N     . ALA A 1 3452 ? 137.696 69.123  241.671 1.00 140.41 ? 3452 ALA A N     1 
ATOM   13617 C  CA    . ALA A 1 3452 ? 137.016 69.821  240.586 1.00 137.55 ? 3452 ALA A CA    1 
ATOM   13618 C  C     . ALA A 1 3452 ? 137.299 71.317  240.635 1.00 138.39 ? 3452 ALA A C     1 
ATOM   13619 O  O     . ALA A 1 3452 ? 137.530 71.948  239.597 1.00 137.44 ? 3452 ALA A O     1 
ATOM   13620 C  CB    . ALA A 1 3452 ? 135.512 69.553  240.648 1.00 129.79 ? 3452 ALA A CB    1 
ATOM   13621 N  N     . VAL A 1 3453 ? 137.294 71.900  241.836 1.00 138.94 ? 3453 VAL A N     1 
ATOM   13622 C  CA    . VAL A 1 3453 ? 137.607 73.319  241.974 1.00 136.50 ? 3453 VAL A CA    1 
ATOM   13623 C  C     . VAL A 1 3453 ? 139.042 73.593  241.538 1.00 135.97 ? 3453 VAL A C     1 
ATOM   13624 O  O     . VAL A 1 3453 ? 139.315 74.573  240.832 1.00 135.02 ? 3453 VAL A O     1 
ATOM   13625 C  CB    . VAL A 1 3453 ? 137.353 73.785  243.419 1.00 130.49 ? 3453 VAL A CB    1 
ATOM   13626 C  CG1   . VAL A 1 3453 ? 137.814 75.223  243.607 1.00 121.60 ? 3453 VAL A CG1   1 
ATOM   13627 C  CG2   . VAL A 1 3453 ? 135.879 73.642  243.770 1.00 124.61 ? 3453 VAL A CG2   1 
ATOM   13628 N  N     . LEU A 1 3454 ? 139.979 72.735  241.949 1.00 135.64 ? 3454 LEU A N     1 
ATOM   13629 C  CA    . LEU A 1 3454 ? 141.375 72.928  241.558 1.00 134.81 ? 3454 LEU A CA    1 
ATOM   13630 C  C     . LEU A 1 3454 ? 141.557 72.828  240.047 1.00 137.58 ? 3454 LEU A C     1 
ATOM   13631 O  O     . LEU A 1 3454 ? 142.272 73.637  239.448 1.00 137.32 ? 3454 LEU A O     1 
ATOM   13632 C  CB    . LEU A 1 3454 ? 142.288 71.934  242.280 1.00 131.74 ? 3454 LEU A CB    1 
ATOM   13633 C  CG    . LEU A 1 3454 ? 142.722 72.235  243.723 1.00 127.47 ? 3454 LEU A CG    1 
ATOM   13634 C  CD1   . LEU A 1 3454 ? 141.606 72.086  244.736 1.00 127.82 ? 3454 LEU A CD1   1 
ATOM   13635 C  CD2   . LEU A 1 3454 ? 143.911 71.362  244.106 1.00 119.34 ? 3454 LEU A CD2   1 
ATOM   13636 N  N     . ILE A 1 3455 ? 140.919 71.844  239.406 1.00 138.79 ? 3455 ILE A N     1 
ATOM   13637 C  CA    . ILE A 1 3455 ? 141.102 71.714  237.961 1.00 136.56 ? 3455 ILE A CA    1 
ATOM   13638 C  C     . ILE A 1 3455 ? 140.416 72.859  237.219 1.00 136.52 ? 3455 ILE A C     1 
ATOM   13639 O  O     . ILE A 1 3455 ? 140.931 73.340  236.201 1.00 134.49 ? 3455 ILE A O     1 
ATOM   13640 C  CB    . ILE A 1 3455 ? 140.630 70.335  237.456 1.00 133.34 ? 3455 ILE A CB    1 
ATOM   13641 C  CG1   . ILE A 1 3455 ? 139.133 70.133  237.687 1.00 131.41 ? 3455 ILE A CG1   1 
ATOM   13642 C  CG2   . ILE A 1 3455 ? 141.438 69.223  238.114 1.00 129.71 ? 3455 ILE A CG2   1 
ATOM   13643 C  CD1   . ILE A 1 3455 ? 138.661 68.715  237.437 1.00 122.35 ? 3455 ILE A CD1   1 
ATOM   13644 N  N     . SER A 1 3456 ? 139.261 73.325  237.706 1.00 137.83 ? 3456 SER A N     1 
ATOM   13645 C  CA    . SER A 1 3456 ? 138.610 74.472  237.080 1.00 134.57 ? 3456 SER A CA    1 
ATOM   13646 C  C     . SER A 1 3456 ? 139.464 75.729  237.205 1.00 135.46 ? 3456 SER A C     1 
ATOM   13647 O  O     . SER A 1 3456 ? 139.594 76.498  236.243 1.00 131.20 ? 3456 SER A O     1 
ATOM   13648 C  CB    . SER A 1 3456 ? 137.230 74.694  237.696 1.00 128.35 ? 3456 SER A CB    1 
ATOM   13649 O  OG    . SER A 1 3456 ? 137.335 75.182  239.022 1.00 129.98 ? 3456 SER A OG    1 
ATOM   13650 N  N     . GLU A 1 3457 ? 140.061 75.953  238.379 1.00 136.72 ? 3457 GLU A N     1 
ATOM   13651 C  CA    . GLU A 1 3457 ? 140.932 77.111  238.539 1.00 135.18 ? 3457 GLU A CA    1 
ATOM   13652 C  C     . GLU A 1 3457 ? 142.203 76.968  237.710 1.00 138.75 ? 3457 GLU A C     1 
ATOM   13653 O  O     . GLU A 1 3457 ? 142.728 77.969  237.213 1.00 138.25 ? 3457 GLU A O     1 
ATOM   13654 C  CB    . GLU A 1 3457 ? 141.255 77.333  240.020 1.00 131.48 ? 3457 GLU A CB    1 
ATOM   13655 C  CG    . GLU A 1 3457 ? 142.487 76.610  240.539 1.00 130.42 ? 3457 GLU A CG    1 
ATOM   13656 C  CD    . GLU A 1 3457 ? 142.615 76.689  242.047 1.00 125.84 ? 3457 GLU A CD    1 
ATOM   13657 O  OE1   . GLU A 1 3457 ? 141.727 77.289  242.689 1.00 123.40 ? 3457 GLU A OE1   1 
ATOM   13658 O  OE2   . GLU A 1 3457 ? 143.603 76.152  242.591 1.00 121.89 ? 3457 GLU A OE2   1 
ATOM   13659 N  N     . ALA A 1 3458 ? 142.697 75.740  237.527 1.00 139.50 ? 3458 ALA A N     1 
ATOM   13660 C  CA    . ALA A 1 3458 ? 143.842 75.529  236.648 1.00 137.26 ? 3458 ALA A CA    1 
ATOM   13661 C  C     . ALA A 1 3458 ? 143.494 75.864  235.204 1.00 137.44 ? 3458 ALA A C     1 
ATOM   13662 O  O     . ALA A 1 3458 ? 144.298 76.471  234.488 1.00 135.90 ? 3458 ALA A O     1 
ATOM   13663 C  CB    . ALA A 1 3458 ? 144.336 74.087  236.765 1.00 126.35 ? 3458 ALA A CB    1 
ATOM   13664 N  N     . GLN A 1 3459 ? 142.299 75.472  234.756 1.00 137.48 ? 3459 GLN A N     1 
ATOM   13665 C  CA    . GLN A 1 3459 ? 141.857 75.832  233.411 1.00 133.39 ? 3459 GLN A CA    1 
ATOM   13666 C  C     . GLN A 1 3459 ? 141.714 77.343  233.263 1.00 134.97 ? 3459 GLN A C     1 
ATOM   13667 O  O     . GLN A 1 3459 ? 142.080 77.915  232.226 1.00 132.62 ? 3459 GLN A O     1 
ATOM   13668 C  CB    . GLN A 1 3459 ? 140.537 75.131  233.090 1.00 128.77 ? 3459 GLN A CB    1 
ATOM   13669 C  CG    . GLN A 1 3459 ? 140.143 75.184  231.624 1.00 120.23 ? 3459 GLN A CG    1 
ATOM   13670 C  CD    . GLN A 1 3459 ? 138.864 74.424  231.339 1.00 114.29 ? 3459 GLN A CD    1 
ATOM   13671 O  OE1   . GLN A 1 3459 ? 138.734 73.252  231.692 1.00 117.40 ? 3459 GLN A OE1   1 
ATOM   13672 N  NE2   . GLN A 1 3459 ? 137.910 75.088  230.697 1.00 102.96 ? 3459 GLN A NE2   1 
ATOM   13673 N  N     . ALA A 1 3460 ? 141.175 78.006  234.290 1.00 136.80 ? 3460 ALA A N     1 
ATOM   13674 C  CA    . ALA A 1 3460 ? 141.063 79.461  234.252 1.00 133.08 ? 3460 ALA A CA    1 
ATOM   13675 C  C     . ALA A 1 3460 ? 142.437 80.118  234.178 1.00 133.55 ? 3460 ALA A C     1 
ATOM   13676 O  O     . ALA A 1 3460 ? 142.629 81.094  233.442 1.00 131.20 ? 3460 ALA A O     1 
ATOM   13677 C  CB    . ALA A 1 3460 ? 140.293 79.960  235.474 1.00 124.73 ? 3460 ALA A CB    1 
ATOM   13678 N  N     . ILE A 1 3461 ? 143.405 79.597  234.935 1.00 134.15 ? 3461 ILE A N     1 
ATOM   13679 C  CA    . ILE A 1 3461 ? 144.763 80.129  234.884 1.00 134.38 ? 3461 ILE A CA    1 
ATOM   13680 C  C     . ILE A 1 3461 ? 145.382 79.886  233.513 1.00 135.39 ? 3461 ILE A C     1 
ATOM   13681 O  O     . ILE A 1 3461 ? 146.124 80.728  232.998 1.00 133.48 ? 3461 ILE A O     1 
ATOM   13682 C  CB    . ILE A 1 3461 ? 145.616 79.526  236.016 1.00 133.10 ? 3461 ILE A CB    1 
ATOM   13683 C  CG1   . ILE A 1 3461 ? 145.103 79.996  237.379 1.00 129.10 ? 3461 ILE A CG1   1 
ATOM   13684 C  CG2   . ILE A 1 3461 ? 147.081 79.906  235.854 1.00 129.47 ? 3461 ILE A CG2   1 
ATOM   13685 C  CD1   . ILE A 1 3461 ? 145.050 81.500  237.528 1.00 122.33 ? 3461 ILE A CD1   1 
ATOM   13686 N  N     . LYS A 1 3462 ? 145.091 78.736  232.900 1.00 136.65 ? 3462 LYS A N     1 
ATOM   13687 C  CA    . LYS A 1 3462 ? 145.577 78.472  231.547 1.00 133.22 ? 3462 LYS A CA    1 
ATOM   13688 C  C     . LYS A 1 3462 ? 145.027 79.496  230.562 1.00 132.36 ? 3462 LYS A C     1 
ATOM   13689 O  O     . LYS A 1 3462 ? 145.763 80.028  229.720 1.00 129.00 ? 3462 LYS A O     1 
ATOM   13690 C  CB    . LYS A 1 3462 ? 145.190 77.058  231.112 1.00 129.23 ? 3462 LYS A CB    1 
ATOM   13691 C  CG    . LYS A 1 3462 ? 145.973 75.946  231.785 1.00 128.45 ? 3462 LYS A CG    1 
ATOM   13692 C  CD    . LYS A 1 3462 ? 145.332 74.591  231.531 1.00 124.90 ? 3462 LYS A CD    1 
ATOM   13693 C  CE    . LYS A 1 3462 ? 146.029 73.494  232.318 1.00 119.44 ? 3462 LYS A CE    1 
ATOM   13694 N  NZ    . LYS A 1 3462 ? 145.898 73.696  233.787 1.00 120.25 ? 3462 LYS A NZ    1 
ATOM   13695 N  N     . ALA A 1 3463 ? 143.726 79.783  230.653 1.00 132.70 ? 3463 ALA A N     1 
ATOM   13696 C  CA    . ALA A 1 3463 ? 143.124 80.777  229.769 1.00 128.19 ? 3463 ALA A CA    1 
ATOM   13697 C  C     . ALA A 1 3463 ? 143.724 82.160  230.002 1.00 131.21 ? 3463 ALA A C     1 
ATOM   13698 O  O     . ALA A 1 3463 ? 144.005 82.896  229.047 1.00 127.50 ? 3463 ALA A O     1 
ATOM   13699 C  CB    . ALA A 1 3463 ? 141.609 80.807  229.967 1.00 119.50 ? 3463 ALA A CB    1 
ATOM   13700 N  N     . ASP A 1 3464 ? 143.925 82.528  231.270 1.00 133.93 ? 3464 ASP A N     1 
ATOM   13701 C  CA    . ASP A 1 3464 ? 144.526 83.821  231.583 1.00 132.02 ? 3464 ASP A CA    1 
ATOM   13702 C  C     . ASP A 1 3464 ? 145.948 83.913  231.043 1.00 133.46 ? 3464 ASP A C     1 
ATOM   13703 O  O     . ASP A 1 3464 ? 146.350 84.952  230.509 1.00 133.21 ? 3464 ASP A O     1 
ATOM   13704 C  CB    . ASP A 1 3464 ? 144.509 84.054  233.094 1.00 130.60 ? 3464 ASP A CB    1 
ATOM   13705 C  CG    . ASP A 1 3464 ? 144.778 85.500  233.465 1.00 133.12 ? 3464 ASP A CG    1 
ATOM   13706 O  OD1   . ASP A 1 3464 ? 144.815 86.354  232.555 1.00 135.17 ? 3464 ASP A OD1   1 
ATOM   13707 O  OD2   . ASP A 1 3464 ? 144.954 85.782  234.669 1.00 129.41 ? 3464 ASP A OD2   1 
ATOM   13708 N  N     . LEU A 1 3465 ? 146.723 82.835  231.175 1.00 133.16 ? 3465 LEU A N     1 
ATOM   13709 C  CA    . LEU A 1 3465 ? 148.084 82.818  230.649 1.00 131.72 ? 3465 LEU A CA    1 
ATOM   13710 C  C     . LEU A 1 3465 ? 148.089 82.946  229.132 1.00 130.50 ? 3465 LEU A C     1 
ATOM   13711 O  O     . LEU A 1 3465 ? 148.930 83.653  228.564 1.00 127.56 ? 3465 LEU A O     1 
ATOM   13712 C  CB    . LEU A 1 3465 ? 148.793 81.535  231.081 1.00 130.19 ? 3465 LEU A CB    1 
ATOM   13713 C  CG    . LEU A 1 3465 ? 150.249 81.365  230.645 1.00 124.76 ? 3465 LEU A CG    1 
ATOM   13714 C  CD1   . LEU A 1 3465 ? 151.186 81.971  231.677 1.00 121.77 ? 3465 LEU A CD1   1 
ATOM   13715 C  CD2   . LEU A 1 3465 ? 150.574 79.897  230.417 1.00 117.24 ? 3465 LEU A CD2   1 
ATOM   13716 N  N     . ALA A 1 3466 ? 147.165 82.257  228.458 1.00 130.23 ? 3466 ALA A N     1 
ATOM   13717 C  CA    . ALA A 1 3466 ? 147.071 82.376  227.007 1.00 125.97 ? 3466 ALA A CA    1 
ATOM   13718 C  C     . ALA A 1 3466 ? 146.741 83.804  226.593 1.00 128.20 ? 3466 ALA A C     1 
ATOM   13719 O  O     . ALA A 1 3466 ? 147.352 84.347  225.664 1.00 125.80 ? 3466 ALA A O     1 
ATOM   13720 C  CB    . ALA A 1 3466 ? 146.025 81.402  226.466 1.00 117.74 ? 3466 ALA A CB    1 
ATOM   13721 N  N     . ALA A 1 3467 ? 145.784 84.434  227.278 1.00 129.82 ? 3467 ALA A N     1 
ATOM   13722 C  CA    . ALA A 1 3467 ? 145.443 85.818  226.962 1.00 125.73 ? 3467 ALA A CA    1 
ATOM   13723 C  C     . ALA A 1 3467 ? 146.623 86.749  227.217 1.00 127.25 ? 3467 ALA A C     1 
ATOM   13724 O  O     . ALA A 1 3467 ? 146.896 87.655  226.417 1.00 123.24 ? 3467 ALA A O     1 
ATOM   13725 C  CB    . ALA A 1 3467 ? 144.225 86.258  227.774 1.00 115.74 ? 3467 ALA A CB    1 
ATOM   13726 N  N     . VAL A 1 3468 ? 147.342 86.533  228.321 1.00 131.11 ? 3468 VAL A N     1 
ATOM   13727 C  CA    . VAL A 1 3468 ? 148.476 87.388  228.659 1.00 131.41 ? 3468 VAL A CA    1 
ATOM   13728 C  C     . VAL A 1 3468 ? 149.579 87.256  227.617 1.00 127.40 ? 3468 VAL A C     1 
ATOM   13729 O  O     . VAL A 1 3468 ? 150.159 88.256  227.180 1.00 125.37 ? 3468 VAL A O     1 
ATOM   13730 C  CB    . VAL A 1 3468 ? 148.987 87.062  230.076 1.00 130.41 ? 3468 VAL A CB    1 
ATOM   13731 C  CG1   . VAL A 1 3468 ? 150.384 87.626  230.285 1.00 126.57 ? 3468 VAL A CG1   1 
ATOM   13732 C  CG2   . VAL A 1 3468 ? 148.030 87.613  231.122 1.00 122.45 ? 3468 VAL A CG2   1 
ATOM   13733 N  N     . GLU A 1 3469 ? 149.887 86.025  227.196 1.00 124.96 ? 3469 GLU A N     1 
ATOM   13734 C  CA    . GLU A 1 3469 ? 150.943 85.851  226.204 1.00 122.31 ? 3469 GLU A CA    1 
ATOM   13735 C  C     . GLU A 1 3469 ? 150.518 86.368  224.835 1.00 120.05 ? 3469 GLU A C     1 
ATOM   13736 O  O     . GLU A 1 3469 ? 151.354 86.889  224.088 1.00 115.98 ? 3469 GLU A O     1 
ATOM   13737 C  CB    . GLU A 1 3469 ? 151.378 84.385  226.123 1.00 120.57 ? 3469 GLU A CB    1 
ATOM   13738 C  CG    . GLU A 1 3469 ? 150.327 83.416  225.620 1.00 120.33 ? 3469 GLU A CG    1 
ATOM   13739 C  CD    . GLU A 1 3469 ? 150.764 81.970  225.752 1.00 114.76 ? 3469 GLU A CD    1 
ATOM   13740 O  OE1   . GLU A 1 3469 ? 151.798 81.605  225.154 1.00 108.35 ? 3469 GLU A OE1   1 
ATOM   13741 O  OE2   . GLU A 1 3469 ? 150.077 81.199  226.454 1.00 114.70 ? 3469 GLU A OE2   1 
ATOM   13742 N  N     . ALA A 1 3470 ? 149.231 86.256  224.491 1.00 120.93 ? 3470 ALA A N     1 
ATOM   13743 C  CA    . ALA A 1 3470 ? 148.754 86.860  223.252 1.00 118.21 ? 3470 ALA A CA    1 
ATOM   13744 C  C     . ALA A 1 3470 ? 148.909 88.376  223.287 1.00 116.67 ? 3470 ALA A C     1 
ATOM   13745 O  O     . ALA A 1 3470 ? 149.354 88.987  222.306 1.00 110.99 ? 3470 ALA A O     1 
ATOM   13746 C  CB    . ALA A 1 3470 ? 147.296 86.473  223.005 1.00 111.89 ? 3470 ALA A CB    1 
ATOM   13747 N  N     . LYS A 1 3471 ? 148.558 88.998  224.416 1.00 118.23 ? 3471 LYS A N     1 
ATOM   13748 C  CA    . LYS A 1 3471 ? 148.734 90.441  224.554 1.00 112.86 ? 3471 LYS A CA    1 
ATOM   13749 C  C     . LYS A 1 3471 ? 150.207 90.825  224.482 1.00 113.65 ? 3471 LYS A C     1 
ATOM   13750 O  O     . LYS A 1 3471 ? 150.564 91.843  223.875 1.00 113.52 ? 3471 LYS A O     1 
ATOM   13751 C  CB    . LYS A 1 3471 ? 148.112 90.917  225.867 1.00 110.29 ? 3471 LYS A CB    1 
ATOM   13752 C  CG    . LYS A 1 3471 ? 148.590 92.283  226.334 1.00 109.83 ? 3471 LYS A CG    1 
ATOM   13753 C  CD    . LYS A 1 3471 ? 147.823 92.743  227.564 1.00 108.28 ? 3471 LYS A CD    1 
ATOM   13754 C  CE    . LYS A 1 3471 ? 146.401 93.145  227.210 1.00 105.78 ? 3471 LYS A CE    1 
ATOM   13755 N  NZ    . LYS A 1 3471 ? 145.706 93.792  228.357 1.00 100.79 ? 3471 LYS A NZ    1 
ATOM   13756 N  N     . VAL A 1 3472 ? 151.077 90.021  225.097 1.00 113.37 ? 3472 VAL A N     1 
ATOM   13757 C  CA    . VAL A 1 3472 ? 152.512 90.295  225.061 1.00 111.65 ? 3472 VAL A CA    1 
ATOM   13758 C  C     . VAL A 1 3472 ? 153.034 90.226  223.632 1.00 113.34 ? 3472 VAL A C     1 
ATOM   13759 O  O     . VAL A 1 3472 ? 153.812 91.084  223.199 1.00 113.90 ? 3472 VAL A O     1 
ATOM   13760 C  CB    . VAL A 1 3472 ? 153.264 89.323  225.989 1.00 112.48 ? 3472 VAL A CB    1 
ATOM   13761 C  CG1   . VAL A 1 3472 ? 154.752 89.327  225.676 1.00 103.73 ? 3472 VAL A CG1   1 
ATOM   13762 C  CG2   . VAL A 1 3472 ? 153.029 89.693  227.445 1.00 117.23 ? 3472 VAL A CG2   1 
ATOM   13763 N  N     . ASN A 1 3473 ? 152.619 89.205  222.879 1.00 116.04 ? 3473 ASN A N     1 
ATOM   13764 C  CA    . ASN A 1 3473 ? 153.045 89.090  221.487 1.00 110.85 ? 3473 ASN A CA    1 
ATOM   13765 C  C     . ASN A 1 3473 ? 152.529 90.257  220.653 1.00 106.01 ? 3473 ASN A C     1 
ATOM   13766 O  O     . ASN A 1 3473 ? 153.249 90.786  219.798 1.00 101.62 ? 3473 ASN A O     1 
ATOM   13767 C  CB    . ASN A 1 3473 ? 152.574 87.759  220.903 1.00 108.27 ? 3473 ASN A CB    1 
ATOM   13768 C  CG    . ASN A 1 3473 ? 153.402 86.587  221.388 1.00 110.94 ? 3473 ASN A CG    1 
ATOM   13769 O  OD1   . ASN A 1 3473 ? 154.390 86.763  222.101 1.00 113.01 ? 3473 ASN A OD1   1 
ATOM   13770 N  ND2   . ASN A 1 3473 ? 153.003 85.380  221.003 1.00 107.55 ? 3473 ASN A ND2   1 
ATOM   13771 N  N     . ARG A 1 3474 ? 151.280 90.670  220.885 1.00 103.80 ? 3474 ARG A N     1 
ATOM   13772 C  CA    . ARG A 1 3474 ? 150.726 91.806  220.153 1.00 100.84 ? 3474 ARG A CA    1 
ATOM   13773 C  C     . ARG A 1 3474 ? 151.507 93.083  220.447 1.00 105.53 ? 3474 ARG A C     1 
ATOM   13774 O  O     . ARG A 1 3474 ? 151.813 93.862  219.534 1.00 106.00 ? 3474 ARG A O     1 
ATOM   13775 C  CB    . ARG A 1 3474 ? 149.250 91.977  220.512 1.00 98.33  ? 3474 ARG A CB    1 
ATOM   13776 C  CG    . ARG A 1 3474 ? 148.442 92.809  219.532 1.00 91.17  ? 3474 ARG A CG    1 
ATOM   13777 C  CD    . ARG A 1 3474 ? 147.076 93.137  220.114 1.00 87.32  ? 3474 ARG A CD    1 
ATOM   13778 N  NE    . ARG A 1 3474 ? 146.304 94.028  219.257 1.00 93.16  ? 3474 ARG A NE    1 
ATOM   13779 C  CZ    . ARG A 1 3474 ? 145.588 93.631  218.214 1.00 98.54  ? 3474 ARG A CZ    1 
ATOM   13780 N  NH1   . ARG A 1 3474 ? 145.519 92.357  217.866 1.00 100.05 ? 3474 ARG A NH1   1 
ATOM   13781 N  NH2   . ARG A 1 3474 ? 144.923 94.537  217.502 1.00 99.19  ? 3474 ARG A NH2   1 
ATOM   13782 N  N     . SER A 1 3475 ? 151.849 93.307  221.716 1.00 106.94 ? 3475 SER A N     1 
ATOM   13783 C  CA    . SER A 1 3475 ? 152.612 94.497  222.080 1.00 104.79 ? 3475 SER A CA    1 
ATOM   13784 C  C     . SER A 1 3475 ? 154.031 94.442  221.521 1.00 103.35 ? 3475 SER A C     1 
ATOM   13785 O  O     . SER A 1 3475 ? 154.591 95.472  221.124 1.00 101.72 ? 3475 SER A O     1 
ATOM   13786 C  CB    . SER A 1 3475 ? 152.629 94.653  223.598 1.00 108.14 ? 3475 SER A CB    1 
ATOM   13787 O  OG    . SER A 1 3475 ? 153.015 93.445  224.229 1.00 108.36 ? 3475 SER A OG    1 
ATOM   13788 N  N     . THR A 1 3476 ? 154.633 93.251  221.488 1.00 104.76 ? 3476 THR A N     1 
ATOM   13789 C  CA    . THR A 1 3476 ? 155.952 93.109  220.880 1.00 100.51 ? 3476 THR A CA    1 
ATOM   13790 C  C     . THR A 1 3476 ? 155.901 93.401  219.386 1.00 103.72 ? 3476 THR A C     1 
ATOM   13791 O  O     . THR A 1 3476 ? 156.823 94.013  218.835 1.00 103.56 ? 3476 THR A O     1 
ATOM   13792 C  CB    . THR A 1 3476 ? 156.503 91.707  221.136 1.00 99.01  ? 3476 THR A CB    1 
ATOM   13793 O  OG1   . THR A 1 3476 ? 156.308 91.359  222.513 1.00 100.39 ? 3476 THR A OG1   1 
ATOM   13794 C  CG2   . THR A 1 3476 ? 157.989 91.653  220.813 1.00 92.77  ? 3476 THR A CG2   1 
ATOM   13795 N  N     . ALA A 1 3477 ? 154.835 92.961  218.712 1.00 101.46 ? 3477 ALA A N     1 
ATOM   13796 C  CA    . ALA A 1 3477 ? 154.656 93.309  217.306 1.00 98.81  ? 3477 ALA A CA    1 
ATOM   13797 C  C     . ALA A 1 3477 ? 154.500 94.814  217.133 1.00 100.69 ? 3477 ALA A C     1 
ATOM   13798 O  O     . ALA A 1 3477 ? 155.032 95.399  216.181 1.00 96.78  ? 3477 ALA A O     1 
ATOM   13799 C  CB    . ALA A 1 3477 ? 153.448 92.571  216.730 1.00 93.81  ? 3477 ALA A CB    1 
ATOM   13800 N  N     . LEU A 1 3478 ? 153.765 95.456  218.046 1.00 104.44 ? 3478 LEU A N     1 
ATOM   13801 C  CA    . LEU A 1 3478 ? 153.664 96.913  218.036 1.00 98.30  ? 3478 LEU A CA    1 
ATOM   13802 C  C     . LEU A 1 3478 ? 155.041 97.558  218.127 1.00 96.27  ? 3478 LEU A C     1 
ATOM   13803 O  O     . LEU A 1 3478 ? 155.355 98.491  217.380 1.00 93.92  ? 3478 LEU A O     1 
ATOM   13804 C  CB    . LEU A 1 3478 ? 152.791 97.389  219.195 1.00 100.69 ? 3478 LEU A CB    1 
ATOM   13805 C  CG    . LEU A 1 3478 ? 151.281 97.505  219.021 1.00 106.89 ? 3478 LEU A CG    1 
ATOM   13806 C  CD1   . LEU A 1 3478 ? 150.678 97.931  220.343 1.00 106.69 ? 3478 LEU A CD1   1 
ATOM   13807 C  CD2   . LEU A 1 3478 ? 150.931 98.496  217.923 1.00 101.05 ? 3478 LEU A CD2   1 
ATOM   13808 N  N     . LEU A 1 3479 ? 155.871 97.080  219.056 1.00 99.34  ? 3479 LEU A N     1 
ATOM   13809 C  CA    . LEU A 1 3479 ? 157.202 97.657  219.228 1.00 96.52  ? 3479 LEU A CA    1 
ATOM   13810 C  C     . LEU A 1 3479 ? 158.077 97.421  218.003 1.00 93.93  ? 3479 LEU A C     1 
ATOM   13811 O  O     . LEU A 1 3479 ? 158.855 98.296  217.609 1.00 94.59  ? 3479 LEU A O     1 
ATOM   13812 C  CB    . LEU A 1 3479 ? 157.871 97.088  220.477 1.00 96.25  ? 3479 LEU A CB    1 
ATOM   13813 C  CG    . LEU A 1 3479 ? 157.228 97.457  221.812 1.00 99.89  ? 3479 LEU A CG    1 
ATOM   13814 C  CD1   . LEU A 1 3479 ? 158.069 96.916  222.945 1.00 98.61  ? 3479 LEU A CD1   1 
ATOM   13815 C  CD2   . LEU A 1 3479 ? 157.057 98.962  221.935 1.00 100.17 ? 3479 LEU A CD2   1 
ATOM   13816 N  N     . LYS A 1 3480 ? 157.978 96.238  217.397 1.00 95.81  ? 3480 LYS A N     1 
ATOM   13817 C  CA    . LYS A 1 3480 ? 158.740 95.973  216.180 1.00 97.42  ? 3480 LYS A CA    1 
ATOM   13818 C  C     . LYS A 1 3480 ? 158.310 96.904  215.053 1.00 96.13  ? 3480 LYS A C     1 
ATOM   13819 O  O     . LYS A 1 3480 ? 159.149 97.401  214.293 1.00 86.52  ? 3480 LYS A O     1 
ATOM   13820 C  CB    . LYS A 1 3480 ? 158.583 94.510  215.766 1.00 99.49  ? 3480 LYS A CB    1 
ATOM   13821 C  CG    . LYS A 1 3480 ? 159.257 93.526  216.709 1.00 99.72  ? 3480 LYS A CG    1 
ATOM   13822 C  CD    . LYS A 1 3480 ? 159.265 92.120  216.132 1.00 98.94  ? 3480 LYS A CD    1 
ATOM   13823 C  CE    . LYS A 1 3480 ? 157.872 91.513  216.141 1.00 95.94  ? 3480 LYS A CE    1 
ATOM   13824 N  NZ    . LYS A 1 3480 ? 157.452 91.115  217.512 1.00 93.95  ? 3480 LYS A NZ    1 
ATOM   13825 N  N     . SER A 1 3481 ? 157.004 97.152  214.930 1.00 97.54  ? 3481 SER A N     1 
ATOM   13826 C  CA    . SER A 1 3481 ? 156.519 98.076  213.910 1.00 93.45  ? 3481 SER A CA    1 
ATOM   13827 C  C     . SER A 1 3481 ? 156.957 99.507  214.202 1.00 94.16  ? 3481 SER A C     1 
ATOM   13828 O  O     . SER A 1 3481 ? 157.224 100.282 213.276 1.00 91.86  ? 3481 SER A O     1 
ATOM   13829 C  CB    . SER A 1 3481 ? 154.997 97.993  213.808 1.00 91.20  ? 3481 SER A CB    1 
ATOM   13830 O  OG    . SER A 1 3481 ? 154.573 96.661  213.580 1.00 96.75  ? 3481 SER A OG    1 
ATOM   13831 N  N     . LEU A 1 3482 ? 157.028 99.877  215.478 1.00 94.35  ? 3482 LEU A N     1 
ATOM   13832 C  CA    . LEU A 1 3482 ? 157.355 101.238 215.880 1.00 91.22  ? 3482 LEU A CA    1 
ATOM   13833 C  C     . LEU A 1 3482 ? 158.847 101.470 216.081 1.00 93.13  ? 3482 LEU A C     1 
ATOM   13834 O  O     . LEU A 1 3482 ? 159.235 102.577 216.461 1.00 98.02  ? 3482 LEU A O     1 
ATOM   13835 C  CB    . LEU A 1 3482 ? 156.607 101.598 217.168 1.00 85.13  ? 3482 LEU A CB    1 
ATOM   13836 C  CG    . LEU A 1 3482 ? 155.104 101.852 217.040 1.00 81.59  ? 3482 LEU A CG    1 
ATOM   13837 C  CD1   . LEU A 1 3482 ? 154.545 102.402 218.341 1.00 83.77  ? 3482 LEU A CD1   1 
ATOM   13838 C  CD2   . LEU A 1 3482 ? 154.814 102.800 215.888 1.00 86.05  ? 3482 LEU A CD2   1 
ATOM   13839 N  N     . SER A 1 3483 ? 159.684 100.452 215.876 1.00 92.27  ? 3483 SER A N     1 
ATOM   13840 C  CA    . SER A 1 3483 ? 161.127 100.648 215.998 1.00 91.28  ? 3483 SER A CA    1 
ATOM   13841 C  C     . SER A 1 3483 ? 161.646 101.651 214.973 1.00 96.01  ? 3483 SER A C     1 
ATOM   13842 O  O     . SER A 1 3483 ? 162.563 102.431 215.264 1.00 95.88  ? 3483 SER A O     1 
ATOM   13843 C  CB    . SER A 1 3483 ? 161.850 99.309  215.851 1.00 89.44  ? 3483 SER A CB    1 
ATOM   13844 O  OG    . SER A 1 3483 ? 163.255 99.478  215.931 1.00 87.66  ? 3483 SER A OG    1 
ATOM   13845 N  N     . ALA A 1 3484 ? 161.087 101.633 213.760 1.00 93.03  ? 3484 ALA A N     1 
ATOM   13846 C  CA    . ALA A 1 3484 ? 161.487 102.610 212.751 1.00 92.90  ? 3484 ALA A CA    1 
ATOM   13847 C  C     . ALA A 1 3484 ? 161.146 104.027 213.193 1.00 95.69  ? 3484 ALA A C     1 
ATOM   13848 O  O     . ALA A 1 3484 ? 161.953 104.951 213.029 1.00 94.02  ? 3484 ALA A O     1 
ATOM   13849 C  CB    . ALA A 1 3484 ? 160.821 102.287 211.414 1.00 88.90  ? 3484 ALA A CB    1 
ATOM   13850 N  N     . GLU A 1 3485 ? 159.950 104.219 213.753 1.00 96.21  ? 3485 GLU A N     1 
ATOM   13851 C  CA    . GLU A 1 3485 ? 159.587 105.527 214.285 1.00 91.06  ? 3485 GLU A CA    1 
ATOM   13852 C  C     . GLU A 1 3485 ? 160.497 105.918 215.441 1.00 92.89  ? 3485 GLU A C     1 
ATOM   13853 O  O     . GLU A 1 3485 ? 160.929 107.071 215.534 1.00 97.40  ? 3485 GLU A O     1 
ATOM   13854 C  CB    . GLU A 1 3485 ? 158.121 105.527 214.717 1.00 93.70  ? 3485 GLU A CB    1 
ATOM   13855 C  CG    . GLU A 1 3485 ? 157.140 105.652 213.560 1.00 95.22  ? 3485 GLU A CG    1 
ATOM   13856 C  CD    . GLU A 1 3485 ? 156.787 104.315 212.936 1.00 99.11  ? 3485 GLU A CD    1 
ATOM   13857 O  OE1   . GLU A 1 3485 ? 157.324 103.284 213.389 1.00 98.53  ? 3485 GLU A OE1   1 
ATOM   13858 O  OE2   . GLU A 1 3485 ? 155.971 104.296 211.990 1.00 100.34 ? 3485 GLU A OE2   1 
ATOM   13859 N  N     . ARG A 1 3486 ? 160.794 104.970 216.334 1.00 95.11  ? 3486 ARG A N     1 
ATOM   13860 C  CA    . ARG A 1 3486 ? 161.785 105.190 217.386 1.00 93.42  ? 3486 ARG A CA    1 
ATOM   13861 C  C     . ARG A 1 3486 ? 163.077 105.769 216.827 1.00 95.05  ? 3486 ARG A C     1 
ATOM   13862 O  O     . ARG A 1 3486 ? 163.515 106.849 217.240 1.00 96.03  ? 3486 ARG A O     1 
ATOM   13863 C  CB    . ARG A 1 3486 ? 162.068 103.877 218.121 1.00 90.05  ? 3486 ARG A CB    1 
ATOM   13864 C  CG    . ARG A 1 3486 ? 163.211 103.955 219.136 1.00 94.29  ? 3486 ARG A CG    1 
ATOM   13865 C  CD    . ARG A 1 3486 ? 162.975 104.847 220.346 1.00 102.70 ? 3486 ARG A CD    1 
ATOM   13866 N  NE    . ARG A 1 3486 ? 161.947 104.347 221.250 1.00 104.91 ? 3486 ARG A NE    1 
ATOM   13867 C  CZ    . ARG A 1 3486 ? 161.441 105.043 222.259 1.00 106.55 ? 3486 ARG A CZ    1 
ATOM   13868 N  NH1   . ARG A 1 3486 ? 161.813 106.290 222.493 1.00 105.24 ? 3486 ARG A NH1   1 
ATOM   13869 N  NH2   . ARG A 1 3486 ? 160.558 104.467 223.068 1.00 102.36 ? 3486 ARG A NH2   1 
ATOM   13870 N  N     . GLU A 1 3487 ? 163.710 105.054 215.893 1.00 97.17  ? 3487 GLU A N     1 
ATOM   13871 C  CA    . GLU A 1 3487 ? 165.026 105.480 215.422 1.00 91.60  ? 3487 GLU A CA    1 
ATOM   13872 C  C     . GLU A 1 3487 ? 164.949 106.802 214.664 1.00 90.00  ? 3487 GLU A C     1 
ATOM   13873 O  O     . GLU A 1 3487 ? 165.802 107.679 214.855 1.00 91.98  ? 3487 GLU A O     1 
ATOM   13874 C  CB    . GLU A 1 3487 ? 165.669 104.391 214.560 1.00 89.16  ? 3487 GLU A CB    1 
ATOM   13875 C  CG    . GLU A 1 3487 ? 164.807 103.862 213.433 1.00 93.24  ? 3487 GLU A CG    1 
ATOM   13876 C  CD    . GLU A 1 3487 ? 165.174 102.447 213.034 1.00 95.77  ? 3487 GLU A CD    1 
ATOM   13877 O  OE1   . GLU A 1 3487 ? 165.972 101.812 213.756 1.00 97.32  ? 3487 GLU A OE1   1 
ATOM   13878 O  OE2   . GLU A 1 3487 ? 164.665 101.969 211.999 1.00 95.32  ? 3487 GLU A OE2   1 
ATOM   13879 N  N     . ARG A 1 3488 ? 163.932 106.977 213.812 1.00 87.73  ? 3488 ARG A N     1 
ATOM   13880 C  CA    . ARG A 1 3488 ? 163.824 108.220 213.053 1.00 90.25  ? 3488 ARG A CA    1 
ATOM   13881 C  C     . ARG A 1 3488 ? 163.592 109.413 213.972 1.00 91.16  ? 3488 ARG A C     1 
ATOM   13882 O  O     . ARG A 1 3488 ? 164.219 110.468 213.805 1.00 92.13  ? 3488 ARG A O     1 
ATOM   13883 C  CB    . ARG A 1 3488 ? 162.701 108.114 212.021 1.00 88.54  ? 3488 ARG A CB    1 
ATOM   13884 C  CG    . ARG A 1 3488 ? 162.487 109.388 211.222 1.00 85.06  ? 3488 ARG A CG    1 
ATOM   13885 C  CD    . ARG A 1 3488 ? 161.176 109.362 210.455 1.00 85.73  ? 3488 ARG A CD    1 
ATOM   13886 N  NE    . ARG A 1 3488 ? 160.789 108.012 210.066 1.00 92.21  ? 3488 ARG A NE    1 
ATOM   13887 C  CZ    . ARG A 1 3488 ? 159.584 107.677 209.627 1.00 87.09  ? 3488 ARG A CZ    1 
ATOM   13888 N  NH1   . ARG A 1 3488 ? 158.620 108.573 209.505 1.00 77.33  ? 3488 ARG A NH1   1 
ATOM   13889 N  NH2   . ARG A 1 3488 ? 159.341 106.411 209.300 1.00 86.94  ? 3488 ARG A NH2   1 
ATOM   13890 N  N     . TRP A 1 3489 ? 162.701 109.263 214.956 1.00 88.30  ? 3489 TRP A N     1 
ATOM   13891 C  CA    . TRP A 1 3489 ? 162.415 110.361 215.869 1.00 88.12  ? 3489 TRP A CA    1 
ATOM   13892 C  C     . TRP A 1 3489 ? 163.609 110.662 216.761 1.00 91.40  ? 3489 TRP A C     1 
ATOM   13893 O  O     . TRP A 1 3489 ? 163.875 111.828 217.067 1.00 94.67  ? 3489 TRP A O     1 
ATOM   13894 C  CB    . TRP A 1 3489 ? 161.177 110.033 216.700 1.00 84.48  ? 3489 TRP A CB    1 
ATOM   13895 C  CG    . TRP A 1 3489 ? 159.940 109.906 215.872 1.00 85.87  ? 3489 TRP A CG    1 
ATOM   13896 C  CD1   . TRP A 1 3489 ? 159.747 110.385 214.610 1.00 85.63  ? 3489 TRP A CD1   1 
ATOM   13897 C  CD2   . TRP A 1 3489 ? 158.723 109.247 216.241 1.00 87.56  ? 3489 TRP A CD2   1 
ATOM   13898 N  NE1   . TRP A 1 3489 ? 158.484 110.072 214.171 1.00 82.78  ? 3489 TRP A NE1   1 
ATOM   13899 C  CE2   . TRP A 1 3489 ? 157.835 109.373 215.154 1.00 86.39  ? 3489 TRP A CE2   1 
ATOM   13900 C  CE3   . TRP A 1 3489 ? 158.298 108.566 217.384 1.00 85.58  ? 3489 TRP A CE3   1 
ATOM   13901 C  CZ2   . TRP A 1 3489 ? 156.549 108.843 215.178 1.00 86.80  ? 3489 TRP A CZ2   1 
ATOM   13902 C  CZ3   . TRP A 1 3489 ? 157.021 108.042 217.405 1.00 88.52  ? 3489 TRP A CZ3   1 
ATOM   13903 C  CH2   . TRP A 1 3489 ? 156.162 108.183 216.309 1.00 89.62  ? 3489 TRP A CH2   1 
ATOM   13904 N  N     . GLU A 1 3490 ? 164.344 109.631 217.184 1.00 92.65  ? 3490 GLU A N     1 
ATOM   13905 C  CA    . GLU A 1 3490 ? 165.558 109.869 217.956 1.00 90.58  ? 3490 GLU A CA    1 
ATOM   13906 C  C     . GLU A 1 3490 ? 166.590 110.632 217.136 1.00 90.54  ? 3490 GLU A C     1 
ATOM   13907 O  O     . GLU A 1 3490 ? 167.229 111.563 217.641 1.00 90.04  ? 3490 GLU A O     1 
ATOM   13908 C  CB    . GLU A 1 3490 ? 166.138 108.544 218.449 1.00 90.78  ? 3490 GLU A CB    1 
ATOM   13909 C  CG    . GLU A 1 3490 ? 165.448 107.983 219.680 1.00 93.72  ? 3490 GLU A CG    1 
ATOM   13910 C  CD    . GLU A 1 3490 ? 165.985 106.622 220.078 1.00 101.50 ? 3490 GLU A CD    1 
ATOM   13911 O  OE1   . GLU A 1 3490 ? 166.069 105.735 219.202 1.00 103.79 ? 3490 GLU A OE1   1 
ATOM   13912 O  OE2   . GLU A 1 3490 ? 166.323 106.438 221.266 1.00 97.79  ? 3490 GLU A OE2   1 
ATOM   13913 N  N     . LYS A 1 3491 ? 166.763 110.258 215.864 1.00 90.19  ? 3491 LYS A N     1 
ATOM   13914 C  CA    . LYS A 1 3491 ? 167.711 110.969 215.012 1.00 92.21  ? 3491 LYS A CA    1 
ATOM   13915 C  C     . LYS A 1 3491 ? 167.301 112.424 214.816 1.00 93.12  ? 3491 LYS A C     1 
ATOM   13916 O  O     . LYS A 1 3491 ? 168.141 113.328 214.889 1.00 91.47  ? 3491 LYS A O     1 
ATOM   13917 C  CB    . LYS A 1 3491 ? 167.841 110.264 213.662 1.00 89.19  ? 3491 LYS A CB    1 
ATOM   13918 C  CG    . LYS A 1 3491 ? 168.600 108.950 213.716 1.00 94.04  ? 3491 LYS A CG    1 
ATOM   13919 C  CD    . LYS A 1 3491 ? 169.937 109.120 214.420 1.00 89.22  ? 3491 LYS A CD    1 
ATOM   13920 C  CE    . LYS A 1 3491 ? 170.512 107.780 214.846 1.00 92.27  ? 3491 LYS A CE    1 
ATOM   13921 N  NZ    . LYS A 1 3491 ? 169.674 107.119 215.883 1.00 91.17  ? 3491 LYS A NZ    1 
ATOM   13922 N  N     . THR A 1 3492 ? 166.014 112.670 214.565 1.00 94.97  ? 3492 THR A N     1 
ATOM   13923 C  CA    . THR A 1 3492 ? 165.560 114.041 214.347 1.00 88.91  ? 3492 THR A CA    1 
ATOM   13924 C  C     . THR A 1 3492 ? 165.639 114.873 215.624 1.00 88.81  ? 3492 THR A C     1 
ATOM   13925 O  O     . THR A 1 3492 ? 165.983 116.060 215.573 1.00 90.56  ? 3492 THR A O     1 
ATOM   13926 C  CB    . THR A 1 3492 ? 164.142 114.041 213.778 1.00 85.59  ? 3492 THR A CB    1 
ATOM   13927 O  OG1   . THR A 1 3492 ? 163.283 113.286 214.638 1.00 92.09  ? 3492 THR A OG1   1 
ATOM   13928 C  CG2   . THR A 1 3492 ? 164.124 113.436 212.383 1.00 80.89  ? 3492 THR A CG2   1 
ATOM   13929 N  N     . SER A 1 3493 ? 165.324 114.277 216.776 1.00 87.77  ? 3493 SER A N     1 
ATOM   13930 C  CA    . SER A 1 3493 ? 165.399 114.998 218.042 1.00 83.46  ? 3493 SER A CA    1 
ATOM   13931 C  C     . SER A 1 3493 ? 166.833 115.211 218.506 1.00 85.86  ? 3493 SER A C     1 
ATOM   13932 O  O     . SER A 1 3493 ? 167.083 116.122 219.301 1.00 84.94  ? 3493 SER A O     1 
ATOM   13933 C  CB    . SER A 1 3493 ? 164.610 114.249 219.117 1.00 82.87  ? 3493 SER A CB    1 
ATOM   13934 O  OG    . SER A 1 3493 ? 164.773 114.854 220.388 1.00 85.50  ? 3493 SER A OG    1 
ATOM   13935 N  N     . GLU A 1 3494 ? 167.774 114.386 218.040 1.00 90.48  ? 3494 GLU A N     1 
ATOM   13936 C  CA    . GLU A 1 3494 ? 169.175 114.588 218.391 1.00 92.03  ? 3494 GLU A CA    1 
ATOM   13937 C  C     . GLU A 1 3494 ? 169.717 115.889 217.815 1.00 91.23  ? 3494 GLU A C     1 
ATOM   13938 O  O     . GLU A 1 3494 ? 170.624 116.494 218.397 1.00 92.26  ? 3494 GLU A O     1 
ATOM   13939 C  CB    . GLU A 1 3494 ? 170.010 113.402 217.907 1.00 95.25  ? 3494 GLU A CB    1 
ATOM   13940 C  CG    . GLU A 1 3494 ? 171.449 113.401 218.396 1.00 97.85  ? 3494 GLU A CG    1 
ATOM   13941 C  CD    . GLU A 1 3494 ? 172.426 113.842 217.323 1.00 103.09 ? 3494 GLU A CD    1 
ATOM   13942 O  OE1   . GLU A 1 3494 ? 172.041 113.852 216.134 1.00 99.16  ? 3494 GLU A OE1   1 
ATOM   13943 O  OE2   . GLU A 1 3494 ? 173.578 114.180 217.667 1.00 106.77 ? 3494 GLU A OE2   1 
ATOM   13944 N  N     . THR A 1 3495 ? 169.173 116.336 216.686 1.00 92.98  ? 3495 THR A N     1 
ATOM   13945 C  CA    . THR A 1 3495 ? 169.639 117.536 216.005 1.00 93.46  ? 3495 THR A CA    1 
ATOM   13946 C  C     . THR A 1 3495 ? 168.887 118.793 216.429 1.00 89.03  ? 3495 THR A C     1 
ATOM   13947 O  O     . THR A 1 3495 ? 169.143 119.863 215.869 1.00 88.75  ? 3495 THR A O     1 
ATOM   13948 C  CB    . THR A 1 3495 ? 169.525 117.357 214.489 1.00 87.44  ? 3495 THR A CB    1 
ATOM   13949 O  OG1   . THR A 1 3495 ? 168.144 117.248 214.121 1.00 77.48  ? 3495 THR A OG1   1 
ATOM   13950 C  CG2   . THR A 1 3495 ? 170.263 116.103 214.046 1.00 85.41  ? 3495 THR A CG2   1 
ATOM   13951 N  N     . PHE A 1 3496 ? 167.977 118.688 217.402 1.00 82.37  ? 3496 PHE A N     1 
ATOM   13952 C  CA    . PHE A 1 3496 ? 167.161 119.832 217.804 1.00 78.70  ? 3496 PHE A CA    1 
ATOM   13953 C  C     . PHE A 1 3496 ? 168.021 121.051 218.114 1.00 82.94  ? 3496 PHE A C     1 
ATOM   13954 O  O     . PHE A 1 3496 ? 167.755 122.157 217.627 1.00 81.92  ? 3496 PHE A O     1 
ATOM   13955 C  CB    . PHE A 1 3496 ? 166.309 119.454 219.014 1.00 79.12  ? 3496 PHE A CB    1 
ATOM   13956 C  CG    . PHE A 1 3496 ? 165.765 120.633 219.771 1.00 76.65  ? 3496 PHE A CG    1 
ATOM   13957 C  CD1   . PHE A 1 3496 ? 164.656 121.318 219.307 1.00 70.93  ? 3496 PHE A CD1   1 
ATOM   13958 C  CD2   . PHE A 1 3496 ? 166.356 121.047 220.953 1.00 70.77  ? 3496 PHE A CD2   1 
ATOM   13959 C  CE1   . PHE A 1 3496 ? 164.151 122.399 220.001 1.00 66.72  ? 3496 PHE A CE1   1 
ATOM   13960 C  CE2   . PHE A 1 3496 ? 165.855 122.128 221.651 1.00 69.31  ? 3496 PHE A CE2   1 
ATOM   13961 C  CZ    . PHE A 1 3496 ? 164.751 122.804 221.174 1.00 69.81  ? 3496 PHE A CZ    1 
ATOM   13962 N  N     . LYS A 1 3497 ? 169.068 120.864 218.920 1.00 82.97  ? 3497 LYS A N     1 
ATOM   13963 C  CA    . LYS A 1 3497 ? 169.969 121.969 219.227 1.00 75.49  ? 3497 LYS A CA    1 
ATOM   13964 C  C     . LYS A 1 3497 ? 170.703 122.442 217.978 1.00 75.53  ? 3497 LYS A C     1 
ATOM   13965 O  O     . LYS A 1 3497 ? 171.033 123.628 217.854 1.00 78.84  ? 3497 LYS A O     1 
ATOM   13966 C  CB    . LYS A 1 3497 ? 170.962 121.547 220.308 1.00 76.07  ? 3497 LYS A CB    1 
ATOM   13967 C  CG    . LYS A 1 3497 ? 170.371 121.501 221.707 1.00 70.91  ? 3497 LYS A CG    1 
ATOM   13968 C  CD    . LYS A 1 3497 ? 171.402 121.048 222.726 1.00 69.05  ? 3497 LYS A CD    1 
ATOM   13969 C  CE    . LYS A 1 3497 ? 172.683 121.857 222.608 1.00 70.53  ? 3497 LYS A CE    1 
ATOM   13970 N  NZ    . LYS A 1 3497 ? 172.436 123.310 222.817 1.00 57.56  ? 3497 LYS A NZ    1 
ATOM   13971 N  N     . ASN A 1 3498 ? 170.967 121.529 217.039 1.00 76.70  ? 3498 ASN A N     1 
ATOM   13972 C  CA    . ASN A 1 3498 ? 171.624 121.924 215.797 1.00 82.12  ? 3498 ASN A CA    1 
ATOM   13973 C  C     . ASN A 1 3498 ? 170.754 122.881 214.991 1.00 80.64  ? 3498 ASN A C     1 
ATOM   13974 O  O     . ASN A 1 3498 ? 171.253 123.876 214.453 1.00 81.24  ? 3498 ASN A O     1 
ATOM   13975 C  CB    . ASN A 1 3498 ? 171.981 120.688 214.970 1.00 87.27  ? 3498 ASN A CB    1 
ATOM   13976 C  CG    . ASN A 1 3498 ? 172.548 121.041 213.612 1.00 86.86  ? 3498 ASN A CG    1 
ATOM   13977 O  OD1   . ASN A 1 3498 ? 172.008 120.645 212.579 1.00 86.08  ? 3498 ASN A OD1   1 
ATOM   13978 N  ND2   . ASN A 1 3498 ? 173.643 121.792 213.604 1.00 82.30  ? 3498 ASN A ND2   1 
ATOM   13979 N  N     . GLN A 1 3499 ? 169.450 122.599 214.888 1.00 78.42  ? 3499 GLN A N     1 
ATOM   13980 C  CA    . GLN A 1 3499 ? 168.556 123.570 214.263 1.00 76.45  ? 3499 GLN A CA    1 
ATOM   13981 C  C     . GLN A 1 3499 ? 168.475 124.856 215.077 1.00 69.33  ? 3499 GLN A C     1 
ATOM   13982 O  O     . GLN A 1 3499 ? 168.490 125.952 214.508 1.00 62.02  ? 3499 GLN A O     1 
ATOM   13983 C  CB    . GLN A 1 3499 ? 167.157 122.986 214.041 1.00 75.34  ? 3499 GLN A CB    1 
ATOM   13984 C  CG    . GLN A 1 3499 ? 167.024 122.004 212.869 1.00 78.75  ? 3499 GLN A CG    1 
ATOM   13985 C  CD    . GLN A 1 3499 ? 167.676 120.660 213.102 1.00 89.31  ? 3499 GLN A CD    1 
ATOM   13986 O  OE1   . GLN A 1 3499 ? 167.298 119.927 214.014 1.00 91.04  ? 3499 GLN A OE1   1 
ATOM   13987 N  NE2   . GLN A 1 3499 ? 168.658 120.324 212.273 1.00 93.90  ? 3499 GLN A NE2   1 
ATOM   13988 N  N     . MET A 1 3500 ? 168.399 124.746 216.410 1.00 72.68  ? 3500 MET A N     1 
ATOM   13989 C  CA    . MET A 1 3500 ? 168.415 125.943 217.255 1.00 66.74  ? 3500 MET A CA    1 
ATOM   13990 C  C     . MET A 1 3500 ? 169.589 126.853 216.925 1.00 63.39  ? 3500 MET A C     1 
ATOM   13991 O  O     . MET A 1 3500 ? 169.438 128.079 216.883 1.00 63.46  ? 3500 MET A O     1 
ATOM   13992 C  CB    . MET A 1 3500 ? 168.459 125.556 218.735 1.00 73.81  ? 3500 MET A CB    1 
ATOM   13993 C  CG    . MET A 1 3500 ? 167.233 124.842 219.273 1.00 75.57  ? 3500 MET A CG    1 
ATOM   13994 S  SD    . MET A 1 3500 ? 165.759 125.875 219.161 1.00 67.22  ? 3500 MET A SD    1 
ATOM   13995 C  CE    . MET A 1 3500 ? 164.950 125.180 217.735 1.00 64.49  ? 3500 MET A CE    1 
ATOM   13996 N  N     . SER A 1 3501 ? 170.766 126.275 216.687 1.00 66.05  ? 3501 SER A N     1 
ATOM   13997 C  CA    . SER A 1 3501 ? 171.955 127.091 216.475 1.00 64.79  ? 3501 SER A CA    1 
ATOM   13998 C  C     . SER A 1 3501 ? 171.960 127.759 215.105 1.00 59.46  ? 3501 SER A C     1 
ATOM   13999 O  O     . SER A 1 3501 ? 172.769 128.663 214.867 1.00 59.76  ? 3501 SER A O     1 
ATOM   14000 C  CB    . SER A 1 3501 ? 173.212 126.239 216.652 1.00 67.60  ? 3501 SER A CB    1 
ATOM   14001 O  OG    . SER A 1 3501 ? 174.349 126.886 216.107 1.00 66.16  ? 3501 SER A OG    1 
ATOM   14002 N  N     . THR A 1 3502 ? 171.079 127.342 214.196 1.00 54.69  ? 3502 THR A N     1 
ATOM   14003 C  CA    . THR A 1 3502 ? 171.139 127.785 212.809 1.00 50.43  ? 3502 THR A CA    1 
ATOM   14004 C  C     . THR A 1 3502 ? 169.898 128.544 212.350 1.00 39.33  ? 3502 THR A C     1 
ATOM   14005 O  O     . THR A 1 3502 ? 169.839 128.952 211.187 1.00 40.81  ? 3502 THR A O     1 
ATOM   14006 C  CB    . THR A 1 3502 ? 171.378 126.589 211.885 1.00 54.00  ? 3502 THR A CB    1 
ATOM   14007 O  OG1   . THR A 1 3502 ? 170.353 125.610 212.092 1.00 57.37  ? 3502 THR A OG1   1 
ATOM   14008 C  CG2   . THR A 1 3502 ? 172.736 125.963 212.164 1.00 50.54  ? 3502 THR A CG2   1 
ATOM   14009 N  N     . ILE A 1 3503 ? 168.907 128.745 213.223 1.00 38.96  ? 3503 ILE A N     1 
ATOM   14010 C  CA    . ILE A 1 3503 ? 167.696 129.439 212.792 1.00 33.17  ? 3503 ILE A CA    1 
ATOM   14011 C  C     . ILE A 1 3503 ? 167.983 130.894 212.447 1.00 29.53  ? 3503 ILE A C     1 
ATOM   14012 O  O     . ILE A 1 3503 ? 167.396 131.438 211.506 1.00 28.83  ? 3503 ILE A O     1 
ATOM   14013 C  CB    . ILE A 1 3503 ? 166.584 129.317 213.852 1.00 36.04  ? 3503 ILE A CB    1 
ATOM   14014 C  CG1   . ILE A 1 3503 ? 166.181 127.857 214.028 1.00 45.12  ? 3503 ILE A CG1   1 
ATOM   14015 C  CG2   . ILE A 1 3503 ? 165.370 130.147 213.474 1.00 34.37  ? 3503 ILE A CG2   1 
ATOM   14016 C  CD1   . ILE A 1 3503 ? 165.294 127.614 215.210 1.00 49.23  ? 3503 ILE A CD1   1 
ATOM   14017 N  N     . ALA A 1 3504 ? 168.887 131.547 213.179 1.00 33.27  ? 3504 ALA A N     1 
ATOM   14018 C  CA    . ALA A 1 3504 ? 169.171 132.953 212.911 1.00 27.68  ? 3504 ALA A CA    1 
ATOM   14019 C  C     . ALA A 1 3504 ? 169.708 133.150 211.498 1.00 28.17  ? 3504 ALA A C     1 
ATOM   14020 O  O     . ALA A 1 3504 ? 169.166 133.946 210.722 1.00 29.93  ? 3504 ALA A O     1 
ATOM   14021 C  CB    . ALA A 1 3504 ? 170.157 133.494 213.945 1.00 27.90  ? 3504 ALA A CB    1 
ATOM   14022 N  N     . GLY A 1 3505 ? 170.756 132.408 211.136 1.00 29.51  ? 3505 GLY A N     1 
ATOM   14023 C  CA    . GLY A 1 3505 ? 171.333 132.557 209.809 1.00 29.57  ? 3505 GLY A CA    1 
ATOM   14024 C  C     . GLY A 1 3505 ? 170.406 132.090 208.703 1.00 22.13  ? 3505 GLY A C     1 
ATOM   14025 O  O     . GLY A 1 3505 ? 170.309 132.731 207.652 1.00 22.87  ? 3505 GLY A O     1 
ATOM   14026 N  N     . ASP A 1 3506 ? 169.721 130.965 208.918 1.00 22.67  ? 3506 ASP A N     1 
ATOM   14027 C  CA    . ASP A 1 3506 ? 168.804 130.448 207.907 1.00 24.63  ? 3506 ASP A CA    1 
ATOM   14028 C  C     . ASP A 1 3506 ? 167.679 131.437 207.637 1.00 24.25  ? 3506 ASP A C     1 
ATOM   14029 O  O     . ASP A 1 3506 ? 167.337 131.711 206.481 1.00 22.94  ? 3506 ASP A O     1 
ATOM   14030 C  CB    . ASP A 1 3506 ? 168.237 129.101 208.356 1.00 26.70  ? 3506 ASP A CB    1 
ATOM   14031 C  CG    . ASP A 1 3506 ? 169.120 127.935 207.963 1.00 46.40  ? 3506 ASP A CG    1 
ATOM   14032 O  OD1   . ASP A 1 3506 ? 170.308 128.162 207.655 1.00 47.59  ? 3506 ASP A OD1   1 
ATOM   14033 O  OD2   . ASP A 1 3506 ? 168.626 126.788 207.962 1.00 56.45  ? 3506 ASP A OD2   1 
ATOM   14034 N  N     . CYS A 1 3507 ? 167.099 131.995 208.702 1.00 22.61  ? 3507 CYS A N     1 
ATOM   14035 C  CA    . CYS A 1 3507 ? 166.022 132.962 208.541 1.00 18.48  ? 3507 CYS A CA    1 
ATOM   14036 C  C     . CYS A 1 3507 ? 166.530 134.257 207.925 1.00 21.40  ? 3507 CYS A C     1 
ATOM   14037 O  O     . CYS A 1 3507 ? 165.825 134.881 207.126 1.00 21.81  ? 3507 CYS A O     1 
ATOM   14038 C  CB    . CYS A 1 3507 ? 165.352 133.227 209.888 1.00 24.06  ? 3507 CYS A CB    1 
ATOM   14039 S  SG    . CYS A 1 3507 ? 164.331 131.862 210.478 1.00 41.84  ? 3507 CYS A SG    1 
ATOM   14040 N  N     . LEU A 1 3508 ? 167.749 134.678 208.275 1.00 19.71  ? 3508 LEU A N     1 
ATOM   14041 C  CA    . LEU A 1 3508 ? 168.324 135.864 207.650 1.00 15.37  ? 3508 LEU A CA    1 
ATOM   14042 C  C     . LEU A 1 3508 ? 168.471 135.666 206.147 1.00 14.39  ? 3508 LEU A C     1 
ATOM   14043 O  O     . LEU A 1 3508 ? 168.088 136.533 205.352 1.00 18.56  ? 3508 LEU A O     1 
ATOM   14044 C  CB    . LEU A 1 3508 ? 169.674 136.187 208.298 1.00 17.75  ? 3508 LEU A CB    1 
ATOM   14045 C  CG    . LEU A 1 3508 ? 170.410 137.487 207.955 1.00 17.69  ? 3508 LEU A CG    1 
ATOM   14046 C  CD1   . LEU A 1 3508 ? 171.284 137.904 209.121 1.00 16.32  ? 3508 LEU A CD1   1 
ATOM   14047 C  CD2   . LEU A 1 3508 ? 171.260 137.345 206.702 1.00 17.04  ? 3508 LEU A CD2   1 
ATOM   14048 N  N     . LEU A 1 3509 ? 169.016 134.517 205.739 1.00 14.35  ? 3509 LEU A N     1 
ATOM   14049 C  CA    . LEU A 1 3509 ? 169.186 134.240 204.317 1.00 12.28  ? 3509 LEU A CA    1 
ATOM   14050 C  C     . LEU A 1 3509 ? 167.843 134.159 203.604 1.00 14.55  ? 3509 LEU A C     1 
ATOM   14051 O  O     . LEU A 1 3509 ? 167.681 134.700 202.502 1.00 16.43  ? 3509 LEU A O     1 
ATOM   14052 C  CB    . LEU A 1 3509 ? 169.970 132.942 204.127 1.00 14.21  ? 3509 LEU A CB    1 
ATOM   14053 C  CG    . LEU A 1 3509 ? 171.432 132.949 204.573 1.00 16.65  ? 3509 LEU A CG    1 
ATOM   14054 C  CD1   . LEU A 1 3509 ? 172.133 131.679 204.126 1.00 22.25  ? 3509 LEU A CD1   1 
ATOM   14055 C  CD2   . LEU A 1 3509 ? 172.145 134.171 204.034 1.00 16.22  ? 3509 LEU A CD2   1 
ATOM   14056 N  N     . SER A 1 3510 ? 166.866 133.489 204.218 1.00 12.83  ? 3510 SER A N     1 
ATOM   14057 C  CA    . SER A 1 3510 ? 165.552 133.361 203.597 1.00 12.71  ? 3510 SER A CA    1 
ATOM   14058 C  C     . SER A 1 3510 ? 164.878 134.717 203.441 1.00 14.87  ? 3510 SER A C     1 
ATOM   14059 O  O     . SER A 1 3510 ? 164.294 135.010 202.391 1.00 21.16  ? 3510 SER A O     1 
ATOM   14060 C  CB    . SER A 1 3510 ? 164.679 132.416 204.420 1.00 16.41  ? 3510 SER A CB    1 
ATOM   14061 O  OG    . SER A 1 3510 ? 165.362 131.205 204.690 1.00 18.14  ? 3510 SER A OG    1 
ATOM   14062 N  N     . ALA A 1 3511 ? 164.951 135.560 204.473 1.00 13.26  ? 3511 ALA A N     1 
ATOM   14063 C  CA    . ALA A 1 3511 ? 164.354 136.887 204.394 1.00 11.21  ? 3511 ALA A CA    1 
ATOM   14064 C  C     . ALA A 1 3511 ? 165.045 137.742 203.342 1.00 13.03  ? 3511 ALA A C     1 
ATOM   14065 O  O     . ALA A 1 3511 ? 164.386 138.481 202.602 1.00 15.90  ? 3511 ALA A O     1 
ATOM   14066 C  CB    . ALA A 1 3511 ? 164.413 137.567 205.759 1.00 13.71  ? 3511 ALA A CB    1 
ATOM   14067 N  N     . ALA A 1 3512 ? 166.377 137.661 203.266 1.00 10.86  ? 3512 ALA A N     1 
ATOM   14068 C  CA    . ALA A 1 3512 ? 167.099 138.408 202.243 1.00 10.10  ? 3512 ALA A CA    1 
ATOM   14069 C  C     . ALA A 1 3512 ? 166.682 137.966 200.849 1.00 11.96  ? 3512 ALA A C     1 
ATOM   14070 O  O     . ALA A 1 3512 ? 166.462 138.802 199.963 1.00 14.61  ? 3512 ALA A O     1 
ATOM   14071 C  CB    . ALA A 1 3512 ? 168.604 138.238 202.436 1.00 11.60  ? 3512 ALA A CB    1 
ATOM   14072 N  N     . PHE A 1 3513 ? 166.554 136.654 200.639 1.00 12.18  ? 3513 PHE A N     1 
ATOM   14073 C  CA    . PHE A 1 3513 ? 166.136 136.159 199.333 1.00 13.42  ? 3513 PHE A CA    1 
ATOM   14074 C  C     . PHE A 1 3513 ? 164.718 136.606 198.998 1.00 13.26  ? 3513 PHE A C     1 
ATOM   14075 O  O     . PHE A 1 3513 ? 164.431 136.973 197.853 1.00 16.63  ? 3513 PHE A O     1 
ATOM   14076 C  CB    . PHE A 1 3513 ? 166.244 134.637 199.282 1.00 12.35  ? 3513 PHE A CB    1 
ATOM   14077 C  CG    . PHE A 1 3513 ? 166.119 134.075 197.899 1.00 12.12  ? 3513 PHE A CG    1 
ATOM   14078 C  CD1   . PHE A 1 3513 ? 167.199 134.086 197.034 1.00 11.18  ? 3513 PHE A CD1   1 
ATOM   14079 C  CD2   . PHE A 1 3513 ? 164.916 133.555 197.455 1.00 9.04   ? 3513 PHE A CD2   1 
ATOM   14080 C  CE1   . PHE A 1 3513 ? 167.085 133.581 195.758 1.00 11.60  ? 3513 PHE A CE1   1 
ATOM   14081 C  CE2   . PHE A 1 3513 ? 164.797 133.048 196.181 1.00 11.44  ? 3513 PHE A CE2   1 
ATOM   14082 C  CZ    . PHE A 1 3513 ? 165.883 133.061 195.331 1.00 13.31  ? 3513 PHE A CZ    1 
ATOM   14083 N  N     . ILE A 1 3514 ? 163.816 136.574 199.981 1.00 9.89   ? 3514 ILE A N     1 
ATOM   14084 C  CA    . ILE A 1 3514 ? 162.435 136.981 199.729 1.00 12.71  ? 3514 ILE A CA    1 
ATOM   14085 C  C     . ILE A 1 3514 ? 162.363 138.461 199.379 1.00 16.14  ? 3514 ILE A C     1 
ATOM   14086 O  O     . ILE A 1 3514 ? 161.675 138.857 198.431 1.00 20.80  ? 3514 ILE A O     1 
ATOM   14087 C  CB    . ILE A 1 3514 ? 161.545 136.648 200.940 1.00 13.83  ? 3514 ILE A CB    1 
ATOM   14088 C  CG1   . ILE A 1 3514 ? 161.430 135.139 201.134 1.00 18.26  ? 3514 ILE A CG1   1 
ATOM   14089 C  CG2   . ILE A 1 3514 ? 160.165 137.250 200.765 1.00 13.32  ? 3514 ILE A CG2   1 
ATOM   14090 C  CD1   . ILE A 1 3514 ? 160.659 134.753 202.375 1.00 19.32  ? 3514 ILE A CD1   1 
ATOM   14091 N  N     . ALA A 1 3515 ? 163.073 139.302 200.129 1.00 15.37  ? 3515 ALA A N     1 
ATOM   14092 C  CA    . ALA A 1 3515 ? 162.916 140.743 200.003 1.00 10.89  ? 3515 ALA A CA    1 
ATOM   14093 C  C     . ALA A 1 3515 ? 163.839 141.382 198.974 1.00 10.92  ? 3515 ALA A C     1 
ATOM   14094 O  O     . ALA A 1 3515 ? 163.667 142.567 198.673 1.00 13.21  ? 3515 ALA A O     1 
ATOM   14095 C  CB    . ALA A 1 3515 ? 163.141 141.415 201.361 1.00 9.22   ? 3515 ALA A CB    1 
ATOM   14096 N  N     . TYR A 1 3516 ? 164.802 140.650 198.424 1.00 8.48   ? 3516 TYR A N     1 
ATOM   14097 C  CA    . TYR A 1 3516 ? 165.749 141.274 197.508 1.00 7.54   ? 3516 TYR A CA    1 
ATOM   14098 C  C     . TYR A 1 3516 ? 165.836 140.598 196.150 1.00 9.85   ? 3516 TYR A C     1 
ATOM   14099 O  O     . TYR A 1 3516 ? 165.964 141.287 195.135 1.00 12.97  ? 3516 TYR A O     1 
ATOM   14100 C  CB    . TYR A 1 3516 ? 167.146 141.305 198.139 1.00 7.76   ? 3516 TYR A CB    1 
ATOM   14101 C  CG    . TYR A 1 3516 ? 167.293 142.285 199.279 1.00 10.83  ? 3516 TYR A CG    1 
ATOM   14102 C  CD1   . TYR A 1 3516 ? 167.090 143.644 199.086 1.00 9.69   ? 3516 TYR A CD1   1 
ATOM   14103 C  CD2   . TYR A 1 3516 ? 167.650 141.852 200.547 1.00 10.74  ? 3516 TYR A CD2   1 
ATOM   14104 C  CE1   . TYR A 1 3516 ? 167.232 144.541 200.123 1.00 7.47   ? 3516 TYR A CE1   1 
ATOM   14105 C  CE2   . TYR A 1 3516 ? 167.792 142.742 201.591 1.00 12.68  ? 3516 TYR A CE2   1 
ATOM   14106 C  CZ    . TYR A 1 3516 ? 167.582 144.085 201.373 1.00 8.84   ? 3516 TYR A CZ    1 
ATOM   14107 O  OH    . TYR A 1 3516 ? 167.724 144.975 202.411 1.00 10.26  ? 3516 TYR A OH    1 
ATOM   14108 N  N     . ALA A 1 3517 ? 165.764 139.272 196.096 1.00 11.82  ? 3517 ALA A N     1 
ATOM   14109 C  CA    . ALA A 1 3517 ? 166.100 138.520 194.895 1.00 9.70   ? 3517 ALA A CA    1 
ATOM   14110 C  C     . ALA A 1 3517 ? 164.930 138.355 193.933 1.00 9.79   ? 3517 ALA A C     1 
ATOM   14111 O  O     . ALA A 1 3517 ? 165.039 137.582 192.977 1.00 13.73  ? 3517 ALA A O     1 
ATOM   14112 C  CB    . ALA A 1 3517 ? 166.648 137.144 195.277 1.00 10.40  ? 3517 ALA A CB    1 
ATOM   14113 N  N     . GLY A 1 3518 ? 163.823 139.062 194.157 1.00 10.11  ? 3518 GLY A N     1 
ATOM   14114 C  CA    . GLY A 1 3518 ? 162.648 138.854 193.326 1.00 7.98   ? 3518 GLY A CA    1 
ATOM   14115 C  C     . GLY A 1 3518 ? 162.849 139.271 191.881 1.00 7.94   ? 3518 GLY A C     1 
ATOM   14116 O  O     . GLY A 1 3518 ? 162.422 138.569 190.961 1.00 10.14  ? 3518 GLY A O     1 
ATOM   14117 N  N     . TYR A 1 3519 ? 163.494 140.416 191.660 1.00 11.13  ? 3519 TYR A N     1 
ATOM   14118 C  CA    . TYR A 1 3519 ? 163.636 140.943 190.308 1.00 8.39   ? 3519 TYR A CA    1 
ATOM   14119 C  C     . TYR A 1 3519 ? 164.700 140.207 189.501 1.00 11.03  ? 3519 TYR A C     1 
ATOM   14120 O  O     . TYR A 1 3519 ? 164.617 140.164 188.269 1.00 10.08  ? 3519 TYR A O     1 
ATOM   14121 C  CB    . TYR A 1 3519 ? 163.964 142.435 190.359 1.00 9.18   ? 3519 TYR A CB    1 
ATOM   14122 C  CG    . TYR A 1 3519 ? 164.136 143.061 188.996 1.00 15.58  ? 3519 TYR A CG    1 
ATOM   14123 C  CD1   . TYR A 1 3519 ? 163.036 143.334 188.195 1.00 15.27  ? 3519 TYR A CD1   1 
ATOM   14124 C  CD2   . TYR A 1 3519 ? 165.396 143.370 188.505 1.00 16.77  ? 3519 TYR A CD2   1 
ATOM   14125 C  CE1   . TYR A 1 3519 ? 163.186 143.898 186.949 1.00 16.17  ? 3519 TYR A CE1   1 
ATOM   14126 C  CE2   . TYR A 1 3519 ? 165.555 143.936 187.258 1.00 18.46  ? 3519 TYR A CE2   1 
ATOM   14127 C  CZ    . TYR A 1 3519 ? 164.447 144.197 186.485 1.00 17.74  ? 3519 TYR A CZ    1 
ATOM   14128 O  OH    . TYR A 1 3519 ? 164.600 144.762 185.241 1.00 28.85  ? 3519 TYR A OH    1 
ATOM   14129 N  N     . PHE A 1 3520 ? 165.693 139.628 190.165 1.00 15.35  ? 3520 PHE A N     1 
ATOM   14130 C  CA    . PHE A 1 3520 ? 166.835 139.053 189.476 1.00 13.09  ? 3520 PHE A CA    1 
ATOM   14131 C  C     . PHE A 1 3520 ? 166.514 137.660 188.939 1.00 14.47  ? 3520 PHE A C     1 
ATOM   14132 O  O     . PHE A 1 3520 ? 165.575 136.993 189.380 1.00 10.75  ? 3520 PHE A O     1 
ATOM   14133 C  CB    . PHE A 1 3520 ? 168.040 138.999 190.413 1.00 13.37  ? 3520 PHE A CB    1 
ATOM   14134 C  CG    . PHE A 1 3520 ? 168.361 140.316 191.053 1.00 15.67  ? 3520 PHE A CG    1 
ATOM   14135 C  CD1   . PHE A 1 3520 ? 169.168 141.237 190.407 1.00 20.89  ? 3520 PHE A CD1   1 
ATOM   14136 C  CD2   . PHE A 1 3520 ? 167.844 140.643 192.294 1.00 15.75  ? 3520 PHE A CD2   1 
ATOM   14137 C  CE1   . PHE A 1 3520 ? 169.462 142.451 190.991 1.00 15.97  ? 3520 PHE A CE1   1 
ATOM   14138 C  CE2   . PHE A 1 3520 ? 168.132 141.857 192.882 1.00 15.58  ? 3520 PHE A CE2   1 
ATOM   14139 C  CZ    . PHE A 1 3520 ? 168.943 142.762 192.229 1.00 17.24  ? 3520 PHE A CZ    1 
ATOM   14140 N  N     . ASP A 1 3521 ? 167.312 137.230 187.964 1.00 21.26  ? 3521 ASP A N     1 
ATOM   14141 C  CA    . ASP A 1 3521 ? 167.160 135.916 187.361 1.00 14.74  ? 3521 ASP A CA    1 
ATOM   14142 C  C     . ASP A 1 3521 ? 167.918 134.868 188.175 1.00 18.19  ? 3521 ASP A C     1 
ATOM   14143 O  O     . ASP A 1 3521 ? 168.473 135.152 189.240 1.00 20.75  ? 3521 ASP A O     1 
ATOM   14144 C  CB    . ASP A 1 3521 ? 167.619 135.947 185.905 1.00 12.65  ? 3521 ASP A CB    1 
ATOM   14145 C  CG    . ASP A 1 3521 ? 169.039 136.447 185.749 1.00 27.15  ? 3521 ASP A CG    1 
ATOM   14146 O  OD1   . ASP A 1 3521 ? 169.658 136.821 186.765 1.00 30.12  ? 3521 ASP A OD1   1 
ATOM   14147 O  OD2   . ASP A 1 3521 ? 169.536 136.474 184.604 1.00 34.79  ? 3521 ASP A OD2   1 
ATOM   14148 N  N     . GLN A 1 3522 ? 167.951 133.637 187.657 1.00 18.85  ? 3522 GLN A N     1 
ATOM   14149 C  CA    . GLN A 1 3522 ? 168.430 132.501 188.443 1.00 20.08  ? 3522 GLN A CA    1 
ATOM   14150 C  C     . GLN A 1 3522 ? 169.881 132.680 188.875 1.00 21.75  ? 3522 GLN A C     1 
ATOM   14151 O  O     . GLN A 1 3522 ? 170.206 132.560 190.062 1.00 22.98  ? 3522 GLN A O     1 
ATOM   14152 C  CB    . GLN A 1 3522 ? 168.283 131.209 187.641 1.00 20.14  ? 3522 GLN A CB    1 
ATOM   14153 C  CG    . GLN A 1 3522 ? 168.678 129.970 188.420 1.00 20.82  ? 3522 GLN A CG    1 
ATOM   14154 C  CD    . GLN A 1 3522 ? 168.478 128.696 187.634 1.00 31.74  ? 3522 GLN A CD    1 
ATOM   14155 O  OE1   . GLN A 1 3522 ? 168.073 128.727 186.474 1.00 34.40  ? 3522 GLN A OE1   1 
ATOM   14156 N  NE2   . GLN A 1 3522 ? 168.760 127.562 188.264 1.00 38.33  ? 3522 GLN A NE2   1 
ATOM   14157 N  N     . GLN A 1 3523 ? 170.770 132.957 187.919 1.00 23.03  ? 3523 GLN A N     1 
ATOM   14158 C  CA    . GLN A 1 3523 ? 172.192 133.026 188.240 1.00 23.39  ? 3523 GLN A CA    1 
ATOM   14159 C  C     . GLN A 1 3523 ? 172.493 134.184 189.180 1.00 21.56  ? 3523 GLN A C     1 
ATOM   14160 O  O     . GLN A 1 3523 ? 173.338 134.063 190.074 1.00 23.25  ? 3523 GLN A O     1 
ATOM   14161 C  CB    . GLN A 1 3523 ? 173.021 133.121 186.955 1.00 23.72  ? 3523 GLN A CB    1 
ATOM   14162 C  CG    . GLN A 1 3523 ? 172.896 134.429 186.195 1.00 35.70  ? 3523 GLN A CG    1 
ATOM   14163 C  CD    . GLN A 1 3523 ? 171.694 134.447 185.271 1.00 38.86  ? 3523 GLN A CD    1 
ATOM   14164 O  OE1   . GLN A 1 3523 ? 170.783 133.630 185.401 1.00 33.08  ? 3523 GLN A OE1   1 
ATOM   14165 N  NE2   . GLN A 1 3523 ? 171.688 135.380 184.325 1.00 34.75  ? 3523 GLN A NE2   1 
ATOM   14166 N  N     . MET A 1 3524 ? 171.790 135.304 189.021 1.00 20.91  ? 3524 MET A N     1 
ATOM   14167 C  CA    . MET A 1 3524 ? 172.043 136.442 189.894 1.00 18.73  ? 3524 MET A CA    1 
ATOM   14168 C  C     . MET A 1 3524 ? 171.499 136.205 191.299 1.00 16.91  ? 3524 MET A C     1 
ATOM   14169 O  O     . MET A 1 3524 ? 172.128 136.611 192.284 1.00 15.46  ? 3524 MET A O     1 
ATOM   14170 C  CB    . MET A 1 3524 ? 171.435 137.709 189.297 1.00 19.03  ? 3524 MET A CB    1 
ATOM   14171 C  CG    . MET A 1 3524 ? 171.812 138.934 190.072 1.00 30.98  ? 3524 MET A CG    1 
ATOM   14172 S  SD    . MET A 1 3524 ? 173.587 139.154 189.888 1.00 46.56  ? 3524 MET A SD    1 
ATOM   14173 C  CE    . MET A 1 3524 ? 173.947 140.100 191.350 1.00 32.09  ? 3524 MET A CE    1 
ATOM   14174 N  N     . ARG A 1 3525 ? 170.343 135.544 191.408 1.00 16.84  ? 3525 ARG A N     1 
ATOM   14175 C  CA    . ARG A 1 3525 ? 169.831 135.133 192.711 1.00 11.78  ? 3525 ARG A CA    1 
ATOM   14176 C  C     . ARG A 1 3525 ? 170.815 134.202 193.406 1.00 14.02  ? 3525 ARG A C     1 
ATOM   14177 O  O     . ARG A 1 3525 ? 171.078 134.335 194.609 1.00 18.24  ? 3525 ARG A O     1 
ATOM   14178 C  CB    . ARG A 1 3525 ? 168.478 134.441 192.542 1.00 10.98  ? 3525 ARG A CB    1 
ATOM   14179 C  CG    . ARG A 1 3525 ? 167.328 135.350 192.155 1.00 8.67   ? 3525 ARG A CG    1 
ATOM   14180 C  CD    . ARG A 1 3525 ? 166.020 134.578 192.171 1.00 8.01   ? 3525 ARG A CD    1 
ATOM   14181 N  NE    . ARG A 1 3525 ? 164.947 135.281 191.480 1.00 7.55   ? 3525 ARG A NE    1 
ATOM   14182 C  CZ    . ARG A 1 3525 ? 163.672 134.920 191.516 1.00 5.68   ? 3525 ARG A CZ    1 
ATOM   14183 N  NH1   . ARG A 1 3525 ? 163.274 133.860 192.198 1.00 7.21   ? 3525 ARG A NH1   1 
ATOM   14184 N  NH2   . ARG A 1 3525 ? 162.775 135.638 190.848 1.00 7.95   ? 3525 ARG A NH2   1 
ATOM   14185 N  N     . GLN A 1 3526 ? 171.367 133.246 192.656 1.00 15.30  ? 3526 GLN A N     1 
ATOM   14186 C  CA    . GLN A 1 3526 ? 172.350 132.333 193.225 1.00 15.20  ? 3526 GLN A CA    1 
ATOM   14187 C  C     . GLN A 1 3526 ? 173.598 133.080 193.676 1.00 17.73  ? 3526 GLN A C     1 
ATOM   14188 O  O     . GLN A 1 3526 ? 174.163 132.774 194.730 1.00 20.91  ? 3526 GLN A O     1 
ATOM   14189 C  CB    . GLN A 1 3526 ? 172.708 131.249 192.209 1.00 16.23  ? 3526 GLN A CB    1 
ATOM   14190 C  CG    . GLN A 1 3526 ? 173.557 130.124 192.770 1.00 13.77  ? 3526 GLN A CG    1 
ATOM   14191 C  CD    . GLN A 1 3526 ? 172.879 129.397 193.913 1.00 23.55  ? 3526 GLN A CD    1 
ATOM   14192 O  OE1   . GLN A 1 3526 ? 173.038 129.762 195.077 1.00 27.74  ? 3526 GLN A OE1   1 
ATOM   14193 N  NE2   . GLN A 1 3526 ? 172.112 128.365 193.586 1.00 24.10  ? 3526 GLN A NE2   1 
ATOM   14194 N  N     . ASN A 1 3527 ? 174.048 134.057 192.885 1.00 15.11  ? 3527 ASN A N     1 
ATOM   14195 C  CA    . ASN A 1 3527 ? 175.221 134.838 193.266 1.00 14.36  ? 3527 ASN A CA    1 
ATOM   14196 C  C     . ASN A 1 3527 ? 174.974 135.627 194.545 1.00 15.04  ? 3527 ASN A C     1 
ATOM   14197 O  O     . ASN A 1 3527 ? 175.841 135.683 195.426 1.00 21.66  ? 3527 ASN A O     1 
ATOM   14198 C  CB    . ASN A 1 3527 ? 175.617 135.778 192.128 1.00 21.91  ? 3527 ASN A CB    1 
ATOM   14199 C  CG    . ASN A 1 3527 ? 176.315 135.059 190.994 1.00 31.21  ? 3527 ASN A CG    1 
ATOM   14200 O  OD1   . ASN A 1 3527 ? 176.579 133.859 191.073 1.00 29.80  ? 3527 ASN A OD1   1 
ATOM   14201 N  ND2   . ASN A 1 3527 ? 176.617 135.789 189.929 1.00 29.25  ? 3527 ASN A ND2   1 
ATOM   14202 N  N     . LEU A 1 3528 ? 173.797 136.248 194.664 1.00 14.50  ? 3528 LEU A N     1 
ATOM   14203 C  CA    . LEU A 1 3528 ? 173.472 136.986 195.881 1.00 9.85   ? 3528 LEU A CA    1 
ATOM   14204 C  C     . LEU A 1 3528 ? 173.419 136.062 197.092 1.00 12.23  ? 3528 LEU A C     1 
ATOM   14205 O  O     . LEU A 1 3528 ? 173.946 136.395 198.164 1.00 15.52  ? 3528 LEU A O     1 
ATOM   14206 C  CB    . LEU A 1 3528 ? 172.144 137.722 195.712 1.00 8.37   ? 3528 LEU A CB    1 
ATOM   14207 C  CG    . LEU A 1 3528 ? 172.165 138.993 194.864 1.00 10.55  ? 3528 LEU A CG    1 
ATOM   14208 C  CD1   . LEU A 1 3528 ? 170.757 139.523 194.659 1.00 10.51  ? 3528 LEU A CD1   1 
ATOM   14209 C  CD2   . LEU A 1 3528 ? 173.043 140.047 195.515 1.00 9.95   ? 3528 LEU A CD2   1 
ATOM   14210 N  N     . PHE A 1 3529 ? 172.789 134.894 196.939 1.00 12.99  ? 3529 PHE A N     1 
ATOM   14211 C  CA    . PHE A 1 3529 ? 172.727 133.945 198.045 1.00 14.70  ? 3529 PHE A CA    1 
ATOM   14212 C  C     . PHE A 1 3529 ? 174.118 133.466 198.436 1.00 15.91  ? 3529 PHE A C     1 
ATOM   14213 O  O     . PHE A 1 3529 ? 174.420 133.321 199.625 1.00 17.25  ? 3529 PHE A O     1 
ATOM   14214 C  CB    . PHE A 1 3529 ? 171.833 132.761 197.677 1.00 16.06  ? 3529 PHE A CB    1 
ATOM   14215 C  CG    . PHE A 1 3529 ? 171.238 132.064 198.865 1.00 14.40  ? 3529 PHE A CG    1 
ATOM   14216 C  CD1   . PHE A 1 3529 ? 170.075 132.534 199.450 1.00 14.43  ? 3529 PHE A CD1   1 
ATOM   14217 C  CD2   . PHE A 1 3529 ? 171.842 130.939 199.399 1.00 15.65  ? 3529 PHE A CD2   1 
ATOM   14218 C  CE1   . PHE A 1 3529 ? 169.525 131.896 200.543 1.00 14.14  ? 3529 PHE A CE1   1 
ATOM   14219 C  CE2   . PHE A 1 3529 ? 171.297 130.296 200.493 1.00 16.30  ? 3529 PHE A CE2   1 
ATOM   14220 C  CZ    . PHE A 1 3529 ? 170.137 130.775 201.065 1.00 16.85  ? 3529 PHE A CZ    1 
ATOM   14221 N  N     . THR A 1 3530 ? 174.978 133.216 197.446 1.00 16.16  ? 3530 THR A N     1 
ATOM   14222 C  CA    . THR A 1 3530 ? 176.344 132.793 197.732 1.00 17.79  ? 3530 THR A CA    1 
ATOM   14223 C  C     . THR A 1 3530 ? 177.114 133.875 198.476 1.00 16.84  ? 3530 THR A C     1 
ATOM   14224 O  O     . THR A 1 3530 ? 177.863 133.580 199.412 1.00 17.54  ? 3530 THR A O     1 
ATOM   14225 C  CB    . THR A 1 3530 ? 177.060 132.424 196.433 1.00 19.23  ? 3530 THR A CB    1 
ATOM   14226 O  OG1   . THR A 1 3530 ? 176.260 131.495 195.692 1.00 24.37  ? 3530 THR A OG1   1 
ATOM   14227 C  CG2   . THR A 1 3530 ? 178.411 131.794 196.730 1.00 18.83  ? 3530 THR A CG2   1 
ATOM   14228 N  N     . THR A 1 3531 ? 176.928 135.131 198.064 1.00 15.33  ? 3531 THR A N     1 
ATOM   14229 C  CA    . THR A 1 3531 ? 177.639 136.257 198.709 1.00 14.00  ? 3531 THR A CA    1 
ATOM   14230 C  C     . THR A 1 3531 ? 177.222 136.351 200.162 1.00 15.46  ? 3531 THR A C     1 
ATOM   14231 O  O     . THR A 1 3531 ? 178.116 136.336 201.035 1.00 20.86  ? 3531 THR A O     1 
ATOM   14232 C  CB    . THR A 1 3531 ? 177.340 137.548 197.949 1.00 15.41  ? 3531 THR A CB    1 
ATOM   14233 O  OG1   . THR A 1 3531 ? 177.789 137.310 196.619 1.00 13.82  ? 3531 THR A OG1   1 
ATOM   14234 C  CG2   . THR A 1 3531 ? 178.061 138.748 198.537 1.00 16.04  ? 3531 THR A CG2   1 
ATOM   14235 N  N     . TRP A 1 3532 ? 175.915 136.441 200.421 1.00 13.55  ? 3532 TRP A N     1 
ATOM   14236 C  CA    . TRP A 1 3532 ? 175.413 136.585 201.810 1.00 14.83  ? 3532 TRP A CA    1 
ATOM   14237 C  C     . TRP A 1 3532 ? 175.873 135.391 202.645 1.00 16.19  ? 3532 TRP A C     1 
ATOM   14238 O  O     . TRP A 1 3532 ? 176.322 135.598 203.793 1.00 18.74  ? 3532 TRP A O     1 
ATOM   14239 C  CB    . TRP A 1 3532 ? 173.882 136.693 201.815 1.00 12.88  ? 3532 TRP A CB    1 
ATOM   14240 C  CG    . TRP A 1 3532 ? 173.330 137.776 200.928 1.00 11.46  ? 3532 TRP A CG    1 
ATOM   14241 C  CD1   . TRP A 1 3532 ? 173.905 138.977 200.632 1.00 12.99  ? 3532 TRP A CD1   1 
ATOM   14242 C  CD2   . TRP A 1 3532 ? 172.076 137.745 200.212 1.00 9.86   ? 3532 TRP A CD2   1 
ATOM   14243 N  NE1   . TRP A 1 3532 ? 173.099 139.695 199.790 1.00 11.88  ? 3532 TRP A NE1   1 
ATOM   14244 C  CE2   . TRP A 1 3532 ? 171.972 138.967 199.513 1.00 10.19  ? 3532 TRP A CE2   1 
ATOM   14245 C  CE3   . TRP A 1 3532 ? 171.040 136.812 200.095 1.00 8.86   ? 3532 TRP A CE3   1 
ATOM   14246 C  CZ2   . TRP A 1 3532 ? 170.874 139.273 198.713 1.00 8.53   ? 3532 TRP A CZ2   1 
ATOM   14247 C  CZ3   . TRP A 1 3532 ? 169.957 137.116 199.302 1.00 10.19  ? 3532 TRP A CZ3   1 
ATOM   14248 C  CH2   . TRP A 1 3532 ? 169.876 138.330 198.622 1.00 8.40   ? 3532 TRP A CH2   1 
ATOM   14249 N  N     . SER A 1 3533 ? 175.775 134.183 202.084 1.00 18.59  ? 3533 SER A N     1 
ATOM   14250 C  CA    . SER A 1 3533 ? 176.154 132.954 202.828 1.00 21.76  ? 3533 SER A CA    1 
ATOM   14251 C  C     . SER A 1 3533 ? 177.624 133.035 203.258 1.00 23.77  ? 3533 SER A C     1 
ATOM   14252 O  O     . SER A 1 3533 ? 177.918 132.717 204.430 1.00 21.43  ? 3533 SER A O     1 
ATOM   14253 C  CB    . SER A 1 3533 ? 175.897 131.726 201.994 1.00 21.56  ? 3533 SER A CB    1 
ATOM   14254 O  OG    . SER A 1 3533 ? 174.529 131.637 201.622 1.00 23.72  ? 3533 SER A OG    1 
ATOM   14255 N  N     . HIS A 1 3534 ? 178.504 133.450 202.344 1.00 24.35  ? 3534 HIS A N     1 
ATOM   14256 C  CA    . HIS A 1 3534 ? 179.954 133.551 202.660 1.00 25.15  ? 3534 HIS A CA    1 
ATOM   14257 C  C     . HIS A 1 3534 ? 180.155 134.554 203.800 1.00 28.26  ? 3534 HIS A C     1 
ATOM   14258 O  O     . HIS A 1 3534 ? 180.926 134.263 204.739 1.00 32.02  ? 3534 HIS A O     1 
ATOM   14259 C  CB    . HIS A 1 3534 ? 180.750 133.942 201.411 1.00 27.46  ? 3534 HIS A CB    1 
ATOM   14260 C  CG    . HIS A 1 3534 ? 182.175 134.282 201.694 1.00 45.22  ? 3534 HIS A CG    1 
ATOM   14261 N  ND1   . HIS A 1 3534 ? 182.889 135.195 200.948 1.00 51.42  ? 3534 HIS A ND1   1 
ATOM   14262 C  CD2   . HIS A 1 3534 ? 183.015 133.840 202.640 1.00 45.46  ? 3534 HIS A CD2   1 
ATOM   14263 C  CE1   . HIS A 1 3534 ? 184.117 135.292 201.435 1.00 53.47  ? 3534 HIS A CE1   1 
ATOM   14264 N  NE2   . HIS A 1 3534 ? 184.215 134.478 202.463 1.00 50.76  ? 3534 HIS A NE2   1 
ATOM   14265 N  N     . HIS A 1 3535 ? 179.475 135.700 203.723 1.00 26.58  ? 3535 HIS A N     1 
ATOM   14266 C  CA    . HIS A 1 3535 ? 179.632 136.749 204.767 1.00 20.96  ? 3535 HIS A CA    1 
ATOM   14267 C  C     . HIS A 1 3535 ? 179.238 136.169 206.128 1.00 20.52  ? 3535 HIS A C     1 
ATOM   14268 O  O     . HIS A 1 3535 ? 179.965 136.396 207.117 1.00 28.56  ? 3535 HIS A O     1 
ATOM   14269 C  CB    . HIS A 1 3535 ? 178.798 137.986 204.421 1.00 18.68  ? 3535 HIS A CB    1 
ATOM   14270 C  CG    . HIS A 1 3535 ? 178.903 139.076 205.434 1.00 20.34  ? 3535 HIS A CG    1 
ATOM   14271 N  ND1   . HIS A 1 3535 ? 178.059 139.175 206.519 1.00 16.81  ? 3535 HIS A ND1   1 
ATOM   14272 C  CD2   . HIS A 1 3535 ? 179.751 140.106 205.530 1.00 20.53  ? 3535 HIS A CD2   1 
ATOM   14273 C  CE1   . HIS A 1 3535 ? 178.396 140.235 207.238 1.00 19.97  ? 3535 HIS A CE1   1 
ATOM   14274 N  NE2   . HIS A 1 3535 ? 179.421 140.816 206.654 1.00 23.18  ? 3535 HIS A NE2   1 
ATOM   14275 N  N     . LEU A 1 3536 ? 178.122 135.439 206.174 1.00 19.32  ? 3536 LEU A N     1 
ATOM   14276 C  CA    . LEU A 1 3536 ? 177.669 134.816 207.444 1.00 20.17  ? 3536 LEU A CA    1 
ATOM   14277 C  C     . LEU A 1 3536 ? 178.758 133.850 207.930 1.00 26.09  ? 3536 LEU A C     1 
ATOM   14278 O  O     . LEU A 1 3536 ? 179.077 133.876 209.137 1.00 28.08  ? 3536 LEU A O     1 
ATOM   14279 C  CB    . LEU A 1 3536 ? 176.335 134.103 207.234 1.00 24.24  ? 3536 LEU A CB    1 
ATOM   14280 C  CG    . LEU A 1 3536 ? 175.142 134.997 206.885 1.00 16.80  ? 3536 LEU A CG    1 
ATOM   14281 C  CD1   . LEU A 1 3536 ? 173.838 134.251 207.101 1.00 21.76  ? 3536 LEU A CD1   1 
ATOM   14282 C  CD2   . LEU A 1 3536 ? 175.169 136.274 207.703 1.00 17.46  ? 3536 LEU A CD2   1 
ATOM   14283 N  N     . GLN A 1 3537 ? 179.303 133.035 207.023 1.00 31.28  ? 3537 GLN A N     1 
ATOM   14284 C  CA    . GLN A 1 3537 ? 180.407 132.111 207.388 1.00 28.05  ? 3537 GLN A CA    1 
ATOM   14285 C  C     . GLN A 1 3537 ? 181.588 132.935 207.912 1.00 30.09  ? 3537 GLN A C     1 
ATOM   14286 O  O     . GLN A 1 3537 ? 182.107 132.606 208.999 1.00 39.63  ? 3537 GLN A O     1 
ATOM   14287 C  CB    . GLN A 1 3537 ? 180.875 131.303 206.180 1.00 27.69  ? 3537 GLN A CB    1 
ATOM   14288 C  CG    . GLN A 1 3537 ? 179.851 130.303 205.658 1.00 35.40  ? 3537 GLN A CG    1 
ATOM   14289 C  CD    . GLN A 1 3537 ? 180.357 129.498 204.482 1.00 31.64  ? 3537 GLN A CD    1 
ATOM   14290 O  OE1   . GLN A 1 3537 ? 181.490 129.675 204.022 1.00 27.66  ? 3537 GLN A OE1   1 
ATOM   14291 N  NE2   . GLN A 1 3537 ? 179.518 128.602 203.983 1.00 32.27  ? 3537 GLN A NE2   1 
ATOM   14292 N  N     . GLN A 1 3538 ? 181.989 133.965 207.163 1.00 29.07  ? 3538 GLN A N     1 
ATOM   14293 C  CA    . GLN A 1 3538 ? 183.128 134.773 207.571 1.00 29.71  ? 3538 GLN A CA    1 
ATOM   14294 C  C     . GLN A 1 3538 ? 182.897 135.460 208.911 1.00 33.81  ? 3538 GLN A C     1 
ATOM   14295 O  O     . GLN A 1 3538 ? 183.862 135.899 209.544 1.00 46.12  ? 3538 GLN A O     1 
ATOM   14296 C  CB    . GLN A 1 3538 ? 183.426 135.801 206.479 1.00 33.15  ? 3538 GLN A CB    1 
ATOM   14297 C  CG    . GLN A 1 3538 ? 184.795 136.440 206.542 1.00 41.07  ? 3538 GLN A CG    1 
ATOM   14298 C  CD    . GLN A 1 3538 ? 185.098 137.246 205.297 1.00 49.18  ? 3538 GLN A CD    1 
ATOM   14299 O  OE1   . GLN A 1 3538 ? 184.328 137.235 204.337 1.00 43.49  ? 3538 GLN A OE1   1 
ATOM   14300 N  NE2   . GLN A 1 3538 ? 186.228 137.939 205.299 1.00 61.74  ? 3538 GLN A NE2   1 
ATOM   14301 N  N     . ALA A 1 3539 ? 181.646 135.554 209.358 1.00 31.74  ? 3539 ALA A N     1 
ATOM   14302 C  CA    . ALA A 1 3539 ? 181.308 136.144 210.645 1.00 33.71  ? 3539 ALA A CA    1 
ATOM   14303 C  C     . ALA A 1 3539 ? 180.923 135.102 211.685 1.00 33.01  ? 3539 ALA A C     1 
ATOM   14304 O  O     . ALA A 1 3539 ? 180.419 135.468 212.752 1.00 36.75  ? 3539 ALA A O     1 
ATOM   14305 C  CB    . ALA A 1 3539 ? 180.175 137.159 210.479 1.00 35.96  ? 3539 ALA A CB    1 
ATOM   14306 N  N     . ASN A 1 3540 ? 181.149 133.818 211.399 1.00 31.39  ? 3540 ASN A N     1 
ATOM   14307 C  CA    . ASN A 1 3540 ? 180.827 132.723 212.319 1.00 34.15  ? 3540 ASN A CA    1 
ATOM   14308 C  C     . ASN A 1 3540 ? 179.349 132.720 212.699 1.00 30.88  ? 3540 ASN A C     1 
ATOM   14309 O  O     . ASN A 1 3540 ? 178.989 132.581 213.869 1.00 33.82  ? 3540 ASN A O     1 
ATOM   14310 C  CB    . ASN A 1 3540 ? 181.708 132.768 213.569 1.00 39.47  ? 3540 ASN A CB    1 
ATOM   14311 C  CG    . ASN A 1 3540 ? 183.121 132.303 213.299 1.00 48.15  ? 3540 ASN A CG    1 
ATOM   14312 O  OD1   . ASN A 1 3540 ? 183.584 132.315 212.159 1.00 44.32  ? 3540 ASN A OD1   1 
ATOM   14313 N  ND2   . ASN A 1 3540 ? 183.817 131.887 214.350 1.00 54.61  ? 3540 ASN A ND2   1 
ATOM   14314 N  N     . ILE A 1 3541 ? 178.485 132.873 211.703 1.00 31.24  ? 3541 ILE A N     1 
ATOM   14315 C  CA    . ILE A 1 3541 ? 177.044 132.767 211.884 1.00 32.08  ? 3541 ILE A CA    1 
ATOM   14316 C  C     . ILE A 1 3541 ? 176.604 131.420 211.330 1.00 36.98  ? 3541 ILE A C     1 
ATOM   14317 O  O     . ILE A 1 3541 ? 176.772 131.146 210.135 1.00 36.28  ? 3541 ILE A O     1 
ATOM   14318 C  CB    . ILE A 1 3541 ? 176.305 133.923 211.196 1.00 26.96  ? 3541 ILE A CB    1 
ATOM   14319 C  CG1   . ILE A 1 3541 ? 176.631 135.241 211.896 1.00 27.64  ? 3541 ILE A CG1   1 
ATOM   14320 C  CG2   . ILE A 1 3541 ? 174.807 133.672 211.198 1.00 24.68  ? 3541 ILE A CG2   1 
ATOM   14321 C  CD1   . ILE A 1 3541 ? 176.029 136.447 211.233 1.00 25.76  ? 3541 ILE A CD1   1 
ATOM   14322 N  N     . GLN A 1 3542 ? 176.044 130.578 212.194 1.00 37.52  ? 3542 GLN A N     1 
ATOM   14323 C  CA    . GLN A 1 3542 ? 175.703 129.215 211.813 1.00 39.68  ? 3542 GLN A CA    1 
ATOM   14324 C  C     . GLN A 1 3542 ? 174.467 129.200 210.924 1.00 46.70  ? 3542 GLN A C     1 
ATOM   14325 O  O     . GLN A 1 3542 ? 173.437 129.792 211.265 1.00 43.42  ? 3542 GLN A O     1 
ATOM   14326 C  CB    . GLN A 1 3542 ? 175.466 128.360 213.057 1.00 42.49  ? 3542 GLN A CB    1 
ATOM   14327 C  CG    . GLN A 1 3542 ? 176.703 128.142 213.912 1.00 48.68  ? 3542 GLN A CG    1 
ATOM   14328 C  CD    . GLN A 1 3542 ? 177.888 127.644 213.111 1.00 51.00  ? 3542 GLN A CD    1 
ATOM   14329 O  OE1   . GLN A 1 3542 ? 177.919 126.492 212.677 1.00 47.19  ? 3542 GLN A OE1   1 
ATOM   14330 N  NE2   . GLN A 1 3542 ? 178.876 128.510 212.913 1.00 48.38  ? 3542 GLN A NE2   1 
ATOM   14331 N  N     . PHE A 1 3543 ? 174.573 128.521 209.785 1.00 42.54  ? 3543 PHE A N     1 
ATOM   14332 C  CA    . PHE A 1 3543 ? 173.436 128.311 208.902 1.00 37.13  ? 3543 PHE A CA    1 
ATOM   14333 C  C     . PHE A 1 3543 ? 173.592 126.958 208.225 1.00 46.98  ? 3543 PHE A C     1 
ATOM   14334 O  O     . PHE A 1 3543 ? 174.704 126.448 208.060 1.00 51.68  ? 3543 PHE A O     1 
ATOM   14335 C  CB    . PHE A 1 3543 ? 173.300 129.438 207.869 1.00 32.30  ? 3543 PHE A CB    1 
ATOM   14336 C  CG    . PHE A 1 3543 ? 174.456 129.536 206.915 1.00 36.57  ? 3543 PHE A CG    1 
ATOM   14337 C  CD1   . PHE A 1 3543 ? 175.588 130.255 207.252 1.00 31.91  ? 3543 PHE A CD1   1 
ATOM   14338 C  CD2   . PHE A 1 3543 ? 174.404 128.923 205.674 1.00 42.16  ? 3543 PHE A CD2   1 
ATOM   14339 C  CE1   . PHE A 1 3543 ? 176.650 130.352 206.376 1.00 30.15  ? 3543 PHE A CE1   1 
ATOM   14340 C  CE2   . PHE A 1 3543 ? 175.463 129.017 204.795 1.00 33.50  ? 3543 PHE A CE2   1 
ATOM   14341 C  CZ    . PHE A 1 3543 ? 176.587 129.732 205.147 1.00 30.05  ? 3543 PHE A CZ    1 
ATOM   14342 N  N     . ARG A 1 3544 ? 172.460 126.381 207.832 1.00 51.49  ? 3544 ARG A N     1 
ATOM   14343 C  CA    . ARG A 1 3544 ? 172.420 125.038 207.262 1.00 54.81  ? 3544 ARG A CA    1 
ATOM   14344 C  C     . ARG A 1 3544 ? 172.508 125.141 205.743 1.00 54.92  ? 3544 ARG A C     1 
ATOM   14345 O  O     . ARG A 1 3544 ? 171.549 125.552 205.082 1.00 63.38  ? 3544 ARG A O     1 
ATOM   14346 C  CB    . ARG A 1 3544 ? 171.153 124.317 207.715 1.00 50.63  ? 3544 ARG A CB    1 
ATOM   14347 C  CG    . ARG A 1 3544 ? 171.169 124.005 209.204 1.00 56.49  ? 3544 ARG A CG    1 
ATOM   14348 C  CD    . ARG A 1 3544 ? 169.950 123.229 209.671 1.00 70.71  ? 3544 ARG A CD    1 
ATOM   14349 N  NE    . ARG A 1 3544 ? 168.742 124.043 209.617 1.00 69.84  ? 3544 ARG A NE    1 
ATOM   14350 C  CZ    . ARG A 1 3544 ? 167.724 123.825 208.796 1.00 61.63  ? 3544 ARG A CZ    1 
ATOM   14351 N  NH1   . ARG A 1 3544 ? 167.705 122.785 207.982 1.00 65.36  ? 3544 ARG A NH1   1 
ATOM   14352 N  NH2   . ARG A 1 3544 ? 166.691 124.663 208.806 1.00 54.82  ? 3544 ARG A NH2   1 
ATOM   14353 N  N     . THR A 1 3545 ? 173.665 124.764 205.193 1.00 58.36  ? 3545 THR A N     1 
ATOM   14354 C  CA    . THR A 1 3545 ? 173.933 124.950 203.770 1.00 65.64  ? 3545 THR A CA    1 
ATOM   14355 C  C     . THR A 1 3545 ? 173.219 123.923 202.899 1.00 64.05  ? 3545 THR A C     1 
ATOM   14356 O  O     . THR A 1 3545 ? 172.805 124.250 201.781 1.00 60.60  ? 3545 THR A O     1 
ATOM   14357 C  CB    . THR A 1 3545 ? 175.442 124.892 203.516 1.00 59.68  ? 3545 THR A CB    1 
ATOM   14358 O  OG1   . THR A 1 3545 ? 176.106 125.840 204.361 1.00 55.13  ? 3545 THR A OG1   1 
ATOM   14359 C  CG2   . THR A 1 3545 ? 175.760 125.220 202.066 1.00 55.67  ? 3545 THR A CG2   1 
ATOM   14360 N  N     . ASP A 1 3546 ? 173.056 122.691 203.388 1.00 67.51  ? 3546 ASP A N     1 
ATOM   14361 C  CA    . ASP A 1 3546 ? 172.515 121.624 202.552 1.00 70.99  ? 3546 ASP A CA    1 
ATOM   14362 C  C     . ASP A 1 3546 ? 171.077 121.895 202.125 1.00 75.38  ? 3546 ASP A C     1 
ATOM   14363 O  O     . ASP A 1 3546 ? 170.691 121.545 201.004 1.00 78.16  ? 3546 ASP A O     1 
ATOM   14364 C  CB    . ASP A 1 3546 ? 172.606 120.286 203.287 1.00 71.88  ? 3546 ASP A CB    1 
ATOM   14365 C  CG    . ASP A 1 3546 ? 171.919 120.314 204.639 1.00 75.43  ? 3546 ASP A CG    1 
ATOM   14366 O  OD1   . ASP A 1 3546 ? 171.472 121.400 205.063 1.00 74.04  ? 3546 ASP A OD1   1 
ATOM   14367 O  OD2   . ASP A 1 3546 ? 171.825 119.245 205.279 1.00 81.56  ? 3546 ASP A OD2   1 
ATOM   14368 N  N     . ILE A 1 3547 ? 170.274 122.509 202.996 1.00 72.48  ? 3547 ILE A N     1 
ATOM   14369 C  CA    . ILE A 1 3547 ? 168.866 122.730 202.683 1.00 64.21  ? 3547 ILE A CA    1 
ATOM   14370 C  C     . ILE A 1 3547 ? 168.723 123.796 201.600 1.00 59.25  ? 3547 ILE A C     1 
ATOM   14371 O  O     . ILE A 1 3547 ? 169.464 124.786 201.547 1.00 52.87  ? 3547 ILE A O     1 
ATOM   14372 C  CB    . ILE A 1 3547 ? 168.091 123.111 203.954 1.00 65.18  ? 3547 ILE A CB    1 
ATOM   14373 C  CG1   . ILE A 1 3547 ? 168.218 121.999 204.993 1.00 72.87  ? 3547 ILE A CG1   1 
ATOM   14374 C  CG2   . ILE A 1 3547 ? 166.624 123.374 203.649 1.00 53.38  ? 3547 ILE A CG2   1 
ATOM   14375 C  CD1   . ILE A 1 3547 ? 167.653 120.670 204.540 1.00 74.50  ? 3547 ILE A CD1   1 
ATOM   14376 N  N     . ALA A 1 3548 ? 167.752 123.581 200.716 1.00 51.49  ? 3548 ALA A N     1 
ATOM   14377 C  CA    . ALA A 1 3548 ? 167.435 124.505 199.639 1.00 42.54  ? 3548 ALA A CA    1 
ATOM   14378 C  C     . ALA A 1 3548 ? 166.423 125.538 200.115 1.00 38.62  ? 3548 ALA A C     1 
ATOM   14379 O  O     . ALA A 1 3548 ? 165.695 125.317 201.087 1.00 40.21  ? 3548 ALA A O     1 
ATOM   14380 C  CB    . ALA A 1 3548 ? 166.885 123.763 198.418 1.00 43.35  ? 3548 ALA A CB    1 
ATOM   14381 N  N     . ARG A 1 3549 ? 166.392 126.676 199.419 1.00 29.22  ? 3549 ARG A N     1 
ATOM   14382 C  CA    . ARG A 1 3549 ? 165.494 127.761 199.803 1.00 26.13  ? 3549 ARG A CA    1 
ATOM   14383 C  C     . ARG A 1 3549 ? 164.033 127.347 199.675 1.00 27.65  ? 3549 ARG A C     1 
ATOM   14384 O  O     . ARG A 1 3549 ? 163.215 127.645 200.554 1.00 31.47  ? 3549 ARG A O     1 
ATOM   14385 C  CB    . ARG A 1 3549 ? 165.772 128.993 198.943 1.00 22.58  ? 3549 ARG A CB    1 
ATOM   14386 C  CG    . ARG A 1 3549 ? 167.243 129.241 198.673 1.00 19.05  ? 3549 ARG A CG    1 
ATOM   14387 C  CD    . ARG A 1 3549 ? 167.455 130.582 197.999 1.00 16.71  ? 3549 ARG A CD    1 
ATOM   14388 N  NE    . ARG A 1 3549 ? 167.413 130.483 196.545 1.00 14.28  ? 3549 ARG A NE    1 
ATOM   14389 C  CZ    . ARG A 1 3549 ? 168.468 130.241 195.779 1.00 16.39  ? 3549 ARG A CZ    1 
ATOM   14390 N  NH1   . ARG A 1 3549 ? 169.669 130.044 196.299 1.00 15.64  ? 3549 ARG A NH1   1 
ATOM   14391 N  NH2   . ARG A 1 3549 ? 168.315 130.196 194.459 1.00 14.45  ? 3549 ARG A NH2   1 
ATOM   14392 N  N     . THR A 1 3550 ? 163.687 126.666 198.581 1.00 31.73  ? 3550 THR A N     1 
ATOM   14393 C  CA    . THR A 1 3550 ? 162.296 126.301 198.335 1.00 31.07  ? 3550 THR A CA    1 
ATOM   14394 C  C     . THR A 1 3550 ? 161.779 125.332 199.390 1.00 28.86  ? 3550 THR A C     1 
ATOM   14395 O  O     . THR A 1 3550 ? 160.641 125.460 199.854 1.00 25.30  ? 3550 THR A O     1 
ATOM   14396 C  CB    . THR A 1 3550 ? 162.155 125.695 196.939 1.00 27.70  ? 3550 THR A CB    1 
ATOM   14397 O  OG1   . THR A 1 3550 ? 163.200 124.738 196.727 1.00 40.14  ? 3550 THR A OG1   1 
ATOM   14398 C  CG2   . THR A 1 3550 ? 162.262 126.777 195.884 1.00 21.82  ? 3550 THR A CG2   1 
ATOM   14399 N  N     . GLU A 1 3551 ? 162.599 124.352 199.774 1.00 30.37  ? 3551 GLU A N     1 
ATOM   14400 C  CA    . GLU A 1 3551 ? 162.182 123.395 200.791 1.00 34.00  ? 3551 GLU A CA    1 
ATOM   14401 C  C     . GLU A 1 3551 ? 162.032 124.054 202.155 1.00 34.10  ? 3551 GLU A C     1 
ATOM   14402 O  O     . GLU A 1 3551 ? 161.150 123.674 202.933 1.00 33.85  ? 3551 GLU A O     1 
ATOM   14403 C  CB    . GLU A 1 3551 ? 163.184 122.242 200.865 1.00 40.61  ? 3551 GLU A CB    1 
ATOM   14404 C  CG    . GLU A 1 3551 ? 162.889 121.081 199.921 1.00 40.66  ? 3551 GLU A CG    1 
ATOM   14405 C  CD    . GLU A 1 3551 ? 161.808 120.146 200.438 1.00 49.39  ? 3551 GLU A CD    1 
ATOM   14406 O  OE1   . GLU A 1 3551 ? 161.708 119.015 199.918 1.00 56.59  ? 3551 GLU A OE1   1 
ATOM   14407 O  OE2   . GLU A 1 3551 ? 161.061 120.532 201.362 1.00 47.36  ? 3551 GLU A OE2   1 
ATOM   14408 N  N     . TYR A 1 3552 ? 162.880 125.035 202.466 1.00 34.61  ? 3552 TYR A N     1 
ATOM   14409 C  CA    . TYR A 1 3552 ? 162.822 125.689 203.767 1.00 26.75  ? 3552 TYR A CA    1 
ATOM   14410 C  C     . TYR A 1 3552 ? 161.675 126.687 203.864 1.00 21.98  ? 3552 TYR A C     1 
ATOM   14411 O  O     . TYR A 1 3552 ? 161.101 126.856 204.944 1.00 25.83  ? 3552 TYR A O     1 
ATOM   14412 C  CB    . TYR A 1 3552 ? 164.149 126.389 204.059 1.00 26.73  ? 3552 TYR A CB    1 
ATOM   14413 C  CG    . TYR A 1 3552 ? 164.248 126.958 205.453 1.00 27.46  ? 3552 TYR A CG    1 
ATOM   14414 C  CD1   . TYR A 1 3552 ? 164.123 126.139 206.566 1.00 34.81  ? 3552 TYR A CD1   1 
ATOM   14415 C  CD2   . TYR A 1 3552 ? 164.472 128.311 205.658 1.00 29.29  ? 3552 TYR A CD2   1 
ATOM   14416 C  CE1   . TYR A 1 3552 ? 164.215 126.652 207.844 1.00 37.00  ? 3552 TYR A CE1   1 
ATOM   14417 C  CE2   . TYR A 1 3552 ? 164.565 128.834 206.932 1.00 29.65  ? 3552 TYR A CE2   1 
ATOM   14418 C  CZ    . TYR A 1 3552 ? 164.436 128.000 208.021 1.00 35.86  ? 3552 TYR A CZ    1 
ATOM   14419 O  OH    . TYR A 1 3552 ? 164.528 128.515 209.292 1.00 43.25  ? 3552 TYR A OH    1 
ATOM   14420 N  N     . LEU A 1 3553 ? 161.329 127.351 202.764 1.00 23.14  ? 3553 LEU A N     1 
ATOM   14421 C  CA    . LEU A 1 3553 ? 160.330 128.411 202.792 1.00 21.78  ? 3553 LEU A CA    1 
ATOM   14422 C  C     . LEU A 1 3553 ? 158.928 127.936 202.429 1.00 27.83  ? 3553 LEU A C     1 
ATOM   14423 O  O     . LEU A 1 3553 ? 158.014 128.763 202.353 1.00 26.02  ? 3553 LEU A O     1 
ATOM   14424 C  CB    . LEU A 1 3553 ? 160.747 129.546 201.854 1.00 21.57  ? 3553 LEU A CB    1 
ATOM   14425 C  CG    . LEU A 1 3553 ? 161.820 130.494 202.393 1.00 20.52  ? 3553 LEU A CG    1 
ATOM   14426 C  CD1   . LEU A 1 3553 ? 162.309 131.429 201.303 1.00 17.43  ? 3553 LEU A CD1   1 
ATOM   14427 C  CD2   . LEU A 1 3553 ? 161.284 131.280 203.575 1.00 18.73  ? 3553 LEU A CD2   1 
ATOM   14428 N  N     . SER A 1 3554 ? 158.733 126.639 202.204 1.00 29.42  ? 3554 SER A N     1 
ATOM   14429 C  CA    . SER A 1 3554 ? 157.413 126.111 201.887 1.00 25.50  ? 3554 SER A CA    1 
ATOM   14430 C  C     . SER A 1 3554 ? 157.375 124.635 202.250 1.00 32.42  ? 3554 SER A C     1 
ATOM   14431 O  O     . SER A 1 3554 ? 158.414 123.990 202.409 1.00 35.49  ? 3554 SER A O     1 
ATOM   14432 C  CB    . SER A 1 3554 ? 157.066 126.313 200.409 1.00 24.89  ? 3554 SER A CB    1 
ATOM   14433 O  OG    . SER A 1 3554 ? 157.993 125.642 199.576 1.00 27.52  ? 3554 SER A OG    1 
ATOM   14434 N  N     . ASN A 1 3555 ? 156.161 124.107 202.382 1.00 31.02  ? 3555 ASN A N     1 
ATOM   14435 C  CA    . ASN A 1 3555 ? 155.962 122.701 202.689 1.00 26.17  ? 3555 ASN A CA    1 
ATOM   14436 C  C     . ASN A 1 3555 ? 155.452 121.966 201.451 1.00 34.59  ? 3555 ASN A C     1 
ATOM   14437 O  O     . ASN A 1 3555 ? 155.175 122.563 200.408 1.00 35.55  ? 3555 ASN A O     1 
ATOM   14438 C  CB    . ASN A 1 3555 ? 155.008 122.533 203.874 1.00 28.20  ? 3555 ASN A CB    1 
ATOM   14439 C  CG    . ASN A 1 3555 ? 153.786 123.421 203.773 1.00 30.40  ? 3555 ASN A CG    1 
ATOM   14440 O  OD1   . ASN A 1 3555 ? 152.882 123.160 202.982 1.00 33.74  ? 3555 ASN A OD1   1 
ATOM   14441 N  ND2   . ASN A 1 3555 ? 153.753 124.477 204.576 1.00 31.58  ? 3555 ASN A ND2   1 
ATOM   14442 N  N     . ALA A 1 3556 ? 155.329 120.644 201.575 1.00 37.40  ? 3556 ALA A N     1 
ATOM   14443 C  CA    . ALA A 1 3556 ? 154.994 119.814 200.423 1.00 36.77  ? 3556 ALA A CA    1 
ATOM   14444 C  C     . ALA A 1 3556 ? 153.537 119.976 199.997 1.00 36.35  ? 3556 ALA A C     1 
ATOM   14445 O  O     . ALA A 1 3556 ? 153.243 119.984 198.797 1.00 38.35  ? 3556 ALA A O     1 
ATOM   14446 C  CB    . ALA A 1 3556 ? 155.304 118.350 200.728 1.00 42.08  ? 3556 ALA A CB    1 
ATOM   14447 N  N     . ASP A 1 3557 ? 152.613 120.089 200.955 1.00 31.39  ? 3557 ASP A N     1 
ATOM   14448 C  CA    . ASP A 1 3557 ? 151.205 120.271 200.605 1.00 37.79  ? 3557 ASP A CA    1 
ATOM   14449 C  C     . ASP A 1 3557 ? 150.986 121.585 199.867 1.00 39.68  ? 3557 ASP A C     1 
ATOM   14450 O  O     . ASP A 1 3557 ? 150.217 121.648 198.901 1.00 37.51  ? 3557 ASP A O     1 
ATOM   14451 C  CB    . ASP A 1 3557 ? 150.337 120.216 201.862 1.00 41.55  ? 3557 ASP A CB    1 
ATOM   14452 C  CG    . ASP A 1 3557 ? 150.528 118.936 202.647 1.00 53.30  ? 3557 ASP A CG    1 
ATOM   14453 O  OD1   . ASP A 1 3557 ? 151.345 118.096 202.221 1.00 57.86  ? 3557 ASP A OD1   1 
ATOM   14454 O  OD2   . ASP A 1 3557 ? 149.861 118.769 203.689 1.00 56.04  ? 3557 ASP A OD2   1 
ATOM   14455 N  N     . GLU A 1 3558 ? 151.652 122.648 200.319 1.00 34.12  ? 3558 GLU A N     1 
ATOM   14456 C  CA    . GLU A 1 3558 ? 151.575 123.940 199.648 1.00 30.92  ? 3558 GLU A CA    1 
ATOM   14457 C  C     . GLU A 1 3558 ? 152.130 123.865 198.230 1.00 29.90  ? 3558 GLU A C     1 
ATOM   14458 O  O     . GLU A 1 3558 ? 151.552 124.444 197.302 1.00 29.89  ? 3558 GLU A O     1 
ATOM   14459 C  CB    . GLU A 1 3558 ? 152.326 124.968 200.494 1.00 32.83  ? 3558 GLU A CB    1 
ATOM   14460 C  CG    . GLU A 1 3558 ? 152.629 126.302 199.863 1.00 31.92  ? 3558 GLU A CG    1 
ATOM   14461 C  CD    . GLU A 1 3558 ? 153.078 127.308 200.907 1.00 39.80  ? 3558 GLU A CD    1 
ATOM   14462 O  OE1   . GLU A 1 3558 ? 153.051 126.963 202.107 1.00 38.26  ? 3558 GLU A OE1   1 
ATOM   14463 O  OE2   . GLU A 1 3558 ? 153.463 128.433 200.539 1.00 47.20  ? 3558 GLU A OE2   1 
ATOM   14464 N  N     . ARG A 1 3559 ? 153.235 123.140 198.044 1.00 32.50  ? 3559 ARG A N     1 
ATOM   14465 C  CA    . ARG A 1 3559 ? 153.794 122.954 196.710 1.00 25.19  ? 3559 ARG A CA    1 
ATOM   14466 C  C     . ARG A 1 3559 ? 152.849 122.159 195.815 1.00 30.97  ? 3559 ARG A C     1 
ATOM   14467 O  O     . ARG A 1 3559 ? 152.723 122.451 194.622 1.00 33.94  ? 3559 ARG A O     1 
ATOM   14468 C  CB    . ARG A 1 3559 ? 155.153 122.266 196.816 1.00 24.90  ? 3559 ARG A CB    1 
ATOM   14469 C  CG    . ARG A 1 3559 ? 156.316 123.233 196.906 1.00 24.90  ? 3559 ARG A CG    1 
ATOM   14470 C  CD    . ARG A 1 3559 ? 157.637 122.501 196.954 1.00 26.12  ? 3559 ARG A CD    1 
ATOM   14471 N  NE    . ARG A 1 3559 ? 158.212 122.557 198.291 1.00 27.80  ? 3559 ARG A NE    1 
ATOM   14472 C  CZ    . ARG A 1 3559 ? 158.566 121.495 199.001 1.00 33.20  ? 3559 ARG A CZ    1 
ATOM   14473 N  NH1   . ARG A 1 3559 ? 158.422 120.269 198.528 1.00 34.66  ? 3559 ARG A NH1   1 
ATOM   14474 N  NH2   . ARG A 1 3559 ? 159.072 121.669 200.218 1.00 30.82  ? 3559 ARG A NH2   1 
ATOM   14475 N  N     . LEU A 1 3560 ? 152.182 121.143 196.370 1.00 34.35  ? 3560 LEU A N     1 
ATOM   14476 C  CA    . LEU A 1 3560 ? 151.203 120.391 195.589 1.00 33.97  ? 3560 LEU A CA    1 
ATOM   14477 C  C     . LEU A 1 3560 ? 150.021 121.267 195.194 1.00 30.69  ? 3560 LEU A C     1 
ATOM   14478 O  O     . LEU A 1 3560 ? 149.505 121.162 194.075 1.00 34.36  ? 3560 LEU A O     1 
ATOM   14479 C  CB    . LEU A 1 3560 ? 150.726 119.167 196.371 1.00 32.03  ? 3560 LEU A CB    1 
ATOM   14480 C  CG    . LEU A 1 3560 ? 151.769 118.083 196.643 1.00 35.46  ? 3560 LEU A CG    1 
ATOM   14481 C  CD1   . LEU A 1 3560 ? 151.195 117.002 197.542 1.00 43.22  ? 3560 LEU A CD1   1 
ATOM   14482 C  CD2   . LEU A 1 3560 ? 152.270 117.488 195.337 1.00 39.17  ? 3560 LEU A CD2   1 
ATOM   14483 N  N     . ARG A 1 3561 ? 149.568 122.128 196.107 1.00 27.47  ? 3561 ARG A N     1 
ATOM   14484 C  CA    . ARG A 1 3561 ? 148.508 123.071 195.767 1.00 28.23  ? 3561 ARG A CA    1 
ATOM   14485 C  C     . ARG A 1 3561 ? 148.946 124.005 194.647 1.00 35.78  ? 3561 ARG A C     1 
ATOM   14486 O  O     . ARG A 1 3561 ? 148.169 124.297 193.729 1.00 40.59  ? 3561 ARG A O     1 
ATOM   14487 C  CB    . ARG A 1 3561 ? 148.104 123.874 197.002 1.00 32.23  ? 3561 ARG A CB    1 
ATOM   14488 C  CG    . ARG A 1 3561 ? 147.325 123.085 198.036 1.00 40.30  ? 3561 ARG A CG    1 
ATOM   14489 C  CD    . ARG A 1 3561 ? 146.545 124.008 198.956 1.00 43.57  ? 3561 ARG A CD    1 
ATOM   14490 N  NE    . ARG A 1 3561 ? 147.424 124.885 199.722 1.00 45.19  ? 3561 ARG A NE    1 
ATOM   14491 C  CZ    . ARG A 1 3561 ? 147.664 126.155 199.426 1.00 50.77  ? 3561 ARG A CZ    1 
ATOM   14492 N  NH1   . ARG A 1 3561 ? 147.104 126.739 198.380 1.00 41.04  ? 3561 ARG A NH1   1 
ATOM   14493 N  NH2   . ARG A 1 3561 ? 148.489 126.856 200.198 1.00 53.59  ? 3561 ARG A NH2   1 
ATOM   14494 N  N     . TRP A 1 3562 ? 150.189 124.485 194.709 1.00 32.91  ? 3562 TRP A N     1 
ATOM   14495 C  CA    . TRP A 1 3562 ? 150.713 125.319 193.632 1.00 26.39  ? 3562 TRP A CA    1 
ATOM   14496 C  C     . TRP A 1 3562 ? 150.743 124.559 192.312 1.00 35.13  ? 3562 TRP A C     1 
ATOM   14497 O  O     . TRP A 1 3562 ? 150.390 125.108 191.262 1.00 37.33  ? 3562 TRP A O     1 
ATOM   14498 C  CB    . TRP A 1 3562 ? 152.110 125.820 193.989 1.00 26.22  ? 3562 TRP A CB    1 
ATOM   14499 C  CG    . TRP A 1 3562 ? 152.117 126.868 195.046 1.00 25.06  ? 3562 TRP A CG    1 
ATOM   14500 C  CD1   . TRP A 1 3562 ? 151.070 127.649 195.433 1.00 22.70  ? 3562 TRP A CD1   1 
ATOM   14501 C  CD2   . TRP A 1 3562 ? 153.233 127.266 195.847 1.00 22.33  ? 3562 TRP A CD2   1 
ATOM   14502 N  NE1   . TRP A 1 3562 ? 151.462 128.502 196.434 1.00 21.16  ? 3562 TRP A NE1   1 
ATOM   14503 C  CE2   . TRP A 1 3562 ? 152.787 128.288 196.704 1.00 19.84  ? 3562 TRP A CE2   1 
ATOM   14504 C  CE3   . TRP A 1 3562 ? 154.567 126.855 195.924 1.00 17.40  ? 3562 TRP A CE3   1 
ATOM   14505 C  CZ2   . TRP A 1 3562 ? 153.627 128.908 197.621 1.00 21.14  ? 3562 TRP A CZ2   1 
ATOM   14506 C  CZ3   . TRP A 1 3562 ? 155.395 127.468 196.839 1.00 18.24  ? 3562 TRP A CZ3   1 
ATOM   14507 C  CH2   . TRP A 1 3562 ? 154.924 128.480 197.677 1.00 19.77  ? 3562 TRP A CH2   1 
ATOM   14508 N  N     . GLN A 1 3563 ? 151.168 123.294 192.350 1.00 35.23  ? 3563 GLN A N     1 
ATOM   14509 C  CA    . GLN A 1 3563 ? 151.170 122.464 191.149 1.00 34.88  ? 3563 GLN A CA    1 
ATOM   14510 C  C     . GLN A 1 3563 ? 149.767 122.339 190.571 1.00 33.11  ? 3563 GLN A C     1 
ATOM   14511 O  O     . GLN A 1 3563 ? 149.576 122.433 189.354 1.00 30.59  ? 3563 GLN A O     1 
ATOM   14512 C  CB    . GLN A 1 3563 ? 151.734 121.077 191.475 1.00 32.81  ? 3563 GLN A CB    1 
ATOM   14513 C  CG    . GLN A 1 3563 ? 153.247 120.982 191.737 1.00 36.09  ? 3563 GLN A CG    1 
ATOM   14514 C  CD    . GLN A 1 3563 ? 154.120 121.840 190.828 1.00 40.94  ? 3563 GLN A CD    1 
ATOM   14515 O  OE1   . GLN A 1 3563 ? 153.740 122.191 189.713 1.00 37.99  ? 3563 GLN A OE1   1 
ATOM   14516 N  NE2   . GLN A 1 3563 ? 155.308 122.181 191.316 1.00 41.35  ? 3563 GLN A NE2   1 
ATOM   14517 N  N     . ALA A 1 3564 ? 148.774 122.122 191.435 1.00 34.66  ? 3564 ALA A N     1 
ATOM   14518 C  CA    . ALA A 1 3564 ? 147.388 122.054 190.991 1.00 33.11  ? 3564 ALA A CA    1 
ATOM   14519 C  C     . ALA A 1 3564 ? 146.889 123.386 190.448 1.00 34.17  ? 3564 ALA A C     1 
ATOM   14520 O  O     . ALA A 1 3564 ? 145.986 123.398 189.605 1.00 31.51  ? 3564 ALA A O     1 
ATOM   14521 C  CB    . ALA A 1 3564 ? 146.490 121.591 192.138 1.00 32.00  ? 3564 ALA A CB    1 
ATOM   14522 N  N     . SER A 1 3565 ? 147.455 124.504 190.908 1.00 39.70  ? 3565 SER A N     1 
ATOM   14523 C  CA    . SER A 1 3565 ? 147.063 125.829 190.444 1.00 33.61  ? 3565 SER A CA    1 
ATOM   14524 C  C     . SER A 1 3565 ? 147.813 126.260 189.188 1.00 30.86  ? 3565 SER A C     1 
ATOM   14525 O  O     . SER A 1 3565 ? 147.931 127.464 188.925 1.00 30.54  ? 3565 SER A O     1 
ATOM   14526 C  CB    . SER A 1 3565 ? 147.259 126.856 191.560 1.00 31.54  ? 3565 SER A CB    1 
ATOM   14527 O  OG    . SER A 1 3565 ? 146.402 126.586 192.655 1.00 33.50  ? 3565 SER A OG    1 
ATOM   14528 N  N     . SER A 1 3566 ? 148.331 125.302 188.415 1.00 32.47  ? 3566 SER A N     1 
ATOM   14529 C  CA    . SER A 1 3566 ? 148.988 125.567 187.133 1.00 31.95  ? 3566 SER A CA    1 
ATOM   14530 C  C     . SER A 1 3566 ? 150.243 126.422 187.308 1.00 29.46  ? 3566 SER A C     1 
ATOM   14531 O  O     . SER A 1 3566 ? 150.422 127.449 186.652 1.00 32.18  ? 3566 SER A O     1 
ATOM   14532 C  CB    . SER A 1 3566 ? 148.019 126.214 186.139 1.00 36.78  ? 3566 SER A CB    1 
ATOM   14533 O  OG    . SER A 1 3566 ? 147.993 127.622 186.297 1.00 41.67  ? 3566 SER A OG    1 
ATOM   14534 N  N     . LEU A 1 3567 ? 151.121 125.983 188.207 1.00 30.86  ? 3567 LEU A N     1 
ATOM   14535 C  CA    . LEU A 1 3567 ? 152.419 126.609 188.396 1.00 29.38  ? 3567 LEU A CA    1 
ATOM   14536 C  C     . LEU A 1 3567 ? 153.511 125.673 187.912 1.00 32.48  ? 3567 LEU A C     1 
ATOM   14537 O  O     . LEU A 1 3567 ? 153.536 124.505 188.320 1.00 37.96  ? 3567 LEU A O     1 
ATOM   14538 C  CB    . LEU A 1 3567 ? 152.652 126.961 189.869 1.00 26.66  ? 3567 LEU A CB    1 
ATOM   14539 C  CG    . LEU A 1 3567 ? 153.973 127.670 190.184 1.00 25.16  ? 3567 LEU A CG    1 
ATOM   14540 C  CD1   . LEU A 1 3567 ? 153.874 129.160 189.900 1.00 20.11  ? 3567 LEU A CD1   1 
ATOM   14541 C  CD2   . LEU A 1 3567 ? 154.390 127.424 191.624 1.00 24.12  ? 3567 LEU A CD2   1 
ATOM   14542 N  N     . PRO A 1 3568 ? 154.409 126.127 187.038 1.00 32.16  ? 3568 PRO A N     1 
ATOM   14543 C  CA    . PRO A 1 3568 ? 155.481 125.246 186.562 1.00 29.00  ? 3568 PRO A CA    1 
ATOM   14544 C  C     . PRO A 1 3568 ? 156.367 124.771 187.704 1.00 30.46  ? 3568 PRO A C     1 
ATOM   14545 O  O     . PRO A 1 3568 ? 156.594 125.482 188.685 1.00 35.71  ? 3568 PRO A O     1 
ATOM   14546 C  CB    . PRO A 1 3568 ? 156.259 126.124 185.573 1.00 27.95  ? 3568 PRO A CB    1 
ATOM   14547 C  CG    . PRO A 1 3568 ? 155.765 127.514 185.779 1.00 26.62  ? 3568 PRO A CG    1 
ATOM   14548 C  CD    . PRO A 1 3568 ? 154.391 127.420 186.338 1.00 32.81  ? 3568 PRO A CD    1 
ATOM   14549 N  N     . ALA A 1 3569 ? 156.869 123.544 187.563 1.00 30.22  ? 3569 ALA A N     1 
ATOM   14550 C  CA    . ALA A 1 3569 ? 157.643 122.877 188.603 1.00 30.53  ? 3569 ALA A CA    1 
ATOM   14551 C  C     . ALA A 1 3569 ? 159.073 123.392 188.716 1.00 34.12  ? 3569 ALA A C     1 
ATOM   14552 O  O     . ALA A 1 3569 ? 159.878 122.781 189.427 1.00 40.24  ? 3569 ALA A O     1 
ATOM   14553 C  CB    . ALA A 1 3569 ? 157.658 121.367 188.355 1.00 24.85  ? 3569 ALA A CB    1 
ATOM   14554 N  N     . ASP A 1 3570 ? 159.405 124.486 188.039 1.00 29.26  ? 3570 ASP A N     1 
ATOM   14555 C  CA    . ASP A 1 3570 ? 160.745 125.046 188.114 1.00 27.83  ? 3570 ASP A CA    1 
ATOM   14556 C  C     . ASP A 1 3570 ? 161.012 125.622 189.502 1.00 26.20  ? 3570 ASP A C     1 
ATOM   14557 O  O     . ASP A 1 3570 ? 160.110 126.132 190.172 1.00 26.27  ? 3570 ASP A O     1 
ATOM   14558 C  CB    . ASP A 1 3570 ? 160.920 126.123 187.042 1.00 29.10  ? 3570 ASP A CB    1 
ATOM   14559 C  CG    . ASP A 1 3570 ? 162.208 126.899 187.194 1.00 28.12  ? 3570 ASP A CG    1 
ATOM   14560 O  OD1   . ASP A 1 3570 ? 163.287 126.270 187.220 1.00 31.67  ? 3570 ASP A OD1   1 
ATOM   14561 O  OD2   . ASP A 1 3570 ? 162.142 128.141 187.274 1.00 21.39  ? 3570 ASP A OD2   1 
ATOM   14562 N  N     . ASP A 1 3571 ? 162.271 125.519 189.938 1.00 28.04  ? 3571 ASP A N     1 
ATOM   14563 C  CA    . ASP A 1 3571 ? 162.647 126.008 191.263 1.00 24.65  ? 3571 ASP A CA    1 
ATOM   14564 C  C     . ASP A 1 3571 ? 162.466 127.517 191.378 1.00 20.78  ? 3571 ASP A C     1 
ATOM   14565 O  O     . ASP A 1 3571 ? 161.996 128.013 192.409 1.00 21.94  ? 3571 ASP A O     1 
ATOM   14566 C  CB    . ASP A 1 3571 ? 164.092 125.622 191.576 1.00 31.29  ? 3571 ASP A CB    1 
ATOM   14567 C  CG    . ASP A 1 3571 ? 164.267 124.130 191.776 1.00 49.17  ? 3571 ASP A CG    1 
ATOM   14568 O  OD1   . ASP A 1 3571 ? 163.304 123.469 192.218 1.00 49.09  ? 3571 ASP A OD1   1 
ATOM   14569 O  OD2   . ASP A 1 3571 ? 165.370 123.617 191.490 1.00 56.85  ? 3571 ASP A OD2   1 
ATOM   14570 N  N     . LEU A 1 3572 ? 162.846 128.263 190.338 1.00 20.59  ? 3572 LEU A N     1 
ATOM   14571 C  CA    . LEU A 1 3572 ? 162.681 129.713 190.374 1.00 14.56  ? 3572 LEU A CA    1 
ATOM   14572 C  C     . LEU A 1 3572 ? 161.209 130.092 190.460 1.00 17.55  ? 3572 LEU A C     1 
ATOM   14573 O  O     . LEU A 1 3572 ? 160.847 131.061 191.136 1.00 20.65  ? 3572 LEU A O     1 
ATOM   14574 C  CB    . LEU A 1 3572 ? 163.351 130.347 189.152 1.00 12.65  ? 3572 LEU A CB    1 
ATOM   14575 C  CG    . LEU A 1 3572 ? 163.472 131.870 189.043 1.00 14.01  ? 3572 LEU A CG    1 
ATOM   14576 C  CD1   . LEU A 1 3572 ? 164.680 132.232 188.203 1.00 14.08  ? 3572 LEU A CD1   1 
ATOM   14577 C  CD2   . LEU A 1 3572 ? 162.227 132.483 188.423 1.00 10.20  ? 3572 LEU A CD2   1 
ATOM   14578 N  N     . CYS A 1 3573 ? 160.341 129.334 189.789 1.00 16.85  ? 3573 CYS A N     1 
ATOM   14579 C  CA    . CYS A 1 3573 ? 158.910 129.591 189.904 1.00 17.23  ? 3573 CYS A CA    1 
ATOM   14580 C  C     . CYS A 1 3573 ? 158.392 129.273 191.301 1.00 17.21  ? 3573 CYS A C     1 
ATOM   14581 O  O     . CYS A 1 3573 ? 157.494 129.960 191.797 1.00 19.46  ? 3573 CYS A O     1 
ATOM   14582 C  CB    . CYS A 1 3573 ? 158.149 128.795 188.847 1.00 23.17  ? 3573 CYS A CB    1 
ATOM   14583 S  SG    . CYS A 1 3573 ? 158.148 129.587 187.224 1.00 44.86  ? 3573 CYS A SG    1 
ATOM   14584 N  N     . THR A 1 3574 ? 158.941 128.244 191.951 1.00 18.15  ? 3574 THR A N     1 
ATOM   14585 C  CA    . THR A 1 3574 ? 158.569 127.971 193.336 1.00 15.08  ? 3574 THR A CA    1 
ATOM   14586 C  C     . THR A 1 3574 ? 159.008 129.107 194.253 1.00 14.89  ? 3574 THR A C     1 
ATOM   14587 O  O     . THR A 1 3574 ? 158.270 129.502 195.163 1.00 16.62  ? 3574 THR A O     1 
ATOM   14588 C  CB    . THR A 1 3574 ? 159.174 126.644 193.795 1.00 15.39  ? 3574 THR A CB    1 
ATOM   14589 O  OG1   . THR A 1 3574 ? 158.731 125.592 192.930 1.00 24.04  ? 3574 THR A OG1   1 
ATOM   14590 C  CG2   . THR A 1 3574 ? 158.738 126.328 195.215 1.00 18.41  ? 3574 THR A CG2   1 
ATOM   14591 N  N     . GLU A 1 3575 ? 160.208 129.647 194.024 1.00 14.11  ? 3575 GLU A N     1 
ATOM   14592 C  CA    . GLU A 1 3575 ? 160.652 130.812 194.785 1.00 13.66  ? 3575 GLU A CA    1 
ATOM   14593 C  C     . GLU A 1 3575 ? 159.731 132.002 194.550 1.00 13.40  ? 3575 GLU A C     1 
ATOM   14594 O  O     . GLU A 1 3575 ? 159.394 132.736 195.487 1.00 14.67  ? 3575 GLU A O     1 
ATOM   14595 C  CB    . GLU A 1 3575 ? 162.087 131.174 194.402 1.00 14.44  ? 3575 GLU A CB    1 
ATOM   14596 C  CG    . GLU A 1 3575 ? 163.129 130.152 194.812 1.00 18.52  ? 3575 GLU A CG    1 
ATOM   14597 C  CD    . GLU A 1 3575 ? 164.414 130.290 194.021 1.00 17.60  ? 3575 GLU A CD    1 
ATOM   14598 O  OE1   . GLU A 1 3575 ? 164.459 131.130 193.099 1.00 13.52  ? 3575 GLU A OE1   1 
ATOM   14599 O  OE2   . GLU A 1 3575 ? 165.380 129.559 194.320 1.00 22.17  ? 3575 GLU A OE2   1 
ATOM   14600 N  N     . ASN A 1 3576 ? 159.318 132.207 193.299 1.00 14.35  ? 3576 ASN A N     1 
ATOM   14601 C  CA    . ASN A 1 3576 ? 158.397 133.292 192.983 1.00 12.49  ? 3576 ASN A CA    1 
ATOM   14602 C  C     . ASN A 1 3576 ? 157.062 133.108 193.694 1.00 12.80  ? 3576 ASN A C     1 
ATOM   14603 O  O     . ASN A 1 3576 ? 156.480 134.076 194.189 1.00 15.02  ? 3576 ASN A O     1 
ATOM   14604 C  CB    . ASN A 1 3576 ? 158.194 133.383 191.472 1.00 11.30  ? 3576 ASN A CB    1 
ATOM   14605 C  CG    . ASN A 1 3576 ? 159.369 134.024 190.763 1.00 10.17  ? 3576 ASN A CG    1 
ATOM   14606 O  OD1   . ASN A 1 3576 ? 160.252 134.599 191.396 1.00 12.27  ? 3576 ASN A OD1   1 
ATOM   14607 N  ND2   . ASN A 1 3576 ? 159.379 133.935 189.441 1.00 10.03  ? 3576 ASN A ND2   1 
ATOM   14608 N  N     . ALA A 1 3577 ? 156.558 131.874 193.746 1.00 12.78  ? 3577 ALA A N     1 
ATOM   14609 C  CA    . ALA A 1 3577 ? 155.324 131.606 194.479 1.00 13.74  ? 3577 ALA A CA    1 
ATOM   14610 C  C     . ALA A 1 3577 ? 155.494 131.856 195.973 1.00 14.15  ? 3577 ALA A C     1 
ATOM   14611 O  O     . ALA A 1 3577 ? 154.578 132.375 196.626 1.00 17.82  ? 3577 ALA A O     1 
ATOM   14612 C  CB    . ALA A 1 3577 ? 154.862 130.172 194.226 1.00 14.46  ? 3577 ALA A CB    1 
ATOM   14613 N  N     . ILE A 1 3578 ? 156.652 131.492 196.525 1.00 14.72  ? 3578 ILE A N     1 
ATOM   14614 C  CA    . ILE A 1 3578 ? 156.940 131.779 197.928 1.00 12.46  ? 3578 ILE A CA    1 
ATOM   14615 C  C     . ILE A 1 3578 ? 156.895 133.280 198.182 1.00 17.08  ? 3578 ILE A C     1 
ATOM   14616 O  O     . ILE A 1 3578 ? 156.317 133.742 199.173 1.00 21.25  ? 3578 ILE A O     1 
ATOM   14617 C  CB    . ILE A 1 3578 ? 158.301 131.176 198.324 1.00 11.78  ? 3578 ILE A CB    1 
ATOM   14618 C  CG1   . ILE A 1 3578 ? 158.207 129.653 198.409 1.00 12.83  ? 3578 ILE A CG1   1 
ATOM   14619 C  CG2   . ILE A 1 3578 ? 158.781 131.754 199.644 1.00 15.97  ? 3578 ILE A CG2   1 
ATOM   14620 C  CD1   . ILE A 1 3578 ? 159.547 128.961 198.488 1.00 13.03  ? 3578 ILE A CD1   1 
ATOM   14621 N  N     . MET A 1 3579 ? 157.504 134.064 197.289 1.00 13.95  ? 3579 MET A N     1 
ATOM   14622 C  CA    . MET A 1 3579 ? 157.436 135.518 197.416 1.00 10.92  ? 3579 MET A CA    1 
ATOM   14623 C  C     . MET A 1 3579 ? 156.003 136.023 197.285 1.00 12.47  ? 3579 MET A C     1 
ATOM   14624 O  O     . MET A 1 3579 ? 155.590 136.930 198.016 1.00 16.06  ? 3579 MET A O     1 
ATOM   14625 C  CB    . MET A 1 3579 ? 158.337 136.184 196.377 1.00 9.45   ? 3579 MET A CB    1 
ATOM   14626 C  CG    . MET A 1 3579 ? 159.760 135.664 196.366 1.00 8.76   ? 3579 MET A CG    1 
ATOM   14627 S  SD    . MET A 1 3579 ? 160.776 136.460 195.113 1.00 24.96  ? 3579 MET A SD    1 
ATOM   14628 C  CE    . MET A 1 3579 ? 162.346 135.641 195.374 1.00 7.79   ? 3579 MET A CE    1 
ATOM   14629 N  N     . LEU A 1 3580 ? 155.233 135.454 196.357 1.00 13.23  ? 3580 LEU A N     1 
ATOM   14630 C  CA    . LEU A 1 3580 ? 153.837 135.833 196.175 1.00 11.40  ? 3580 LEU A CA    1 
ATOM   14631 C  C     . LEU A 1 3580 ? 152.965 135.465 197.364 1.00 14.18  ? 3580 LEU A C     1 
ATOM   14632 O  O     . LEU A 1 3580 ? 151.860 136.003 197.486 1.00 17.77  ? 3580 LEU A O     1 
ATOM   14633 C  CB    . LEU A 1 3580 ? 153.272 135.191 194.907 1.00 10.28  ? 3580 LEU A CB    1 
ATOM   14634 C  CG    . LEU A 1 3580 ? 153.832 135.700 193.580 1.00 9.94   ? 3580 LEU A CG    1 
ATOM   14635 C  CD1   . LEU A 1 3580 ? 153.328 134.851 192.430 1.00 12.04  ? 3580 LEU A CD1   1 
ATOM   14636 C  CD2   . LEU A 1 3580 ? 153.457 137.155 193.374 1.00 10.15  ? 3580 LEU A CD2   1 
ATOM   14637 N  N     . LYS A 1 3581 ? 153.413 134.554 198.224 1.00 14.75  ? 3581 LYS A N     1 
ATOM   14638 C  CA    . LYS A 1 3581 ? 152.733 134.323 199.492 1.00 14.26  ? 3581 LYS A CA    1 
ATOM   14639 C  C     . LYS A 1 3581 ? 153.309 135.155 200.629 1.00 20.12  ? 3581 LYS A C     1 
ATOM   14640 O  O     . LYS A 1 3581 ? 152.556 135.812 201.353 1.00 23.21  ? 3581 LYS A O     1 
ATOM   14641 C  CB    . LYS A 1 3581 ? 152.791 132.844 199.880 1.00 16.59  ? 3581 LYS A CB    1 
ATOM   14642 C  CG    . LYS A 1 3581 ? 152.019 132.542 201.153 1.00 26.91  ? 3581 LYS A CG    1 
ATOM   14643 C  CD    . LYS A 1 3581 ? 152.036 131.069 201.503 1.00 34.54  ? 3581 LYS A CD    1 
ATOM   14644 C  CE    . LYS A 1 3581 ? 151.177 130.793 202.726 1.00 48.29  ? 3581 LYS A CE    1 
ATOM   14645 N  NZ    . LYS A 1 3581 ? 151.754 131.400 203.956 1.00 54.74  ? 3581 LYS A NZ    1 
ATOM   14646 N  N     . ARG A 1 3582 ? 154.629 135.143 200.797 1.00 20.17  ? 3582 ARG A N     1 
ATOM   14647 C  CA    . ARG A 1 3582 ? 155.304 135.850 201.884 1.00 13.49  ? 3582 ARG A CA    1 
ATOM   14648 C  C     . ARG A 1 3582 ? 155.807 137.185 201.346 1.00 20.93  ? 3582 ARG A C     1 
ATOM   14649 O  O     . ARG A 1 3582 ? 156.961 137.313 200.937 1.00 35.63  ? 3582 ARG A O     1 
ATOM   14650 C  CB    . ARG A 1 3582 ? 156.451 135.013 202.437 1.00 18.21  ? 3582 ARG A CB    1 
ATOM   14651 C  CG    . ARG A 1 3582 ? 156.033 133.688 203.037 1.00 22.32  ? 3582 ARG A CG    1 
ATOM   14652 C  CD    . ARG A 1 3582 ? 157.245 132.908 203.506 1.00 21.12  ? 3582 ARG A CD    1 
ATOM   14653 N  NE    . ARG A 1 3582 ? 156.877 131.606 204.045 1.00 30.94  ? 3582 ARG A NE    1 
ATOM   14654 C  CZ    . ARG A 1 3582 ? 156.519 131.392 205.303 1.00 39.11  ? 3582 ARG A CZ    1 
ATOM   14655 N  NH1   . ARG A 1 3582 ? 156.463 132.379 206.182 1.00 38.42  ? 3582 ARG A NH1   1 
ATOM   14656 N  NH2   . ARG A 1 3582 ? 156.207 130.159 205.688 1.00 46.78  ? 3582 ARG A NH2   1 
ATOM   14657 N  N     . PHE A 1 3583 ? 154.934 138.189 201.344 1.00 15.74  ? 3583 PHE A N     1 
ATOM   14658 C  CA    . PHE A 1 3583 ? 155.302 139.525 200.898 1.00 17.11  ? 3583 PHE A CA    1 
ATOM   14659 C  C     . PHE A 1 3583 ? 154.798 140.557 201.894 1.00 20.68  ? 3583 PHE A C     1 
ATOM   14660 O  O     . PHE A 1 3583 ? 153.726 140.392 202.483 1.00 28.59  ? 3583 PHE A O     1 
ATOM   14661 C  CB    . PHE A 1 3583 ? 154.745 139.828 199.496 1.00 16.29  ? 3583 PHE A CB    1 
ATOM   14662 C  CG    . PHE A 1 3583 ? 153.243 139.805 199.414 1.00 19.44  ? 3583 PHE A CG    1 
ATOM   14663 C  CD1   . PHE A 1 3583 ? 152.506 140.956 199.640 1.00 16.82  ? 3583 PHE A CD1   1 
ATOM   14664 C  CD2   . PHE A 1 3583 ? 152.569 138.639 199.099 1.00 20.68  ? 3583 PHE A CD2   1 
ATOM   14665 C  CE1   . PHE A 1 3583 ? 151.130 140.943 199.564 1.00 15.68  ? 3583 PHE A CE1   1 
ATOM   14666 C  CE2   . PHE A 1 3583 ? 151.189 138.622 199.021 1.00 21.81  ? 3583 PHE A CE2   1 
ATOM   14667 C  CZ    . PHE A 1 3583 ? 150.471 139.775 199.253 1.00 17.39  ? 3583 PHE A CZ    1 
ATOM   14668 N  N     . ASN A 1 3584 ? 155.582 141.618 202.083 1.00 18.71  ? 3584 ASN A N     1 
ATOM   14669 C  CA    . ASN A 1 3584 ? 155.177 142.764 202.887 1.00 16.71  ? 3584 ASN A CA    1 
ATOM   14670 C  C     . ASN A 1 3584 ? 154.602 143.885 202.031 1.00 21.00  ? 3584 ASN A C     1 
ATOM   14671 O  O     . ASN A 1 3584 ? 153.529 144.412 202.338 1.00 35.39  ? 3584 ASN A O     1 
ATOM   14672 C  CB    . ASN A 1 3584 ? 156.360 143.285 203.710 1.00 15.70  ? 3584 ASN A CB    1 
ATOM   14673 C  CG    . ASN A 1 3584 ? 156.906 142.244 204.661 1.00 23.90  ? 3584 ASN A CG    1 
ATOM   14674 O  OD1   . ASN A 1 3584 ? 158.106 141.976 204.681 1.00 25.13  ? 3584 ASN A OD1   1 
ATOM   14675 N  ND2   . ASN A 1 3584 ? 156.025 141.640 205.449 1.00 24.09  ? 3584 ASN A ND2   1 
ATOM   14676 N  N     . ARG A 1 3585 ? 155.296 144.265 200.962 1.00 12.57  ? 3585 ARG A N     1 
ATOM   14677 C  CA    . ARG A 1 3585 ? 154.725 145.149 199.959 1.00 12.83  ? 3585 ARG A CA    1 
ATOM   14678 C  C     . ARG A 1 3585 ? 154.018 144.329 198.890 1.00 16.24  ? 3585 ARG A C     1 
ATOM   14679 O  O     . ARG A 1 3585 ? 154.362 143.172 198.636 1.00 21.62  ? 3585 ARG A O     1 
ATOM   14680 C  CB    . ARG A 1 3585 ? 155.789 146.037 199.310 1.00 16.32  ? 3585 ARG A CB    1 
ATOM   14681 C  CG    . ARG A 1 3585 ? 156.439 147.028 200.250 1.00 14.58  ? 3585 ARG A CG    1 
ATOM   14682 C  CD    . ARG A 1 3585 ? 157.686 147.635 199.639 1.00 12.87  ? 3585 ARG A CD    1 
ATOM   14683 N  NE    . ARG A 1 3585 ? 158.667 146.630 199.253 1.00 13.29  ? 3585 ARG A NE    1 
ATOM   14684 C  CZ    . ARG A 1 3585 ? 159.673 146.851 198.418 1.00 13.00  ? 3585 ARG A CZ    1 
ATOM   14685 N  NH1   . ARG A 1 3585 ? 159.856 148.034 197.857 1.00 12.12  ? 3585 ARG A NH1   1 
ATOM   14686 N  NH2   . ARG A 1 3585 ? 160.515 145.862 198.141 1.00 13.01  ? 3585 ARG A NH2   1 
ATOM   14687 N  N     . TYR A 1 3586 ? 153.022 144.941 198.269 1.00 14.50  ? 3586 TYR A N     1 
ATOM   14688 C  CA    . TYR A 1 3586 ? 152.239 144.253 197.253 1.00 10.18  ? 3586 TYR A CA    1 
ATOM   14689 C  C     . TYR A 1 3586 ? 153.131 143.862 196.081 1.00 12.54  ? 3586 TYR A C     1 
ATOM   14690 O  O     . TYR A 1 3586 ? 153.934 144.680 195.620 1.00 11.47  ? 3586 TYR A O     1 
ATOM   14691 C  CB    . TYR A 1 3586 ? 151.095 145.136 196.777 1.00 13.92  ? 3586 TYR A CB    1 
ATOM   14692 C  CG    . TYR A 1 3586 ? 150.043 145.358 197.832 1.00 19.39  ? 3586 TYR A CG    1 
ATOM   14693 C  CD1   . TYR A 1 3586 ? 149.396 144.287 198.435 1.00 19.01  ? 3586 TYR A CD1   1 
ATOM   14694 C  CD2   . TYR A 1 3586 ? 149.709 146.640 198.245 1.00 21.57  ? 3586 TYR A CD2   1 
ATOM   14695 C  CE1   . TYR A 1 3586 ? 148.446 144.485 199.413 1.00 21.41  ? 3586 TYR A CE1   1 
ATOM   14696 C  CE2   . TYR A 1 3586 ? 148.757 146.847 199.221 1.00 28.21  ? 3586 TYR A CE2   1 
ATOM   14697 C  CZ    . TYR A 1 3586 ? 148.118 145.762 199.798 1.00 32.80  ? 3586 TYR A CZ    1 
ATOM   14698 O  OH    . TYR A 1 3586 ? 147.171 145.961 200.769 1.00 36.39  ? 3586 TYR A OH    1 
ATOM   14699 N  N     . PRO A 1 3587 ? 153.027 142.637 195.580 1.00 11.88  ? 3587 PRO A N     1 
ATOM   14700 C  CA    . PRO A 1 3587 ? 153.969 142.180 194.557 1.00 10.43  ? 3587 PRO A CA    1 
ATOM   14701 C  C     . PRO A 1 3587 ? 153.711 142.814 193.200 1.00 10.31  ? 3587 PRO A C     1 
ATOM   14702 O  O     . PRO A 1 3587 ? 152.581 143.159 192.848 1.00 12.02  ? 3587 PRO A O     1 
ATOM   14703 C  CB    . PRO A 1 3587 ? 153.738 140.664 194.509 1.00 8.00   ? 3587 PRO A CB    1 
ATOM   14704 C  CG    . PRO A 1 3587 ? 152.824 140.346 195.659 1.00 9.54   ? 3587 PRO A CG    1 
ATOM   14705 C  CD    . PRO A 1 3587 ? 152.066 141.588 195.951 1.00 9.49   ? 3587 PRO A CD    1 
ATOM   14706 N  N     . LEU A 1 3588 ? 154.787 142.955 192.433 1.00 9.20   ? 3588 LEU A N     1 
ATOM   14707 C  CA    . LEU A 1 3588 ? 154.720 143.286 191.017 1.00 9.06   ? 3588 LEU A CA    1 
ATOM   14708 C  C     . LEU A 1 3588 ? 155.215 142.073 190.242 1.00 13.15  ? 3588 LEU A C     1 
ATOM   14709 O  O     . LEU A 1 3588 ? 156.332 141.600 190.474 1.00 14.64  ? 3588 LEU A O     1 
ATOM   14710 C  CB    . LEU A 1 3588 ? 155.556 144.524 190.693 1.00 10.87  ? 3588 LEU A CB    1 
ATOM   14711 C  CG    . LEU A 1 3588 ? 155.273 145.224 189.361 1.00 12.36  ? 3588 LEU A CG    1 
ATOM   14712 C  CD1   . LEU A 1 3588 ? 155.474 146.722 189.497 1.00 16.54  ? 3588 LEU A CD1   1 
ATOM   14713 C  CD2   . LEU A 1 3588 ? 156.146 144.673 188.246 1.00 16.13  ? 3588 LEU A CD2   1 
ATOM   14714 N  N     . ILE A 1 3589 ? 154.386 141.571 189.331 1.00 13.34  ? 3589 ILE A N     1 
ATOM   14715 C  CA    . ILE A 1 3589 ? 154.663 140.336 188.608 1.00 12.40  ? 3589 ILE A CA    1 
ATOM   14716 C  C     . ILE A 1 3589 ? 155.149 140.676 187.208 1.00 14.91  ? 3589 ILE A C     1 
ATOM   14717 O  O     . ILE A 1 3589 ? 154.524 141.473 186.499 1.00 16.81  ? 3589 ILE A O     1 
ATOM   14718 C  CB    . ILE A 1 3589 ? 153.419 139.434 188.555 1.00 13.26  ? 3589 ILE A CB    1 
ATOM   14719 C  CG1   . ILE A 1 3589 ? 152.867 139.206 189.963 1.00 15.63  ? 3589 ILE A CG1   1 
ATOM   14720 C  CG2   . ILE A 1 3589 ? 153.750 138.113 187.888 1.00 15.38  ? 3589 ILE A CG2   1 
ATOM   14721 C  CD1   . ILE A 1 3589 ? 151.413 138.801 189.989 1.00 18.52  ? 3589 ILE A CD1   1 
ATOM   14722 N  N     . ILE A 1 3590 ? 156.269 140.076 186.812 1.00 14.41  ? 3590 ILE A N     1 
ATOM   14723 C  CA    . ILE A 1 3590 ? 156.796 140.240 185.463 1.00 17.17  ? 3590 ILE A CA    1 
ATOM   14724 C  C     . ILE A 1 3590 ? 156.783 138.890 184.759 1.00 20.82  ? 3590 ILE A C     1 
ATOM   14725 O  O     . ILE A 1 3590 ? 157.734 138.111 184.876 1.00 23.14  ? 3590 ILE A O     1 
ATOM   14726 C  CB    . ILE A 1 3590 ? 158.214 140.837 185.483 1.00 14.55  ? 3590 ILE A CB    1 
ATOM   14727 C  CG1   . ILE A 1 3590 ? 158.286 142.015 186.456 1.00 13.82  ? 3590 ILE A CG1   1 
ATOM   14728 C  CG2   . ILE A 1 3590 ? 158.637 141.265 184.085 1.00 19.08  ? 3590 ILE A CG2   1 
ATOM   14729 C  CD1   . ILE A 1 3590 ? 159.657 142.639 186.558 1.00 14.27  ? 3590 ILE A CD1   1 
ATOM   14730 N  N     . ASP A 1 3591 ? 155.706 138.601 184.030 1.00 21.38  ? 3591 ASP A N     1 
ATOM   14731 C  CA    . ASP A 1 3591 ? 155.594 137.362 183.265 1.00 23.86  ? 3591 ASP A CA    1 
ATOM   14732 C  C     . ASP A 1 3591 ? 155.322 137.645 181.791 1.00 23.27  ? 3591 ASP A C     1 
ATOM   14733 O  O     . ASP A 1 3591 ? 154.240 138.157 181.444 1.00 26.18  ? 3591 ASP A O     1 
ATOM   14734 C  CB    . ASP A 1 3591 ? 154.544 136.421 183.883 1.00 23.13  ? 3591 ASP A CB    1 
ATOM   14735 C  CG    . ASP A 1 3591 ? 153.126 136.999 183.903 1.00 37.35  ? 3591 ASP A CG    1 
ATOM   14736 O  OD1   . ASP A 1 3591 ? 152.899 138.153 183.494 1.00 40.50  ? 3591 ASP A OD1   1 
ATOM   14737 O  OD2   . ASP A 1 3591 ? 152.209 136.265 184.326 1.00 40.52  ? 3591 ASP A OD2   1 
ATOM   14738 N  N     . PRO A 1 3592 ? 156.259 137.356 180.895 1.00 21.95  ? 3592 PRO A N     1 
ATOM   14739 C  CA    . PRO A 1 3592 ? 155.970 137.509 179.465 1.00 22.14  ? 3592 PRO A CA    1 
ATOM   14740 C  C     . PRO A 1 3592 ? 155.128 136.361 178.931 1.00 22.28  ? 3592 PRO A C     1 
ATOM   14741 O  O     . PRO A 1 3592 ? 154.362 136.531 177.979 1.00 26.38  ? 3592 PRO A O     1 
ATOM   14742 C  CB    . PRO A 1 3592 ? 157.364 137.543 178.830 1.00 22.52  ? 3592 PRO A CB    1 
ATOM   14743 C  CG    . PRO A 1 3592 ? 158.209 136.748 179.759 1.00 23.27  ? 3592 PRO A CG    1 
ATOM   14744 C  CD    . PRO A 1 3592 ? 157.658 136.968 181.144 1.00 16.83  ? 3592 PRO A CD    1 
ATOM   14745 N  N     . SER A 1 3593 ? 155.261 135.185 179.547 1.00 24.94  ? 3593 SER A N     1 
ATOM   14746 C  CA    . SER A 1 3593 ? 154.469 134.031 179.140 1.00 24.86  ? 3593 SER A CA    1 
ATOM   14747 C  C     . SER A 1 3593 ? 153.031 134.115 179.636 1.00 26.13  ? 3593 SER A C     1 
ATOM   14748 O  O     . SER A 1 3593 ? 152.134 133.531 179.019 1.00 33.28  ? 3593 SER A O     1 
ATOM   14749 C  CB    . SER A 1 3593 ? 155.123 132.743 179.642 1.00 26.57  ? 3593 SER A CB    1 
ATOM   14750 O  OG    . SER A 1 3593 ? 155.103 132.680 181.057 1.00 28.60  ? 3593 SER A OG    1 
ATOM   14751 N  N     . GLY A 1 3594 ? 152.792 134.823 180.736 1.00 27.61  ? 3594 GLY A N     1 
ATOM   14752 C  CA    . GLY A 1 3594 ? 151.463 134.949 181.293 1.00 25.90  ? 3594 GLY A CA    1 
ATOM   14753 C  C     . GLY A 1 3594 ? 151.036 133.821 182.205 1.00 27.94  ? 3594 GLY A C     1 
ATOM   14754 O  O     . GLY A 1 3594 ? 149.878 133.807 182.642 1.00 33.94  ? 3594 GLY A O     1 
ATOM   14755 N  N     . GLN A 1 3595 ? 151.928 132.875 182.505 1.00 24.77  ? 3595 GLN A N     1 
ATOM   14756 C  CA    . GLN A 1 3595 ? 151.566 131.759 183.372 1.00 24.30  ? 3595 GLN A CA    1 
ATOM   14757 C  C     . GLN A 1 3595 ? 151.307 132.223 184.799 1.00 27.36  ? 3595 GLN A C     1 
ATOM   14758 O  O     . GLN A 1 3595 ? 150.442 131.671 185.491 1.00 34.26  ? 3595 GLN A O     1 
ATOM   14759 C  CB    . GLN A 1 3595 ? 152.668 130.702 183.348 1.00 29.66  ? 3595 GLN A CB    1 
ATOM   14760 C  CG    . GLN A 1 3595 ? 152.631 129.791 182.135 1.00 34.97  ? 3595 GLN A CG    1 
ATOM   14761 C  CD    . GLN A 1 3595 ? 153.683 128.704 182.198 1.00 46.24  ? 3595 GLN A CD    1 
ATOM   14762 O  OE1   . GLN A 1 3595 ? 154.881 128.986 182.238 1.00 47.90  ? 3595 GLN A OE1   1 
ATOM   14763 N  NE2   . GLN A 1 3595 ? 153.242 127.453 182.207 1.00 46.52  ? 3595 GLN A NE2   1 
ATOM   14764 N  N     . ALA A 1 3596 ? 152.053 133.229 185.261 1.00 24.54  ? 3596 ALA A N     1 
ATOM   14765 C  CA    . ALA A 1 3596 ? 151.895 133.701 186.632 1.00 19.48  ? 3596 ALA A CA    1 
ATOM   14766 C  C     . ALA A 1 3596 ? 150.524 134.328 186.849 1.00 24.87  ? 3596 ALA A C     1 
ATOM   14767 O  O     . ALA A 1 3596 ? 149.948 134.214 187.936 1.00 26.45  ? 3596 ALA A O     1 
ATOM   14768 C  CB    . ALA A 1 3596 ? 153.001 134.695 186.974 1.00 18.16  ? 3596 ALA A CB    1 
ATOM   14769 N  N     . THR A 1 3597 ? 149.989 135.004 185.831 1.00 28.39  ? 3597 THR A N     1 
ATOM   14770 C  CA    . THR A 1 3597 ? 148.646 135.564 185.940 1.00 30.03  ? 3597 THR A CA    1 
ATOM   14771 C  C     . THR A 1 3597 ? 147.612 134.464 186.152 1.00 37.28  ? 3597 THR A C     1 
ATOM   14772 O  O     . THR A 1 3597 ? 146.732 134.576 187.016 1.00 42.12  ? 3597 THR A O     1 
ATOM   14773 C  CB    . THR A 1 3597 ? 148.320 136.382 184.690 1.00 30.41  ? 3597 THR A CB    1 
ATOM   14774 O  OG1   . THR A 1 3597 ? 149.133 137.561 184.667 1.00 34.46  ? 3597 THR A OG1   1 
ATOM   14775 C  CG2   . THR A 1 3597 ? 146.854 136.781 184.673 1.00 39.78  ? 3597 THR A CG2   1 
ATOM   14776 N  N     . GLU A 1 3598 ? 147.718 133.380 185.381 1.00 35.90  ? 3598 GLU A N     1 
ATOM   14777 C  CA    . GLU A 1 3598 ? 146.806 132.255 185.554 1.00 35.13  ? 3598 GLU A CA    1 
ATOM   14778 C  C     . GLU A 1 3598 ? 146.989 131.601 186.918 1.00 33.05  ? 3598 GLU A C     1 
ATOM   14779 O  O     . GLU A 1 3598 ? 146.011 131.191 187.553 1.00 33.26  ? 3598 GLU A O     1 
ATOM   14780 C  CB    . GLU A 1 3598 ? 147.010 131.235 184.436 1.00 42.57  ? 3598 GLU A CB    1 
ATOM   14781 C  CG    . GLU A 1 3598 ? 146.606 131.734 183.059 1.00 56.02  ? 3598 GLU A CG    1 
ATOM   14782 C  CD    . GLU A 1 3598 ? 146.840 130.703 181.972 1.00 81.77  ? 3598 GLU A CD    1 
ATOM   14783 O  OE1   . GLU A 1 3598 ? 147.433 129.645 182.271 1.00 76.99  ? 3598 GLU A OE1   1 
ATOM   14784 O  OE2   . GLU A 1 3598 ? 146.428 130.949 180.818 1.00 94.98  ? 3598 GLU A OE2   1 
ATOM   14785 N  N     . PHE A 1 3599 ? 148.236 131.487 187.380 1.00 31.54  ? 3599 PHE A N     1 
ATOM   14786 C  CA    . PHE A 1 3599 ? 148.487 130.905 188.695 1.00 27.57  ? 3599 PHE A CA    1 
ATOM   14787 C  C     . PHE A 1 3599 ? 147.852 131.744 189.797 1.00 27.19  ? 3599 PHE A C     1 
ATOM   14788 O  O     . PHE A 1 3599 ? 147.239 131.205 190.726 1.00 31.20  ? 3599 PHE A O     1 
ATOM   14789 C  CB    . PHE A 1 3599 ? 149.992 130.761 188.921 1.00 21.55  ? 3599 PHE A CB    1 
ATOM   14790 C  CG    . PHE A 1 3599 ? 150.385 130.625 190.364 1.00 23.02  ? 3599 PHE A CG    1 
ATOM   14791 C  CD1   . PHE A 1 3599 ? 150.247 129.415 191.021 1.00 24.34  ? 3599 PHE A CD1   1 
ATOM   14792 C  CD2   . PHE A 1 3599 ? 150.902 131.703 191.062 1.00 24.09  ? 3599 PHE A CD2   1 
ATOM   14793 C  CE1   . PHE A 1 3599 ? 150.613 129.283 192.345 1.00 21.50  ? 3599 PHE A CE1   1 
ATOM   14794 C  CE2   . PHE A 1 3599 ? 151.267 131.577 192.387 1.00 20.41  ? 3599 PHE A CE2   1 
ATOM   14795 C  CZ    . PHE A 1 3599 ? 151.122 130.365 193.029 1.00 19.97  ? 3599 PHE A CZ    1 
ATOM   14796 N  N     . ILE A 1 3600 ? 147.986 133.069 189.705 1.00 27.02  ? 3600 ILE A N     1 
ATOM   14797 C  CA    . ILE A 1 3600 ? 147.373 133.958 190.687 1.00 30.25  ? 3600 ILE A CA    1 
ATOM   14798 C  C     . ILE A 1 3600 ? 145.856 133.838 190.641 1.00 28.09  ? 3600 ILE A C     1 
ATOM   14799 O  O     . ILE A 1 3600 ? 145.192 133.790 191.683 1.00 31.25  ? 3600 ILE A O     1 
ATOM   14800 C  CB    . ILE A 1 3600 ? 147.839 135.409 190.453 1.00 28.79  ? 3600 ILE A CB    1 
ATOM   14801 C  CG1   . ILE A 1 3600 ? 149.258 135.611 190.987 1.00 23.94  ? 3600 ILE A CG1   1 
ATOM   14802 C  CG2   . ILE A 1 3600 ? 146.889 136.397 191.108 1.00 24.08  ? 3600 ILE A CG2   1 
ATOM   14803 C  CD1   . ILE A 1 3600 ? 149.376 135.445 192.485 1.00 19.38  ? 3600 ILE A CD1   1 
ATOM   14804 N  N     . MET A 1 3601 ? 145.284 133.784 189.437 1.00 31.86  ? 3601 MET A N     1 
ATOM   14805 C  CA    . MET A 1 3601 ? 143.834 133.664 189.313 1.00 30.73  ? 3601 MET A CA    1 
ATOM   14806 C  C     . MET A 1 3601 ? 143.328 132.356 189.907 1.00 34.68  ? 3601 MET A C     1 
ATOM   14807 O  O     . MET A 1 3601 ? 142.278 132.327 190.559 1.00 35.66  ? 3601 MET A O     1 
ATOM   14808 C  CB    . MET A 1 3601 ? 143.423 133.785 187.849 1.00 28.70  ? 3601 MET A CB    1 
ATOM   14809 C  CG    . MET A 1 3601 ? 143.537 135.193 187.323 1.00 33.92  ? 3601 MET A CG    1 
ATOM   14810 S  SD    . MET A 1 3601 ? 142.249 136.230 188.030 1.00 41.75  ? 3601 MET A SD    1 
ATOM   14811 C  CE    . MET A 1 3601 ? 142.275 137.599 186.893 1.00 46.24  ? 3601 MET A CE    1 
ATOM   14812 N  N     . ASN A 1 3602 ? 144.051 131.259 189.679 1.00 32.55  ? 3602 ASN A N     1 
ATOM   14813 C  CA    . ASN A 1 3602 ? 143.651 129.979 190.251 1.00 28.79  ? 3602 ASN A CA    1 
ATOM   14814 C  C     . ASN A 1 3602 ? 143.789 129.982 191.768 1.00 28.37  ? 3602 ASN A C     1 
ATOM   14815 O  O     . ASN A 1 3602 ? 142.939 129.427 192.475 1.00 28.98  ? 3602 ASN A O     1 
ATOM   14816 C  CB    . ASN A 1 3602 ? 144.476 128.849 189.638 1.00 31.85  ? 3602 ASN A CB    1 
ATOM   14817 C  CG    . ASN A 1 3602 ? 144.289 128.741 188.139 1.00 32.70  ? 3602 ASN A CG    1 
ATOM   14818 O  OD1   . ASN A 1 3602 ? 143.189 128.933 187.624 1.00 34.72  ? 3602 ASN A OD1   1 
ATOM   14819 N  ND2   . ASN A 1 3602 ? 145.367 128.429 187.430 1.00 32.76  ? 3602 ASN A ND2   1 
ATOM   14820 N  N     . GLU A 1 3603 ? 144.853 130.599 192.288 1.00 30.03  ? 3603 GLU A N     1 
ATOM   14821 C  CA    . GLU A 1 3603 ? 145.082 130.593 193.730 1.00 29.28  ? 3603 GLU A CA    1 
ATOM   14822 C  C     . GLU A 1 3603 ? 144.015 131.386 194.473 1.00 29.24  ? 3603 GLU A C     1 
ATOM   14823 O  O     . GLU A 1 3603 ? 143.587 130.991 195.563 1.00 36.05  ? 3603 GLU A O     1 
ATOM   14824 C  CB    . GLU A 1 3603 ? 146.471 131.143 194.044 1.00 26.58  ? 3603 GLU A CB    1 
ATOM   14825 C  CG    . GLU A 1 3603 ? 147.589 130.158 193.780 1.00 27.98  ? 3603 GLU A CG    1 
ATOM   14826 C  CD    . GLU A 1 3603 ? 147.933 129.332 195.001 1.00 36.71  ? 3603 GLU A CD    1 
ATOM   14827 O  OE1   . GLU A 1 3603 ? 148.067 129.916 196.096 1.00 44.51  ? 3603 GLU A OE1   1 
ATOM   14828 O  OE2   . GLU A 1 3603 ? 148.066 128.098 194.866 1.00 38.94  ? 3603 GLU A OE2   1 
ATOM   14829 N  N     . TYR A 1 3604 ? 143.577 132.509 193.907 1.00 32.89  ? 3604 TYR A N     1 
ATOM   14830 C  CA    . TYR A 1 3604 ? 142.607 133.380 194.556 1.00 35.71  ? 3604 TYR A CA    1 
ATOM   14831 C  C     . TYR A 1 3604 ? 141.217 133.267 193.941 1.00 38.88  ? 3604 TYR A C     1 
ATOM   14832 O  O     . TYR A 1 3604 ? 140.412 134.194 194.070 1.00 45.95  ? 3604 TYR A O     1 
ATOM   14833 C  CB    . TYR A 1 3604 ? 143.095 134.828 194.516 1.00 33.87  ? 3604 TYR A CB    1 
ATOM   14834 C  CG    . TYR A 1 3604 ? 144.258 135.100 195.443 1.00 31.28  ? 3604 TYR A CG    1 
ATOM   14835 C  CD1   . TYR A 1 3604 ? 145.550 134.734 195.093 1.00 25.51  ? 3604 TYR A CD1   1 
ATOM   14836 C  CD2   . TYR A 1 3604 ? 144.062 135.719 196.669 1.00 33.91  ? 3604 TYR A CD2   1 
ATOM   14837 C  CE1   . TYR A 1 3604 ? 146.613 134.977 195.937 1.00 23.77  ? 3604 TYR A CE1   1 
ATOM   14838 C  CE2   . TYR A 1 3604 ? 145.121 135.968 197.519 1.00 33.22  ? 3604 TYR A CE2   1 
ATOM   14839 C  CZ    . TYR A 1 3604 ? 146.394 135.594 197.148 1.00 30.59  ? 3604 TYR A CZ    1 
ATOM   14840 O  OH    . TYR A 1 3604 ? 147.452 135.839 197.991 1.00 39.07  ? 3604 TYR A OH    1 
ATOM   14841 N  N     . LYS A 1 3605 ? 140.921 132.149 193.274 1.00 40.74  ? 3605 LYS A N     1 
ATOM   14842 C  CA    . LYS A 1 3605 ? 139.597 131.966 192.688 1.00 39.34  ? 3605 LYS A CA    1 
ATOM   14843 C  C     . LYS A 1 3605 ? 138.533 131.821 193.768 1.00 40.23  ? 3605 LYS A C     1 
ATOM   14844 O  O     . LYS A 1 3605 ? 137.392 132.264 193.590 1.00 45.91  ? 3605 LYS A O     1 
ATOM   14845 C  CB    . LYS A 1 3605 ? 139.598 130.750 191.763 1.00 35.52  ? 3605 LYS A CB    1 
ATOM   14846 C  CG    . LYS A 1 3605 ? 138.301 130.547 191.001 1.00 38.35  ? 3605 LYS A CG    1 
ATOM   14847 C  CD    . LYS A 1 3605 ? 138.353 129.288 190.155 1.00 45.11  ? 3605 LYS A CD    1 
ATOM   14848 C  CE    . LYS A 1 3605 ? 139.246 129.481 188.940 1.00 48.87  ? 3605 LYS A CE    1 
ATOM   14849 N  NZ    . LYS A 1 3605 ? 139.217 128.296 188.037 1.00 58.86  ? 3605 LYS A NZ    1 
ATOM   14850 N  N     . ASP A 1 3606 ? 138.887 131.199 194.895 1.00 40.21  ? 3606 ASP A N     1 
ATOM   14851 C  CA    . ASP A 1 3606 ? 137.926 131.017 195.978 1.00 44.29  ? 3606 ASP A CA    1 
ATOM   14852 C  C     . ASP A 1 3606 ? 137.486 132.356 196.555 1.00 50.56  ? 3606 ASP A C     1 
ATOM   14853 O  O     . ASP A 1 3606 ? 136.319 132.521 196.928 1.00 55.99  ? 3606 ASP A O     1 
ATOM   14854 C  CB    . ASP A 1 3606 ? 138.539 130.131 197.066 1.00 56.45  ? 3606 ASP A CB    1 
ATOM   14855 C  CG    . ASP A 1 3606 ? 137.527 129.683 198.110 1.00 71.68  ? 3606 ASP A CG    1 
ATOM   14856 O  OD1   . ASP A 1 3606 ? 136.342 130.064 198.018 1.00 70.44  ? 3606 ASP A OD1   1 
ATOM   14857 O  OD2   . ASP A 1 3606 ? 137.925 128.941 199.032 1.00 80.70  ? 3606 ASP A OD2   1 
ATOM   14858 N  N     . ARG A 1 3607 ? 138.395 133.326 196.620 1.00 50.75  ? 3607 ARG A N     1 
ATOM   14859 C  CA    . ARG A 1 3607 ? 138.099 134.650 197.146 1.00 45.80  ? 3607 ARG A CA    1 
ATOM   14860 C  C     . ARG A 1 3607 ? 137.580 135.608 196.080 1.00 44.04  ? 3607 ARG A C     1 
ATOM   14861 O  O     . ARG A 1 3607 ? 137.448 136.805 196.355 1.00 54.16  ? 3607 ARG A O     1 
ATOM   14862 C  CB    . ARG A 1 3607 ? 139.343 135.240 197.812 1.00 44.70  ? 3607 ARG A CB    1 
ATOM   14863 C  CG    . ARG A 1 3607 ? 139.392 135.041 199.316 1.00 45.68  ? 3607 ARG A CG    1 
ATOM   14864 C  CD    . ARG A 1 3607 ? 139.881 133.646 199.669 1.00 48.53  ? 3607 ARG A CD    1 
ATOM   14865 N  NE    . ARG A 1 3607 ? 141.228 133.388 199.173 1.00 52.21  ? 3607 ARG A NE    1 
ATOM   14866 C  CZ    . ARG A 1 3607 ? 142.331 133.941 199.660 1.00 47.86  ? 3607 ARG A CZ    1 
ATOM   14867 N  NH1   . ARG A 1 3607 ? 142.291 134.785 200.678 1.00 38.95  ? 3607 ARG A NH1   1 
ATOM   14868 N  NH2   . ARG A 1 3607 ? 143.505 133.632 199.118 1.00 42.70  ? 3607 ARG A NH2   1 
ATOM   14869 N  N     . LYS A 1 3608 ? 137.292 135.110 194.876 1.00 38.40  ? 3608 LYS A N     1 
ATOM   14870 C  CA    . LYS A 1 3608 ? 136.741 135.908 193.780 1.00 47.51  ? 3608 LYS A CA    1 
ATOM   14871 C  C     . LYS A 1 3608 ? 137.671 137.065 193.405 1.00 46.13  ? 3608 LYS A C     1 
ATOM   14872 O  O     . LYS A 1 3608 ? 137.325 138.242 193.512 1.00 46.31  ? 3608 LYS A O     1 
ATOM   14873 C  CB    . LYS A 1 3608 ? 135.336 136.418 194.125 1.00 53.43  ? 3608 LYS A CB    1 
ATOM   14874 C  CG    . LYS A 1 3608 ? 134.337 135.323 194.470 1.00 57.90  ? 3608 LYS A CG    1 
ATOM   14875 C  CD    . LYS A 1 3608 ? 133.942 134.513 193.240 1.00 58.08  ? 3608 LYS A CD    1 
ATOM   14876 C  CE    . LYS A 1 3608 ? 133.664 135.410 192.041 1.00 51.77  ? 3608 LYS A CE    1 
ATOM   14877 N  NZ    . LYS A 1 3608 ? 133.726 134.661 190.755 1.00 52.50  ? 3608 LYS A NZ    1 
ATOM   14878 N  N     . ILE A 1 3609 ? 138.872 136.701 192.955 1.00 41.97  ? 3609 ILE A N     1 
ATOM   14879 C  CA    . ILE A 1 3609 ? 139.799 137.686 192.414 1.00 36.46  ? 3609 ILE A CA    1 
ATOM   14880 C  C     . ILE A 1 3609 ? 139.319 138.130 191.038 1.00 33.64  ? 3609 ILE A C     1 
ATOM   14881 O  O     . ILE A 1 3609 ? 138.757 137.340 190.268 1.00 40.65  ? 3609 ILE A O     1 
ATOM   14882 C  CB    . ILE A 1 3609 ? 141.226 137.110 192.369 1.00 34.14  ? 3609 ILE A CB    1 
ATOM   14883 C  CG1   . ILE A 1 3609 ? 142.244 138.206 192.046 1.00 35.18  ? 3609 ILE A CG1   1 
ATOM   14884 C  CG2   . ILE A 1 3609 ? 141.317 135.944 191.399 1.00 36.76  ? 3609 ILE A CG2   1 
ATOM   14885 C  CD1   . ILE A 1 3609 ? 143.674 137.800 192.295 1.00 35.33  ? 3609 ILE A CD1   1 
ATOM   14886 N  N     . THR A 1 3610 ? 139.523 139.408 190.727 1.00 30.00  ? 3610 THR A N     1 
ATOM   14887 C  CA    . THR A 1 3610 ? 138.967 140.026 189.531 1.00 33.97  ? 3610 THR A CA    1 
ATOM   14888 C  C     . THR A 1 3610 ? 140.083 140.585 188.658 1.00 37.28  ? 3610 THR A C     1 
ATOM   14889 O  O     . THR A 1 3610 ? 141.049 141.161 189.169 1.00 37.27  ? 3610 THR A O     1 
ATOM   14890 C  CB    . THR A 1 3610 ? 137.984 141.138 189.905 1.00 35.78  ? 3610 THR A CB    1 
ATOM   14891 O  OG1   . THR A 1 3610 ? 137.027 140.633 190.843 1.00 38.95  ? 3610 THR A OG1   1 
ATOM   14892 C  CG2   . THR A 1 3610 ? 137.252 141.645 188.673 1.00 35.57  ? 3610 THR A CG2   1 
ATOM   14893 N  N     . ARG A 1 3611 ? 139.945 140.411 187.345 1.00 42.24  ? 3611 ARG A N     1 
ATOM   14894 C  CA    . ARG A 1 3611 ? 140.897 140.980 186.403 1.00 36.96  ? 3611 ARG A CA    1 
ATOM   14895 C  C     . ARG A 1 3611 ? 140.590 142.451 186.155 1.00 38.47  ? 3611 ARG A C     1 
ATOM   14896 O  O     . ARG A 1 3611 ? 139.429 142.850 186.033 1.00 37.33  ? 3611 ARG A O     1 
ATOM   14897 C  CB    . ARG A 1 3611 ? 140.865 140.211 185.081 1.00 48.66  ? 3611 ARG A CB    1 
ATOM   14898 C  CG    . ARG A 1 3611 ? 141.706 140.828 183.976 1.00 51.11  ? 3611 ARG A CG    1 
ATOM   14899 C  CD    . ARG A 1 3611 ? 143.127 140.294 184.004 1.00 53.12  ? 3611 ARG A CD    1 
ATOM   14900 N  NE    . ARG A 1 3611 ? 143.166 138.838 184.009 1.00 51.98  ? 3611 ARG A NE    1 
ATOM   14901 C  CZ    . ARG A 1 3611 ? 143.558 138.095 182.983 1.00 60.58  ? 3611 ARG A CZ    1 
ATOM   14902 N  NH1   . ARG A 1 3611 ? 143.962 138.642 181.849 1.00 62.69  ? 3611 ARG A NH1   1 
ATOM   14903 N  NH2   . ARG A 1 3611 ? 143.545 136.770 183.099 1.00 59.43  ? 3611 ARG A NH2   1 
ATOM   14904 N  N     . THR A 1 3612 ? 141.644 143.258 186.084 1.00 39.41  ? 3612 THR A N     1 
ATOM   14905 C  CA    . THR A 1 3612 ? 141.518 144.686 185.840 1.00 34.71  ? 3612 THR A CA    1 
ATOM   14906 C  C     . THR A 1 3612 ? 142.803 145.149 185.165 1.00 34.78  ? 3612 THR A C     1 
ATOM   14907 O  O     . THR A 1 3612 ? 143.833 144.475 185.225 1.00 46.00  ? 3612 THR A O     1 
ATOM   14908 C  CB    . THR A 1 3612 ? 141.237 145.438 187.152 1.00 42.55  ? 3612 THR A CB    1 
ATOM   14909 O  OG1   . THR A 1 3612 ? 140.030 144.935 187.736 1.00 53.29  ? 3612 THR A OG1   1 
ATOM   14910 C  CG2   . THR A 1 3612 ? 141.054 146.928 186.919 1.00 40.28  ? 3612 THR A CG2   1 
ATOM   14911 N  N     . SER A 1 3613 ? 142.728 146.288 184.481 1.00 34.09  ? 3613 SER A N     1 
ATOM   14912 C  CA    . SER A 1 3613 ? 143.902 146.912 183.891 1.00 36.83  ? 3613 SER A CA    1 
ATOM   14913 C  C     . SER A 1 3613 ? 143.868 148.405 184.182 1.00 42.42  ? 3613 SER A C     1 
ATOM   14914 O  O     . SER A 1 3613 ? 142.795 149.001 184.302 1.00 48.14  ? 3613 SER A O     1 
ATOM   14915 C  CB    . SER A 1 3613 ? 143.974 146.669 182.379 1.00 40.89  ? 3613 SER A CB    1 
ATOM   14916 O  OG    . SER A 1 3613 ? 145.055 147.378 181.801 1.00 42.50  ? 3613 SER A OG    1 
ATOM   14917 N  N     . PHE A 1 3614 ? 145.057 149.003 184.302 1.00 45.67  ? 3614 PHE A N     1 
ATOM   14918 C  CA    . PHE A 1 3614 ? 145.132 150.447 184.503 1.00 41.42  ? 3614 PHE A CA    1 
ATOM   14919 C  C     . PHE A 1 3614 ? 144.504 151.205 183.341 1.00 46.35  ? 3614 PHE A C     1 
ATOM   14920 O  O     . PHE A 1 3614 ? 143.917 152.274 183.541 1.00 51.66  ? 3614 PHE A O     1 
ATOM   14921 C  CB    . PHE A 1 3614 ? 146.586 150.890 184.688 1.00 43.38  ? 3614 PHE A CB    1 
ATOM   14922 C  CG    . PHE A 1 3614 ? 147.111 150.706 186.084 1.00 42.18  ? 3614 PHE A CG    1 
ATOM   14923 C  CD1   . PHE A 1 3614 ? 146.679 151.522 187.114 1.00 42.36  ? 3614 PHE A CD1   1 
ATOM   14924 C  CD2   . PHE A 1 3614 ? 148.076 149.754 186.356 1.00 35.28  ? 3614 PHE A CD2   1 
ATOM   14925 C  CE1   . PHE A 1 3614 ? 147.170 151.360 188.394 1.00 36.66  ? 3614 PHE A CE1   1 
ATOM   14926 C  CE2   . PHE A 1 3614 ? 148.568 149.589 187.631 1.00 33.37  ? 3614 PHE A CE2   1 
ATOM   14927 C  CZ    . PHE A 1 3614 ? 148.116 150.393 188.650 1.00 35.70  ? 3614 PHE A CZ    1 
ATOM   14928 N  N     . LEU A 1 3615 ? 144.617 150.671 182.123 1.00 44.71  ? 3615 LEU A N     1 
ATOM   14929 C  CA    . LEU A 1 3615 ? 144.020 151.317 180.961 1.00 46.42  ? 3615 LEU A CA    1 
ATOM   14930 C  C     . LEU A 1 3615 ? 142.500 151.223 180.959 1.00 52.77  ? 3615 LEU A C     1 
ATOM   14931 O  O     . LEU A 1 3615 ? 141.844 152.022 180.282 1.00 61.38  ? 3615 LEU A O     1 
ATOM   14932 C  CB    . LEU A 1 3615 ? 144.581 150.706 179.678 1.00 48.43  ? 3615 LEU A CB    1 
ATOM   14933 C  CG    . LEU A 1 3615 ? 146.096 150.810 179.500 1.00 48.63  ? 3615 LEU A CG    1 
ATOM   14934 C  CD1   . LEU A 1 3615 ? 146.523 150.223 178.166 1.00 42.09  ? 3615 LEU A CD1   1 
ATOM   14935 C  CD2   . LEU A 1 3615 ? 146.535 152.258 179.612 1.00 46.89  ? 3615 LEU A CD2   1 
ATOM   14936 N  N     . ASP A 1 3616 ? 141.929 150.269 181.690 1.00 49.95  ? 3616 ASP A N     1 
ATOM   14937 C  CA    . ASP A 1 3616 ? 140.480 150.140 181.747 1.00 55.05  ? 3616 ASP A CA    1 
ATOM   14938 C  C     . ASP A 1 3616 ? 139.863 151.356 182.426 1.00 60.66  ? 3616 ASP A C     1 
ATOM   14939 O  O     . ASP A 1 3616 ? 140.360 151.839 183.447 1.00 64.40  ? 3616 ASP A O     1 
ATOM   14940 C  CB    . ASP A 1 3616 ? 140.091 148.867 182.500 1.00 48.05  ? 3616 ASP A CB    1 
ATOM   14941 C  CG    . ASP A 1 3616 ? 140.159 147.632 181.627 1.00 54.34  ? 3616 ASP A CG    1 
ATOM   14942 O  OD1   . ASP A 1 3616 ? 140.563 147.754 180.452 1.00 62.24  ? 3616 ASP A OD1   1 
ATOM   14943 O  OD2   . ASP A 1 3616 ? 139.811 146.538 182.118 1.00 49.81  ? 3616 ASP A OD2   1 
ATOM   14944 N  N     . ASP A 1 3617 ? 138.767 151.852 181.848 1.00 57.56  ? 3617 ASP A N     1 
ATOM   14945 C  CA    . ASP A 1 3617 ? 138.076 152.993 182.438 1.00 62.26  ? 3617 ASP A CA    1 
ATOM   14946 C  C     . ASP A 1 3617 ? 137.386 152.617 183.742 1.00 63.08  ? 3617 ASP A C     1 
ATOM   14947 O  O     . ASP A 1 3617 ? 137.081 153.496 184.556 1.00 69.94  ? 3617 ASP A O     1 
ATOM   14948 C  CB    . ASP A 1 3617 ? 137.063 153.565 181.447 1.00 71.69  ? 3617 ASP A CB    1 
ATOM   14949 C  CG    . ASP A 1 3617 ? 136.172 152.499 180.843 1.00 78.69  ? 3617 ASP A CG    1 
ATOM   14950 O  OD1   . ASP A 1 3617 ? 136.432 151.300 181.080 1.00 79.78  ? 3617 ASP A OD1   1 
ATOM   14951 O  OD2   . ASP A 1 3617 ? 135.210 152.859 180.132 1.00 79.01  ? 3617 ASP A OD2   1 
ATOM   14952 N  N     . ALA A 1 3618 ? 137.132 151.329 183.958 1.00 57.62  ? 3618 ALA A N     1 
ATOM   14953 C  CA    . ALA A 1 3618 ? 136.468 150.860 185.166 1.00 56.79  ? 3618 ALA A CA    1 
ATOM   14954 C  C     . ALA A 1 3618 ? 137.440 150.504 186.281 1.00 52.76  ? 3618 ALA A C     1 
ATOM   14955 O  O     . ALA A 1 3618 ? 137.001 150.006 187.323 1.00 51.86  ? 3618 ALA A O     1 
ATOM   14956 C  CB    . ALA A 1 3618 ? 135.590 149.648 184.845 1.00 46.55  ? 3618 ALA A CB    1 
ATOM   14957 N  N     . PHE A 1 3619 ? 138.739 150.753 186.093 1.00 53.48  ? 3619 PHE A N     1 
ATOM   14958 C  CA    . PHE A 1 3619 ? 139.731 150.335 187.079 1.00 52.75  ? 3619 PHE A CA    1 
ATOM   14959 C  C     . PHE A 1 3619 ? 139.495 151.005 188.426 1.00 51.06  ? 3619 PHE A C     1 
ATOM   14960 O  O     . PHE A 1 3619 ? 139.665 150.376 189.477 1.00 45.26  ? 3619 PHE A O     1 
ATOM   14961 C  CB    . PHE A 1 3619 ? 141.138 150.637 186.565 1.00 44.60  ? 3619 PHE A CB    1 
ATOM   14962 C  CG    . PHE A 1 3619 ? 142.150 150.850 187.654 1.00 44.21  ? 3619 PHE A CG    1 
ATOM   14963 C  CD1   . PHE A 1 3619 ? 142.563 149.795 188.451 1.00 43.82  ? 3619 PHE A CD1   1 
ATOM   14964 C  CD2   . PHE A 1 3619 ? 142.690 152.104 187.879 1.00 40.50  ? 3619 PHE A CD2   1 
ATOM   14965 C  CE1   . PHE A 1 3619 ? 143.492 149.988 189.453 1.00 41.16  ? 3619 PHE A CE1   1 
ATOM   14966 C  CE2   . PHE A 1 3619 ? 143.620 152.302 188.879 1.00 43.34  ? 3619 PHE A CE2   1 
ATOM   14967 C  CZ    . PHE A 1 3619 ? 144.020 151.241 189.667 1.00 41.25  ? 3619 PHE A CZ    1 
ATOM   14968 N  N     . ARG A 1 3620 ? 139.110 152.283 188.416 1.00 55.19  ? 3620 ARG A N     1 
ATOM   14969 C  CA    . ARG A 1 3620 ? 138.852 152.985 189.669 1.00 49.24  ? 3620 ARG A CA    1 
ATOM   14970 C  C     . ARG A 1 3620 ? 137.732 152.316 190.456 1.00 47.56  ? 3620 ARG A C     1 
ATOM   14971 O  O     . ARG A 1 3620 ? 137.854 152.106 191.668 1.00 47.32  ? 3620 ARG A O     1 
ATOM   14972 C  CB    . ARG A 1 3620 ? 138.512 154.447 189.385 1.00 52.41  ? 3620 ARG A CB    1 
ATOM   14973 C  CG    . ARG A 1 3620 ? 139.632 155.226 188.712 1.00 53.46  ? 3620 ARG A CG    1 
ATOM   14974 C  CD    . ARG A 1 3620 ? 140.622 155.849 189.702 1.00 54.53  ? 3620 ARG A CD    1 
ATOM   14975 N  NE    . ARG A 1 3620 ? 139.990 156.666 190.733 1.00 56.99  ? 3620 ARG A NE    1 
ATOM   14976 C  CZ    . ARG A 1 3620 ? 139.598 156.222 191.921 1.00 58.28  ? 3620 ARG A CZ    1 
ATOM   14977 N  NH1   . ARG A 1 3620 ? 139.779 154.963 192.284 1.00 56.97  ? 3620 ARG A NH1   1 
ATOM   14978 N  NH2   . ARG A 1 3620 ? 139.016 157.066 192.769 1.00 52.79  ? 3620 ARG A NH2   1 
ATOM   14979 N  N     . LYS A 1 3621 ? 136.641 151.955 189.779 1.00 51.64  ? 3621 LYS A N     1 
ATOM   14980 C  CA    . LYS A 1 3621 ? 135.517 151.329 190.467 1.00 48.77  ? 3621 LYS A CA    1 
ATOM   14981 C  C     . LYS A 1 3621 ? 135.855 149.923 190.946 1.00 41.40  ? 3621 LYS A C     1 
ATOM   14982 O  O     . LYS A 1 3621 ? 135.453 149.532 192.048 1.00 43.42  ? 3621 LYS A O     1 
ATOM   14983 C  CB    . LYS A 1 3621 ? 134.289 151.306 189.556 1.00 55.71  ? 3621 LYS A CB    1 
ATOM   14984 C  CG    . LYS A 1 3621 ? 133.747 152.689 189.212 1.00 58.81  ? 3621 LYS A CG    1 
ATOM   14985 C  CD    . LYS A 1 3621 ? 133.165 153.406 190.429 1.00 64.49  ? 3621 LYS A CD    1 
ATOM   14986 C  CE    . LYS A 1 3621 ? 132.328 152.482 191.305 1.00 70.89  ? 3621 LYS A CE    1 
ATOM   14987 N  NZ    . LYS A 1 3621 ? 131.556 153.239 192.330 1.00 70.19  ? 3621 LYS A NZ    1 
ATOM   14988 N  N     . ASN A 1 3622 ? 136.586 149.149 190.139 1.00 43.72  ? 3622 ASN A N     1 
ATOM   14989 C  CA    . ASN A 1 3622 ? 137.008 147.824 190.583 1.00 44.50  ? 3622 ASN A CA    1 
ATOM   14990 C  C     . ASN A 1 3622 ? 137.906 147.917 191.809 1.00 45.50  ? 3622 ASN A C     1 
ATOM   14991 O  O     . ASN A 1 3622 ? 137.755 147.140 192.759 1.00 44.58  ? 3622 ASN A O     1 
ATOM   14992 C  CB    . ASN A 1 3622 ? 137.721 147.077 189.455 1.00 42.53  ? 3622 ASN A CB    1 
ATOM   14993 C  CG    . ASN A 1 3622 ? 136.816 146.800 188.272 1.00 49.07  ? 3622 ASN A CG    1 
ATOM   14994 O  OD1   . ASN A 1 3622 ? 137.026 147.321 187.178 1.00 55.21  ? 3622 ASN A OD1   1 
ATOM   14995 N  ND2   . ASN A 1 3622 ? 135.798 145.976 188.488 1.00 42.21  ? 3622 ASN A ND2   1 
ATOM   14996 N  N     . LEU A 1 3623 ? 138.842 148.868 191.809 1.00 44.97  ? 3623 LEU A N     1 
ATOM   14997 C  CA    . LEU A 1 3623 ? 139.722 149.048 192.959 1.00 38.52  ? 3623 LEU A CA    1 
ATOM   14998 C  C     . LEU A 1 3623 ? 138.933 149.473 194.192 1.00 38.34  ? 3623 LEU A C     1 
ATOM   14999 O  O     . LEU A 1 3623 ? 139.171 148.975 195.299 1.00 40.51  ? 3623 LEU A O     1 
ATOM   15000 C  CB    . LEU A 1 3623 ? 140.808 150.070 192.623 1.00 35.24  ? 3623 LEU A CB    1 
ATOM   15001 C  CG    . LEU A 1 3623 ? 141.588 150.685 193.783 1.00 35.58  ? 3623 LEU A CG    1 
ATOM   15002 C  CD1   . LEU A 1 3623 ? 142.587 149.687 194.340 1.00 36.93  ? 3623 LEU A CD1   1 
ATOM   15003 C  CD2   . LEU A 1 3623 ? 142.292 151.952 193.330 1.00 31.97  ? 3623 LEU A CD2   1 
ATOM   15004 N  N     . GLU A 1 3624 ? 137.981 150.393 194.016 1.00 41.01  ? 3624 GLU A N     1 
ATOM   15005 C  CA    . GLU A 1 3624 ? 137.159 150.837 195.137 1.00 45.73  ? 3624 GLU A CA    1 
ATOM   15006 C  C     . GLU A 1 3624 ? 136.359 149.682 195.724 1.00 44.17  ? 3624 GLU A C     1 
ATOM   15007 O  O     . GLU A 1 3624 ? 136.289 149.517 196.948 1.00 41.97  ? 3624 GLU A O     1 
ATOM   15008 C  CB    . GLU A 1 3624 ? 136.228 151.964 194.687 1.00 43.04  ? 3624 GLU A CB    1 
ATOM   15009 C  CG    . GLU A 1 3624 ? 135.380 152.554 195.801 1.00 54.88  ? 3624 GLU A CG    1 
ATOM   15010 C  CD    . GLU A 1 3624 ? 134.508 153.701 195.326 1.00 65.25  ? 3624 GLU A CD    1 
ATOM   15011 O  OE1   . GLU A 1 3624 ? 134.550 154.022 194.120 1.00 68.47  ? 3624 GLU A OE1   1 
ATOM   15012 O  OE2   . GLU A 1 3624 ? 133.777 154.279 196.158 1.00 60.77  ? 3624 GLU A OE2   1 
ATOM   15013 N  N     . SER A 1 3625 ? 135.747 148.867 194.861 1.00 41.29  ? 3625 SER A N     1 
ATOM   15014 C  CA    . SER A 1 3625 ? 134.976 147.725 195.339 1.00 40.28  ? 3625 SER A CA    1 
ATOM   15015 C  C     . SER A 1 3625 ? 135.871 146.711 196.038 1.00 45.00  ? 3625 SER A C     1 
ATOM   15016 O  O     . SER A 1 3625 ? 135.487 146.136 197.063 1.00 44.70  ? 3625 SER A O     1 
ATOM   15017 C  CB    . SER A 1 3625 ? 134.229 147.071 194.178 1.00 40.86  ? 3625 SER A CB    1 
ATOM   15018 O  OG    . SER A 1 3625 ? 135.056 146.972 193.034 1.00 41.96  ? 3625 SER A OG    1 
ATOM   15019 N  N     . ALA A 1 3626 ? 137.067 146.472 195.493 1.00 44.96  ? 3626 ALA A N     1 
ATOM   15020 C  CA    . ALA A 1 3626 ? 137.994 145.539 196.121 1.00 34.06  ? 3626 ALA A CA    1 
ATOM   15021 C  C     . ALA A 1 3626 ? 138.418 146.016 197.502 1.00 31.67  ? 3626 ALA A C     1 
ATOM   15022 O  O     . ALA A 1 3626 ? 138.512 145.209 198.433 1.00 32.98  ? 3626 ALA A O     1 
ATOM   15023 C  CB    . ALA A 1 3626 ? 139.217 145.333 195.229 1.00 35.54  ? 3626 ALA A CB    1 
ATOM   15024 N  N     . LEU A 1 3627 ? 138.681 147.314 197.656 1.00 36.03  ? 3627 LEU A N     1 
ATOM   15025 C  CA    . LEU A 1 3627 ? 139.040 147.830 198.973 1.00 33.59  ? 3627 LEU A CA    1 
ATOM   15026 C  C     . LEU A 1 3627 ? 137.863 147.774 199.940 1.00 40.73  ? 3627 LEU A C     1 
ATOM   15027 O  O     . LEU A 1 3627 ? 138.043 147.437 201.115 1.00 47.31  ? 3627 LEU A O     1 
ATOM   15028 C  CB    . LEU A 1 3627 ? 139.564 149.262 198.866 1.00 34.38  ? 3627 LEU A CB    1 
ATOM   15029 C  CG    . LEU A 1 3627 ? 140.816 149.489 198.020 1.00 32.32  ? 3627 LEU A CG    1 
ATOM   15030 C  CD1   . LEU A 1 3627 ? 140.732 150.833 197.333 1.00 33.78  ? 3627 LEU A CD1   1 
ATOM   15031 C  CD2   . LEU A 1 3627 ? 142.070 149.398 198.863 1.00 27.63  ? 3627 LEU A CD2   1 
ATOM   15032 N  N     . ARG A 1 3628 ? 136.656 148.101 199.470 1.00 43.55  ? 3628 ARG A N     1 
ATOM   15033 C  CA    . ARG A 1 3628 ? 135.501 148.130 200.363 1.00 37.60  ? 3628 ARG A CA    1 
ATOM   15034 C  C     . ARG A 1 3628 ? 135.123 146.730 200.831 1.00 43.02  ? 3628 ARG A C     1 
ATOM   15035 O  O     . ARG A 1 3628 ? 134.889 146.507 202.025 1.00 44.02  ? 3628 ARG A O     1 
ATOM   15036 C  CB    . ARG A 1 3628 ? 134.315 148.802 199.669 1.00 42.90  ? 3628 ARG A CB    1 
ATOM   15037 C  CG    . ARG A 1 3628 ? 134.432 150.311 199.571 1.00 51.84  ? 3628 ARG A CG    1 
ATOM   15038 C  CD    . ARG A 1 3628 ? 133.084 150.977 199.355 1.00 47.80  ? 3628 ARG A CD    1 
ATOM   15039 N  NE    . ARG A 1 3628 ? 133.229 152.314 198.792 1.00 58.03  ? 3628 ARG A NE    1 
ATOM   15040 C  CZ    . ARG A 1 3628 ? 133.368 153.421 199.510 1.00 67.03  ? 3628 ARG A CZ    1 
ATOM   15041 N  NH1   . ARG A 1 3628 ? 133.392 153.389 200.832 1.00 60.57  ? 3628 ARG A NH1   1 
ATOM   15042 N  NH2   . ARG A 1 3628 ? 133.488 154.588 198.885 1.00 65.27  ? 3628 ARG A NH2   1 
ATOM   15043 N  N     . PHE A 1 3629 ? 135.059 145.774 199.909 1.00 42.21  ? 3629 PHE A N     1 
ATOM   15044 C  CA    . PHE A 1 3629 ? 134.614 144.424 200.229 1.00 38.76  ? 3629 PHE A CA    1 
ATOM   15045 C  C     . PHE A 1 3629 ? 135.760 143.476 200.550 1.00 39.73  ? 3629 PHE A C     1 
ATOM   15046 O  O     . PHE A 1 3629 ? 135.508 142.298 200.824 1.00 45.30  ? 3629 PHE A O     1 
ATOM   15047 C  CB    . PHE A 1 3629 ? 133.783 143.850 199.074 1.00 46.29  ? 3629 PHE A CB    1 
ATOM   15048 C  CG    . PHE A 1 3629 ? 132.708 144.776 198.574 1.00 49.25  ? 3629 PHE A CG    1 
ATOM   15049 C  CD1   . PHE A 1 3629 ? 132.059 145.646 199.437 1.00 44.23  ? 3629 PHE A CD1   1 
ATOM   15050 C  CD2   . PHE A 1 3629 ? 132.348 144.778 197.236 1.00 51.14  ? 3629 PHE A CD2   1 
ATOM   15051 C  CE1   . PHE A 1 3629 ? 131.076 146.496 198.976 1.00 48.96  ? 3629 PHE A CE1   1 
ATOM   15052 C  CE2   . PHE A 1 3629 ? 131.364 145.626 196.770 1.00 51.79  ? 3629 PHE A CE2   1 
ATOM   15053 C  CZ    . PHE A 1 3629 ? 130.727 146.486 197.641 1.00 56.81  ? 3629 PHE A CZ    1 
ATOM   15054 N  N     . GLY A 1 3630 ? 137.000 143.952 200.530 1.00 36.09  ? 3630 GLY A N     1 
ATOM   15055 C  CA    . GLY A 1 3630 ? 138.135 143.095 200.824 1.00 36.07  ? 3630 GLY A CA    1 
ATOM   15056 C  C     . GLY A 1 3630 ? 138.345 141.981 199.823 1.00 37.80  ? 3630 GLY A C     1 
ATOM   15057 O  O     . GLY A 1 3630 ? 138.611 140.839 200.219 1.00 43.47  ? 3630 GLY A O     1 
ATOM   15058 N  N     . ASN A 1 3631 ? 138.231 142.281 198.534 1.00 32.64  ? 3631 ASN A N     1 
ATOM   15059 C  CA    . ASN A 1 3631 ? 138.397 141.208 197.566 1.00 34.28  ? 3631 ASN A CA    1 
ATOM   15060 C  C     . ASN A 1 3631 ? 139.746 141.316 196.867 1.00 39.58  ? 3631 ASN A C     1 
ATOM   15061 O  O     . ASN A 1 3631 ? 140.224 142.426 196.610 1.00 34.67  ? 3631 ASN A O     1 
ATOM   15062 C  CB    . ASN A 1 3631 ? 137.282 141.249 196.521 1.00 39.91  ? 3631 ASN A CB    1 
ATOM   15063 C  CG    . ASN A 1 3631 ? 135.905 141.116 197.135 1.00 40.42  ? 3631 ASN A CG    1 
ATOM   15064 O  OD1   . ASN A 1 3631 ? 135.723 140.429 198.138 1.00 41.50  ? 3631 ASN A OD1   1 
ATOM   15065 N  ND2   . ASN A 1 3631 ? 134.924 141.776 196.532 1.00 39.30  ? 3631 ASN A ND2   1 
ATOM   15066 N  N     . PRO A 1 3632 ? 140.378 140.183 196.564 1.00 41.57  ? 3632 PRO A N     1 
ATOM   15067 C  CA    . PRO A 1 3632 ? 141.638 140.223 195.814 1.00 30.03  ? 3632 PRO A CA    1 
ATOM   15068 C  C     . PRO A 1 3632 ? 141.446 140.857 194.445 1.00 31.15  ? 3632 PRO A C     1 
ATOM   15069 O  O     . PRO A 1 3632 ? 140.421 140.664 193.788 1.00 37.43  ? 3632 PRO A O     1 
ATOM   15070 C  CB    . PRO A 1 3632 ? 142.029 138.746 195.702 1.00 36.35  ? 3632 PRO A CB    1 
ATOM   15071 C  CG    . PRO A 1 3632 ? 141.351 138.094 196.857 1.00 39.34  ? 3632 PRO A CG    1 
ATOM   15072 C  CD    . PRO A 1 3632 ? 140.048 138.821 197.016 1.00 40.89  ? 3632 PRO A CD    1 
ATOM   15073 N  N     . LEU A 1 3633 ? 142.448 141.620 194.019 1.00 30.98  ? 3633 LEU A N     1 
ATOM   15074 C  CA    . LEU A 1 3633 ? 142.407 142.339 192.755 1.00 27.10  ? 3633 LEU A CA    1 
ATOM   15075 C  C     . LEU A 1 3633 ? 143.736 142.175 192.034 1.00 26.06  ? 3633 LEU A C     1 
ATOM   15076 O  O     . LEU A 1 3633 ? 144.800 142.230 192.656 1.00 28.40  ? 3633 LEU A O     1 
ATOM   15077 C  CB    . LEU A 1 3633 ? 142.104 143.826 192.980 1.00 23.23  ? 3633 LEU A CB    1 
ATOM   15078 C  CG    . LEU A 1 3633 ? 142.194 144.765 191.777 1.00 33.01  ? 3633 LEU A CG    1 
ATOM   15079 C  CD1   . LEU A 1 3633 ? 141.060 144.501 190.802 1.00 30.58  ? 3633 LEU A CD1   1 
ATOM   15080 C  CD2   . LEU A 1 3633 ? 142.188 146.216 192.230 1.00 29.03  ? 3633 LEU A CD2   1 
ATOM   15081 N  N     . LEU A 1 3634 ? 143.671 141.967 190.722 1.00 23.28  ? 3634 LEU A N     1 
ATOM   15082 C  CA    . LEU A 1 3634 ? 144.859 141.842 189.886 1.00 21.15  ? 3634 LEU A CA    1 
ATOM   15083 C  C     . LEU A 1 3634 ? 144.763 142.854 188.757 1.00 25.96  ? 3634 LEU A C     1 
ATOM   15084 O  O     . LEU A 1 3634 ? 143.733 142.933 188.080 1.00 37.98  ? 3634 LEU A O     1 
ATOM   15085 C  CB    . LEU A 1 3634 ? 144.999 140.421 189.331 1.00 22.70  ? 3634 LEU A CB    1 
ATOM   15086 C  CG    . LEU A 1 3634 ? 146.029 140.219 188.218 1.00 23.04  ? 3634 LEU A CG    1 
ATOM   15087 C  CD1   . LEU A 1 3634 ? 147.424 140.067 188.794 1.00 20.02  ? 3634 LEU A CD1   1 
ATOM   15088 C  CD2   . LEU A 1 3634 ? 145.671 139.013 187.370 1.00 25.90  ? 3634 LEU A CD2   1 
ATOM   15089 N  N     . VAL A 1 3635 ? 145.828 143.625 188.556 1.00 19.62  ? 3635 VAL A N     1 
ATOM   15090 C  CA    . VAL A 1 3635 ? 145.895 144.627 187.499 1.00 23.80  ? 3635 VAL A CA    1 
ATOM   15091 C  C     . VAL A 1 3635 ? 147.049 144.259 186.577 1.00 29.16  ? 3635 VAL A C     1 
ATOM   15092 O  O     . VAL A 1 3635 ? 148.166 144.009 187.044 1.00 32.21  ? 3635 VAL A O     1 
ATOM   15093 C  CB    . VAL A 1 3635 ? 146.061 146.044 188.071 1.00 28.92  ? 3635 VAL A CB    1 
ATOM   15094 C  CG1   . VAL A 1 3635 ? 146.205 147.039 186.947 1.00 37.60  ? 3635 VAL A CG1   1 
ATOM   15095 C  CG2   . VAL A 1 3635 ? 144.880 146.403 188.956 1.00 25.50  ? 3635 VAL A CG2   1 
ATOM   15096 N  N     . GLN A 1 3636 ? 146.782 144.230 185.270 1.00 29.51  ? 3636 GLN A N     1 
ATOM   15097 C  CA    . GLN A 1 3636 ? 147.653 143.539 184.328 1.00 32.60  ? 3636 GLN A CA    1 
ATOM   15098 C  C     . GLN A 1 3636 ? 148.526 144.451 183.472 1.00 33.54  ? 3636 GLN A C     1 
ATOM   15099 O  O     . GLN A 1 3636 ? 149.362 143.937 182.722 1.00 37.01  ? 3636 GLN A O     1 
ATOM   15100 C  CB    . GLN A 1 3636 ? 146.819 142.642 183.404 1.00 35.21  ? 3636 GLN A CB    1 
ATOM   15101 C  CG    . GLN A 1 3636 ? 145.871 143.397 182.495 1.00 39.91  ? 3636 GLN A CG    1 
ATOM   15102 C  CD    . GLN A 1 3636 ? 145.032 142.475 181.638 1.00 49.98  ? 3636 GLN A CD    1 
ATOM   15103 O  OE1   . GLN A 1 3636 ? 145.191 141.255 181.682 1.00 51.38  ? 3636 GLN A OE1   1 
ATOM   15104 N  NE2   . GLN A 1 3636 ? 144.135 143.053 180.848 1.00 55.40  ? 3636 GLN A NE2   1 
ATOM   15105 N  N     . ASP A 1 3637 ? 148.370 145.775 183.549 1.00 31.84  ? 3637 ASP A N     1 
ATOM   15106 C  CA    . ASP A 1 3637 ? 149.163 146.693 182.722 1.00 35.18  ? 3637 ASP A CA    1 
ATOM   15107 C  C     . ASP A 1 3637 ? 149.765 147.769 183.626 1.00 39.22  ? 3637 ASP A C     1 
ATOM   15108 O  O     . ASP A 1 3637 ? 149.227 148.871 183.741 1.00 45.86  ? 3637 ASP A O     1 
ATOM   15109 C  CB    . ASP A 1 3637 ? 148.307 147.299 181.606 1.00 41.31  ? 3637 ASP A CB    1 
ATOM   15110 C  CG    . ASP A 1 3637 ? 148.031 146.317 180.482 1.00 48.16  ? 3637 ASP A CG    1 
ATOM   15111 O  OD1   . ASP A 1 3637 ? 147.014 145.598 180.555 1.00 46.37  ? 3637 ASP A OD1   1 
ATOM   15112 O  OD2   . ASP A 1 3637 ? 148.827 146.261 179.524 1.00 52.96  ? 3637 ASP A OD2   1 
ATOM   15113 N  N     . VAL A 1 3638 ? 150.911 147.454 184.238 1.00 34.26  ? 3638 VAL A N     1 
ATOM   15114 C  CA    . VAL A 1 3638 ? 151.521 148.348 185.220 1.00 26.65  ? 3638 VAL A CA    1 
ATOM   15115 C  C     . VAL A 1 3638 ? 152.393 149.414 184.567 1.00 35.76  ? 3638 VAL A C     1 
ATOM   15116 O  O     . VAL A 1 3638 ? 152.761 150.396 185.230 1.00 41.23  ? 3638 VAL A O     1 
ATOM   15117 C  CB    . VAL A 1 3638 ? 152.336 147.525 186.242 1.00 22.08  ? 3638 VAL A CB    1 
ATOM   15118 C  CG1   . VAL A 1 3638 ? 153.511 146.848 185.567 1.00 22.73  ? 3638 VAL A CG1   1 
ATOM   15119 C  CG2   . VAL A 1 3638 ? 152.768 148.366 187.442 1.00 28.30  ? 3638 VAL A CG2   1 
ATOM   15120 N  N     . GLU A 1 3639 ? 152.714 149.269 183.279 1.00 37.54  ? 3639 GLU A N     1 
ATOM   15121 C  CA    . GLU A 1 3639 ? 153.450 150.293 182.547 1.00 33.67  ? 3639 GLU A CA    1 
ATOM   15122 C  C     . GLU A 1 3639 ? 152.719 151.628 182.527 1.00 34.04  ? 3639 GLU A C     1 
ATOM   15123 O  O     . GLU A 1 3639 ? 153.357 152.665 182.313 1.00 45.73  ? 3639 GLU A O     1 
ATOM   15124 C  CB    . GLU A 1 3639 ? 153.698 149.829 181.112 1.00 36.13  ? 3639 GLU A CB    1 
ATOM   15125 C  CG    . GLU A 1 3639 ? 152.429 149.768 180.282 1.00 45.94  ? 3639 GLU A CG    1 
ATOM   15126 C  CD    . GLU A 1 3639 ? 151.676 148.467 180.454 1.00 49.94  ? 3639 GLU A CD    1 
ATOM   15127 O  OE1   . GLU A 1 3639 ? 151.960 147.732 181.423 1.00 49.67  ? 3639 GLU A OE1   1 
ATOM   15128 O  OE2   . GLU A 1 3639 ? 150.778 148.193 179.636 1.00 50.98  ? 3639 GLU A OE2   1 
ATOM   15129 N  N     . SER A 1 3640 ? 151.407 151.621 182.743 1.00 30.14  ? 3640 SER A N     1 
ATOM   15130 C  CA    . SER A 1 3640 ? 150.591 152.823 182.848 1.00 36.57  ? 3640 SER A CA    1 
ATOM   15131 C  C     . SER A 1 3640 ? 150.056 152.971 184.268 1.00 36.21  ? 3640 SER A C     1 
ATOM   15132 O  O     . SER A 1 3640 ? 148.875 153.248 184.484 1.00 37.96  ? 3640 SER A O     1 
ATOM   15133 C  CB    . SER A 1 3640 ? 149.448 152.794 181.839 1.00 46.75  ? 3640 SER A CB    1 
ATOM   15134 O  OG    . SER A 1 3640 ? 148.478 151.826 182.199 1.00 47.50  ? 3640 SER A OG    1 
ATOM   15135 N  N     . TYR A 1 3641 ? 150.934 152.754 185.246 1.00 35.96  ? 3641 TYR A N     1 
ATOM   15136 C  CA    . TYR A 1 3641 ? 150.554 152.798 186.651 1.00 33.70  ? 3641 TYR A CA    1 
ATOM   15137 C  C     . TYR A 1 3641 ? 149.912 154.133 187.001 1.00 34.12  ? 3641 TYR A C     1 
ATOM   15138 O  O     . TYR A 1 3641 ? 150.459 155.199 186.704 1.00 38.11  ? 3641 TYR A O     1 
ATOM   15139 C  CB    . TYR A 1 3641 ? 151.787 152.556 187.521 1.00 30.15  ? 3641 TYR A CB    1 
ATOM   15140 C  CG    . TYR A 1 3641 ? 151.603 152.880 188.985 1.00 28.32  ? 3641 TYR A CG    1 
ATOM   15141 C  CD1   . TYR A 1 3641 ? 150.879 152.040 189.817 1.00 26.92  ? 3641 TYR A CD1   1 
ATOM   15142 C  CD2   . TYR A 1 3641 ? 152.167 154.022 189.538 1.00 25.53  ? 3641 TYR A CD2   1 
ATOM   15143 C  CE1   . TYR A 1 3641 ? 150.714 152.331 191.155 1.00 29.87  ? 3641 TYR A CE1   1 
ATOM   15144 C  CE2   . TYR A 1 3641 ? 152.007 154.322 190.874 1.00 23.56  ? 3641 TYR A CE2   1 
ATOM   15145 C  CZ    . TYR A 1 3641 ? 151.281 153.474 191.678 1.00 26.76  ? 3641 TYR A CZ    1 
ATOM   15146 O  OH    . TYR A 1 3641 ? 151.118 153.767 193.011 1.00 27.75  ? 3641 TYR A OH    1 
ATOM   15147 N  N     . ASP A 1 3642 ? 148.744 154.069 187.635 1.00 32.61  ? 3642 ASP A N     1 
ATOM   15148 C  CA    . ASP A 1 3642 ? 148.022 155.267 188.032 1.00 33.71  ? 3642 ASP A CA    1 
ATOM   15149 C  C     . ASP A 1 3642 ? 148.404 155.622 189.462 1.00 34.17  ? 3642 ASP A C     1 
ATOM   15150 O  O     . ASP A 1 3642 ? 148.321 154.757 190.343 1.00 34.85  ? 3642 ASP A O     1 
ATOM   15151 C  CB    . ASP A 1 3642 ? 146.521 155.050 187.926 1.00 38.26  ? 3642 ASP A CB    1 
ATOM   15152 C  CG    . ASP A 1 3642 ? 145.728 156.339 188.064 1.00 46.85  ? 3642 ASP A CG    1 
ATOM   15153 O  OD1   . ASP A 1 3642 ? 145.022 156.702 187.100 1.00 47.37  ? 3642 ASP A OD1   1 
ATOM   15154 O  OD2   . ASP A 1 3642 ? 145.814 156.998 189.121 1.00 43.86  ? 3642 ASP A OD2   1 
ATOM   15155 N  N     . PRO A 1 3643 ? 148.829 156.858 189.739 1.00 33.29  ? 3643 PRO A N     1 
ATOM   15156 C  CA    . PRO A 1 3643 ? 149.273 157.200 191.101 1.00 26.61  ? 3643 PRO A CA    1 
ATOM   15157 C  C     . PRO A 1 3643 ? 148.183 157.103 192.161 1.00 25.85  ? 3643 PRO A C     1 
ATOM   15158 O  O     . PRO A 1 3643 ? 148.488 157.297 193.344 1.00 25.10  ? 3643 PRO A O     1 
ATOM   15159 C  CB    . PRO A 1 3643 ? 149.776 158.643 190.956 1.00 26.89  ? 3643 PRO A CB    1 
ATOM   15160 C  CG    . PRO A 1 3643 ? 150.066 158.803 189.496 1.00 33.64  ? 3643 PRO A CG    1 
ATOM   15161 C  CD    . PRO A 1 3643 ? 149.043 157.966 188.795 1.00 36.26  ? 3643 PRO A CD    1 
ATOM   15162 N  N     . VAL A 1 3644 ? 146.936 156.799 191.785 1.00 27.13  ? 3644 VAL A N     1 
ATOM   15163 C  CA    . VAL A 1 3644 ? 145.867 156.664 192.768 1.00 30.49  ? 3644 VAL A CA    1 
ATOM   15164 C  C     . VAL A 1 3644 ? 146.182 155.562 193.768 1.00 28.79  ? 3644 VAL A C     1 
ATOM   15165 O  O     . VAL A 1 3644 ? 145.706 155.600 194.907 1.00 29.38  ? 3644 VAL A O     1 
ATOM   15166 C  CB    . VAL A 1 3644 ? 144.516 156.404 192.061 1.00 34.80  ? 3644 VAL A CB    1 
ATOM   15167 C  CG1   . VAL A 1 3644 ? 144.558 155.097 191.279 1.00 38.39  ? 3644 VAL A CG1   1 
ATOM   15168 C  CG2   . VAL A 1 3644 ? 143.360 156.416 193.054 1.00 34.73  ? 3644 VAL A CG2   1 
ATOM   15169 N  N     . LEU A 1 3645 ? 147.000 154.591 193.377 1.00 30.17  ? 3645 LEU A N     1 
ATOM   15170 C  CA    . LEU A 1 3645 ? 147.384 153.486 194.241 1.00 25.22  ? 3645 LEU A CA    1 
ATOM   15171 C  C     . LEU A 1 3645 ? 148.504 153.844 195.207 1.00 21.99  ? 3645 LEU A C     1 
ATOM   15172 O  O     . LEU A 1 3645 ? 148.879 153.001 196.029 1.00 20.72  ? 3645 LEU A O     1 
ATOM   15173 C  CB    . LEU A 1 3645 ? 147.808 152.285 193.392 1.00 26.49  ? 3645 LEU A CB    1 
ATOM   15174 C  CG    . LEU A 1 3645 ? 146.703 151.312 192.986 1.00 29.00  ? 3645 LEU A CG    1 
ATOM   15175 C  CD1   . LEU A 1 3645 ? 147.253 150.254 192.050 1.00 27.91  ? 3645 LEU A CD1   1 
ATOM   15176 C  CD2   . LEU A 1 3645 ? 146.077 150.674 194.210 1.00 24.49  ? 3645 LEU A CD2   1 
ATOM   15177 N  N     . ASN A 1 3646 ? 149.052 155.059 195.127 1.00 22.47  ? 3646 ASN A N     1 
ATOM   15178 C  CA    . ASN A 1 3646 ? 150.160 155.426 196.009 1.00 20.43  ? 3646 ASN A CA    1 
ATOM   15179 C  C     . ASN A 1 3646 ? 149.806 155.308 197.486 1.00 23.71  ? 3646 ASN A C     1 
ATOM   15180 O  O     . ASN A 1 3646 ? 150.593 154.705 198.236 1.00 28.09  ? 3646 ASN A O     1 
ATOM   15181 C  CB    . ASN A 1 3646 ? 150.659 156.834 195.663 1.00 18.26  ? 3646 ASN A CB    1 
ATOM   15182 C  CG    . ASN A 1 3646 ? 151.438 156.875 194.367 1.00 18.17  ? 3646 ASN A CG    1 
ATOM   15183 O  OD1   . ASN A 1 3646 ? 151.590 155.860 193.689 1.00 26.08  ? 3646 ASN A OD1   1 
ATOM   15184 N  ND2   . ASN A 1 3646 ? 151.942 158.052 194.017 1.00 16.69  ? 3646 ASN A ND2   1 
ATOM   15185 N  N     . PRO A 1 3647 ? 148.682 155.844 197.978 1.00 22.13  ? 3647 PRO A N     1 
ATOM   15186 C  CA    . PRO A 1 3647 ? 148.323 155.577 199.381 1.00 20.92  ? 3647 PRO A CA    1 
ATOM   15187 C  C     . PRO A 1 3647 ? 148.073 154.108 199.668 1.00 22.98  ? 3647 PRO A C     1 
ATOM   15188 O  O     . PRO A 1 3647 ? 148.351 153.648 200.782 1.00 24.40  ? 3647 PRO A O     1 
ATOM   15189 C  CB    . PRO A 1 3647 ? 147.056 156.420 199.586 1.00 24.70  ? 3647 PRO A CB    1 
ATOM   15190 C  CG    . PRO A 1 3647 ? 146.518 156.634 198.220 1.00 26.90  ? 3647 PRO A CG    1 
ATOM   15191 C  CD    . PRO A 1 3647 ? 147.715 156.758 197.344 1.00 21.46  ? 3647 PRO A CD    1 
ATOM   15192 N  N     . VAL A 1 3648 ? 147.549 153.358 198.696 1.00 22.01  ? 3648 VAL A N     1 
ATOM   15193 C  CA    . VAL A 1 3648 ? 147.255 151.946 198.919 1.00 20.09  ? 3648 VAL A CA    1 
ATOM   15194 C  C     . VAL A 1 3648 ? 148.540 151.138 199.035 1.00 17.73  ? 3648 VAL A C     1 
ATOM   15195 O  O     . VAL A 1 3648 ? 148.672 150.278 199.914 1.00 19.75  ? 3648 VAL A O     1 
ATOM   15196 C  CB    . VAL A 1 3648 ? 146.345 151.409 197.800 1.00 24.09  ? 3648 VAL A CB    1 
ATOM   15197 C  CG1   . VAL A 1 3648 ? 146.055 149.933 198.011 1.00 23.62  ? 3648 VAL A CG1   1 
ATOM   15198 C  CG2   . VAL A 1 3648 ? 145.054 152.207 197.741 1.00 26.71  ? 3648 VAL A CG2   1 
ATOM   15199 N  N     . LEU A 1 3649 ? 149.506 151.395 198.152 1.00 22.71  ? 3649 LEU A N     1 
ATOM   15200 C  CA    . LEU A 1 3649 ? 150.758 150.646 198.187 1.00 17.20  ? 3649 LEU A CA    1 
ATOM   15201 C  C     . LEU A 1 3649 ? 151.557 150.961 199.445 1.00 20.11  ? 3649 LEU A C     1 
ATOM   15202 O  O     . LEU A 1 3649 ? 152.260 150.092 199.974 1.00 25.46  ? 3649 LEU A O     1 
ATOM   15203 C  CB    . LEU A 1 3649 ? 151.580 150.941 196.933 1.00 16.11  ? 3649 LEU A CB    1 
ATOM   15204 C  CG    . LEU A 1 3649 ? 150.962 150.507 195.601 1.00 16.74  ? 3649 LEU A CG    1 
ATOM   15205 C  CD1   . LEU A 1 3649 ? 151.960 150.656 194.466 1.00 19.22  ? 3649 LEU A CD1   1 
ATOM   15206 C  CD2   . LEU A 1 3649 ? 150.452 149.079 195.683 1.00 18.05  ? 3649 LEU A CD2   1 
ATOM   15207 N  N     . ASN A 1 3650 ? 151.470 152.198 199.936 1.00 20.95  ? 3650 ASN A N     1 
ATOM   15208 C  CA    . ASN A 1 3650 ? 152.179 152.593 201.147 1.00 19.90  ? 3650 ASN A CA    1 
ATOM   15209 C  C     . ASN A 1 3650 ? 151.429 152.239 202.423 1.00 20.89  ? 3650 ASN A C     1 
ATOM   15210 O  O     . ASN A 1 3650 ? 151.960 152.481 203.514 1.00 22.70  ? 3650 ASN A O     1 
ATOM   15211 C  CB    . ASN A 1 3650 ? 152.455 154.097 201.135 1.00 22.30  ? 3650 ASN A CB    1 
ATOM   15212 C  CG    . ASN A 1 3650 ? 153.279 154.530 199.943 1.00 22.44  ? 3650 ASN A CG    1 
ATOM   15213 O  OD1   . ASN A 1 3650 ? 154.322 153.948 199.652 1.00 30.03  ? 3650 ASN A OD1   1 
ATOM   15214 N  ND2   . ASN A 1 3650 ? 152.820 155.565 199.252 1.00 19.37  ? 3650 ASN A ND2   1 
ATOM   15215 N  N     . ARG A 1 3651 ? 150.219 151.682 202.315 1.00 20.21  ? 3651 ARG A N     1 
ATOM   15216 C  CA    . ARG A 1 3651 ? 149.376 151.392 203.476 1.00 23.20  ? 3651 ARG A CA    1 
ATOM   15217 C  C     . ARG A 1 3651 ? 149.113 152.652 204.298 1.00 25.42  ? 3651 ARG A C     1 
ATOM   15218 O  O     . ARG A 1 3651 ? 149.088 152.617 205.530 1.00 28.59  ? 3651 ARG A O     1 
ATOM   15219 C  CB    . ARG A 1 3651 ? 149.984 150.292 204.354 1.00 30.59  ? 3651 ARG A CB    1 
ATOM   15220 C  CG    . ARG A 1 3651 ? 150.176 148.938 203.676 1.00 35.44  ? 3651 ARG A CG    1 
ATOM   15221 C  CD    . ARG A 1 3651 ? 148.840 148.274 203.372 1.00 47.23  ? 3651 ARG A CD    1 
ATOM   15222 N  NE    . ARG A 1 3651 ? 148.992 146.983 202.715 1.00 59.96  ? 3651 ARG A NE    1 
ATOM   15223 C  CZ    . ARG A 1 3651 ? 149.091 145.826 203.356 1.00 54.65  ? 3651 ARG A CZ    1 
ATOM   15224 N  NH1   . ARG A 1 3651 ? 149.088 145.765 204.677 1.00 45.53  ? 3651 ARG A NH1   1 
ATOM   15225 N  NH2   . ARG A 1 3651 ? 149.190 144.702 202.655 1.00 52.54  ? 3651 ARG A NH2   1 
ATOM   15226 N  N     . GLU A 1 3652 ? 148.910 153.778 203.612 1.00 25.59  ? 3652 GLU A N     1 
ATOM   15227 C  CA    . GLU A 1 3652 ? 148.609 155.047 204.275 1.00 24.53  ? 3652 GLU A CA    1 
ATOM   15228 C  C     . GLU A 1 3652 ? 147.159 155.019 204.749 1.00 27.63  ? 3652 GLU A C     1 
ATOM   15229 O  O     . GLU A 1 3652 ? 146.247 155.574 204.130 1.00 31.11  ? 3652 GLU A O     1 
ATOM   15230 C  CB    . GLU A 1 3652 ? 148.880 156.223 203.344 1.00 26.39  ? 3652 GLU A CB    1 
ATOM   15231 C  CG    . GLU A 1 3652 ? 150.350 156.485 203.082 1.00 24.28  ? 3652 GLU A CG    1 
ATOM   15232 C  CD    . GLU A 1 3652 ? 150.583 157.301 201.827 1.00 34.44  ? 3652 GLU A CD    1 
ATOM   15233 O  OE1   . GLU A 1 3652 ? 149.622 157.926 201.332 1.00 43.61  ? 3652 GLU A OE1   1 
ATOM   15234 O  OE2   . GLU A 1 3652 ? 151.735 157.334 201.346 1.00 40.97  ? 3652 GLU A OE2   1 
ATOM   15235 N  N     . VAL A 1 3653 ? 146.952 154.370 205.891 1.00 29.79  ? 3653 VAL A N     1 
ATOM   15236 C  CA    . VAL A 1 3653 ? 145.627 154.157 206.459 1.00 36.53  ? 3653 VAL A CA    1 
ATOM   15237 C  C     . VAL A 1 3653 ? 145.546 154.866 207.802 1.00 39.38  ? 3653 VAL A C     1 
ATOM   15238 O  O     . VAL A 1 3653 ? 146.507 154.862 208.580 1.00 38.11  ? 3653 VAL A O     1 
ATOM   15239 C  CB    . VAL A 1 3653 ? 145.311 152.656 206.607 1.00 34.19  ? 3653 VAL A CB    1 
ATOM   15240 C  CG1   . VAL A 1 3653 ? 145.051 152.040 205.246 1.00 30.50  ? 3653 VAL A CG1   1 
ATOM   15241 C  CG2   . VAL A 1 3653 ? 146.450 151.937 207.310 1.00 27.28  ? 3653 VAL A CG2   1 
ATOM   15242 N  N     . ARG A 1 3654 ? 144.402 155.490 208.064 1.00 45.92  ? 3654 ARG A N     1 
ATOM   15243 C  CA    . ARG A 1 3654 ? 144.144 156.185 209.317 1.00 48.84  ? 3654 ARG A CA    1 
ATOM   15244 C  C     . ARG A 1 3654 ? 143.045 155.451 210.074 1.00 45.23  ? 3654 ARG A C     1 
ATOM   15245 O  O     . ARG A 1 3654 ? 141.974 155.187 209.520 1.00 49.70  ? 3654 ARG A O     1 
ATOM   15246 C  CB    . ARG A 1 3654 ? 143.749 157.641 209.058 1.00 44.60  ? 3654 ARG A CB    1 
ATOM   15247 C  CG    . ARG A 1 3654 ? 143.556 158.478 210.311 1.00 44.94  ? 3654 ARG A CG    1 
ATOM   15248 C  CD    . ARG A 1 3654 ? 142.357 159.398 210.167 1.00 49.91  ? 3654 ARG A CD    1 
ATOM   15249 N  NE    . ARG A 1 3654 ? 142.509 160.305 209.036 1.00 60.75  ? 3654 ARG A NE    1 
ATOM   15250 C  CZ    . ARG A 1 3654 ? 141.587 160.499 208.103 1.00 61.82  ? 3654 ARG A CZ    1 
ATOM   15251 N  NH1   . ARG A 1 3654 ? 140.431 159.856 208.130 1.00 61.90  ? 3654 ARG A NH1   1 
ATOM   15252 N  NH2   . ARG A 1 3654 ? 141.833 161.355 207.116 1.00 53.58  ? 3654 ARG A NH2   1 
ATOM   15253 N  N     . ARG A 1 3655 ? 143.315 155.116 211.333 1.00 47.75  ? 3655 ARG A N     1 
ATOM   15254 C  CA    . ARG A 1 3655 ? 142.400 154.315 212.146 1.00 54.84  ? 3655 ARG A CA    1 
ATOM   15255 C  C     . ARG A 1 3655 ? 141.657 155.251 213.093 1.00 62.75  ? 3655 ARG A C     1 
ATOM   15256 O  O     . ARG A 1 3655 ? 142.154 155.609 214.161 1.00 56.32  ? 3655 ARG A O     1 
ATOM   15257 C  CB    . ARG A 1 3655 ? 143.159 153.232 212.903 1.00 46.62  ? 3655 ARG A CB    1 
ATOM   15258 C  CG    . ARG A 1 3655 ? 143.870 152.241 212.001 1.00 45.61  ? 3655 ARG A CG    1 
ATOM   15259 C  CD    . ARG A 1 3655 ? 144.644 151.210 212.801 1.00 47.87  ? 3655 ARG A CD    1 
ATOM   15260 N  NE    . ARG A 1 3655 ? 144.695 149.926 212.113 1.00 54.93  ? 3655 ARG A NE    1 
ATOM   15261 C  CZ    . ARG A 1 3655 ? 145.680 149.546 211.312 1.00 56.73  ? 3655 ARG A CZ    1 
ATOM   15262 N  NH1   . ARG A 1 3655 ? 146.723 150.326 211.080 1.00 55.93  ? 3655 ARG A NH1   1 
ATOM   15263 N  NH2   . ARG A 1 3655 ? 145.619 148.352 210.730 1.00 55.51  ? 3655 ARG A NH2   1 
ATOM   15264 N  N     . THR A 1 3656 ? 140.450 155.647 212.697 1.00 65.93  ? 3656 THR A N     1 
ATOM   15265 C  CA    . THR A 1 3656 ? 139.612 156.531 213.497 1.00 71.22  ? 3656 THR A CA    1 
ATOM   15266 C  C     . THR A 1 3656 ? 138.404 155.744 213.985 1.00 71.79  ? 3656 THR A C     1 
ATOM   15267 O  O     . THR A 1 3656 ? 137.620 155.239 213.174 1.00 70.43  ? 3656 THR A O     1 
ATOM   15268 C  CB    . THR A 1 3656 ? 139.171 157.753 212.691 1.00 65.87  ? 3656 THR A CB    1 
ATOM   15269 O  OG1   . THR A 1 3656 ? 140.293 158.618 212.485 1.00 56.87  ? 3656 THR A OG1   1 
ATOM   15270 C  CG2   . THR A 1 3656 ? 138.082 158.516 213.433 1.00 65.81  ? 3656 THR A CG2   1 
ATOM   15271 N  N     . GLY A 1 3657 ? 138.253 155.656 215.303 1.00 68.73  ? 3657 GLY A N     1 
ATOM   15272 C  CA    . GLY A 1 3657 ? 137.183 154.846 215.861 1.00 75.92  ? 3657 GLY A CA    1 
ATOM   15273 C  C     . GLY A 1 3657 ? 137.316 153.408 215.404 1.00 74.86  ? 3657 GLY A C     1 
ATOM   15274 O  O     . GLY A 1 3657 ? 138.386 152.796 215.501 1.00 72.75  ? 3657 GLY A O     1 
ATOM   15275 N  N     . GLY A 1 3658 ? 136.221 152.858 214.895 1.00 70.72  ? 3658 GLY A N     1 
ATOM   15276 C  CA    . GLY A 1 3658 ? 136.213 151.535 214.313 1.00 71.65  ? 3658 GLY A CA    1 
ATOM   15277 C  C     . GLY A 1 3658 ? 136.447 151.495 212.820 1.00 71.63  ? 3658 GLY A C     1 
ATOM   15278 O  O     . GLY A 1 3658 ? 136.287 150.434 212.209 1.00 63.38  ? 3658 GLY A O     1 
ATOM   15279 N  N     . ARG A 1 3659 ? 136.825 152.616 212.211 1.00 72.65  ? 3659 ARG A N     1 
ATOM   15280 C  CA    . ARG A 1 3659 ? 136.978 152.717 210.765 1.00 66.40  ? 3659 ARG A CA    1 
ATOM   15281 C  C     . ARG A 1 3659 ? 138.452 152.855 210.411 1.00 67.44  ? 3659 ARG A C     1 
ATOM   15282 O  O     . ARG A 1 3659 ? 139.127 153.779 210.882 1.00 70.27  ? 3659 ARG A O     1 
ATOM   15283 C  CB    . ARG A 1 3659 ? 136.188 153.904 210.214 1.00 65.53  ? 3659 ARG A CB    1 
ATOM   15284 C  CG    . ARG A 1 3659 ? 134.714 153.900 210.575 1.00 62.67  ? 3659 ARG A CG    1 
ATOM   15285 C  CD    . ARG A 1 3659 ? 134.082 155.256 210.304 1.00 58.82  ? 3659 ARG A CD    1 
ATOM   15286 N  NE    . ARG A 1 3659 ? 134.185 155.640 208.901 1.00 61.22  ? 3659 ARG A NE    1 
ATOM   15287 C  CZ    . ARG A 1 3659 ? 133.931 156.856 208.438 1.00 65.07  ? 3659 ARG A CZ    1 
ATOM   15288 N  NH1   . ARG A 1 3659 ? 133.559 157.838 209.242 1.00 70.93  ? 3659 ARG A NH1   1 
ATOM   15289 N  NH2   . ARG A 1 3659 ? 134.052 157.093 207.135 1.00 62.53  ? 3659 ARG A NH2   1 
ATOM   15290 N  N     . VAL A 1 3660 ? 138.942 151.945 209.575 1.00 58.71  ? 3660 VAL A N     1 
ATOM   15291 C  CA    . VAL A 1 3660 ? 140.271 152.042 208.983 1.00 49.90  ? 3660 VAL A CA    1 
ATOM   15292 C  C     . VAL A 1 3660 ? 140.066 152.644 207.598 1.00 48.70  ? 3660 VAL A C     1 
ATOM   15293 O  O     . VAL A 1 3660 ? 139.587 151.973 206.680 1.00 50.49  ? 3660 VAL A O     1 
ATOM   15294 C  CB    . VAL A 1 3660 ? 140.967 150.680 208.922 1.00 47.48  ? 3660 VAL A CB    1 
ATOM   15295 C  CG1   . VAL A 1 3660 ? 142.174 150.735 207.993 1.00 49.40  ? 3660 VAL A CG1   1 
ATOM   15296 C  CG2   . VAL A 1 3660 ? 141.372 150.224 210.315 1.00 46.40  ? 3660 VAL A CG2   1 
ATOM   15297 N  N     . LEU A 1 3661 ? 140.411 153.918 207.443 1.00 51.59  ? 3661 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3661 ? 140.116 154.661 206.228 1.00 49.56  ? 3661 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3661 ? 141.375 154.879 205.402 1.00 46.61  ? 3661 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3661 ? 142.467 155.069 205.945 1.00 51.30  ? 3661 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3661 ? 139.475 156.009 206.560 1.00 54.74  ? 3661 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3661 ? 138.284 155.963 207.517 1.00 56.16  ? 3661 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3661 ? 138.113 157.298 208.222 1.00 57.10  ? 3661 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3661 ? 137.022 155.583 206.764 1.00 55.37  ? 3661 LEU A CD2   1 
ATOM   15305 N  N     . ILE A 1 3662 ? 141.209 154.849 204.084 1.00 45.81  ? 3662 ILE A N     1 
ATOM   15306 C  CA    . ILE A 1 3662 ? 142.270 155.148 203.133 1.00 42.85  ? 3662 ILE A CA    1 
ATOM   15307 C  C     . ILE A 1 3662 ? 141.737 156.179 202.147 1.00 51.01  ? 3662 ILE A C     1 
ATOM   15308 O  O     . ILE A 1 3662 ? 140.565 156.130 201.756 1.00 59.62  ? 3662 ILE A O     1 
ATOM   15309 C  CB    . ILE A 1 3662 ? 142.766 153.874 202.413 1.00 39.75  ? 3662 ILE A CB    1 
ATOM   15310 C  CG1   . ILE A 1 3662 ? 143.995 154.178 201.556 1.00 41.88  ? 3662 ILE A CG1   1 
ATOM   15311 C  CG2   . ILE A 1 3662 ? 141.656 153.241 201.582 1.00 45.25  ? 3662 ILE A CG2   1 
ATOM   15312 C  CD1   . ILE A 1 3662 ? 144.962 153.027 201.471 1.00 31.72  ? 3662 ILE A CD1   1 
ATOM   15313 N  N     . THR A 1 3663 ? 142.584 157.131 201.767 1.00 50.31  ? 3663 THR A N     1 
ATOM   15314 C  CA    . THR A 1 3663 ? 142.163 158.272 200.961 1.00 54.86  ? 3663 THR A CA    1 
ATOM   15315 C  C     . THR A 1 3663 ? 142.564 158.047 199.507 1.00 53.89  ? 3663 THR A C     1 
ATOM   15316 O  O     . THR A 1 3663 ? 143.753 158.067 199.174 1.00 63.52  ? 3663 THR A O     1 
ATOM   15317 C  CB    . THR A 1 3663 ? 142.771 159.565 201.499 1.00 64.41  ? 3663 THR A CB    1 
ATOM   15318 O  OG1   . THR A 1 3663 ? 142.272 159.817 202.819 1.00 64.99  ? 3663 THR A OG1   1 
ATOM   15319 C  CG2   . THR A 1 3663 ? 142.409 160.737 200.599 1.00 67.19  ? 3663 THR A CG2   1 
ATOM   15320 N  N     . LEU A 1 3664 ? 141.571 157.840 198.643 1.00 59.35  ? 3664 LEU A N     1 
ATOM   15321 C  CA    . LEU A 1 3664 ? 141.779 157.774 197.200 1.00 62.25  ? 3664 LEU A CA    1 
ATOM   15322 C  C     . LEU A 1 3664 ? 141.265 159.073 196.595 1.00 66.27  ? 3664 LEU A C     1 
ATOM   15323 O  O     . LEU A 1 3664 ? 140.065 159.361 196.658 1.00 74.24  ? 3664 LEU A O     1 
ATOM   15324 C  CB    . LEU A 1 3664 ? 141.062 156.576 196.583 1.00 56.74  ? 3664 LEU A CB    1 
ATOM   15325 C  CG    . LEU A 1 3664 ? 141.588 155.178 196.888 1.00 53.43  ? 3664 LEU A CG    1 
ATOM   15326 C  CD1   . LEU A 1 3664 ? 140.797 154.158 196.094 1.00 43.91  ? 3664 LEU A CD1   1 
ATOM   15327 C  CD2   . LEU A 1 3664 ? 143.063 155.083 196.572 1.00 57.26  ? 3664 LEU A CD2   1 
ATOM   15328 N  N     . GLY A 1 3665 ? 142.167 159.847 195.997 1.00 64.39  ? 3665 GLY A N     1 
ATOM   15329 C  CA    . GLY A 1 3665 ? 141.793 161.134 195.451 1.00 68.94  ? 3665 GLY A CA    1 
ATOM   15330 C  C     . GLY A 1 3665 ? 141.213 162.047 196.511 1.00 78.60  ? 3665 GLY A C     1 
ATOM   15331 O  O     . GLY A 1 3665 ? 141.933 162.536 197.386 1.00 78.02  ? 3665 GLY A O     1 
ATOM   15332 N  N     . ASP A 1 3666 ? 139.901 162.276 196.443 1.00 78.24  ? 3666 ASP A N     1 
ATOM   15333 C  CA    . ASP A 1 3666 ? 139.196 163.097 197.419 1.00 84.75  ? 3666 ASP A CA    1 
ATOM   15334 C  C     . ASP A 1 3666 ? 138.123 162.310 198.163 1.00 82.29  ? 3666 ASP A C     1 
ATOM   15335 O  O     . ASP A 1 3666 ? 137.149 162.898 198.645 1.00 85.48  ? 3666 ASP A O     1 
ATOM   15336 C  CB    . ASP A 1 3666 ? 138.581 164.322 196.738 1.00 86.48  ? 3666 ASP A CB    1 
ATOM   15337 C  CG    . ASP A 1 3666 ? 137.620 163.948 195.625 1.00 86.53  ? 3666 ASP A CG    1 
ATOM   15338 O  OD1   . ASP A 1 3666 ? 137.643 162.781 195.182 1.00 81.35  ? 3666 ASP A OD1   1 
ATOM   15339 O  OD2   . ASP A 1 3666 ? 136.840 164.823 195.193 1.00 86.20  ? 3666 ASP A OD2   1 
ATOM   15340 N  N     . GLN A 1 3667 ? 138.276 160.991 198.267 1.00 76.52  ? 3667 GLN A N     1 
ATOM   15341 C  CA    . GLN A 1 3667 ? 137.274 160.136 198.892 1.00 73.37  ? 3667 GLN A CA    1 
ATOM   15342 C  C     . GLN A 1 3667 ? 137.930 159.238 199.929 1.00 68.76  ? 3667 GLN A C     1 
ATOM   15343 O  O     . GLN A 1 3667 ? 138.989 158.656 199.675 1.00 70.72  ? 3667 GLN A O     1 
ATOM   15344 C  CB    . GLN A 1 3667 ? 136.548 159.287 197.843 1.00 73.12  ? 3667 GLN A CB    1 
ATOM   15345 C  CG    . GLN A 1 3667 ? 135.181 158.791 198.284 1.00 75.84  ? 3667 GLN A CG    1 
ATOM   15346 C  CD    . GLN A 1 3667 ? 134.629 157.721 197.366 1.00 74.65  ? 3667 GLN A CD    1 
ATOM   15347 O  OE1   . GLN A 1 3667 ? 134.051 156.734 197.821 1.00 72.57  ? 3667 GLN A OE1   1 
ATOM   15348 N  NE2   . GLN A 1 3667 ? 134.802 157.912 196.063 1.00 68.70  ? 3667 GLN A NE2   1 
ATOM   15349 N  N     . ASP A 1 3668 ? 137.292 159.116 201.091 1.00 70.67  ? 3668 ASP A N     1 
ATOM   15350 C  CA    . ASP A 1 3668 ? 137.755 158.216 202.138 1.00 67.17  ? 3668 ASP A CA    1 
ATOM   15351 C  C     . ASP A 1 3668 ? 136.980 156.906 202.063 1.00 66.40  ? 3668 ASP A C     1 
ATOM   15352 O  O     . ASP A 1 3668 ? 135.746 156.909 202.026 1.00 67.41  ? 3668 ASP A O     1 
ATOM   15353 C  CB    . ASP A 1 3668 ? 137.588 158.855 203.517 1.00 66.10  ? 3668 ASP A CB    1 
ATOM   15354 C  CG    . ASP A 1 3668 ? 138.529 160.021 203.735 1.00 70.54  ? 3668 ASP A CG    1 
ATOM   15355 O  OD1   . ASP A 1 3668 ? 139.628 160.017 203.142 1.00 74.21  ? 3668 ASP A OD1   1 
ATOM   15356 O  OD2   . ASP A 1 3668 ? 138.170 160.942 204.497 1.00 73.32  ? 3668 ASP A OD2   1 
ATOM   15357 N  N     . ILE A 1 3669 ? 137.708 155.793 202.042 1.00 57.23  ? 3669 ILE A N     1 
ATOM   15358 C  CA    . ILE A 1 3669 ? 137.137 154.465 201.861 1.00 53.29  ? 3669 ILE A CA    1 
ATOM   15359 C  C     . ILE A 1 3669 ? 137.535 153.602 203.048 1.00 50.99  ? 3669 ILE A C     1 
ATOM   15360 O  O     . ILE A 1 3669 ? 138.713 153.558 203.420 1.00 51.17  ? 3669 ILE A O     1 
ATOM   15361 C  CB    . ILE A 1 3669 ? 137.605 153.827 200.541 1.00 50.24  ? 3669 ILE A CB    1 
ATOM   15362 C  CG1   . ILE A 1 3669 ? 137.116 154.648 199.349 1.00 55.80  ? 3669 ILE A CG1   1 
ATOM   15363 C  CG2   . ILE A 1 3669 ? 137.141 152.388 200.445 1.00 49.95  ? 3669 ILE A CG2   1 
ATOM   15364 C  CD1   . ILE A 1 3669 ? 137.741 154.242 198.040 1.00 53.47  ? 3669 ILE A CD1   1 
ATOM   15365 N  N     . ASP A 1 3670 ? 136.557 152.922 203.640 1.00 50.45  ? 3670 ASP A N     1 
ATOM   15366 C  CA    . ASP A 1 3670 ? 136.820 152.024 204.760 1.00 52.72  ? 3670 ASP A CA    1 
ATOM   15367 C  C     . ASP A 1 3670 ? 137.546 150.784 204.252 1.00 60.05  ? 3670 ASP A C     1 
ATOM   15368 O  O     . ASP A 1 3670 ? 136.949 149.935 203.582 1.00 58.13  ? 3670 ASP A O     1 
ATOM   15369 C  CB    . ASP A 1 3670 ? 135.515 151.649 205.454 1.00 54.78  ? 3670 ASP A CB    1 
ATOM   15370 C  CG    . ASP A 1 3670 ? 135.719 151.242 206.900 1.00 62.44  ? 3670 ASP A CG    1 
ATOM   15371 O  OD1   . ASP A 1 3670 ? 136.555 150.351 207.160 1.00 55.77  ? 3670 ASP A OD1   1 
ATOM   15372 O  OD2   . ASP A 1 3670 ? 135.042 151.814 207.780 1.00 70.84  ? 3670 ASP A OD2   1 
ATOM   15373 N  N     . LEU A 1 3671 ? 138.834 150.681 204.567 1.00 56.86  ? 3671 LEU A N     1 
ATOM   15374 C  CA    . LEU A 1 3671 ? 139.625 149.539 204.131 1.00 45.90  ? 3671 LEU A CA    1 
ATOM   15375 C  C     . LEU A 1 3671 ? 139.190 148.270 204.851 1.00 48.66  ? 3671 LEU A C     1 
ATOM   15376 O  O     . LEU A 1 3671 ? 138.812 148.297 206.026 1.00 47.27  ? 3671 LEU A O     1 
ATOM   15377 C  CB    . LEU A 1 3671 ? 141.110 149.799 204.384 1.00 45.12  ? 3671 LEU A CB    1 
ATOM   15378 C  CG    . LEU A 1 3671 ? 142.091 148.733 203.894 1.00 42.57  ? 3671 LEU A CG    1 
ATOM   15379 C  CD1   . LEU A 1 3671 ? 142.277 148.820 202.393 1.00 40.37  ? 3671 LEU A CD1   1 
ATOM   15380 C  CD2   . LEU A 1 3671 ? 143.423 148.856 204.612 1.00 37.04  ? 3671 LEU A CD2   1 
ATOM   15381 N  N     . SER A 1 3672 ? 139.245 147.146 204.133 1.00 47.90  ? 3672 SER A N     1 
ATOM   15382 C  CA    . SER A 1 3672 ? 138.986 145.835 204.700 1.00 43.29  ? 3672 SER A CA    1 
ATOM   15383 C  C     . SER A 1 3672 ? 140.273 145.021 204.753 1.00 41.40  ? 3672 SER A C     1 
ATOM   15384 O  O     . SER A 1 3672 ? 141.058 145.044 203.799 1.00 47.04  ? 3672 SER A O     1 
ATOM   15385 C  CB    . SER A 1 3672 ? 137.937 145.075 203.882 1.00 42.87  ? 3672 SER A CB    1 
ATOM   15386 O  OG    . SER A 1 3672 ? 137.667 143.806 204.450 1.00 47.12  ? 3672 SER A OG    1 
ATOM   15387 N  N     . PRO A 1 3673 ? 140.522 144.300 205.849 1.00 38.58  ? 3673 PRO A N     1 
ATOM   15388 C  CA    . PRO A 1 3673 ? 141.786 143.554 205.966 1.00 43.20  ? 3673 PRO A CA    1 
ATOM   15389 C  C     . PRO A 1 3673 ? 141.948 142.452 204.934 1.00 41.54  ? 3673 PRO A C     1 
ATOM   15390 O  O     . PRO A 1 3673 ? 143.077 142.000 204.706 1.00 37.04  ? 3673 PRO A O     1 
ATOM   15391 C  CB    . PRO A 1 3673 ? 141.728 142.985 207.390 1.00 35.35  ? 3673 PRO A CB    1 
ATOM   15392 C  CG    . PRO A 1 3673 ? 140.277 142.951 207.726 1.00 38.97  ? 3673 PRO A CG    1 
ATOM   15393 C  CD    . PRO A 1 3673 ? 139.663 144.128 207.032 1.00 38.24  ? 3673 PRO A CD    1 
ATOM   15394 N  N     . SER A 1 3674 ? 140.866 142.004 204.305 1.00 42.49  ? 3674 SER A N     1 
ATOM   15395 C  CA    . SER A 1 3674 ? 140.938 140.926 203.327 1.00 39.38  ? 3674 SER A CA    1 
ATOM   15396 C  C     . SER A 1 3674 ? 141.352 141.406 201.944 1.00 38.58  ? 3674 SER A C     1 
ATOM   15397 O  O     . SER A 1 3674 ? 141.494 140.580 201.037 1.00 37.56  ? 3674 SER A O     1 
ATOM   15398 C  CB    . SER A 1 3674 ? 139.588 140.209 203.243 1.00 44.42  ? 3674 SER A CB    1 
ATOM   15399 O  OG    . SER A 1 3674 ? 139.270 139.580 204.472 1.00 49.76  ? 3674 SER A OG    1 
ATOM   15400 N  N     . PHE A 1 3675 ? 141.544 142.709 201.759 1.00 39.54  ? 3675 PHE A N     1 
ATOM   15401 C  CA    . PHE A 1 3675 ? 141.956 143.230 200.464 1.00 31.18  ? 3675 PHE A CA    1 
ATOM   15402 C  C     . PHE A 1 3675 ? 143.411 142.881 200.177 1.00 27.93  ? 3675 PHE A C     1 
ATOM   15403 O  O     . PHE A 1 3675 ? 144.268 142.928 201.063 1.00 29.72  ? 3675 PHE A O     1 
ATOM   15404 C  CB    . PHE A 1 3675 ? 141.765 144.746 200.416 1.00 25.92  ? 3675 PHE A CB    1 
ATOM   15405 C  CG    . PHE A 1 3675 ? 142.515 145.418 199.300 1.00 25.76  ? 3675 PHE A CG    1 
ATOM   15406 C  CD1   . PHE A 1 3675 ? 142.030 145.388 198.006 1.00 26.36  ? 3675 PHE A CD1   1 
ATOM   15407 C  CD2   . PHE A 1 3675 ? 143.707 146.080 199.547 1.00 24.31  ? 3675 PHE A CD2   1 
ATOM   15408 C  CE1   . PHE A 1 3675 ? 142.717 146.003 196.979 1.00 24.99  ? 3675 PHE A CE1   1 
ATOM   15409 C  CE2   . PHE A 1 3675 ? 144.399 146.694 198.524 1.00 23.44  ? 3675 PHE A CE2   1 
ATOM   15410 C  CZ    . PHE A 1 3675 ? 143.902 146.657 197.239 1.00 24.75  ? 3675 PHE A CZ    1 
ATOM   15411 N  N     . VAL A 1 3676 ? 143.684 142.529 198.924 1.00 27.19  ? 3676 VAL A N     1 
ATOM   15412 C  CA    . VAL A 1 3676 ? 145.044 142.312 198.444 1.00 24.68  ? 3676 VAL A CA    1 
ATOM   15413 C  C     . VAL A 1 3676 ? 145.063 142.629 196.955 1.00 25.48  ? 3676 VAL A C     1 
ATOM   15414 O  O     . VAL A 1 3676 ? 144.090 142.370 196.242 1.00 29.79  ? 3676 VAL A O     1 
ATOM   15415 C  CB    . VAL A 1 3676 ? 145.530 140.875 198.741 1.00 20.98  ? 3676 VAL A CB    1 
ATOM   15416 C  CG1   . VAL A 1 3676 ? 144.712 139.852 197.969 1.00 27.61  ? 3676 VAL A CG1   1 
ATOM   15417 C  CG2   . VAL A 1 3676 ? 147.012 140.733 198.431 1.00 21.47  ? 3676 VAL A CG2   1 
ATOM   15418 N  N     . ILE A 1 3677 ? 146.162 143.216 196.489 1.00 20.85  ? 3677 ILE A N     1 
ATOM   15419 C  CA    . ILE A 1 3677 ? 146.286 143.647 195.103 1.00 19.80  ? 3677 ILE A CA    1 
ATOM   15420 C  C     . ILE A 1 3677 ? 147.584 143.104 194.522 1.00 20.82  ? 3677 ILE A C     1 
ATOM   15421 O  O     . ILE A 1 3677 ? 148.627 143.108 195.186 1.00 21.94  ? 3677 ILE A O     1 
ATOM   15422 C  CB    . ILE A 1 3677 ? 146.221 145.186 194.976 1.00 21.28  ? 3677 ILE A CB    1 
ATOM   15423 C  CG1   . ILE A 1 3677 ? 146.375 145.619 193.518 1.00 23.52  ? 3677 ILE A CG1   1 
ATOM   15424 C  CG2   . ILE A 1 3677 ? 147.263 145.852 195.854 1.00 21.67  ? 3677 ILE A CG2   1 
ATOM   15425 C  CD1   . ILE A 1 3677 ? 145.968 147.046 193.269 1.00 26.61  ? 3677 ILE A CD1   1 
ATOM   15426 N  N     . PHE A 1 3678 ? 147.509 142.613 193.288 1.00 20.76  ? 3678 PHE A N     1 
ATOM   15427 C  CA    . PHE A 1 3678 ? 148.664 142.119 192.552 1.00 12.75  ? 3678 PHE A CA    1 
ATOM   15428 C  C     . PHE A 1 3678 ? 148.834 142.937 191.281 1.00 13.79  ? 3678 PHE A C     1 
ATOM   15429 O  O     . PHE A 1 3678 ? 147.867 143.156 190.546 1.00 16.15  ? 3678 PHE A O     1 
ATOM   15430 C  CB    . PHE A 1 3678 ? 148.511 140.636 192.205 1.00 12.48  ? 3678 PHE A CB    1 
ATOM   15431 C  CG    . PHE A 1 3678 ? 148.416 139.738 193.402 1.00 16.27  ? 3678 PHE A CG    1 
ATOM   15432 C  CD1   . PHE A 1 3678 ? 147.194 139.481 194.000 1.00 17.95  ? 3678 PHE A CD1   1 
ATOM   15433 C  CD2   . PHE A 1 3678 ? 149.551 139.143 193.927 1.00 14.63  ? 3678 PHE A CD2   1 
ATOM   15434 C  CE1   . PHE A 1 3678 ? 147.108 138.655 195.100 1.00 19.23  ? 3678 PHE A CE1   1 
ATOM   15435 C  CE2   . PHE A 1 3678 ? 149.469 138.315 195.027 1.00 13.52  ? 3678 PHE A CE2   1 
ATOM   15436 C  CZ    . PHE A 1 3678 ? 148.246 138.071 195.614 1.00 16.72  ? 3678 PHE A CZ    1 
ATOM   15437 N  N     . LEU A 1 3679 ? 150.058 143.386 191.029 1.00 15.51  ? 3679 LEU A N     1 
ATOM   15438 C  CA    . LEU A 1 3679 ? 150.399 144.092 189.802 1.00 12.19  ? 3679 LEU A CA    1 
ATOM   15439 C  C     . LEU A 1 3679 ? 151.193 143.159 188.899 1.00 12.81  ? 3679 LEU A C     1 
ATOM   15440 O  O     . LEU A 1 3679 ? 152.144 142.514 189.351 1.00 17.24  ? 3679 LEU A O     1 
ATOM   15441 C  CB    . LEU A 1 3679 ? 151.203 145.358 190.100 1.00 13.37  ? 3679 LEU A CB    1 
ATOM   15442 C  CG    . LEU A 1 3679 ? 150.655 146.270 191.200 1.00 15.85  ? 3679 LEU A CG    1 
ATOM   15443 C  CD1   . LEU A 1 3679 ? 151.548 147.484 191.379 1.00 17.82  ? 3679 LEU A CD1   1 
ATOM   15444 C  CD2   . LEU A 1 3679 ? 149.228 146.693 190.891 1.00 16.19  ? 3679 LEU A CD2   1 
ATOM   15445 N  N     . SER A 1 3680 ? 150.798 143.081 187.633 1.00 16.43  ? 3680 SER A N     1 
ATOM   15446 C  CA    . SER A 1 3680 ? 151.435 142.182 186.685 1.00 17.91  ? 3680 SER A CA    1 
ATOM   15447 C  C     . SER A 1 3680 ? 151.746 142.921 185.392 1.00 18.81  ? 3680 SER A C     1 
ATOM   15448 O  O     . SER A 1 3680 ? 151.110 143.924 185.059 1.00 18.18  ? 3680 SER A O     1 
ATOM   15449 C  CB    . SER A 1 3680 ? 150.560 140.955 186.394 1.00 20.32  ? 3680 SER A CB    1 
ATOM   15450 O  OG    . SER A 1 3680 ? 149.293 141.333 185.891 1.00 18.55  ? 3680 SER A OG    1 
ATOM   15451 N  N     . THR A 1 3681 ? 152.746 142.416 184.674 1.00 21.98  ? 3681 THR A N     1 
ATOM   15452 C  CA    . THR A 1 3681 ? 153.139 142.971 183.389 1.00 19.00  ? 3681 THR A CA    1 
ATOM   15453 C  C     . THR A 1 3681 ? 153.642 141.845 182.502 1.00 21.29  ? 3681 THR A C     1 
ATOM   15454 O  O     . THR A 1 3681 ? 154.001 140.765 182.977 1.00 27.13  ? 3681 THR A O     1 
ATOM   15455 C  CB    . THR A 1 3681 ? 154.216 144.053 183.535 1.00 21.22  ? 3681 THR A CB    1 
ATOM   15456 O  OG1   . THR A 1 3681 ? 154.293 144.821 182.328 1.00 22.76  ? 3681 THR A OG1   1 
ATOM   15457 C  CG2   . THR A 1 3681 ? 155.573 143.430 183.818 1.00 21.52  ? 3681 THR A CG2   1 
ATOM   15458 N  N     . ARG A 1 3682 ? 153.652 142.108 181.198 1.00 20.64  ? 3682 ARG A N     1 
ATOM   15459 C  CA    . ARG A 1 3682 ? 154.141 141.153 180.216 1.00 16.88  ? 3682 ARG A CA    1 
ATOM   15460 C  C     . ARG A 1 3682 ? 155.419 141.614 179.533 1.00 22.77  ? 3682 ARG A C     1 
ATOM   15461 O  O     . ARG A 1 3682 ? 156.015 140.842 178.776 1.00 28.80  ? 3682 ARG A O     1 
ATOM   15462 C  CB    . ARG A 1 3682 ? 153.061 140.877 179.166 1.00 18.64  ? 3682 ARG A CB    1 
ATOM   15463 C  CG    . ARG A 1 3682 ? 151.883 140.074 179.689 1.00 18.77  ? 3682 ARG A CG    1 
ATOM   15464 C  CD    . ARG A 1 3682 ? 150.818 139.896 178.621 1.00 20.56  ? 3682 ARG A CD    1 
ATOM   15465 N  NE    . ARG A 1 3682 ? 150.267 141.169 178.175 1.00 21.36  ? 3682 ARG A NE    1 
ATOM   15466 C  CZ    . ARG A 1 3682 ? 150.544 141.737 177.009 1.00 26.64  ? 3682 ARG A CZ    1 
ATOM   15467 N  NH1   . ARG A 1 3682 ? 151.373 141.173 176.146 1.00 23.41  ? 3682 ARG A NH1   1 
ATOM   15468 N  NH2   . ARG A 1 3682 ? 149.977 142.899 176.702 1.00 28.62  ? 3682 ARG A NH2   1 
ATOM   15469 N  N     . ASP A 1 3683 ? 155.859 142.847 179.783 1.00 24.95  ? 3683 ASP A N     1 
ATOM   15470 C  CA    . ASP A 1 3683 ? 157.078 143.368 179.188 1.00 22.18  ? 3683 ASP A CA    1 
ATOM   15471 C  C     . ASP A 1 3683 ? 158.238 143.126 180.139 1.00 27.57  ? 3683 ASP A C     1 
ATOM   15472 O  O     . ASP A 1 3683 ? 158.271 143.727 181.222 1.00 27.55  ? 3683 ASP A O     1 
ATOM   15473 C  CB    . ASP A 1 3683 ? 156.933 144.859 178.893 1.00 22.50  ? 3683 ASP A CB    1 
ATOM   15474 C  CG    . ASP A 1 3683 ? 158.066 145.400 178.044 1.00 30.33  ? 3683 ASP A CG    1 
ATOM   15475 O  OD1   . ASP A 1 3683 ? 158.262 146.632 178.033 1.00 25.30  ? 3683 ASP A OD1   1 
ATOM   15476 O  OD2   . ASP A 1 3683 ? 158.758 144.596 177.386 1.00 36.43  ? 3683 ASP A OD2   1 
ATOM   15477 N  N     . PRO A 1 3684 ? 159.202 142.266 179.794 1.00 27.61  ? 3684 PRO A N     1 
ATOM   15478 C  CA    . PRO A 1 3684 ? 160.337 142.030 180.695 1.00 26.82  ? 3684 PRO A CA    1 
ATOM   15479 C  C     . PRO A 1 3684 ? 161.392 143.122 180.665 1.00 28.09  ? 3684 PRO A C     1 
ATOM   15480 O  O     . PRO A 1 3684 ? 162.280 143.121 181.527 1.00 35.59  ? 3684 PRO A O     1 
ATOM   15481 C  CB    . PRO A 1 3684 ? 160.912 140.705 180.181 1.00 27.57  ? 3684 PRO A CB    1 
ATOM   15482 C  CG    . PRO A 1 3684 ? 160.584 140.709 178.729 1.00 21.92  ? 3684 PRO A CG    1 
ATOM   15483 C  CD    . PRO A 1 3684 ? 159.261 141.418 178.592 1.00 21.90  ? 3684 PRO A CD    1 
ATOM   15484 N  N     . THR A 1 3685 ? 161.329 144.046 179.708 1.00 28.17  ? 3685 THR A N     1 
ATOM   15485 C  CA    . THR A 1 3685 ? 162.332 145.091 179.556 1.00 33.39  ? 3685 THR A CA    1 
ATOM   15486 C  C     . THR A 1 3685 ? 161.825 146.462 179.985 1.00 36.20  ? 3685 THR A C     1 
ATOM   15487 O  O     . THR A 1 3685 ? 162.490 147.468 179.717 1.00 40.49  ? 3685 THR A O     1 
ATOM   15488 C  CB    . THR A 1 3685 ? 162.821 145.148 178.108 1.00 36.10  ? 3685 THR A CB    1 
ATOM   15489 O  OG1   . THR A 1 3685 ? 161.718 145.435 177.240 1.00 32.86  ? 3685 THR A OG1   1 
ATOM   15490 C  CG2   . THR A 1 3685 ? 163.441 143.820 177.705 1.00 32.25  ? 3685 THR A CG2   1 
ATOM   15491 N  N     . VAL A 1 3686 ? 160.672 146.529 180.638 1.00 32.78  ? 3686 VAL A N     1 
ATOM   15492 C  CA    . VAL A 1 3686 ? 160.109 147.806 181.058 1.00 30.37  ? 3686 VAL A CA    1 
ATOM   15493 C  C     . VAL A 1 3686 ? 160.896 148.341 182.246 1.00 32.41  ? 3686 VAL A C     1 
ATOM   15494 O  O     . VAL A 1 3686 ? 161.258 147.596 183.165 1.00 34.59  ? 3686 VAL A O     1 
ATOM   15495 C  CB    . VAL A 1 3686 ? 158.611 147.657 181.384 1.00 24.53  ? 3686 VAL A CB    1 
ATOM   15496 C  CG1   . VAL A 1 3686 ? 158.397 146.644 182.493 1.00 27.59  ? 3686 VAL A CG1   1 
ATOM   15497 C  CG2   . VAL A 1 3686 ? 158.008 149.001 181.763 1.00 24.44  ? 3686 VAL A CG2   1 
ATOM   15498 N  N     . GLU A 1 3687 ? 161.188 149.638 182.216 1.00 38.83  ? 3687 GLU A N     1 
ATOM   15499 C  CA    . GLU A 1 3687 ? 161.870 150.317 183.308 1.00 28.92  ? 3687 GLU A CA    1 
ATOM   15500 C  C     . GLU A 1 3687 ? 160.840 151.022 184.178 1.00 29.92  ? 3687 GLU A C     1 
ATOM   15501 O  O     . GLU A 1 3687 ? 159.966 151.729 183.666 1.00 32.55  ? 3687 GLU A O     1 
ATOM   15502 C  CB    . GLU A 1 3687 ? 162.896 151.321 182.780 1.00 28.77  ? 3687 GLU A CB    1 
ATOM   15503 C  CG    . GLU A 1 3687 ? 164.084 150.690 182.068 1.00 44.18  ? 3687 GLU A CG    1 
ATOM   15504 C  CD    . GLU A 1 3687 ? 163.793 150.351 180.621 1.00 54.44  ? 3687 GLU A CD    1 
ATOM   15505 O  OE1   . GLU A 1 3687 ? 162.683 150.666 180.145 1.00 59.77  ? 3687 GLU A OE1   1 
ATOM   15506 O  OE2   . GLU A 1 3687 ? 164.675 149.763 179.961 1.00 48.57  ? 3687 GLU A OE2   1 
ATOM   15507 N  N     . PHE A 1 3688 ? 160.942 150.823 185.484 1.00 29.00  ? 3688 PHE A N     1 
ATOM   15508 C  CA    . PHE A 1 3688 ? 160.012 151.425 186.418 1.00 23.42  ? 3688 PHE A CA    1 
ATOM   15509 C  C     . PHE A 1 3688 ? 160.662 152.599 187.141 1.00 26.94  ? 3688 PHE A C     1 
ATOM   15510 O  O     . PHE A 1 3688 ? 161.866 152.580 187.415 1.00 35.08  ? 3688 PHE A O     1 
ATOM   15511 C  CB    . PHE A 1 3688 ? 159.529 150.401 187.451 1.00 25.57  ? 3688 PHE A CB    1 
ATOM   15512 C  CG    . PHE A 1 3688 ? 158.704 149.295 186.865 1.00 22.41  ? 3688 PHE A CG    1 
ATOM   15513 C  CD1   . PHE A 1 3688 ? 157.370 149.498 186.560 1.00 18.91  ? 3688 PHE A CD1   1 
ATOM   15514 C  CD2   . PHE A 1 3688 ? 159.264 148.057 186.611 1.00 18.25  ? 3688 PHE A CD2   1 
ATOM   15515 C  CE1   . PHE A 1 3688 ? 156.609 148.485 186.020 1.00 17.27  ? 3688 PHE A CE1   1 
ATOM   15516 C  CE2   . PHE A 1 3688 ? 158.507 147.040 186.071 1.00 17.99  ? 3688 PHE A CE2   1 
ATOM   15517 C  CZ    . PHE A 1 3688 ? 157.178 147.254 185.775 1.00 17.60  ? 3688 PHE A CZ    1 
ATOM   15518 N  N     . PRO A 1 3689 ? 159.892 153.642 187.457 1.00 27.97  ? 3689 PRO A N     1 
ATOM   15519 C  CA    . PRO A 1 3689 ? 160.452 154.752 188.220 1.00 24.03  ? 3689 PRO A CA    1 
ATOM   15520 C  C     . PRO A 1 3689 ? 160.778 154.317 189.637 1.00 25.36  ? 3689 PRO A C     1 
ATOM   15521 O  O     . PRO A 1 3689 ? 160.165 153.376 190.170 1.00 23.82  ? 3689 PRO A O     1 
ATOM   15522 C  CB    . PRO A 1 3689 ? 159.327 155.801 188.196 1.00 29.89  ? 3689 PRO A CB    1 
ATOM   15523 C  CG    . PRO A 1 3689 ? 158.085 155.004 188.007 1.00 28.13  ? 3689 PRO A CG    1 
ATOM   15524 C  CD    . PRO A 1 3689 ? 158.469 153.847 187.135 1.00 30.65  ? 3689 PRO A CD    1 
ATOM   15525 N  N     . PRO A 1 3690 ? 161.750 154.965 190.286 1.00 23.43  ? 3690 PRO A N     1 
ATOM   15526 C  CA    . PRO A 1 3690 ? 162.121 154.551 191.649 1.00 21.73  ? 3690 PRO A CA    1 
ATOM   15527 C  C     . PRO A 1 3690 ? 160.979 154.634 192.646 1.00 19.79  ? 3690 PRO A C     1 
ATOM   15528 O  O     . PRO A 1 3690 ? 160.930 153.826 193.583 1.00 21.33  ? 3690 PRO A O     1 
ATOM   15529 C  CB    . PRO A 1 3690 ? 163.257 155.519 192.012 1.00 18.01  ? 3690 PRO A CB    1 
ATOM   15530 C  CG    . PRO A 1 3690 ? 163.778 156.009 190.706 1.00 17.24  ? 3690 PRO A CG    1 
ATOM   15531 C  CD    . PRO A 1 3690 ? 162.596 156.062 189.790 1.00 17.34  ? 3690 PRO A CD    1 
ATOM   15532 N  N     . ASP A 1 3691 ? 160.058 155.586 192.476 1.00 19.91  ? 3691 ASP A N     1 
ATOM   15533 C  CA    . ASP A 1 3691 ? 158.946 155.709 193.413 1.00 24.38  ? 3691 ASP A CA    1 
ATOM   15534 C  C     . ASP A 1 3691 ? 158.067 154.465 193.396 1.00 25.47  ? 3691 ASP A C     1 
ATOM   15535 O  O     . ASP A 1 3691 ? 157.631 153.990 194.450 1.00 23.11  ? 3691 ASP A O     1 
ATOM   15536 C  CB    . ASP A 1 3691 ? 158.131 156.968 193.104 1.00 25.28  ? 3691 ASP A CB    1 
ATOM   15537 C  CG    . ASP A 1 3691 ? 157.487 156.937 191.729 1.00 37.06  ? 3691 ASP A CG    1 
ATOM   15538 O  OD1   . ASP A 1 3691 ? 157.697 155.962 190.981 1.00 36.22  ? 3691 ASP A OD1   1 
ATOM   15539 O  OD2   . ASP A 1 3691 ? 156.762 157.896 191.394 1.00 48.24  ? 3691 ASP A OD2   1 
ATOM   15540 N  N     . LEU A 1 3692 ? 157.797 153.920 192.208 1.00 27.07  ? 3692 LEU A N     1 
ATOM   15541 C  CA    . LEU A 1 3692 ? 157.043 152.676 192.119 1.00 20.23  ? 3692 LEU A CA    1 
ATOM   15542 C  C     . LEU A 1 3692 ? 157.873 151.479 192.559 1.00 17.05  ? 3692 LEU A C     1 
ATOM   15543 O  O     . LEU A 1 3692 ? 157.333 150.546 193.162 1.00 18.10  ? 3692 LEU A O     1 
ATOM   15544 C  CB    . LEU A 1 3692 ? 156.532 152.470 190.692 1.00 23.11  ? 3692 LEU A CB    1 
ATOM   15545 C  CG    . LEU A 1 3692 ? 155.648 151.243 190.463 1.00 21.25  ? 3692 LEU A CG    1 
ATOM   15546 C  CD1   . LEU A 1 3692 ? 154.465 151.252 191.415 1.00 18.54  ? 3692 LEU A CD1   1 
ATOM   15547 C  CD2   . LEU A 1 3692 ? 155.174 151.186 189.023 1.00 21.08  ? 3692 LEU A CD2   1 
ATOM   15548 N  N     . CYS A 1 3693 ? 159.179 151.489 192.273 1.00 16.72  ? 3693 CYS A N     1 
ATOM   15549 C  CA    . CYS A 1 3693 ? 160.046 150.404 192.719 1.00 15.76  ? 3693 CYS A CA    1 
ATOM   15550 C  C     . CYS A 1 3693 ? 160.095 150.317 194.236 1.00 16.65  ? 3693 CYS A C     1 
ATOM   15551 O  O     . CYS A 1 3693 ? 160.315 149.234 194.790 1.00 20.82  ? 3693 CYS A O     1 
ATOM   15552 C  CB    . CYS A 1 3693 ? 161.458 150.592 192.163 1.00 20.46  ? 3693 CYS A CB    1 
ATOM   15553 S  SG    . CYS A 1 3693 ? 161.594 150.469 190.371 1.00 28.66  ? 3693 CYS A SG    1 
ATOM   15554 N  N     . SER A 1 3694 ? 159.904 151.444 194.923 1.00 15.86  ? 3694 SER A N     1 
ATOM   15555 C  CA    . SER A 1 3694 ? 159.927 151.437 196.380 1.00 13.33  ? 3694 SER A CA    1 
ATOM   15556 C  C     . SER A 1 3694 ? 158.664 150.831 196.982 1.00 15.06  ? 3694 SER A C     1 
ATOM   15557 O  O     . SER A 1 3694 ? 158.727 150.238 198.063 1.00 16.33  ? 3694 SER A O     1 
ATOM   15558 C  CB    . SER A 1 3694 ? 160.129 152.859 196.907 1.00 10.48  ? 3694 SER A CB    1 
ATOM   15559 O  OG    . SER A 1 3694 ? 159.116 153.728 196.435 1.00 16.41  ? 3694 SER A OG    1 
ATOM   15560 N  N     . ARG A 1 3695 ? 157.519 150.959 196.311 1.00 14.22  ? 3695 ARG A N     1 
ATOM   15561 C  CA    . ARG A 1 3695 ? 156.243 150.562 196.894 1.00 13.01  ? 3695 ARG A CA    1 
ATOM   15562 C  C     . ARG A 1 3695 ? 155.860 149.114 196.617 1.00 14.34  ? 3695 ARG A C     1 
ATOM   15563 O  O     . ARG A 1 3695 ? 154.883 148.631 197.199 1.00 15.24  ? 3695 ARG A O     1 
ATOM   15564 C  CB    . ARG A 1 3695 ? 155.120 151.473 196.388 1.00 14.33  ? 3695 ARG A CB    1 
ATOM   15565 C  CG    . ARG A 1 3695 ? 155.431 152.958 196.444 1.00 13.66  ? 3695 ARG A CG    1 
ATOM   15566 C  CD    . ARG A 1 3695 ? 154.277 153.782 195.888 1.00 15.96  ? 3695 ARG A CD    1 
ATOM   15567 N  NE    . ARG A 1 3695 ? 154.729 155.027 195.278 1.00 21.35  ? 3695 ARG A NE    1 
ATOM   15568 C  CZ    . ARG A 1 3695 ? 155.026 156.130 195.951 1.00 17.28  ? 3695 ARG A CZ    1 
ATOM   15569 N  NH1   . ARG A 1 3695 ? 154.926 156.185 197.269 1.00 15.10  ? 3695 ARG A NH1   1 
ATOM   15570 N  NH2   . ARG A 1 3695 ? 155.434 157.207 195.286 1.00 16.76  ? 3695 ARG A NH2   1 
ATOM   15571 N  N     . VAL A 1 3696 ? 156.590 148.409 195.755 1.00 15.38  ? 3696 VAL A N     1 
ATOM   15572 C  CA    . VAL A 1 3696 ? 156.236 147.050 195.376 1.00 11.77  ? 3696 VAL A CA    1 
ATOM   15573 C  C     . VAL A 1 3696 ? 157.464 146.163 195.507 1.00 14.48  ? 3696 VAL A C     1 
ATOM   15574 O  O     . VAL A 1 3696 ? 158.603 146.633 195.525 1.00 21.53  ? 3696 VAL A O     1 
ATOM   15575 C  CB    . VAL A 1 3696 ? 155.677 146.964 193.939 1.00 11.49  ? 3696 VAL A CB    1 
ATOM   15576 C  CG1   . VAL A 1 3696 ? 154.432 147.825 193.793 1.00 14.53  ? 3696 VAL A CG1   1 
ATOM   15577 C  CG2   . VAL A 1 3696 ? 156.742 147.363 192.935 1.00 11.16  ? 3696 VAL A CG2   1 
ATOM   15578 N  N     . THR A 1 3697 ? 157.213 144.861 195.604 1.00 13.21  ? 3697 THR A N     1 
ATOM   15579 C  CA    . THR A 1 3697 ? 158.262 143.850 195.550 1.00 11.45  ? 3697 THR A CA    1 
ATOM   15580 C  C     . THR A 1 3697 ? 158.163 143.135 194.205 1.00 12.04  ? 3697 THR A C     1 
ATOM   15581 O  O     . THR A 1 3697 ? 157.107 142.606 193.845 1.00 12.27  ? 3697 THR A O     1 
ATOM   15582 C  CB    . THR A 1 3697 ? 158.171 142.883 196.734 1.00 13.71  ? 3697 THR A CB    1 
ATOM   15583 O  OG1   . THR A 1 3697 ? 159.308 142.010 196.734 1.00 30.26  ? 3697 THR A OG1   1 
ATOM   15584 C  CG2   . THR A 1 3697 ? 156.875 142.068 196.739 1.00 11.01  ? 3697 THR A CG2   1 
ATOM   15585 N  N     . PHE A 1 3698 ? 159.248 143.172 193.440 1.00 13.68  ? 3698 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3698 ? 159.249 142.568 192.117 1.00 10.47  ? 3698 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3698 ? 159.288 141.050 192.216 1.00 11.57  ? 3698 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3698 ? 159.968 140.484 193.075 1.00 13.55  ? 3698 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3698 ? 160.435 143.081 191.304 1.00 9.79   ? 3698 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3698 ? 160.352 144.542 190.972 1.00 11.83  ? 3698 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3698 ? 159.455 144.998 190.022 1.00 16.28  ? 3698 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3698 ? 161.164 145.460 191.615 1.00 11.08  ? 3698 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3698 ? 159.374 146.340 189.713 1.00 12.33  ? 3698 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3698 ? 161.084 146.804 191.312 1.00 15.72  ? 3698 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3698 ? 160.187 147.244 190.359 1.00 14.87  ? 3698 PHE A CZ    1 
ATOM   15596 N  N     . VAL A 1 3699 ? 158.533 140.392 191.341 1.00 13.17  ? 3699 VAL A N     1 
ATOM   15597 C  CA    . VAL A 1 3699 ? 158.516 138.938 191.228 1.00 10.65  ? 3699 VAL A CA    1 
ATOM   15598 C  C     . VAL A 1 3699 ? 158.721 138.629 189.750 1.00 10.81  ? 3699 VAL A C     1 
ATOM   15599 O  O     . VAL A 1 3699 ? 157.767 138.652 188.965 1.00 13.10  ? 3699 VAL A O     1 
ATOM   15600 C  CB    . VAL A 1 3699 ? 157.216 138.318 191.751 1.00 11.27  ? 3699 VAL A CB    1 
ATOM   15601 C  CG1   . VAL A 1 3699 ? 157.354 136.817 191.845 1.00 10.63  ? 3699 VAL A CG1   1 
ATOM   15602 C  CG2   . VAL A 1 3699 ? 156.855 138.900 193.107 1.00 13.71  ? 3699 VAL A CG2   1 
ATOM   15603 N  N     . ASN A 1 3700 ? 159.961 138.342 189.366 1.00 9.77   ? 3700 ASN A N     1 
ATOM   15604 C  CA    . ASN A 1 3700 ? 160.327 138.174 187.964 1.00 10.74  ? 3700 ASN A CA    1 
ATOM   15605 C  C     . ASN A 1 3700 ? 160.186 136.706 187.577 1.00 11.90  ? 3700 ASN A C     1 
ATOM   15606 O  O     . ASN A 1 3700 ? 160.915 135.849 188.085 1.00 12.48  ? 3700 ASN A O     1 
ATOM   15607 C  CB    . ASN A 1 3700 ? 161.749 138.672 187.726 1.00 11.12  ? 3700 ASN A CB    1 
ATOM   15608 C  CG    . ASN A 1 3700 ? 161.961 139.171 186.316 1.00 12.45  ? 3700 ASN A CG    1 
ATOM   15609 O  OD1   . ASN A 1 3700 ? 161.164 138.895 185.422 1.00 16.39  ? 3700 ASN A OD1   1 
ATOM   15610 N  ND2   . ASN A 1 3700 ? 163.038 139.917 186.111 1.00 10.48  ? 3700 ASN A ND2   1 
ATOM   15611 N  N     . PHE A 1 3701 ? 159.251 136.419 186.671 1.00 11.51  ? 3701 PHE A N     1 
ATOM   15612 C  CA    . PHE A 1 3701 ? 159.046 135.064 186.160 1.00 8.65   ? 3701 PHE A CA    1 
ATOM   15613 C  C     . PHE A 1 3701 ? 159.836 134.913 184.864 1.00 13.94  ? 3701 PHE A C     1 
ATOM   15614 O  O     . PHE A 1 3701 ? 159.301 134.978 183.755 1.00 16.52  ? 3701 PHE A O     1 
ATOM   15615 C  CB    . PHE A 1 3701 ? 157.564 134.785 185.947 1.00 11.94  ? 3701 PHE A CB    1 
ATOM   15616 C  CG    . PHE A 1 3701 ? 156.815 134.471 187.208 1.00 11.25  ? 3701 PHE A CG    1 
ATOM   15617 C  CD1   . PHE A 1 3701 ? 156.366 135.486 188.033 1.00 11.00  ? 3701 PHE A CD1   1 
ATOM   15618 C  CD2   . PHE A 1 3701 ? 156.547 133.160 187.559 1.00 7.11   ? 3701 PHE A CD2   1 
ATOM   15619 C  CE1   . PHE A 1 3701 ? 155.671 135.199 189.189 1.00 9.73   ? 3701 PHE A CE1   1 
ATOM   15620 C  CE2   . PHE A 1 3701 ? 155.853 132.868 188.714 1.00 9.77   ? 3701 PHE A CE2   1 
ATOM   15621 C  CZ    . PHE A 1 3701 ? 155.413 133.888 189.528 1.00 11.27  ? 3701 PHE A CZ    1 
ATOM   15622 N  N     . THR A 1 3702 ? 161.138 134.711 185.015 1.00 16.73  ? 3702 THR A N     1 
ATOM   15623 C  CA    . THR A 1 3702 ? 162.012 134.512 183.871 1.00 10.79  ? 3702 THR A CA    1 
ATOM   15624 C  C     . THR A 1 3702 ? 162.078 133.034 183.498 1.00 11.05  ? 3702 THR A C     1 
ATOM   15625 O  O     . THR A 1 3702 ? 161.647 132.153 184.244 1.00 13.27  ? 3702 THR A O     1 
ATOM   15626 C  CB    . THR A 1 3702 ? 163.414 135.049 184.162 1.00 10.62  ? 3702 THR A CB    1 
ATOM   15627 O  OG1   . THR A 1 3702 ? 163.973 134.352 185.282 1.00 17.98  ? 3702 THR A OG1   1 
ATOM   15628 C  CG2   . THR A 1 3702 ? 163.361 136.534 184.468 1.00 11.24  ? 3702 THR A CG2   1 
ATOM   15629 N  N     . VAL A 1 3703 ? 162.625 132.771 182.317 1.00 12.90  ? 3703 VAL A N     1 
ATOM   15630 C  CA    . VAL A 1 3703 ? 162.785 131.418 181.800 1.00 11.78  ? 3703 VAL A CA    1 
ATOM   15631 C  C     . VAL A 1 3703 ? 164.187 130.936 182.140 1.00 14.47  ? 3703 VAL A C     1 
ATOM   15632 O  O     . VAL A 1 3703 ? 165.176 131.612 181.834 1.00 12.15  ? 3703 VAL A O     1 
ATOM   15633 C  CB    . VAL A 1 3703 ? 162.536 131.368 180.283 1.00 12.22  ? 3703 VAL A CB    1 
ATOM   15634 C  CG1   . VAL A 1 3703 ? 162.633 129.940 179.773 1.00 13.38  ? 3703 VAL A CG1   1 
ATOM   15635 C  CG2   . VAL A 1 3703 ? 161.180 131.965 179.952 1.00 15.71  ? 3703 VAL A CG2   1 
ATOM   15636 N  N     . THR A 1 3704 ? 164.274 129.775 182.776 1.00 15.56  ? 3704 THR A N     1 
ATOM   15637 C  CA    . THR A 1 3704 ? 165.547 129.181 183.148 1.00 14.05  ? 3704 THR A CA    1 
ATOM   15638 C  C     . THR A 1 3704 ? 165.927 128.086 182.159 1.00 17.64  ? 3704 THR A C     1 
ATOM   15639 O  O     . THR A 1 3704 ? 165.088 127.560 181.424 1.00 19.19  ? 3704 THR A O     1 
ATOM   15640 C  CB    . THR A 1 3704 ? 165.490 128.603 184.564 1.00 17.81  ? 3704 THR A CB    1 
ATOM   15641 O  OG1   . THR A 1 3704 ? 164.719 127.397 184.557 1.00 15.43  ? 3704 THR A OG1   1 
ATOM   15642 C  CG2   . THR A 1 3704 ? 164.850 129.599 185.519 1.00 18.84  ? 3704 THR A CG2   1 
ATOM   15643 N  N     . ARG A 1 3705 ? 167.219 127.754 182.145 1.00 18.93  ? 3705 ARG A N     1 
ATOM   15644 C  CA    . ARG A 1 3705 ? 167.694 126.697 181.259 1.00 12.57  ? 3705 ARG A CA    1 
ATOM   15645 C  C     . ARG A 1 3705 ? 167.090 125.351 181.630 1.00 15.34  ? 3705 ARG A C     1 
ATOM   15646 O  O     . ARG A 1 3705 ? 166.628 124.608 180.757 1.00 20.15  ? 3705 ARG A O     1 
ATOM   15647 C  CB    . ARG A 1 3705 ? 169.220 126.630 181.292 1.00 13.45  ? 3705 ARG A CB    1 
ATOM   15648 C  CG    . ARG A 1 3705 ? 169.884 127.506 180.252 1.00 18.35  ? 3705 ARG A CG    1 
ATOM   15649 C  CD    . ARG A 1 3705 ? 171.269 127.950 180.675 1.00 23.25  ? 3705 ARG A CD    1 
ATOM   15650 N  NE    . ARG A 1 3705 ? 171.616 129.236 180.082 1.00 24.42  ? 3705 ARG A NE    1 
ATOM   15651 C  CZ    . ARG A 1 3705 ? 172.035 129.397 178.835 1.00 31.89  ? 3705 ARG A CZ    1 
ATOM   15652 N  NH1   . ARG A 1 3705 ? 172.177 128.369 178.015 1.00 33.56  ? 3705 ARG A NH1   1 
ATOM   15653 N  NH2   . ARG A 1 3705 ? 172.316 130.621 178.399 1.00 27.44  ? 3705 ARG A NH2   1 
ATOM   15654 N  N     . SER A 1 3706 ? 167.072 125.025 182.924 1.00 15.56  ? 3706 SER A N     1 
ATOM   15655 C  CA    . SER A 1 3706 ? 166.563 123.729 183.359 1.00 12.94  ? 3706 SER A CA    1 
ATOM   15656 C  C     . SER A 1 3706 ? 165.077 123.578 183.053 1.00 16.48  ? 3706 SER A C     1 
ATOM   15657 O  O     . SER A 1 3706 ? 164.639 122.518 182.591 1.00 21.00  ? 3706 SER A O     1 
ATOM   15658 C  CB    . SER A 1 3706 ? 166.826 123.544 184.851 1.00 16.86  ? 3706 SER A CB    1 
ATOM   15659 O  OG    . SER A 1 3706 ? 166.345 124.652 185.590 1.00 22.19  ? 3706 SER A OG    1 
ATOM   15660 N  N     . SER A 1 3707 ? 164.286 124.623 183.309 1.00 16.25  ? 3707 SER A N     1 
ATOM   15661 C  CA    . SER A 1 3707 ? 162.853 124.537 183.052 1.00 14.62  ? 3707 SER A CA    1 
ATOM   15662 C  C     . SER A 1 3707 ? 162.569 124.373 181.567 1.00 17.44  ? 3707 SER A C     1 
ATOM   15663 O  O     . SER A 1 3707 ? 161.696 123.590 181.176 1.00 29.03  ? 3707 SER A O     1 
ATOM   15664 C  CB    . SER A 1 3707 ? 162.142 125.774 183.600 1.00 15.52  ? 3707 SER A CB    1 
ATOM   15665 O  OG    . SER A 1 3707 ? 162.515 126.936 182.883 1.00 22.42  ? 3707 SER A OG    1 
ATOM   15666 N  N     . LEU A 1 3708 ? 163.297 125.104 180.721 1.00 15.46  ? 3708 LEU A N     1 
ATOM   15667 C  CA    . LEU A 1 3708 ? 163.099 124.968 179.283 1.00 11.85  ? 3708 LEU A CA    1 
ATOM   15668 C  C     . LEU A 1 3708 ? 163.528 123.592 178.792 1.00 15.57  ? 3708 LEU A C     1 
ATOM   15669 O  O     . LEU A 1 3708 ? 162.874 123.011 177.920 1.00 21.88  ? 3708 LEU A O     1 
ATOM   15670 C  CB    . LEU A 1 3708 ? 163.857 126.063 178.538 1.00 13.16  ? 3708 LEU A CB    1 
ATOM   15671 C  CG    . LEU A 1 3708 ? 163.529 126.120 177.048 1.00 11.41  ? 3708 LEU A CG    1 
ATOM   15672 C  CD1   . LEU A 1 3708 ? 162.067 126.469 176.835 1.00 11.44  ? 3708 LEU A CD1   1 
ATOM   15673 C  CD2   . LEU A 1 3708 ? 164.423 127.114 176.356 1.00 9.58   ? 3708 LEU A CD2   1 
ATOM   15674 N  N     . GLN A 1 3709 ? 164.628 123.059 179.330 1.00 16.47  ? 3709 GLN A N     1 
ATOM   15675 C  CA    . GLN A 1 3709 ? 165.035 121.704 178.970 1.00 13.89  ? 3709 GLN A CA    1 
ATOM   15676 C  C     . GLN A 1 3709 ? 163.972 120.689 179.363 1.00 17.97  ? 3709 GLN A C     1 
ATOM   15677 O  O     . GLN A 1 3709 ? 163.658 119.779 178.589 1.00 25.95  ? 3709 GLN A O     1 
ATOM   15678 C  CB    . GLN A 1 3709 ? 166.371 121.357 179.625 1.00 14.60  ? 3709 GLN A CB    1 
ATOM   15679 C  CG    . GLN A 1 3709 ? 167.545 122.162 179.111 1.00 19.43  ? 3709 GLN A CG    1 
ATOM   15680 C  CD    . GLN A 1 3709 ? 168.842 121.801 179.799 1.00 26.56  ? 3709 GLN A CD    1 
ATOM   15681 O  OE1   . GLN A 1 3709 ? 168.862 120.984 180.719 1.00 36.20  ? 3709 GLN A OE1   1 
ATOM   15682 N  NE2   . GLN A 1 3709 ? 169.935 122.412 179.359 1.00 23.29  ? 3709 GLN A NE2   1 
ATOM   15683 N  N     . SER A 1 3710 ? 163.404 120.831 180.563 1.00 16.91  ? 3710 SER A N     1 
ATOM   15684 C  CA    . SER A 1 3710 ? 162.345 119.922 180.989 1.00 18.74  ? 3710 SER A CA    1 
ATOM   15685 C  C     . SER A 1 3710 ? 161.122 120.041 180.088 1.00 19.44  ? 3710 SER A C     1 
ATOM   15686 O  O     . SER A 1 3710 ? 160.521 119.029 179.708 1.00 28.78  ? 3710 SER A O     1 
ATOM   15687 C  CB    . SER A 1 3710 ? 161.970 120.199 182.444 1.00 19.35  ? 3710 SER A CB    1 
ATOM   15688 O  OG    . SER A 1 3710 ? 162.940 119.669 183.329 1.00 25.15  ? 3710 SER A OG    1 
ATOM   15689 N  N     . GLN A 1 3711 ? 160.742 121.270 179.735 1.00 14.63  ? 3711 GLN A N     1 
ATOM   15690 C  CA    . GLN A 1 3711 ? 159.586 121.478 178.868 1.00 16.61  ? 3711 GLN A CA    1 
ATOM   15691 C  C     . GLN A 1 3711 ? 159.804 120.847 177.499 1.00 18.90  ? 3711 GLN A C     1 
ATOM   15692 O  O     . GLN A 1 3711 ? 158.920 120.164 176.966 1.00 23.55  ? 3711 GLN A O     1 
ATOM   15693 C  CB    . GLN A 1 3711 ? 159.307 122.975 178.734 1.00 21.92  ? 3711 GLN A CB    1 
ATOM   15694 C  CG    . GLN A 1 3711 ? 158.010 123.319 178.028 1.00 32.04  ? 3711 GLN A CG    1 
ATOM   15695 C  CD    . GLN A 1 3711 ? 157.666 124.791 178.136 1.00 39.64  ? 3711 GLN A CD    1 
ATOM   15696 O  OE1   . GLN A 1 3711 ? 158.477 125.597 178.590 1.00 34.18  ? 3711 GLN A OE1   1 
ATOM   15697 N  NE2   . GLN A 1 3711 ? 156.459 125.151 177.714 1.00 35.56  ? 3711 GLN A NE2   1 
ATOM   15698 N  N     . CYS A 1 3712 ? 160.986 121.059 176.916 1.00 17.63  ? 3712 CYS A N     1 
ATOM   15699 C  CA    . CYS A 1 3712 ? 161.275 120.505 175.598 1.00 16.12  ? 3712 CYS A CA    1 
ATOM   15700 C  C     . CYS A 1 3712 ? 161.354 118.984 175.638 1.00 17.41  ? 3712 CYS A C     1 
ATOM   15701 O  O     . CYS A 1 3712 ? 160.890 118.311 174.711 1.00 22.08  ? 3712 CYS A O     1 
ATOM   15702 C  CB    . CYS A 1 3712 ? 162.569 121.105 175.053 1.00 15.15  ? 3712 CYS A CB    1 
ATOM   15703 S  SG    . CYS A 1 3712 ? 162.463 122.878 174.722 1.00 23.80  ? 3712 CYS A SG    1 
ATOM   15704 N  N     . LEU A 1 3713 ? 161.936 118.424 176.703 1.00 16.93  ? 3713 LEU A N     1 
ATOM   15705 C  CA    . LEU A 1 3713 ? 161.984 116.973 176.839 1.00 17.96  ? 3713 LEU A CA    1 
ATOM   15706 C  C     . LEU A 1 3713 ? 160.585 116.387 176.963 1.00 20.66  ? 3713 LEU A C     1 
ATOM   15707 O  O     . LEU A 1 3713 ? 160.271 115.369 176.336 1.00 23.79  ? 3713 LEU A O     1 
ATOM   15708 C  CB    . LEU A 1 3713 ? 162.838 116.588 178.046 1.00 19.28  ? 3713 LEU A CB    1 
ATOM   15709 C  CG    . LEU A 1 3713 ? 162.955 115.096 178.365 1.00 22.91  ? 3713 LEU A CG    1 
ATOM   15710 C  CD1   . LEU A 1 3713 ? 163.385 114.314 177.137 1.00 21.59  ? 3713 LEU A CD1   1 
ATOM   15711 C  CD2   . LEU A 1 3713 ? 163.921 114.865 179.513 1.00 21.53  ? 3713 LEU A CD2   1 
ATOM   15712 N  N     . ASN A 1 3714 ? 159.725 117.020 177.764 1.00 20.05  ? 3714 ASN A N     1 
ATOM   15713 C  CA    . ASN A 1 3714 ? 158.354 116.540 177.888 1.00 23.37  ? 3714 ASN A CA    1 
ATOM   15714 C  C     . ASN A 1 3714 ? 157.625 116.619 176.554 1.00 23.50  ? 3714 ASN A C     1 
ATOM   15715 O  O     . ASN A 1 3714 ? 156.895 115.692 176.180 1.00 29.23  ? 3714 ASN A O     1 
ATOM   15716 C  CB    . ASN A 1 3714 ? 157.613 117.341 178.957 1.00 25.73  ? 3714 ASN A CB    1 
ATOM   15717 C  CG    . ASN A 1 3714 ? 157.893 116.838 180.357 1.00 34.02  ? 3714 ASN A CG    1 
ATOM   15718 O  OD1   . ASN A 1 3714 ? 159.045 116.754 180.780 1.00 32.06  ? 3714 ASN A OD1   1 
ATOM   15719 N  ND2   . ASN A 1 3714 ? 156.836 116.502 181.087 1.00 44.65  ? 3714 ASN A ND2   1 
ATOM   15720 N  N     . GLU A 1 3715 ? 157.818 117.715 175.817 1.00 20.84  ? 3715 GLU A N     1 
ATOM   15721 C  CA    . GLU A 1 3715 ? 157.146 117.866 174.530 1.00 26.12  ? 3715 GLU A CA    1 
ATOM   15722 C  C     . GLU A 1 3715 ? 157.617 116.813 173.531 1.00 24.90  ? 3715 GLU A C     1 
ATOM   15723 O  O     . GLU A 1 3715 ? 156.799 116.221 172.816 1.00 24.74  ? 3715 GLU A O     1 
ATOM   15724 C  CB    . GLU A 1 3715 ? 157.376 119.276 173.986 1.00 23.53  ? 3715 GLU A CB    1 
ATOM   15725 C  CG    . GLU A 1 3715 ? 156.508 119.638 172.795 1.00 32.02  ? 3715 GLU A CG    1 
ATOM   15726 C  CD    . GLU A 1 3715 ? 155.032 119.678 173.142 1.00 46.75  ? 3715 GLU A CD    1 
ATOM   15727 O  OE1   . GLU A 1 3715 ? 154.701 120.000 174.302 1.00 47.25  ? 3715 GLU A OE1   1 
ATOM   15728 O  OE2   . GLU A 1 3715 ? 154.202 119.387 172.255 1.00 51.32  ? 3715 GLU A OE2   1 
ATOM   15729 N  N     . VAL A 1 3716 ? 158.927 116.555 173.472 1.00 23.86  ? 3716 VAL A N     1 
ATOM   15730 C  CA    . VAL A 1 3716 ? 159.429 115.571 172.518 1.00 22.95  ? 3716 VAL A CA    1 
ATOM   15731 C  C     . VAL A 1 3716 ? 159.015 114.159 172.917 1.00 26.25  ? 3716 VAL A C     1 
ATOM   15732 O  O     . VAL A 1 3716 ? 158.759 113.318 172.049 1.00 28.69  ? 3716 VAL A O     1 
ATOM   15733 C  CB    . VAL A 1 3716 ? 160.957 115.693 172.340 1.00 21.15  ? 3716 VAL A CB    1 
ATOM   15734 C  CG1   . VAL A 1 3716 ? 161.703 115.265 173.585 1.00 21.16  ? 3716 VAL A CG1   1 
ATOM   15735 C  CG2   . VAL A 1 3716 ? 161.414 114.883 171.138 1.00 22.23  ? 3716 VAL A CG2   1 
ATOM   15736 N  N     . LEU A 1 3717 ? 158.937 113.863 174.219 1.00 28.77  ? 3717 LEU A N     1 
ATOM   15737 C  CA    . LEU A 1 3717 ? 158.454 112.547 174.623 1.00 29.57  ? 3717 LEU A CA    1 
ATOM   15738 C  C     . LEU A 1 3717 ? 156.975 112.381 174.304 1.00 30.89  ? 3717 LEU A C     1 
ATOM   15739 O  O     . LEU A 1 3717 ? 156.542 111.297 173.900 1.00 36.51  ? 3717 LEU A O     1 
ATOM   15740 C  CB    . LEU A 1 3717 ? 158.716 112.307 176.110 1.00 28.19  ? 3717 LEU A CB    1 
ATOM   15741 C  CG    . LEU A 1 3717 ? 160.183 112.211 176.528 1.00 34.03  ? 3717 LEU A CG    1 
ATOM   15742 C  CD1   . LEU A 1 3717 ? 160.307 112.112 178.042 1.00 33.41  ? 3717 LEU A CD1   1 
ATOM   15743 C  CD2   . LEU A 1 3717 ? 160.837 111.020 175.853 1.00 36.15  ? 3717 LEU A CD2   1 
ATOM   15744 N  N     . LYS A 1 3718 ? 156.184 113.441 174.473 1.00 32.72  ? 3718 LYS A N     1 
ATOM   15745 C  CA    . LYS A 1 3718 ? 154.776 113.368 174.099 1.00 35.07  ? 3718 LYS A CA    1 
ATOM   15746 C  C     . LYS A 1 3718 ? 154.616 113.172 172.596 1.00 36.72  ? 3718 LYS A C     1 
ATOM   15747 O  O     . LYS A 1 3718 ? 153.738 112.425 172.151 1.00 40.08  ? 3718 LYS A O     1 
ATOM   15748 C  CB    . LYS A 1 3718 ? 154.042 114.625 174.564 1.00 32.64  ? 3718 LYS A CB    1 
ATOM   15749 C  CG    . LYS A 1 3718 ? 152.556 114.626 174.256 1.00 39.24  ? 3718 LYS A CG    1 
ATOM   15750 C  CD    . LYS A 1 3718 ? 151.864 115.831 174.869 1.00 44.44  ? 3718 LYS A CD    1 
ATOM   15751 C  CE    . LYS A 1 3718 ? 152.232 117.110 174.140 1.00 48.96  ? 3718 LYS A CE    1 
ATOM   15752 N  NZ    . LYS A 1 3718 ? 151.670 117.138 172.762 1.00 59.32  ? 3718 LYS A NZ    1 
ATOM   15753 N  N     . ALA A 1 3719 ? 155.456 113.837 171.800 1.00 37.57  ? 3719 ALA A N     1 
ATOM   15754 C  CA    . ALA A 1 3719 ? 155.335 113.739 170.348 1.00 31.63  ? 3719 ALA A CA    1 
ATOM   15755 C  C     . ALA A 1 3719 ? 155.805 112.384 169.829 1.00 29.75  ? 3719 ALA A C     1 
ATOM   15756 O  O     . ALA A 1 3719 ? 155.144 111.777 168.978 1.00 34.81  ? 3719 ALA A O     1 
ATOM   15757 C  CB    . ALA A 1 3719 ? 156.119 114.868 169.682 1.00 26.10  ? 3719 ALA A CB    1 
ATOM   15758 N  N     . GLU A 1 3720 ? 156.940 111.891 170.324 1.00 31.08  ? 3720 GLU A N     1 
ATOM   15759 C  CA    . GLU A 1 3720 ? 157.570 110.703 169.759 1.00 31.64  ? 3720 GLU A CA    1 
ATOM   15760 C  C     . GLU A 1 3720 ? 157.140 109.413 170.447 1.00 36.60  ? 3720 GLU A C     1 
ATOM   15761 O  O     . GLU A 1 3720 ? 156.949 108.393 169.778 1.00 40.58  ? 3720 GLU A O     1 
ATOM   15762 C  CB    . GLU A 1 3720 ? 159.093 110.838 169.827 1.00 32.82  ? 3720 GLU A CB    1 
ATOM   15763 C  CG    . GLU A 1 3720 ? 159.663 111.840 168.843 1.00 37.23  ? 3720 GLU A CG    1 
ATOM   15764 C  CD    . GLU A 1 3720 ? 159.290 111.519 167.411 1.00 40.18  ? 3720 GLU A CD    1 
ATOM   15765 O  OE1   . GLU A 1 3720 ? 159.736 110.469 166.904 1.00 38.45  ? 3720 GLU A OE1   1 
ATOM   15766 O  OE2   . GLU A 1 3720 ? 158.550 112.313 166.794 1.00 38.58  ? 3720 GLU A OE2   1 
ATOM   15767 N  N     . ARG A 1 3721 ? 156.985 109.432 171.768 1.00 37.26  ? 3721 ARG A N     1 
ATOM   15768 C  CA    . ARG A 1 3721 ? 156.613 108.249 172.543 1.00 37.33  ? 3721 ARG A CA    1 
ATOM   15769 C  C     . ARG A 1 3721 ? 155.402 108.588 173.400 1.00 38.03  ? 3721 ARG A C     1 
ATOM   15770 O  O     . ARG A 1 3721 ? 155.513 108.745 174.622 1.00 40.56  ? 3721 ARG A O     1 
ATOM   15771 C  CB    . ARG A 1 3721 ? 157.783 107.770 173.404 1.00 34.74  ? 3721 ARG A CB    1 
ATOM   15772 C  CG    . ARG A 1 3721 ? 159.080 107.553 172.639 1.00 31.64  ? 3721 ARG A CG    1 
ATOM   15773 C  CD    . ARG A 1 3721 ? 159.019 106.301 171.780 1.00 42.55  ? 3721 ARG A CD    1 
ATOM   15774 N  NE    . ARG A 1 3721 ? 159.585 105.139 172.454 1.00 48.56  ? 3721 ARG A NE    1 
ATOM   15775 C  CZ    . ARG A 1 3721 ? 160.884 104.903 172.582 1.00 43.81  ? 3721 ARG A CZ    1 
ATOM   15776 N  NH1   . ARG A 1 3721 ? 161.789 105.731 172.086 1.00 38.78  ? 3721 ARG A NH1   1 
ATOM   15777 N  NH2   . ARG A 1 3721 ? 161.284 103.808 173.220 1.00 35.98  ? 3721 ARG A NH2   1 
ATOM   15778 N  N     . PRO A 1 3722 ? 154.223 108.720 172.783 1.00 37.38  ? 3722 PRO A N     1 
ATOM   15779 C  CA    . PRO A 1 3722 ? 153.035 109.122 173.559 1.00 40.57  ? 3722 PRO A CA    1 
ATOM   15780 C  C     . PRO A 1 3722 ? 152.688 108.162 174.683 1.00 43.66  ? 3722 PRO A C     1 
ATOM   15781 O  O     . PRO A 1 3722 ? 152.244 108.601 175.752 1.00 46.35  ? 3722 PRO A O     1 
ATOM   15782 C  CB    . PRO A 1 3722 ? 151.930 109.181 172.495 1.00 40.64  ? 3722 PRO A CB    1 
ATOM   15783 C  CG    . PRO A 1 3722 ? 152.411 108.289 171.396 1.00 38.46  ? 3722 PRO A CG    1 
ATOM   15784 C  CD    . PRO A 1 3722 ? 153.898 108.442 171.375 1.00 34.41  ? 3722 PRO A CD    1 
ATOM   15785 N  N     . ASP A 1 3723 ? 152.880 106.857 174.473 1.00 44.80  ? 3723 ASP A N     1 
ATOM   15786 C  CA    . ASP A 1 3723 ? 152.615 105.896 175.538 1.00 45.30  ? 3723 ASP A CA    1 
ATOM   15787 C  C     . ASP A 1 3723 ? 153.553 106.114 176.718 1.00 48.60  ? 3723 ASP A C     1 
ATOM   15788 O  O     . ASP A 1 3723 ? 153.125 106.072 177.877 1.00 55.37  ? 3723 ASP A O     1 
ATOM   15789 C  CB    . ASP A 1 3723 ? 152.736 104.469 175.002 1.00 42.84  ? 3723 ASP A CB    1 
ATOM   15790 C  CG    . ASP A 1 3723 ? 154.101 104.181 174.411 1.00 47.16  ? 3723 ASP A CG    1 
ATOM   15791 O  OD1   . ASP A 1 3723 ? 154.630 105.046 173.682 1.00 45.51  ? 3723 ASP A OD1   1 
ATOM   15792 O  OD2   . ASP A 1 3723 ? 154.645 103.089 174.676 1.00 49.09  ? 3723 ASP A OD2   1 
ATOM   15793 N  N     . VAL A 1 3724 ? 154.834 106.368 176.441 1.00 41.38  ? 3724 VAL A N     1 
ATOM   15794 C  CA    . VAL A 1 3724 ? 155.794 106.612 177.514 1.00 41.21  ? 3724 VAL A CA    1 
ATOM   15795 C  C     . VAL A 1 3724 ? 155.456 107.903 178.249 1.00 48.50  ? 3724 VAL A C     1 
ATOM   15796 O  O     . VAL A 1 3724 ? 155.585 107.988 179.475 1.00 54.19  ? 3724 VAL A O     1 
ATOM   15797 C  CB    . VAL A 1 3724 ? 157.228 106.632 176.953 1.00 40.43  ? 3724 VAL A CB    1 
ATOM   15798 C  CG1   . VAL A 1 3724 ? 158.234 106.893 178.062 1.00 37.26  ? 3724 VAL A CG1   1 
ATOM   15799 C  CG2   . VAL A 1 3724 ? 157.536 105.323 176.248 1.00 37.77  ? 3724 VAL A CG2   1 
ATOM   15800 N  N     . ASP A 1 3725 ? 155.024 108.931 177.513 1.00 47.71  ? 3725 ASP A N     1 
ATOM   15801 C  CA    . ASP A 1 3725 ? 154.652 110.191 178.151 1.00 46.02  ? 3725 ASP A CA    1 
ATOM   15802 C  C     . ASP A 1 3725 ? 153.430 110.022 179.047 1.00 52.79  ? 3725 ASP A C     1 
ATOM   15803 O  O     . ASP A 1 3725 ? 153.387 110.556 180.162 1.00 63.52  ? 3725 ASP A O     1 
ATOM   15804 C  CB    . ASP A 1 3725 ? 154.399 111.262 177.092 1.00 41.89  ? 3725 ASP A CB    1 
ATOM   15805 C  CG    . ASP A 1 3725 ? 153.876 112.555 177.687 1.00 56.00  ? 3725 ASP A CG    1 
ATOM   15806 O  OD1   . ASP A 1 3725 ? 154.541 113.108 178.588 1.00 52.72  ? 3725 ASP A OD1   1 
ATOM   15807 O  OD2   . ASP A 1 3725 ? 152.800 113.018 177.254 1.00 62.60  ? 3725 ASP A OD2   1 
ATOM   15808 N  N     . GLU A 1 3726 ? 152.424 109.282 178.580 1.00 52.84  ? 3726 GLU A N     1 
ATOM   15809 C  CA    . GLU A 1 3726 ? 151.248 109.048 179.409 1.00 51.83  ? 3726 GLU A CA    1 
ATOM   15810 C  C     . GLU A 1 3726 ? 151.614 108.220 180.636 1.00 52.55  ? 3726 GLU A C     1 
ATOM   15811 O  O     . GLU A 1 3726 ? 151.120 108.478 181.744 1.00 57.12  ? 3726 GLU A O     1 
ATOM   15812 C  CB    . GLU A 1 3726 ? 150.162 108.369 178.570 1.00 53.90  ? 3726 GLU A CB    1 
ATOM   15813 C  CG    . GLU A 1 3726 ? 148.781 108.273 179.208 1.00 65.76  ? 3726 GLU A CG    1 
ATOM   15814 C  CD    . GLU A 1 3726 ? 148.623 107.086 180.131 1.00 75.19  ? 3726 GLU A CD    1 
ATOM   15815 O  OE1   . GLU A 1 3726 ? 149.301 106.062 179.913 1.00 73.01  ? 3726 GLU A OE1   1 
ATOM   15816 O  OE2   . GLU A 1 3726 ? 147.795 107.175 181.061 1.00 73.89  ? 3726 GLU A OE2   1 
ATOM   15817 N  N     . LYS A 1 3727 ? 152.512 107.246 180.464 1.00 54.00  ? 3727 LYS A N     1 
ATOM   15818 C  CA    . LYS A 1 3727 ? 152.955 106.434 181.590 1.00 58.05  ? 3727 LYS A CA    1 
ATOM   15819 C  C     . LYS A 1 3727 ? 153.707 107.268 182.622 1.00 57.89  ? 3727 LYS A C     1 
ATOM   15820 O  O     . LYS A 1 3727 ? 153.487 107.111 183.827 1.00 67.38  ? 3727 LYS A O     1 
ATOM   15821 C  CB    . LYS A 1 3727 ? 153.824 105.279 181.092 1.00 54.99  ? 3727 LYS A CB    1 
ATOM   15822 C  CG    . LYS A 1 3727 ? 154.598 104.565 182.185 1.00 57.15  ? 3727 LYS A CG    1 
ATOM   15823 C  CD    . LYS A 1 3727 ? 155.515 103.504 181.603 1.00 60.15  ? 3727 LYS A CD    1 
ATOM   15824 C  CE    . LYS A 1 3727 ? 154.728 102.491 180.791 1.00 61.67  ? 3727 LYS A CE    1 
ATOM   15825 N  NZ    . LYS A 1 3727 ? 153.745 101.748 181.628 1.00 57.53  ? 3727 LYS A NZ    1 
ATOM   15826 N  N     . ARG A 1 3728 ? 154.598 108.160 182.179 1.00 52.15  ? 3728 ARG A N     1 
ATOM   15827 C  CA    . ARG A 1 3728 ? 155.310 108.998 183.142 1.00 54.33  ? 3728 ARG A CA    1 
ATOM   15828 C  C     . ARG A 1 3728 ? 154.368 109.982 183.823 1.00 57.58  ? 3728 ARG A C     1 
ATOM   15829 O  O     . ARG A 1 3728 ? 154.552 110.307 185.000 1.00 62.09  ? 3728 ARG A O     1 
ATOM   15830 C  CB    . ARG A 1 3728 ? 156.477 109.748 182.494 1.00 47.64  ? 3728 ARG A CB    1 
ATOM   15831 C  CG    . ARG A 1 3728 ? 156.112 110.623 181.322 1.00 53.33  ? 3728 ARG A CG    1 
ATOM   15832 C  CD    . ARG A 1 3728 ? 157.172 111.671 181.037 1.00 50.91  ? 3728 ARG A CD    1 
ATOM   15833 N  NE    . ARG A 1 3728 ? 157.186 112.691 182.080 1.00 47.24  ? 3728 ARG A NE    1 
ATOM   15834 C  CZ    . ARG A 1 3728 ? 158.282 113.247 182.578 1.00 46.70  ? 3728 ARG A CZ    1 
ATOM   15835 N  NH1   . ARG A 1 3728 ? 159.486 112.905 182.151 1.00 43.64  ? 3728 ARG A NH1   1 
ATOM   15836 N  NH2   . ARG A 1 3728 ? 158.165 114.172 183.526 1.00 54.65  ? 3728 ARG A NH2   1 
ATOM   15837 N  N     . SER A 1 3729 ? 153.359 110.481 183.104 1.00 53.44  ? 3729 SER A N     1 
ATOM   15838 C  CA    . SER A 1 3729 ? 152.375 111.341 183.755 1.00 53.80  ? 3729 SER A CA    1 
ATOM   15839 C  C     . SER A 1 3729 ? 151.644 110.587 184.862 1.00 59.03  ? 3729 SER A C     1 
ATOM   15840 O  O     . SER A 1 3729 ? 151.482 111.100 185.981 1.00 57.62  ? 3729 SER A O     1 
ATOM   15841 C  CB    . SER A 1 3729 ? 151.386 111.878 182.722 1.00 57.01  ? 3729 SER A CB    1 
ATOM   15842 O  OG    . SER A 1 3729 ? 152.066 112.476 181.632 1.00 59.81  ? 3729 SER A OG    1 
ATOM   15843 N  N     . ASP A 1 3730 ? 151.225 109.351 184.573 1.00 58.99  ? 3730 ASP A N     1 
ATOM   15844 C  CA    . ASP A 1 3730 ? 150.599 108.525 185.600 1.00 61.90  ? 3730 ASP A CA    1 
ATOM   15845 C  C     . ASP A 1 3730 ? 151.550 108.276 186.762 1.00 64.27  ? 3730 ASP A C     1 
ATOM   15846 O  O     . ASP A 1 3730 ? 151.137 108.289 187.925 1.00 69.00  ? 3730 ASP A O     1 
ATOM   15847 C  CB    . ASP A 1 3730 ? 150.140 107.195 185.006 1.00 63.29  ? 3730 ASP A CB    1 
ATOM   15848 C  CG    . ASP A 1 3730 ? 148.953 107.344 184.087 1.00 68.46  ? 3730 ASP A CG    1 
ATOM   15849 O  OD1   . ASP A 1 3730 ? 148.402 108.461 183.993 1.00 66.30  ? 3730 ASP A OD1   1 
ATOM   15850 O  OD2   . ASP A 1 3730 ? 148.563 106.332 183.469 1.00 69.95  ? 3730 ASP A OD2   1 
ATOM   15851 N  N     . LEU A 1 3731 ? 152.826 108.031 186.462 1.00 58.96  ? 3731 LEU A N     1 
ATOM   15852 C  CA    . LEU A 1 3731 ? 153.799 107.750 187.512 1.00 59.92  ? 3731 LEU A CA    1 
ATOM   15853 C  C     . LEU A 1 3731 ? 154.023 108.956 188.413 1.00 63.05  ? 3731 LEU A C     1 
ATOM   15854 O  O     . LEU A 1 3731 ? 154.118 108.808 189.635 1.00 67.44  ? 3731 LEU A O     1 
ATOM   15855 C  CB    . LEU A 1 3731 ? 155.115 107.287 186.895 1.00 62.80  ? 3731 LEU A CB    1 
ATOM   15856 C  CG    . LEU A 1 3731 ? 155.370 105.781 186.928 1.00 63.87  ? 3731 LEU A CG    1 
ATOM   15857 C  CD1   . LEU A 1 3731 ? 154.389 105.028 186.045 1.00 58.71  ? 3731 LEU A CD1   1 
ATOM   15858 C  CD2   . LEU A 1 3731 ? 156.790 105.508 186.498 1.00 66.17  ? 3731 LEU A CD2   1 
ATOM   15859 N  N     . LEU A 1 3732 ? 154.127 110.155 187.835 1.00 63.70  ? 3732 LEU A N     1 
ATOM   15860 C  CA    . LEU A 1 3732 ? 154.260 111.358 188.653 1.00 62.81  ? 3732 LEU A CA    1 
ATOM   15861 C  C     . LEU A 1 3732 ? 153.028 111.569 189.524 1.00 64.07  ? 3732 LEU A C     1 
ATOM   15862 O  O     . LEU A 1 3732 ? 153.146 111.900 190.711 1.00 62.41  ? 3732 LEU A O     1 
ATOM   15863 C  CB    . LEU A 1 3732 ? 154.517 112.588 187.780 1.00 54.89  ? 3732 LEU A CB    1 
ATOM   15864 C  CG    . LEU A 1 3732 ? 155.949 112.951 187.365 1.00 55.59  ? 3732 LEU A CG    1 
ATOM   15865 C  CD1   . LEU A 1 3732 ? 156.773 113.311 188.595 1.00 57.99  ? 3732 LEU A CD1   1 
ATOM   15866 C  CD2   . LEU A 1 3732 ? 156.639 111.862 186.574 1.00 55.44  ? 3732 LEU A CD2   1 
ATOM   15867 N  N     . LYS A 1 3733 ? 151.833 111.382 188.954 1.00 67.71  ? 3733 LYS A N     1 
ATOM   15868 C  CA    . LYS A 1 3733 ? 150.623 111.532 189.759 1.00 63.48  ? 3733 LYS A CA    1 
ATOM   15869 C  C     . LYS A 1 3733 ? 150.596 110.527 190.906 1.00 69.70  ? 3733 LYS A C     1 
ATOM   15870 O  O     . LYS A 1 3733 ? 150.289 110.884 192.054 1.00 72.59  ? 3733 LYS A O     1 
ATOM   15871 C  CB    . LYS A 1 3733 ? 149.383 111.378 188.880 1.00 60.12  ? 3733 LYS A CB    1 
ATOM   15872 C  CG    . LYS A 1 3733 ? 148.110 111.906 189.513 1.00 65.99  ? 3733 LYS A CG    1 
ATOM   15873 C  CD    . LYS A 1 3733 ? 147.985 113.409 189.327 1.00 67.58  ? 3733 LYS A CD    1 
ATOM   15874 C  CE    . LYS A 1 3733 ? 146.549 113.870 189.516 1.00 68.77  ? 3733 LYS A CE    1 
ATOM   15875 N  NZ    . LYS A 1 3733 ? 146.288 114.304 190.916 1.00 67.73  ? 3733 LYS A NZ    1 
ATOM   15876 N  N     . LEU A 1 3734 ? 150.934 109.269 190.615 1.00 68.86  ? 3734 LEU A N     1 
ATOM   15877 C  CA    . LEU A 1 3734 ? 150.931 108.235 191.643 1.00 68.43  ? 3734 LEU A CA    1 
ATOM   15878 C  C     . LEU A 1 3734 ? 151.968 108.521 192.718 1.00 69.73  ? 3734 LEU A C     1 
ATOM   15879 O  O     . LEU A 1 3734 ? 151.700 108.332 193.906 1.00 74.42  ? 3734 LEU A O     1 
ATOM   15880 C  CB    . LEU A 1 3734 ? 151.180 106.864 191.013 1.00 63.24  ? 3734 LEU A CB    1 
ATOM   15881 C  CG    . LEU A 1 3734 ? 149.955 105.998 190.712 1.00 71.68  ? 3734 LEU A CG    1 
ATOM   15882 C  CD1   . LEU A 1 3734 ? 148.902 106.779 189.936 1.00 72.75  ? 3734 LEU A CD1   1 
ATOM   15883 C  CD2   . LEU A 1 3734 ? 150.360 104.739 189.961 1.00 68.95  ? 3734 LEU A CD2   1 
ATOM   15884 N  N     . GLN A 1 3735 ? 153.160 108.972 192.322 1.00 67.00  ? 3735 GLN A N     1 
ATOM   15885 C  CA    . GLN A 1 3735 ? 154.203 109.271 193.297 1.00 62.12  ? 3735 GLN A CA    1 
ATOM   15886 C  C     . GLN A 1 3735 ? 153.808 110.440 194.189 1.00 63.09  ? 3735 GLN A C     1 
ATOM   15887 O  O     . GLN A 1 3735 ? 154.057 110.413 195.400 1.00 66.47  ? 3735 GLN A O     1 
ATOM   15888 C  CB    . GLN A 1 3735 ? 155.521 109.559 192.581 1.00 64.84  ? 3735 GLN A CB    1 
ATOM   15889 C  CG    . GLN A 1 3735 ? 156.230 108.319 192.068 1.00 68.04  ? 3735 GLN A CG    1 
ATOM   15890 C  CD    . GLN A 1 3735 ? 157.578 108.630 191.450 1.00 79.67  ? 3735 GLN A CD    1 
ATOM   15891 O  OE1   . GLN A 1 3735 ? 157.871 109.779 191.117 1.00 79.67  ? 3735 GLN A OE1   1 
ATOM   15892 N  NE2   . GLN A 1 3735 ? 158.407 107.605 191.289 1.00 74.82  ? 3735 GLN A NE2   1 
ATOM   15893 N  N     . GLY A 1 3736 ? 153.196 111.477 193.613 1.00 63.63  ? 3736 GLY A N     1 
ATOM   15894 C  CA    . GLY A 1 3736 ? 152.726 112.583 194.432 1.00 65.16  ? 3736 GLY A CA    1 
ATOM   15895 C  C     . GLY A 1 3736 ? 151.667 112.151 195.426 1.00 69.48  ? 3736 GLY A C     1 
ATOM   15896 O  O     . GLY A 1 3736 ? 151.733 112.487 196.614 1.00 67.31  ? 3736 GLY A O     1 
ATOM   15897 N  N     . GLU A 1 3737 ? 150.683 111.376 194.956 1.00 73.64  ? 3737 GLU A N     1 
ATOM   15898 C  CA    . GLU A 1 3737 ? 149.652 110.866 195.856 1.00 69.36  ? 3737 GLU A CA    1 
ATOM   15899 C  C     . GLU A 1 3737 ? 150.255 109.977 196.935 1.00 63.81  ? 3737 GLU A C     1 
ATOM   15900 O  O     . GLU A 1 3737 ? 149.832 110.018 198.095 1.00 69.27  ? 3737 GLU A O     1 
ATOM   15901 C  CB    . GLU A 1 3737 ? 148.596 110.100 195.061 1.00 70.99  ? 3737 GLU A CB    1 
ATOM   15902 C  CG    . GLU A 1 3737 ? 147.674 110.980 194.238 1.00 77.25  ? 3737 GLU A CG    1 
ATOM   15903 C  CD    . GLU A 1 3737 ? 146.785 110.177 193.311 1.00 89.62  ? 3737 GLU A CD    1 
ATOM   15904 O  OE1   . GLU A 1 3737 ? 146.914 108.935 193.292 1.00 85.69  ? 3737 GLU A OE1   1 
ATOM   15905 O  OE2   . GLU A 1 3737 ? 145.958 110.786 192.600 1.00 91.00  ? 3737 GLU A OE2   1 
ATOM   15906 N  N     . PHE A 1 3738 ? 151.255 109.175 196.573 1.00 64.04  ? 3738 PHE A N     1 
ATOM   15907 C  CA    . PHE A 1 3738 ? 151.854 108.235 197.511 1.00 68.69  ? 3738 PHE A CA    1 
ATOM   15908 C  C     . PHE A 1 3738 ? 152.644 108.966 198.589 1.00 69.64  ? 3738 PHE A C     1 
ATOM   15909 O  O     . PHE A 1 3738 ? 152.580 108.605 199.770 1.00 71.83  ? 3738 PHE A O     1 
ATOM   15910 C  CB    . PHE A 1 3738 ? 152.756 107.270 196.746 1.00 66.68  ? 3738 PHE A CB    1 
ATOM   15911 C  CG    . PHE A 1 3738 ? 152.013 106.160 196.061 1.00 69.95  ? 3738 PHE A CG    1 
ATOM   15912 C  CD1   . PHE A 1 3738 ? 150.632 106.083 196.131 1.00 66.97  ? 3738 PHE A CD1   1 
ATOM   15913 C  CD2   . PHE A 1 3738 ? 152.693 105.223 195.302 1.00 71.91  ? 3738 PHE A CD2   1 
ATOM   15914 C  CE1   . PHE A 1 3738 ? 149.946 105.074 195.485 1.00 67.09  ? 3738 PHE A CE1   1 
ATOM   15915 C  CE2   . PHE A 1 3738 ? 152.012 104.215 194.650 1.00 69.37  ? 3738 PHE A CE2   1 
ATOM   15916 C  CZ    . PHE A 1 3738 ? 150.637 104.140 194.742 1.00 69.03  ? 3738 PHE A CZ    1 
ATOM   15917 N  N     . GLN A 1 3739 ? 153.399 109.994 198.197 1.00 69.86  ? 3739 GLN A N     1 
ATOM   15918 C  CA    . GLN A 1 3739 ? 154.133 110.787 199.177 1.00 69.10  ? 3739 GLN A CA    1 
ATOM   15919 C  C     . GLN A 1 3739 ? 153.180 111.555 200.083 1.00 65.76  ? 3739 GLN A C     1 
ATOM   15920 O  O     . GLN A 1 3739 ? 153.421 111.672 201.292 1.00 66.81  ? 3739 GLN A O     1 
ATOM   15921 C  CB    . GLN A 1 3739 ? 155.097 111.737 198.468 1.00 68.31  ? 3739 GLN A CB    1 
ATOM   15922 C  CG    . GLN A 1 3739 ? 156.250 111.059 197.719 1.00 69.74  ? 3739 GLN A CG    1 
ATOM   15923 C  CD    . GLN A 1 3739 ? 157.267 110.364 198.621 1.00 76.19  ? 3739 GLN A CD    1 
ATOM   15924 O  OE1   . GLN A 1 3739 ? 156.945 109.882 199.707 1.00 72.01  ? 3739 GLN A OE1   1 
ATOM   15925 N  NE2   . GLN A 1 3739 ? 158.512 110.313 198.160 1.00 75.85  ? 3739 GLN A NE2   1 
ATOM   15926 N  N     . LEU A 1 3740 ? 152.085 112.079 199.520 1.00 65.54  ? 3740 LEU A N     1 
ATOM   15927 C  CA    . LEU A 1 3740 ? 151.073 112.720 200.353 1.00 59.93  ? 3740 LEU A CA    1 
ATOM   15928 C  C     . LEU A 1 3740 ? 150.485 111.735 201.354 1.00 64.58  ? 3740 LEU A C     1 
ATOM   15929 O  O     . LEU A 1 3740 ? 150.294 112.071 202.528 1.00 71.99  ? 3740 LEU A O     1 
ATOM   15930 C  CB    . LEU A 1 3740 ? 149.971 113.313 199.478 1.00 55.58  ? 3740 LEU A CB    1 
ATOM   15931 C  CG    . LEU A 1 3740 ? 148.799 113.955 200.223 1.00 56.21  ? 3740 LEU A CG    1 
ATOM   15932 C  CD1   . LEU A 1 3740 ? 149.096 115.409 200.538 1.00 57.96  ? 3740 LEU A CD1   1 
ATOM   15933 C  CD2   . LEU A 1 3740 ? 147.518 113.828 199.416 1.00 58.68  ? 3740 LEU A CD2   1 
ATOM   15934 N  N     . ARG A 1 3741 ? 150.193 110.512 200.906 1.00 66.40  ? 3741 ARG A N     1 
ATOM   15935 C  CA    . ARG A 1 3741 ? 149.648 109.499 201.802 1.00 67.61  ? 3741 ARG A CA    1 
ATOM   15936 C  C     . ARG A 1 3741 ? 150.637 109.144 202.905 1.00 66.04  ? 3741 ARG A C     1 
ATOM   15937 O  O     . ARG A 1 3741 ? 150.247 108.981 204.064 1.00 68.84  ? 3741 ARG A O     1 
ATOM   15938 C  CB    . ARG A 1 3741 ? 149.257 108.253 201.008 1.00 71.55  ? 3741 ARG A CB    1 
ATOM   15939 C  CG    . ARG A 1 3741 ? 148.259 107.350 201.717 1.00 79.16  ? 3741 ARG A CG    1 
ATOM   15940 C  CD    . ARG A 1 3741 ? 147.038 108.123 202.184 1.00 76.01  ? 3741 ARG A CD    1 
ATOM   15941 N  NE    . ARG A 1 3741 ? 146.344 107.432 203.263 1.00 82.83  ? 3741 ARG A NE    1 
ATOM   15942 C  CZ    . ARG A 1 3741 ? 145.229 107.863 203.836 1.00 88.37  ? 3741 ARG A CZ    1 
ATOM   15943 N  NH1   . ARG A 1 3741 ? 144.648 108.989 203.456 1.00 84.08  ? 3741 ARG A NH1   1 
ATOM   15944 N  NH2   . ARG A 1 3741 ? 144.682 107.147 204.814 1.00 86.78  ? 3741 ARG A NH2   1 
ATOM   15945 N  N     . LEU A 1 3742 ? 151.921 109.017 202.563 1.00 62.72  ? 3742 LEU A N     1 
ATOM   15946 C  CA    . LEU A 1 3742 ? 152.927 108.720 203.580 1.00 57.54  ? 3742 LEU A CA    1 
ATOM   15947 C  C     . LEU A 1 3742 ? 153.027 109.844 204.605 1.00 67.61  ? 3742 LEU A C     1 
ATOM   15948 O  O     . LEU A 1 3742 ? 153.127 109.588 205.813 1.00 73.77  ? 3742 LEU A O     1 
ATOM   15949 C  CB    . LEU A 1 3742 ? 154.286 108.475 202.924 1.00 55.40  ? 3742 LEU A CB    1 
ATOM   15950 C  CG    . LEU A 1 3742 ? 154.548 107.072 202.376 1.00 60.87  ? 3742 LEU A CG    1 
ATOM   15951 C  CD1   . LEU A 1 3742 ? 156.001 106.926 201.959 1.00 58.46  ? 3742 LEU A CD1   1 
ATOM   15952 C  CD2   . LEU A 1 3742 ? 154.172 106.012 203.398 1.00 65.27  ? 3742 LEU A CD2   1 
ATOM   15953 N  N     . ARG A 1 3743 ? 153.006 111.096 204.142 1.00 68.15  ? 3743 ARG A N     1 
ATOM   15954 C  CA    . ARG A 1 3743 ? 153.058 112.227 205.064 1.00 64.02  ? 3743 ARG A CA    1 
ATOM   15955 C  C     . ARG A 1 3743 ? 151.834 112.255 205.974 1.00 69.48  ? 3743 ARG A C     1 
ATOM   15956 O  O     . ARG A 1 3743 ? 151.954 112.489 207.185 1.00 71.71  ? 3743 ARG A O     1 
ATOM   15957 C  CB    . ARG A 1 3743 ? 153.184 113.530 204.278 1.00 60.39  ? 3743 ARG A CB    1 
ATOM   15958 C  CG    . ARG A 1 3743 ? 154.592 113.809 203.778 1.00 64.57  ? 3743 ARG A CG    1 
ATOM   15959 C  CD    . ARG A 1 3743 ? 154.695 115.181 203.133 1.00 56.60  ? 3743 ARG A CD    1 
ATOM   15960 N  NE    . ARG A 1 3743 ? 154.431 115.127 201.701 1.00 53.18  ? 3743 ARG A NE    1 
ATOM   15961 C  CZ    . ARG A 1 3743 ? 153.339 115.607 201.121 1.00 53.20  ? 3743 ARG A CZ    1 
ATOM   15962 N  NH1   . ARG A 1 3743 ? 152.376 116.175 201.826 1.00 46.57  ? 3743 ARG A NH1   1 
ATOM   15963 N  NH2   . ARG A 1 3743 ? 153.211 115.514 199.801 1.00 55.75  ? 3743 ARG A NH2   1 
ATOM   15964 N  N     . GLN A 1 3744 ? 150.648 112.012 205.409 1.00 67.97  ? 3744 GLN A N     1 
ATOM   15965 C  CA    . GLN A 1 3744 ? 149.436 111.968 206.219 1.00 65.78  ? 3744 GLN A CA    1 
ATOM   15966 C  C     . GLN A 1 3744 ? 149.490 110.834 207.233 1.00 68.67  ? 3744 GLN A C     1 
ATOM   15967 O  O     . GLN A 1 3744 ? 149.045 110.993 208.373 1.00 70.11  ? 3744 GLN A O     1 
ATOM   15968 C  CB    . GLN A 1 3744 ? 148.202 111.824 205.328 1.00 65.47  ? 3744 GLN A CB    1 
ATOM   15969 C  CG    . GLN A 1 3744 ? 147.964 112.987 204.383 1.00 67.90  ? 3744 GLN A CG    1 
ATOM   15970 C  CD    . GLN A 1 3744 ? 146.546 113.015 203.846 1.00 73.83  ? 3744 GLN A CD    1 
ATOM   15971 O  OE1   . GLN A 1 3744 ? 146.324 112.888 202.642 1.00 71.67  ? 3744 GLN A OE1   1 
ATOM   15972 N  NE2   . GLN A 1 3744 ? 145.579 113.187 204.739 1.00 71.22  ? 3744 GLN A NE2   1 
ATOM   15973 N  N     . LEU A 1 3745 ? 150.020 109.676 206.833 1.00 71.49  ? 3745 LEU A N     1 
ATOM   15974 C  CA    . LEU A 1 3745 ? 150.131 108.552 207.756 1.00 74.00  ? 3745 LEU A CA    1 
ATOM   15975 C  C     . LEU A 1 3745 ? 151.082 108.869 208.900 1.00 73.08  ? 3745 LEU A C     1 
ATOM   15976 O  O     . LEU A 1 3745 ? 150.799 108.541 210.058 1.00 81.66  ? 3745 LEU A O     1 
ATOM   15977 C  CB    . LEU A 1 3745 ? 150.592 107.302 207.008 1.00 69.49  ? 3745 LEU A CB    1 
ATOM   15978 C  CG    . LEU A 1 3745 ? 149.560 106.653 206.087 1.00 71.59  ? 3745 LEU A CG    1 
ATOM   15979 C  CD1   . LEU A 1 3745 ? 150.100 105.354 205.523 1.00 79.27  ? 3745 LEU A CD1   1 
ATOM   15980 C  CD2   . LEU A 1 3745 ? 148.252 106.424 206.817 1.00 74.30  ? 3745 LEU A CD2   1 
ATOM   15981 N  N     . GLU A 1 3746 ? 152.216 109.503 208.596 1.00 68.85  ? 3746 GLU A N     1 
ATOM   15982 C  CA    . GLU A 1 3746 ? 153.148 109.887 209.651 1.00 74.71  ? 3746 GLU A CA    1 
ATOM   15983 C  C     . GLU A 1 3746 ? 152.505 110.880 210.612 1.00 74.69  ? 3746 GLU A C     1 
ATOM   15984 O  O     . GLU A 1 3746 ? 152.608 110.735 211.838 1.00 78.29  ? 3746 GLU A O     1 
ATOM   15985 C  CB    . GLU A 1 3746 ? 154.420 110.473 209.037 1.00 73.74  ? 3746 GLU A CB    1 
ATOM   15986 C  CG    . GLU A 1 3746 ? 155.576 110.606 210.013 1.00 74.44  ? 3746 GLU A CG    1 
ATOM   15987 C  CD    . GLU A 1 3746 ? 155.763 109.368 210.867 1.00 86.45  ? 3746 GLU A CD    1 
ATOM   15988 O  OE1   . GLU A 1 3746 ? 156.439 108.424 210.407 1.00 81.49  ? 3746 GLU A OE1   1 
ATOM   15989 O  OE2   . GLU A 1 3746 ? 155.242 109.342 212.002 1.00 92.06  ? 3746 GLU A OE2   1 
ATOM   15990 N  N     . LYS A 1 3747 ? 151.816 111.888 210.068 1.00 74.15  ? 3747 LYS A N     1 
ATOM   15991 C  CA    . LYS A 1 3747 ? 151.154 112.873 210.917 1.00 72.23  ? 3747 LYS A CA    1 
ATOM   15992 C  C     . LYS A 1 3747 ? 150.079 112.226 211.780 1.00 75.01  ? 3747 LYS A C     1 
ATOM   15993 O  O     . LYS A 1 3747 ? 149.961 112.532 212.972 1.00 79.20  ? 3747 LYS A O     1 
ATOM   15994 C  CB    . LYS A 1 3747 ? 150.553 113.988 210.061 1.00 71.69  ? 3747 LYS A CB    1 
ATOM   15995 C  CG    . LYS A 1 3747 ? 151.514 115.122 209.750 1.00 72.26  ? 3747 LYS A CG    1 
ATOM   15996 C  CD    . LYS A 1 3747 ? 150.782 116.450 209.646 1.00 74.30  ? 3747 LYS A CD    1 
ATOM   15997 C  CE    . LYS A 1 3747 ? 150.326 116.718 208.221 1.00 75.88  ? 3747 LYS A CE    1 
ATOM   15998 N  NZ    . LYS A 1 3747 ? 150.363 118.169 207.889 1.00 73.28  ? 3747 LYS A NZ    1 
ATOM   15999 N  N     . SER A 1 3748 ? 149.284 111.327 211.195 1.00 75.84  ? 3748 SER A N     1 
ATOM   16000 C  CA    . SER A 1 3748 ? 148.217 110.670 211.939 1.00 74.95  ? 3748 SER A CA    1 
ATOM   16001 C  C     . SER A 1 3748 ? 148.773 109.779 213.042 1.00 78.03  ? 3748 SER A C     1 
ATOM   16002 O  O     . SER A 1 3748 ? 148.229 109.747 214.151 1.00 81.28  ? 3748 SER A O     1 
ATOM   16003 C  CB    . SER A 1 3748 ? 147.339 109.861 210.985 1.00 72.78  ? 3748 SER A CB    1 
ATOM   16004 O  OG    . SER A 1 3748 ? 147.996 108.677 210.570 1.00 73.56  ? 3748 SER A OG    1 
ATOM   16005 N  N     . LEU A 1 3749 ? 149.849 109.042 212.756 1.00 73.13  ? 3749 LEU A N     1 
ATOM   16006 C  CA    . LEU A 1 3749 ? 150.444 108.188 213.778 1.00 71.98  ? 3749 LEU A CA    1 
ATOM   16007 C  C     . LEU A 1 3749 ? 151.016 109.021 214.918 1.00 76.45  ? 3749 LEU A C     1 
ATOM   16008 O  O     . LEU A 1 3749 ? 150.840 108.681 216.096 1.00 84.50  ? 3749 LEU A O     1 
ATOM   16009 C  CB    . LEU A 1 3749 ? 151.515 107.296 213.147 1.00 82.33  ? 3749 LEU A CB    1 
ATOM   16010 C  CG    . LEU A 1 3749 ? 152.159 106.170 213.962 1.00 88.55  ? 3749 LEU A CG    1 
ATOM   16011 C  CD1   . LEU A 1 3749 ? 152.612 105.062 213.027 1.00 79.70  ? 3749 LEU A CD1   1 
ATOM   16012 C  CD2   . LEU A 1 3749 ? 153.338 106.669 214.782 1.00 85.79  ? 3749 LEU A CD2   1 
ATOM   16013 N  N     . LEU A 1 3750 ? 151.696 110.124 214.588 1.00 81.80  ? 3750 LEU A N     1 
ATOM   16014 C  CA    . LEU A 1 3750 ? 152.222 110.998 215.633 1.00 80.65  ? 3750 LEU A CA    1 
ATOM   16015 C  C     . LEU A 1 3750 ? 151.098 111.604 216.465 1.00 79.25  ? 3750 LEU A C     1 
ATOM   16016 O  O     . LEU A 1 3750 ? 151.201 111.688 217.693 1.00 78.75  ? 3750 LEU A O     1 
ATOM   16017 C  CB    . LEU A 1 3750 ? 153.090 112.094 215.015 1.00 79.17  ? 3750 LEU A CB    1 
ATOM   16018 C  CG    . LEU A 1 3750 ? 154.152 112.709 215.930 1.00 79.32  ? 3750 LEU A CG    1 
ATOM   16019 C  CD1   . LEU A 1 3750 ? 154.843 111.638 216.759 1.00 78.33  ? 3750 LEU A CD1   1 
ATOM   16020 C  CD2   . LEU A 1 3750 ? 155.166 113.495 215.118 1.00 70.37  ? 3750 LEU A CD2   1 
ATOM   16021 N  N     . GLN A 1 3751 ? 150.008 112.020 215.814 1.00 75.02  ? 3751 GLN A N     1 
ATOM   16022 C  CA    . GLN A 1 3751 ? 148.875 112.580 216.545 1.00 77.93  ? 3751 GLN A CA    1 
ATOM   16023 C  C     . GLN A 1 3751 ? 148.232 111.540 217.456 1.00 85.36  ? 3751 GLN A C     1 
ATOM   16024 O  O     . GLN A 1 3751 ? 147.860 111.846 218.596 1.00 92.20  ? 3751 GLN A O     1 
ATOM   16025 C  CB    . GLN A 1 3751 ? 147.851 113.144 215.559 1.00 77.27  ? 3751 GLN A CB    1 
ATOM   16026 C  CG    . GLN A 1 3751 ? 146.472 113.379 216.148 1.00 83.44  ? 3751 GLN A CG    1 
ATOM   16027 C  CD    . GLN A 1 3751 ? 145.419 113.612 215.083 1.00 88.39  ? 3751 GLN A CD    1 
ATOM   16028 O  OE1   . GLN A 1 3751 ? 144.666 112.705 214.730 1.00 95.00  ? 3751 GLN A OE1   1 
ATOM   16029 N  NE2   . GLN A 1 3751 ? 145.363 114.832 214.563 1.00 83.18  ? 3751 GLN A NE2   1 
ATOM   16030 N  N     . ALA A 1 3752 ? 148.089 110.305 216.969 1.00 83.34  ? 3752 ALA A N     1 
ATOM   16031 C  CA    . ALA A 1 3752 ? 147.514 109.245 217.790 1.00 82.69  ? 3752 ALA A CA    1 
ATOM   16032 C  C     . ALA A 1 3752 ? 148.388 108.951 219.001 1.00 85.75  ? 3752 ALA A C     1 
ATOM   16033 O  O     . ALA A 1 3752 ? 147.879 108.770 220.113 1.00 87.53  ? 3752 ALA A O     1 
ATOM   16034 C  CB    . ALA A 1 3752 ? 147.309 107.983 216.954 1.00 80.91  ? 3752 ALA A CB    1 
ATOM   16035 N  N     . LEU A 1 3753 ? 149.709 108.898 218.807 1.00 81.58  ? 3753 LEU A N     1 
ATOM   16036 C  CA    . LEU A 1 3753 ? 150.599 108.720 219.950 1.00 85.55  ? 3753 LEU A CA    1 
ATOM   16037 C  C     . LEU A 1 3753 ? 150.552 109.918 220.890 1.00 91.15  ? 3753 LEU A C     1 
ATOM   16038 O  O     . LEU A 1 3753 ? 150.796 109.771 222.092 1.00 96.73  ? 3753 LEU A O     1 
ATOM   16039 C  CB    . LEU A 1 3753 ? 152.030 108.468 219.480 1.00 83.70  ? 3753 LEU A CB    1 
ATOM   16040 C  CG    . LEU A 1 3753 ? 152.302 107.053 218.972 1.00 85.73  ? 3753 LEU A CG    1 
ATOM   16041 C  CD1   . LEU A 1 3753 ? 153.726 106.930 218.471 1.00 93.26  ? 3753 LEU A CD1   1 
ATOM   16042 C  CD2   . LEU A 1 3753 ? 152.033 106.043 220.071 1.00 91.14  ? 3753 LEU A CD2   1 
ATOM   16043 N  N     . ASN A 1 3754 ? 150.257 111.106 220.362 1.00 92.00  ? 3754 ASN A N     1 
ATOM   16044 C  CA    . ASN A 1 3754 ? 150.094 112.274 221.218 1.00 90.08  ? 3754 ASN A CA    1 
ATOM   16045 C  C     . ASN A 1 3754 ? 148.836 112.176 222.071 1.00 90.34  ? 3754 ASN A C     1 
ATOM   16046 O  O     . ASN A 1 3754 ? 148.852 112.565 223.244 1.00 90.22  ? 3754 ASN A O     1 
ATOM   16047 C  CB    . ASN A 1 3754 ? 150.050 113.545 220.370 1.00 89.16  ? 3754 ASN A CB    1 
ATOM   16048 C  CG    . ASN A 1 3754 ? 151.419 114.159 220.168 1.00 87.76  ? 3754 ASN A CG    1 
ATOM   16049 O  OD1   . ASN A 1 3754 ? 152.421 113.451 220.068 1.00 87.62  ? 3754 ASN A OD1   1 
ATOM   16050 N  ND2   . ASN A 1 3754 ? 151.468 115.484 220.107 1.00 79.84  ? 3754 ASN A ND2   1 
ATOM   16051 N  N     . GLU A 1 3755 ? 147.745 111.661 221.505 1.00 93.40  ? 3755 GLU A N     1 
ATOM   16052 C  CA    . GLU A 1 3755 ? 146.449 111.665 222.170 1.00 91.71  ? 3755 GLU A CA    1 
ATOM   16053 C  C     . GLU A 1 3755 ? 146.209 110.451 223.062 1.00 92.74  ? 3755 GLU A C     1 
ATOM   16054 O  O     . GLU A 1 3755 ? 145.177 110.401 223.740 1.00 85.36  ? 3755 GLU A O     1 
ATOM   16055 C  CB    . GLU A 1 3755 ? 145.327 111.753 221.130 1.00 89.18  ? 3755 GLU A CB    1 
ATOM   16056 C  CG    . GLU A 1 3755 ? 145.282 113.072 220.377 1.00 95.96  ? 3755 GLU A CG    1 
ATOM   16057 C  CD    . GLU A 1 3755 ? 145.549 114.266 221.272 1.00 100.60 ? 3755 GLU A CD    1 
ATOM   16058 O  OE1   . GLU A 1 3755 ? 144.713 114.546 222.157 1.00 99.59  ? 3755 GLU A OE1   1 
ATOM   16059 O  OE2   . GLU A 1 3755 ? 146.596 114.923 221.092 1.00 99.46  ? 3755 GLU A OE2   1 
ATOM   16060 N  N     . VAL A 1 3756 ? 147.120 109.475 223.080 1.00 96.69  ? 3756 VAL A N     1 
ATOM   16061 C  CA    . VAL A 1 3756 ? 146.918 108.309 223.937 1.00 98.47  ? 3756 VAL A CA    1 
ATOM   16062 C  C     . VAL A 1 3756 ? 147.130 108.701 225.398 1.00 102.49 ? 3756 VAL A C     1 
ATOM   16063 O  O     . VAL A 1 3756 ? 147.854 109.649 225.725 1.00 104.57 ? 3756 VAL A O     1 
ATOM   16064 C  CB    . VAL A 1 3756 ? 147.845 107.154 223.517 1.00 105.08 ? 3756 VAL A CB    1 
ATOM   16065 C  CG1   . VAL A 1 3756 ? 149.299 107.512 223.756 1.00 103.65 ? 3756 VAL A CG1   1 
ATOM   16066 C  CG2   . VAL A 1 3756 ? 147.472 105.851 224.223 1.00 104.50 ? 3756 VAL A CG2   1 
ATOM   16067 N  N     . LYS A 1 3757 ? 146.479 107.956 226.293 1.00 104.48 ? 3757 LYS A N     1 
ATOM   16068 C  CA    . LYS A 1 3757 ? 146.439 108.278 227.714 1.00 102.22 ? 3757 LYS A CA    1 
ATOM   16069 C  C     . LYS A 1 3757 ? 147.586 107.640 228.493 1.00 105.16 ? 3757 LYS A C     1 
ATOM   16070 O  O     . LYS A 1 3757 ? 147.452 107.380 229.693 1.00 102.71 ? 3757 LYS A O     1 
ATOM   16071 C  CB    . LYS A 1 3757 ? 145.095 107.861 228.310 1.00 98.23  ? 3757 LYS A CB    1 
ATOM   16072 C  CG    . LYS A 1 3757 ? 143.891 108.239 227.459 1.00 95.01  ? 3757 LYS A CG    1 
ATOM   16073 C  CD    . LYS A 1 3757 ? 143.860 109.732 227.166 1.00 92.38  ? 3757 LYS A CD    1 
ATOM   16074 C  CE    . LYS A 1 3757 ? 143.606 110.539 228.430 1.00 90.80  ? 3757 LYS A CE    1 
ATOM   16075 N  NZ    . LYS A 1 3757 ? 143.567 112.002 228.156 1.00 82.86  ? 3757 LYS A NZ    1 
ATOM   16076 N  N     . GLY A 1 3758 ? 148.713 107.380 227.833 1.00 109.02 ? 3758 GLY A N     1 
ATOM   16077 C  CA    . GLY A 1 3758 ? 149.894 106.878 228.501 1.00 107.42 ? 3758 GLY A CA    1 
ATOM   16078 C  C     . GLY A 1 3758 ? 149.994 105.375 228.624 1.00 111.04 ? 3758 GLY A C     1 
ATOM   16079 O  O     . GLY A 1 3758 ? 150.998 104.883 229.156 1.00 109.84 ? 3758 GLY A O     1 
ATOM   16080 N  N     . ARG A 1 3759 ? 148.998 104.623 228.151 1.00 114.97 ? 3759 ARG A N     1 
ATOM   16081 C  CA    . ARG A 1 3759 ? 149.012 103.159 228.234 1.00 116.04 ? 3759 ARG A CA    1 
ATOM   16082 C  C     . ARG A 1 3759 ? 148.421 102.611 226.935 1.00 118.30 ? 3759 ARG A C     1 
ATOM   16083 O  O     . ARG A 1 3759 ? 147.201 102.477 226.802 1.00 115.89 ? 3759 ARG A O     1 
ATOM   16084 C  CB    . ARG A 1 3759 ? 148.248 102.670 229.457 1.00 115.31 ? 3759 ARG A CB    1 
ATOM   16085 C  CG    . ARG A 1 3759 ? 149.024 102.780 230.759 1.00 111.26 ? 3759 ARG A CG    1 
ATOM   16086 C  CD    . ARG A 1 3759 ? 150.235 101.862 230.761 1.00 115.36 ? 3759 ARG A CD    1 
ATOM   16087 N  NE    . ARG A 1 3759 ? 149.938 100.566 230.164 1.00 120.83 ? 3759 ARG A NE    1 
ATOM   16088 C  CZ    . ARG A 1 3759 ? 149.815 99.436  230.847 1.00 120.52 ? 3759 ARG A CZ    1 
ATOM   16089 N  NH1   . ARG A 1 3759 ? 149.954 99.405  232.162 1.00 118.09 ? 3759 ARG A NH1   1 
ATOM   16090 N  NH2   . ARG A 1 3759 ? 149.543 98.310  230.194 1.00 116.76 ? 3759 ARG A NH2   1 
ATOM   16091 N  N     . ILE A 1 3760 ? 149.298 102.294 225.981 1.00 116.13 ? 3760 ILE A N     1 
ATOM   16092 C  CA    . ILE A 1 3760 ? 148.846 101.776 224.694 1.00 114.85 ? 3760 ILE A CA    1 
ATOM   16093 C  C     . ILE A 1 3760 ? 148.265 100.376 224.850 1.00 117.07 ? 3760 ILE A C     1 
ATOM   16094 O  O     . ILE A 1 3760 ? 147.261 100.034 224.214 1.00 120.29 ? 3760 ILE A O     1 
ATOM   16095 C  CB    . ILE A 1 3760 ? 150.000 101.805 223.675 1.00 113.07 ? 3760 ILE A CB    1 
ATOM   16096 C  CG1   . ILE A 1 3760 ? 150.504 103.235 223.482 1.00 110.78 ? 3760 ILE A CG1   1 
ATOM   16097 C  CG2   . ILE A 1 3760 ? 149.560 101.217 222.344 1.00 112.74 ? 3760 ILE A CG2   1 
ATOM   16098 C  CD1   . ILE A 1 3760 ? 151.667 103.344 222.522 1.00 106.98 ? 3760 ILE A CD1   1 
ATOM   16099 N  N     . LEU A 1 3761 ? 148.880 99.546  225.696 1.00 113.68 ? 3761 LEU A N     1 
ATOM   16100 C  CA    . LEU A 1 3761 ? 148.391 98.182  225.883 1.00 114.24 ? 3761 LEU A CA    1 
ATOM   16101 C  C     . LEU A 1 3761 ? 146.986 98.160  226.472 1.00 119.74 ? 3761 LEU A C     1 
ATOM   16102 O  O     . LEU A 1 3761 ? 146.200 97.257  226.162 1.00 118.12 ? 3761 LEU A O     1 
ATOM   16103 C  CB    . LEU A 1 3761 ? 149.343 97.390  226.782 1.00 116.20 ? 3761 LEU A CB    1 
ATOM   16104 C  CG    . LEU A 1 3761 ? 150.647 96.841  226.195 1.00 116.68 ? 3761 LEU A CG    1 
ATOM   16105 C  CD1   . LEU A 1 3761 ? 151.652 97.946  225.926 1.00 110.44 ? 3761 LEU A CD1   1 
ATOM   16106 C  CD2   . LEU A 1 3761 ? 151.244 95.789  227.118 1.00 114.74 ? 3761 LEU A CD2   1 
ATOM   16107 N  N     . ASP A 1 3762 ? 146.656 99.132  227.324 1.00 121.57 ? 3762 ASP A N     1 
ATOM   16108 C  CA    . ASP A 1 3762 ? 145.346 99.140  227.968 1.00 121.22 ? 3762 ASP A CA    1 
ATOM   16109 C  C     . ASP A 1 3762 ? 144.222 99.324  226.955 1.00 118.72 ? 3762 ASP A C     1 
ATOM   16110 O  O     . ASP A 1 3762 ? 143.175 98.673  227.053 1.00 116.39 ? 3762 ASP A O     1 
ATOM   16111 C  CB    . ASP A 1 3762 ? 145.292 100.234 229.034 1.00 120.18 ? 3762 ASP A CB    1 
ATOM   16112 C  CG    . ASP A 1 3762 ? 146.178 99.930  230.225 1.00 119.22 ? 3762 ASP A CG    1 
ATOM   16113 O  OD1   . ASP A 1 3762 ? 146.831 98.866  230.225 1.00 120.37 ? 3762 ASP A OD1   1 
ATOM   16114 O  OD2   . ASP A 1 3762 ? 146.222 100.755 231.162 1.00 114.34 ? 3762 ASP A OD2   1 
ATOM   16115 N  N     . ASP A 1 3763 ? 144.416 100.205 225.975 1.00 117.72 ? 3763 ASP A N     1 
ATOM   16116 C  CA    . ASP A 1 3763 ? 143.385 100.528 224.994 1.00 119.06 ? 3763 ASP A CA    1 
ATOM   16117 C  C     . ASP A 1 3763 ? 143.679 99.779  223.699 1.00 120.02 ? 3763 ASP A C     1 
ATOM   16118 O  O     . ASP A 1 3763 ? 144.708 100.014 223.057 1.00 118.78 ? 3763 ASP A O     1 
ATOM   16119 C  CB    . ASP A 1 3763 ? 143.319 102.035 224.755 1.00 120.33 ? 3763 ASP A CB    1 
ATOM   16120 C  CG    . ASP A 1 3763 ? 141.963 102.485 224.247 1.00 116.79 ? 3763 ASP A CG    1 
ATOM   16121 O  OD1   . ASP A 1 3763 ? 140.985 102.417 225.021 1.00 108.83 ? 3763 ASP A OD1   1 
ATOM   16122 O  OD2   . ASP A 1 3763 ? 141.875 102.908 223.076 1.00 115.18 ? 3763 ASP A OD2   1 
ATOM   16123 N  N     . ASP A 1 3764 ? 142.770 98.882  223.314 1.00 119.78 ? 3764 ASP A N     1 
ATOM   16124 C  CA    . ASP A 1 3764 ? 142.939 98.112  222.089 1.00 117.41 ? 3764 ASP A CA    1 
ATOM   16125 C  C     . ASP A 1 3764 ? 142.655 98.927  220.834 1.00 116.02 ? 3764 ASP A C     1 
ATOM   16126 O  O     . ASP A 1 3764 ? 143.195 98.606  219.769 1.00 114.19 ? 3764 ASP A O     1 
ATOM   16127 C  CB    . ASP A 1 3764 ? 142.037 96.876  222.117 1.00 115.23 ? 3764 ASP A CB    1 
ATOM   16128 C  CG    . ASP A 1 3764 ? 142.438 95.888  223.195 1.00 111.77 ? 3764 ASP A CG    1 
ATOM   16129 O  OD1   . ASP A 1 3764 ? 143.395 96.179  223.943 1.00 113.25 ? 3764 ASP A OD1   1 
ATOM   16130 O  OD2   . ASP A 1 3764 ? 141.798 94.820  223.294 1.00 105.27 ? 3764 ASP A OD2   1 
ATOM   16131 N  N     . THR A 1 3765 ? 141.815 99.962  220.930 1.00 114.99 ? 3765 THR A N     1 
ATOM   16132 C  CA    . THR A 1 3765 ? 141.525 100.793 219.764 1.00 117.40 ? 3765 THR A CA    1 
ATOM   16133 C  C     . THR A 1 3765 ? 142.772 101.526 219.284 1.00 117.13 ? 3765 THR A C     1 
ATOM   16134 O  O     . THR A 1 3765 ? 143.023 101.613 218.075 1.00 115.20 ? 3765 THR A O     1 
ATOM   16135 C  CB    . THR A 1 3765 ? 140.410 101.787 220.091 1.00 116.46 ? 3765 THR A CB    1 
ATOM   16136 O  OG1   . THR A 1 3765 ? 139.283 101.085 220.630 1.00 109.60 ? 3765 THR A OG1   1 
ATOM   16137 C  CG2   . THR A 1 3765 ? 139.981 102.536 218.838 1.00 105.73 ? 3765 THR A CG2   1 
ATOM   16138 N  N     . ILE A 1 3766 ? 143.564 102.059 220.218 1.00 115.65 ? 3766 ILE A N     1 
ATOM   16139 C  CA    . ILE A 1 3766 ? 144.808 102.729 219.850 1.00 115.14 ? 3766 ILE A CA    1 
ATOM   16140 C  C     . ILE A 1 3766 ? 145.764 101.744 219.190 1.00 113.52 ? 3766 ILE A C     1 
ATOM   16141 O  O     . ILE A 1 3766 ? 146.436 102.072 218.204 1.00 112.34 ? 3766 ILE A O     1 
ATOM   16142 C  CB    . ILE A 1 3766 ? 145.438 103.395 221.088 1.00 114.53 ? 3766 ILE A CB    1 
ATOM   16143 C  CG1   . ILE A 1 3766 ? 144.522 104.497 221.623 1.00 108.68 ? 3766 ILE A CG1   1 
ATOM   16144 C  CG2   . ILE A 1 3766 ? 146.810 103.960 220.757 1.00 110.40 ? 3766 ILE A CG2   1 
ATOM   16145 C  CD1   . ILE A 1 3766 ? 144.257 105.607 220.630 1.00 99.39  ? 3766 ILE A CD1   1 
ATOM   16146 N  N     . ILE A 1 3767 ? 145.835 100.521 219.720 1.00 112.99 ? 3767 ILE A N     1 
ATOM   16147 C  CA    . ILE A 1 3767 ? 146.693 99.493  219.136 1.00 111.68 ? 3767 ILE A CA    1 
ATOM   16148 C  C     . ILE A 1 3767 ? 146.261 99.187  217.708 1.00 109.71 ? 3767 ILE A C     1 
ATOM   16149 O  O     . ILE A 1 3767 ? 147.093 99.078  216.796 1.00 107.11 ? 3767 ILE A O     1 
ATOM   16150 C  CB    . ILE A 1 3767 ? 146.676 98.225  220.008 1.00 108.65 ? 3767 ILE A CB    1 
ATOM   16151 C  CG1   . ILE A 1 3767 ? 147.312 98.499  221.371 1.00 110.50 ? 3767 ILE A CG1   1 
ATOM   16152 C  CG2   . ILE A 1 3767 ? 147.378 97.082  219.298 1.00 103.86 ? 3767 ILE A CG2   1 
ATOM   16153 C  CD1   . ILE A 1 3767 ? 147.361 97.288  222.275 1.00 107.34 ? 3767 ILE A CD1   1 
ATOM   16154 N  N     . THR A 1 3768 ? 144.952 99.027  217.496 1.00 108.91 ? 3768 THR A N     1 
ATOM   16155 C  CA    . THR A 1 3768 ? 144.454 98.721  216.159 1.00 108.40 ? 3768 THR A CA    1 
ATOM   16156 C  C     . THR A 1 3768 ? 144.745 99.859  215.191 1.00 106.04 ? 3768 THR A C     1 
ATOM   16157 O  O     . THR A 1 3768 ? 145.160 99.621  214.051 1.00 103.36 ? 3768 THR A O     1 
ATOM   16158 C  CB    . THR A 1 3768 ? 142.954 98.426  216.202 1.00 108.54 ? 3768 THR A CB    1 
ATOM   16159 O  OG1   . THR A 1 3768 ? 142.283 99.452  216.941 1.00 113.50 ? 3768 THR A OG1   1 
ATOM   16160 C  CG2   . THR A 1 3768 ? 142.695 97.078  216.859 1.00 102.43 ? 3768 THR A CG2   1 
ATOM   16161 N  N     . THR A 1 3769 ? 144.539 101.104 215.627 1.00 106.57 ? 3769 THR A N     1 
ATOM   16162 C  CA    . THR A 1 3769 ? 144.839 102.238 214.758 1.00 102.94 ? 3769 THR A CA    1 
ATOM   16163 C  C     . THR A 1 3769 ? 146.321 102.285 214.410 1.00 101.29 ? 3769 THR A C     1 
ATOM   16164 O  O     . THR A 1 3769 ? 146.685 102.512 213.250 1.00 99.20  ? 3769 THR A O     1 
ATOM   16165 C  CB    . THR A 1 3769 ? 144.404 103.545 215.419 1.00 100.73 ? 3769 THR A CB    1 
ATOM   16166 O  OG1   . THR A 1 3769 ? 144.970 103.632 216.733 1.00 106.45 ? 3769 THR A OG1   1 
ATOM   16167 C  CG2   . THR A 1 3769 ? 142.887 103.615 215.515 1.00 92.61  ? 3769 THR A CG2   1 
ATOM   16168 N  N     . LEU A 1 3770 ? 147.191 102.053 215.397 1.00 99.53  ? 3770 LEU A N     1 
ATOM   16169 C  CA    . LEU A 1 3770 ? 148.628 102.088 215.142 1.00 98.26  ? 3770 LEU A CA    1 
ATOM   16170 C  C     . LEU A 1 3770 ? 149.041 101.004 214.154 1.00 100.63 ? 3770 LEU A C     1 
ATOM   16171 O  O     . LEU A 1 3770 ? 149.807 101.261 213.217 1.00 102.31 ? 3770 LEU A O     1 
ATOM   16172 C  CB    . LEU A 1 3770 ? 149.398 101.938 216.455 1.00 97.77  ? 3770 LEU A CB    1 
ATOM   16173 C  CG    . LEU A 1 3770 ? 149.480 103.166 217.363 1.00 100.49 ? 3770 LEU A CG    1 
ATOM   16174 C  CD1   . LEU A 1 3770 ? 150.574 102.986 218.404 1.00 91.28  ? 3770 LEU A CD1   1 
ATOM   16175 C  CD2   . LEU A 1 3770 ? 149.712 104.429 216.549 1.00 98.27  ? 3770 LEU A CD2   1 
ATOM   16176 N  N     . GLU A 1 3771 ? 148.537 99.781  214.343 1.00 101.49 ? 3771 GLU A N     1 
ATOM   16177 C  CA    . GLU A 1 3771 ? 148.934 98.692  213.455 1.00 93.87  ? 3771 GLU A CA    1 
ATOM   16178 C  C     . GLU A 1 3771 ? 148.371 98.889  212.051 1.00 94.09  ? 3771 GLU A C     1 
ATOM   16179 O  O     . GLU A 1 3771 ? 149.044 98.579  211.061 1.00 93.63  ? 3771 GLU A O     1 
ATOM   16180 C  CB    . GLU A 1 3771 ? 148.511 97.342  214.040 1.00 101.20 ? 3771 GLU A CB    1 
ATOM   16181 C  CG    . GLU A 1 3771 ? 147.014 97.117  214.147 1.00 104.92 ? 3771 GLU A CG    1 
ATOM   16182 C  CD    . GLU A 1 3771 ? 146.670 95.790  214.793 1.00 105.15 ? 3771 GLU A CD    1 
ATOM   16183 O  OE1   . GLU A 1 3771 ? 147.603 95.056  215.180 1.00 104.53 ? 3771 GLU A OE1   1 
ATOM   16184 O  OE2   . GLU A 1 3771 ? 145.466 95.482  214.917 1.00 105.26 ? 3771 GLU A OE2   1 
ATOM   16185 N  N     . ASN A 1 3772 ? 147.147 99.418  211.939 1.00 96.76  ? 3772 ASN A N     1 
ATOM   16186 C  CA    . ASN A 1 3772 ? 146.592 99.716  210.623 1.00 95.24  ? 3772 ASN A CA    1 
ATOM   16187 C  C     . ASN A 1 3772 ? 147.408 100.789 209.912 1.00 94.19  ? 3772 ASN A C     1 
ATOM   16188 O  O     . ASN A 1 3772 ? 147.686 100.675 208.711 1.00 93.74  ? 3772 ASN A O     1 
ATOM   16189 C  CB    . ASN A 1 3772 ? 145.133 100.151 210.754 1.00 88.74  ? 3772 ASN A CB    1 
ATOM   16190 C  CG    . ASN A 1 3772 ? 144.235 99.034  211.248 1.00 93.54  ? 3772 ASN A CG    1 
ATOM   16191 O  OD1   . ASN A 1 3772 ? 144.675 97.899  211.426 1.00 96.15  ? 3772 ASN A OD1   1 
ATOM   16192 N  ND2   . ASN A 1 3772 ? 142.966 99.353  211.476 1.00 89.24  ? 3772 ASN A ND2   1 
ATOM   16193 N  N     . LEU A 1 3773 ? 147.803 101.838 210.640 1.00 91.95  ? 3773 LEU A N     1 
ATOM   16194 C  CA    . LEU A 1 3773 ? 148.621 102.886 210.040 1.00 89.52  ? 3773 LEU A CA    1 
ATOM   16195 C  C     . LEU A 1 3773 ? 149.972 102.342 209.595 1.00 90.86  ? 3773 LEU A C     1 
ATOM   16196 O  O     . LEU A 1 3773 ? 150.467 102.695 208.518 1.00 92.62  ? 3773 LEU A O     1 
ATOM   16197 C  CB    . LEU A 1 3773 ? 148.802 104.040 211.026 1.00 86.71  ? 3773 LEU A CB    1 
ATOM   16198 C  CG    . LEU A 1 3773 ? 147.560 104.875 211.342 1.00 81.60  ? 3773 LEU A CG    1 
ATOM   16199 C  CD1   . LEU A 1 3773 ? 147.872 105.917 212.402 1.00 78.88  ? 3773 LEU A CD1   1 
ATOM   16200 C  CD2   . LEU A 1 3773 ? 147.006 105.529 210.090 1.00 83.12  ? 3773 LEU A CD2   1 
ATOM   16201 N  N     . LYS A 1 3774 ? 150.584 101.478 210.409 1.00 83.47  ? 3774 LYS A N     1 
ATOM   16202 C  CA    . LYS A 1 3774 ? 151.867 100.892 210.030 1.00 88.07  ? 3774 LYS A CA    1 
ATOM   16203 C  C     . LYS A 1 3774 ? 151.734 100.002 208.797 1.00 91.79  ? 3774 LYS A C     1 
ATOM   16204 O  O     . LYS A 1 3774 ? 152.599 100.020 207.912 1.00 90.80  ? 3774 LYS A O     1 
ATOM   16205 C  CB    . LYS A 1 3774 ? 152.452 100.105 211.202 1.00 88.27  ? 3774 LYS A CB    1 
ATOM   16206 C  CG    . LYS A 1 3774 ? 153.452 100.890 212.031 1.00 87.42  ? 3774 LYS A CG    1 
ATOM   16207 C  CD    . LYS A 1 3774 ? 154.713 101.189 211.234 1.00 92.12  ? 3774 LYS A CD    1 
ATOM   16208 C  CE    . LYS A 1 3774 ? 155.311 99.920  210.640 1.00 95.21  ? 3774 LYS A CE    1 
ATOM   16209 N  NZ    . LYS A 1 3774 ? 156.675 100.148 210.089 1.00 99.13  ? 3774 LYS A NZ    1 
ATOM   16210 N  N     . ARG A 1 3775 ? 150.661 99.209  208.726 1.00 86.80  ? 3775 ARG A N     1 
ATOM   16211 C  CA    . ARG A 1 3775 ? 150.444 98.362  207.557 1.00 87.21  ? 3775 ARG A CA    1 
ATOM   16212 C  C     . ARG A 1 3775 ? 150.241 99.200  206.301 1.00 89.69  ? 3775 ARG A C     1 
ATOM   16213 O  O     . ARG A 1 3775 ? 150.789 98.884  205.233 1.00 92.62  ? 3775 ARG A O     1 
ATOM   16214 C  CB    . ARG A 1 3775 ? 149.243 97.448  207.797 1.00 85.72  ? 3775 ARG A CB    1 
ATOM   16215 C  CG    . ARG A 1 3775 ? 149.066 96.357  206.757 1.00 87.06  ? 3775 ARG A CG    1 
ATOM   16216 C  CD    . ARG A 1 3775 ? 147.869 95.484  207.088 1.00 91.82  ? 3775 ARG A CD    1 
ATOM   16217 N  NE    . ARG A 1 3775 ? 147.792 95.188  208.514 1.00 98.12  ? 3775 ARG A NE    1 
ATOM   16218 C  CZ    . ARG A 1 3775 ? 146.714 95.378  209.261 1.00 95.29  ? 3775 ARG A CZ    1 
ATOM   16219 N  NH1   . ARG A 1 3775 ? 145.594 95.861  208.750 1.00 87.04  ? 3775 ARG A NH1   1 
ATOM   16220 N  NH2   . ARG A 1 3775 ? 146.760 95.075  210.556 1.00 92.07  ? 3775 ARG A NH2   1 
ATOM   16221 N  N     . GLU A 1 3776 ? 149.457 100.276 206.410 1.00 86.19  ? 3776 GLU A N     1 
ATOM   16222 C  CA    . GLU A 1 3776 ? 149.264 101.166 205.271 1.00 86.96  ? 3776 GLU A CA    1 
ATOM   16223 C  C     . GLU A 1 3776 ? 150.581 101.805 204.849 1.00 89.23  ? 3776 GLU A C     1 
ATOM   16224 O  O     . GLU A 1 3776 ? 150.866 101.924 203.652 1.00 92.07  ? 3776 GLU A O     1 
ATOM   16225 C  CB    . GLU A 1 3776 ? 148.230 102.238 205.612 1.00 82.47  ? 3776 GLU A CB    1 
ATOM   16226 C  CG    . GLU A 1 3776 ? 147.619 102.916 204.397 1.00 88.01  ? 3776 GLU A CG    1 
ATOM   16227 C  CD    . GLU A 1 3776 ? 146.459 103.821 204.756 1.00 94.28  ? 3776 GLU A CD    1 
ATOM   16228 O  OE1   . GLU A 1 3776 ? 146.136 103.928 205.957 1.00 97.81  ? 3776 GLU A OE1   1 
ATOM   16229 O  OE2   . GLU A 1 3776 ? 145.869 104.425 203.837 1.00 92.61  ? 3776 GLU A OE2   1 
ATOM   16230 N  N     . ALA A 1 3777 ? 151.400 102.215 205.821 1.00 86.32  ? 3777 ALA A N     1 
ATOM   16231 C  CA    . ALA A 1 3777 ? 152.696 102.798 205.497 1.00 86.79  ? 3777 ALA A CA    1 
ATOM   16232 C  C     . ALA A 1 3777 ? 153.579 101.802 204.758 1.00 86.44  ? 3777 ALA A C     1 
ATOM   16233 O  O     . ALA A 1 3777 ? 154.234 102.157 203.772 1.00 86.20  ? 3777 ALA A O     1 
ATOM   16234 C  CB    . ALA A 1 3777 ? 153.386 103.285 206.771 1.00 83.48  ? 3777 ALA A CB    1 
ATOM   16235 N  N     . ALA A 1 3778 ? 153.605 100.548 205.217 1.00 88.81  ? 3778 ALA A N     1 
ATOM   16236 C  CA    . ALA A 1 3778 ? 154.430 99.540  204.557 1.00 85.19  ? 3778 ALA A CA    1 
ATOM   16237 C  C     . ALA A 1 3778 ? 153.965 99.288  203.127 1.00 84.52  ? 3778 ALA A C     1 
ATOM   16238 O  O     . ALA A 1 3778 ? 154.785 99.217  202.199 1.00 83.16  ? 3778 ALA A O     1 
ATOM   16239 C  CB    . ALA A 1 3778 ? 154.416 98.241  205.362 1.00 80.22  ? 3778 ALA A CB    1 
ATOM   16240 N  N     . GLU A 1 3779 ? 152.650 99.150  202.926 1.00 86.59  ? 3779 GLU A N     1 
ATOM   16241 C  CA    . GLU A 1 3779 ? 152.153 98.889  201.577 1.00 84.56  ? 3779 GLU A CA    1 
ATOM   16242 C  C     . GLU A 1 3779 ? 152.416 100.074 200.651 1.00 82.11  ? 3779 GLU A C     1 
ATOM   16243 O  O     . GLU A 1 3779 ? 152.799 99.888  199.487 1.00 84.61  ? 3779 GLU A O     1 
ATOM   16244 C  CB    . GLU A 1 3779 ? 150.665 98.523  201.616 1.00 89.01  ? 3779 GLU A CB    1 
ATOM   16245 C  CG    . GLU A 1 3779 ? 149.699 99.678  201.814 1.00 92.91  ? 3779 GLU A CG    1 
ATOM   16246 C  CD    . GLU A 1 3779 ? 148.253 99.226  201.857 1.00 103.70 ? 3779 GLU A CD    1 
ATOM   16247 O  OE1   . GLU A 1 3779 ? 148.010 98.001  201.809 1.00 103.78 ? 3779 GLU A OE1   1 
ATOM   16248 O  OE2   . GLU A 1 3779 ? 147.359 100.094 201.937 1.00 104.74 ? 3779 GLU A OE2   1 
ATOM   16249 N  N     . VAL A 1 3780 ? 152.252 101.300 201.156 1.00 82.80  ? 3780 VAL A N     1 
ATOM   16250 C  CA    . VAL A 1 3780 ? 152.517 102.472 200.330 1.00 77.67  ? 3780 VAL A CA    1 
ATOM   16251 C  C     . VAL A 1 3780 ? 154.004 102.576 200.013 1.00 78.99  ? 3780 VAL A C     1 
ATOM   16252 O  O     . VAL A 1 3780 ? 154.384 102.987 198.914 1.00 82.32  ? 3780 VAL A O     1 
ATOM   16253 C  CB    . VAL A 1 3780 ? 151.980 103.743 201.013 1.00 71.72  ? 3780 VAL A CB    1 
ATOM   16254 C  CG1   . VAL A 1 3780 ? 152.415 104.984 200.255 1.00 69.10  ? 3780 VAL A CG1   1 
ATOM   16255 C  CG2   . VAL A 1 3780 ? 150.465 103.690 201.092 1.00 74.16  ? 3780 VAL A CG2   1 
ATOM   16256 N  N     . THR A 1 3781 ? 154.870 102.199 200.957 1.00 73.01  ? 3781 THR A N     1 
ATOM   16257 C  CA    . THR A 1 3781 ? 156.307 102.223 200.693 1.00 72.53  ? 3781 THR A CA    1 
ATOM   16258 C  C     . THR A 1 3781 ? 156.690 101.217 199.611 1.00 82.55  ? 3781 THR A C     1 
ATOM   16259 O  O     . THR A 1 3781 ? 157.524 101.510 198.744 1.00 84.19  ? 3781 THR A O     1 
ATOM   16260 C  CB    . THR A 1 3781 ? 157.081 101.946 201.981 1.00 75.01  ? 3781 THR A CB    1 
ATOM   16261 O  OG1   . THR A 1 3781 ? 156.578 102.782 203.030 1.00 79.93  ? 3781 THR A OG1   1 
ATOM   16262 C  CG2   . THR A 1 3781 ? 158.562 102.230 201.785 1.00 71.08  ? 3781 THR A CG2   1 
ATOM   16263 N  N     . ARG A 1 3782 ? 156.098 100.020 199.653 1.00 81.56  ? 3782 ARG A N     1 
ATOM   16264 C  CA    . ARG A 1 3782 ? 156.354 99.040  198.599 1.00 79.42  ? 3782 ARG A CA    1 
ATOM   16265 C  C     . ARG A 1 3782 ? 155.874 99.551  197.244 1.00 79.91  ? 3782 ARG A C     1 
ATOM   16266 O  O     . ARG A 1 3782 ? 156.566 99.404  196.223 1.00 82.50  ? 3782 ARG A O     1 
ATOM   16267 C  CB    . ARG A 1 3782 ? 155.679 97.714  198.948 1.00 80.49  ? 3782 ARG A CB    1 
ATOM   16268 C  CG    . ARG A 1 3782 ? 155.738 96.673  197.846 1.00 89.11  ? 3782 ARG A CG    1 
ATOM   16269 C  CD    . ARG A 1 3782 ? 154.658 95.620  198.032 1.00 86.84  ? 3782 ARG A CD    1 
ATOM   16270 N  NE    . ARG A 1 3782 ? 153.380 96.051  197.479 1.00 89.82  ? 3782 ARG A NE    1 
ATOM   16271 C  CZ    . ARG A 1 3782 ? 153.082 96.046  196.186 1.00 94.04  ? 3782 ARG A CZ    1 
ATOM   16272 N  NH1   . ARG A 1 3782 ? 153.948 95.627  195.278 1.00 93.67  ? 3782 ARG A NH1   1 
ATOM   16273 N  NH2   . ARG A 1 3782 ? 151.883 96.469  195.795 1.00 92.70  ? 3782 ARG A NH2   1 
ATOM   16274 N  N     . LYS A 1 3783 ? 154.688 100.163 197.215 1.00 76.03  ? 3783 LYS A N     1 
ATOM   16275 C  CA    . LYS A 1 3783 ? 154.198 100.744 195.970 1.00 79.34  ? 3783 LYS A CA    1 
ATOM   16276 C  C     . LYS A 1 3783 ? 155.121 101.860 195.488 1.00 75.49  ? 3783 LYS A C     1 
ATOM   16277 O  O     . LYS A 1 3783 ? 155.361 102.007 194.284 1.00 76.03  ? 3783 LYS A O     1 
ATOM   16278 C  CB    . LYS A 1 3783 ? 152.770 101.249 196.166 1.00 71.65  ? 3783 LYS A CB    1 
ATOM   16279 C  CG    . LYS A 1 3783 ? 151.751 100.130 196.306 1.00 71.54  ? 3783 LYS A CG    1 
ATOM   16280 C  CD    . LYS A 1 3783 ? 150.575 100.540 197.175 1.00 68.63  ? 3783 LYS A CD    1 
ATOM   16281 C  CE    . LYS A 1 3783 ? 149.548 101.325 196.384 1.00 63.47  ? 3783 LYS A CE    1 
ATOM   16282 N  NZ    . LYS A 1 3783 ? 148.953 100.508 195.291 1.00 65.43  ? 3783 LYS A NZ    1 
ATOM   16283 N  N     . VAL A 1 3784 ? 155.668 102.640 196.421 1.00 74.03  ? 3784 VAL A N     1 
ATOM   16284 C  CA    . VAL A 1 3784 ? 156.583 103.720 196.067 1.00 72.90  ? 3784 VAL A CA    1 
ATOM   16285 C  C     . VAL A 1 3784 ? 157.851 103.163 195.436 1.00 77.90  ? 3784 VAL A C     1 
ATOM   16286 O  O     . VAL A 1 3784 ? 158.348 103.699 194.440 1.00 83.76  ? 3784 VAL A O     1 
ATOM   16287 C  CB    . VAL A 1 3784 ? 156.896 104.582 197.305 1.00 70.68  ? 3784 VAL A CB    1 
ATOM   16288 C  CG1   . VAL A 1 3784 ? 158.191 105.356 197.110 1.00 65.33  ? 3784 VAL A CG1   1 
ATOM   16289 C  CG2   . VAL A 1 3784 ? 155.753 105.534 197.587 1.00 70.90  ? 3784 VAL A CG2   1 
ATOM   16290 N  N     . GLU A 1 3785 ? 158.402 102.087 196.003 1.00 74.56  ? 3785 GLU A N     1 
ATOM   16291 C  CA    . GLU A 1 3785 ? 159.646 101.553 195.451 1.00 80.24  ? 3785 GLU A CA    1 
ATOM   16292 C  C     . GLU A 1 3785 ? 159.422 100.933 194.072 1.00 79.57  ? 3785 GLU A C     1 
ATOM   16293 O  O     . GLU A 1 3785 ? 160.256 101.100 193.168 1.00 81.97  ? 3785 GLU A O     1 
ATOM   16294 C  CB    . GLU A 1 3785 ? 160.289 100.549 196.414 1.00 83.33  ? 3785 GLU A CB    1 
ATOM   16295 C  CG    . GLU A 1 3785 ? 159.523 99.265  196.648 1.00 84.76  ? 3785 GLU A CG    1 
ATOM   16296 C  CD    . GLU A 1 3785 ? 160.196 98.361  197.661 1.00 88.05  ? 3785 GLU A CD    1 
ATOM   16297 O  OE1   . GLU A 1 3785 ? 161.252 98.752  198.200 1.00 92.30  ? 3785 GLU A OE1   1 
ATOM   16298 O  OE2   . GLU A 1 3785 ? 159.667 97.259  197.921 1.00 90.55  ? 3785 GLU A OE2   1 
ATOM   16299 N  N     . GLU A 1 3786 ? 158.298 100.235 193.872 1.00 77.78  ? 3786 GLU A N     1 
ATOM   16300 C  CA    . GLU A 1 3786 ? 158.043 99.695  192.536 1.00 76.96  ? 3786 GLU A CA    1 
ATOM   16301 C  C     . GLU A 1 3786 ? 157.801 100.816 191.524 1.00 78.68  ? 3786 GLU A C     1 
ATOM   16302 O  O     . GLU A 1 3786 ? 158.269 100.742 190.375 1.00 79.86  ? 3786 GLU A O     1 
ATOM   16303 C  CB    . GLU A 1 3786 ? 156.876 98.704  192.567 1.00 75.94  ? 3786 GLU A CB    1 
ATOM   16304 C  CG    . GLU A 1 3786 ? 155.532 99.285  192.949 1.00 76.69  ? 3786 GLU A CG    1 
ATOM   16305 C  CD    . GLU A 1 3786 ? 154.496 98.218  193.235 1.00 83.91  ? 3786 GLU A CD    1 
ATOM   16306 O  OE1   . GLU A 1 3786 ? 154.870 97.029  193.304 1.00 87.35  ? 3786 GLU A OE1   1 
ATOM   16307 O  OE2   . GLU A 1 3786 ? 153.308 98.570  193.391 1.00 86.68  ? 3786 GLU A OE2   1 
ATOM   16308 N  N     . THR A 1 3787 ? 157.098 101.876 191.937 1.00 74.90  ? 3787 THR A N     1 
ATOM   16309 C  CA    . THR A 1 3787 ? 156.910 103.020 191.053 1.00 72.03  ? 3787 THR A CA    1 
ATOM   16310 C  C     . THR A 1 3787 ? 158.235 103.701 190.739 1.00 76.61  ? 3787 THR A C     1 
ATOM   16311 O  O     . THR A 1 3787 ? 158.427 104.198 189.627 1.00 78.82  ? 3787 THR A O     1 
ATOM   16312 C  CB    . THR A 1 3787 ? 155.932 104.013 191.681 1.00 74.02  ? 3787 THR A CB    1 
ATOM   16313 O  OG1   . THR A 1 3787 ? 154.771 103.311 192.141 1.00 79.12  ? 3787 THR A OG1   1 
ATOM   16314 C  CG2   . THR A 1 3787 ? 155.503 105.055 190.661 1.00 73.89  ? 3787 THR A CG2   1 
ATOM   16315 N  N     . ASP A 1 3788 ? 159.159 103.732 191.702 1.00 77.88  ? 3788 ASP A N     1 
ATOM   16316 C  CA    . ASP A 1 3788 ? 160.486 104.286 191.449 1.00 77.21  ? 3788 ASP A CA    1 
ATOM   16317 C  C     . ASP A 1 3788 ? 161.250 103.447 190.434 1.00 71.78  ? 3788 ASP A C     1 
ATOM   16318 O  O     . ASP A 1 3788 ? 161.975 103.989 189.590 1.00 72.42  ? 3788 ASP A O     1 
ATOM   16319 C  CB    . ASP A 1 3788 ? 161.268 104.390 192.757 1.00 78.04  ? 3788 ASP A CB    1 
ATOM   16320 C  CG    . ASP A 1 3788 ? 161.059 105.718 193.457 1.00 87.45  ? 3788 ASP A CG    1 
ATOM   16321 O  OD1   . ASP A 1 3788 ? 160.288 106.551 192.936 1.00 88.72  ? 3788 ASP A OD1   1 
ATOM   16322 O  OD2   . ASP A 1 3788 ? 161.666 105.930 194.528 1.00 92.95  ? 3788 ASP A OD2   1 
ATOM   16323 N  N     . ILE A 1 3789 ? 161.114 102.122 190.510 1.00 69.90  ? 3789 ILE A N     1 
ATOM   16324 C  CA    . ILE A 1 3789 ? 161.740 101.258 189.509 1.00 74.65  ? 3789 ILE A CA    1 
ATOM   16325 C  C     . ILE A 1 3789 ? 161.196 101.577 188.120 1.00 71.27  ? 3789 ILE A C     1 
ATOM   16326 O  O     . ILE A 1 3789 ? 161.953 101.722 187.147 1.00 67.46  ? 3789 ILE A O     1 
ATOM   16327 C  CB    . ILE A 1 3789 ? 161.531 99.777  189.871 1.00 69.55  ? 3789 ILE A CB    1 
ATOM   16328 C  CG1   . ILE A 1 3789 ? 162.260 99.436  191.172 1.00 68.48  ? 3789 ILE A CG1   1 
ATOM   16329 C  CG2   . ILE A 1 3789 ? 162.002 98.879  188.738 1.00 61.24  ? 3789 ILE A CG2   1 
ATOM   16330 C  CD1   . ILE A 1 3789 ? 162.210 97.968  191.533 1.00 66.44  ? 3789 ILE A CD1   1 
ATOM   16331 N  N     . VAL A 1 3790 ? 159.872 101.708 188.010 1.00 70.48  ? 3790 VAL A N     1 
ATOM   16332 C  CA    . VAL A 1 3790 ? 159.278 102.025 186.711 1.00 67.72  ? 3790 VAL A CA    1 
ATOM   16333 C  C     . VAL A 1 3790 ? 159.711 103.415 186.244 1.00 66.68  ? 3790 VAL A C     1 
ATOM   16334 O  O     . VAL A 1 3790 ? 159.901 103.656 185.044 1.00 67.04  ? 3790 VAL A O     1 
ATOM   16335 C  CB    . VAL A 1 3790 ? 157.745 101.891 186.777 1.00 69.07  ? 3790 VAL A CB    1 
ATOM   16336 C  CG1   . VAL A 1 3790 ? 157.127 102.148 185.412 1.00 61.48  ? 3790 VAL A CG1   1 
ATOM   16337 C  CG2   . VAL A 1 3790 ? 157.359 100.511 187.283 1.00 70.29  ? 3790 VAL A CG2   1 
ATOM   16338 N  N     . MET A 1 3791 ? 159.874 104.351 187.183 1.00 66.93  ? 3791 MET A N     1 
ATOM   16339 C  CA    . MET A 1 3791 ? 160.333 105.692 186.836 1.00 63.18  ? 3791 MET A CA    1 
ATOM   16340 C  C     . MET A 1 3791 ? 161.751 105.669 186.286 1.00 67.11  ? 3791 MET A C     1 
ATOM   16341 O  O     . MET A 1 3791 ? 162.064 106.388 185.331 1.00 67.12  ? 3791 MET A O     1 
ATOM   16342 C  CB    . MET A 1 3791 ? 160.249 106.604 188.059 1.00 72.05  ? 3791 MET A CB    1 
ATOM   16343 C  CG    . MET A 1 3791 ? 160.918 107.953 187.872 1.00 78.31  ? 3791 MET A CG    1 
ATOM   16344 S  SD    . MET A 1 3791 ? 160.015 108.980 186.700 1.00 84.08  ? 3791 MET A SD    1 
ATOM   16345 C  CE    . MET A 1 3791 ? 158.362 108.852 187.373 1.00 68.10  ? 3791 MET A CE    1 
ATOM   16346 N  N     . GLN A 1 3792 ? 162.628 104.862 186.887 1.00 71.30  ? 3792 GLN A N     1 
ATOM   16347 C  CA    . GLN A 1 3792 ? 163.967 104.692 186.332 1.00 66.19  ? 3792 GLN A CA    1 
ATOM   16348 C  C     . GLN A 1 3792 ? 163.909 104.083 184.938 1.00 62.66  ? 3792 GLN A C     1 
ATOM   16349 O  O     . GLN A 1 3792 ? 164.680 104.478 184.051 1.00 61.49  ? 3792 GLN A O     1 
ATOM   16350 C  CB    . GLN A 1 3792 ? 164.818 103.823 187.256 1.00 66.84  ? 3792 GLN A CB    1 
ATOM   16351 C  CG    . GLN A 1 3792 ? 165.140 104.464 188.594 1.00 71.39  ? 3792 GLN A CG    1 
ATOM   16352 C  CD    . GLN A 1 3792 ? 165.925 103.539 189.504 1.00 84.38  ? 3792 GLN A CD    1 
ATOM   16353 O  OE1   . GLN A 1 3792 ? 165.855 102.316 189.375 1.00 83.36  ? 3792 GLN A OE1   1 
ATOM   16354 N  NE2   . GLN A 1 3792 ? 166.680 104.119 190.430 1.00 77.59  ? 3792 GLN A NE2   1 
ATOM   16355 N  N     . GLU A 1 3793 ? 162.998 103.130 184.728 1.00 60.34  ? 3793 GLU A N     1 
ATOM   16356 C  CA    . GLU A 1 3793 ? 162.819 102.565 183.394 1.00 65.33  ? 3793 GLU A CA    1 
ATOM   16357 C  C     . GLU A 1 3793 ? 162.446 103.647 182.384 1.00 62.65  ? 3793 GLU A C     1 
ATOM   16358 O  O     . GLU A 1 3793 ? 162.998 103.694 181.279 1.00 62.53  ? 3793 GLU A O     1 
ATOM   16359 C  CB    . GLU A 1 3793 ? 161.756 101.465 183.434 1.00 67.86  ? 3793 GLU A CB    1 
ATOM   16360 C  CG    . GLU A 1 3793 ? 161.001 101.237 182.128 1.00 68.00  ? 3793 GLU A CG    1 
ATOM   16361 C  CD    . GLU A 1 3793 ? 161.912 100.850 180.977 1.00 75.63  ? 3793 GLU A CD    1 
ATOM   16362 O  OE1   . GLU A 1 3793 ? 162.668 99.867  181.120 1.00 78.17  ? 3793 GLU A OE1   1 
ATOM   16363 O  OE2   . GLU A 1 3793 ? 161.865 101.526 179.927 1.00 74.81  ? 3793 GLU A OE2   1 
ATOM   16364 N  N     . VAL A 1 3794 ? 161.520 104.534 182.753 1.00 60.44  ? 3794 VAL A N     1 
ATOM   16365 C  CA    . VAL A 1 3794 ? 161.107 105.607 181.847 1.00 54.63  ? 3794 VAL A CA    1 
ATOM   16366 C  C     . VAL A 1 3794 ? 162.252 106.591 181.611 1.00 55.26  ? 3794 VAL A C     1 
ATOM   16367 O  O     . VAL A 1 3794 ? 162.456 107.081 180.489 1.00 53.36  ? 3794 VAL A O     1 
ATOM   16368 C  CB    . VAL A 1 3794 ? 159.855 106.314 182.398 1.00 49.12  ? 3794 VAL A CB    1 
ATOM   16369 C  CG1   . VAL A 1 3794 ? 159.504 107.525 181.549 1.00 51.77  ? 3794 VAL A CG1   1 
ATOM   16370 C  CG2   . VAL A 1 3794 ? 158.685 105.348 182.458 1.00 54.78  ? 3794 VAL A CG2   1 
ATOM   16371 N  N     . GLU A 1 3795 ? 163.010 106.906 182.664 1.00 54.33  ? 3795 GLU A N     1 
ATOM   16372 C  CA    . GLU A 1 3795 ? 164.140 107.819 182.525 1.00 48.91  ? 3795 GLU A CA    1 
ATOM   16373 C  C     . GLU A 1 3795 ? 165.196 107.256 181.586 1.00 50.45  ? 3795 GLU A C     1 
ATOM   16374 O  O     . GLU A 1 3795 ? 165.879 108.018 180.888 1.00 51.33  ? 3795 GLU A O     1 
ATOM   16375 C  CB    . GLU A 1 3795 ? 164.745 108.111 183.899 1.00 53.65  ? 3795 GLU A CB    1 
ATOM   16376 C  CG    . GLU A 1 3795 ? 165.883 109.116 183.884 1.00 58.47  ? 3795 GLU A CG    1 
ATOM   16377 C  CD    . GLU A 1 3795 ? 166.416 109.409 185.272 1.00 66.55  ? 3795 GLU A CD    1 
ATOM   16378 O  OE1   . GLU A 1 3795 ? 165.909 108.810 186.243 1.00 69.33  ? 3795 GLU A OE1   1 
ATOM   16379 O  OE2   . GLU A 1 3795 ? 167.342 110.238 185.392 1.00 70.89  ? 3795 GLU A OE2   1 
ATOM   16380 N  N     . THR A 1 3796 ? 165.346 105.929 181.557 1.00 55.70  ? 3796 THR A N     1 
ATOM   16381 C  CA    . THR A 1 3796 ? 166.259 105.313 180.598 1.00 55.77  ? 3796 THR A CA    1 
ATOM   16382 C  C     . THR A 1 3796 ? 165.897 105.702 179.168 1.00 46.23  ? 3796 THR A C     1 
ATOM   16383 O  O     . THR A 1 3796 ? 166.776 106.029 178.363 1.00 45.52  ? 3796 THR A O     1 
ATOM   16384 C  CB    . THR A 1 3796 ? 166.247 103.792 180.758 1.00 60.26  ? 3796 THR A CB    1 
ATOM   16385 O  OG1   . THR A 1 3796 ? 166.669 103.445 182.083 1.00 67.00  ? 3796 THR A OG1   1 
ATOM   16386 C  CG2   . THR A 1 3796 ? 167.178 103.139 179.748 1.00 50.30  ? 3796 THR A CG2   1 
ATOM   16387 N  N     . VAL A 1 3797 ? 164.604 105.680 178.838 1.00 48.65  ? 3797 VAL A N     1 
ATOM   16388 C  CA    . VAL A 1 3797 ? 164.164 106.105 177.512 1.00 44.52  ? 3797 VAL A CA    1 
ATOM   16389 C  C     . VAL A 1 3797 ? 164.370 107.606 177.332 1.00 44.40  ? 3797 VAL A C     1 
ATOM   16390 O  O     . VAL A 1 3797 ? 164.810 108.063 176.271 1.00 43.50  ? 3797 VAL A O     1 
ATOM   16391 C  CB    . VAL A 1 3797 ? 162.696 105.699 177.289 1.00 39.61  ? 3797 VAL A CB    1 
ATOM   16392 C  CG1   . VAL A 1 3797 ? 162.124 106.388 176.059 1.00 35.72  ? 3797 VAL A CG1   1 
ATOM   16393 C  CG2   . VAL A 1 3797 ? 162.577 104.189 177.166 1.00 44.42  ? 3797 VAL A CG2   1 
ATOM   16394 N  N     . SER A 1 3798 ? 164.058 108.395 178.365 1.00 41.55  ? 3798 SER A N     1 
ATOM   16395 C  CA    . SER A 1 3798 ? 164.174 109.850 178.259 1.00 36.24  ? 3798 SER A CA    1 
ATOM   16396 C  C     . SER A 1 3798 ? 165.612 110.319 178.043 1.00 37.63  ? 3798 SER A C     1 
ATOM   16397 O  O     . SER A 1 3798 ? 165.824 111.428 177.525 1.00 33.12  ? 3798 SER A O     1 
ATOM   16398 C  CB    . SER A 1 3798 ? 163.598 110.512 179.511 1.00 36.22  ? 3798 SER A CB    1 
ATOM   16399 O  OG    . SER A 1 3798 ? 162.345 109.949 179.852 1.00 47.09  ? 3798 SER A OG    1 
ATOM   16400 N  N     . GLN A 1 3799 ? 166.596 109.516 178.458 1.00 37.02  ? 3799 GLN A N     1 
ATOM   16401 C  CA    . GLN A 1 3799 ? 167.995 109.888 178.252 1.00 34.93  ? 3799 GLN A CA    1 
ATOM   16402 C  C     . GLN A 1 3799 ? 168.312 110.125 176.780 1.00 36.67  ? 3799 GLN A C     1 
ATOM   16403 O  O     . GLN A 1 3799 ? 169.154 110.970 176.457 1.00 35.09  ? 3799 GLN A O     1 
ATOM   16404 C  CB    . GLN A 1 3799 ? 168.924 108.809 178.812 1.00 41.68  ? 3799 GLN A CB    1 
ATOM   16405 C  CG    . GLN A 1 3799 ? 168.866 108.629 180.319 1.00 44.78  ? 3799 GLN A CG    1 
ATOM   16406 C  CD    . GLN A 1 3799 ? 169.298 109.868 181.074 1.00 54.13  ? 3799 GLN A CD    1 
ATOM   16407 O  OE1   . GLN A 1 3799 ? 168.481 110.547 181.695 1.00 58.89  ? 3799 GLN A OE1   1 
ATOM   16408 N  NE2   . GLN A 1 3799 ? 170.590 110.171 181.024 1.00 48.89  ? 3799 GLN A NE2   1 
ATOM   16409 N  N     . GLN A 1 3800 ? 167.662 109.386 175.877 1.00 32.61  ? 3800 GLN A N     1 
ATOM   16410 C  CA    . GLN A 1 3800 ? 167.951 109.534 174.453 1.00 26.46  ? 3800 GLN A CA    1 
ATOM   16411 C  C     . GLN A 1 3800 ? 167.518 110.899 173.931 1.00 30.74  ? 3800 GLN A C     1 
ATOM   16412 O  O     . GLN A 1 3800 ? 168.212 111.502 173.106 1.00 31.99  ? 3800 GLN A O     1 
ATOM   16413 C  CB    . GLN A 1 3800 ? 167.272 108.418 173.662 1.00 31.00  ? 3800 GLN A CB    1 
ATOM   16414 C  CG    . GLN A 1 3800 ? 167.827 108.230 172.261 1.00 40.68  ? 3800 GLN A CG    1 
ATOM   16415 C  CD    . GLN A 1 3800 ? 166.986 107.293 171.421 1.00 38.14  ? 3800 GLN A CD    1 
ATOM   16416 O  OE1   . GLN A 1 3800 ? 165.918 106.852 171.842 1.00 41.00  ? 3800 GLN A OE1   1 
ATOM   16417 N  NE2   . GLN A 1 3800 ? 167.465 106.981 170.225 1.00 38.83  ? 3800 GLN A NE2   1 
ATOM   16418 N  N     . TYR A 1 3801 ? 166.372 111.397 174.391 1.00 29.46  ? 3801 TYR A N     1 
ATOM   16419 C  CA    . TYR A 1 3801 ? 165.853 112.679 173.936 1.00 22.61  ? 3801 TYR A CA    1 
ATOM   16420 C  C     . TYR A 1 3801 ? 166.360 113.859 174.754 1.00 23.73  ? 3801 TYR A C     1 
ATOM   16421 O  O     . TYR A 1 3801 ? 166.097 115.006 174.378 1.00 22.31  ? 3801 TYR A O     1 
ATOM   16422 C  CB    . TYR A 1 3801 ? 164.321 112.662 173.956 1.00 26.21  ? 3801 TYR A CB    1 
ATOM   16423 C  CG    . TYR A 1 3801 ? 163.714 111.621 173.047 1.00 25.93  ? 3801 TYR A CG    1 
ATOM   16424 C  CD1   . TYR A 1 3801 ? 163.462 110.335 173.501 1.00 28.26  ? 3801 TYR A CD1   1 
ATOM   16425 C  CD2   . TYR A 1 3801 ? 163.390 111.926 171.733 1.00 26.48  ? 3801 TYR A CD2   1 
ATOM   16426 C  CE1   . TYR A 1 3801 ? 162.908 109.380 172.671 1.00 34.18  ? 3801 TYR A CE1   1 
ATOM   16427 C  CE2   . TYR A 1 3801 ? 162.835 110.979 170.895 1.00 27.24  ? 3801 TYR A CE2   1 
ATOM   16428 C  CZ    . TYR A 1 3801 ? 162.596 109.709 171.370 1.00 34.77  ? 3801 TYR A CZ    1 
ATOM   16429 O  OH    . TYR A 1 3801 ? 162.043 108.763 170.539 1.00 39.54  ? 3801 TYR A OH    1 
ATOM   16430 N  N     . LEU A 1 3802 ? 167.057 113.609 175.861 1.00 26.74  ? 3802 LEU A N     1 
ATOM   16431 C  CA    . LEU A 1 3802 ? 167.661 114.699 176.631 1.00 24.34  ? 3802 LEU A CA    1 
ATOM   16432 C  C     . LEU A 1 3802 ? 168.562 115.628 175.814 1.00 19.57  ? 3802 LEU A C     1 
ATOM   16433 O  O     . LEU A 1 3802 ? 168.441 116.857 175.968 1.00 22.17  ? 3802 LEU A O     1 
ATOM   16434 C  CB    . LEU A 1 3802 ? 168.423 114.095 177.819 1.00 28.34  ? 3802 LEU A CB    1 
ATOM   16435 C  CG    . LEU A 1 3802 ? 168.957 115.059 178.877 1.00 30.19  ? 3802 LEU A CG    1 
ATOM   16436 C  CD1   . LEU A 1 3802 ? 167.809 115.693 179.643 1.00 29.28  ? 3802 LEU A CD1   1 
ATOM   16437 C  CD2   . LEU A 1 3802 ? 169.903 114.339 179.821 1.00 28.22  ? 3802 LEU A CD2   1 
ATOM   16438 N  N     . PRO A 1 3803 ? 169.480 115.139 174.965 1.00 21.77  ? 3803 PRO A N     1 
ATOM   16439 C  CA    . PRO A 1 3803 ? 170.336 116.075 174.210 1.00 17.90  ? 3803 PRO A CA    1 
ATOM   16440 C  C     . PRO A 1 3803 ? 169.564 117.022 173.311 1.00 16.41  ? 3803 PRO A C     1 
ATOM   16441 O  O     . PRO A 1 3803 ? 169.991 118.169 173.122 1.00 14.35  ? 3803 PRO A O     1 
ATOM   16442 C  CB    . PRO A 1 3803 ? 171.243 115.143 173.394 1.00 12.28  ? 3803 PRO A CB    1 
ATOM   16443 C  CG    . PRO A 1 3803 ? 171.244 113.869 174.140 1.00 22.63  ? 3803 PRO A CG    1 
ATOM   16444 C  CD    . PRO A 1 3803 ? 169.866 113.740 174.705 1.00 25.02  ? 3803 PRO A CD    1 
ATOM   16445 N  N     . LEU A 1 3804 ? 168.441 116.577 172.745 1.00 17.52  ? 3804 LEU A N     1 
ATOM   16446 C  CA    . LEU A 1 3804 ? 167.620 117.477 171.945 1.00 11.91  ? 3804 LEU A CA    1 
ATOM   16447 C  C     . LEU A 1 3804 ? 167.085 118.623 172.793 1.00 14.36  ? 3804 LEU A C     1 
ATOM   16448 O  O     . LEU A 1 3804 ? 167.066 119.774 172.349 1.00 15.78  ? 3804 LEU A O     1 
ATOM   16449 C  CB    . LEU A 1 3804 ? 166.473 116.708 171.292 1.00 11.36  ? 3804 LEU A CB    1 
ATOM   16450 C  CG    . LEU A 1 3804 ? 165.489 117.552 170.481 1.00 16.77  ? 3804 LEU A CG    1 
ATOM   16451 C  CD1   . LEU A 1 3804 ? 166.215 118.299 169.376 1.00 15.19  ? 3804 LEU A CD1   1 
ATOM   16452 C  CD2   . LEU A 1 3804 ? 164.380 116.690 169.906 1.00 15.69  ? 3804 LEU A CD2   1 
ATOM   16453 N  N     . SER A 1 3805 ? 166.651 118.326 174.021 1.00 14.03  ? 3805 SER A N     1 
ATOM   16454 C  CA    . SER A 1 3805 ? 166.175 119.379 174.913 1.00 12.96  ? 3805 SER A CA    1 
ATOM   16455 C  C     . SER A 1 3805 ? 167.296 120.347 175.274 1.00 13.42  ? 3805 SER A C     1 
ATOM   16456 O  O     . SER A 1 3805 ? 167.079 121.565 175.346 1.00 15.12  ? 3805 SER A O     1 
ATOM   16457 C  CB    . SER A 1 3805 ? 165.568 118.764 176.172 1.00 14.76  ? 3805 SER A CB    1 
ATOM   16458 O  OG    . SER A 1 3805 ? 166.539 118.043 176.910 1.00 21.34  ? 3805 SER A OG    1 
ATOM   16459 N  N     . THR A 1 3806 ? 168.502 119.824 175.514 1.00 12.63  ? 3806 THR A N     1 
ATOM   16460 C  CA    . THR A 1 3806 ? 169.633 120.709 175.790 1.00 14.30  ? 3806 THR A CA    1 
ATOM   16461 C  C     . THR A 1 3806 ? 169.914 121.632 174.608 1.00 12.41  ? 3806 THR A C     1 
ATOM   16462 O  O     . THR A 1 3806 ? 170.131 122.840 174.783 1.00 12.90  ? 3806 THR A O     1 
ATOM   16463 C  CB    . THR A 1 3806 ? 170.872 119.884 176.135 1.00 17.32  ? 3806 THR A CB    1 
ATOM   16464 O  OG1   . THR A 1 3806 ? 170.616 119.104 177.309 1.00 18.93  ? 3806 THR A OG1   1 
ATOM   16465 C  CG2   . THR A 1 3806 ? 172.065 120.792 176.388 1.00 13.49  ? 3806 THR A CG2   1 
ATOM   16466 N  N     . ALA A 1 3807 ? 169.901 121.079 173.392 1.00 13.67  ? 3807 ALA A N     1 
ATOM   16467 C  CA    . ALA A 1 3807 ? 170.116 121.898 172.203 1.00 11.94  ? 3807 ALA A CA    1 
ATOM   16468 C  C     . ALA A 1 3807 ? 169.015 122.938 172.046 1.00 12.54  ? 3807 ALA A C     1 
ATOM   16469 O  O     . ALA A 1 3807 ? 169.280 124.078 171.647 1.00 14.24  ? 3807 ALA A O     1 
ATOM   16470 C  CB    . ALA A 1 3807 ? 170.199 121.010 170.963 1.00 10.72  ? 3807 ALA A CB    1 
ATOM   16471 N  N     . CYS A 1 3808 ? 167.771 122.559 172.343 1.00 11.93  ? 3808 CYS A N     1 
ATOM   16472 C  CA    . CYS A 1 3808 ? 166.661 123.502 172.261 1.00 12.31  ? 3808 CYS A CA    1 
ATOM   16473 C  C     . CYS A 1 3808 ? 166.857 124.667 173.218 1.00 12.83  ? 3808 CYS A C     1 
ATOM   16474 O  O     . CYS A 1 3808 ? 166.638 125.829 172.852 1.00 14.88  ? 3808 CYS A O     1 
ATOM   16475 C  CB    . CYS A 1 3808 ? 165.347 122.785 172.564 1.00 11.35  ? 3808 CYS A CB    1 
ATOM   16476 S  SG    . CYS A 1 3808 ? 164.810 121.636 171.296 1.00 24.69  ? 3808 CYS A SG    1 
ATOM   16477 N  N     . SER A 1 3809 ? 167.259 124.373 174.456 1.00 10.62  ? 3809 SER A N     1 
ATOM   16478 C  CA    . SER A 1 3809 ? 167.515 125.441 175.417 1.00 10.20  ? 3809 SER A CA    1 
ATOM   16479 C  C     . SER A 1 3809 ? 168.635 126.353 174.935 1.00 12.82  ? 3809 SER A C     1 
ATOM   16480 O  O     . SER A 1 3809 ? 168.532 127.584 175.030 1.00 16.34  ? 3809 SER A O     1 
ATOM   16481 C  CB    . SER A 1 3809 ? 167.852 124.849 176.783 1.00 14.60  ? 3809 SER A CB    1 
ATOM   16482 O  OG    . SER A 1 3809 ? 169.234 124.551 176.883 1.00 15.53  ? 3809 SER A OG    1 
ATOM   16483 N  N     . SER A 1 3810 ? 169.710 125.764 174.404 1.00 12.56  ? 3810 SER A N     1 
ATOM   16484 C  CA    . SER A 1 3810 ? 170.815 126.575 173.902 1.00 8.50   ? 3810 SER A CA    1 
ATOM   16485 C  C     . SER A 1 3810 ? 170.361 127.488 172.769 1.00 8.82   ? 3810 SER A C     1 
ATOM   16486 O  O     . SER A 1 3810 ? 170.717 128.672 172.732 1.00 8.62   ? 3810 SER A O     1 
ATOM   16487 C  CB    . SER A 1 3810 ? 171.957 125.671 173.440 1.00 7.99   ? 3810 SER A CB    1 
ATOM   16488 O  OG    . SER A 1 3810 ? 172.297 124.730 174.441 1.00 11.20  ? 3810 SER A OG    1 
ATOM   16489 N  N     . ILE A 1 3811 ? 169.558 126.958 171.845 1.00 11.00  ? 3811 ILE A N     1 
ATOM   16490 C  CA    . ILE A 1 3811 ? 169.107 127.746 170.703 1.00 9.23   ? 3811 ILE A CA    1 
ATOM   16491 C  C     . ILE A 1 3811 ? 168.187 128.875 171.154 1.00 10.24  ? 3811 ILE A C     1 
ATOM   16492 O  O     . ILE A 1 3811 ? 168.289 130.012 170.669 1.00 13.54  ? 3811 ILE A O     1 
ATOM   16493 C  CB    . ILE A 1 3811 ? 168.424 126.833 169.669 1.00 8.43   ? 3811 ILE A CB    1 
ATOM   16494 C  CG1   . ILE A 1 3811 ? 169.432 125.855 169.070 1.00 10.20  ? 3811 ILE A CG1   1 
ATOM   16495 C  CG2   . ILE A 1 3811 ? 167.823 127.652 168.559 1.00 10.41  ? 3811 ILE A CG2   1 
ATOM   16496 C  CD1   . ILE A 1 3811 ? 168.820 124.883 168.091 1.00 11.02  ? 3811 ILE A CD1   1 
ATOM   16497 N  N     . TYR A 1 3812 ? 167.269 128.587 172.082 1.00 10.84  ? 3812 TYR A N     1 
ATOM   16498 C  CA    . TYR A 1 3812 ? 166.381 129.639 172.567 1.00 10.88  ? 3812 TYR A CA    1 
ATOM   16499 C  C     . TYR A 1 3812 ? 167.160 130.740 173.268 1.00 9.82   ? 3812 TYR A C     1 
ATOM   16500 O  O     . TYR A 1 3812 ? 166.871 131.928 173.084 1.00 11.40  ? 3812 TYR A O     1 
ATOM   16501 C  CB    . TYR A 1 3812 ? 165.326 129.080 173.515 1.00 13.52  ? 3812 TYR A CB    1 
ATOM   16502 C  CG    . TYR A 1 3812 ? 164.599 130.184 174.253 1.00 13.86  ? 3812 TYR A CG    1 
ATOM   16503 C  CD1   . TYR A 1 3812 ? 163.717 131.022 173.588 1.00 15.28  ? 3812 TYR A CD1   1 
ATOM   16504 C  CD2   . TYR A 1 3812 ? 164.832 130.419 175.602 1.00 14.08  ? 3812 TYR A CD2   1 
ATOM   16505 C  CE1   . TYR A 1 3812 ? 163.064 132.041 174.250 1.00 15.90  ? 3812 TYR A CE1   1 
ATOM   16506 C  CE2   . TYR A 1 3812 ? 164.184 131.435 176.271 1.00 14.87  ? 3812 TYR A CE2   1 
ATOM   16507 C  CZ    . TYR A 1 3812 ? 163.302 132.243 175.591 1.00 17.18  ? 3812 TYR A CZ    1 
ATOM   16508 O  OH    . TYR A 1 3812 ? 162.655 133.257 176.256 1.00 22.66  ? 3812 TYR A OH    1 
ATOM   16509 N  N     . PHE A 1 3813 ? 168.139 130.371 174.097 1.00 9.86   ? 3813 PHE A N     1 
ATOM   16510 C  CA    . PHE A 1 3813 ? 168.909 131.402 174.782 1.00 9.61   ? 3813 PHE A CA    1 
ATOM   16511 C  C     . PHE A 1 3813 ? 169.789 132.180 173.812 1.00 10.53  ? 3813 PHE A C     1 
ATOM   16512 O  O     . PHE A 1 3813 ? 170.050 133.368 174.033 1.00 13.92  ? 3813 PHE A O     1 
ATOM   16513 C  CB    . PHE A 1 3813 ? 169.728 130.782 175.911 1.00 12.93  ? 3813 PHE A CB    1 
ATOM   16514 C  CG    . PHE A 1 3813 ? 168.961 130.647 177.195 1.00 19.21  ? 3813 PHE A CG    1 
ATOM   16515 C  CD1   . PHE A 1 3813 ? 168.206 129.516 177.452 1.00 19.68  ? 3813 PHE A CD1   1 
ATOM   16516 C  CD2   . PHE A 1 3813 ? 168.979 131.661 178.136 1.00 22.19  ? 3813 PHE A CD2   1 
ATOM   16517 C  CE1   . PHE A 1 3813 ? 167.489 129.396 178.627 1.00 17.98  ? 3813 PHE A CE1   1 
ATOM   16518 C  CE2   . PHE A 1 3813 ? 168.267 131.545 179.314 1.00 21.37  ? 3813 PHE A CE2   1 
ATOM   16519 C  CZ    . PHE A 1 3813 ? 167.523 130.410 179.559 1.00 19.60  ? 3813 PHE A CZ    1 
ATOM   16520 N  N     . THR A 1 3814 ? 170.228 131.545 172.723 1.00 9.13   ? 3814 THR A N     1 
ATOM   16521 C  CA    . THR A 1 3814 ? 170.914 132.285 171.670 1.00 7.72   ? 3814 THR A CA    1 
ATOM   16522 C  C     . THR A 1 3814 ? 169.993 133.320 171.032 1.00 9.94   ? 3814 THR A C     1 
ATOM   16523 O  O     . THR A 1 3814 ? 170.394 134.470 170.816 1.00 11.64  ? 3814 THR A O     1 
ATOM   16524 C  CB    . THR A 1 3814 ? 171.455 131.318 170.618 1.00 11.10  ? 3814 THR A CB    1 
ATOM   16525 O  OG1   . THR A 1 3814 ? 172.416 130.446 171.224 1.00 11.77  ? 3814 THR A OG1   1 
ATOM   16526 C  CG2   . THR A 1 3814 ? 172.118 132.076 169.480 1.00 11.50  ? 3814 THR A CG2   1 
ATOM   16527 N  N     . MET A 1 3815 ? 168.746 132.936 170.736 1.00 10.28  ? 3815 MET A N     1 
ATOM   16528 C  CA    . MET A 1 3815 ? 167.798 133.924 170.222 1.00 8.86   ? 3815 MET A CA    1 
ATOM   16529 C  C     . MET A 1 3815 ? 167.569 135.045 171.227 1.00 9.50   ? 3815 MET A C     1 
ATOM   16530 O  O     . MET A 1 3815 ? 167.467 136.217 170.848 1.00 16.24  ? 3815 MET A O     1 
ATOM   16531 C  CB    . MET A 1 3815 ? 166.456 133.291 169.853 1.00 8.96   ? 3815 MET A CB    1 
ATOM   16532 C  CG    . MET A 1 3815 ? 166.479 132.136 168.882 1.00 7.09   ? 3815 MET A CG    1 
ATOM   16533 S  SD    . MET A 1 3815 ? 164.850 131.364 168.875 1.00 20.14  ? 3815 MET A SD    1 
ATOM   16534 C  CE    . MET A 1 3815 ? 165.179 129.832 168.023 1.00 14.81  ? 3815 MET A CE    1 
ATOM   16535 N  N     . GLU A 1 3816 ? 167.462 134.700 172.510 1.00 9.80   ? 3816 GLU A N     1 
ATOM   16536 C  CA    . GLU A 1 3816 ? 167.234 135.717 173.530 1.00 12.75  ? 3816 GLU A CA    1 
ATOM   16537 C  C     . GLU A 1 3816 ? 168.399 136.698 173.598 1.00 12.41  ? 3816 GLU A C     1 
ATOM   16538 O  O     . GLU A 1 3816 ? 168.194 137.909 173.737 1.00 13.61  ? 3816 GLU A O     1 
ATOM   16539 C  CB    . GLU A 1 3816 ? 167.003 135.057 174.889 1.00 13.12  ? 3816 GLU A CB    1 
ATOM   16540 C  CG    . GLU A 1 3816 ? 166.677 136.036 176.002 1.00 24.03  ? 3816 GLU A CG    1 
ATOM   16541 C  CD    . GLU A 1 3816 ? 166.404 135.348 177.324 1.00 40.95  ? 3816 GLU A CD    1 
ATOM   16542 O  OE1   . GLU A 1 3816 ? 166.490 134.103 177.375 1.00 48.32  ? 3816 GLU A OE1   1 
ATOM   16543 O  OE2   . GLU A 1 3816 ? 166.107 136.050 178.312 1.00 37.24  ? 3816 GLU A OE2   1 
ATOM   16544 N  N     . SER A 1 3817 ? 169.629 136.195 173.498 1.00 11.44  ? 3817 SER A N     1 
ATOM   16545 C  CA    . SER A 1 3817 ? 170.805 137.054 173.494 1.00 12.75  ? 3817 SER A CA    1 
ATOM   16546 C  C     . SER A 1 3817 ? 170.994 137.802 172.180 1.00 12.02  ? 3817 SER A C     1 
ATOM   16547 O  O     . SER A 1 3817 ? 171.774 138.759 172.142 1.00 12.54  ? 3817 SER A O     1 
ATOM   16548 C  CB    . SER A 1 3817 ? 172.059 136.232 173.794 1.00 14.52  ? 3817 SER A CB    1 
ATOM   16549 O  OG    . SER A 1 3817 ? 172.461 135.486 172.659 1.00 16.64  ? 3817 SER A OG    1 
ATOM   16550 N  N     . LEU A 1 3818 ? 170.310 137.388 171.110 1.00 13.40  ? 3818 LEU A N     1 
ATOM   16551 C  CA    . LEU A 1 3818 ? 170.440 138.074 169.827 1.00 9.94   ? 3818 LEU A CA    1 
ATOM   16552 C  C     . LEU A 1 3818 ? 170.045 139.544 169.896 1.00 11.67  ? 3818 LEU A C     1 
ATOM   16553 O  O     . LEU A 1 3818 ? 170.465 140.324 169.035 1.00 13.32  ? 3818 LEU A O     1 
ATOM   16554 C  CB    . LEU A 1 3818 ? 169.591 137.375 168.766 1.00 9.35   ? 3818 LEU A CB    1 
ATOM   16555 C  CG    . LEU A 1 3818 ? 170.255 136.284 167.927 1.00 12.77  ? 3818 LEU A CG    1 
ATOM   16556 C  CD1   . LEU A 1 3818 ? 169.200 135.527 167.143 1.00 9.97   ? 3818 LEU A CD1   1 
ATOM   16557 C  CD2   . LEU A 1 3818 ? 171.298 136.875 166.997 1.00 11.71  ? 3818 LEU A CD2   1 
ATOM   16558 N  N     . LYS A 1 3819 ? 169.248 139.943 170.889 1.00 12.63  ? 3819 LYS A N     1 
ATOM   16559 C  CA    . LYS A 1 3819 ? 168.828 141.335 171.004 1.00 8.05   ? 3819 LYS A CA    1 
ATOM   16560 C  C     . LYS A 1 3819 ? 169.971 142.273 171.365 1.00 13.00  ? 3819 LYS A C     1 
ATOM   16561 O  O     . LYS A 1 3819 ? 169.791 143.493 171.295 1.00 13.53  ? 3819 LYS A O     1 
ATOM   16562 C  CB    . LYS A 1 3819 ? 167.707 141.463 172.038 1.00 7.38   ? 3819 LYS A CB    1 
ATOM   16563 C  CG    . LYS A 1 3819 ? 168.165 141.358 173.482 1.00 10.69  ? 3819 LYS A CG    1 
ATOM   16564 C  CD    . LYS A 1 3819 ? 167.029 141.669 174.442 1.00 10.70  ? 3819 LYS A CD    1 
ATOM   16565 C  CE    . LYS A 1 3819 ? 166.303 140.406 174.875 1.00 18.06  ? 3819 LYS A CE    1 
ATOM   16566 N  NZ    . LYS A 1 3819 ? 167.032 139.665 175.940 1.00 24.74  ? 3819 LYS A NZ    1 
ATOM   16567 N  N     . GLN A 1 3820 ? 171.133 141.743 171.751 1.00 17.40  ? 3820 GLN A N     1 
ATOM   16568 C  CA    . GLN A 1 3820 ? 172.272 142.592 172.075 1.00 14.83  ? 3820 GLN A CA    1 
ATOM   16569 C  C     . GLN A 1 3820 ? 172.941 143.177 170.839 1.00 16.85  ? 3820 GLN A C     1 
ATOM   16570 O  O     . GLN A 1 3820 ? 173.616 144.205 170.948 1.00 24.22  ? 3820 GLN A O     1 
ATOM   16571 C  CB    . GLN A 1 3820 ? 173.295 141.808 172.895 1.00 16.75  ? 3820 GLN A CB    1 
ATOM   16572 C  CG    . GLN A 1 3820 ? 172.731 141.208 174.168 1.00 17.03  ? 3820 GLN A CG    1 
ATOM   16573 C  CD    . GLN A 1 3820 ? 172.271 142.264 175.148 1.00 29.47  ? 3820 GLN A CD    1 
ATOM   16574 O  OE1   . GLN A 1 3820 ? 171.128 142.249 175.604 1.00 38.63  ? 3820 GLN A OE1   1 
ATOM   16575 N  NE2   . GLN A 1 3820 ? 173.162 143.191 175.480 1.00 35.44  ? 3820 GLN A NE2   1 
ATOM   16576 N  N     . ILE A 1 3821 ? 172.780 142.551 169.670 1.00 12.02  ? 3821 ILE A N     1 
ATOM   16577 C  CA    . ILE A 1 3821 ? 173.423 143.042 168.454 1.00 11.39  ? 3821 ILE A CA    1 
ATOM   16578 C  C     . ILE A 1 3821 ? 172.510 143.923 167.614 1.00 13.54  ? 3821 ILE A C     1 
ATOM   16579 O  O     . ILE A 1 3821 ? 173.003 144.608 166.703 1.00 19.31  ? 3821 ILE A O     1 
ATOM   16580 C  CB    . ILE A 1 3821 ? 173.960 141.879 167.592 1.00 14.20  ? 3821 ILE A CB    1 
ATOM   16581 C  CG1   . ILE A 1 3821 ? 172.811 141.110 166.941 1.00 15.58  ? 3821 ILE A CG1   1 
ATOM   16582 C  CG2   . ILE A 1 3821 ? 174.822 140.950 168.429 1.00 13.20  ? 3821 ILE A CG2   1 
ATOM   16583 C  CD1   . ILE A 1 3821 ? 173.264 140.058 165.954 1.00 10.90  ? 3821 ILE A CD1   1 
ATOM   16584 N  N     . HIS A 1 3822 ? 171.207 143.936 167.888 1.00 12.26  ? 3822 HIS A N     1 
ATOM   16585 C  CA    . HIS A 1 3822 ? 170.275 144.793 167.170 1.00 7.77   ? 3822 HIS A CA    1 
ATOM   16586 C  C     . HIS A 1 3822 ? 168.975 144.866 167.953 1.00 9.89   ? 3822 HIS A C     1 
ATOM   16587 O  O     . HIS A 1 3822 ? 168.488 143.846 168.447 1.00 13.97  ? 3822 HIS A O     1 
ATOM   16588 C  CB    . HIS A 1 3822 ? 170.010 144.273 165.752 1.00 7.85   ? 3822 HIS A CB    1 
ATOM   16589 C  CG    . HIS A 1 3822 ? 169.540 145.326 164.799 1.00 8.13   ? 3822 HIS A CG    1 
ATOM   16590 N  ND1   . HIS A 1 3822 ? 168.229 145.745 164.741 1.00 7.78   ? 3822 HIS A ND1   1 
ATOM   16591 C  CD2   . HIS A 1 3822 ? 170.207 146.043 163.864 1.00 10.29  ? 3822 HIS A CD2   1 
ATOM   16592 C  CE1   . HIS A 1 3822 ? 168.108 146.677 163.812 1.00 7.96   ? 3822 HIS A CE1   1 
ATOM   16593 N  NE2   . HIS A 1 3822 ? 169.294 146.876 163.265 1.00 9.70   ? 3822 HIS A NE2   1 
ATOM   16594 N  N     . PHE A 1 3823 ? 168.418 146.075 168.056 1.00 11.84  ? 3823 PHE A N     1 
ATOM   16595 C  CA    . PHE A 1 3823 ? 167.195 146.278 168.824 1.00 7.96   ? 3823 PHE A CA    1 
ATOM   16596 C  C     . PHE A 1 3823 ? 165.989 145.595 168.194 1.00 7.86   ? 3823 PHE A C     1 
ATOM   16597 O  O     . PHE A 1 3823 ? 165.002 145.343 168.893 1.00 13.82  ? 3823 PHE A O     1 
ATOM   16598 C  CB    . PHE A 1 3823 ? 166.921 147.773 168.986 1.00 6.54   ? 3823 PHE A CB    1 
ATOM   16599 C  CG    . PHE A 1 3823 ? 166.837 148.519 167.684 1.00 11.25  ? 3823 PHE A CG    1 
ATOM   16600 C  CD1   . PHE A 1 3823 ? 165.637 148.618 167.001 1.00 11.93  ? 3823 PHE A CD1   1 
ATOM   16601 C  CD2   . PHE A 1 3823 ? 167.959 149.123 167.144 1.00 10.64  ? 3823 PHE A CD2   1 
ATOM   16602 C  CE1   . PHE A 1 3823 ? 165.559 149.297 165.806 1.00 9.89   ? 3823 PHE A CE1   1 
ATOM   16603 C  CE2   . PHE A 1 3823 ? 167.885 149.806 165.949 1.00 12.63  ? 3823 PHE A CE2   1 
ATOM   16604 C  CZ    . PHE A 1 3823 ? 166.683 149.893 165.280 1.00 12.56  ? 3823 PHE A CZ    1 
ATOM   16605 N  N     . LEU A 1 3824 ? 166.040 145.295 166.898 1.00 7.42   ? 3824 LEU A N     1 
ATOM   16606 C  CA    . LEU A 1 3824 ? 164.921 144.664 166.212 1.00 7.01   ? 3824 LEU A CA    1 
ATOM   16607 C  C     . LEU A 1 3824 ? 164.844 143.163 166.451 1.00 7.07   ? 3824 LEU A C     1 
ATOM   16608 O  O     . LEU A 1 3824 ? 163.825 142.551 166.116 1.00 10.35  ? 3824 LEU A O     1 
ATOM   16609 C  CB    . LEU A 1 3824 ? 165.011 144.936 164.709 1.00 6.63   ? 3824 LEU A CB    1 
ATOM   16610 C  CG    . LEU A 1 3824 ? 163.723 144.822 163.896 1.00 5.98   ? 3824 LEU A CG    1 
ATOM   16611 C  CD1   . LEU A 1 3824 ? 162.849 146.041 164.117 1.00 12.50  ? 3824 LEU A CD1   1 
ATOM   16612 C  CD2   . LEU A 1 3824 ? 164.045 144.652 162.425 1.00 7.66   ? 3824 LEU A CD2   1 
ATOM   16613 N  N     . TYR A 1 3825 ? 165.880 142.557 167.025 1.00 7.30   ? 3825 TYR A N     1 
ATOM   16614 C  CA    . TYR A 1 3825 ? 165.931 141.104 167.183 1.00 7.81   ? 3825 TYR A CA    1 
ATOM   16615 C  C     . TYR A 1 3825 ? 165.283 140.688 168.505 1.00 6.77   ? 3825 TYR A C     1 
ATOM   16616 O  O     . TYR A 1 3825 ? 165.912 140.131 169.402 1.00 8.49   ? 3825 TYR A O     1 
ATOM   16617 C  CB    . TYR A 1 3825 ? 167.371 140.611 167.088 1.00 8.96   ? 3825 TYR A CB    1 
ATOM   16618 C  CG    . TYR A 1 3825 ? 168.072 140.942 165.785 1.00 6.75   ? 3825 TYR A CG    1 
ATOM   16619 C  CD1   . TYR A 1 3825 ? 167.369 141.434 164.693 1.00 7.12   ? 3825 TYR A CD1   1 
ATOM   16620 C  CD2   . TYR A 1 3825 ? 169.441 140.766 165.653 1.00 8.63   ? 3825 TYR A CD2   1 
ATOM   16621 C  CE1   . TYR A 1 3825 ? 168.008 141.739 163.511 1.00 7.15   ? 3825 TYR A CE1   1 
ATOM   16622 C  CE2   . TYR A 1 3825 ? 170.088 141.068 164.474 1.00 10.51  ? 3825 TYR A CE2   1 
ATOM   16623 C  CZ    . TYR A 1 3825 ? 169.367 141.554 163.407 1.00 7.71   ? 3825 TYR A CZ    1 
ATOM   16624 O  OH    . TYR A 1 3825 ? 170.007 141.855 162.230 1.00 8.72   ? 3825 TYR A OH    1 
ATOM   16625 N  N     . GLN A 1 3826 ? 163.989 140.973 168.608 1.00 6.43   ? 3826 GLN A N     1 
ATOM   16626 C  CA    . GLN A 1 3826 ? 163.204 140.663 169.795 1.00 6.36   ? 3826 GLN A CA    1 
ATOM   16627 C  C     . GLN A 1 3826 ? 162.399 139.397 169.541 1.00 7.48   ? 3826 GLN A C     1 
ATOM   16628 O  O     . GLN A 1 3826 ? 161.568 139.358 168.627 1.00 10.11  ? 3826 GLN A O     1 
ATOM   16629 C  CB    . GLN A 1 3826 ? 162.279 141.824 170.157 1.00 7.50   ? 3826 GLN A CB    1 
ATOM   16630 C  CG    . GLN A 1 3826 ? 162.984 143.159 170.303 1.00 6.80   ? 3826 GLN A CG    1 
ATOM   16631 C  CD    . GLN A 1 3826 ? 163.956 143.179 171.463 1.00 5.91   ? 3826 GLN A CD    1 
ATOM   16632 O  OE1   . GLN A 1 3826 ? 163.728 142.542 172.490 1.00 8.09   ? 3826 GLN A OE1   1 
ATOM   16633 N  NE2   . GLN A 1 3826 ? 165.045 143.920 171.308 1.00 4.36   ? 3826 GLN A NE2   1 
ATOM   16634 N  N     . TYR A 1 3827 ? 162.643 138.369 170.348 1.00 8.42   ? 3827 TYR A N     1 
ATOM   16635 C  CA    . TYR A 1 3827 ? 161.967 137.089 170.207 1.00 9.25   ? 3827 TYR A CA    1 
ATOM   16636 C  C     . TYR A 1 3827 ? 161.434 136.644 171.559 1.00 11.65  ? 3827 TYR A C     1 
ATOM   16637 O  O     . TYR A 1 3827 ? 162.127 136.749 172.575 1.00 17.83  ? 3827 TYR A O     1 
ATOM   16638 C  CB    . TYR A 1 3827 ? 162.908 136.024 169.637 1.00 5.93   ? 3827 TYR A CB    1 
ATOM   16639 C  CG    . TYR A 1 3827 ? 163.605 136.460 168.374 1.00 7.51   ? 3827 TYR A CG    1 
ATOM   16640 C  CD1   . TYR A 1 3827 ? 162.896 136.648 167.197 1.00 7.57   ? 3827 TYR A CD1   1 
ATOM   16641 C  CD2   . TYR A 1 3827 ? 164.971 136.698 168.360 1.00 8.63   ? 3827 TYR A CD2   1 
ATOM   16642 C  CE1   . TYR A 1 3827 ? 163.528 137.053 166.042 1.00 7.63   ? 3827 TYR A CE1   1 
ATOM   16643 C  CE2   . TYR A 1 3827 ? 165.611 137.104 167.210 1.00 8.53   ? 3827 TYR A CE2   1 
ATOM   16644 C  CZ    . TYR A 1 3827 ? 164.886 137.280 166.053 1.00 9.09   ? 3827 TYR A CZ    1 
ATOM   16645 O  OH    . TYR A 1 3827 ? 165.522 137.684 164.903 1.00 11.91  ? 3827 TYR A OH    1 
ATOM   16646 N  N     . SER A 1 3828 ? 160.203 136.150 171.564 1.00 11.07  ? 3828 SER A N     1 
ATOM   16647 C  CA    . SER A 1 3828 ? 159.591 135.632 172.775 1.00 11.60  ? 3828 SER A CA    1 
ATOM   16648 C  C     . SER A 1 3828 ? 159.790 134.123 172.860 1.00 15.91  ? 3828 SER A C     1 
ATOM   16649 O  O     . SER A 1 3828 ? 160.224 133.470 171.909 1.00 20.03  ? 3828 SER A O     1 
ATOM   16650 C  CB    . SER A 1 3828 ? 158.103 135.976 172.814 1.00 12.43  ? 3828 SER A CB    1 
ATOM   16651 O  OG    . SER A 1 3828 ? 157.449 135.535 171.638 1.00 13.14  ? 3828 SER A OG    1 
ATOM   16652 N  N     . LEU A 1 3829 ? 159.472 133.567 174.030 1.00 13.31  ? 3829 LEU A N     1 
ATOM   16653 C  CA    . LEU A 1 3829 ? 159.512 132.118 174.184 1.00 10.28  ? 3829 LEU A CA    1 
ATOM   16654 C  C     . LEU A 1 3829 ? 158.503 131.439 173.269 1.00 11.57  ? 3829 LEU A C     1 
ATOM   16655 O  O     . LEU A 1 3829 ? 158.736 130.315 172.813 1.00 15.05  ? 3829 LEU A O     1 
ATOM   16656 C  CB    . LEU A 1 3829 ? 159.257 131.735 175.641 1.00 13.10  ? 3829 LEU A CB    1 
ATOM   16657 C  CG    . LEU A 1 3829 ? 159.251 130.238 175.955 1.00 10.62  ? 3829 LEU A CG    1 
ATOM   16658 C  CD1   . LEU A 1 3829 ? 160.617 129.637 175.681 1.00 13.30  ? 3829 LEU A CD1   1 
ATOM   16659 C  CD2   . LEU A 1 3829 ? 158.828 129.983 177.390 1.00 11.28  ? 3829 LEU A CD2   1 
ATOM   16660 N  N     . GLN A 1 3830 ? 157.386 132.111 172.982 1.00 10.28  ? 3830 GLN A N     1 
ATOM   16661 C  CA    . GLN A 1 3830 ? 156.367 131.523 172.121 1.00 10.85  ? 3830 GLN A CA    1 
ATOM   16662 C  C     . GLN A 1 3830 ? 156.869 131.326 170.696 1.00 14.10  ? 3830 GLN A C     1 
ATOM   16663 O  O     . GLN A 1 3830 ? 156.478 130.360 170.038 1.00 16.56  ? 3830 GLN A O     1 
ATOM   16664 C  CB    . GLN A 1 3830 ? 155.110 132.390 172.128 1.00 12.01  ? 3830 GLN A CB    1 
ATOM   16665 C  CG    . GLN A 1 3830 ? 153.864 131.668 171.650 1.00 15.11  ? 3830 GLN A CG    1 
ATOM   16666 C  CD    . GLN A 1 3830 ? 153.795 130.238 172.144 1.00 23.35  ? 3830 GLN A CD    1 
ATOM   16667 O  OE1   . GLN A 1 3830 ? 153.732 129.987 173.347 1.00 27.80  ? 3830 GLN A OE1   1 
ATOM   16668 N  NE2   . GLN A 1 3830 ? 153.811 129.290 171.215 1.00 19.26  ? 3830 GLN A NE2   1 
ATOM   16669 N  N     . PHE A 1 3831 ? 157.725 132.222 170.202 1.00 13.25  ? 3831 PHE A N     1 
ATOM   16670 C  CA    . PHE A 1 3831 ? 158.284 132.056 168.862 1.00 10.17  ? 3831 PHE A CA    1 
ATOM   16671 C  C     . PHE A 1 3831 ? 159.121 130.785 168.773 1.00 14.47  ? 3831 PHE A C     1 
ATOM   16672 O  O     . PHE A 1 3831 ? 158.976 129.985 167.837 1.00 19.57  ? 3831 PHE A O     1 
ATOM   16673 C  CB    . PHE A 1 3831 ? 159.118 133.287 168.504 1.00 9.57   ? 3831 PHE A CB    1 
ATOM   16674 C  CG    . PHE A 1 3831 ? 159.687 133.259 167.116 1.00 11.58  ? 3831 PHE A CG    1 
ATOM   16675 C  CD1   . PHE A 1 3831 ? 158.859 133.159 166.013 1.00 12.97  ? 3831 PHE A CD1   1 
ATOM   16676 C  CD2   . PHE A 1 3831 ? 161.054 133.344 166.915 1.00 11.93  ? 3831 PHE A CD2   1 
ATOM   16677 C  CE1   . PHE A 1 3831 ? 159.384 133.138 164.736 1.00 15.64  ? 3831 PHE A CE1   1 
ATOM   16678 C  CE2   . PHE A 1 3831 ? 161.584 133.323 165.642 1.00 9.46   ? 3831 PHE A CE2   1 
ATOM   16679 C  CZ    . PHE A 1 3831 ? 160.748 133.221 164.552 1.00 9.80   ? 3831 PHE A CZ    1 
ATOM   16680 N  N     . PHE A 1 3832 ? 159.997 130.573 169.757 1.00 16.06  ? 3832 PHE A N     1 
ATOM   16681 C  CA    . PHE A 1 3832 ? 160.799 129.356 169.784 1.00 12.10  ? 3832 PHE A CA    1 
ATOM   16682 C  C     . PHE A 1 3832 ? 159.925 128.126 169.978 1.00 12.50  ? 3832 PHE A C     1 
ATOM   16683 O  O     . PHE A 1 3832 ? 160.207 127.064 169.414 1.00 15.71  ? 3832 PHE A O     1 
ATOM   16684 C  CB    . PHE A 1 3832 ? 161.851 129.440 170.887 1.00 10.48  ? 3832 PHE A CB    1 
ATOM   16685 C  CG    . PHE A 1 3832 ? 162.535 128.137 171.161 1.00 14.58  ? 3832 PHE A CG    1 
ATOM   16686 C  CD1   . PHE A 1 3832 ? 163.468 127.633 170.273 1.00 15.95  ? 3832 PHE A CD1   1 
ATOM   16687 C  CD2   . PHE A 1 3832 ? 162.233 127.406 172.296 1.00 14.99  ? 3832 PHE A CD2   1 
ATOM   16688 C  CE1   . PHE A 1 3832 ? 164.095 126.432 170.518 1.00 17.16  ? 3832 PHE A CE1   1 
ATOM   16689 C  CE2   . PHE A 1 3832 ? 162.856 126.204 172.544 1.00 13.80  ? 3832 PHE A CE2   1 
ATOM   16690 C  CZ    . PHE A 1 3832 ? 163.786 125.716 171.653 1.00 14.80  ? 3832 PHE A CZ    1 
ATOM   16691 N  N     . LEU A 1 3833 ? 158.869 128.242 170.784 1.00 12.57  ? 3833 LEU A N     1 
ATOM   16692 C  CA    . LEU A 1 3833 ? 157.965 127.114 170.976 1.00 9.47   ? 3833 LEU A CA    1 
ATOM   16693 C  C     . LEU A 1 3833 ? 157.240 126.762 169.684 1.00 11.80  ? 3833 LEU A C     1 
ATOM   16694 O  O     . LEU A 1 3833 ? 157.016 125.584 169.396 1.00 18.98  ? 3833 LEU A O     1 
ATOM   16695 C  CB    . LEU A 1 3833 ? 156.968 127.424 172.092 1.00 13.39  ? 3833 LEU A CB    1 
ATOM   16696 C  CG    . LEU A 1 3833 ? 157.522 127.399 173.519 1.00 11.38  ? 3833 LEU A CG    1 
ATOM   16697 C  CD1   . LEU A 1 3833 ? 156.404 127.561 174.533 1.00 15.68  ? 3833 LEU A CD1   1 
ATOM   16698 C  CD2   . LEU A 1 3833 ? 158.303 126.124 173.780 1.00 7.70   ? 3833 LEU A CD2   1 
ATOM   16699 N  N     . ASP A 1 3834 ? 156.861 127.770 168.894 1.00 16.89  ? 3834 ASP A N     1 
ATOM   16700 C  CA    . ASP A 1 3834 ? 156.259 127.507 167.590 1.00 14.54  ? 3834 ASP A CA    1 
ATOM   16701 C  C     . ASP A 1 3834 ? 157.255 126.849 166.644 1.00 15.75  ? 3834 ASP A C     1 
ATOM   16702 O  O     . ASP A 1 3834 ? 156.887 125.953 165.876 1.00 18.22  ? 3834 ASP A O     1 
ATOM   16703 C  CB    . ASP A 1 3834 ? 155.718 128.801 166.980 1.00 15.24  ? 3834 ASP A CB    1 
ATOM   16704 C  CG    . ASP A 1 3834 ? 154.698 129.483 167.867 1.00 24.11  ? 3834 ASP A CG    1 
ATOM   16705 O  OD1   . ASP A 1 3834 ? 154.616 130.729 167.831 1.00 23.34  ? 3834 ASP A OD1   1 
ATOM   16706 O  OD2   . ASP A 1 3834 ? 153.977 128.776 168.602 1.00 25.89  ? 3834 ASP A OD2   1 
ATOM   16707 N  N     . ILE A 1 3835 ? 158.517 127.284 166.677 1.00 14.63  ? 3835 ILE A N     1 
ATOM   16708 C  CA    . ILE A 1 3835 ? 159.547 126.620 165.876 1.00 13.72  ? 3835 ILE A CA    1 
ATOM   16709 C  C     . ILE A 1 3835 ? 159.664 125.153 166.278 1.00 13.15  ? 3835 ILE A C     1 
ATOM   16710 O  O     . ILE A 1 3835 ? 159.703 124.250 165.431 1.00 17.13  ? 3835 ILE A O     1 
ATOM   16711 C  CB    . ILE A 1 3835 ? 160.896 127.348 166.023 1.00 14.00  ? 3835 ILE A CB    1 
ATOM   16712 C  CG1   . ILE A 1 3835 ? 160.875 128.685 165.283 1.00 12.02  ? 3835 ILE A CG1   1 
ATOM   16713 C  CG2   . ILE A 1 3835 ? 162.036 126.476 165.521 1.00 14.01  ? 3835 ILE A CG2   1 
ATOM   16714 C  CD1   . ILE A 1 3835 ? 162.126 129.507 165.488 1.00 11.72  ? 3835 ILE A CD1   1 
ATOM   16715 N  N     . TYR A 1 3836 ? 159.703 124.899 167.584 1.00 13.80  ? 3836 TYR A N     1 
ATOM   16716 C  CA    . TYR A 1 3836 ? 159.849 123.542 168.096 1.00 13.79  ? 3836 TYR A CA    1 
ATOM   16717 C  C     . TYR A 1 3836 ? 158.639 122.684 167.742 1.00 15.61  ? 3836 TYR A C     1 
ATOM   16718 O  O     . TYR A 1 3836 ? 158.781 121.495 167.433 1.00 18.82  ? 3836 TYR A O     1 
ATOM   16719 C  CB    . TYR A 1 3836 ? 160.072 123.607 169.607 1.00 12.65  ? 3836 TYR A CB    1 
ATOM   16720 C  CG    . TYR A 1 3836 ? 160.427 122.304 170.274 1.00 16.34  ? 3836 TYR A CG    1 
ATOM   16721 C  CD1   . TYR A 1 3836 ? 161.518 121.561 169.852 1.00 17.83  ? 3836 TYR A CD1   1 
ATOM   16722 C  CD2   . TYR A 1 3836 ? 159.709 121.850 171.369 1.00 16.92  ? 3836 TYR A CD2   1 
ATOM   16723 C  CE1   . TYR A 1 3836 ? 161.852 120.378 170.470 1.00 17.80  ? 3836 TYR A CE1   1 
ATOM   16724 C  CE2   . TYR A 1 3836 ? 160.042 120.674 171.999 1.00 16.45  ? 3836 TYR A CE2   1 
ATOM   16725 C  CZ    . TYR A 1 3836 ? 161.115 119.943 171.546 1.00 17.73  ? 3836 TYR A CZ    1 
ATOM   16726 O  OH    . TYR A 1 3836 ? 161.451 118.770 172.170 1.00 25.49  ? 3836 TYR A OH    1 
ATOM   16727 N  N     . HIS A 1 3837 ? 157.442 123.273 167.781 1.00 14.89  ? 3837 HIS A N     1 
ATOM   16728 C  CA    . HIS A 1 3837 ? 156.236 122.565 167.366 1.00 19.01  ? 3837 HIS A CA    1 
ATOM   16729 C  C     . HIS A 1 3837 ? 156.274 122.226 165.881 1.00 22.52  ? 3837 HIS A C     1 
ATOM   16730 O  O     . HIS A 1 3837 ? 155.950 121.101 165.485 1.00 27.41  ? 3837 HIS A O     1 
ATOM   16731 C  CB    . HIS A 1 3837 ? 155.006 123.413 167.691 1.00 22.22  ? 3837 HIS A CB    1 
ATOM   16732 C  CG    . HIS A 1 3837 ? 153.715 122.658 167.642 1.00 35.94  ? 3837 HIS A CG    1 
ATOM   16733 N  ND1   . HIS A 1 3837 ? 152.875 122.693 166.550 1.00 37.81  ? 3837 HIS A ND1   1 
ATOM   16734 C  CD2   . HIS A 1 3837 ? 153.112 121.861 168.555 1.00 38.15  ? 3837 HIS A CD2   1 
ATOM   16735 C  CE1   . HIS A 1 3837 ? 151.815 121.943 166.788 1.00 42.32  ? 3837 HIS A CE1   1 
ATOM   16736 N  NE2   . HIS A 1 3837 ? 151.933 121.428 167.999 1.00 46.48  ? 3837 HIS A NE2   1 
ATOM   16737 N  N     . ASN A 1 3838 ? 156.664 123.190 165.044 1.00 25.20  ? 3838 ASN A N     1 
ATOM   16738 C  CA    . ASN A 1 3838 ? 156.771 122.948 163.610 1.00 20.48  ? 3838 ASN A CA    1 
ATOM   16739 C  C     . ASN A 1 3838 ? 157.860 121.940 163.278 1.00 23.87  ? 3838 ASN A C     1 
ATOM   16740 O  O     . ASN A 1 3838 ? 157.842 121.360 162.187 1.00 35.02  ? 3838 ASN A O     1 
ATOM   16741 C  CB    . ASN A 1 3838 ? 157.045 124.260 162.874 1.00 22.98  ? 3838 ASN A CB    1 
ATOM   16742 C  CG    . ASN A 1 3838 ? 157.001 124.104 161.368 1.00 27.19  ? 3838 ASN A CG    1 
ATOM   16743 O  OD1   . ASN A 1 3838 ? 155.933 123.946 160.780 1.00 31.87  ? 3838 ASN A OD1   1 
ATOM   16744 N  ND2   . ASN A 1 3838 ? 158.168 124.136 160.736 1.00 24.50  ? 3838 ASN A ND2   1 
ATOM   16745 N  N     . VAL A 1 3839 ? 158.821 121.742 164.176 1.00 21.06  ? 3839 VAL A N     1 
ATOM   16746 C  CA    . VAL A 1 3839 ? 159.853 120.740 163.934 1.00 17.34  ? 3839 VAL A CA    1 
ATOM   16747 C  C     . VAL A 1 3839 ? 159.381 119.359 164.381 1.00 19.35  ? 3839 VAL A C     1 
ATOM   16748 O  O     . VAL A 1 3839 ? 159.563 118.366 163.669 1.00 22.89  ? 3839 VAL A O     1 
ATOM   16749 C  CB    . VAL A 1 3839 ? 161.162 121.155 164.628 1.00 15.84  ? 3839 VAL A CB    1 
ATOM   16750 C  CG1   . VAL A 1 3839 ? 162.114 119.980 164.727 1.00 18.81  ? 3839 VAL A CG1   1 
ATOM   16751 C  CG2   . VAL A 1 3839 ? 161.805 122.301 163.872 1.00 12.81  ? 3839 VAL A CG2   1 
ATOM   16752 N  N     . LEU A 1 3840 ? 158.766 119.274 165.564 1.00 26.26  ? 3840 LEU A N     1 
ATOM   16753 C  CA    . LEU A 1 3840 ? 158.248 117.995 166.043 1.00 21.27  ? 3840 LEU A CA    1 
ATOM   16754 C  C     . LEU A 1 3840 ? 157.059 117.531 165.211 1.00 22.58  ? 3840 LEU A C     1 
ATOM   16755 O  O     . LEU A 1 3840 ? 157.006 116.377 164.771 1.00 23.45  ? 3840 LEU A O     1 
ATOM   16756 C  CB    . LEU A 1 3840 ? 157.855 118.102 167.516 1.00 19.93  ? 3840 LEU A CB    1 
ATOM   16757 C  CG    . LEU A 1 3840 ? 158.976 118.236 168.545 1.00 20.78  ? 3840 LEU A CG    1 
ATOM   16758 C  CD1   . LEU A 1 3840 ? 158.388 118.367 169.934 1.00 21.47  ? 3840 LEU A CD1   1 
ATOM   16759 C  CD2   . LEU A 1 3840 ? 159.908 117.042 168.475 1.00 21.38  ? 3840 LEU A CD2   1 
ATOM   16760 N  N     . TYR A 1 3841 ? 156.093 118.415 164.991 1.00 28.80  ? 3841 TYR A N     1 
ATOM   16761 C  CA    . TYR A 1 3841 ? 154.906 118.123 164.204 1.00 26.37  ? 3841 TYR A CA    1 
ATOM   16762 C  C     . TYR A 1 3841 ? 155.000 118.824 162.857 1.00 32.02  ? 3841 TYR A C     1 
ATOM   16763 O  O     . TYR A 1 3841 ? 155.916 119.612 162.614 1.00 38.70  ? 3841 TYR A O     1 
ATOM   16764 C  CB    . TYR A 1 3841 ? 153.639 118.564 164.943 1.00 23.55  ? 3841 TYR A CB    1 
ATOM   16765 C  CG    . TYR A 1 3841 ? 153.439 117.870 166.268 1.00 30.35  ? 3841 TYR A CG    1 
ATOM   16766 C  CD1   . TYR A 1 3841 ? 153.618 116.501 166.392 1.00 37.19  ? 3841 TYR A CD1   1 
ATOM   16767 C  CD2   . TYR A 1 3841 ? 153.092 118.589 167.401 1.00 31.28  ? 3841 TYR A CD2   1 
ATOM   16768 C  CE1   . TYR A 1 3841 ? 153.439 115.865 167.604 1.00 35.35  ? 3841 TYR A CE1   1 
ATOM   16769 C  CE2   . TYR A 1 3841 ? 152.914 117.964 168.617 1.00 37.46  ? 3841 TYR A CE2   1 
ATOM   16770 C  CZ    . TYR A 1 3841 ? 153.088 116.604 168.714 1.00 40.31  ? 3841 TYR A CZ    1 
ATOM   16771 O  OH    . TYR A 1 3841 ? 152.909 115.982 169.927 1.00 47.18  ? 3841 TYR A OH    1 
ATOM   16772 N  N     . GLU A 1 3842 ? 154.032 118.523 161.985 1.00 27.03  ? 3842 GLU A N     1 
ATOM   16773 C  CA    . GLU A 1 3842 ? 153.958 119.065 160.620 1.00 32.07  ? 3842 GLU A CA    1 
ATOM   16774 C  C     . GLU A 1 3842 ? 155.333 119.139 159.956 1.00 34.53  ? 3842 GLU A C     1 
ATOM   16775 O  O     . GLU A 1 3842 ? 155.674 120.118 159.289 1.00 31.35  ? 3842 GLU A O     1 
ATOM   16776 C  CB    . GLU A 1 3842 ? 153.254 120.430 160.587 1.00 33.02  ? 3842 GLU A CB    1 
ATOM   16777 C  CG    . GLU A 1 3842 ? 153.869 121.536 161.432 1.00 32.69  ? 3842 GLU A CG    1 
ATOM   16778 C  CD    . GLU A 1 3842 ? 152.845 122.550 161.901 1.00 35.62  ? 3842 GLU A CD    1 
ATOM   16779 O  OE1   . GLU A 1 3842 ? 151.830 122.738 161.200 1.00 32.69  ? 3842 GLU A OE1   1 
ATOM   16780 O  OE2   . GLU A 1 3842 ? 153.054 123.159 162.971 1.00 34.48  ? 3842 GLU A OE2   1 
ATOM   16781 N  N     . ASN A 1 3843 ? 156.131 118.086 160.137 1.00 31.68  ? 3843 ASN A N     1 
ATOM   16782 C  CA    . ASN A 1 3843 ? 157.452 118.001 159.537 1.00 27.61  ? 3843 ASN A CA    1 
ATOM   16783 C  C     . ASN A 1 3843 ? 157.380 117.127 158.297 1.00 35.69  ? 3843 ASN A C     1 
ATOM   16784 O  O     . ASN A 1 3843 ? 157.061 115.934 158.413 1.00 43.83  ? 3843 ASN A O     1 
ATOM   16785 C  CB    . ASN A 1 3843 ? 158.461 117.432 160.532 1.00 29.37  ? 3843 ASN A CB    1 
ATOM   16786 C  CG    . ASN A 1 3843 ? 159.869 117.939 160.290 1.00 31.66  ? 3843 ASN A CG    1 
ATOM   16787 O  OD1   . ASN A 1 3843 ? 160.102 118.758 159.402 1.00 39.49  ? 3843 ASN A OD1   1 
ATOM   16788 N  ND2   . ASN A 1 3843 ? 160.816 117.455 161.082 1.00 26.32  ? 3843 ASN A ND2   1 
ATOM   16789 N  N     . PRO A 1 3844 ? 157.653 117.658 157.104 1.00 37.40  ? 3844 PRO A N     1 
ATOM   16790 C  CA    . PRO A 1 3844 ? 157.603 116.817 155.897 1.00 37.38  ? 3844 PRO A CA    1 
ATOM   16791 C  C     . PRO A 1 3844 ? 158.613 115.683 155.901 1.00 36.41  ? 3844 PRO A C     1 
ATOM   16792 O  O     . PRO A 1 3844 ? 158.406 114.689 155.195 1.00 43.04  ? 3844 PRO A O     1 
ATOM   16793 C  CB    . PRO A 1 3844 ? 157.886 117.812 154.762 1.00 36.62  ? 3844 PRO A CB    1 
ATOM   16794 C  CG    . PRO A 1 3844 ? 157.577 119.158 155.341 1.00 39.06  ? 3844 PRO A CG    1 
ATOM   16795 C  CD    . PRO A 1 3844 ? 157.944 119.065 156.786 1.00 34.12  ? 3844 PRO A CD    1 
ATOM   16796 N  N     . ASN A 1 3845 ? 159.693 115.794 156.670 1.00 33.72  ? 3845 ASN A N     1 
ATOM   16797 C  CA    . ASN A 1 3845 ? 160.729 114.771 156.695 1.00 34.61  ? 3845 ASN A CA    1 
ATOM   16798 C  C     . ASN A 1 3845 ? 160.367 113.570 157.558 1.00 32.12  ? 3845 ASN A C     1 
ATOM   16799 O  O     . ASN A 1 3845 ? 161.130 112.599 157.585 1.00 36.34  ? 3845 ASN A O     1 
ATOM   16800 C  CB    . ASN A 1 3845 ? 162.049 115.372 157.186 1.00 36.09  ? 3845 ASN A CB    1 
ATOM   16801 C  CG    . ASN A 1 3845 ? 162.442 116.619 156.422 1.00 33.57  ? 3845 ASN A CG    1 
ATOM   16802 O  OD1   . ASN A 1 3845 ? 161.712 117.609 156.409 1.00 35.75  ? 3845 ASN A OD1   1 
ATOM   16803 N  ND2   . ASN A 1 3845 ? 163.602 116.577 155.780 1.00 38.73  ? 3845 ASN A ND2   1 
ATOM   16804 N  N     . LEU A 1 3846 ? 159.237 113.609 158.265 1.00 30.81  ? 3846 LEU A N     1 
ATOM   16805 C  CA    . LEU A 1 3846 ? 158.831 112.531 159.157 1.00 36.02  ? 3846 LEU A CA    1 
ATOM   16806 C  C     . LEU A 1 3846 ? 157.562 111.828 158.686 1.00 40.64  ? 3846 LEU A C     1 
ATOM   16807 O  O     . LEU A 1 3846 ? 156.916 111.134 159.476 1.00 45.43  ? 3846 LEU A O     1 
ATOM   16808 C  CB    . LEU A 1 3846 ? 158.635 113.067 160.576 1.00 34.99  ? 3846 LEU A CB    1 
ATOM   16809 C  CG    . LEU A 1 3846 ? 159.888 113.481 161.345 1.00 28.56  ? 3846 LEU A CG    1 
ATOM   16810 C  CD1   . LEU A 1 3846 ? 159.514 113.992 162.723 1.00 23.49  ? 3846 LEU A CD1   1 
ATOM   16811 C  CD2   . LEU A 1 3846 ? 160.854 112.319 161.447 1.00 28.10  ? 3846 LEU A CD2   1 
ATOM   16812 N  N     . LYS A 1 3847 ? 157.189 111.998 157.415 1.00 45.49  ? 3847 LYS A N     1 
ATOM   16813 C  CA    . LYS A 1 3847 ? 155.913 111.473 156.938 1.00 52.07  ? 3847 LYS A CA    1 
ATOM   16814 C  C     . LYS A 1 3847 ? 155.877 109.951 156.992 1.00 58.41  ? 3847 LYS A C     1 
ATOM   16815 O  O     . LYS A 1 3847 ? 154.948 109.362 157.558 1.00 58.10  ? 3847 LYS A O     1 
ATOM   16816 C  CB    . LYS A 1 3847 ? 155.644 111.967 155.517 1.00 48.07  ? 3847 LYS A CB    1 
ATOM   16817 C  CG    . LYS A 1 3847 ? 154.749 113.192 155.450 1.00 56.67  ? 3847 LYS A CG    1 
ATOM   16818 C  CD    . LYS A 1 3847 ? 153.511 113.017 156.314 1.00 58.50  ? 3847 LYS A CD    1 
ATOM   16819 C  CE    . LYS A 1 3847 ? 152.320 113.758 155.731 1.00 53.70  ? 3847 LYS A CE    1 
ATOM   16820 N  NZ    . LYS A 1 3847 ? 151.064 113.459 156.473 1.00 53.62  ? 3847 LYS A NZ    1 
ATOM   16821 N  N     . GLY A 1 3848 ? 156.876 109.295 156.412 1.00 50.27  ? 3848 GLY A N     1 
ATOM   16822 C  CA    . GLY A 1 3848 ? 156.927 107.852 156.371 1.00 48.61  ? 3848 GLY A CA    1 
ATOM   16823 C  C     . GLY A 1 3848 ? 157.983 107.214 157.240 1.00 44.53  ? 3848 GLY A C     1 
ATOM   16824 O  O     . GLY A 1 3848 ? 158.110 105.986 157.236 1.00 47.05  ? 3848 GLY A O     1 
ATOM   16825 N  N     . VAL A 1 3849 ? 158.741 108.004 157.987 1.00 48.30  ? 3849 VAL A N     1 
ATOM   16826 C  CA    . VAL A 1 3849 ? 159.850 107.486 158.777 1.00 44.49  ? 3849 VAL A CA    1 
ATOM   16827 C  C     . VAL A 1 3849 ? 159.317 106.931 160.090 1.00 39.20  ? 3849 VAL A C     1 
ATOM   16828 O  O     . VAL A 1 3849 ? 158.504 107.568 160.769 1.00 36.85  ? 3849 VAL A O     1 
ATOM   16829 C  CB    . VAL A 1 3849 ? 160.894 108.591 159.010 1.00 38.62  ? 3849 VAL A CB    1 
ATOM   16830 C  CG1   . VAL A 1 3849 ? 162.005 108.084 159.889 1.00 30.25  ? 3849 VAL A CG1   1 
ATOM   16831 C  CG2   . VAL A 1 3849 ? 161.440 109.090 157.683 1.00 44.63  ? 3849 VAL A CG2   1 
ATOM   16832 N  N     . THR A 1 3850 ? 159.774 105.735 160.453 1.00 35.50  ? 3850 THR A N     1 
ATOM   16833 C  CA    . THR A 1 3850 ? 159.272 105.027 161.626 1.00 38.54  ? 3850 THR A CA    1 
ATOM   16834 C  C     . THR A 1 3850 ? 160.313 104.846 162.720 1.00 40.90  ? 3850 THR A C     1 
ATOM   16835 O  O     . THR A 1 3850 ? 159.985 104.990 163.902 1.00 37.17  ? 3850 THR A O     1 
ATOM   16836 C  CB    . THR A 1 3850 ? 158.717 103.653 161.207 1.00 41.92  ? 3850 THR A CB    1 
ATOM   16837 O  OG1   . THR A 1 3850 ? 157.444 103.826 160.572 1.00 34.96  ? 3850 THR A OG1   1 
ATOM   16838 C  CG2   . THR A 1 3850 ? 158.550 102.734 162.409 1.00 38.18  ? 3850 THR A CG2   1 
ATOM   16839 N  N     . ASP A 1 3851 ? 161.563 104.552 162.362 1.00 42.12  ? 3851 ASP A N     1 
ATOM   16840 C  CA    . ASP A 1 3851 ? 162.593 104.294 163.363 1.00 46.28  ? 3851 ASP A CA    1 
ATOM   16841 C  C     . ASP A 1 3851 ? 162.768 105.491 164.288 1.00 46.50  ? 3851 ASP A C     1 
ATOM   16842 O  O     . ASP A 1 3851 ? 162.871 106.634 163.834 1.00 45.70  ? 3851 ASP A O     1 
ATOM   16843 C  CB    . ASP A 1 3851 ? 163.918 103.956 162.684 1.00 40.20  ? 3851 ASP A CB    1 
ATOM   16844 C  CG    . ASP A 1 3851 ? 164.923 103.351 163.641 1.00 47.00  ? 3851 ASP A CG    1 
ATOM   16845 O  OD1   . ASP A 1 3851 ? 164.530 103.002 164.774 1.00 44.20  ? 3851 ASP A OD1   1 
ATOM   16846 O  OD2   . ASP A 1 3851 ? 166.106 103.225 163.264 1.00 59.14  ? 3851 ASP A OD2   1 
ATOM   16847 N  N     . HIS A 1 3852 ? 162.808 105.219 165.594 1.00 40.46  ? 3852 HIS A N     1 
ATOM   16848 C  CA    . HIS A 1 3852 ? 162.839 106.296 166.579 1.00 37.34  ? 3852 HIS A CA    1 
ATOM   16849 C  C     . HIS A 1 3852 ? 164.140 107.087 166.514 1.00 40.58  ? 3852 HIS A C     1 
ATOM   16850 O  O     . HIS A 1 3852 ? 164.124 108.319 166.602 1.00 45.79  ? 3852 HIS A O     1 
ATOM   16851 C  CB    . HIS A 1 3852 ? 162.627 105.728 167.981 1.00 38.72  ? 3852 HIS A CB    1 
ATOM   16852 C  CG    . HIS A 1 3852 ? 161.209 105.344 168.270 1.00 43.29  ? 3852 HIS A CG    1 
ATOM   16853 N  ND1   . HIS A 1 3852 ? 160.849 104.079 168.680 1.00 41.54  ? 3852 HIS A ND1   1 
ATOM   16854 C  CD2   . HIS A 1 3852 ? 160.062 106.060 168.205 1.00 43.02  ? 3852 HIS A CD2   1 
ATOM   16855 C  CE1   . HIS A 1 3852 ? 159.541 104.032 168.858 1.00 40.54  ? 3852 HIS A CE1   1 
ATOM   16856 N  NE2   . HIS A 1 3852 ? 159.039 105.221 168.576 1.00 40.29  ? 3852 HIS A NE2   1 
ATOM   16857 N  N     . THR A 1 3853 ? 165.277 106.401 166.373 1.00 36.76  ? 3853 THR A N     1 
ATOM   16858 C  CA    . THR A 1 3853 ? 166.563 107.091 166.410 1.00 35.18  ? 3853 THR A CA    1 
ATOM   16859 C  C     . THR A 1 3853 ? 166.762 107.975 165.184 1.00 38.17  ? 3853 THR A C     1 
ATOM   16860 O  O     . THR A 1 3853 ? 167.228 109.116 165.298 1.00 33.60  ? 3853 THR A O     1 
ATOM   16861 C  CB    . THR A 1 3853 ? 167.698 106.076 166.529 1.00 37.31  ? 3853 THR A CB    1 
ATOM   16862 O  OG1   . THR A 1 3853 ? 167.341 105.072 167.487 1.00 36.84  ? 3853 THR A OG1   1 
ATOM   16863 C  CG2   . THR A 1 3853 ? 168.979 106.763 166.979 1.00 38.51  ? 3853 THR A CG2   1 
ATOM   16864 N  N     . GLN A 1 3854 ? 166.416 107.468 163.999 1.00 37.92  ? 3854 GLN A N     1 
ATOM   16865 C  CA    . GLN A 1 3854 ? 166.550 108.285 162.800 1.00 37.33  ? 3854 GLN A CA    1 
ATOM   16866 C  C     . GLN A 1 3854 ? 165.514 109.404 162.770 1.00 29.76  ? 3854 GLN A C     1 
ATOM   16867 O  O     . GLN A 1 3854 ? 165.797 110.492 162.254 1.00 28.46  ? 3854 GLN A O     1 
ATOM   16868 C  CB    . GLN A 1 3854 ? 166.473 107.398 161.555 1.00 37.58  ? 3854 GLN A CB    1 
ATOM   16869 C  CG    . GLN A 1 3854 ? 165.080 107.006 161.125 1.00 42.51  ? 3854 GLN A CG    1 
ATOM   16870 C  CD    . GLN A 1 3854 ? 165.044 106.449 159.717 1.00 46.27  ? 3854 GLN A CD    1 
ATOM   16871 O  OE1   . GLN A 1 3854 ? 164.980 107.197 158.742 1.00 43.69  ? 3854 GLN A OE1   1 
ATOM   16872 N  NE2   . GLN A 1 3854 ? 165.080 105.127 159.603 1.00 41.93  ? 3854 GLN A NE2   1 
ATOM   16873 N  N     . ARG A 1 3855 ? 164.332 109.177 163.352 1.00 31.55  ? 3855 ARG A N     1 
ATOM   16874 C  CA    . ARG A 1 3855 ? 163.389 110.274 163.544 1.00 29.79  ? 3855 ARG A CA    1 
ATOM   16875 C  C     . ARG A 1 3855 ? 163.977 111.347 164.449 1.00 26.38  ? 3855 ARG A C     1 
ATOM   16876 O  O     . ARG A 1 3855 ? 163.821 112.542 164.186 1.00 24.90  ? 3855 ARG A O     1 
ATOM   16877 C  CB    . ARG A 1 3855 ? 162.071 109.761 164.125 1.00 28.44  ? 3855 ARG A CB    1 
ATOM   16878 C  CG    . ARG A 1 3855 ? 161.138 109.133 163.112 1.00 27.69  ? 3855 ARG A CG    1 
ATOM   16879 C  CD    . ARG A 1 3855 ? 159.797 108.779 163.728 1.00 25.50  ? 3855 ARG A CD    1 
ATOM   16880 N  NE    . ARG A 1 3855 ? 159.067 109.965 164.160 1.00 26.29  ? 3855 ARG A NE    1 
ATOM   16881 C  CZ    . ARG A 1 3855 ? 157.980 110.433 163.562 1.00 27.78  ? 3855 ARG A CZ    1 
ATOM   16882 N  NH1   . ARG A 1 3855 ? 157.475 109.847 162.489 1.00 31.59  ? 3855 ARG A NH1   1 
ATOM   16883 N  NH2   . ARG A 1 3855 ? 157.386 111.517 164.052 1.00 24.44  ? 3855 ARG A NH2   1 
ATOM   16884 N  N     . LEU A 1 3856 ? 164.648 110.936 165.527 1.00 23.41  ? 3856 LEU A N     1 
ATOM   16885 C  CA    . LEU A 1 3856 ? 165.267 111.900 166.430 1.00 22.70  ? 3856 LEU A CA    1 
ATOM   16886 C  C     . LEU A 1 3856 ? 166.358 112.692 165.724 1.00 19.51  ? 3856 LEU A C     1 
ATOM   16887 O  O     . LEU A 1 3856 ? 166.488 113.903 165.931 1.00 20.14  ? 3856 LEU A O     1 
ATOM   16888 C  CB    . LEU A 1 3856 ? 165.828 111.183 167.658 1.00 21.86  ? 3856 LEU A CB    1 
ATOM   16889 C  CG    . LEU A 1 3856 ? 166.385 112.062 168.781 1.00 22.95  ? 3856 LEU A CG    1 
ATOM   16890 C  CD1   . LEU A 1 3856 ? 165.438 113.207 169.091 1.00 22.21  ? 3856 LEU A CD1   1 
ATOM   16891 C  CD2   . LEU A 1 3856 ? 166.647 111.234 170.026 1.00 25.97  ? 3856 LEU A CD2   1 
ATOM   16892 N  N     . SER A 1 3857 ? 167.157 112.023 164.891 1.00 24.97  ? 3857 SER A N     1 
ATOM   16893 C  CA    . SER A 1 3857 ? 168.175 112.732 164.118 1.00 20.98  ? 3857 SER A CA    1 
ATOM   16894 C  C     . SER A 1 3857 ? 167.542 113.731 163.156 1.00 18.78  ? 3857 SER A C     1 
ATOM   16895 O  O     . SER A 1 3857 ? 168.029 114.862 163.006 1.00 20.72  ? 3857 SER A O     1 
ATOM   16896 C  CB    . SER A 1 3857 ? 169.046 111.734 163.358 1.00 22.08  ? 3857 SER A CB    1 
ATOM   16897 O  OG    . SER A 1 3857 ? 168.315 111.114 162.315 1.00 31.03  ? 3857 SER A OG    1 
ATOM   16898 N  N     . ILE A 1 3858 ? 166.453 113.330 162.495 1.00 19.32  ? 3858 ILE A N     1 
ATOM   16899 C  CA    . ILE A 1 3858 ? 165.749 114.230 161.585 1.00 20.49  ? 3858 ILE A CA    1 
ATOM   16900 C  C     . ILE A 1 3858 ? 165.235 115.450 162.339 1.00 21.47  ? 3858 ILE A C     1 
ATOM   16901 O  O     . ILE A 1 3858 ? 165.364 116.589 161.875 1.00 26.43  ? 3858 ILE A O     1 
ATOM   16902 C  CB    . ILE A 1 3858 ? 164.606 113.482 160.875 1.00 23.39  ? 3858 ILE A CB    1 
ATOM   16903 C  CG1   . ILE A 1 3858 ? 165.155 112.599 159.755 1.00 25.72  ? 3858 ILE A CG1   1 
ATOM   16904 C  CG2   . ILE A 1 3858 ? 163.585 114.460 160.328 1.00 22.13  ? 3858 ILE A CG2   1 
ATOM   16905 C  CD1   . ILE A 1 3858 ? 164.100 111.748 159.082 1.00 24.46  ? 3858 ILE A CD1   1 
ATOM   16906 N  N     . ILE A 1 3859 ? 164.641 115.226 163.513 1.00 19.55  ? 3859 ILE A N     1 
ATOM   16907 C  CA    . ILE A 1 3859 ? 164.138 116.331 164.327 1.00 16.37  ? 3859 ILE A CA    1 
ATOM   16908 C  C     . ILE A 1 3859 ? 165.276 117.245 164.759 1.00 16.02  ? 3859 ILE A C     1 
ATOM   16909 O  O     . ILE A 1 3859 ? 165.140 118.472 164.744 1.00 16.36  ? 3859 ILE A O     1 
ATOM   16910 C  CB    . ILE A 1 3859 ? 163.351 115.795 165.539 1.00 17.94  ? 3859 ILE A CB    1 
ATOM   16911 C  CG1   . ILE A 1 3859 ? 162.171 114.937 165.083 1.00 21.42  ? 3859 ILE A CG1   1 
ATOM   16912 C  CG2   . ILE A 1 3859 ? 162.883 116.933 166.425 1.00 22.08  ? 3859 ILE A CG2   1 
ATOM   16913 C  CD1   . ILE A 1 3859 ? 161.377 114.342 166.221 1.00 23.39  ? 3859 ILE A CD1   1 
ATOM   16914 N  N     . THR A 1 3860 ? 166.410 116.667 165.158 1.00 17.88  ? 3860 THR A N     1 
ATOM   16915 C  CA    . THR A 1 3860 ? 167.538 117.480 165.599 1.00 15.41  ? 3860 THR A CA    1 
ATOM   16916 C  C     . THR A 1 3860 ? 168.060 118.363 164.473 1.00 18.55  ? 3860 THR A C     1 
ATOM   16917 O  O     . THR A 1 3860 ? 168.376 119.538 164.692 1.00 19.53  ? 3860 THR A O     1 
ATOM   16918 C  CB    . THR A 1 3860 ? 168.652 116.585 166.141 1.00 16.74  ? 3860 THR A CB    1 
ATOM   16919 O  OG1   . THR A 1 3860 ? 168.094 115.614 167.035 1.00 18.91  ? 3860 THR A OG1   1 
ATOM   16920 C  CG2   . THR A 1 3860 ? 169.683 117.414 166.887 1.00 16.96  ? 3860 THR A CG2   1 
ATOM   16921 N  N     . LYS A 1 3861 ? 168.160 117.817 163.259 1.00 17.91  ? 3861 LYS A N     1 
ATOM   16922 C  CA    . LYS A 1 3861 ? 168.623 118.620 162.129 1.00 15.12  ? 3861 LYS A CA    1 
ATOM   16923 C  C     . LYS A 1 3861 ? 167.603 119.695 161.759 1.00 14.87  ? 3861 LYS A C     1 
ATOM   16924 O  O     . LYS A 1 3861 ? 167.956 120.868 161.554 1.00 12.59  ? 3861 LYS A O     1 
ATOM   16925 C  CB    . LYS A 1 3861 ? 168.914 117.713 160.934 1.00 15.70  ? 3861 LYS A CB    1 
ATOM   16926 C  CG    . LYS A 1 3861 ? 169.505 118.428 159.733 1.00 20.25  ? 3861 LYS A CG    1 
ATOM   16927 C  CD    . LYS A 1 3861 ? 169.841 117.446 158.624 1.00 22.21  ? 3861 LYS A CD    1 
ATOM   16928 C  CE    . LYS A 1 3861 ? 170.424 118.155 157.416 1.00 27.19  ? 3861 LYS A CE    1 
ATOM   16929 N  NZ    . LYS A 1 3861 ? 170.751 117.200 156.322 1.00 30.72  ? 3861 LYS A NZ    1 
ATOM   16930 N  N     . ASP A 1 3862 ? 166.327 119.311 161.675 1.00 19.17  ? 3862 ASP A N     1 
ATOM   16931 C  CA    . ASP A 1 3862 ? 165.283 120.252 161.301 1.00 15.60  ? 3862 ASP A CA    1 
ATOM   16932 C  C     . ASP A 1 3862 ? 165.090 121.344 162.339 1.00 14.63  ? 3862 ASP A C     1 
ATOM   16933 O  O     . ASP A 1 3862 ? 164.657 122.439 161.982 1.00 15.02  ? 3862 ASP A O     1 
ATOM   16934 C  CB    . ASP A 1 3862 ? 163.966 119.514 161.068 1.00 16.92  ? 3862 ASP A CB    1 
ATOM   16935 C  CG    . ASP A 1 3862 ? 164.000 118.639 159.832 1.00 37.51  ? 3862 ASP A CG    1 
ATOM   16936 O  OD1   . ASP A 1 3862 ? 164.740 118.974 158.883 1.00 39.80  ? 3862 ASP A OD1   1 
ATOM   16937 O  OD2   . ASP A 1 3862 ? 163.285 117.617 159.805 1.00 45.21  ? 3862 ASP A OD2   1 
ATOM   16938 N  N     . LEU A 1 3863 ? 165.407 121.079 163.606 1.00 13.68  ? 3863 LEU A N     1 
ATOM   16939 C  CA    . LEU A 1 3863 ? 165.319 122.123 164.619 1.00 9.90   ? 3863 LEU A CA    1 
ATOM   16940 C  C     . LEU A 1 3863 ? 166.257 123.273 164.287 1.00 9.43   ? 3863 LEU A C     1 
ATOM   16941 O  O     . LEU A 1 3863 ? 165.835 124.433 164.215 1.00 11.72  ? 3863 LEU A O     1 
ATOM   16942 C  CB    . LEU A 1 3863 ? 165.636 121.543 165.996 1.00 10.94  ? 3863 LEU A CB    1 
ATOM   16943 C  CG    . LEU A 1 3863 ? 165.837 122.550 167.127 1.00 11.20  ? 3863 LEU A CG    1 
ATOM   16944 C  CD1   . LEU A 1 3863 ? 164.504 123.103 167.604 1.00 9.82   ? 3863 LEU A CD1   1 
ATOM   16945 C  CD2   . LEU A 1 3863 ? 166.608 121.919 168.272 1.00 9.65   ? 3863 LEU A CD2   1 
ATOM   16946 N  N     . PHE A 1 3864 ? 167.533 122.961 164.047 1.00 10.41  ? 3864 PHE A N     1 
ATOM   16947 C  CA    . PHE A 1 3864 ? 168.486 123.993 163.659 1.00 9.19   ? 3864 PHE A CA    1 
ATOM   16948 C  C     . PHE A 1 3864 ? 168.069 124.664 162.359 1.00 7.44   ? 3864 PHE A C     1 
ATOM   16949 O  O     . PHE A 1 3864 ? 168.111 125.896 162.247 1.00 7.63   ? 3864 PHE A O     1 
ATOM   16950 C  CB    . PHE A 1 3864 ? 169.886 123.395 163.517 1.00 7.98   ? 3864 PHE A CB    1 
ATOM   16951 C  CG    . PHE A 1 3864 ? 170.547 123.070 164.825 1.00 11.56  ? 3864 PHE A CG    1 
ATOM   16952 C  CD1   . PHE A 1 3864 ? 171.298 124.022 165.491 1.00 8.34   ? 3864 PHE A CD1   1 
ATOM   16953 C  CD2   . PHE A 1 3864 ? 170.432 121.808 165.380 1.00 13.72  ? 3864 PHE A CD2   1 
ATOM   16954 C  CE1   . PHE A 1 3864 ? 171.913 123.724 166.689 1.00 8.81   ? 3864 PHE A CE1   1 
ATOM   16955 C  CE2   . PHE A 1 3864 ? 171.045 121.505 166.579 1.00 10.74  ? 3864 PHE A CE2   1 
ATOM   16956 C  CZ    . PHE A 1 3864 ? 171.785 122.463 167.234 1.00 8.59   ? 3864 PHE A CZ    1 
ATOM   16957 N  N     . GLN A 1 3865 ? 167.646 123.871 161.368 1.00 8.22   ? 3865 GLN A N     1 
ATOM   16958 C  CA    . GLN A 1 3865 ? 167.300 124.450 160.072 1.00 7.59   ? 3865 GLN A CA    1 
ATOM   16959 C  C     . GLN A 1 3865 ? 166.138 125.434 160.189 1.00 8.35   ? 3865 GLN A C     1 
ATOM   16960 O  O     . GLN A 1 3865 ? 166.224 126.575 159.716 1.00 8.21   ? 3865 GLN A O     1 
ATOM   16961 C  CB    . GLN A 1 3865 ? 166.970 123.342 159.072 1.00 8.85   ? 3865 GLN A CB    1 
ATOM   16962 C  CG    . GLN A 1 3865 ? 166.790 123.843 157.650 1.00 7.70   ? 3865 GLN A CG    1 
ATOM   16963 C  CD    . GLN A 1 3865 ? 168.043 124.489 157.100 1.00 7.49   ? 3865 GLN A CD    1 
ATOM   16964 O  OE1   . GLN A 1 3865 ? 168.976 123.805 156.683 1.00 10.49  ? 3865 GLN A OE1   1 
ATOM   16965 N  NE2   . GLN A 1 3865 ? 168.074 125.815 157.100 1.00 8.77   ? 3865 GLN A NE2   1 
ATOM   16966 N  N     . VAL A 1 3866 ? 165.045 125.011 160.827 1.00 7.47   ? 3866 VAL A N     1 
ATOM   16967 C  CA    . VAL A 1 3866 ? 163.857 125.850 160.929 1.00 6.59   ? 3866 VAL A CA    1 
ATOM   16968 C  C     . VAL A 1 3866 ? 164.122 127.052 161.826 1.00 8.37   ? 3866 VAL A C     1 
ATOM   16969 O  O     . VAL A 1 3866 ? 163.647 128.160 161.551 1.00 11.64  ? 3866 VAL A O     1 
ATOM   16970 C  CB    . VAL A 1 3866 ? 162.661 125.017 161.426 1.00 8.34   ? 3866 VAL A CB    1 
ATOM   16971 C  CG1   . VAL A 1 3866 ? 161.476 125.912 161.749 1.00 10.53  ? 3866 VAL A CG1   1 
ATOM   16972 C  CG2   . VAL A 1 3866 ? 162.274 123.978 160.386 1.00 6.67   ? 3866 VAL A CG2   1 
ATOM   16973 N  N     . ALA A 1 3867 ? 164.878 126.861 162.912 1.00 8.17   ? 3867 ALA A N     1 
ATOM   16974 C  CA    . ALA A 1 3867 ? 165.213 127.987 163.773 1.00 6.79   ? 3867 ALA A CA    1 
ATOM   16975 C  C     . ALA A 1 3867 ? 165.992 129.043 163.004 1.00 8.09   ? 3867 ALA A C     1 
ATOM   16976 O  O     . ALA A 1 3867 ? 165.666 130.235 163.062 1.00 12.02  ? 3867 ALA A O     1 
ATOM   16977 C  CB    . ALA A 1 3867 ? 166.008 127.503 164.985 1.00 8.10   ? 3867 ALA A CB    1 
ATOM   16978 N  N     . PHE A 1 3868 ? 167.011 128.618 162.250 1.00 8.03   ? 3868 PHE A N     1 
ATOM   16979 C  CA    . PHE A 1 3868 ? 167.780 129.572 161.461 1.00 6.49   ? 3868 PHE A CA    1 
ATOM   16980 C  C     . PHE A 1 3868 ? 166.898 130.270 160.439 1.00 7.11   ? 3868 PHE A C     1 
ATOM   16981 O  O     . PHE A 1 3868 ? 166.958 131.492 160.290 1.00 9.19   ? 3868 PHE A O     1 
ATOM   16982 C  CB    . PHE A 1 3868 ? 168.945 128.880 160.760 1.00 6.36   ? 3868 PHE A CB    1 
ATOM   16983 C  CG    . PHE A 1 3868 ? 169.723 129.790 159.852 1.00 7.78   ? 3868 PHE A CG    1 
ATOM   16984 C  CD1   . PHE A 1 3868 ? 170.629 130.697 160.372 1.00 8.97   ? 3868 PHE A CD1   1 
ATOM   16985 C  CD2   . PHE A 1 3868 ? 169.534 129.753 158.483 1.00 6.78   ? 3868 PHE A CD2   1 
ATOM   16986 C  CE1   . PHE A 1 3868 ? 171.339 131.539 159.542 1.00 7.05   ? 3868 PHE A CE1   1 
ATOM   16987 C  CE2   . PHE A 1 3868 ? 170.240 130.596 157.650 1.00 6.93   ? 3868 PHE A CE2   1 
ATOM   16988 C  CZ    . PHE A 1 3868 ? 171.143 131.488 158.180 1.00 6.69   ? 3868 PHE A CZ    1 
ATOM   16989 N  N     . ASN A 1 3869 ? 166.065 129.508 159.727 1.00 6.76   ? 3869 ASN A N     1 
ATOM   16990 C  CA    . ASN A 1 3869 ? 165.224 130.110 158.697 1.00 5.44   ? 3869 ASN A CA    1 
ATOM   16991 C  C     . ASN A 1 3869 ? 164.303 131.168 159.290 1.00 6.87   ? 3869 ASN A C     1 
ATOM   16992 O  O     . ASN A 1 3869 ? 164.280 132.320 158.834 1.00 10.92  ? 3869 ASN A O     1 
ATOM   16993 C  CB    . ASN A 1 3869 ? 164.413 129.027 157.986 1.00 5.84   ? 3869 ASN A CB    1 
ATOM   16994 C  CG    . ASN A 1 3869 ? 165.264 128.154 157.088 1.00 9.14   ? 3869 ASN A CG    1 
ATOM   16995 O  OD1   . ASN A 1 3869 ? 166.458 128.394 156.920 1.00 13.83  ? 3869 ASN A OD1   1 
ATOM   16996 N  ND2   . ASN A 1 3869 ? 164.652 127.133 156.504 1.00 9.25   ? 3869 ASN A ND2   1 
ATOM   16997 N  N     . ARG A 1 3870 ? 163.558 130.800 160.336 1.00 6.90   ? 3870 ARG A N     1 
ATOM   16998 C  CA    . ARG A 1 3870 ? 162.583 131.716 160.915 1.00 7.38   ? 3870 ARG A CA    1 
ATOM   16999 C  C     . ARG A 1 3870 ? 163.255 132.939 161.524 1.00 6.39   ? 3870 ARG A C     1 
ATOM   17000 O  O     . ARG A 1 3870 ? 162.770 134.065 161.360 1.00 6.17   ? 3870 ARG A O     1 
ATOM   17001 C  CB    . ARG A 1 3870 ? 161.742 130.990 161.963 1.00 6.70   ? 3870 ARG A CB    1 
ATOM   17002 C  CG    . ARG A 1 3870 ? 160.849 129.902 161.401 1.00 7.72   ? 3870 ARG A CG    1 
ATOM   17003 C  CD    . ARG A 1 3870 ? 159.512 129.869 162.114 1.00 10.97  ? 3870 ARG A CD    1 
ATOM   17004 N  NE    . ARG A 1 3870 ? 158.682 128.758 161.664 1.00 20.34  ? 3870 ARG A NE    1 
ATOM   17005 C  CZ    . ARG A 1 3870 ? 157.487 128.470 162.158 1.00 20.58  ? 3870 ARG A CZ    1 
ATOM   17006 N  NH1   . ARG A 1 3870 ? 156.941 129.199 163.117 1.00 22.83  ? 3870 ARG A NH1   1 
ATOM   17007 N  NH2   . ARG A 1 3870 ? 156.825 127.419 161.683 1.00 19.37  ? 3870 ARG A NH2   1 
ATOM   17008 N  N     . VAL A 1 3871 ? 164.366 132.746 162.238 1.00 6.45   ? 3871 VAL A N     1 
ATOM   17009 C  CA    . VAL A 1 3871 ? 165.012 133.873 162.901 1.00 6.51   ? 3871 VAL A CA    1 
ATOM   17010 C  C     . VAL A 1 3871 ? 165.671 134.794 161.878 1.00 7.02   ? 3871 VAL A C     1 
ATOM   17011 O  O     . VAL A 1 3871 ? 165.562 136.022 161.967 1.00 6.48   ? 3871 VAL A O     1 
ATOM   17012 C  CB    . VAL A 1 3871 ? 166.015 133.368 163.953 1.00 6.69   ? 3871 VAL A CB    1 
ATOM   17013 C  CG1   . VAL A 1 3871 ? 166.886 134.501 164.449 1.00 6.41   ? 3871 VAL A CG1   1 
ATOM   17014 C  CG2   . VAL A 1 3871 ? 165.277 132.726 165.115 1.00 6.58   ? 3871 VAL A CG2   1 
ATOM   17015 N  N     . ALA A 1 3872 ? 166.351 134.218 160.881 1.00 8.23   ? 3872 ALA A N     1 
ATOM   17016 C  CA    . ALA A 1 3872 ? 167.059 135.014 159.889 1.00 4.65   ? 3872 ALA A CA    1 
ATOM   17017 C  C     . ALA A 1 3872 ? 166.122 135.693 158.904 1.00 6.50   ? 3872 ALA A C     1 
ATOM   17018 O  O     . ALA A 1 3872 ? 166.535 136.653 158.246 1.00 10.02  ? 3872 ALA A O     1 
ATOM   17019 C  CB    . ALA A 1 3872 ? 168.059 134.140 159.133 1.00 3.96   ? 3872 ALA A CB    1 
ATOM   17020 N  N     . ARG A 1 3873 ? 164.880 135.220 158.774 1.00 7.14   ? 3873 ARG A N     1 
ATOM   17021 C  CA    . ARG A 1 3873 ? 163.923 135.951 157.951 1.00 6.78   ? 3873 ARG A CA    1 
ATOM   17022 C  C     . ARG A 1 3873 ? 163.637 137.341 158.504 1.00 6.93   ? 3873 ARG A C     1 
ATOM   17023 O  O     . ARG A 1 3873 ? 163.179 138.211 157.755 1.00 7.62   ? 3873 ARG A O     1 
ATOM   17024 C  CB    . ARG A 1 3873 ? 162.622 135.160 157.821 1.00 10.42  ? 3873 ARG A CB    1 
ATOM   17025 C  CG    . ARG A 1 3873 ? 162.581 134.242 156.613 1.00 16.58  ? 3873 ARG A CG    1 
ATOM   17026 C  CD    . ARG A 1 3873 ? 163.060 134.959 155.364 1.00 18.46  ? 3873 ARG A CD    1 
ATOM   17027 N  NE    . ARG A 1 3873 ? 163.065 134.085 154.197 1.00 23.84  ? 3873 ARG A NE    1 
ATOM   17028 C  CZ    . ARG A 1 3873 ? 163.750 134.323 153.088 1.00 21.71  ? 3873 ARG A CZ    1 
ATOM   17029 N  NH1   . ARG A 1 3873 ? 164.499 135.406 152.958 1.00 17.31  ? 3873 ARG A NH1   1 
ATOM   17030 N  NH2   . ARG A 1 3873 ? 163.686 133.452 152.086 1.00 19.65  ? 3873 ARG A NH2   1 
ATOM   17031 N  N     . GLY A 1 3874 ? 163.896 137.569 159.789 1.00 6.16   ? 3874 GLY A N     1 
ATOM   17032 C  CA    . GLY A 1 3874 ? 163.688 138.870 160.390 1.00 5.52   ? 3874 GLY A CA    1 
ATOM   17033 C  C     . GLY A 1 3874 ? 164.967 139.511 160.884 1.00 6.85   ? 3874 GLY A C     1 
ATOM   17034 O  O     . GLY A 1 3874 ? 164.955 140.268 161.858 1.00 11.49  ? 3874 GLY A O     1 
ATOM   17035 N  N     . MET A 1 3875 ? 166.079 139.215 160.217 1.00 6.04   ? 3875 MET A N     1 
ATOM   17036 C  CA    . MET A 1 3875 ? 167.377 139.770 160.564 1.00 6.48   ? 3875 MET A CA    1 
ATOM   17037 C  C     . MET A 1 3875 ? 168.014 140.390 159.331 1.00 9.59   ? 3875 MET A C     1 
ATOM   17038 O  O     . MET A 1 3875 ? 167.698 140.021 158.197 1.00 10.77  ? 3875 MET A O     1 
ATOM   17039 C  CB    . MET A 1 3875 ? 168.319 138.701 161.134 1.00 5.72   ? 3875 MET A CB    1 
ATOM   17040 C  CG    . MET A 1 3875 ? 167.900 138.137 162.472 1.00 8.78   ? 3875 MET A CG    1 
ATOM   17041 S  SD    . MET A 1 3875 ? 169.006 136.829 163.032 1.00 28.20  ? 3875 MET A SD    1 
ATOM   17042 C  CE    . MET A 1 3875 ? 170.480 137.752 163.425 1.00 9.48   ? 3875 MET A CE    1 
ATOM   17043 N  N     . LEU A 1 3876 ? 168.911 141.343 159.564 1.00 8.56   ? 3876 LEU A N     1 
ATOM   17044 C  CA    . LEU A 1 3876 ? 169.732 141.867 158.487 1.00 5.96   ? 3876 LEU A CA    1 
ATOM   17045 C  C     . LEU A 1 3876 ? 170.660 140.776 157.965 1.00 8.97   ? 3876 LEU A C     1 
ATOM   17046 O  O     . LEU A 1 3876 ? 171.099 139.896 158.709 1.00 12.02  ? 3876 LEU A O     1 
ATOM   17047 C  CB    . LEU A 1 3876 ? 170.544 143.069 158.968 1.00 7.25   ? 3876 LEU A CB    1 
ATOM   17048 C  CG    . LEU A 1 3876 ? 169.754 144.183 159.659 1.00 7.50   ? 3876 LEU A CG    1 
ATOM   17049 C  CD1   . LEU A 1 3876 ? 170.690 145.130 160.387 1.00 10.56  ? 3876 LEU A CD1   1 
ATOM   17050 C  CD2   . LEU A 1 3876 ? 168.896 144.939 158.661 1.00 4.16   ? 3876 LEU A CD2   1 
ATOM   17051 N  N     . HIS A 1 3877 ? 170.949 140.834 156.663 1.00 7.40   ? 3877 HIS A N     1 
ATOM   17052 C  CA    . HIS A 1 3877 ? 171.736 139.776 156.037 1.00 6.15   ? 3877 HIS A CA    1 
ATOM   17053 C  C     . HIS A 1 3877 ? 173.146 139.710 156.609 1.00 7.06   ? 3877 HIS A C     1 
ATOM   17054 O  O     . HIS A 1 3877 ? 173.782 138.649 156.588 1.00 9.16   ? 3877 HIS A O     1 
ATOM   17055 C  CB    . HIS A 1 3877 ? 171.782 139.976 154.524 1.00 6.98   ? 3877 HIS A CB    1 
ATOM   17056 C  CG    . HIS A 1 3877 ? 172.262 138.773 153.777 1.00 8.85   ? 3877 HIS A CG    1 
ATOM   17057 N  ND1   . HIS A 1 3877 ? 173.592 138.564 153.478 1.00 8.16   ? 3877 HIS A ND1   1 
ATOM   17058 C  CD2   . HIS A 1 3877 ? 171.593 137.707 153.277 1.00 6.84   ? 3877 HIS A CD2   1 
ATOM   17059 C  CE1   . HIS A 1 3877 ? 173.720 137.424 152.824 1.00 10.82  ? 3877 HIS A CE1   1 
ATOM   17060 N  NE2   . HIS A 1 3877 ? 172.522 136.885 152.688 1.00 11.36  ? 3877 HIS A NE2   1 
ATOM   17061 N  N     . GLN A 1 3878 ? 173.656 140.832 157.121 1.00 9.47   ? 3878 GLN A N     1 
ATOM   17062 C  CA    . GLN A 1 3878 ? 175.000 140.838 157.688 1.00 7.53   ? 3878 GLN A CA    1 
ATOM   17063 C  C     . GLN A 1 3878 ? 175.083 140.004 158.960 1.00 11.85  ? 3878 GLN A C     1 
ATOM   17064 O  O     . GLN A 1 3878 ? 176.153 139.479 159.288 1.00 19.28  ? 3878 GLN A O     1 
ATOM   17065 C  CB    . GLN A 1 3878 ? 175.443 142.274 157.960 1.00 9.96   ? 3878 GLN A CB    1 
ATOM   17066 C  CG    . GLN A 1 3878 ? 174.358 143.155 158.551 1.00 12.46  ? 3878 GLN A CG    1 
ATOM   17067 C  CD    . GLN A 1 3878 ? 174.908 144.438 159.137 1.00 20.25  ? 3878 GLN A CD    1 
ATOM   17068 O  OE1   . GLN A 1 3878 ? 176.048 144.485 159.596 1.00 25.71  ? 3878 GLN A OE1   1 
ATOM   17069 N  NE2   . GLN A 1 3878 ? 174.098 145.489 159.121 1.00 18.26  ? 3878 GLN A NE2   1 
ATOM   17070 N  N     . ASP A 1 3879 ? 173.974 139.866 159.684 1.00 11.05  ? 3879 ASP A N     1 
ATOM   17071 C  CA    . ASP A 1 3879 ? 173.946 139.105 160.925 1.00 8.73   ? 3879 ASP A CA    1 
ATOM   17072 C  C     . ASP A 1 3879 ? 173.577 137.642 160.716 1.00 9.55   ? 3879 ASP A C     1 
ATOM   17073 O  O     . ASP A 1 3879 ? 173.567 136.871 161.687 1.00 14.60  ? 3879 ASP A O     1 
ATOM   17074 C  CB    . ASP A 1 3879 ? 172.962 139.750 161.902 1.00 9.69   ? 3879 ASP A CB    1 
ATOM   17075 C  CG    . ASP A 1 3879 ? 173.217 141.229 162.086 1.00 14.33  ? 3879 ASP A CG    1 
ATOM   17076 O  OD1   . ASP A 1 3879 ? 174.398 141.625 162.120 1.00 14.00  ? 3879 ASP A OD1   1 
ATOM   17077 O  OD2   . ASP A 1 3879 ? 172.239 141.996 162.196 1.00 16.94  ? 3879 ASP A OD2   1 
ATOM   17078 N  N     . HIS A 1 3880 ? 173.274 137.249 159.478 1.00 8.42   ? 3880 HIS A N     1 
ATOM   17079 C  CA    . HIS A 1 3880 ? 172.917 135.865 159.194 1.00 8.76   ? 3880 HIS A CA    1 
ATOM   17080 C  C     . HIS A 1 3880 ? 174.077 134.934 159.516 1.00 10.73  ? 3880 HIS A C     1 
ATOM   17081 O  O     . HIS A 1 3880 ? 173.897 133.883 160.142 1.00 15.39  ? 3880 HIS A O     1 
ATOM   17082 C  CB    . HIS A 1 3880 ? 172.516 135.730 157.724 1.00 7.83   ? 3880 HIS A CB    1 
ATOM   17083 C  CG    . HIS A 1 3880 ? 171.128 136.203 157.429 1.00 6.84   ? 3880 HIS A CG    1 
ATOM   17084 N  ND1   . HIS A 1 3880 ? 170.525 136.022 156.204 1.00 5.91   ? 3880 HIS A ND1   1 
ATOM   17085 C  CD2   . HIS A 1 3880 ? 170.232 136.870 158.194 1.00 7.17   ? 3880 HIS A CD2   1 
ATOM   17086 C  CE1   . HIS A 1 3880 ? 169.314 136.547 156.229 1.00 6.18   ? 3880 HIS A CE1   1 
ATOM   17087 N  NE2   . HIS A 1 3880 ? 169.111 137.068 157.425 1.00 6.57   ? 3880 HIS A NE2   1 
ATOM   17088 N  N     . ILE A 1 3881 ? 175.286 135.317 159.098 1.00 11.69  ? 3881 ILE A N     1 
ATOM   17089 C  CA    . ILE A 1 3881 ? 176.466 134.504 159.376 1.00 10.34  ? 3881 ILE A CA    1 
ATOM   17090 C  C     . ILE A 1 3881 ? 176.751 134.482 160.871 1.00 9.62   ? 3881 ILE A C     1 
ATOM   17091 O  O     . ILE A 1 3881 ? 177.186 133.464 161.418 1.00 10.24  ? 3881 ILE A O     1 
ATOM   17092 C  CB    . ILE A 1 3881 ? 177.672 135.015 158.564 1.00 10.51  ? 3881 ILE A CB    1 
ATOM   17093 C  CG1   . ILE A 1 3881 ? 178.922 134.187 158.872 1.00 11.32  ? 3881 ILE A CG1   1 
ATOM   17094 C  CG2   . ILE A 1 3881 ? 177.921 136.494 158.827 1.00 9.02   ? 3881 ILE A CG2   1 
ATOM   17095 C  CD1   . ILE A 1 3881 ? 178.773 132.716 158.556 1.00 8.39   ? 3881 ILE A CD1   1 
ATOM   17096 N  N     . THR A 1 3882 ? 176.496 135.599 161.557 1.00 9.78   ? 3882 THR A N     1 
ATOM   17097 C  CA    . THR A 1 3882 ? 176.702 135.642 163.000 1.00 8.84   ? 3882 THR A CA    1 
ATOM   17098 C  C     . THR A 1 3882 ? 175.791 134.654 163.717 1.00 9.50   ? 3882 THR A C     1 
ATOM   17099 O  O     . THR A 1 3882 ? 176.225 133.951 164.636 1.00 13.03  ? 3882 THR A O     1 
ATOM   17100 C  CB    . THR A 1 3882 ? 176.467 137.061 163.520 1.00 11.36  ? 3882 THR A CB    1 
ATOM   17101 O  OG1   . THR A 1 3882 ? 177.370 137.965 162.871 1.00 17.60  ? 3882 THR A OG1   1 
ATOM   17102 C  CG2   . THR A 1 3882 ? 176.694 137.122 165.019 1.00 11.26  ? 3882 THR A CG2   1 
ATOM   17103 N  N     . PHE A 1 3883 ? 174.522 134.587 163.310 1.00 8.14   ? 3883 PHE A N     1 
ATOM   17104 C  CA    . PHE A 1 3883 ? 173.606 133.629 163.925 1.00 5.21   ? 3883 PHE A CA    1 
ATOM   17105 C  C     . PHE A 1 3883 ? 173.972 132.194 163.559 1.00 7.36   ? 3883 PHE A C     1 
ATOM   17106 O  O     . PHE A 1 3883 ? 173.917 131.289 164.405 1.00 8.43   ? 3883 PHE A O     1 
ATOM   17107 C  CB    . PHE A 1 3883 ? 172.165 133.931 163.517 1.00 6.05   ? 3883 PHE A CB    1 
ATOM   17108 C  CG    . PHE A 1 3883 ? 171.147 133.128 164.273 1.00 5.71   ? 3883 PHE A CG    1 
ATOM   17109 C  CD1   . PHE A 1 3883 ? 171.262 132.953 165.639 1.00 5.53   ? 3883 PHE A CD1   1 
ATOM   17110 C  CD2   . PHE A 1 3883 ? 170.088 132.531 163.614 1.00 6.75   ? 3883 PHE A CD2   1 
ATOM   17111 C  CE1   . PHE A 1 3883 ? 170.333 132.210 166.336 1.00 5.67   ? 3883 PHE A CE1   1 
ATOM   17112 C  CE2   . PHE A 1 3883 ? 169.157 131.784 164.308 1.00 6.00   ? 3883 PHE A CE2   1 
ATOM   17113 C  CZ    . PHE A 1 3883 ? 169.278 131.625 165.670 1.00 4.82   ? 3883 PHE A CZ    1 
ATOM   17114 N  N     . ALA A 1 3884 ? 174.338 131.964 162.295 1.00 8.99   ? 3884 ALA A N     1 
ATOM   17115 C  CA    . ALA A 1 3884 ? 174.671 130.613 161.857 1.00 7.50   ? 3884 ALA A CA    1 
ATOM   17116 C  C     . ALA A 1 3884 ? 175.924 130.102 162.552 1.00 7.67   ? 3884 ALA A C     1 
ATOM   17117 O  O     . ALA A 1 3884 ? 176.049 128.902 162.815 1.00 8.81   ? 3884 ALA A O     1 
ATOM   17118 C  CB    . ALA A 1 3884 ? 174.846 130.580 160.341 1.00 8.46   ? 3884 ALA A CB    1 
ATOM   17119 N  N     . MET A 1 3885 ? 176.863 130.997 162.860 1.00 8.27   ? 3885 MET A N     1 
ATOM   17120 C  CA    . MET A 1 3885 ? 178.070 130.597 163.572 1.00 9.42   ? 3885 MET A CA    1 
ATOM   17121 C  C     . MET A 1 3885 ? 177.732 130.091 164.969 1.00 9.80   ? 3885 MET A C     1 
ATOM   17122 O  O     . MET A 1 3885 ? 178.257 129.066 165.421 1.00 9.82   ? 3885 MET A O     1 
ATOM   17123 C  CB    . MET A 1 3885 ? 179.035 131.781 163.641 1.00 13.15  ? 3885 MET A CB    1 
ATOM   17124 C  CG    . MET A 1 3885 ? 179.915 131.947 162.414 1.00 11.58  ? 3885 MET A CG    1 
ATOM   17125 S  SD    . MET A 1 3885 ? 181.194 130.692 162.266 1.00 26.93  ? 3885 MET A SD    1 
ATOM   17126 C  CE    . MET A 1 3885 ? 182.564 131.510 163.075 1.00 19.57  ? 3885 MET A CE    1 
ATOM   17127 N  N     . LEU A 1 3886 ? 176.839 130.799 165.664 1.00 10.08  ? 3886 LEU A N     1 
ATOM   17128 C  CA    . LEU A 1 3886 ? 176.415 130.365 166.990 1.00 8.63   ? 3886 LEU A CA    1 
ATOM   17129 C  C     . LEU A 1 3886 ? 175.652 129.050 166.922 1.00 6.57   ? 3886 LEU A C     1 
ATOM   17130 O  O     . LEU A 1 3886 ? 175.810 128.186 167.792 1.00 8.53   ? 3886 LEU A O     1 
ATOM   17131 C  CB    . LEU A 1 3886 ? 175.559 131.446 167.646 1.00 7.16   ? 3886 LEU A CB    1 
ATOM   17132 C  CG    . LEU A 1 3886 ? 176.244 132.786 167.901 1.00 6.23   ? 3886 LEU A CG    1 
ATOM   17133 C  CD1   . LEU A 1 3886 ? 175.276 133.736 168.570 1.00 8.32   ? 3886 LEU A CD1   1 
ATOM   17134 C  CD2   . LEU A 1 3886 ? 177.492 132.606 168.744 1.00 6.28   ? 3886 LEU A CD2   1 
ATOM   17135 N  N     . LEU A 1 3887 ? 174.808 128.885 165.902 1.00 6.77   ? 3887 LEU A N     1 
ATOM   17136 C  CA    . LEU A 1 3887 ? 174.094 127.620 165.745 1.00 7.10   ? 3887 LEU A CA    1 
ATOM   17137 C  C     . LEU A 1 3887 ? 175.062 126.470 165.484 1.00 7.21   ? 3887 LEU A C     1 
ATOM   17138 O  O     . LEU A 1 3887 ? 174.886 125.364 166.011 1.00 9.98   ? 3887 LEU A O     1 
ATOM   17139 C  CB    . LEU A 1 3887 ? 173.068 127.733 164.621 1.00 8.49   ? 3887 LEU A CB    1 
ATOM   17140 C  CG    . LEU A 1 3887 ? 171.851 128.602 164.937 1.00 4.91   ? 3887 LEU A CG    1 
ATOM   17141 C  CD1   . LEU A 1 3887 ? 170.949 128.712 163.727 1.00 5.63   ? 3887 LEU A CD1   1 
ATOM   17142 C  CD2   . LEU A 1 3887 ? 171.087 128.045 166.124 1.00 4.61   ? 3887 LEU A CD2   1 
ATOM   17143 N  N     . ALA A 1 3888 ? 176.090 126.714 164.669 1.00 7.97   ? 3888 ALA A N     1 
ATOM   17144 C  CA    . ALA A 1 3888 ? 177.105 125.697 164.421 1.00 9.33   ? 3888 ALA A CA    1 
ATOM   17145 C  C     . ALA A 1 3888 ? 177.865 125.357 165.694 1.00 8.69   ? 3888 ALA A C     1 
ATOM   17146 O  O     . ALA A 1 3888 ? 178.199 124.193 165.931 1.00 11.77  ? 3888 ALA A O     1 
ATOM   17147 C  CB    . ALA A 1 3888 ? 178.064 126.168 163.329 1.00 8.14   ? 3888 ALA A CB    1 
ATOM   17148 N  N     . ARG A 1 3889 ? 178.159 126.362 166.522 1.00 7.63   ? 3889 ARG A N     1 
ATOM   17149 C  CA    . ARG A 1 3889 ? 178.812 126.092 167.800 1.00 8.92   ? 3889 ARG A CA    1 
ATOM   17150 C  C     . ARG A 1 3889 ? 177.917 125.265 168.717 1.00 11.30  ? 3889 ARG A C     1 
ATOM   17151 O  O     . ARG A 1 3889 ? 178.396 124.364 169.418 1.00 15.41  ? 3889 ARG A O     1 
ATOM   17152 C  CB    . ARG A 1 3889 ? 179.211 127.402 168.477 1.00 9.99   ? 3889 ARG A CB    1 
ATOM   17153 C  CG    . ARG A 1 3889 ? 180.304 128.160 167.751 1.00 14.01  ? 3889 ARG A CG    1 
ATOM   17154 C  CD    . ARG A 1 3889 ? 181.079 129.043 168.705 1.00 18.51  ? 3889 ARG A CD    1 
ATOM   17155 N  NE    . ARG A 1 3889 ? 181.620 128.287 169.827 1.00 16.63  ? 3889 ARG A NE    1 
ATOM   17156 C  CZ    . ARG A 1 3889 ? 182.314 128.821 170.822 1.00 19.47  ? 3889 ARG A CZ    1 
ATOM   17157 N  NH1   . ARG A 1 3889 ? 182.575 130.117 170.864 1.00 19.66  ? 3889 ARG A NH1   1 
ATOM   17158 N  NH2   . ARG A 1 3889 ? 182.759 128.036 171.797 1.00 22.64  ? 3889 ARG A NH2   1 
ATOM   17159 N  N     . ILE A 1 3890 ? 176.616 125.564 168.733 1.00 9.95   ? 3890 ILE A N     1 
ATOM   17160 C  CA    . ILE A 1 3890 ? 175.681 124.788 169.545 1.00 7.93   ? 3890 ILE A CA    1 
ATOM   17161 C  C     . ILE A 1 3890 ? 175.659 123.336 169.084 1.00 9.58   ? 3890 ILE A C     1 
ATOM   17162 O  O     . ILE A 1 3890 ? 175.697 122.405 169.897 1.00 12.28  ? 3890 ILE A O     1 
ATOM   17163 C  CB    . ILE A 1 3890 ? 174.275 125.412 169.497 1.00 7.91   ? 3890 ILE A CB    1 
ATOM   17164 C  CG1   . ILE A 1 3890 ? 174.226 126.699 170.317 1.00 8.27   ? 3890 ILE A CG1   1 
ATOM   17165 C  CG2   . ILE A 1 3890 ? 173.234 124.430 170.009 1.00 10.94  ? 3890 ILE A CG2   1 
ATOM   17166 C  CD1   . ILE A 1 3890 ? 173.155 127.653 169.858 1.00 7.09   ? 3890 ILE A CD1   1 
ATOM   17167 N  N     . LYS A 1 3891 ? 175.596 123.122 167.768 1.00 9.55   ? 3891 LYS A N     1 
ATOM   17168 C  CA    . LYS A 1 3891 ? 175.643 121.762 167.240 1.00 10.19  ? 3891 LYS A CA    1 
ATOM   17169 C  C     . LYS A 1 3891 ? 176.960 121.064 167.551 1.00 16.51  ? 3891 LYS A C     1 
ATOM   17170 O  O     . LYS A 1 3891 ? 176.954 119.873 167.876 1.00 24.58  ? 3891 LYS A O     1 
ATOM   17171 C  CB    . LYS A 1 3891 ? 175.409 121.763 165.730 1.00 10.71  ? 3891 LYS A CB    1 
ATOM   17172 C  CG    . LYS A 1 3891 ? 175.006 120.406 165.183 1.00 11.88  ? 3891 LYS A CG    1 
ATOM   17173 C  CD    . LYS A 1 3891 ? 174.906 120.418 163.671 1.00 19.05  ? 3891 LYS A CD    1 
ATOM   17174 C  CE    . LYS A 1 3891 ? 174.250 119.148 163.161 1.00 26.68  ? 3891 LYS A CE    1 
ATOM   17175 N  NZ    . LYS A 1 3891 ? 172.902 118.946 163.758 1.00 33.12  ? 3891 LYS A NZ    1 
ATOM   17176 N  N     . LEU A 1 3892 ? 178.083 121.777 167.453 1.00 13.87  ? 3892 LEU A N     1 
ATOM   17177 C  CA    . LEU A 1 3892 ? 179.387 121.206 167.760 1.00 15.42  ? 3892 LEU A CA    1 
ATOM   17178 C  C     . LEU A 1 3892 ? 179.497 120.783 169.217 1.00 17.20  ? 3892 LEU A C     1 
ATOM   17179 O  O     . LEU A 1 3892 ? 180.062 119.723 169.510 1.00 16.80  ? 3892 LEU A O     1 
ATOM   17180 C  CB    . LEU A 1 3892 ? 180.484 122.215 167.419 1.00 16.03  ? 3892 LEU A CB    1 
ATOM   17181 C  CG    . LEU A 1 3892 ? 181.938 121.761 167.536 1.00 18.13  ? 3892 LEU A CG    1 
ATOM   17182 C  CD1   . LEU A 1 3892 ? 182.144 120.444 166.813 1.00 24.33  ? 3892 LEU A CD1   1 
ATOM   17183 C  CD2   . LEU A 1 3892 ? 182.869 122.829 166.992 1.00 18.82  ? 3892 LEU A CD2   1 
ATOM   17184 N  N     . LYS A 1 3893 ? 178.971 121.592 170.138 1.00 18.98  ? 3893 LYS A N     1 
ATOM   17185 C  CA    . LYS A 1 3893 ? 178.975 121.222 171.548 1.00 21.01  ? 3893 LYS A CA    1 
ATOM   17186 C  C     . LYS A 1 3893 ? 178.143 119.972 171.810 1.00 25.47  ? 3893 LYS A C     1 
ATOM   17187 O  O     . LYS A 1 3893 ? 178.436 119.222 172.749 1.00 33.13  ? 3893 LYS A O     1 
ATOM   17188 C  CB    . LYS A 1 3893 ? 178.462 122.389 172.393 1.00 16.32  ? 3893 LYS A CB    1 
ATOM   17189 C  CG    . LYS A 1 3893 ? 178.524 122.162 173.892 1.00 21.87  ? 3893 LYS A CG    1 
ATOM   17190 C  CD    . LYS A 1 3893 ? 178.069 123.394 174.652 1.00 28.03  ? 3893 LYS A CD    1 
ATOM   17191 C  CE    . LYS A 1 3893 ? 178.118 123.167 176.153 1.00 33.38  ? 3893 LYS A CE    1 
ATOM   17192 N  NZ    . LYS A 1 3893 ? 177.670 124.370 176.906 1.00 34.64  ? 3893 LYS A NZ    1 
ATOM   17193 N  N     . GLY A 1 3894 ? 177.124 119.725 170.995 1.00 20.99  ? 3894 GLY A N     1 
ATOM   17194 C  CA    . GLY A 1 3894 ? 176.248 118.585 171.143 1.00 23.67  ? 3894 GLY A CA    1 
ATOM   17195 C  C     . GLY A 1 3894 ? 176.704 117.311 170.472 1.00 29.25  ? 3894 GLY A C     1 
ATOM   17196 O  O     . GLY A 1 3894 ? 175.951 116.333 170.455 1.00 34.06  ? 3894 GLY A O     1 
ATOM   17197 N  N     . THR A 1 3895 ? 177.910 117.286 169.913 1.00 33.23  ? 3895 THR A N     1 
ATOM   17198 C  CA    . THR A 1 3895 ? 178.452 116.101 169.262 1.00 38.20  ? 3895 THR A CA    1 
ATOM   17199 C  C     . THR A 1 3895 ? 179.418 115.402 170.209 1.00 42.81  ? 3895 THR A C     1 
ATOM   17200 O  O     . THR A 1 3895 ? 180.361 116.024 170.710 1.00 43.35  ? 3895 THR A O     1 
ATOM   17201 C  CB    . THR A 1 3895 ? 179.161 116.466 167.957 1.00 38.69  ? 3895 THR A CB    1 
ATOM   17202 O  OG1   . THR A 1 3895 ? 178.231 117.090 167.063 1.00 24.44  ? 3895 THR A OG1   1 
ATOM   17203 C  CG2   . THR A 1 3895 ? 179.734 115.222 167.298 1.00 36.28  ? 3895 THR A CG2   1 
ATOM   17204 N  N     . VAL A 1 3896 ? 179.175 114.113 170.457 1.00 48.14  ? 3896 VAL A N     1 
ATOM   17205 C  CA    . VAL A 1 3896 ? 179.986 113.373 171.419 1.00 51.92  ? 3896 VAL A CA    1 
ATOM   17206 C  C     . VAL A 1 3896 ? 181.403 113.175 170.895 1.00 51.62  ? 3896 VAL A C     1 
ATOM   17207 O  O     . VAL A 1 3896 ? 182.382 113.399 171.617 1.00 52.88  ? 3896 VAL A O     1 
ATOM   17208 C  CB    . VAL A 1 3896 ? 179.317 112.030 171.758 1.00 56.68  ? 3896 VAL A CB    1 
ATOM   17209 C  CG1   . VAL A 1 3896 ? 180.080 111.323 172.867 1.00 57.29  ? 3896 VAL A CG1   1 
ATOM   17210 C  CG2   . VAL A 1 3896 ? 177.866 112.247 172.158 1.00 50.70  ? 3896 VAL A CG2   1 
ATOM   17211 N  N     . GLY A 1 3897 ? 181.539 112.757 169.640 1.00 47.34  ? 3897 GLY A N     1 
ATOM   17212 C  CA    . GLY A 1 3897 ? 182.846 112.474 169.081 1.00 46.03  ? 3897 GLY A CA    1 
ATOM   17213 C  C     . GLY A 1 3897 ? 183.552 113.692 168.524 1.00 45.03  ? 3897 GLY A C     1 
ATOM   17214 O  O     . GLY A 1 3897 ? 184.077 113.654 167.408 1.00 52.04  ? 3897 GLY A O     1 
ATOM   17215 N  N     . GLU A 1 3898 ? 183.572 114.782 169.291 1.00 43.28  ? 3898 GLU A N     1 
ATOM   17216 C  CA    . GLU A 1 3898 ? 184.221 116.014 168.876 1.00 48.63  ? 3898 GLU A CA    1 
ATOM   17217 C  C     . GLU A 1 3898 ? 184.902 116.672 170.066 1.00 44.65  ? 3898 GLU A C     1 
ATOM   17218 O  O     . GLU A 1 3898 ? 184.343 116.686 171.173 1.00 42.77  ? 3898 GLU A O     1 
ATOM   17219 C  CB    . GLU A 1 3898 ? 183.219 116.995 168.253 1.00 44.80  ? 3898 GLU A CB    1 
ATOM   17220 C  CG    . GLU A 1 3898 ? 183.026 116.826 166.756 1.00 45.36  ? 3898 GLU A CG    1 
ATOM   17221 C  CD    . GLU A 1 3898 ? 184.306 117.044 165.976 1.00 50.34  ? 3898 GLU A CD    1 
ATOM   17222 O  OE1   . GLU A 1 3898 ? 185.019 118.029 166.263 1.00 50.95  ? 3898 GLU A OE1   1 
ATOM   17223 O  OE2   . GLU A 1 3898 ? 184.600 116.232 165.076 1.00 52.37  ? 3898 GLU A OE2   1 
ATOM   17224 N  N     . PRO A 1 3899 ? 186.100 117.217 169.875 1.00 37.18  ? 3899 PRO A N     1 
ATOM   17225 C  CA    . PRO A 1 3899 ? 186.735 117.999 170.939 1.00 41.12  ? 3899 PRO A CA    1 
ATOM   17226 C  C     . PRO A 1 3899 ? 185.972 119.287 171.207 1.00 39.96  ? 3899 PRO A C     1 
ATOM   17227 O  O     . PRO A 1 3899 ? 185.257 119.813 170.352 1.00 48.28  ? 3899 PRO A O     1 
ATOM   17228 C  CB    . PRO A 1 3899 ? 188.136 118.289 170.388 1.00 41.32  ? 3899 PRO A CB    1 
ATOM   17229 C  CG    . PRO A 1 3899 ? 188.342 117.283 169.300 1.00 43.09  ? 3899 PRO A CG    1 
ATOM   17230 C  CD    . PRO A 1 3899 ? 186.989 117.033 168.718 1.00 39.69  ? 3899 PRO A CD    1 
ATOM   17231 N  N     . THR A 1 3900 ? 186.129 119.789 172.433 1.00 36.29  ? 3900 THR A N     1 
ATOM   17232 C  CA    . THR A 1 3900 ? 185.454 121.025 172.814 1.00 42.42  ? 3900 THR A CA    1 
ATOM   17233 C  C     . THR A 1 3900 ? 185.946 122.203 171.983 1.00 45.54  ? 3900 THR A C     1 
ATOM   17234 O  O     . THR A 1 3900 ? 185.166 123.106 171.655 1.00 47.77  ? 3900 THR A O     1 
ATOM   17235 C  CB    . THR A 1 3900 ? 185.657 121.302 174.303 1.00 48.22  ? 3900 THR A CB    1 
ATOM   17236 O  OG1   . THR A 1 3900 ? 187.054 121.464 174.577 1.00 45.81  ? 3900 THR A OG1   1 
ATOM   17237 C  CG2   . THR A 1 3900 ? 185.114 120.150 175.135 1.00 46.01  ? 3900 THR A CG2   1 
ATOM   17238 N  N     . TYR A 1 3901 ? 187.235 122.209 171.635 1.00 46.45  ? 3901 TYR A N     1 
ATOM   17239 C  CA    . TYR A 1 3901 ? 187.850 123.287 170.858 1.00 38.72  ? 3901 TYR A CA    1 
ATOM   17240 C  C     . TYR A 1 3901 ? 187.636 124.640 171.531 1.00 39.79  ? 3901 TYR A C     1 
ATOM   17241 O  O     . TYR A 1 3901 ? 187.419 125.656 170.869 1.00 41.06  ? 3901 TYR A O     1 
ATOM   17242 C  CB    . TYR A 1 3901 ? 187.331 123.302 169.418 1.00 33.84  ? 3901 TYR A CB    1 
ATOM   17243 C  CG    . TYR A 1 3901 ? 187.995 122.273 168.536 1.00 43.06  ? 3901 TYR A CG    1 
ATOM   17244 C  CD1   . TYR A 1 3901 ? 187.290 121.173 168.067 1.00 36.47  ? 3901 TYR A CD1   1 
ATOM   17245 C  CD2   . TYR A 1 3901 ? 189.334 122.388 168.192 1.00 47.53  ? 3901 TYR A CD2   1 
ATOM   17246 C  CE1   . TYR A 1 3901 ? 187.896 120.225 167.268 1.00 36.91  ? 3901 TYR A CE1   1 
ATOM   17247 C  CE2   . TYR A 1 3901 ? 189.950 121.444 167.394 1.00 48.23  ? 3901 TYR A CE2   1 
ATOM   17248 C  CZ    . TYR A 1 3901 ? 189.227 120.364 166.937 1.00 45.42  ? 3901 TYR A CZ    1 
ATOM   17249 O  OH    . TYR A 1 3901 ? 189.840 119.423 166.143 1.00 51.81  ? 3901 TYR A OH    1 
ATOM   17250 N  N     . ASP A 1 3902 ? 187.700 124.648 172.864 1.00 44.39  ? 3902 ASP A N     1 
ATOM   17251 C  CA    . ASP A 1 3902 ? 187.428 125.870 173.611 1.00 40.36  ? 3902 ASP A CA    1 
ATOM   17252 C  C     . ASP A 1 3902 ? 188.518 126.911 173.395 1.00 35.15  ? 3902 ASP A C     1 
ATOM   17253 O  O     . ASP A 1 3902 ? 188.220 128.087 173.160 1.00 35.35  ? 3902 ASP A O     1 
ATOM   17254 C  CB    . ASP A 1 3902 ? 187.279 125.551 175.098 1.00 43.68  ? 3902 ASP A CB    1 
ATOM   17255 C  CG    . ASP A 1 3902 ? 185.833 125.385 175.515 1.00 48.49  ? 3902 ASP A CG    1 
ATOM   17256 O  OD1   . ASP A 1 3902 ? 184.950 125.443 174.635 1.00 49.97  ? 3902 ASP A OD1   1 
ATOM   17257 O  OD2   . ASP A 1 3902 ? 185.579 125.196 176.723 1.00 54.67  ? 3902 ASP A OD2   1 
ATOM   17258 N  N     . ALA A 1 3903 ? 189.786 126.499 173.468 1.00 37.62  ? 3903 ALA A N     1 
ATOM   17259 C  CA    . ALA A 1 3903 ? 190.885 127.450 173.332 1.00 34.19  ? 3903 ALA A CA    1 
ATOM   17260 C  C     . ALA A 1 3903 ? 190.915 128.068 171.941 1.00 35.36  ? 3903 ALA A C     1 
ATOM   17261 O  O     . ALA A 1 3903 ? 191.201 129.263 171.790 1.00 37.67  ? 3903 ALA A O     1 
ATOM   17262 C  CB    . ALA A 1 3903 ? 192.214 126.762 173.644 1.00 37.63  ? 3903 ALA A CB    1 
ATOM   17263 N  N     . GLU A 1 3904 ? 190.627 127.268 170.913 1.00 33.16  ? 3904 GLU A N     1 
ATOM   17264 C  CA    . GLU A 1 3904 ? 190.608 127.784 169.549 1.00 28.79  ? 3904 GLU A CA    1 
ATOM   17265 C  C     . GLU A 1 3904 ? 189.556 128.875 169.393 1.00 33.15  ? 3904 GLU A C     1 
ATOM   17266 O  O     . GLU A 1 3904 ? 189.821 129.929 168.806 1.00 37.23  ? 3904 GLU A O     1 
ATOM   17267 C  CB    . GLU A 1 3904 ? 190.357 126.641 168.566 1.00 33.98  ? 3904 GLU A CB    1 
ATOM   17268 C  CG    . GLU A 1 3904 ? 191.618 125.945 168.087 1.00 40.74  ? 3904 GLU A CG    1 
ATOM   17269 C  CD    . GLU A 1 3904 ? 192.191 124.994 169.120 1.00 49.09  ? 3904 GLU A CD    1 
ATOM   17270 O  OE1   . GLU A 1 3904 ? 191.489 124.692 170.108 1.00 47.65  ? 3904 GLU A OE1   1 
ATOM   17271 O  OE2   . GLU A 1 3904 ? 193.344 124.548 168.942 1.00 44.32  ? 3904 GLU A OE2   1 
ATOM   17272 N  N     . PHE A 1 3905 ? 188.357 128.650 169.934 1.00 27.72  ? 3905 PHE A N     1 
ATOM   17273 C  CA    . PHE A 1 3905 ? 187.310 129.660 169.834 1.00 25.54  ? 3905 PHE A CA    1 
ATOM   17274 C  C     . PHE A 1 3905 ? 187.605 130.876 170.704 1.00 28.49  ? 3905 PHE A C     1 
ATOM   17275 O  O     . PHE A 1 3905 ? 187.261 132.001 170.325 1.00 33.56  ? 3905 PHE A O     1 
ATOM   17276 C  CB    . PHE A 1 3905 ? 185.956 129.052 170.194 1.00 26.94  ? 3905 PHE A CB    1 
ATOM   17277 C  CG    . PHE A 1 3905 ? 185.313 128.306 169.062 1.00 27.22  ? 3905 PHE A CG    1 
ATOM   17278 C  CD1   . PHE A 1 3905 ? 184.940 128.968 167.906 1.00 22.77  ? 3905 PHE A CD1   1 
ATOM   17279 C  CD2   . PHE A 1 3905 ? 185.096 126.942 169.146 1.00 30.15  ? 3905 PHE A CD2   1 
ATOM   17280 C  CE1   . PHE A 1 3905 ? 184.355 128.286 166.860 1.00 22.90  ? 3905 PHE A CE1   1 
ATOM   17281 C  CE2   . PHE A 1 3905 ? 184.512 126.255 168.103 1.00 26.94  ? 3905 PHE A CE2   1 
ATOM   17282 C  CZ    . PHE A 1 3905 ? 184.141 126.928 166.958 1.00 24.42  ? 3905 PHE A CZ    1 
ATOM   17283 N  N     . GLN A 1 3906 ? 188.233 130.678 171.867 1.00 30.54  ? 3906 GLN A N     1 
ATOM   17284 C  CA    . GLN A 1 3906 ? 188.633 131.820 172.685 1.00 30.12  ? 3906 GLN A CA    1 
ATOM   17285 C  C     . GLN A 1 3906 ? 189.637 132.696 171.951 1.00 31.66  ? 3906 GLN A C     1 
ATOM   17286 O  O     . GLN A 1 3906 ? 189.551 133.928 172.004 1.00 34.64  ? 3906 GLN A O     1 
ATOM   17287 C  CB    . GLN A 1 3906 ? 189.210 131.353 174.023 1.00 32.19  ? 3906 GLN A CB    1 
ATOM   17288 C  CG    . GLN A 1 3906 ? 188.224 130.621 174.917 1.00 45.79  ? 3906 GLN A CG    1 
ATOM   17289 C  CD    . GLN A 1 3906 ? 187.101 131.517 175.400 1.00 50.37  ? 3906 GLN A CD    1 
ATOM   17290 O  OE1   . GLN A 1 3906 ? 187.316 132.686 175.716 1.00 44.53  ? 3906 GLN A OE1   1 
ATOM   17291 N  NE2   . GLN A 1 3906 ? 185.891 130.971 175.459 1.00 55.49  ? 3906 GLN A NE2   1 
ATOM   17292 N  N     . HIS A 1 3907 ? 190.602 132.082 171.263 1.00 29.50  ? 3907 HIS A N     1 
ATOM   17293 C  CA    . HIS A 1 3907 ? 191.543 132.877 170.481 1.00 30.86  ? 3907 HIS A CA    1 
ATOM   17294 C  C     . HIS A 1 3907 ? 190.883 133.471 169.244 1.00 31.41  ? 3907 HIS A C     1 
ATOM   17295 O  O     . HIS A 1 3907 ? 191.306 134.527 168.764 1.00 35.60  ? 3907 HIS A O     1 
ATOM   17296 C  CB    . HIS A 1 3907 ? 192.753 132.041 170.076 1.00 36.07  ? 3907 HIS A CB    1 
ATOM   17297 C  CG    . HIS A 1 3907 ? 193.801 132.827 169.355 1.00 37.34  ? 3907 HIS A CG    1 
ATOM   17298 N  ND1   . HIS A 1 3907 ? 193.978 132.757 167.990 1.00 39.87  ? 3907 HIS A ND1   1 
ATOM   17299 C  CD2   . HIS A 1 3907 ? 194.713 133.720 169.807 1.00 40.27  ? 3907 HIS A CD2   1 
ATOM   17300 C  CE1   . HIS A 1 3907 ? 194.960 133.566 167.634 1.00 41.26  ? 3907 HIS A CE1   1 
ATOM   17301 N  NE2   . HIS A 1 3907 ? 195.423 134.161 168.717 1.00 45.27  ? 3907 HIS A NE2   1 
ATOM   17302 N  N     . PHE A 1 3908 ? 189.863 132.804 168.705 1.00 31.75  ? 3908 PHE A N     1 
ATOM   17303 C  CA    . PHE A 1 3908 ? 189.136 133.358 167.570 1.00 24.72  ? 3908 PHE A CA    1 
ATOM   17304 C  C     . PHE A 1 3908 ? 188.367 134.609 167.972 1.00 22.30  ? 3908 PHE A C     1 
ATOM   17305 O  O     . PHE A 1 3908 ? 188.267 135.564 167.193 1.00 23.84  ? 3908 PHE A O     1 
ATOM   17306 C  CB    . PHE A 1 3908 ? 188.190 132.303 166.998 1.00 23.67  ? 3908 PHE A CB    1 
ATOM   17307 C  CG    . PHE A 1 3908 ? 187.474 132.736 165.752 1.00 24.02  ? 3908 PHE A CG    1 
ATOM   17308 C  CD1   . PHE A 1 3908 ? 188.184 133.105 164.623 1.00 18.41  ? 3908 PHE A CD1   1 
ATOM   17309 C  CD2   . PHE A 1 3908 ? 186.092 132.766 165.707 1.00 23.82  ? 3908 PHE A CD2   1 
ATOM   17310 C  CE1   . PHE A 1 3908 ? 187.529 133.499 163.476 1.00 14.55  ? 3908 PHE A CE1   1 
ATOM   17311 C  CE2   . PHE A 1 3908 ? 185.433 133.159 164.560 1.00 19.24  ? 3908 PHE A CE2   1 
ATOM   17312 C  CZ    . PHE A 1 3908 ? 186.153 133.525 163.444 1.00 14.80  ? 3908 PHE A CZ    1 
ATOM   17313 N  N     . LEU A 1 3909 ? 187.820 134.623 169.187 1.00 25.47  ? 3909 LEU A N     1 
ATOM   17314 C  CA    . LEU A 1 3909 ? 186.989 135.744 169.614 1.00 29.40  ? 3909 LEU A CA    1 
ATOM   17315 C  C     . LEU A 1 3909 ? 187.808 136.847 170.272 1.00 32.94  ? 3909 LEU A C     1 
ATOM   17316 O  O     . LEU A 1 3909 ? 187.598 138.030 169.988 1.00 36.27  ? 3909 LEU A O     1 
ATOM   17317 C  CB    . LEU A 1 3909 ? 185.900 135.252 170.567 1.00 25.73  ? 3909 LEU A CB    1 
ATOM   17318 C  CG    . LEU A 1 3909 ? 184.866 134.316 169.945 1.00 25.18  ? 3909 LEU A CG    1 
ATOM   17319 C  CD1   . LEU A 1 3909 ? 183.917 133.779 171.001 1.00 32.47  ? 3909 LEU A CD1   1 
ATOM   17320 C  CD2   . LEU A 1 3909 ? 184.107 135.030 168.848 1.00 21.33  ? 3909 LEU A CD2   1 
ATOM   17321 N  N     . ARG A 1 3910 ? 188.738 136.486 171.152 1.00 35.00  ? 3910 ARG A N     1 
ATOM   17322 C  CA    . ARG A 1 3910 ? 189.517 137.449 171.920 1.00 34.41  ? 3910 ARG A CA    1 
ATOM   17323 C  C     . ARG A 1 3910 ? 191.010 137.286 171.663 1.00 42.16  ? 3910 ARG A C     1 
ATOM   17324 O  O     . ARG A 1 3910 ? 191.834 137.439 172.566 1.00 51.14  ? 3910 ARG A O     1 
ATOM   17325 C  CB    . ARG A 1 3910 ? 189.216 137.323 173.411 1.00 38.85  ? 3910 ARG A CB    1 
ATOM   17326 C  CG    . ARG A 1 3910 ? 187.810 137.733 173.800 1.00 37.89  ? 3910 ARG A CG    1 
ATOM   17327 C  CD    . ARG A 1 3910 ? 187.591 137.576 175.294 1.00 47.76  ? 3910 ARG A CD    1 
ATOM   17328 N  NE    . ARG A 1 3910 ? 186.238 137.946 175.690 1.00 58.10  ? 3910 ARG A NE    1 
ATOM   17329 C  CZ    . ARG A 1 3910 ? 185.768 137.849 176.925 1.00 59.02  ? 3910 ARG A CZ    1 
ATOM   17330 N  NH1   . ARG A 1 3910 ? 186.517 137.395 177.916 1.00 55.17  ? 3910 ARG A NH1   1 
ATOM   17331 N  NH2   . ARG A 1 3910 ? 184.513 138.215 177.172 1.00 54.69  ? 3910 ARG A NH2   1 
ATOM   17332 N  N     . GLY A 1 3911 ? 191.379 136.969 170.420 1.00 42.65  ? 3911 GLY A N     1 
ATOM   17333 C  CA    . GLY A 1 3911 ? 192.785 136.867 170.078 1.00 45.69  ? 3911 GLY A CA    1 
ATOM   17334 C  C     . GLY A 1 3911 ? 193.490 138.195 169.924 1.00 53.64  ? 3911 GLY A C     1 
ATOM   17335 O  O     . GLY A 1 3911 ? 194.720 138.244 170.017 1.00 58.57  ? 3911 GLY A O     1 
ATOM   17336 N  N     . ASN A 1 3912 ? 192.742 139.271 169.700 1.00 53.15  ? 3912 ASN A N     1 
ATOM   17337 C  CA    . ASN A 1 3912 ? 193.306 140.604 169.553 1.00 53.45  ? 3912 ASN A CA    1 
ATOM   17338 C  C     . ASN A 1 3912 ? 193.569 141.288 170.888 1.00 64.99  ? 3912 ASN A C     1 
ATOM   17339 O  O     . ASN A 1 3912 ? 194.042 142.429 170.902 1.00 69.67  ? 3912 ASN A O     1 
ATOM   17340 C  CB    . ASN A 1 3912 ? 192.384 141.469 168.682 1.00 56.29  ? 3912 ASN A CB    1 
ATOM   17341 C  CG    . ASN A 1 3912 ? 191.003 141.668 169.292 1.00 65.54  ? 3912 ASN A CG    1 
ATOM   17342 O  OD1   . ASN A 1 3912 ? 190.737 141.263 170.424 1.00 66.88  ? 3912 ASN A OD1   1 
ATOM   17343 N  ND2   . ASN A 1 3912 ? 190.113 142.294 168.531 1.00 59.61  ? 3912 ASN A ND2   1 
ATOM   17344 N  N     . GLU A 1 3913 ? 193.271 140.623 172.002 1.00 62.69  ? 3913 GLU A N     1 
ATOM   17345 C  CA    . GLU A 1 3913 ? 193.517 141.157 173.333 1.00 64.08  ? 3913 GLU A CA    1 
ATOM   17346 C  C     . GLU A 1 3913 ? 194.846 140.700 173.918 1.00 69.36  ? 3913 GLU A C     1 
ATOM   17347 O  O     . GLU A 1 3913 ? 195.133 141.006 175.080 1.00 73.56  ? 3913 GLU A O     1 
ATOM   17348 C  CB    . GLU A 1 3913 ? 192.376 140.761 174.276 1.00 62.18  ? 3913 GLU A CB    1 
ATOM   17349 C  CG    . GLU A 1 3913 ? 190.992 141.104 173.753 1.00 55.19  ? 3913 GLU A CG    1 
ATOM   17350 C  CD    . GLU A 1 3913 ? 189.905 140.872 174.785 1.00 60.04  ? 3913 GLU A CD    1 
ATOM   17351 O  OE1   . GLU A 1 3913 ? 190.232 140.427 175.905 1.00 59.45  ? 3913 GLU A OE1   1 
ATOM   17352 O  OE2   . GLU A 1 3913 ? 188.724 141.136 174.477 1.00 61.92  ? 3913 GLU A OE2   1 
ATOM   17353 N  N     . ILE A 1 3914 ? 195.658 139.976 173.153 1.00 67.33  ? 3914 ILE A N     1 
ATOM   17354 C  CA    . ILE A 1 3914 ? 196.947 139.499 173.641 1.00 71.81  ? 3914 ILE A CA    1 
ATOM   17355 C  C     . ILE A 1 3914 ? 197.953 140.641 173.591 1.00 78.31  ? 3914 ILE A C     1 
ATOM   17356 O  O     . ILE A 1 3914 ? 198.147 141.270 172.544 1.00 72.11  ? 3914 ILE A O     1 
ATOM   17357 C  CB    . ILE A 1 3914 ? 197.432 138.297 172.815 1.00 67.67  ? 3914 ILE A CB    1 
ATOM   17358 C  CG1   . ILE A 1 3914 ? 196.418 137.154 172.888 1.00 66.64  ? 3914 ILE A CG1   1 
ATOM   17359 C  CG2   . ILE A 1 3914 ? 198.794 137.830 173.300 1.00 66.55  ? 3914 ILE A CG2   1 
ATOM   17360 C  CD1   . ILE A 1 3914 ? 196.190 136.630 174.287 1.00 67.64  ? 3914 ILE A CD1   1 
ATOM   17361 N  N     . VAL A 1 3915 ? 198.598 140.909 174.726 1.00 86.55  ? 3915 VAL A N     1 
ATOM   17362 C  CA    . VAL A 1 3915 ? 199.582 141.982 174.799 1.00 88.50  ? 3915 VAL A CA    1 
ATOM   17363 C  C     . VAL A 1 3915 ? 200.845 141.559 174.063 1.00 84.76  ? 3915 VAL A C     1 
ATOM   17364 O  O     . VAL A 1 3915 ? 201.372 140.460 174.279 1.00 82.49  ? 3915 VAL A O     1 
ATOM   17365 C  CB    . VAL A 1 3915 ? 199.883 142.338 176.262 1.00 89.20  ? 3915 VAL A CB    1 
ATOM   17366 C  CG1   . VAL A 1 3915 ? 200.764 143.577 176.337 1.00 86.05  ? 3915 VAL A CG1   1 
ATOM   17367 C  CG2   . VAL A 1 3915 ? 198.590 142.545 177.036 1.00 79.80  ? 3915 VAL A CG2   1 
ATOM   17368 N  N     . LEU A 1 3916 ? 201.336 142.430 173.188 1.00 83.55  ? 3916 LEU A N     1 
ATOM   17369 C  CA    . LEU A 1 3916 ? 202.531 142.170 172.398 1.00 88.68  ? 3916 LEU A CA    1 
ATOM   17370 C  C     . LEU A 1 3916 ? 203.601 143.213 172.720 1.00 101.72 ? 3916 LEU A C     1 
ATOM   17371 O  O     . LEU A 1 3916 ? 203.444 144.045 173.617 1.00 104.40 ? 3916 LEU A O     1 
ATOM   17372 C  CB    . LEU A 1 3916 ? 202.198 142.154 170.905 1.00 81.28  ? 3916 LEU A CB    1 
ATOM   17373 C  CG    . LEU A 1 3916 ? 201.489 140.903 170.385 1.00 81.47  ? 3916 LEU A CG    1 
ATOM   17374 C  CD1   . LEU A 1 3916 ? 201.241 141.012 168.890 1.00 69.70  ? 3916 LEU A CD1   1 
ATOM   17375 C  CD2   . LEU A 1 3916 ? 202.295 139.656 170.714 1.00 75.79  ? 3916 LEU A CD2   1 
ATOM   17376 N  N     . SER A 1 3917 ? 204.699 143.159 171.969 1.00 106.14 ? 3917 SER A N     1 
ATOM   17377 C  CA    . SER A 1 3917 ? 205.812 144.077 172.152 1.00 107.96 ? 3917 SER A CA    1 
ATOM   17378 C  C     . SER A 1 3917 ? 206.506 144.278 170.813 1.00 109.60 ? 3917 SER A C     1 
ATOM   17379 O  O     . SER A 1 3917 ? 206.268 143.545 169.849 1.00 106.80 ? 3917 SER A O     1 
ATOM   17380 C  CB    . SER A 1 3917 ? 206.798 143.561 173.207 1.00 106.02 ? 3917 SER A CB    1 
ATOM   17381 O  OG    . SER A 1 3917 ? 206.160 143.381 174.459 1.00 105.10 ? 3917 SER A OG    1 
ATOM   17382 N  N     . ALA A 1 3918 ? 207.370 145.295 170.762 1.00 110.88 ? 3918 ALA A N     1 
ATOM   17383 C  CA    . ALA A 1 3918 ? 208.110 145.577 169.536 1.00 107.04 ? 3918 ALA A CA    1 
ATOM   17384 C  C     . ALA A 1 3918 ? 209.027 144.418 169.166 1.00 109.09 ? 3918 ALA A C     1 
ATOM   17385 O  O     . ALA A 1 3918 ? 209.150 144.066 167.986 1.00 103.90 ? 3918 ALA A O     1 
ATOM   17386 C  CB    . ALA A 1 3918 ? 208.911 146.869 169.691 1.00 92.21  ? 3918 ALA A CB    1 
ATOM   17387 N  N     . GLY A 1 3919 ? 209.679 143.812 170.160 1.00 111.54 ? 3919 GLY A N     1 
ATOM   17388 C  CA    . GLY A 1 3919 ? 210.568 142.696 169.893 1.00 107.76 ? 3919 GLY A CA    1 
ATOM   17389 C  C     . GLY A 1 3919 ? 209.857 141.412 169.522 1.00 99.99  ? 3919 GLY A C     1 
ATOM   17390 O  O     . GLY A 1 3919 ? 210.476 140.526 168.924 1.00 91.70  ? 3919 GLY A O     1 
ATOM   17391 N  N     . SER A 1 3920 ? 208.573 141.289 169.867 1.00 103.59 ? 3920 SER A N     1 
ATOM   17392 C  CA    . SER A 1 3920 ? 207.829 140.080 169.527 1.00 98.99  ? 3920 SER A CA    1 
ATOM   17393 C  C     . SER A 1 3920 ? 207.696 139.919 168.018 1.00 96.03  ? 3920 SER A C     1 
ATOM   17394 O  O     . SER A 1 3920 ? 207.783 138.800 167.497 1.00 91.59  ? 3920 SER A O     1 
ATOM   17395 C  CB    . SER A 1 3920 ? 206.450 140.105 170.187 1.00 93.82  ? 3920 SER A CB    1 
ATOM   17396 O  OG    . SER A 1 3920 ? 206.557 140.029 171.597 1.00 91.13  ? 3920 SER A OG    1 
ATOM   17397 N  N     . THR A 1 3921 ? 207.485 141.016 167.304 1.00 94.52  ? 3921 THR A N     1 
ATOM   17398 C  CA    . THR A 1 3921 ? 207.332 140.955 165.855 1.00 88.59  ? 3921 THR A CA    1 
ATOM   17399 C  C     . THR A 1 3921 ? 208.669 140.630 165.202 1.00 84.26  ? 3921 THR A C     1 
ATOM   17400 O  O     . THR A 1 3921 ? 209.621 141.408 165.344 1.00 84.21  ? 3921 THR A O     1 
ATOM   17401 C  CB    . THR A 1 3921 ? 206.795 142.282 165.328 1.00 86.98  ? 3921 THR A CB    1 
ATOM   17402 O  OG1   . THR A 1 3921 ? 205.559 142.595 165.983 1.00 81.29  ? 3921 THR A OG1   1 
ATOM   17403 C  CG2   . THR A 1 3921 ? 206.567 142.208 163.828 1.00 75.91  ? 3921 THR A CG2   1 
ATOM   17404 N  N     . PRO A 1 3922 ? 208.790 139.516 164.482 1.00 85.69  ? 3922 PRO A N     1 
ATOM   17405 C  CA    . PRO A 1 3922 ? 210.070 139.149 163.865 1.00 86.91  ? 3922 PRO A CA    1 
ATOM   17406 C  C     . PRO A 1 3922 ? 210.241 139.580 162.416 1.00 87.95  ? 3922 PRO A C     1 
ATOM   17407 O  O     . PRO A 1 3922 ? 211.264 139.231 161.815 1.00 91.02  ? 3922 PRO A O     1 
ATOM   17408 C  CB    . PRO A 1 3922 ? 210.053 137.619 163.975 1.00 86.66  ? 3922 PRO A CB    1 
ATOM   17409 C  CG    . PRO A 1 3922 ? 208.604 137.252 163.901 1.00 89.04  ? 3922 PRO A CG    1 
ATOM   17410 C  CD    . PRO A 1 3922 ? 207.783 138.455 164.320 1.00 90.20  ? 3922 PRO A CD    1 
ATOM   17411 N  N     . ARG A 1 3923 ? 209.286 140.319 161.849 1.00 86.35  ? 3923 ARG A N     1 
ATOM   17412 C  CA    . ARG A 1 3923 ? 209.395 140.861 160.493 1.00 77.92  ? 3923 ARG A CA    1 
ATOM   17413 C  C     . ARG A 1 3923 ? 209.591 139.723 159.481 1.00 75.11  ? 3923 ARG A C     1 
ATOM   17414 O  O     . ARG A 1 3923 ? 210.663 139.515 158.908 1.00 77.04  ? 3923 ARG A O     1 
ATOM   17415 C  CB    . ARG A 1 3923 ? 210.499 141.937 160.444 1.00 76.49  ? 3923 ARG A CB    1 
ATOM   17416 C  CG    . ARG A 1 3923 ? 211.149 142.296 159.102 1.00 76.33  ? 3923 ARG A CG    1 
ATOM   17417 C  CD    . ARG A 1 3923 ? 210.156 142.929 158.135 1.00 78.74  ? 3923 ARG A CD    1 
ATOM   17418 N  NE    . ARG A 1 3923 ? 210.592 142.871 156.742 1.00 78.90  ? 3923 ARG A NE    1 
ATOM   17419 C  CZ    . ARG A 1 3923 ? 210.836 141.760 156.058 1.00 81.17  ? 3923 ARG A CZ    1 
ATOM   17420 N  NH1   . ARG A 1 3923 ? 210.694 140.564 156.604 1.00 83.67  ? 3923 ARG A NH1   1 
ATOM   17421 N  NH2   . ARG A 1 3923 ? 211.233 141.852 154.792 1.00 79.81  ? 3923 ARG A NH2   1 
ATOM   17422 N  N     . ILE A 1 3924 ? 208.535 138.919 159.345 1.00 70.66  ? 3924 ILE A N     1 
ATOM   17423 C  CA    . ILE A 1 3924 ? 208.535 137.828 158.377 1.00 67.55  ? 3924 ILE A CA    1 
ATOM   17424 C  C     . ILE A 1 3924 ? 208.563 138.412 156.971 1.00 70.40  ? 3924 ILE A C     1 
ATOM   17425 O  O     . ILE A 1 3924 ? 207.865 139.391 156.674 1.00 68.63  ? 3924 ILE A O     1 
ATOM   17426 C  CB    . ILE A 1 3924 ? 207.305 136.924 158.565 1.00 66.97  ? 3924 ILE A CB    1 
ATOM   17427 C  CG1   . ILE A 1 3924 ? 207.301 136.251 159.940 1.00 71.53  ? 3924 ILE A CG1   1 
ATOM   17428 C  CG2   . ILE A 1 3924 ? 207.244 135.866 157.473 1.00 65.95  ? 3924 ILE A CG2   1 
ATOM   17429 C  CD1   . ILE A 1 3924 ? 206.614 137.061 161.019 1.00 70.07  ? 3924 ILE A CD1   1 
ATOM   17430 N  N     . GLN A 1 3925 ? 209.381 137.823 156.100 1.00 72.92  ? 3925 GLN A N     1 
ATOM   17431 C  CA    . GLN A 1 3925 ? 209.445 138.280 154.719 1.00 73.36  ? 3925 GLN A CA    1 
ATOM   17432 C  C     . GLN A 1 3925 ? 208.121 138.015 154.015 1.00 72.29  ? 3925 GLN A C     1 
ATOM   17433 O  O     . GLN A 1 3925 ? 207.547 136.928 154.131 1.00 69.07  ? 3925 GLN A O     1 
ATOM   17434 C  CB    . GLN A 1 3925 ? 210.591 137.586 153.984 1.00 76.86  ? 3925 GLN A CB    1 
ATOM   17435 C  CG    . GLN A 1 3925 ? 210.920 138.197 152.631 1.00 79.10  ? 3925 GLN A CG    1 
ATOM   17436 C  CD    . GLN A 1 3925 ? 210.290 137.446 151.478 1.00 84.40  ? 3925 GLN A CD    1 
ATOM   17437 O  OE1   . GLN A 1 3925 ? 209.615 136.436 151.675 1.00 82.97  ? 3925 GLN A OE1   1 
ATOM   17438 N  NE2   . GLN A 1 3925 ? 210.508 137.936 150.263 1.00 83.14  ? 3925 GLN A NE2   1 
ATOM   17439 N  N     . GLY A 1 3926 ? 207.635 139.015 153.284 1.00 75.26  ? 3926 GLY A N     1 
ATOM   17440 C  CA    . GLY A 1 3926 ? 206.367 138.911 152.597 1.00 67.01  ? 3926 GLY A CA    1 
ATOM   17441 C  C     . GLY A 1 3926 ? 205.146 139.112 153.466 1.00 60.53  ? 3926 GLY A C     1 
ATOM   17442 O  O     . GLY A 1 3926 ? 204.024 138.942 152.973 1.00 57.63  ? 3926 GLY A O     1 
ATOM   17443 N  N     . LEU A 1 3927 ? 205.322 139.466 154.736 1.00 58.07  ? 3927 LEU A N     1 
ATOM   17444 C  CA    . LEU A 1 3927 ? 204.221 139.668 155.667 1.00 48.94  ? 3927 LEU A CA    1 
ATOM   17445 C  C     . LEU A 1 3927 ? 204.239 141.106 156.161 1.00 52.92  ? 3927 LEU A C     1 
ATOM   17446 O  O     . LEU A 1 3927 ? 205.289 141.609 156.575 1.00 61.06  ? 3927 LEU A O     1 
ATOM   17447 C  CB    . LEU A 1 3927 ? 204.318 138.702 156.851 1.00 54.47  ? 3927 LEU A CB    1 
ATOM   17448 C  CG    . LEU A 1 3927 ? 203.434 137.455 156.820 1.00 49.65  ? 3927 LEU A CG    1 
ATOM   17449 C  CD1   . LEU A 1 3927 ? 203.733 136.611 155.594 1.00 50.95  ? 3927 LEU A CD1   1 
ATOM   17450 C  CD2   . LEU A 1 3927 ? 203.620 136.641 158.090 1.00 43.69  ? 3927 LEU A CD2   1 
ATOM   17451 N  N     . THR A 1 3928 ? 203.083 141.761 156.122 1.00 55.82  ? 3928 THR A N     1 
ATOM   17452 C  CA    . THR A 1 3928 ? 202.984 143.119 156.631 1.00 56.30  ? 3928 THR A CA    1 
ATOM   17453 C  C     . THR A 1 3928 ? 203.035 143.115 158.159 1.00 53.06  ? 3928 THR A C     1 
ATOM   17454 O  O     . THR A 1 3928 ? 203.040 142.065 158.808 1.00 48.04  ? 3928 THR A O     1 
ATOM   17455 C  CB    . THR A 1 3928 ? 201.700 143.789 156.142 1.00 55.03  ? 3928 THR A CB    1 
ATOM   17456 O  OG1   . THR A 1 3928 ? 200.565 143.064 156.628 1.00 57.06  ? 3928 THR A OG1   1 
ATOM   17457 C  CG2   . THR A 1 3928 ? 201.660 143.816 154.623 1.00 47.76  ? 3928 THR A CG2   1 
ATOM   17458 N  N     . VAL A 1 3929 ? 203.075 144.319 158.734 1.00 60.26  ? 3929 VAL A N     1 
ATOM   17459 C  CA    . VAL A 1 3929 ? 203.227 144.448 160.182 1.00 56.64  ? 3929 VAL A CA    1 
ATOM   17460 C  C     . VAL A 1 3929 ? 202.040 143.821 160.903 1.00 57.67  ? 3929 VAL A C     1 
ATOM   17461 O  O     . VAL A 1 3929 ? 202.209 143.026 161.834 1.00 61.71  ? 3929 VAL A O     1 
ATOM   17462 C  CB    . VAL A 1 3929 ? 203.409 145.926 160.573 1.00 58.87  ? 3929 VAL A CB    1 
ATOM   17463 C  CG1   . VAL A 1 3929 ? 203.452 146.072 162.085 1.00 58.09  ? 3929 VAL A CG1   1 
ATOM   17464 C  CG2   . VAL A 1 3929 ? 204.675 146.486 159.944 1.00 58.41  ? 3929 VAL A CG2   1 
ATOM   17465 N  N     . GLU A 1 3930 ? 200.821 144.163 160.478 1.00 59.62  ? 3930 GLU A N     1 
ATOM   17466 C  CA    . GLU A 1 3930 ? 199.637 143.612 161.132 1.00 60.30  ? 3930 GLU A CA    1 
ATOM   17467 C  C     . GLU A 1 3930 ? 199.541 142.103 160.942 1.00 52.37  ? 3930 GLU A C     1 
ATOM   17468 O  O     . GLU A 1 3930 ? 199.152 141.388 161.873 1.00 54.68  ? 3930 GLU A O     1 
ATOM   17469 C  CB    . GLU A 1 3930 ? 198.375 144.316 160.625 1.00 60.33  ? 3930 GLU A CB    1 
ATOM   17470 C  CG    . GLU A 1 3930 ? 197.988 144.015 159.185 1.00 63.73  ? 3930 GLU A CG    1 
ATOM   17471 C  CD    . GLU A 1 3930 ? 198.732 144.879 158.183 1.00 66.75  ? 3930 GLU A CD    1 
ATOM   17472 O  OE1   . GLU A 1 3930 ? 199.743 145.505 158.563 1.00 63.15  ? 3930 GLU A OE1   1 
ATOM   17473 O  OE2   . GLU A 1 3930 ? 198.302 144.933 157.011 1.00 66.51  ? 3930 GLU A OE2   1 
ATOM   17474 N  N     . GLN A 1 3931 ? 199.910 141.599 159.762 1.00 54.35  ? 3931 GLN A N     1 
ATOM   17475 C  CA    . GLN A 1 3931 ? 199.956 140.155 159.561 1.00 54.01  ? 3931 GLN A CA    1 
ATOM   17476 C  C     . GLN A 1 3931 ? 200.981 139.508 160.483 1.00 52.03  ? 3931 GLN A C     1 
ATOM   17477 O  O     . GLN A 1 3931 ? 200.745 138.418 161.014 1.00 55.44  ? 3931 GLN A O     1 
ATOM   17478 C  CB    . GLN A 1 3931 ? 200.268 139.832 158.101 1.00 45.29  ? 3931 GLN A CB    1 
ATOM   17479 C  CG    . GLN A 1 3931 ? 199.176 140.234 157.127 1.00 45.30  ? 3931 GLN A CG    1 
ATOM   17480 C  CD    . GLN A 1 3931 ? 199.531 139.914 155.690 1.00 53.65  ? 3931 GLN A CD    1 
ATOM   17481 O  OE1   . GLN A 1 3931 ? 200.631 139.447 155.399 1.00 55.42  ? 3931 GLN A OE1   1 
ATOM   17482 N  NE2   . GLN A 1 3931 ? 198.598 140.166 154.781 1.00 57.83  ? 3931 GLN A NE2   1 
ATOM   17483 N  N     . ALA A 1 3932 ? 202.127 140.162 160.681 1.00 51.38  ? 3932 ALA A N     1 
ATOM   17484 C  CA    . ALA A 1 3932 ? 203.143 139.619 161.575 1.00 50.69  ? 3932 ALA A CA    1 
ATOM   17485 C  C     . ALA A 1 3932 ? 202.646 139.564 163.015 1.00 49.29  ? 3932 ALA A C     1 
ATOM   17486 O  O     . ALA A 1 3932 ? 202.866 138.569 163.718 1.00 49.92  ? 3932 ALA A O     1 
ATOM   17487 C  CB    . ALA A 1 3932 ? 204.422 140.448 161.478 1.00 60.93  ? 3932 ALA A CB    1 
ATOM   17488 N  N     . GLU A 1 3933 ? 201.976 140.624 163.477 1.00 51.25  ? 3933 GLU A N     1 
ATOM   17489 C  CA    . GLU A 1 3933 ? 201.418 140.601 164.827 1.00 53.17  ? 3933 GLU A CA    1 
ATOM   17490 C  C     . GLU A 1 3933 ? 200.348 139.526 164.960 1.00 50.09  ? 3933 GLU A C     1 
ATOM   17491 O  O     . GLU A 1 3933 ? 200.260 138.855 165.995 1.00 53.43  ? 3933 GLU A O     1 
ATOM   17492 C  CB    . GLU A 1 3933 ? 200.853 141.971 165.206 1.00 57.01  ? 3933 GLU A CB    1 
ATOM   17493 C  CG    . GLU A 1 3933 ? 201.740 143.147 164.845 1.00 60.49  ? 3933 GLU A CG    1 
ATOM   17494 C  CD    . GLU A 1 3933 ? 200.968 144.449 164.739 1.00 71.40  ? 3933 GLU A CD    1 
ATOM   17495 O  OE1   . GLU A 1 3933 ? 201.513 145.499 165.139 1.00 66.93  ? 3933 GLU A OE1   1 
ATOM   17496 O  OE2   . GLU A 1 3933 ? 199.814 144.422 164.262 1.00 74.27  ? 3933 GLU A OE2   1 
ATOM   17497 N  N     . ALA A 1 3934 ? 199.524 139.348 163.925 1.00 50.36  ? 3934 ALA A N     1 
ATOM   17498 C  CA    . ALA A 1 3934 ? 198.522 138.287 163.955 1.00 45.28  ? 3934 ALA A CA    1 
ATOM   17499 C  C     . ALA A 1 3934 ? 199.177 136.913 164.028 1.00 44.46  ? 3934 ALA A C     1 
ATOM   17500 O  O     . ALA A 1 3934 ? 198.702 136.029 164.750 1.00 47.35  ? 3934 ALA A O     1 
ATOM   17501 C  CB    . ALA A 1 3934 ? 197.615 138.387 162.730 1.00 34.50  ? 3934 ALA A CB    1 
ATOM   17502 N  N     . VAL A 1 3935 ? 200.266 136.715 163.284 1.00 45.96  ? 3935 VAL A N     1 
ATOM   17503 C  CA    . VAL A 1 3935 ? 200.980 135.440 163.317 1.00 45.30  ? 3935 VAL A CA    1 
ATOM   17504 C  C     . VAL A 1 3935 ? 201.550 135.187 164.706 1.00 48.99  ? 3935 VAL A C     1 
ATOM   17505 O  O     . VAL A 1 3935 ? 201.449 134.080 165.248 1.00 55.68  ? 3935 VAL A O     1 
ATOM   17506 C  CB    . VAL A 1 3935 ? 202.082 135.417 162.242 1.00 43.71  ? 3935 VAL A CB    1 
ATOM   17507 C  CG1   . VAL A 1 3935 ? 203.039 134.259 162.479 1.00 46.26  ? 3935 VAL A CG1   1 
ATOM   17508 C  CG2   . VAL A 1 3935 ? 201.468 135.325 160.867 1.00 39.49  ? 3935 VAL A CG2   1 
ATOM   17509 N  N     . VAL A 1 3936 ? 202.160 136.213 165.304 1.00 44.41  ? 3936 VAL A N     1 
ATOM   17510 C  CA    . VAL A 1 3936 ? 202.723 136.058 166.642 1.00 45.67  ? 3936 VAL A CA    1 
ATOM   17511 C  C     . VAL A 1 3936 ? 201.625 135.740 167.651 1.00 47.64  ? 3936 VAL A C     1 
ATOM   17512 O  O     . VAL A 1 3936 ? 201.797 134.882 168.525 1.00 52.44  ? 3936 VAL A O     1 
ATOM   17513 C  CB    . VAL A 1 3936 ? 203.517 137.315 167.041 1.00 55.70  ? 3936 VAL A CB    1 
ATOM   17514 C  CG1   . VAL A 1 3936 ? 204.007 137.202 168.476 1.00 55.34  ? 3936 VAL A CG1   1 
ATOM   17515 C  CG2   . VAL A 1 3936 ? 204.693 137.514 166.103 1.00 59.17  ? 3936 VAL A CG2   1 
ATOM   17516 N  N     . ARG A 1 3937 ? 200.481 136.419 167.544 1.00 43.52  ? 3937 ARG A N     1 
ATOM   17517 C  CA    . ARG A 1 3937 ? 199.374 136.157 168.459 1.00 45.82  ? 3937 ARG A CA    1 
ATOM   17518 C  C     . ARG A 1 3937 ? 198.836 134.741 168.288 1.00 47.13  ? 3937 ARG A C     1 
ATOM   17519 O  O     . ARG A 1 3937 ? 198.514 134.069 169.275 1.00 54.48  ? 3937 ARG A O     1 
ATOM   17520 C  CB    . ARG A 1 3937 ? 198.266 137.186 168.241 1.00 48.61  ? 3937 ARG A CB    1 
ATOM   17521 C  CG    . ARG A 1 3937 ? 198.537 138.535 168.884 1.00 51.32  ? 3937 ARG A CG    1 
ATOM   17522 C  CD    . ARG A 1 3937 ? 197.343 139.461 168.738 1.00 60.31  ? 3937 ARG A CD    1 
ATOM   17523 N  NE    . ARG A 1 3937 ? 197.451 140.643 169.585 1.00 70.67  ? 3937 ARG A NE    1 
ATOM   17524 C  CZ    . ARG A 1 3937 ? 197.718 141.863 169.140 1.00 69.97  ? 3937 ARG A CZ    1 
ATOM   17525 N  NH1   . ARG A 1 3937 ? 197.911 142.102 167.854 1.00 67.39  ? 3937 ARG A NH1   1 
ATOM   17526 N  NH2   . ARG A 1 3937 ? 197.789 142.868 170.007 1.00 68.27  ? 3937 ARG A NH2   1 
ATOM   17527 N  N     . LEU A 1 3938 ? 198.725 134.272 167.043 1.00 47.05  ? 3938 LEU A N     1 
ATOM   17528 C  CA    . LEU A 1 3938 ? 198.268 132.908 166.800 1.00 45.56  ? 3938 LEU A CA    1 
ATOM   17529 C  C     . LEU A 1 3938 ? 199.284 131.881 167.284 1.00 53.34  ? 3938 LEU A C     1 
ATOM   17530 O  O     . LEU A 1 3938 ? 198.909 130.754 167.627 1.00 57.22  ? 3938 LEU A O     1 
ATOM   17531 C  CB    . LEU A 1 3938 ? 197.975 132.714 165.311 1.00 40.49  ? 3938 LEU A CB    1 
ATOM   17532 C  CG    . LEU A 1 3938 ? 197.405 131.367 164.858 1.00 49.11  ? 3938 LEU A CG    1 
ATOM   17533 C  CD1   . LEU A 1 3938 ? 196.082 131.069 165.546 1.00 40.52  ? 3938 LEU A CD1   1 
ATOM   17534 C  CD2   . LEU A 1 3938 ? 197.243 131.334 163.347 1.00 43.60  ? 3938 LEU A CD2   1 
ATOM   17535 N  N     . SER A 1 3939 ? 200.566 132.251 167.323 1.00 55.54  ? 3939 SER A N     1 
ATOM   17536 C  CA    . SER A 1 3939 ? 201.599 131.322 167.770 1.00 55.92  ? 3939 SER A CA    1 
ATOM   17537 C  C     . SER A 1 3939 ? 201.445 130.933 169.235 1.00 58.29  ? 3939 SER A C     1 
ATOM   17538 O  O     . SER A 1 3939 ? 202.054 129.950 169.669 1.00 55.66  ? 3939 SER A O     1 
ATOM   17539 C  CB    . SER A 1 3939 ? 202.983 131.930 167.541 1.00 55.01  ? 3939 SER A CB    1 
ATOM   17540 O  OG    . SER A 1 3939 ? 203.225 132.993 168.446 1.00 52.40  ? 3939 SER A OG    1 
ATOM   17541 N  N     . CYS A 1 3940 ? 200.653 131.682 170.007 1.00 58.95  ? 3940 CYS A N     1 
ATOM   17542 C  CA    . CYS A 1 3940 ? 200.457 131.348 171.414 1.00 54.58  ? 3940 CYS A CA    1 
ATOM   17543 C  C     . CYS A 1 3940 ? 199.738 130.016 171.583 1.00 60.29  ? 3940 CYS A C     1 
ATOM   17544 O  O     . CYS A 1 3940 ? 199.916 129.342 172.604 1.00 67.42  ? 3940 CYS A O     1 
ATOM   17545 C  CB    . CYS A 1 3940 ? 199.680 132.461 172.116 1.00 52.05  ? 3940 CYS A CB    1 
ATOM   17546 S  SG    . CYS A 1 3940 ? 200.516 134.063 172.131 1.00 65.67  ? 3940 CYS A SG    1 
ATOM   17547 N  N     . LEU A 1 3941 ? 198.925 129.625 170.608 1.00 61.84  ? 3941 LEU A N     1 
ATOM   17548 C  CA    . LEU A 1 3941 ? 198.222 128.355 170.696 1.00 57.44  ? 3941 LEU A CA    1 
ATOM   17549 C  C     . LEU A 1 3941 ? 199.206 127.196 170.543 1.00 57.90  ? 3941 LEU A C     1 
ATOM   17550 O  O     . LEU A 1 3941 ? 200.186 127.309 169.800 1.00 59.91  ? 3941 LEU A O     1 
ATOM   17551 C  CB    . LEU A 1 3941 ? 197.137 128.267 169.624 1.00 57.85  ? 3941 LEU A CB    1 
ATOM   17552 C  CG    . LEU A 1 3941 ? 195.711 128.520 170.114 1.00 53.18  ? 3941 LEU A CG    1 
ATOM   17553 C  CD1   . LEU A 1 3941 ? 195.605 129.904 170.732 1.00 51.90  ? 3941 LEU A CD1   1 
ATOM   17554 C  CD2   . LEU A 1 3941 ? 194.710 128.354 168.984 1.00 45.53  ? 3941 LEU A CD2   1 
ATOM   17555 N  N     . PRO A 1 3942 ? 198.977 126.077 171.235 1.00 58.46  ? 3942 PRO A N     1 
ATOM   17556 C  CA    . PRO A 1 3942 ? 199.907 124.940 171.111 1.00 58.49  ? 3942 PRO A CA    1 
ATOM   17557 C  C     . PRO A 1 3942 ? 199.969 124.351 169.713 1.00 55.89  ? 3942 PRO A C     1 
ATOM   17558 O  O     . PRO A 1 3942 ? 200.996 123.769 169.343 1.00 57.68  ? 3942 PRO A O     1 
ATOM   17559 C  CB    . PRO A 1 3942 ? 199.368 123.922 172.126 1.00 53.79  ? 3942 PRO A CB    1 
ATOM   17560 C  CG    . PRO A 1 3942 ? 197.981 124.339 172.434 1.00 56.08  ? 3942 PRO A CG    1 
ATOM   17561 C  CD    . PRO A 1 3942 ? 197.826 125.788 172.107 1.00 56.51  ? 3942 PRO A CD    1 
ATOM   17562 N  N     . ALA A 1 3943 ? 198.902 124.476 168.923 1.00 54.43  ? 3943 ALA A N     1 
ATOM   17563 C  CA    . ALA A 1 3943 ? 198.901 123.897 167.585 1.00 58.18  ? 3943 ALA A CA    1 
ATOM   17564 C  C     . ALA A 1 3943 ? 199.637 124.764 166.572 1.00 59.61  ? 3943 ALA A C     1 
ATOM   17565 O  O     . ALA A 1 3943 ? 199.888 124.305 165.452 1.00 58.03  ? 3943 ALA A O     1 
ATOM   17566 C  CB    . ALA A 1 3943 ? 197.466 123.656 167.117 1.00 54.68  ? 3943 ALA A CB    1 
ATOM   17567 N  N     . PHE A 1 3944 ? 199.983 126.000 166.930 1.00 56.41  ? 3944 PHE A N     1 
ATOM   17568 C  CA    . PHE A 1 3944 ? 200.618 126.935 166.010 1.00 51.89  ? 3944 PHE A CA    1 
ATOM   17569 C  C     . PHE A 1 3944 ? 201.957 127.441 166.537 1.00 59.39  ? 3944 PHE A C     1 
ATOM   17570 O  O     . PHE A 1 3944 ? 202.391 128.540 166.183 1.00 59.54  ? 3944 PHE A O     1 
ATOM   17571 C  CB    . PHE A 1 3944 ? 199.686 128.110 165.720 1.00 52.43  ? 3944 PHE A CB    1 
ATOM   17572 C  CG    . PHE A 1 3944 ? 198.440 127.729 164.976 1.00 46.55  ? 3944 PHE A CG    1 
ATOM   17573 C  CD1   . PHE A 1 3944 ? 198.458 127.568 163.603 1.00 41.75  ? 3944 PHE A CD1   1 
ATOM   17574 C  CD2   . PHE A 1 3944 ? 197.248 127.533 165.651 1.00 52.05  ? 3944 PHE A CD2   1 
ATOM   17575 C  CE1   . PHE A 1 3944 ? 197.313 127.217 162.919 1.00 44.37  ? 3944 PHE A CE1   1 
ATOM   17576 C  CE2   . PHE A 1 3944 ? 196.099 127.184 164.971 1.00 48.29  ? 3944 PHE A CE2   1 
ATOM   17577 C  CZ    . PHE A 1 3944 ? 196.132 127.027 163.603 1.00 44.01  ? 3944 PHE A CZ    1 
ATOM   17578 N  N     . LYS A 1 3945 ? 202.621 126.655 167.389 1.00 63.78  ? 3945 LYS A N     1 
ATOM   17579 C  CA    . LYS A 1 3945 ? 203.908 127.079 167.931 1.00 62.73  ? 3945 LYS A CA    1 
ATOM   17580 C  C     . LYS A 1 3945 ? 204.948 127.229 166.829 1.00 67.17  ? 3945 LYS A C     1 
ATOM   17581 O  O     . LYS A 1 3945 ? 205.710 128.203 166.812 1.00 70.43  ? 3945 LYS A O     1 
ATOM   17582 C  CB    . LYS A 1 3945 ? 204.388 126.087 168.990 1.00 61.86  ? 3945 LYS A CB    1 
ATOM   17583 C  CG    . LYS A 1 3945 ? 203.354 125.772 170.054 1.00 64.40  ? 3945 LYS A CG    1 
ATOM   17584 C  CD    . LYS A 1 3945 ? 203.180 126.934 171.018 1.00 64.74  ? 3945 LYS A CD    1 
ATOM   17585 C  CE    . LYS A 1 3945 ? 203.169 126.458 172.461 1.00 61.34  ? 3945 LYS A CE    1 
ATOM   17586 N  NZ    . LYS A 1 3945 ? 202.477 127.427 173.355 1.00 62.62  ? 3945 LYS A NZ    1 
ATOM   17587 N  N     . ASP A 1 3946 ? 204.996 126.278 165.901 1.00 64.72  ? 3946 ASP A N     1 
ATOM   17588 C  CA    . ASP A 1 3946 ? 205.904 126.357 164.760 1.00 68.91  ? 3946 ASP A CA    1 
ATOM   17589 C  C     . ASP A 1 3946 ? 205.150 126.913 163.554 1.00 64.65  ? 3946 ASP A C     1 
ATOM   17590 O  O     . ASP A 1 3946 ? 204.825 126.211 162.597 1.00 70.77  ? 3946 ASP A O     1 
ATOM   17591 C  CB    . ASP A 1 3946 ? 206.511 124.987 164.470 1.00 72.72  ? 3946 ASP A CB    1 
ATOM   17592 C  CG    . ASP A 1 3946 ? 207.717 125.065 163.551 1.00 74.66  ? 3946 ASP A CG    1 
ATOM   17593 O  OD1   . ASP A 1 3946 ? 207.559 125.491 162.388 1.00 67.77  ? 3946 ASP A OD1   1 
ATOM   17594 O  OD2   . ASP A 1 3946 ? 208.826 124.701 163.996 1.00 81.16  ? 3946 ASP A OD2   1 
ATOM   17595 N  N     . LEU A 1 3947 ? 204.864 128.210 163.625 1.00 53.94  ? 3947 LEU A N     1 
ATOM   17596 C  CA    . LEU A 1 3947 ? 204.141 128.910 162.570 1.00 60.23  ? 3947 LEU A CA    1 
ATOM   17597 C  C     . LEU A 1 3947 ? 205.020 129.845 161.757 1.00 62.75  ? 3947 LEU A C     1 
ATOM   17598 O  O     . LEU A 1 3947 ? 204.932 129.851 160.527 1.00 62.97  ? 3947 LEU A O     1 
ATOM   17599 C  CB    . LEU A 1 3947 ? 202.975 129.707 163.166 1.00 57.67  ? 3947 LEU A CB    1 
ATOM   17600 C  CG    . LEU A 1 3947 ? 202.099 130.472 162.174 1.00 50.52  ? 3947 LEU A CG    1 
ATOM   17601 C  CD1   . LEU A 1 3947 ? 201.528 129.527 161.130 1.00 45.49  ? 3947 LEU A CD1   1 
ATOM   17602 C  CD2   . LEU A 1 3947 ? 200.986 131.207 162.898 1.00 48.85  ? 3947 LEU A CD2   1 
ATOM   17603 N  N     . ILE A 1 3948 ? 205.864 130.640 162.416 1.00 61.30  ? 3948 ILE A N     1 
ATOM   17604 C  CA    . ILE A 1 3948 ? 206.773 131.525 161.693 1.00 58.86  ? 3948 ILE A CA    1 
ATOM   17605 C  C     . ILE A 1 3948 ? 207.749 130.705 160.857 1.00 66.36  ? 3948 ILE A C     1 
ATOM   17606 O  O     . ILE A 1 3948 ? 208.000 131.005 159.682 1.00 63.01  ? 3948 ILE A O     1 
ATOM   17607 C  CB    . ILE A 1 3948 ? 207.513 132.455 162.673 1.00 58.70  ? 3948 ILE A CB    1 
ATOM   17608 C  CG1   . ILE A 1 3948 ? 206.533 133.372 163.413 1.00 62.73  ? 3948 ILE A CG1   1 
ATOM   17609 C  CG2   . ILE A 1 3948 ? 208.552 133.284 161.940 1.00 65.63  ? 3948 ILE A CG2   1 
ATOM   17610 C  CD1   . ILE A 1 3948 ? 205.993 132.799 164.710 1.00 56.14  ? 3948 ILE A CD1   1 
ATOM   17611 N  N     . ALA A 1 3949 ? 208.306 129.648 161.454 1.00 62.26  ? 3949 ALA A N     1 
ATOM   17612 C  CA    . ALA A 1 3949 ? 209.230 128.785 160.727 1.00 61.23  ? 3949 ALA A CA    1 
ATOM   17613 C  C     . ALA A 1 3949 ? 208.533 128.080 159.572 1.00 58.37  ? 3949 ALA A C     1 
ATOM   17614 O  O     . ALA A 1 3949 ? 209.115 127.918 158.494 1.00 66.99  ? 3949 ALA A O     1 
ATOM   17615 C  CB    . ALA A 1 3949 ? 209.858 127.768 161.679 1.00 65.35  ? 3949 ALA A CB    1 
ATOM   17616 N  N     . LYS A 1 3950 ? 207.290 127.642 159.781 1.00 56.19  ? 3950 LYS A N     1 
ATOM   17617 C  CA    . LYS A 1 3950 ? 206.545 126.994 158.706 1.00 59.84  ? 3950 LYS A CA    1 
ATOM   17618 C  C     . LYS A 1 3950 ? 206.264 127.962 157.563 1.00 65.01  ? 3950 LYS A C     1 
ATOM   17619 O  O     . LYS A 1 3950 ? 206.336 127.581 156.389 1.00 61.51  ? 3950 LYS A O     1 
ATOM   17620 C  CB    . LYS A 1 3950 ? 205.242 126.409 159.249 1.00 54.64  ? 3950 LYS A CB    1 
ATOM   17621 C  CG    . LYS A 1 3950 ? 205.363 124.974 159.732 1.00 54.58  ? 3950 LYS A CG    1 
ATOM   17622 C  CD    . LYS A 1 3950 ? 203.999 124.318 159.847 1.00 48.01  ? 3950 LYS A CD    1 
ATOM   17623 C  CE    . LYS A 1 3950 ? 204.104 122.928 160.451 1.00 47.85  ? 3950 LYS A CE    1 
ATOM   17624 N  NZ    . LYS A 1 3950 ? 204.603 122.970 161.852 1.00 52.54  ? 3950 LYS A NZ    1 
ATOM   17625 N  N     . VAL A 1 3951 ? 205.931 129.213 157.887 1.00 61.04  ? 3951 VAL A N     1 
ATOM   17626 C  CA    . VAL A 1 3951 ? 205.690 130.212 156.851 1.00 55.10  ? 3951 VAL A CA    1 
ATOM   17627 C  C     . VAL A 1 3951 ? 206.970 130.500 156.076 1.00 64.08  ? 3951 VAL A C     1 
ATOM   17628 O  O     . VAL A 1 3951 ? 206.954 130.606 154.843 1.00 66.26  ? 3951 VAL A O     1 
ATOM   17629 C  CB    . VAL A 1 3951 ? 205.096 131.490 157.471 1.00 56.54  ? 3951 VAL A CB    1 
ATOM   17630 C  CG1   . VAL A 1 3951 ? 205.259 132.674 156.528 1.00 49.88  ? 3951 VAL A CG1   1 
ATOM   17631 C  CG2   . VAL A 1 3951 ? 203.631 131.278 157.812 1.00 54.54  ? 3951 VAL A CG2   1 
ATOM   17632 N  N     . GLN A 1 3952 ? 208.099 130.630 156.779 1.00 64.45  ? 3952 GLN A N     1 
ATOM   17633 C  CA    . GLN A 1 3952 ? 209.366 130.868 156.091 1.00 63.05  ? 3952 GLN A CA    1 
ATOM   17634 C  C     . GLN A 1 3952 ? 209.754 129.687 155.210 1.00 60.73  ? 3952 GLN A C     1 
ATOM   17635 O  O     . GLN A 1 3952 ? 210.277 129.873 154.106 1.00 64.14  ? 3952 GLN A O     1 
ATOM   17636 C  CB    . GLN A 1 3952 ? 210.476 131.163 157.100 1.00 63.92  ? 3952 GLN A CB    1 
ATOM   17637 C  CG    . GLN A 1 3952 ? 210.363 132.509 157.794 1.00 65.05  ? 3952 GLN A CG    1 
ATOM   17638 C  CD    . GLN A 1 3952 ? 211.155 132.562 159.086 1.00 71.45  ? 3952 GLN A CD    1 
ATOM   17639 O  OE1   . GLN A 1 3952 ? 211.906 131.641 159.404 1.00 74.34  ? 3952 GLN A OE1   1 
ATOM   17640 N  NE2   . GLN A 1 3952 ? 211.007 133.653 159.827 1.00 70.84  ? 3952 GLN A NE2   1 
ATOM   17641 N  N     . ALA A 1 3953 ? 209.515 128.463 155.686 1.00 62.80  ? 3953 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3953 ? 209.937 127.278 154.944 1.00 70.42  ? 3953 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3953 ? 209.196 127.149 153.619 1.00 74.20  ? 3953 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3953 ? 209.795 126.783 152.601 1.00 79.14  ? 3953 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3953 ? 209.730 126.027 155.797 1.00 63.27  ? 3953 ALA A CB    1 
ATOM   17646 N  N     . ASP A 1 3954 ? 207.898 127.437 153.610 1.00 75.30  ? 3954 ASP A N     1 
ATOM   17647 C  CA    . ASP A 1 3954 ? 207.094 127.250 152.410 1.00 78.10  ? 3954 ASP A CA    1 
ATOM   17648 C  C     . ASP A 1 3954 ? 207.439 128.297 151.358 1.00 76.71  ? 3954 ASP A C     1 
ATOM   17649 O  O     . ASP A 1 3954 ? 207.506 129.494 151.652 1.00 72.52  ? 3954 ASP A O     1 
ATOM   17650 C  CB    . ASP A 1 3954 ? 205.607 127.317 152.756 1.00 74.45  ? 3954 ASP A CB    1 
ATOM   17651 C  CG    . ASP A 1 3954 ? 204.722 126.817 151.629 1.00 74.99  ? 3954 ASP A CG    1 
ATOM   17652 O  OD1   . ASP A 1 3954 ? 205.258 126.263 150.646 1.00 75.27  ? 3954 ASP A OD1   1 
ATOM   17653 O  OD2   . ASP A 1 3954 ? 203.487 126.978 151.726 1.00 69.22  ? 3954 ASP A OD2   1 
ATOM   17654 N  N     . GLU A 1 3955 ? 207.658 127.839 150.125 1.00 80.36  ? 3955 GLU A N     1 
ATOM   17655 C  CA    . GLU A 1 3955 ? 207.858 128.729 148.991 1.00 88.02  ? 3955 GLU A CA    1 
ATOM   17656 C  C     . GLU A 1 3955 ? 206.578 128.995 148.212 1.00 83.46  ? 3955 GLU A C     1 
ATOM   17657 O  O     . GLU A 1 3955 ? 206.531 129.953 147.433 1.00 81.53  ? 3955 GLU A O     1 
ATOM   17658 C  CB    . GLU A 1 3955 ? 208.915 128.152 148.039 1.00 88.70  ? 3955 GLU A CB    1 
ATOM   17659 C  CG    . GLU A 1 3955 ? 208.523 126.824 147.408 1.00 86.09  ? 3955 GLU A CG    1 
ATOM   17660 C  CD    . GLU A 1 3955 ? 208.925 125.632 148.255 1.00 85.74  ? 3955 GLU A CD    1 
ATOM   17661 O  OE1   . GLU A 1 3955 ? 209.534 125.840 149.326 1.00 85.10  ? 3955 GLU A OE1   1 
ATOM   17662 O  OE2   . GLU A 1 3955 ? 208.633 124.488 147.850 1.00 83.62  ? 3955 GLU A OE2   1 
ATOM   17663 N  N     . GLN A 1 3956 ? 205.550 128.172 148.404 1.00 79.48  ? 3956 GLN A N     1 
ATOM   17664 C  CA    . GLN A 1 3956 ? 204.247 128.362 147.783 1.00 73.28  ? 3956 GLN A CA    1 
ATOM   17665 C  C     . GLN A 1 3956 ? 203.335 129.266 148.603 1.00 68.94  ? 3956 GLN A C     1 
ATOM   17666 O  O     . GLN A 1 3956 ? 202.199 129.520 148.190 1.00 68.48  ? 3956 GLN A O     1 
ATOM   17667 C  CB    . GLN A 1 3956 ? 203.573 127.001 147.568 1.00 76.73  ? 3956 GLN A CB    1 
ATOM   17668 C  CG    . GLN A 1 3956 ? 202.610 126.945 146.399 1.00 75.88  ? 3956 GLN A CG    1 
ATOM   17669 C  CD    . GLN A 1 3956 ? 202.559 125.576 145.751 1.00 89.86  ? 3956 GLN A CD    1 
ATOM   17670 O  OE1   . GLN A 1 3956 ? 202.790 124.559 146.405 1.00 95.89  ? 3956 GLN A OE1   1 
ATOM   17671 N  NE2   . GLN A 1 3956 ? 202.255 125.543 144.459 1.00 91.02  ? 3956 GLN A NE2   1 
ATOM   17672 N  N     . PHE A 1 3957 ? 203.804 129.749 149.755 1.00 68.00  ? 3957 PHE A N     1 
ATOM   17673 C  CA    . PHE A 1 3957 ? 202.968 130.575 150.619 1.00 60.18  ? 3957 PHE A CA    1 
ATOM   17674 C  C     . PHE A 1 3957 ? 202.670 131.931 149.990 1.00 53.49  ? 3957 PHE A C     1 
ATOM   17675 O  O     . PHE A 1 3957 ? 201.614 132.520 150.254 1.00 52.54  ? 3957 PHE A O     1 
ATOM   17676 C  CB    . PHE A 1 3957 ? 203.655 130.748 151.975 1.00 53.86  ? 3957 PHE A CB    1 
ATOM   17677 C  CG    . PHE A 1 3957 ? 202.853 131.531 152.971 1.00 49.44  ? 3957 PHE A CG    1 
ATOM   17678 C  CD1   . PHE A 1 3957 ? 201.779 130.951 153.623 1.00 46.75  ? 3957 PHE A CD1   1 
ATOM   17679 C  CD2   . PHE A 1 3957 ? 203.182 132.842 153.267 1.00 42.58  ? 3957 PHE A CD2   1 
ATOM   17680 C  CE1   . PHE A 1 3957 ? 201.043 131.666 154.546 1.00 43.01  ? 3957 PHE A CE1   1 
ATOM   17681 C  CE2   . PHE A 1 3957 ? 202.449 133.562 154.187 1.00 43.57  ? 3957 PHE A CE2   1 
ATOM   17682 C  CZ    . PHE A 1 3957 ? 201.379 132.973 154.828 1.00 44.77  ? 3957 PHE A CZ    1 
ATOM   17683 N  N     . GLY A 1 3958 ? 203.582 132.438 149.158 1.00 51.24  ? 3958 GLY A N     1 
ATOM   17684 C  CA    . GLY A 1 3958 ? 203.397 133.763 148.588 1.00 45.55  ? 3958 GLY A CA    1 
ATOM   17685 C  C     . GLY A 1 3958 ? 202.194 133.854 147.669 1.00 47.84  ? 3958 GLY A C     1 
ATOM   17686 O  O     . GLY A 1 3958 ? 201.420 134.812 147.739 1.00 48.92  ? 3958 GLY A O     1 
ATOM   17687 N  N     . ILE A 1 3959 ? 202.021 132.863 146.792 1.00 48.29  ? 3959 ILE A N     1 
ATOM   17688 C  CA    . ILE A 1 3959 ? 200.884 132.885 145.876 1.00 47.88  ? 3959 ILE A CA    1 
ATOM   17689 C  C     . ILE A 1 3959 ? 199.581 132.676 146.638 1.00 47.68  ? 3959 ILE A C     1 
ATOM   17690 O  O     . ILE A 1 3959 ? 198.530 133.204 146.254 1.00 43.09  ? 3959 ILE A O     1 
ATOM   17691 C  CB    . ILE A 1 3959 ? 201.066 131.845 144.753 1.00 46.68  ? 3959 ILE A CB    1 
ATOM   17692 C  CG1   . ILE A 1 3959 ? 201.132 130.427 145.319 1.00 51.60  ? 3959 ILE A CG1   1 
ATOM   17693 C  CG2   . ILE A 1 3959 ? 202.313 132.152 143.939 1.00 51.54  ? 3959 ILE A CG2   1 
ATOM   17694 C  CD1   . ILE A 1 3959 ? 201.076 129.355 144.254 1.00 67.74  ? 3959 ILE A CD1   1 
ATOM   17695 N  N     . TRP A 1 3960 ? 199.624 131.898 147.722 1.00 46.12  ? 3960 TRP A N     1 
ATOM   17696 C  CA    . TRP A 1 3960 ? 198.430 131.712 148.538 1.00 37.14  ? 3960 TRP A CA    1 
ATOM   17697 C  C     . TRP A 1 3960 ? 198.036 133.001 149.247 1.00 35.57  ? 3960 TRP A C     1 
ATOM   17698 O  O     . TRP A 1 3960 ? 196.844 133.303 149.377 1.00 38.28  ? 3960 TRP A O     1 
ATOM   17699 C  CB    . TRP A 1 3960 ? 198.646 130.597 149.558 1.00 32.32  ? 3960 TRP A CB    1 
ATOM   17700 C  CG    . TRP A 1 3960 ? 197.478 130.439 150.476 1.00 28.92  ? 3960 TRP A CG    1 
ATOM   17701 C  CD1   . TRP A 1 3960 ? 196.335 129.741 150.228 1.00 29.48  ? 3960 TRP A CD1   1 
ATOM   17702 C  CD2   . TRP A 1 3960 ? 197.321 131.017 151.776 1.00 29.12  ? 3960 TRP A CD2   1 
ATOM   17703 N  NE1   . TRP A 1 3960 ? 195.482 129.833 151.299 1.00 27.74  ? 3960 TRP A NE1   1 
ATOM   17704 C  CE2   . TRP A 1 3960 ? 196.063 130.615 152.262 1.00 23.88  ? 3960 TRP A CE2   1 
ATOM   17705 C  CE3   . TRP A 1 3960 ? 198.125 131.832 152.578 1.00 34.61  ? 3960 TRP A CE3   1 
ATOM   17706 C  CZ2   . TRP A 1 3960 ? 195.591 130.996 153.513 1.00 25.65  ? 3960 TRP A CZ2   1 
ATOM   17707 C  CZ3   . TRP A 1 3960 ? 197.654 132.210 153.818 1.00 30.16  ? 3960 TRP A CZ3   1 
ATOM   17708 C  CH2   . TRP A 1 3960 ? 196.399 131.792 154.274 1.00 30.81  ? 3960 TRP A CH2   1 
ATOM   17709 N  N     . LEU A 1 3961 ? 199.021 133.764 149.726 1.00 33.83  ? 3961 LEU A N     1 
ATOM   17710 C  CA    . LEU A 1 3961 ? 198.713 135.006 150.428 1.00 40.38  ? 3961 LEU A CA    1 
ATOM   17711 C  C     . LEU A 1 3961 ? 198.012 136.002 149.513 1.00 41.23  ? 3961 LEU A C     1 
ATOM   17712 O  O     . LEU A 1 3961 ? 197.120 136.737 149.951 1.00 39.75  ? 3961 LEU A O     1 
ATOM   17713 C  CB    . LEU A 1 3961 ? 199.989 135.614 151.009 1.00 41.00  ? 3961 LEU A CB    1 
ATOM   17714 C  CG    . LEU A 1 3961 ? 199.791 136.533 152.215 1.00 40.79  ? 3961 LEU A CG    1 
ATOM   17715 C  CD1   . LEU A 1 3961 ? 199.603 135.726 153.486 1.00 39.32  ? 3961 LEU A CD1   1 
ATOM   17716 C  CD2   . LEU A 1 3961 ? 200.964 137.491 152.355 1.00 46.08  ? 3961 LEU A CD2   1 
ATOM   17717 N  N     . ASP A 1 3962 ? 198.399 136.043 148.241 1.00 41.71  ? 3962 ASP A N     1 
ATOM   17718 C  CA    . ASP A 1 3962 ? 197.784 136.932 147.265 1.00 44.17  ? 3962 ASP A CA    1 
ATOM   17719 C  C     . ASP A 1 3962 ? 196.713 136.238 146.433 1.00 40.03  ? 3962 ASP A C     1 
ATOM   17720 O  O     . ASP A 1 3962 ? 196.270 136.795 145.424 1.00 41.28  ? 3962 ASP A O     1 
ATOM   17721 C  CB    . ASP A 1 3962 ? 198.853 137.533 146.351 1.00 54.26  ? 3962 ASP A CB    1 
ATOM   17722 C  CG    . ASP A 1 3962 ? 199.758 138.508 147.078 1.00 64.97  ? 3962 ASP A CG    1 
ATOM   17723 O  OD1   . ASP A 1 3962 ? 199.293 139.141 148.049 1.00 60.18  ? 3962 ASP A OD1   1 
ATOM   17724 O  OD2   . ASP A 1 3962 ? 200.933 138.644 146.678 1.00 77.47  ? 3962 ASP A OD2   1 
ATOM   17725 N  N     . SER A 1 3963 ? 196.294 135.040 146.830 1.00 41.11  ? 3963 SER A N     1 
ATOM   17726 C  CA    . SER A 1 3963 ? 195.253 134.324 146.108 1.00 34.63  ? 3963 SER A CA    1 
ATOM   17727 C  C     . SER A 1 3963 ? 193.917 135.049 146.226 1.00 35.57  ? 3963 SER A C     1 
ATOM   17728 O  O     . SER A 1 3963 ? 193.627 135.707 147.228 1.00 33.17  ? 3963 SER A O     1 
ATOM   17729 C  CB    . SER A 1 3963 ? 195.121 132.897 146.639 1.00 33.02  ? 3963 SER A CB    1 
ATOM   17730 O  OG    . SER A 1 3963 ? 194.089 132.195 145.968 1.00 38.15  ? 3963 SER A OG    1 
ATOM   17731 N  N     . SER A 1 3964 ? 193.101 134.925 145.177 1.00 36.55  ? 3964 SER A N     1 
ATOM   17732 C  CA    . SER A 1 3964 ? 191.798 135.582 145.170 1.00 33.44  ? 3964 SER A CA    1 
ATOM   17733 C  C     . SER A 1 3964 ? 190.883 135.014 146.248 1.00 34.14  ? 3964 SER A C     1 
ATOM   17734 O  O     . SER A 1 3964 ? 190.186 135.764 146.940 1.00 35.48  ? 3964 SER A O     1 
ATOM   17735 C  CB    . SER A 1 3964 ? 191.152 135.448 143.792 1.00 35.19  ? 3964 SER A CB    1 
ATOM   17736 O  OG    . SER A 1 3964 ? 190.845 134.096 143.505 1.00 36.95  ? 3964 SER A OG    1 
ATOM   17737 N  N     . SER A 1 3965 ? 190.873 133.692 146.406 1.00 37.24  ? 3965 SER A N     1 
ATOM   17738 C  CA    . SER A 1 3965 ? 190.049 133.012 147.405 1.00 31.98  ? 3965 SER A CA    1 
ATOM   17739 C  C     . SER A 1 3965 ? 190.935 132.057 148.193 1.00 30.11  ? 3965 SER A C     1 
ATOM   17740 O  O     . SER A 1 3965 ? 190.878 130.835 148.002 1.00 32.98  ? 3965 SER A O     1 
ATOM   17741 C  CB    . SER A 1 3965 ? 188.883 132.275 146.747 1.00 31.22  ? 3965 SER A CB    1 
ATOM   17742 O  OG    . SER A 1 3965 ? 189.350 131.212 145.936 1.00 43.17  ? 3965 SER A OG    1 
ATOM   17743 N  N     . PRO A 1 3966 ? 191.772 132.584 149.091 1.00 26.82  ? 3966 PRO A N     1 
ATOM   17744 C  CA    . PRO A 1 3966 ? 192.693 131.712 149.839 1.00 25.68  ? 3966 PRO A CA    1 
ATOM   17745 C  C     . PRO A 1 3966 ? 191.997 130.711 150.742 1.00 23.88  ? 3966 PRO A C     1 
ATOM   17746 O  O     . PRO A 1 3966 ? 192.594 129.679 151.070 1.00 28.12  ? 3966 PRO A O     1 
ATOM   17747 C  CB    . PRO A 1 3966 ? 193.531 132.709 150.651 1.00 24.80  ? 3966 PRO A CB    1 
ATOM   17748 C  CG    . PRO A 1 3966 ? 192.647 133.895 150.802 1.00 22.24  ? 3966 PRO A CG    1 
ATOM   17749 C  CD    . PRO A 1 3966 ? 191.870 133.988 149.523 1.00 25.53  ? 3966 PRO A CD    1 
ATOM   17750 N  N     . GLU A 1 3967 ? 190.758 130.980 151.157 1.00 28.38  ? 3967 GLU A N     1 
ATOM   17751 C  CA    . GLU A 1 3967 ? 190.049 130.075 152.054 1.00 24.24  ? 3967 GLU A CA    1 
ATOM   17752 C  C     . GLU A 1 3967 ? 189.703 128.747 151.392 1.00 25.92  ? 3967 GLU A C     1 
ATOM   17753 O  O     . GLU A 1 3967 ? 189.426 127.773 152.099 1.00 30.14  ? 3967 GLU A O     1 
ATOM   17754 C  CB    . GLU A 1 3967 ? 188.780 130.750 152.575 1.00 23.10  ? 3967 GLU A CB    1 
ATOM   17755 C  CG    . GLU A 1 3967 ? 187.553 130.528 151.707 1.00 24.68  ? 3967 GLU A CG    1 
ATOM   17756 C  CD    . GLU A 1 3967 ? 187.307 131.673 150.745 1.00 27.68  ? 3967 GLU A CD    1 
ATOM   17757 O  OE1   . GLU A 1 3967 ? 188.129 132.611 150.714 1.00 27.75  ? 3967 GLU A OE1   1 
ATOM   17758 O  OE2   . GLU A 1 3967 ? 186.292 131.635 150.020 1.00 33.78  ? 3967 GLU A OE2   1 
ATOM   17759 N  N     . GLN A 1 3968 ? 189.704 128.688 150.058 1.00 29.94  ? 3968 GLN A N     1 
ATOM   17760 C  CA    . GLN A 1 3968 ? 189.398 127.436 149.373 1.00 27.75  ? 3968 GLN A CA    1 
ATOM   17761 C  C     . GLN A 1 3968 ? 190.460 126.379 149.648 1.00 30.45  ? 3968 GLN A C     1 
ATOM   17762 O  O     . GLN A 1 3968 ? 190.133 125.211 149.887 1.00 39.38  ? 3968 GLN A O     1 
ATOM   17763 C  CB    . GLN A 1 3968 ? 189.266 127.680 147.871 1.00 33.07  ? 3968 GLN A CB    1 
ATOM   17764 C  CG    . GLN A 1 3968 ? 188.162 128.651 147.493 1.00 37.02  ? 3968 GLN A CG    1 
ATOM   17765 C  CD    . GLN A 1 3968 ? 186.780 128.105 147.776 1.00 35.74  ? 3968 GLN A CD    1 
ATOM   17766 O  OE1   . GLN A 1 3968 ? 186.102 128.550 148.701 1.00 37.43  ? 3968 GLN A OE1   1 
ATOM   17767 N  NE2   . GLN A 1 3968 ? 186.351 127.139 146.974 1.00 38.70  ? 3968 GLN A NE2   1 
ATOM   17768 N  N     . THR A 1 3969 ? 191.735 126.766 149.613 1.00 31.38  ? 3969 THR A N     1 
ATOM   17769 C  CA    . THR A 1 3969 ? 192.860 125.853 149.824 1.00 33.41  ? 3969 THR A CA    1 
ATOM   17770 C  C     . THR A 1 3969 ? 193.822 126.509 150.810 1.00 31.48  ? 3969 THR A C     1 
ATOM   17771 O  O     . THR A 1 3969 ? 194.749 127.215 150.407 1.00 32.43  ? 3969 THR A O     1 
ATOM   17772 C  CB    . THR A 1 3969 ? 193.558 125.517 148.505 1.00 36.93  ? 3969 THR A CB    1 
ATOM   17773 O  OG1   . THR A 1 3969 ? 194.083 126.716 147.921 1.00 33.40  ? 3969 THR A OG1   1 
ATOM   17774 C  CG2   . THR A 1 3969 ? 192.593 124.859 147.529 1.00 33.79  ? 3969 THR A CG2   1 
ATOM   17775 N  N     . VAL A 1 3970 ? 193.605 126.268 152.099 1.00 28.97  ? 3970 VAL A N     1 
ATOM   17776 C  CA    . VAL A 1 3970 ? 194.469 126.806 153.147 1.00 31.28  ? 3970 VAL A CA    1 
ATOM   17777 C  C     . VAL A 1 3970 ? 195.586 125.806 153.425 1.00 36.43  ? 3970 VAL A C     1 
ATOM   17778 O  O     . VAL A 1 3970 ? 195.308 124.621 153.661 1.00 40.88  ? 3970 VAL A O     1 
ATOM   17779 C  CB    . VAL A 1 3970 ? 193.671 127.120 154.422 1.00 27.54  ? 3970 VAL A CB    1 
ATOM   17780 C  CG1   . VAL A 1 3970 ? 194.549 127.832 155.436 1.00 25.90  ? 3970 VAL A CG1   1 
ATOM   17781 C  CG2   . VAL A 1 3970 ? 192.451 127.960 154.088 1.00 24.54  ? 3970 VAL A CG2   1 
ATOM   17782 N  N     . PRO A 1 3971 ? 196.851 126.224 153.395 1.00 32.01  ? 3971 PRO A N     1 
ATOM   17783 C  CA    . PRO A 1 3971 ? 197.945 125.277 153.639 1.00 36.00  ? 3971 PRO A CA    1 
ATOM   17784 C  C     . PRO A 1 3971 ? 197.899 124.713 155.051 1.00 42.61  ? 3971 PRO A C     1 
ATOM   17785 O  O     . PRO A 1 3971 ? 197.444 125.365 155.994 1.00 45.00  ? 3971 PRO A O     1 
ATOM   17786 C  CB    . PRO A 1 3971 ? 199.204 126.122 153.413 1.00 35.42  ? 3971 PRO A CB    1 
ATOM   17787 C  CG    . PRO A 1 3971 ? 198.759 127.531 153.629 1.00 33.43  ? 3971 PRO A CG    1 
ATOM   17788 C  CD    . PRO A 1 3971 ? 197.347 127.585 153.131 1.00 32.70  ? 3971 PRO A CD    1 
ATOM   17789 N  N     . TYR A 1 3972 ? 198.384 123.478 155.186 1.00 43.86  ? 3972 TYR A N     1 
ATOM   17790 C  CA    . TYR A 1 3972 ? 198.386 122.763 156.463 1.00 43.31  ? 3972 TYR A CA    1 
ATOM   17791 C  C     . TYR A 1 3972 ? 199.513 123.314 157.340 1.00 41.67  ? 3972 TYR A C     1 
ATOM   17792 O  O     . TYR A 1 3972 ? 200.545 122.682 157.576 1.00 50.80  ? 3972 TYR A O     1 
ATOM   17793 C  CB    . TYR A 1 3972 ? 198.519 121.265 156.221 1.00 44.71  ? 3972 TYR A CB    1 
ATOM   17794 C  CG    . TYR A 1 3972 ? 198.492 120.406 157.466 1.00 54.26  ? 3972 TYR A CG    1 
ATOM   17795 C  CD1   . TYR A 1 3972 ? 197.301 120.155 158.134 1.00 50.54  ? 3972 TYR A CD1   1 
ATOM   17796 C  CD2   . TYR A 1 3972 ? 199.653 119.819 157.955 1.00 61.47  ? 3972 TYR A CD2   1 
ATOM   17797 C  CE1   . TYR A 1 3972 ? 197.271 119.363 159.266 1.00 57.34  ? 3972 TYR A CE1   1 
ATOM   17798 C  CE2   . TYR A 1 3972 ? 199.633 119.028 159.085 1.00 62.93  ? 3972 TYR A CE2   1 
ATOM   17799 C  CZ    . TYR A 1 3972 ? 198.440 118.802 159.736 1.00 66.19  ? 3972 TYR A CZ    1 
ATOM   17800 O  OH    . TYR A 1 3972 ? 198.419 118.011 160.862 1.00 76.92  ? 3972 TYR A OH    1 
ATOM   17801 N  N     . LEU A 1 3973 ? 199.301 124.537 157.815 1.00 39.89  ? 3973 LEU A N     1 
ATOM   17802 C  CA    . LEU A 1 3973 ? 200.298 125.257 158.608 1.00 41.94  ? 3973 LEU A CA    1 
ATOM   17803 C  C     . LEU A 1 3973 ? 200.076 125.087 160.108 1.00 45.21  ? 3973 LEU A C     1 
ATOM   17804 O  O     . LEU A 1 3973 ? 200.013 126.063 160.853 1.00 49.85  ? 3973 LEU A O     1 
ATOM   17805 C  CB    . LEU A 1 3973 ? 200.292 126.731 158.223 1.00 42.60  ? 3973 LEU A CB    1 
ATOM   17806 C  CG    . LEU A 1 3973 ? 200.886 127.097 156.864 1.00 40.15  ? 3973 LEU A CG    1 
ATOM   17807 C  CD1   . LEU A 1 3973 ? 201.109 128.595 156.775 1.00 42.47  ? 3973 LEU A CD1   1 
ATOM   17808 C  CD2   . LEU A 1 3973 ? 202.186 126.344 156.629 1.00 40.18  ? 3973 LEU A CD2   1 
ATOM   17809 N  N     . TRP A 1 3974 ? 199.961 123.844 160.569 1.00 46.28  ? 3974 TRP A N     1 
ATOM   17810 C  CA    . TRP A 1 3974 ? 199.861 123.584 161.999 1.00 53.89  ? 3974 TRP A CA    1 
ATOM   17811 C  C     . TRP A 1 3974 ? 200.283 122.148 162.267 1.00 59.57  ? 3974 TRP A C     1 
ATOM   17812 O  O     . TRP A 1 3974 ? 200.273 121.300 161.371 1.00 59.34  ? 3974 TRP A O     1 
ATOM   17813 C  CB    . TRP A 1 3974 ? 198.447 123.851 162.534 1.00 49.44  ? 3974 TRP A CB    1 
ATOM   17814 C  CG    . TRP A 1 3974 ? 197.389 122.919 162.023 1.00 56.07  ? 3974 TRP A CG    1 
ATOM   17815 C  CD1   . TRP A 1 3974 ? 197.069 121.690 162.522 1.00 55.94  ? 3974 TRP A CD1   1 
ATOM   17816 C  CD2   . TRP A 1 3974 ? 196.498 123.149 160.926 1.00 51.20  ? 3974 TRP A CD2   1 
ATOM   17817 N  NE1   . TRP A 1 3974 ? 196.042 121.138 161.800 1.00 51.59  ? 3974 TRP A NE1   1 
ATOM   17818 C  CE2   . TRP A 1 3974 ? 195.672 122.014 160.814 1.00 49.78  ? 3974 TRP A CE2   1 
ATOM   17819 C  CE3   . TRP A 1 3974 ? 196.321 124.203 160.025 1.00 39.46  ? 3974 TRP A CE3   1 
ATOM   17820 C  CZ2   . TRP A 1 3974 ? 194.686 121.903 159.838 1.00 44.11  ? 3974 TRP A CZ2   1 
ATOM   17821 C  CZ3   . TRP A 1 3974 ? 195.343 124.090 159.058 1.00 40.42  ? 3974 TRP A CZ3   1 
ATOM   17822 C  CH2   . TRP A 1 3974 ? 194.537 122.949 158.972 1.00 46.04  ? 3974 TRP A CH2   1 
ATOM   17823 N  N     . SER A 1 3975 ? 200.651 121.889 163.517 1.00 61.34  ? 3975 SER A N     1 
ATOM   17824 C  CA    . SER A 1 3975 ? 201.168 120.595 163.939 1.00 64.67  ? 3975 SER A CA    1 
ATOM   17825 C  C     . SER A 1 3975 ? 200.159 119.910 164.848 1.00 66.38  ? 3975 SER A C     1 
ATOM   17826 O  O     . SER A 1 3975 ? 199.739 120.481 165.860 1.00 67.13  ? 3975 SER A O     1 
ATOM   17827 C  CB    . SER A 1 3975 ? 202.507 120.753 164.661 1.00 69.37  ? 3975 SER A CB    1 
ATOM   17828 O  OG    . SER A 1 3975 ? 202.391 121.649 165.753 1.00 67.47  ? 3975 SER A OG    1 
ATOM   17829 N  N     . GLU A 1 3976 ? 199.778 118.687 164.487 1.00 70.23  ? 3976 GLU A N     1 
ATOM   17830 C  CA    . GLU A 1 3976 ? 198.839 117.890 165.264 1.00 79.48  ? 3976 GLU A CA    1 
ATOM   17831 C  C     . GLU A 1 3976 ? 199.419 116.501 165.470 1.00 84.93  ? 3976 GLU A C     1 
ATOM   17832 O  O     . GLU A 1 3976 ? 199.902 115.880 164.518 1.00 84.08  ? 3976 GLU A O     1 
ATOM   17833 C  CB    . GLU A 1 3976 ? 197.477 117.799 164.566 1.00 80.21  ? 3976 GLU A CB    1 
ATOM   17834 C  CG    . GLU A 1 3976 ? 196.605 119.033 164.731 1.00 80.98  ? 3976 GLU A CG    1 
ATOM   17835 C  CD    . GLU A 1 3976 ? 195.706 118.954 165.950 1.00 83.55  ? 3976 GLU A CD    1 
ATOM   17836 O  OE1   . GLU A 1 3976 ? 195.981 118.122 166.841 1.00 86.12  ? 3976 GLU A OE1   1 
ATOM   17837 O  OE2   . GLU A 1 3976 ? 194.725 119.724 166.017 1.00 76.54  ? 3976 GLU A OE2   1 
ATOM   17838 N  N     . GLU A 1 3977 ? 199.378 116.020 166.714 1.00 86.44  ? 3977 GLU A N     1 
ATOM   17839 C  CA    . GLU A 1 3977 ? 199.840 114.664 166.994 1.00 89.23  ? 3977 GLU A CA    1 
ATOM   17840 C  C     . GLU A 1 3977 ? 198.964 113.630 166.298 1.00 87.53  ? 3977 GLU A C     1 
ATOM   17841 O  O     . GLU A 1 3977 ? 199.471 112.655 165.731 1.00 87.76  ? 3977 GLU A O     1 
ATOM   17842 C  CB    . GLU A 1 3977 ? 199.864 114.423 168.504 1.00 83.84  ? 3977 GLU A CB    1 
ATOM   17843 C  CG    . GLU A 1 3977 ? 201.151 114.872 169.177 1.00 89.70  ? 3977 GLU A CG    1 
ATOM   17844 C  CD    . GLU A 1 3977 ? 201.232 116.377 169.340 1.00 92.52  ? 3977 GLU A CD    1 
ATOM   17845 O  OE1   . GLU A 1 3977 ? 200.201 117.057 169.150 1.00 89.28  ? 3977 GLU A OE1   1 
ATOM   17846 O  OE2   . GLU A 1 3977 ? 202.330 116.882 169.658 1.00 91.06  ? 3977 GLU A OE2   1 
ATOM   17847 N  N     . THR A 1 3978 ? 197.648 113.827 166.329 1.00 84.14  ? 3978 THR A N     1 
ATOM   17848 C  CA    . THR A 1 3978 ? 196.701 112.955 165.660 1.00 84.07  ? 3978 THR A CA    1 
ATOM   17849 C  C     . THR A 1 3978 ? 195.983 113.723 164.557 1.00 85.03  ? 3978 THR A C     1 
ATOM   17850 O  O     . THR A 1 3978 ? 195.829 114.945 164.651 1.00 85.44  ? 3978 THR A O     1 
ATOM   17851 C  CB    . THR A 1 3978 ? 195.666 112.392 166.643 1.00 82.06  ? 3978 THR A CB    1 
ATOM   17852 O  OG1   . THR A 1 3978 ? 194.919 113.469 167.223 1.00 86.67  ? 3978 THR A OG1   1 
ATOM   17853 C  CG2   . THR A 1 3978 ? 196.353 111.605 167.748 1.00 75.97  ? 3978 THR A CG2   1 
ATOM   17854 N  N     . PRO A 1 3979 ? 195.551 113.043 163.494 1.00 77.24  ? 3979 PRO A N     1 
ATOM   17855 C  CA    . PRO A 1 3979 ? 194.824 113.741 162.427 1.00 66.92  ? 3979 PRO A CA    1 
ATOM   17856 C  C     . PRO A 1 3979 ? 193.566 114.405 162.964 1.00 70.86  ? 3979 PRO A C     1 
ATOM   17857 O  O     . PRO A 1 3979 ? 192.855 113.850 163.803 1.00 73.77  ? 3979 PRO A O     1 
ATOM   17858 C  CB    . PRO A 1 3979 ? 194.494 112.623 161.432 1.00 70.93  ? 3979 PRO A CB    1 
ATOM   17859 C  CG    . PRO A 1 3979 ? 195.521 111.573 161.692 1.00 72.17  ? 3979 PRO A CG    1 
ATOM   17860 C  CD    . PRO A 1 3979 ? 195.796 111.629 163.163 1.00 71.50  ? 3979 PRO A CD    1 
ATOM   17861 N  N     . ALA A 1 3980 ? 193.296 115.607 162.467 1.00 71.56  ? 3980 ALA A N     1 
ATOM   17862 C  CA    . ALA A 1 3980 ? 192.187 116.409 162.955 1.00 62.18  ? 3980 ALA A CA    1 
ATOM   17863 C  C     . ALA A 1 3980 ? 190.902 116.074 162.208 1.00 55.84  ? 3980 ALA A C     1 
ATOM   17864 O  O     . ALA A 1 3980 ? 190.921 115.675 161.041 1.00 53.71  ? 3980 ALA A O     1 
ATOM   17865 C  CB    . ALA A 1 3980 ? 192.495 117.900 162.817 1.00 53.33  ? 3980 ALA A CB    1 
ATOM   17866 N  N     . THR A 1 3981 ? 189.781 116.239 162.904 1.00 50.89  ? 3981 THR A N     1 
ATOM   17867 C  CA    . THR A 1 3981 ? 188.479 116.054 162.297 1.00 43.56  ? 3981 THR A CA    1 
ATOM   17868 C  C     . THR A 1 3981 ? 188.201 117.179 161.303 1.00 40.96  ? 3981 THR A C     1 
ATOM   17869 O  O     . THR A 1 3981 ? 188.818 118.244 161.373 1.00 41.62  ? 3981 THR A O     1 
ATOM   17870 C  CB    . THR A 1 3981 ? 187.397 116.016 163.374 1.00 46.54  ? 3981 THR A CB    1 
ATOM   17871 O  OG1   . THR A 1 3981 ? 187.381 117.261 164.083 1.00 46.91  ? 3981 THR A OG1   1 
ATOM   17872 C  CG2   . THR A 1 3981 ? 187.662 114.884 164.352 1.00 48.97  ? 3981 THR A CG2   1 
ATOM   17873 N  N     . PRO A 1 3982 ? 187.286 116.960 160.353 1.00 42.91  ? 3982 PRO A N     1 
ATOM   17874 C  CA    . PRO A 1 3982 ? 186.960 118.034 159.400 1.00 39.29  ? 3982 PRO A CA    1 
ATOM   17875 C  C     . PRO A 1 3982 ? 186.493 119.314 160.069 1.00 31.82  ? 3982 PRO A C     1 
ATOM   17876 O  O     . PRO A 1 3982 ? 186.803 120.405 159.577 1.00 29.74  ? 3982 PRO A O     1 
ATOM   17877 C  CB    . PRO A 1 3982 ? 185.855 117.413 158.530 1.00 33.70  ? 3982 PRO A CB    1 
ATOM   17878 C  CG    . PRO A 1 3982 ? 185.408 116.182 159.259 1.00 35.84  ? 3982 PRO A CG    1 
ATOM   17879 C  CD    . PRO A 1 3982 ? 186.601 115.703 160.011 1.00 37.45  ? 3982 PRO A CD    1 
ATOM   17880 N  N     . ILE A 1 3983 ? 185.761 119.218 161.180 1.00 34.61  ? 3983 ILE A N     1 
ATOM   17881 C  CA    . ILE A 1 3983 ? 185.368 120.418 161.911 1.00 31.60  ? 3983 ILE A CA    1 
ATOM   17882 C  C     . ILE A 1 3983 ? 186.591 121.102 162.510 1.00 29.26  ? 3983 ILE A C     1 
ATOM   17883 O  O     . ILE A 1 3983 ? 186.718 122.331 162.463 1.00 32.85  ? 3983 ILE A O     1 
ATOM   17884 C  CB    . ILE A 1 3983 ? 184.324 120.073 162.987 1.00 31.59  ? 3983 ILE A CB    1 
ATOM   17885 C  CG1   . ILE A 1 3983 ? 183.098 119.417 162.350 1.00 32.00  ? 3983 ILE A CG1   1 
ATOM   17886 C  CG2   . ILE A 1 3983 ? 183.912 121.319 163.744 1.00 25.36  ? 3983 ILE A CG2   1 
ATOM   17887 C  CD1   . ILE A 1 3983 ? 183.053 117.912 162.518 1.00 40.28  ? 3983 ILE A CD1   1 
ATOM   17888 N  N     . GLY A 1 3984 ? 187.510 120.323 163.080 1.00 29.98  ? 3984 GLY A N     1 
ATOM   17889 C  CA    . GLY A 1 3984 ? 188.733 120.908 163.605 1.00 32.57  ? 3984 GLY A CA    1 
ATOM   17890 C  C     . GLY A 1 3984 ? 189.615 121.487 162.517 1.00 31.96  ? 3984 GLY A C     1 
ATOM   17891 O  O     . GLY A 1 3984 ? 190.256 122.526 162.709 1.00 35.53  ? 3984 GLY A O     1 
ATOM   17892 N  N     . GLN A 1 3985 ? 189.665 120.822 161.361 1.00 34.39  ? 3985 GLN A N     1 
ATOM   17893 C  CA    . GLN A 1 3985 ? 190.377 121.380 160.218 1.00 32.83  ? 3985 GLN A CA    1 
ATOM   17894 C  C     . GLN A 1 3985 ? 189.761 122.705 159.793 1.00 30.63  ? 3985 GLN A C     1 
ATOM   17895 O  O     . GLN A 1 3985 ? 190.479 123.658 159.468 1.00 34.28  ? 3985 GLN A O     1 
ATOM   17896 C  CB    . GLN A 1 3985 ? 190.364 120.384 159.061 1.00 33.65  ? 3985 GLN A CB    1 
ATOM   17897 C  CG    . GLN A 1 3985 ? 191.363 119.251 159.207 1.00 45.43  ? 3985 GLN A CG    1 
ATOM   17898 C  CD    . GLN A 1 3985 ? 191.366 118.322 158.011 1.00 61.30  ? 3985 GLN A CD    1 
ATOM   17899 O  OE1   . GLN A 1 3985 ? 191.357 118.768 156.863 1.00 57.61  ? 3985 GLN A OE1   1 
ATOM   17900 N  NE2   . GLN A 1 3985 ? 191.383 117.021 158.272 1.00 61.54  ? 3985 GLN A NE2   1 
ATOM   17901 N  N     . ALA A 1 3986 ? 188.429 122.785 159.797 1.00 27.37  ? 3986 ALA A N     1 
ATOM   17902 C  CA    . ALA A 1 3986 ? 187.755 124.037 159.473 1.00 25.47  ? 3986 ALA A CA    1 
ATOM   17903 C  C     . ALA A 1 3986 ? 188.082 125.123 160.489 1.00 24.70  ? 3986 ALA A C     1 
ATOM   17904 O  O     . ALA A 1 3986 ? 188.278 126.284 160.122 1.00 26.69  ? 3986 ALA A O     1 
ATOM   17905 C  CB    . ALA A 1 3986 ? 186.246 123.814 159.392 1.00 20.77  ? 3986 ALA A CB    1 
ATOM   17906 N  N     . ILE A 1 3987 ? 188.138 124.765 161.774 1.00 23.13  ? 3987 ILE A N     1 
ATOM   17907 C  CA    . ILE A 1 3987 ? 188.469 125.745 162.808 1.00 24.92  ? 3987 ILE A CA    1 
ATOM   17908 C  C     . ILE A 1 3987 ? 189.889 126.267 162.619 1.00 25.18  ? 3987 ILE A C     1 
ATOM   17909 O  O     . ILE A 1 3987 ? 190.148 127.473 162.735 1.00 29.36  ? 3987 ILE A O     1 
ATOM   17910 C  CB    . ILE A 1 3987 ? 188.273 125.134 164.208 1.00 27.73  ? 3987 ILE A CB    1 
ATOM   17911 C  CG1   . ILE A 1 3987 ? 186.803 124.783 164.437 1.00 28.18  ? 3987 ILE A CG1   1 
ATOM   17912 C  CG2   . ILE A 1 3987 ? 188.758 126.091 165.283 1.00 31.96  ? 3987 ILE A CG2   1 
ATOM   17913 C  CD1   . ILE A 1 3987 ? 186.529 124.133 165.770 1.00 32.02  ? 3987 ILE A CD1   1 
ATOM   17914 N  N     . HIS A 1 3988 ? 190.832 125.369 162.332 1.00 26.75  ? 3988 HIS A N     1 
ATOM   17915 C  CA    . HIS A 1 3988 ? 192.212 125.791 162.114 1.00 28.25  ? 3988 HIS A CA    1 
ATOM   17916 C  C     . HIS A 1 3988 ? 192.339 126.654 160.862 1.00 29.44  ? 3988 HIS A C     1 
ATOM   17917 O  O     . HIS A 1 3988 ? 193.089 127.639 160.853 1.00 30.65  ? 3988 HIS A O     1 
ATOM   17918 C  CB    . HIS A 1 3988 ? 193.122 124.568 162.032 1.00 35.08  ? 3988 HIS A CB    1 
ATOM   17919 C  CG    . HIS A 1 3988 ? 193.387 123.930 163.359 1.00 34.68  ? 3988 HIS A CG    1 
ATOM   17920 N  ND1   . HIS A 1 3988 ? 192.858 122.709 163.718 1.00 40.37  ? 3988 HIS A ND1   1 
ATOM   17921 C  CD2   . HIS A 1 3988 ? 194.120 124.347 164.418 1.00 35.48  ? 3988 HIS A CD2   1 
ATOM   17922 C  CE1   . HIS A 1 3988 ? 193.255 122.401 164.939 1.00 44.88  ? 3988 HIS A CE1   1 
ATOM   17923 N  NE2   . HIS A 1 3988 ? 194.022 123.379 165.387 1.00 40.92  ? 3988 HIS A NE2   1 
ATOM   17924 N  N     . ARG A 1 3989 ? 191.617 126.300 159.796 1.00 27.37  ? 3989 ARG A N     1 
ATOM   17925 C  CA    . ARG A 1 3989 ? 191.608 127.134 158.599 1.00 22.64  ? 3989 ARG A CA    1 
ATOM   17926 C  C     . ARG A 1 3989 ? 191.009 128.503 158.889 1.00 21.43  ? 3989 ARG A C     1 
ATOM   17927 O  O     . ARG A 1 3989 ? 191.472 129.516 158.358 1.00 21.32  ? 3989 ARG A O     1 
ATOM   17928 C  CB    . ARG A 1 3989 ? 190.838 126.442 157.476 1.00 23.90  ? 3989 ARG A CB    1 
ATOM   17929 C  CG    . ARG A 1 3989 ? 191.553 125.258 156.857 1.00 24.39  ? 3989 ARG A CG    1 
ATOM   17930 C  CD    . ARG A 1 3989 ? 190.904 124.875 155.541 1.00 30.98  ? 3989 ARG A CD    1 
ATOM   17931 N  NE    . ARG A 1 3989 ? 190.642 123.444 155.445 1.00 34.97  ? 3989 ARG A NE    1 
ATOM   17932 C  CZ    . ARG A 1 3989 ? 191.544 122.541 155.086 1.00 41.99  ? 3989 ARG A CZ    1 
ATOM   17933 N  NH1   . ARG A 1 3989 ? 192.782 122.887 154.776 1.00 39.40  ? 3989 ARG A NH1   1 
ATOM   17934 N  NH2   . ARG A 1 3989 ? 191.193 121.260 155.034 1.00 43.85  ? 3989 ARG A NH2   1 
ATOM   17935 N  N     . LEU A 1 3990 ? 189.970 128.548 159.724 1.00 18.66  ? 3990 LEU A N     1 
ATOM   17936 C  CA    . LEU A 1 3990 ? 189.377 129.820 160.117 1.00 18.41  ? 3990 LEU A CA    1 
ATOM   17937 C  C     . LEU A 1 3990 ? 190.382 130.680 160.869 1.00 24.41  ? 3990 LEU A C     1 
ATOM   17938 O  O     . LEU A 1 3990 ? 190.484 131.889 160.627 1.00 25.55  ? 3990 LEU A O     1 
ATOM   17939 C  CB    . LEU A 1 3990 ? 188.137 129.561 160.971 1.00 15.27  ? 3990 LEU A CB    1 
ATOM   17940 C  CG    . LEU A 1 3990 ? 187.183 130.710 161.292 1.00 14.00  ? 3990 LEU A CG    1 
ATOM   17941 C  CD1   . LEU A 1 3990 ? 186.751 131.429 160.031 1.00 14.46  ? 3990 LEU A CD1   1 
ATOM   17942 C  CD2   . LEU A 1 3990 ? 185.976 130.185 162.050 1.00 14.18  ? 3990 LEU A CD2   1 
ATOM   17943 N  N     . LEU A 1 3991 ? 191.139 130.070 161.783 1.00 27.32  ? 3991 LEU A N     1 
ATOM   17944 C  CA    . LEU A 1 3991 ? 192.157 130.815 162.517 1.00 25.01  ? 3991 LEU A CA    1 
ATOM   17945 C  C     . LEU A 1 3991 ? 193.243 131.340 161.584 1.00 25.81  ? 3991 LEU A C     1 
ATOM   17946 O  O     . LEU A 1 3991 ? 193.661 132.501 161.693 1.00 28.88  ? 3991 LEU A O     1 
ATOM   17947 C  CB    . LEU A 1 3991 ? 192.765 129.934 163.607 1.00 28.96  ? 3991 LEU A CB    1 
ATOM   17948 C  CG    . LEU A 1 3991 ? 191.929 129.771 164.875 1.00 33.35  ? 3991 LEU A CG    1 
ATOM   17949 C  CD1   . LEU A 1 3991 ? 192.216 128.431 165.523 1.00 35.31  ? 3991 LEU A CD1   1 
ATOM   17950 C  CD2   . LEU A 1 3991 ? 192.185 130.909 165.846 1.00 30.94  ? 3991 LEU A CD2   1 
ATOM   17951 N  N     . LEU A 1 3992 ? 193.712 130.499 160.658 1.00 23.06  ? 3992 LEU A N     1 
ATOM   17952 C  CA    . LEU A 1 3992 ? 194.732 130.944 159.711 1.00 25.58  ? 3992 LEU A CA    1 
ATOM   17953 C  C     . LEU A 1 3992 ? 194.215 132.060 158.814 1.00 25.97  ? 3992 LEU A C     1 
ATOM   17954 O  O     . LEU A 1 3992 ? 194.953 132.999 158.499 1.00 30.74  ? 3992 LEU A O     1 
ATOM   17955 C  CB    . LEU A 1 3992 ? 195.234 129.774 158.867 1.00 29.37  ? 3992 LEU A CB    1 
ATOM   17956 C  CG    . LEU A 1 3992 ? 196.003 128.682 159.602 1.00 28.60  ? 3992 LEU A CG    1 
ATOM   17957 C  CD1   . LEU A 1 3992 ? 196.308 127.534 158.663 1.00 33.77  ? 3992 LEU A CD1   1 
ATOM   17958 C  CD2   . LEU A 1 3992 ? 197.287 129.271 160.149 1.00 24.04  ? 3992 LEU A CD2   1 
ATOM   17959 N  N     . ILE A 1 3993 ? 192.959 131.968 158.377 1.00 25.14  ? 3993 ILE A N     1 
ATOM   17960 C  CA    . ILE A 1 3993 ? 192.384 133.023 157.551 1.00 20.58  ? 3993 ILE A CA    1 
ATOM   17961 C  C     . ILE A 1 3993 ? 192.290 134.322 158.340 1.00 19.26  ? 3993 ILE A C     1 
ATOM   17962 O  O     . ILE A 1 3993 ? 192.619 135.398 157.829 1.00 23.48  ? 3993 ILE A O     1 
ATOM   17963 C  CB    . ILE A 1 3993 ? 191.014 132.582 157.004 1.00 19.28  ? 3993 ILE A CB    1 
ATOM   17964 C  CG1   . ILE A 1 3993 ? 191.195 131.656 155.800 1.00 19.21  ? 3993 ILE A CG1   1 
ATOM   17965 C  CG2   . ILE A 1 3993 ? 190.175 133.784 156.617 1.00 18.03  ? 3993 ILE A CG2   1 
ATOM   17966 C  CD1   . ILE A 1 3993 ? 191.761 132.341 154.582 1.00 16.79  ? 3993 ILE A CD1   1 
ATOM   17967 N  N     . GLN A 1 3994 ? 191.857 134.243 159.600 1.00 23.28  ? 3994 GLN A N     1 
ATOM   17968 C  CA    . GLN A 1 3994 ? 191.756 135.444 160.423 1.00 22.22  ? 3994 GLN A CA    1 
ATOM   17969 C  C     . GLN A 1 3994 ? 193.123 136.081 160.637 1.00 23.98  ? 3994 GLN A C     1 
ATOM   17970 O  O     . GLN A 1 3994 ? 193.245 137.311 160.668 1.00 24.84  ? 3994 GLN A O     1 
ATOM   17971 C  CB    . GLN A 1 3994 ? 191.103 135.106 161.763 1.00 21.22  ? 3994 GLN A CB    1 
ATOM   17972 C  CG    . GLN A 1 3994 ? 190.669 136.316 162.570 1.00 16.14  ? 3994 GLN A CG    1 
ATOM   17973 C  CD    . GLN A 1 3994 ? 190.397 135.981 164.022 1.00 18.26  ? 3994 GLN A CD    1 
ATOM   17974 O  OE1   . GLN A 1 3994 ? 190.786 134.922 164.510 1.00 25.96  ? 3994 GLN A OE1   1 
ATOM   17975 N  NE2   . GLN A 1 3994 ? 189.719 136.883 164.719 1.00 26.17  ? 3994 GLN A NE2   1 
ATOM   17976 N  N     . ALA A 1 3995 ? 194.162 135.260 160.793 1.00 27.52  ? 3995 ALA A N     1 
ATOM   17977 C  CA    . ALA A 1 3995 ? 195.502 135.805 160.992 1.00 25.93  ? 3995 ALA A CA    1 
ATOM   17978 C  C     . ALA A 1 3995 ? 196.071 136.388 159.703 1.00 27.90  ? 3995 ALA A C     1 
ATOM   17979 O  O     . ALA A 1 3995 ? 196.727 137.436 159.726 1.00 31.76  ? 3995 ALA A O     1 
ATOM   17980 C  CB    . ALA A 1 3995 ? 196.428 134.724 161.546 1.00 30.77  ? 3995 ALA A CB    1 
ATOM   17981 N  N     . PHE A 1 3996 ? 195.828 135.730 158.570 1.00 32.52  ? 3996 PHE A N     1 
ATOM   17982 C  CA    . PHE A 1 3996 ? 196.464 136.084 157.303 1.00 24.32  ? 3996 PHE A CA    1 
ATOM   17983 C  C     . PHE A 1 3996 ? 195.598 137.010 156.453 1.00 26.70  ? 3996 PHE A C     1 
ATOM   17984 O  O     . PHE A 1 3996 ? 196.028 138.107 156.085 1.00 35.56  ? 3996 PHE A O     1 
ATOM   17985 C  CB    . PHE A 1 3996 ? 196.798 134.807 156.524 1.00 24.48  ? 3996 PHE A CB    1 
ATOM   17986 C  CG    . PHE A 1 3996 ? 197.948 134.031 157.094 1.00 35.82  ? 3996 PHE A CG    1 
ATOM   17987 C  CD1   . PHE A 1 3996 ? 199.092 134.678 157.524 1.00 35.34  ? 3996 PHE A CD1   1 
ATOM   17988 C  CD2   . PHE A 1 3996 ? 197.879 132.654 157.214 1.00 37.92  ? 3996 PHE A CD2   1 
ATOM   17989 C  CE1   . PHE A 1 3996 ? 200.151 133.964 158.046 1.00 34.71  ? 3996 PHE A CE1   1 
ATOM   17990 C  CE2   . PHE A 1 3996 ? 198.934 131.936 157.740 1.00 40.18  ? 3996 PHE A CE2   1 
ATOM   17991 C  CZ    . PHE A 1 3996 ? 200.071 132.593 158.157 1.00 42.30  ? 3996 PHE A CZ    1 
ATOM   17992 N  N     . ARG A 1 3997 ? 194.381 136.579 156.129 1.00 26.61  ? 3997 ARG A N     1 
ATOM   17993 C  CA    . ARG A 1 3997 ? 193.511 137.281 155.187 1.00 21.50  ? 3997 ARG A CA    1 
ATOM   17994 C  C     . ARG A 1 3997 ? 192.170 137.547 155.854 1.00 19.02  ? 3997 ARG A C     1 
ATOM   17995 O  O     . ARG A 1 3997 ? 191.190 136.830 155.611 1.00 23.18  ? 3997 ARG A O     1 
ATOM   17996 C  CB    . ARG A 1 3997 ? 193.332 136.474 153.900 1.00 20.06  ? 3997 ARG A CB    1 
ATOM   17997 C  CG    . ARG A 1 3997 ? 194.610 136.277 153.103 1.00 18.50  ? 3997 ARG A CG    1 
ATOM   17998 C  CD    . ARG A 1 3997 ? 194.983 137.532 152.339 1.00 23.37  ? 3997 ARG A CD    1 
ATOM   17999 N  NE    . ARG A 1 3997 ? 193.946 137.921 151.391 1.00 23.33  ? 3997 ARG A NE    1 
ATOM   18000 C  CZ    . ARG A 1 3997 ? 193.786 137.378 150.192 1.00 22.06  ? 3997 ARG A CZ    1 
ATOM   18001 N  NH1   . ARG A 1 3997 ? 194.585 136.419 149.755 1.00 24.37  ? 3997 ARG A NH1   1 
ATOM   18002 N  NH2   . ARG A 1 3997 ? 192.800 137.809 149.412 1.00 24.15  ? 3997 ARG A NH2   1 
ATOM   18003 N  N     . PRO A 1 3998 ? 192.091 138.568 156.712 1.00 18.11  ? 3998 PRO A N     1 
ATOM   18004 C  CA    . PRO A 1 3998 ? 190.809 138.868 157.371 1.00 19.31  ? 3998 PRO A CA    1 
ATOM   18005 C  C     . PRO A 1 3998 ? 189.699 139.229 156.402 1.00 17.25  ? 3998 PRO A C     1 
ATOM   18006 O  O     . PRO A 1 3998 ? 188.521 139.029 156.724 1.00 21.29  ? 3998 PRO A O     1 
ATOM   18007 C  CB    . PRO A 1 3998 ? 191.158 140.043 158.297 1.00 18.59  ? 3998 PRO A CB    1 
ATOM   18008 C  CG    . PRO A 1 3998 ? 192.403 140.628 157.728 1.00 16.13  ? 3998 PRO A CG    1 
ATOM   18009 C  CD    . PRO A 1 3998 ? 193.160 139.487 157.131 1.00 17.93  ? 3998 PRO A CD    1 
ATOM   18010 N  N     . ASP A 1 3999 ? 190.039 139.754 155.222 1.00 18.66  ? 3999 ASP A N     1 
ATOM   18011 C  CA    . ASP A 1 3999 ? 189.018 140.118 154.245 1.00 15.91  ? 3999 ASP A CA    1 
ATOM   18012 C  C     . ASP A 1 3999 ? 188.203 138.911 153.803 1.00 16.13  ? 3999 ASP A C     1 
ATOM   18013 O  O     . ASP A 1 3999 ? 187.029 139.053 153.445 1.00 22.06  ? 3999 ASP A O     1 
ATOM   18014 C  CB    . ASP A 1 3999 ? 189.669 140.793 153.038 1.00 17.95  ? 3999 ASP A CB    1 
ATOM   18015 C  CG    . ASP A 1 3999 ? 190.787 139.961 152.437 1.00 26.51  ? 3999 ASP A CG    1 
ATOM   18016 O  OD1   . ASP A 1 3999 ? 191.881 139.909 153.036 1.00 28.13  ? 3999 ASP A OD1   1 
ATOM   18017 O  OD2   . ASP A 1 3999 ? 190.573 139.361 151.363 1.00 26.77  ? 3999 ASP A OD2   1 
ATOM   18018 N  N     . ARG A 1 4000 ? 188.800 137.723 153.817 1.00 15.53  ? 4000 ARG A N     1 
ATOM   18019 C  CA    . ARG A 1 4000 ? 188.096 136.497 153.469 1.00 17.09  ? 4000 ARG A CA    1 
ATOM   18020 C  C     . ARG A 1 4000 ? 187.472 135.812 154.676 1.00 14.56  ? 4000 ARG A C     1 
ATOM   18021 O  O     . ARG A 1 4000 ? 186.848 134.756 154.512 1.00 16.38  ? 4000 ARG A O     1 
ATOM   18022 C  CB    . ARG A 1 4000 ? 189.046 135.527 152.761 1.00 16.38  ? 4000 ARG A CB    1 
ATOM   18023 C  CG    . ARG A 1 4000 ? 189.783 136.137 151.586 1.00 18.68  ? 4000 ARG A CG    1 
ATOM   18024 C  CD    . ARG A 1 4000 ? 188.813 136.681 150.555 1.00 19.18  ? 4000 ARG A CD    1 
ATOM   18025 N  NE    . ARG A 1 4000 ? 187.868 135.668 150.105 1.00 18.96  ? 4000 ARG A NE    1 
ATOM   18026 C  CZ    . ARG A 1 4000 ? 186.762 135.929 149.423 1.00 24.03  ? 4000 ARG A CZ    1 
ATOM   18027 N  NH1   . ARG A 1 4000 ? 186.421 137.167 149.107 1.00 25.51  ? 4000 ARG A NH1   1 
ATOM   18028 N  NH2   . ARG A 1 4000 ? 185.976 134.923 149.050 1.00 21.44  ? 4000 ARG A NH2   1 
ATOM   18029 N  N     . LEU A 1 4001 ? 187.603 136.401 155.869 1.00 13.26  ? 4001 LEU A N     1 
ATOM   18030 C  CA    . LEU A 1 4001 ? 187.143 135.753 157.094 1.00 10.53  ? 4001 LEU A CA    1 
ATOM   18031 C  C     . LEU A 1 4001 ? 185.691 135.313 156.978 1.00 9.29   ? 4001 LEU A C     1 
ATOM   18032 O  O     . LEU A 1 4001 ? 185.365 134.143 157.211 1.00 14.27  ? 4001 LEU A O     1 
ATOM   18033 C  CB    . LEU A 1 4001 ? 187.318 136.703 158.280 1.00 8.79   ? 4001 LEU A CB    1 
ATOM   18034 C  CG    . LEU A 1 4001 ? 187.119 136.106 159.674 1.00 9.84   ? 4001 LEU A CG    1 
ATOM   18035 C  CD1   . LEU A 1 4001 ? 188.000 134.886 159.862 1.00 16.56  ? 4001 LEU A CD1   1 
ATOM   18036 C  CD2   . LEU A 1 4001 ? 187.389 137.141 160.753 1.00 10.95  ? 4001 LEU A CD2   1 
ATOM   18037 N  N     . LEU A 1 4002 ? 184.812 136.236 156.578 1.00 9.02   ? 4002 LEU A N     1 
ATOM   18038 C  CA    . LEU A 1 4002 ? 183.400 135.906 156.418 1.00 7.93   ? 4002 LEU A CA    1 
ATOM   18039 C  C     . LEU A 1 4002 ? 183.227 134.685 155.528 1.00 9.07   ? 4002 LEU A C     1 
ATOM   18040 O  O     . LEU A 1 4002 ? 182.526 133.732 155.890 1.00 12.21  ? 4002 LEU A O     1 
ATOM   18041 C  CB    . LEU A 1 4002 ? 182.644 137.103 155.840 1.00 9.12   ? 4002 LEU A CB    1 
ATOM   18042 C  CG    . LEU A 1 4002 ? 182.210 138.185 156.828 1.00 9.30   ? 4002 LEU A CG    1 
ATOM   18043 C  CD1   . LEU A 1 4002 ? 181.372 139.236 156.123 1.00 14.78  ? 4002 LEU A CD1   1 
ATOM   18044 C  CD2   . LEU A 1 4002 ? 181.448 137.580 157.992 1.00 11.89  ? 4002 LEU A CD2   1 
ATOM   18045 N  N     . ALA A 1 4003 ? 183.901 134.679 154.375 1.00 10.63  ? 4003 ALA A N     1 
ATOM   18046 C  CA    . ALA A 1 4003 ? 183.825 133.526 153.486 1.00 10.15  ? 4003 ALA A CA    1 
ATOM   18047 C  C     . ALA A 1 4003 ? 184.236 132.259 154.219 1.00 12.54  ? 4003 ALA A C     1 
ATOM   18048 O  O     . ALA A 1 4003 ? 183.497 131.265 154.229 1.00 12.61  ? 4003 ALA A O     1 
ATOM   18049 C  CB    . ALA A 1 4003 ? 184.705 133.753 152.257 1.00 9.17   ? 4003 ALA A CB    1 
ATOM   18050 N  N     . MET A 1 4004 ? 185.385 132.301 154.898 1.00 13.89  ? 4004 MET A N     1 
ATOM   18051 C  CA    . MET A 1 4004 ? 185.830 131.139 155.654 1.00 12.67  ? 4004 MET A CA    1 
ATOM   18052 C  C     . MET A 1 4004 ? 184.795 130.755 156.699 1.00 12.47  ? 4004 MET A C     1 
ATOM   18053 O  O     . MET A 1 4004 ? 184.509 129.566 156.894 1.00 16.65  ? 4004 MET A O     1 
ATOM   18054 C  CB    . MET A 1 4004 ? 187.183 131.424 156.305 1.00 11.00  ? 4004 MET A CB    1 
ATOM   18055 C  CG    . MET A 1 4004 ? 187.888 130.197 156.856 1.00 16.93  ? 4004 MET A CG    1 
ATOM   18056 S  SD    . MET A 1 4004 ? 188.109 128.881 155.646 1.00 31.91  ? 4004 MET A SD    1 
ATOM   18057 C  CE    . MET A 1 4004 ? 187.373 127.501 156.514 1.00 20.15  ? 4004 MET A CE    1 
ATOM   18058 N  N     . ALA A 1 4005 ? 184.184 131.754 157.343 1.00 9.81   ? 4005 ALA A N     1 
ATOM   18059 C  CA    . ALA A 1 4005 ? 183.148 131.470 158.325 1.00 7.39   ? 4005 ALA A CA    1 
ATOM   18060 C  C     . ALA A 1 4005 ? 182.028 130.654 157.702 1.00 10.33  ? 4005 ALA A C     1 
ATOM   18061 O  O     . ALA A 1 4005 ? 181.587 129.651 158.277 1.00 14.94  ? 4005 ALA A O     1 
ATOM   18062 C  CB    . ALA A 1 4005 ? 182.607 132.771 158.914 1.00 9.79   ? 4005 ALA A CB    1 
ATOM   18063 N  N     . HIS A 1 4006 ? 181.591 131.039 156.498 1.00 10.54  ? 4006 HIS A N     1 
ATOM   18064 C  CA    . HIS A 1 4006 ? 180.558 130.267 155.821 1.00 12.14  ? 4006 HIS A CA    1 
ATOM   18065 C  C     . HIS A 1 4006 ? 180.995 128.822 155.655 1.00 11.24  ? 4006 HIS A C     1 
ATOM   18066 O  O     . HIS A 1 4006 ? 180.229 127.896 155.951 1.00 13.60  ? 4006 HIS A O     1 
ATOM   18067 C  CB    . HIS A 1 4006 ? 180.230 130.893 154.466 1.00 10.98  ? 4006 HIS A CB    1 
ATOM   18068 C  CG    . HIS A 1 4006 ? 179.252 132.023 154.545 1.00 11.01  ? 4006 HIS A CG    1 
ATOM   18069 N  ND1   . HIS A 1 4006 ? 179.606 133.286 154.966 1.00 13.10  ? 4006 HIS A ND1   1 
ATOM   18070 C  CD2   . HIS A 1 4006 ? 177.929 132.078 154.262 1.00 12.89  ? 4006 HIS A CD2   1 
ATOM   18071 C  CE1   . HIS A 1 4006 ? 178.544 134.072 154.935 1.00 15.65  ? 4006 HIS A CE1   1 
ATOM   18072 N  NE2   . HIS A 1 4006 ? 177.514 133.363 154.512 1.00 16.63  ? 4006 HIS A NE2   1 
ATOM   18073 N  N     . MET A 1 4007 ? 182.247 128.613 155.238 1.00 13.81  ? 4007 MET A N     1 
ATOM   18074 C  CA    . MET A 1 4007 ? 182.757 127.256 155.100 1.00 12.37  ? 4007 MET A CA    1 
ATOM   18075 C  C     . MET A 1 4007 ? 182.623 126.496 156.409 1.00 12.38  ? 4007 MET A C     1 
ATOM   18076 O  O     . MET A 1 4007 ? 182.159 125.349 156.423 1.00 14.27  ? 4007 MET A O     1 
ATOM   18077 C  CB    . MET A 1 4007 ? 184.211 127.287 154.631 1.00 13.11  ? 4007 MET A CB    1 
ATOM   18078 C  CG    . MET A 1 4007 ? 184.368 127.478 153.131 1.00 14.12  ? 4007 MET A CG    1 
ATOM   18079 S  SD    . MET A 1 4007 ? 186.062 127.252 152.559 1.00 34.85  ? 4007 MET A SD    1 
ATOM   18080 C  CE    . MET A 1 4007 ? 185.949 125.640 151.789 1.00 24.02  ? 4007 MET A CE    1 
ATOM   18081 N  N     . PHE A 1 4008 ? 182.967 127.143 157.527 1.00 14.61  ? 4008 PHE A N     1 
ATOM   18082 C  CA    . PHE A 1 4008 ? 182.832 126.491 158.825 1.00 12.60  ? 4008 PHE A CA    1 
ATOM   18083 C  C     . PHE A 1 4008 ? 181.399 126.038 159.056 1.00 11.64  ? 4008 PHE A C     1 
ATOM   18084 O  O     . PHE A 1 4008 ? 181.160 124.899 159.478 1.00 14.08  ? 4008 PHE A O     1 
ATOM   18085 C  CB    . PHE A 1 4008 ? 183.289 127.434 159.937 1.00 10.60  ? 4008 PHE A CB    1 
ATOM   18086 C  CG    . PHE A 1 4008 ? 183.061 126.896 161.321 1.00 12.94  ? 4008 PHE A CG    1 
ATOM   18087 C  CD1   . PHE A 1 4008 ? 183.848 125.874 161.819 1.00 16.34  ? 4008 PHE A CD1   1 
ATOM   18088 C  CD2   . PHE A 1 4008 ? 182.061 127.414 162.123 1.00 11.05  ? 4008 PHE A CD2   1 
ATOM   18089 C  CE1   . PHE A 1 4008 ? 183.639 125.379 163.090 1.00 15.30  ? 4008 PHE A CE1   1 
ATOM   18090 C  CE2   . PHE A 1 4008 ? 181.849 126.924 163.395 1.00 12.35  ? 4008 PHE A CE2   1 
ATOM   18091 C  CZ    . PHE A 1 4008 ? 182.640 125.906 163.880 1.00 14.31  ? 4008 PHE A CZ    1 
ATOM   18092 N  N     . VAL A 1 4009 ? 180.429 126.900 158.741 1.00 9.83   ? 4009 VAL A N     1 
ATOM   18093 C  CA    . VAL A 1 4009 ? 179.031 126.516 158.897 1.00 9.72   ? 4009 VAL A CA    1 
ATOM   18094 C  C     . VAL A 1 4009 ? 178.725 125.302 158.033 1.00 13.82  ? 4009 VAL A C     1 
ATOM   18095 O  O     . VAL A 1 4009 ? 178.069 124.351 158.479 1.00 20.60  ? 4009 VAL A O     1 
ATOM   18096 C  CB    . VAL A 1 4009 ? 178.108 127.704 158.565 1.00 9.39   ? 4009 VAL A CB    1 
ATOM   18097 C  CG1   . VAL A 1 4009 ? 176.653 127.274 158.603 1.00 11.29  ? 4009 VAL A CG1   1 
ATOM   18098 C  CG2   . VAL A 1 4009 ? 178.351 128.847 159.534 1.00 7.98   ? 4009 VAL A CG2   1 
ATOM   18099 N  N     . SER A 1 4010 ? 179.233 125.294 156.799 1.00 12.61  ? 4010 SER A N     1 
ATOM   18100 C  CA    . SER A 1 4010 ? 179.004 124.161 155.913 1.00 13.11  ? 4010 SER A CA    1 
ATOM   18101 C  C     . SER A 1 4010 ? 179.612 122.876 156.456 1.00 16.28  ? 4010 SER A C     1 
ATOM   18102 O  O     . SER A 1 4010 ? 179.143 121.788 156.107 1.00 20.04  ? 4010 SER A O     1 
ATOM   18103 C  CB    . SER A 1 4010 ? 179.565 124.462 154.524 1.00 18.04  ? 4010 SER A CB    1 
ATOM   18104 O  OG    . SER A 1 4010 ? 178.879 125.545 153.923 1.00 22.93  ? 4010 SER A OG    1 
ATOM   18105 N  N     . THR A 1 4011 ? 180.637 122.972 157.306 1.00 16.04  ? 4011 THR A N     1 
ATOM   18106 C  CA    . THR A 1 4011 ? 181.224 121.759 157.862 1.00 14.80  ? 4011 THR A CA    1 
ATOM   18107 C  C     . THR A 1 4011 ? 180.390 121.206 159.008 1.00 20.70  ? 4011 THR A C     1 
ATOM   18108 O  O     . THR A 1 4011 ? 180.575 120.050 159.403 1.00 30.94  ? 4011 THR A O     1 
ATOM   18109 C  CB    . THR A 1 4011 ? 182.655 122.022 158.333 1.00 16.87  ? 4011 THR A CB    1 
ATOM   18110 O  OG1   . THR A 1 4011 ? 182.641 122.942 159.431 1.00 22.03  ? 4011 THR A OG1   1 
ATOM   18111 C  CG2   . THR A 1 4011 ? 183.494 122.589 157.202 1.00 15.48  ? 4011 THR A CG2   1 
ATOM   18112 N  N     . ASN A 1 4012 ? 179.471 122.003 159.552 1.00 15.71  ? 4012 ASN A N     1 
ATOM   18113 C  CA    . ASN A 1 4012 ? 178.676 121.584 160.701 1.00 15.39  ? 4012 ASN A CA    1 
ATOM   18114 C  C     . ASN A 1 4012 ? 177.208 121.378 160.343 1.00 17.39  ? 4012 ASN A C     1 
ATOM   18115 O  O     . ASN A 1 4012 ? 176.634 120.327 160.643 1.00 19.84  ? 4012 ASN A O     1 
ATOM   18116 C  CB    . ASN A 1 4012 ? 178.811 122.610 161.833 1.00 16.60  ? 4012 ASN A CB    1 
ATOM   18117 C  CG    . ASN A 1 4012 ? 180.128 122.493 162.570 1.00 18.64  ? 4012 ASN A CG    1 
ATOM   18118 O  OD1   . ASN A 1 4012 ? 180.515 121.409 163.002 1.00 33.21  ? 4012 ASN A OD1   1 
ATOM   18119 N  ND2   . ASN A 1 4012 ? 180.825 123.609 162.713 1.00 14.79  ? 4012 ASN A ND2   1 
ATOM   18120 N  N     . LEU A 1 4013 ? 176.588 122.367 159.707 1.00 14.94  ? 4013 LEU A N     1 
ATOM   18121 C  CA    . LEU A 1 4013 ? 175.155 122.352 159.460 1.00 13.42  ? 4013 LEU A CA    1 
ATOM   18122 C  C     . LEU A 1 4013 ? 174.788 122.016 158.021 1.00 16.68  ? 4013 LEU A C     1 
ATOM   18123 O  O     . LEU A 1 4013 ? 173.606 122.072 157.671 1.00 19.83  ? 4013 LEU A O     1 
ATOM   18124 C  CB    . LEU A 1 4013 ? 174.550 123.702 159.848 1.00 14.45  ? 4013 LEU A CB    1 
ATOM   18125 C  CG    . LEU A 1 4013 ? 174.720 124.109 161.312 1.00 9.64   ? 4013 LEU A CG    1 
ATOM   18126 C  CD1   . LEU A 1 4013 ? 174.885 125.612 161.430 1.00 7.37   ? 4013 LEU A CD1   1 
ATOM   18127 C  CD2   . LEU A 1 4013 ? 173.542 123.631 162.139 1.00 10.81  ? 4013 LEU A CD2   1 
ATOM   18128 N  N     . GLY A 1 4014 ? 175.757 121.669 157.184 1.00 16.84  ? 4014 GLY A N     1 
ATOM   18129 C  CA    . GLY A 1 4014 ? 175.473 121.292 155.817 1.00 13.08  ? 4014 GLY A CA    1 
ATOM   18130 C  C     . GLY A 1 4014 ? 175.748 122.418 154.833 1.00 22.33  ? 4014 GLY A C     1 
ATOM   18131 O  O     . GLY A 1 4014 ? 175.802 123.600 155.183 1.00 23.23  ? 4014 GLY A O     1 
ATOM   18132 N  N     . GLU A 1 4015 ? 175.917 122.032 153.567 1.00 28.41  ? 4015 GLU A N     1 
ATOM   18133 C  CA    . GLU A 1 4015 ? 176.272 122.999 152.533 1.00 24.99  ? 4015 GLU A CA    1 
ATOM   18134 C  C     . GLU A 1 4015 ? 175.112 123.926 152.193 1.00 26.60  ? 4015 GLU A C     1 
ATOM   18135 O  O     . GLU A 1 4015 ? 175.337 125.059 151.754 1.00 26.20  ? 4015 GLU A O     1 
ATOM   18136 C  CB    . GLU A 1 4015 ? 176.749 122.271 151.278 1.00 22.33  ? 4015 GLU A CB    1 
ATOM   18137 C  CG    . GLU A 1 4015 ? 178.049 121.509 151.459 1.00 32.56  ? 4015 GLU A CG    1 
ATOM   18138 C  CD    . GLU A 1 4015 ? 179.231 122.423 151.705 1.00 43.06  ? 4015 GLU A CD    1 
ATOM   18139 O  OE1   . GLU A 1 4015 ? 179.230 123.554 151.177 1.00 47.19  ? 4015 GLU A OE1   1 
ATOM   18140 O  OE2   . GLU A 1 4015 ? 180.164 122.009 152.426 1.00 40.96  ? 4015 GLU A OE2   1 
ATOM   18141 N  N     . SER A 1 4016 ? 173.875 123.470 152.382 1.00 22.34  ? 4016 SER A N     1 
ATOM   18142 C  CA    . SER A 1 4016 ? 172.693 124.240 152.018 1.00 19.44  ? 4016 SER A CA    1 
ATOM   18143 C  C     . SER A 1 4016 ? 171.968 124.804 153.235 1.00 22.17  ? 4016 SER A C     1 
ATOM   18144 O  O     . SER A 1 4016 ? 170.770 125.090 153.160 1.00 22.76  ? 4016 SER A O     1 
ATOM   18145 C  CB    . SER A 1 4016 ? 171.741 123.382 151.185 1.00 23.53  ? 4016 SER A CB    1 
ATOM   18146 O  OG    . SER A 1 4016 ? 171.431 122.170 151.850 1.00 26.73  ? 4016 SER A OG    1 
ATOM   18147 N  N     . PHE A 1 4017 ? 172.671 124.965 154.358 1.00 18.86  ? 4017 PHE A N     1 
ATOM   18148 C  CA    . PHE A 1 4017 ? 172.032 125.471 155.568 1.00 13.33  ? 4017 PHE A CA    1 
ATOM   18149 C  C     . PHE A 1 4017 ? 171.558 126.908 155.385 1.00 13.12  ? 4017 PHE A C     1 
ATOM   18150 O  O     . PHE A 1 4017 ? 170.465 127.273 155.834 1.00 15.93  ? 4017 PHE A O     1 
ATOM   18151 C  CB    . PHE A 1 4017 ? 172.995 125.366 156.750 1.00 12.49  ? 4017 PHE A CB    1 
ATOM   18152 C  CG    . PHE A 1 4017 ? 172.363 125.680 158.073 1.00 9.72   ? 4017 PHE A CG    1 
ATOM   18153 C  CD1   . PHE A 1 4017 ? 171.479 124.793 158.659 1.00 7.02   ? 4017 PHE A CD1   1 
ATOM   18154 C  CD2   . PHE A 1 4017 ? 172.653 126.862 158.732 1.00 10.83  ? 4017 PHE A CD2   1 
ATOM   18155 C  CE1   . PHE A 1 4017 ? 170.899 125.076 159.875 1.00 7.06   ? 4017 PHE A CE1   1 
ATOM   18156 C  CE2   . PHE A 1 4017 ? 172.072 127.151 159.947 1.00 8.92   ? 4017 PHE A CE2   1 
ATOM   18157 C  CZ    . PHE A 1 4017 ? 171.196 126.255 160.520 1.00 6.19   ? 4017 PHE A CZ    1 
ATOM   18158 N  N     . MET A 1 4018 ? 172.366 127.738 154.728 1.00 13.22  ? 4018 MET A N     1 
ATOM   18159 C  CA    . MET A 1 4018 ? 172.043 129.141 154.511 1.00 12.93  ? 4018 MET A CA    1 
ATOM   18160 C  C     . MET A 1 4018 ? 171.522 129.417 153.105 1.00 19.33  ? 4018 MET A C     1 
ATOM   18161 O  O     . MET A 1 4018 ? 171.451 130.580 152.696 1.00 23.63  ? 4018 MET A O     1 
ATOM   18162 C  CB    . MET A 1 4018 ? 173.264 130.015 154.794 1.00 11.55  ? 4018 MET A CB    1 
ATOM   18163 C  CG    . MET A 1 4018 ? 173.829 129.876 156.191 1.00 7.85   ? 4018 MET A CG    1 
ATOM   18164 S  SD    . MET A 1 4018 ? 175.354 130.815 156.367 1.00 14.65  ? 4018 MET A SD    1 
ATOM   18165 C  CE    . MET A 1 4018 ? 174.730 132.292 157.155 1.00 6.50   ? 4018 MET A CE    1 
ATOM   18166 N  N     . SER A 1 4019 ? 171.158 128.376 152.359 1.00 20.76  ? 4019 SER A N     1 
ATOM   18167 C  CA    . SER A 1 4019 ? 170.696 128.553 150.989 1.00 21.49  ? 4019 SER A CA    1 
ATOM   18168 C  C     . SER A 1 4019 ? 169.301 129.158 150.898 1.00 22.22  ? 4019 SER A C     1 
ATOM   18169 O  O     . SER A 1 4019 ? 168.938 129.674 149.837 1.00 27.33  ? 4019 SER A O     1 
ATOM   18170 C  CB    . SER A 1 4019 ? 170.724 127.214 150.250 1.00 23.11  ? 4019 SER A CB    1 
ATOM   18171 O  OG    . SER A 1 4019 ? 169.788 126.307 150.803 1.00 30.00  ? 4019 SER A OG    1 
ATOM   18172 N  N     . ILE A 1 4020 ? 168.509 129.103 151.969 1.00 20.58  ? 4020 ILE A N     1 
ATOM   18173 C  CA    . ILE A 1 4020 ? 167.166 129.674 151.924 1.00 19.92  ? 4020 ILE A CA    1 
ATOM   18174 C  C     . ILE A 1 4020 ? 167.230 131.196 151.879 1.00 20.86  ? 4020 ILE A C     1 
ATOM   18175 O  O     . ILE A 1 4020 ? 166.441 131.844 151.180 1.00 22.05  ? 4020 ILE A O     1 
ATOM   18176 C  CB    . ILE A 1 4020 ? 166.333 129.172 153.117 1.00 19.49  ? 4020 ILE A CB    1 
ATOM   18177 C  CG1   . ILE A 1 4020 ? 166.221 127.648 153.074 1.00 22.47  ? 4020 ILE A CG1   1 
ATOM   18178 C  CG2   . ILE A 1 4020 ? 164.952 129.803 153.114 1.00 12.53  ? 4020 ILE A CG2   1 
ATOM   18179 C  CD1   . ILE A 1 4020 ? 165.460 127.132 151.877 1.00 15.75  ? 4020 ILE A CD1   1 
ATOM   18180 N  N     . MET A 1 4021 ? 168.168 131.791 152.617 1.00 21.21  ? 4021 MET A N     1 
ATOM   18181 C  CA    . MET A 1 4021 ? 168.267 133.244 152.696 1.00 17.96  ? 4021 MET A CA    1 
ATOM   18182 C  C     . MET A 1 4021 ? 168.661 133.893 151.376 1.00 22.43  ? 4021 MET A C     1 
ATOM   18183 O  O     . MET A 1 4021 ? 168.462 135.103 151.223 1.00 26.61  ? 4021 MET A O     1 
ATOM   18184 C  CB    . MET A 1 4021 ? 169.266 133.638 153.783 1.00 15.39  ? 4021 MET A CB    1 
ATOM   18185 C  CG    . MET A 1 4021 ? 168.846 133.231 155.185 1.00 15.12  ? 4021 MET A CG    1 
ATOM   18186 S  SD    . MET A 1 4021 ? 167.168 133.760 155.584 1.00 24.42  ? 4021 MET A SD    1 
ATOM   18187 C  CE    . MET A 1 4021 ? 166.315 132.188 155.641 1.00 10.22  ? 4021 MET A CE    1 
ATOM   18188 N  N     . GLU A 1 4022 ? 169.208 133.137 150.429 1.00 27.17  ? 4022 GLU A N     1 
ATOM   18189 C  CA    . GLU A 1 4022 ? 169.561 133.680 149.125 1.00 22.65  ? 4022 GLU A CA    1 
ATOM   18190 C  C     . GLU A 1 4022 ? 168.435 133.549 148.110 1.00 19.30  ? 4022 GLU A C     1 
ATOM   18191 O  O     . GLU A 1 4022 ? 168.610 133.952 146.956 1.00 22.58  ? 4022 GLU A O     1 
ATOM   18192 C  CB    . GLU A 1 4022 ? 170.826 132.997 148.591 1.00 25.02  ? 4022 GLU A CB    1 
ATOM   18193 C  CG    . GLU A 1 4022 ? 170.602 131.603 148.033 1.00 29.32  ? 4022 GLU A CG    1 
ATOM   18194 C  CD    . GLU A 1 4022 ? 171.897 130.847 147.810 1.00 38.50  ? 4022 GLU A CD    1 
ATOM   18195 O  OE1   . GLU A 1 4022 ? 172.834 131.014 148.619 1.00 41.24  ? 4022 GLU A OE1   1 
ATOM   18196 O  OE2   . GLU A 1 4022 ? 171.981 130.087 146.823 1.00 37.74  ? 4022 GLU A OE2   1 
ATOM   18197 N  N     . GLN A 1 4023 ? 167.289 133.002 148.510 1.00 21.76  ? 4023 GLN A N     1 
ATOM   18198 C  CA    . GLN A 1 4023 ? 166.106 132.836 147.684 1.00 20.60  ? 4023 GLN A CA    1 
ATOM   18199 C  C     . GLN A 1 4023 ? 165.066 133.897 148.024 1.00 26.34  ? 4023 GLN A C     1 
ATOM   18200 O  O     . GLN A 1 4023 ? 165.027 134.397 149.152 1.00 26.23  ? 4023 GLN A O     1 
ATOM   18201 C  CB    . GLN A 1 4023 ? 165.497 131.445 147.881 1.00 17.44  ? 4023 GLN A CB    1 
ATOM   18202 C  CG    . GLN A 1 4023 ? 166.489 130.305 147.729 1.00 23.31  ? 4023 GLN A CG    1 
ATOM   18203 C  CD    . GLN A 1 4023 ? 167.070 130.219 146.331 1.00 30.35  ? 4023 GLN A CD    1 
ATOM   18204 O  OE1   . GLN A 1 4023 ? 166.417 130.575 145.351 1.00 30.61  ? 4023 GLN A OE1   1 
ATOM   18205 N  NE2   . GLN A 1 4023 ? 168.306 129.744 146.234 1.00 26.85  ? 4023 GLN A NE2   1 
ATOM   18206 N  N     . PRO A 1 4024 ? 164.221 134.273 147.064 1.00 26.75  ? 4024 PRO A N     1 
ATOM   18207 C  CA    . PRO A 1 4024 ? 163.182 135.268 147.352 1.00 21.30  ? 4024 PRO A CA    1 
ATOM   18208 C  C     . PRO A 1 4024 ? 162.240 134.785 148.445 1.00 23.03  ? 4024 PRO A C     1 
ATOM   18209 O  O     . PRO A 1 4024 ? 161.911 133.600 148.532 1.00 27.37  ? 4024 PRO A O     1 
ATOM   18210 C  CB    . PRO A 1 4024 ? 162.458 135.428 146.010 1.00 13.65  ? 4024 PRO A CB    1 
ATOM   18211 C  CG    . PRO A 1 4024 ? 162.842 134.227 145.209 1.00 16.95  ? 4024 PRO A CG    1 
ATOM   18212 C  CD    . PRO A 1 4024 ? 164.222 133.875 145.647 1.00 20.37  ? 4024 PRO A CD    1 
ATOM   18213 N  N     . LEU A 1 4025 ? 161.812 135.724 149.285 1.00 24.27  ? 4025 LEU A N     1 
ATOM   18214 C  CA    . LEU A 1 4025 ? 160.927 135.395 150.392 1.00 24.52  ? 4025 LEU A CA    1 
ATOM   18215 C  C     . LEU A 1 4025 ? 159.585 134.899 149.870 1.00 32.60  ? 4025 LEU A C     1 
ATOM   18216 O  O     . LEU A 1 4025 ? 158.950 135.547 149.033 1.00 31.70  ? 4025 LEU A O     1 
ATOM   18217 C  CB    . LEU A 1 4025 ? 160.731 136.622 151.284 1.00 21.66  ? 4025 LEU A CB    1 
ATOM   18218 C  CG    . LEU A 1 4025 ? 159.693 136.539 152.402 1.00 18.68  ? 4025 LEU A CG    1 
ATOM   18219 C  CD1   . LEU A 1 4025 ? 159.969 135.354 153.304 1.00 26.71  ? 4025 LEU A CD1   1 
ATOM   18220 C  CD2   . LEU A 1 4025 ? 159.671 137.827 153.203 1.00 16.39  ? 4025 LEU A CD2   1 
ATOM   18221 N  N     . ASP A 1 4026 ? 159.156 133.744 150.369 1.00 31.70  ? 4026 ASP A N     1 
ATOM   18222 C  CA    . ASP A 1 4026 ? 157.888 133.129 149.989 1.00 31.47  ? 4026 ASP A CA    1 
ATOM   18223 C  C     . ASP A 1 4026 ? 156.888 133.433 151.099 1.00 30.89  ? 4026 ASP A C     1 
ATOM   18224 O  O     . ASP A 1 4026 ? 156.661 132.618 151.994 1.00 33.92  ? 4026 ASP A O     1 
ATOM   18225 C  CB    . ASP A 1 4026 ? 158.042 131.630 149.767 1.00 38.89  ? 4026 ASP A CB    1 
ATOM   18226 C  CG    . ASP A 1 4026 ? 156.743 130.967 149.361 1.00 42.49  ? 4026 ASP A CG    1 
ATOM   18227 O  OD1   . ASP A 1 4026 ? 156.162 131.372 148.332 1.00 48.12  ? 4026 ASP A OD1   1 
ATOM   18228 O  OD2   . ASP A 1 4026 ? 156.302 130.042 150.072 1.00 34.22  ? 4026 ASP A OD2   1 
ATOM   18229 N  N     . LEU A 1 4027 ? 156.283 134.618 151.028 1.00 31.46  ? 4027 LEU A N     1 
ATOM   18230 C  CA    . LEU A 1 4027 ? 155.378 135.060 152.078 1.00 29.55  ? 4027 LEU A CA    1 
ATOM   18231 C  C     . LEU A 1 4027 ? 154.047 134.322 152.056 1.00 26.52  ? 4027 LEU A C     1 
ATOM   18232 O  O     . LEU A 1 4027 ? 153.318 134.367 153.049 1.00 26.31  ? 4027 LEU A O     1 
ATOM   18233 C  CB    . LEU A 1 4027 ? 155.145 136.563 151.957 1.00 25.41  ? 4027 LEU A CB    1 
ATOM   18234 C  CG    . LEU A 1 4027 ? 156.040 137.475 152.789 1.00 27.08  ? 4027 LEU A CG    1 
ATOM   18235 C  CD1   . LEU A 1 4027 ? 155.627 138.910 152.570 1.00 24.63  ? 4027 LEU A CD1   1 
ATOM   18236 C  CD2   . LEU A 1 4027 ? 155.961 137.111 154.262 1.00 26.45  ? 4027 LEU A CD2   1 
ATOM   18237 N  N     . THR A 1 4028 ? 153.714 133.645 150.956 1.00 30.25  ? 4028 THR A N     1 
ATOM   18238 C  CA    . THR A 1 4028 ? 152.435 132.946 150.881 1.00 32.83  ? 4028 THR A CA    1 
ATOM   18239 C  C     . THR A 1 4028 ? 152.369 131.806 151.891 1.00 32.18  ? 4028 THR A C     1 
ATOM   18240 O  O     . THR A 1 4028 ? 151.411 131.698 152.665 1.00 35.65  ? 4028 THR A O     1 
ATOM   18241 C  CB    . THR A 1 4028 ? 152.206 132.422 149.464 1.00 34.20  ? 4028 THR A CB    1 
ATOM   18242 O  OG1   . THR A 1 4028 ? 152.195 133.520 148.544 1.00 37.23  ? 4028 THR A OG1   1 
ATOM   18243 C  CG2   . THR A 1 4028 ? 150.877 131.688 149.380 1.00 33.36  ? 4028 THR A CG2   1 
ATOM   18244 N  N     . HIS A 1 4029 ? 153.389 130.945 151.902 1.00 28.23  ? 4029 HIS A N     1 
ATOM   18245 C  CA    . HIS A 1 4029 ? 153.401 129.824 152.834 1.00 27.91  ? 4029 HIS A CA    1 
ATOM   18246 C  C     . HIS A 1 4029 ? 153.593 130.289 154.271 1.00 31.46  ? 4029 HIS A C     1 
ATOM   18247 O  O     . HIS A 1 4029 ? 153.085 129.652 155.201 1.00 31.37  ? 4029 HIS A O     1 
ATOM   18248 C  CB    . HIS A 1 4029 ? 154.495 128.829 152.445 1.00 31.42  ? 4029 HIS A CB    1 
ATOM   18249 C  CG    . HIS A 1 4029 ? 154.637 127.683 153.398 1.00 42.69  ? 4029 HIS A CG    1 
ATOM   18250 N  ND1   . HIS A 1 4029 ? 155.852 127.296 153.920 1.00 44.74  ? 4029 HIS A ND1   1 
ATOM   18251 C  CD2   . HIS A 1 4029 ? 153.716 126.841 153.924 1.00 37.48  ? 4029 HIS A CD2   1 
ATOM   18252 C  CE1   . HIS A 1 4029 ? 155.674 126.265 154.727 1.00 47.72  ? 4029 HIS A CE1   1 
ATOM   18253 N  NE2   . HIS A 1 4029 ? 154.387 125.969 154.747 1.00 40.49  ? 4029 HIS A NE2   1 
ATOM   18254 N  N     . ILE A 1 4030 ? 154.316 131.393 154.473 1.00 33.41  ? 4030 ILE A N     1 
ATOM   18255 C  CA    . ILE A 1 4030 ? 154.568 131.896 155.821 1.00 27.28  ? 4030 ILE A CA    1 
ATOM   18256 C  C     . ILE A 1 4030 ? 153.423 132.743 156.353 1.00 25.09  ? 4030 ILE A C     1 
ATOM   18257 O  O     . ILE A 1 4030 ? 153.391 133.042 157.551 1.00 30.50  ? 4030 ILE A O     1 
ATOM   18258 C  CB    . ILE A 1 4030 ? 155.896 132.679 155.830 1.00 23.80  ? 4030 ILE A CB    1 
ATOM   18259 C  CG1   . ILE A 1 4030 ? 156.979 131.872 155.119 1.00 24.27  ? 4030 ILE A CG1   1 
ATOM   18260 C  CG2   . ILE A 1 4030 ? 156.362 132.958 157.242 1.00 25.52  ? 4030 ILE A CG2   1 
ATOM   18261 C  CD1   . ILE A 1 4030 ? 158.261 132.631 154.912 1.00 24.36  ? 4030 ILE A CD1   1 
ATOM   18262 N  N     . VAL A 1 4031 ? 152.472 133.128 155.509 1.00 26.51  ? 4031 VAL A N     1 
ATOM   18263 C  CA    . VAL A 1 4031 ? 151.303 133.875 155.949 1.00 25.94  ? 4031 VAL A CA    1 
ATOM   18264 C  C     . VAL A 1 4031 ? 150.079 132.975 156.076 1.00 28.41  ? 4031 VAL A C     1 
ATOM   18265 O  O     . VAL A 1 4031 ? 149.332 133.078 157.049 1.00 29.73  ? 4031 VAL A O     1 
ATOM   18266 C  CB    . VAL A 1 4031 ? 151.035 135.061 154.996 1.00 26.76  ? 4031 VAL A CB    1 
ATOM   18267 C  CG1   . VAL A 1 4031 ? 149.595 135.535 155.110 1.00 23.22  ? 4031 VAL A CG1   1 
ATOM   18268 C  CG2   . VAL A 1 4031 ? 151.992 136.202 155.300 1.00 22.51  ? 4031 VAL A CG2   1 
ATOM   18269 N  N     . GLY A 1 4032 ? 149.863 132.083 155.106 1.00 26.96  ? 4032 GLY A N     1 
ATOM   18270 C  CA    . GLY A 1 4032 ? 148.769 131.133 155.227 1.00 28.14  ? 4032 GLY A CA    1 
ATOM   18271 C  C     . GLY A 1 4032 ? 148.939 130.205 156.414 1.00 31.62  ? 4032 GLY A C     1 
ATOM   18272 O  O     . GLY A 1 4032 ? 147.975 129.901 157.121 1.00 35.01  ? 4032 GLY A O     1 
ATOM   18273 N  N     . THR A 1 4033 ? 150.161 129.741 156.643 1.00 31.22  ? 4033 THR A N     1 
ATOM   18274 C  CA    . THR A 1 4033 ? 150.525 128.973 157.822 1.00 26.17  ? 4033 THR A CA    1 
ATOM   18275 C  C     . THR A 1 4033 ? 151.635 129.707 158.562 1.00 31.54  ? 4033 THR A C     1 
ATOM   18276 O  O     . THR A 1 4033 ? 152.065 130.790 158.162 1.00 38.18  ? 4033 THR A O     1 
ATOM   18277 C  CB    . THR A 1 4033 ? 150.977 127.556 157.448 1.00 28.94  ? 4033 THR A CB    1 
ATOM   18278 O  OG1   . THR A 1 4033 ? 151.914 127.621 156.367 1.00 27.28  ? 4033 THR A OG1   1 
ATOM   18279 C  CG2   . THR A 1 4033 ? 149.784 126.713 157.023 1.00 33.21  ? 4033 THR A CG2   1 
ATOM   18280 N  N     . GLU A 1 4034 ? 152.082 129.117 159.669 1.00 27.22  ? 4034 GLU A N     1 
ATOM   18281 C  CA    . GLU A 1 4034 ? 153.208 129.574 160.481 1.00 25.59  ? 4034 GLU A CA    1 
ATOM   18282 C  C     . GLU A 1 4034 ? 152.949 130.900 161.187 1.00 27.71  ? 4034 GLU A C     1 
ATOM   18283 O  O     . GLU A 1 4034 ? 153.815 131.356 161.943 1.00 28.63  ? 4034 GLU A O     1 
ATOM   18284 C  CB    . GLU A 1 4034 ? 154.499 129.712 159.660 1.00 27.96  ? 4034 GLU A CB    1 
ATOM   18285 C  CG    . GLU A 1 4034 ? 155.056 128.400 159.147 1.00 36.52  ? 4034 GLU A CG    1 
ATOM   18286 C  CD    . GLU A 1 4034 ? 156.317 128.586 158.329 1.00 43.04  ? 4034 GLU A CD    1 
ATOM   18287 O  OE1   . GLU A 1 4034 ? 156.685 129.748 158.059 1.00 34.00  ? 4034 GLU A OE1   1 
ATOM   18288 O  OE2   . GLU A 1 4034 ? 156.937 127.569 157.950 1.00 48.50  ? 4034 GLU A OE2   1 
ATOM   18289 N  N     . VAL A 1 4035 ? 151.798 131.534 160.974 1.00 24.51  ? 4035 VAL A N     1 
ATOM   18290 C  CA    . VAL A 1 4035 ? 151.436 132.775 161.650 1.00 24.68  ? 4035 VAL A CA    1 
ATOM   18291 C  C     . VAL A 1 4035 ? 150.005 132.645 162.147 1.00 26.99  ? 4035 VAL A C     1 
ATOM   18292 O  O     . VAL A 1 4035 ? 149.095 132.359 161.360 1.00 24.65  ? 4035 VAL A O     1 
ATOM   18293 C  CB    . VAL A 1 4035 ? 151.580 134.006 160.738 1.00 18.71  ? 4035 VAL A CB    1 
ATOM   18294 C  CG1   . VAL A 1 4035 ? 151.056 135.244 161.439 1.00 18.04  ? 4035 VAL A CG1   1 
ATOM   18295 C  CG2   . VAL A 1 4035 ? 153.031 134.219 160.367 1.00 21.18  ? 4035 VAL A CG2   1 
ATOM   18296 N  N     . LYS A 1 4036 ? 149.809 132.852 163.444 1.00 27.79  ? 4036 LYS A N     1 
ATOM   18297 C  CA    . LYS A 1 4036 ? 148.479 132.837 164.025 1.00 22.96  ? 4036 LYS A CA    1 
ATOM   18298 C  C     . LYS A 1 4036 ? 147.728 134.116 163.661 1.00 22.86  ? 4036 LYS A C     1 
ATOM   18299 O  O     . LYS A 1 4036 ? 148.346 135.143 163.367 1.00 26.71  ? 4036 LYS A O     1 
ATOM   18300 C  CB    . LYS A 1 4036 ? 148.565 132.697 165.541 1.00 30.52  ? 4036 LYS A CB    1 
ATOM   18301 C  CG    . LYS A 1 4036 ? 149.131 131.365 166.002 1.00 37.92  ? 4036 LYS A CG    1 
ATOM   18302 C  CD    . LYS A 1 4036 ? 149.179 131.278 167.517 1.00 45.04  ? 4036 LYS A CD    1 
ATOM   18303 C  CE    . LYS A 1 4036 ? 149.661 129.911 167.972 1.00 41.79  ? 4036 LYS A CE    1 
ATOM   18304 N  NZ    . LYS A 1 4036 ? 151.083 129.676 167.600 1.00 39.53  ? 4036 LYS A NZ    1 
ATOM   18305 N  N     . PRO A 1 4037 ? 146.393 134.076 163.656 1.00 23.58  ? 4037 PRO A N     1 
ATOM   18306 C  CA    . PRO A 1 4037 ? 145.631 135.293 163.332 1.00 24.78  ? 4037 PRO A CA    1 
ATOM   18307 C  C     . PRO A 1 4037 ? 145.893 136.448 164.282 1.00 22.03  ? 4037 PRO A C     1 
ATOM   18308 O  O     . PRO A 1 4037 ? 145.812 137.609 163.862 1.00 28.45  ? 4037 PRO A O     1 
ATOM   18309 C  CB    . PRO A 1 4037 ? 144.170 134.823 163.399 1.00 20.77  ? 4037 PRO A CB    1 
ATOM   18310 C  CG    . PRO A 1 4037 ? 144.201 133.545 164.170 1.00 24.01  ? 4037 PRO A CG    1 
ATOM   18311 C  CD    . PRO A 1 4037 ? 145.512 132.913 163.849 1.00 27.85  ? 4037 PRO A CD    1 
ATOM   18312 N  N     . ASN A 1 4038 ? 146.203 136.173 165.545 1.00 19.83  ? 4038 ASN A N     1 
ATOM   18313 C  CA    . ASN A 1 4038 ? 146.484 137.219 166.518 1.00 23.64  ? 4038 ASN A CA    1 
ATOM   18314 C  C     . ASN A 1 4038 ? 147.934 137.687 166.496 1.00 24.20  ? 4038 ASN A C     1 
ATOM   18315 O  O     . ASN A 1 4038 ? 148.280 138.617 167.233 1.00 21.65  ? 4038 ASN A O     1 
ATOM   18316 C  CB    . ASN A 1 4038 ? 146.107 136.745 167.929 1.00 23.74  ? 4038 ASN A CB    1 
ATOM   18317 C  CG    . ASN A 1 4038 ? 146.933 135.557 168.399 1.00 35.27  ? 4038 ASN A CG    1 
ATOM   18318 O  OD1   . ASN A 1 4038 ? 147.884 135.133 167.742 1.00 31.80  ? 4038 ASN A OD1   1 
ATOM   18319 N  ND2   . ASN A 1 4038 ? 146.571 135.018 169.555 1.00 52.81  ? 4038 ASN A ND2   1 
ATOM   18320 N  N     . THR A 1 4039 ? 148.784 137.074 165.676 1.00 22.43  ? 4039 THR A N     1 
ATOM   18321 C  CA    . THR A 1 4039 ? 150.187 137.447 165.610 1.00 18.55  ? 4039 THR A CA    1 
ATOM   18322 C  C     . THR A 1 4039 ? 150.394 138.406 164.449 1.00 17.51  ? 4039 THR A C     1 
ATOM   18323 O  O     . THR A 1 4039 ? 150.246 137.996 163.288 1.00 20.83  ? 4039 THR A O     1 
ATOM   18324 C  CB    . THR A 1 4039 ? 151.065 136.209 165.441 1.00 19.87  ? 4039 THR A CB    1 
ATOM   18325 O  OG1   . THR A 1 4039 ? 150.730 135.245 166.446 1.00 36.03  ? 4039 THR A OG1   1 
ATOM   18326 C  CG2   . THR A 1 4039 ? 152.532 136.573 165.568 1.00 13.47  ? 4039 THR A CG2   1 
ATOM   18327 N  N     . PRO A 1 4040 ? 150.723 139.670 164.698 1.00 13.54  ? 4040 PRO A N     1 
ATOM   18328 C  CA    . PRO A 1 4040 ? 150.929 140.606 163.589 1.00 12.46  ? 4040 PRO A CA    1 
ATOM   18329 C  C     . PRO A 1 4040 ? 152.155 140.249 162.765 1.00 11.91  ? 4040 PRO A C     1 
ATOM   18330 O  O     . PRO A 1 4040 ? 153.144 139.714 163.269 1.00 13.81  ? 4040 PRO A O     1 
ATOM   18331 C  CB    . PRO A 1 4040 ? 151.109 141.957 164.292 1.00 10.63  ? 4040 PRO A CB    1 
ATOM   18332 C  CG    . PRO A 1 4040 ? 151.552 141.608 165.670 1.00 13.55  ? 4040 PRO A CG    1 
ATOM   18333 C  CD    . PRO A 1 4040 ? 150.876 140.320 166.010 1.00 12.23  ? 4040 PRO A CD    1 
ATOM   18334 N  N     . VAL A 1 4041 ? 152.076 140.559 161.477 1.00 11.35  ? 4041 VAL A N     1 
ATOM   18335 C  CA    . VAL A 1 4041 ? 153.182 140.383 160.545 1.00 9.85   ? 4041 VAL A CA    1 
ATOM   18336 C  C     . VAL A 1 4041 ? 153.886 141.730 160.449 1.00 10.30  ? 4041 VAL A C     1 
ATOM   18337 O  O     . VAL A 1 4041 ? 153.428 142.635 159.746 1.00 10.15  ? 4041 VAL A O     1 
ATOM   18338 C  CB    . VAL A 1 4041 ? 152.700 139.895 159.177 1.00 10.01  ? 4041 VAL A CB    1 
ATOM   18339 C  CG1   . VAL A 1 4041 ? 153.883 139.585 158.278 1.00 11.44  ? 4041 VAL A CG1   1 
ATOM   18340 C  CG2   . VAL A 1 4041 ? 151.807 138.676 159.331 1.00 8.95   ? 4041 VAL A CG2   1 
ATOM   18341 N  N     . LEU A 1 4042 ? 154.993 141.875 161.173 1.00 11.54  ? 4042 LEU A N     1 
ATOM   18342 C  CA    . LEU A 1 4042 ? 155.777 143.099 161.131 1.00 9.44   ? 4042 LEU A CA    1 
ATOM   18343 C  C     . LEU A 1 4042 ? 156.709 143.034 159.932 1.00 9.90   ? 4042 LEU A C     1 
ATOM   18344 O  O     . LEU A 1 4042 ? 157.476 142.078 159.793 1.00 11.38  ? 4042 LEU A O     1 
ATOM   18345 C  CB    . LEU A 1 4042 ? 156.580 143.263 162.419 1.00 9.58   ? 4042 LEU A CB    1 
ATOM   18346 C  CG    . LEU A 1 4042 ? 155.830 143.081 163.738 1.00 7.46   ? 4042 LEU A CG    1 
ATOM   18347 C  CD1   . LEU A 1 4042 ? 156.734 143.432 164.897 1.00 12.38  ? 4042 LEU A CD1   1 
ATOM   18348 C  CD2   . LEU A 1 4042 ? 154.577 143.927 163.765 1.00 8.87   ? 4042 LEU A CD2   1 
ATOM   18349 N  N     . MET A 1 4043 ? 156.620 144.021 159.050 1.00 14.84  ? 4043 MET A N     1 
ATOM   18350 C  CA    . MET A 1 4043 ? 157.531 144.113 157.915 1.00 13.66  ? 4043 MET A CA    1 
ATOM   18351 C  C     . MET A 1 4043 ? 158.420 145.342 158.080 1.00 17.07  ? 4043 MET A C     1 
ATOM   18352 O  O     . MET A 1 4043 ? 158.068 146.468 157.726 1.00 15.08  ? 4043 MET A O     1 
ATOM   18353 C  CB    . MET A 1 4043 ? 156.751 144.132 156.608 1.00 9.95   ? 4043 MET A CB    1 
ATOM   18354 C  CG    . MET A 1 4043 ? 156.051 142.818 156.341 1.00 15.65  ? 4043 MET A CG    1 
ATOM   18355 S  SD    . MET A 1 4043 ? 155.119 142.806 154.815 1.00 43.47  ? 4043 MET A SD    1 
ATOM   18356 C  CE    . MET A 1 4043 ? 154.380 141.181 154.910 1.00 39.20  ? 4043 MET A CE    1 
ATOM   18357 N  N     . CYS A 1 4044 ? 159.588 145.096 158.669 1.00 17.46  ? 4044 CYS A N     1 
ATOM   18358 C  CA    . CYS A 1 4044 ? 160.550 146.162 158.900 1.00 13.28  ? 4044 CYS A CA    1 
ATOM   18359 C  C     . CYS A 1 4044 ? 161.464 146.296 157.692 1.00 12.36  ? 4044 CYS A C     1 
ATOM   18360 O  O     . CYS A 1 4044 ? 162.032 145.308 157.216 1.00 13.04  ? 4044 CYS A O     1 
ATOM   18361 C  CB    . CYS A 1 4044 ? 161.370 145.878 160.156 1.00 16.40  ? 4044 CYS A CB    1 
ATOM   18362 S  SG    . CYS A 1 4044 ? 160.395 145.386 161.596 1.00 37.28  ? 4044 CYS A SG    1 
ATOM   18363 N  N     . SER A 1 4045 ? 161.614 147.518 157.200 1.00 14.47  ? 4045 SER A N     1 
ATOM   18364 C  CA    . SER A 1 4045 ? 162.367 147.756 155.981 1.00 10.49  ? 4045 SER A CA    1 
ATOM   18365 C  C     . SER A 1 4045 ? 163.444 148.801 156.223 1.00 12.07  ? 4045 SER A C     1 
ATOM   18366 O  O     . SER A 1 4045 ? 163.257 149.749 156.989 1.00 15.99  ? 4045 SER A O     1 
ATOM   18367 C  CB    . SER A 1 4045 ? 161.449 148.210 154.845 1.00 13.22  ? 4045 SER A CB    1 
ATOM   18368 O  OG    . SER A 1 4045 ? 160.632 147.147 154.390 1.00 26.96  ? 4045 SER A OG    1 
ATOM   18369 N  N     . VAL A 1 4046 ? 164.579 148.607 155.560 1.00 13.93  ? 4046 VAL A N     1 
ATOM   18370 C  CA    . VAL A 1 4046 ? 165.653 149.595 155.528 1.00 15.67  ? 4046 VAL A CA    1 
ATOM   18371 C  C     . VAL A 1 4046 ? 165.150 150.766 154.693 1.00 20.36  ? 4046 VAL A C     1 
ATOM   18372 O  O     . VAL A 1 4046 ? 164.215 150.589 153.899 1.00 24.93  ? 4046 VAL A O     1 
ATOM   18373 C  CB    . VAL A 1 4046 ? 166.947 148.996 154.954 1.00 16.48  ? 4046 VAL A CB    1 
ATOM   18374 C  CG1   . VAL A 1 4046 ? 167.449 147.869 155.839 1.00 12.88  ? 4046 VAL A CG1   1 
ATOM   18375 C  CG2   . VAL A 1 4046 ? 166.720 148.505 153.536 1.00 15.10  ? 4046 VAL A CG2   1 
ATOM   18376 N  N     . PRO A 1 4047 ? 165.707 151.969 154.841 1.00 19.05  ? 4047 PRO A N     1 
ATOM   18377 C  CA    . PRO A 1 4047 ? 165.202 153.106 154.062 1.00 19.79  ? 4047 PRO A CA    1 
ATOM   18378 C  C     . PRO A 1 4047 ? 165.289 152.844 152.566 1.00 21.80  ? 4047 PRO A C     1 
ATOM   18379 O  O     . PRO A 1 4047 ? 166.271 152.294 152.065 1.00 22.34  ? 4047 PRO A O     1 
ATOM   18380 C  CB    . PRO A 1 4047 ? 166.112 154.264 154.489 1.00 16.59  ? 4047 PRO A CB    1 
ATOM   18381 C  CG    . PRO A 1 4047 ? 167.312 153.613 155.093 1.00 20.68  ? 4047 PRO A CG    1 
ATOM   18382 C  CD    . PRO A 1 4047 ? 166.798 152.372 155.742 1.00 17.44  ? 4047 PRO A CD    1 
ATOM   18383 N  N     . GLY A 1 4048 ? 164.239 153.248 151.853 1.00 22.48  ? 4048 GLY A N     1 
ATOM   18384 C  CA    . GLY A 1 4048 ? 164.141 153.031 150.429 1.00 21.10  ? 4048 GLY A CA    1 
ATOM   18385 C  C     . GLY A 1 4048 ? 163.446 151.755 150.010 1.00 19.74  ? 4048 GLY A C     1 
ATOM   18386 O  O     . GLY A 1 4048 ? 163.214 151.562 148.810 1.00 21.30  ? 4048 GLY A O     1 
ATOM   18387 N  N     . TYR A 1 4049 ? 163.109 150.878 150.949 1.00 19.32  ? 4049 TYR A N     1 
ATOM   18388 C  CA    . TYR A 1 4049 ? 162.369 149.662 150.648 1.00 20.78  ? 4049 TYR A CA    1 
ATOM   18389 C  C     . TYR A 1 4049 ? 161.011 149.724 151.327 1.00 24.32  ? 4049 TYR A C     1 
ATOM   18390 O  O     . TYR A 1 4049 ? 160.903 150.143 152.482 1.00 27.09  ? 4049 TYR A O     1 
ATOM   18391 C  CB    . TYR A 1 4049 ? 163.138 148.412 151.090 1.00 15.59  ? 4049 TYR A CB    1 
ATOM   18392 C  CG    . TYR A 1 4049 ? 164.121 147.939 150.048 1.00 19.98  ? 4049 TYR A CG    1 
ATOM   18393 C  CD1   . TYR A 1 4049 ? 165.272 148.665 149.774 1.00 19.74  ? 4049 TYR A CD1   1 
ATOM   18394 C  CD2   . TYR A 1 4049 ? 163.887 146.782 149.319 1.00 15.22  ? 4049 TYR A CD2   1 
ATOM   18395 C  CE1   . TYR A 1 4049 ? 166.166 148.248 148.812 1.00 16.28  ? 4049 TYR A CE1   1 
ATOM   18396 C  CE2   . TYR A 1 4049 ? 164.779 146.355 148.356 1.00 21.23  ? 4049 TYR A CE2   1 
ATOM   18397 C  CZ    . TYR A 1 4049 ? 165.916 147.093 148.107 1.00 21.79  ? 4049 TYR A CZ    1 
ATOM   18398 O  OH    . TYR A 1 4049 ? 166.808 146.675 147.147 1.00 22.63  ? 4049 TYR A OH    1 
ATOM   18399 N  N     . ASP A 1 4050 ? 159.976 149.329 150.594 1.00 21.48  ? 4050 ASP A N     1 
ATOM   18400 C  CA    . ASP A 1 4050 ? 158.610 149.362 151.091 1.00 28.54  ? 4050 ASP A CA    1 
ATOM   18401 C  C     . ASP A 1 4050 ? 157.971 148.003 150.863 1.00 30.55  ? 4050 ASP A C     1 
ATOM   18402 O  O     . ASP A 1 4050 ? 157.986 147.488 149.740 1.00 34.09  ? 4050 ASP A O     1 
ATOM   18403 C  CB    . ASP A 1 4050 ? 157.800 150.463 150.399 1.00 28.55  ? 4050 ASP A CB    1 
ATOM   18404 C  CG    . ASP A 1 4050 ? 156.347 150.467 150.817 1.00 32.28  ? 4050 ASP A CG    1 
ATOM   18405 O  OD1   . ASP A 1 4050 ? 156.079 150.553 152.033 1.00 29.64  ? 4050 ASP A OD1   1 
ATOM   18406 O  OD2   . ASP A 1 4050 ? 155.474 150.387 149.929 1.00 29.86  ? 4050 ASP A OD2   1 
ATOM   18407 N  N     . ALA A 1 4051 ? 157.414 147.427 151.924 1.00 27.33  ? 4051 ALA A N     1 
ATOM   18408 C  CA    . ALA A 1 4051 ? 156.794 146.113 151.861 1.00 25.92  ? 4051 ALA A CA    1 
ATOM   18409 C  C     . ALA A 1 4051 ? 155.290 146.173 151.630 1.00 25.30  ? 4051 ALA A C     1 
ATOM   18410 O  O     . ALA A 1 4051 ? 154.649 145.121 151.554 1.00 29.64  ? 4051 ALA A O     1 
ATOM   18411 C  CB    . ALA A 1 4051 ? 157.091 145.332 153.144 1.00 22.05  ? 4051 ALA A CB    1 
ATOM   18412 N  N     . SER A 1 4052 ? 154.714 147.371 151.516 1.00 21.65  ? 4052 SER A N     1 
ATOM   18413 C  CA    . SER A 1 4052 ? 153.276 147.486 151.290 1.00 23.04  ? 4052 SER A CA    1 
ATOM   18414 C  C     . SER A 1 4052 ? 152.879 146.878 149.951 1.00 26.24  ? 4052 SER A C     1 
ATOM   18415 O  O     . SER A 1 4052 ? 151.832 146.225 149.838 1.00 25.74  ? 4052 SER A O     1 
ATOM   18416 C  CB    . SER A 1 4052 ? 152.855 148.953 151.366 1.00 25.43  ? 4052 SER A CB    1 
ATOM   18417 O  OG    . SER A 1 4052 ? 153.318 149.557 152.562 1.00 24.97  ? 4052 SER A OG    1 
ATOM   18418 N  N     . GLY A 1 4053 ? 153.703 147.090 148.921 1.00 21.84  ? 4053 GLY A N     1 
ATOM   18419 C  CA    . GLY A 1 4053 ? 153.416 146.508 147.621 1.00 20.72  ? 4053 GLY A CA    1 
ATOM   18420 C  C     . GLY A 1 4053 ? 153.402 144.994 147.653 1.00 23.71  ? 4053 GLY A C     1 
ATOM   18421 O  O     . GLY A 1 4053 ? 152.598 144.358 146.971 1.00 28.26  ? 4053 GLY A O     1 
ATOM   18422 N  N     . HIS A 1 4054 ? 154.290 144.396 148.449 1.00 23.62  ? 4054 HIS A N     1 
ATOM   18423 C  CA    . HIS A 1 4054 ? 154.296 142.945 148.588 1.00 21.50  ? 4054 HIS A CA    1 
ATOM   18424 C  C     . HIS A 1 4054 ? 152.993 142.444 149.197 1.00 22.76  ? 4054 HIS A C     1 
ATOM   18425 O  O     . HIS A 1 4054 ? 152.427 141.446 148.736 1.00 25.82  ? 4054 HIS A O     1 
ATOM   18426 C  CB    . HIS A 1 4054 ? 155.489 142.509 149.436 1.00 24.22  ? 4054 HIS A CB    1 
ATOM   18427 C  CG    . HIS A 1 4054 ? 156.816 142.890 148.855 1.00 33.14  ? 4054 HIS A CG    1 
ATOM   18428 N  ND1   . HIS A 1 4054 ? 157.932 143.108 149.632 1.00 38.99  ? 4054 HIS A ND1   1 
ATOM   18429 C  CD2   . HIS A 1 4054 ? 157.206 143.087 147.573 1.00 31.67  ? 4054 HIS A CD2   1 
ATOM   18430 C  CE1   . HIS A 1 4054 ? 158.953 143.422 148.856 1.00 39.74  ? 4054 HIS A CE1   1 
ATOM   18431 N  NE2   . HIS A 1 4054 ? 158.540 143.417 147.602 1.00 48.71  ? 4054 HIS A NE2   1 
ATOM   18432 N  N     . VAL A 1 4055 ? 152.502 143.121 150.235 1.00 26.15  ? 4055 VAL A N     1 
ATOM   18433 C  CA    . VAL A 1 4055 ? 151.254 142.700 150.861 1.00 22.63  ? 4055 VAL A CA    1 
ATOM   18434 C  C     . VAL A 1 4055 ? 150.095 142.858 149.890 1.00 24.07  ? 4055 VAL A C     1 
ATOM   18435 O  O     . VAL A 1 4055 ? 149.223 141.986 149.798 1.00 26.74  ? 4055 VAL A O     1 
ATOM   18436 C  CB    . VAL A 1 4055 ? 151.012 143.494 152.155 1.00 20.14  ? 4055 VAL A CB    1 
ATOM   18437 C  CG1   . VAL A 1 4055 ? 149.829 142.931 152.922 1.00 14.90  ? 4055 VAL A CG1   1 
ATOM   18438 C  CG2   . VAL A 1 4055 ? 152.258 143.506 153.014 1.00 20.62  ? 4055 VAL A CG2   1 
ATOM   18439 N  N     . GLU A 1 4056 ? 150.055 143.977 149.164 1.00 25.31  ? 4056 GLU A N     1 
ATOM   18440 C  CA    . GLU A 1 4056 ? 148.989 144.177 148.188 1.00 26.56  ? 4056 GLU A CA    1 
ATOM   18441 C  C     . GLU A 1 4056 ? 149.021 143.102 147.109 1.00 28.32  ? 4056 GLU A C     1 
ATOM   18442 O  O     . GLU A 1 4056 ? 147.979 142.537 146.751 1.00 26.54  ? 4056 GLU A O     1 
ATOM   18443 C  CB    . GLU A 1 4056 ? 149.110 145.567 147.567 1.00 31.66  ? 4056 GLU A CB    1 
ATOM   18444 C  CG    . GLU A 1 4056 ? 148.714 146.695 148.511 1.00 33.46  ? 4056 GLU A CG    1 
ATOM   18445 C  CD    . GLU A 1 4056 ? 149.273 148.052 148.098 1.00 48.02  ? 4056 GLU A CD    1 
ATOM   18446 O  OE1   . GLU A 1 4056 ? 149.722 148.198 146.943 1.00 43.02  ? 4056 GLU A OE1   1 
ATOM   18447 O  OE2   . GLU A 1 4056 ? 149.255 148.982 148.932 1.00 52.17  ? 4056 GLU A OE2   1 
ATOM   18448 N  N     . ASP A 1 4057 ? 150.212 142.800 146.585 1.00 29.33  ? 4057 ASP A N     1 
ATOM   18449 C  CA    . ASP A 1 4057 ? 150.330 141.778 145.553 1.00 31.32  ? 4057 ASP A CA    1 
ATOM   18450 C  C     . ASP A 1 4057 ? 149.905 140.417 146.076 1.00 31.07  ? 4057 ASP A C     1 
ATOM   18451 O  O     . ASP A 1 4057 ? 149.184 139.684 145.392 1.00 39.04  ? 4057 ASP A O     1 
ATOM   18452 C  CB    . ASP A 1 4057 ? 151.762 141.722 145.019 1.00 31.03  ? 4057 ASP A CB    1 
ATOM   18453 C  CG    . ASP A 1 4057 ? 152.136 142.950 144.214 1.00 46.70  ? 4057 ASP A CG    1 
ATOM   18454 O  OD1   . ASP A 1 4057 ? 151.237 143.560 143.599 1.00 45.24  ? 4057 ASP A OD1   1 
ATOM   18455 O  OD2   . ASP A 1 4057 ? 153.335 143.301 144.196 1.00 39.89  ? 4057 ASP A OD2   1 
ATOM   18456 N  N     . LEU A 1 4058 ? 150.335 140.062 147.289 1.00 25.29  ? 4058 LEU A N     1 
ATOM   18457 C  CA    . LEU A 1 4058 ? 149.997 138.753 147.833 1.00 25.29  ? 4058 LEU A CA    1 
ATOM   18458 C  C     . LEU A 1 4058 ? 148.503 138.638 148.100 1.00 27.77  ? 4058 LEU A C     1 
ATOM   18459 O  O     . LEU A 1 4058 ? 147.903 137.584 147.861 1.00 38.57  ? 4058 LEU A O     1 
ATOM   18460 C  CB    . LEU A 1 4058 ? 150.807 138.490 149.103 1.00 22.32  ? 4058 LEU A CB    1 
ATOM   18461 C  CG    . LEU A 1 4058 ? 150.742 137.088 149.716 1.00 25.80  ? 4058 LEU A CG    1 
ATOM   18462 C  CD1   . LEU A 1 4058 ? 152.021 136.800 150.458 1.00 27.97  ? 4058 LEU A CD1   1 
ATOM   18463 C  CD2   . LEU A 1 4058 ? 149.572 136.922 150.661 1.00 28.97  ? 4058 LEU A CD2   1 
ATOM   18464 N  N     . ALA A 1 4059 ? 147.885 139.708 148.607 1.00 24.96  ? 4059 ALA A N     1 
ATOM   18465 C  CA    . ALA A 1 4059 ? 146.440 139.701 148.802 1.00 24.29  ? 4059 ALA A CA    1 
ATOM   18466 C  C     . ALA A 1 4059 ? 145.710 139.561 147.473 1.00 33.33  ? 4059 ALA A C     1 
ATOM   18467 O  O     . ALA A 1 4059 ? 144.670 138.897 147.396 1.00 32.44  ? 4059 ALA A O     1 
ATOM   18468 C  CB    . ALA A 1 4059 ? 146.001 140.970 149.530 1.00 21.29  ? 4059 ALA A CB    1 
ATOM   18469 N  N     . ALA A 1 4060 ? 146.236 140.187 146.418 1.00 33.31  ? 4060 ALA A N     1 
ATOM   18470 C  CA    . ALA A 1 4060 ? 145.654 140.007 145.093 1.00 29.49  ? 4060 ALA A CA    1 
ATOM   18471 C  C     . ALA A 1 4060 ? 145.788 138.568 144.608 1.00 35.35  ? 4060 ALA A C     1 
ATOM   18472 O  O     . ALA A 1 4060 ? 144.865 138.043 143.975 1.00 45.86  ? 4060 ALA A O     1 
ATOM   18473 C  CB    . ALA A 1 4060 ? 146.306 140.965 144.099 1.00 30.55  ? 4060 ALA A CB    1 
ATOM   18474 N  N     . GLU A 1 4061 ? 146.926 137.924 144.881 1.00 33.24  ? 4061 GLU A N     1 
ATOM   18475 C  CA    . GLU A 1 4061 ? 147.130 136.548 144.431 1.00 37.02  ? 4061 GLU A CA    1 
ATOM   18476 C  C     . GLU A 1 4061 ? 146.154 135.586 145.096 1.00 34.48  ? 4061 GLU A C     1 
ATOM   18477 O  O     . GLU A 1 4061 ? 145.620 134.684 144.441 1.00 39.33  ? 4061 GLU A O     1 
ATOM   18478 C  CB    . GLU A 1 4061 ? 148.571 136.111 144.701 1.00 43.79  ? 4061 GLU A CB    1 
ATOM   18479 C  CG    . GLU A 1 4061 ? 149.644 136.956 144.022 1.00 51.11  ? 4061 GLU A CG    1 
ATOM   18480 C  CD    . GLU A 1 4061 ? 149.813 136.647 142.543 1.00 59.72  ? 4061 GLU A CD    1 
ATOM   18481 O  OE1   . GLU A 1 4061 ? 148.871 136.117 141.918 1.00 56.41  ? 4061 GLU A OE1   1 
ATOM   18482 O  OE2   . GLU A 1 4061 ? 150.901 136.936 142.002 1.00 67.42  ? 4061 GLU A OE2   1 
ATOM   18483 N  N     . GLN A 1 4062 ? 145.911 135.758 146.392 1.00 37.73  ? 4062 GLN A N     1 
ATOM   18484 C  CA    . GLN A 1 4062 ? 145.052 134.858 147.149 1.00 35.12  ? 4062 GLN A CA    1 
ATOM   18485 C  C     . GLN A 1 4062 ? 143.575 135.195 147.022 1.00 39.17  ? 4062 GLN A C     1 
ATOM   18486 O  O     . GLN A 1 4062 ? 142.745 134.487 147.603 1.00 41.01  ? 4062 GLN A O     1 
ATOM   18487 C  CB    . GLN A 1 4062 ? 145.447 134.870 148.630 1.00 32.08  ? 4062 GLN A CB    1 
ATOM   18488 C  CG    . GLN A 1 4062 ? 146.790 134.232 148.929 1.00 31.99  ? 4062 GLN A CG    1 
ATOM   18489 C  CD    . GLN A 1 4062 ? 146.945 133.876 150.393 1.00 48.88  ? 4062 GLN A CD    1 
ATOM   18490 O  OE1   . GLN A 1 4062 ? 148.020 134.028 150.972 1.00 51.84  ? 4062 GLN A OE1   1 
ATOM   18491 N  NE2   . GLN A 1 4062 ? 145.865 133.400 151.002 1.00 42.52  ? 4062 GLN A NE2   1 
ATOM   18492 N  N     . ASN A 1 4063 ? 143.232 136.249 146.279 1.00 37.77  ? 4063 ASN A N     1 
ATOM   18493 C  CA    . ASN A 1 4063 ? 141.857 136.737 146.175 1.00 38.90  ? 4063 ASN A CA    1 
ATOM   18494 C  C     . ASN A 1 4063 ? 141.308 137.006 147.579 1.00 37.66  ? 4063 ASN A C     1 
ATOM   18495 O  O     . ASN A 1 4063 ? 140.307 136.435 148.017 1.00 35.99  ? 4063 ASN A O     1 
ATOM   18496 C  CB    . ASN A 1 4063 ? 140.984 135.756 145.376 1.00 43.53  ? 4063 ASN A CB    1 
ATOM   18497 C  CG    . ASN A 1 4063 ? 139.496 136.074 145.447 1.00 50.81  ? 4063 ASN A CG    1 
ATOM   18498 O  OD1   . ASN A 1 4063 ? 139.100 137.231 145.589 1.00 51.04  ? 4063 ASN A OD1   1 
ATOM   18499 N  ND2   . ASN A 1 4063 ? 138.667 135.041 145.350 1.00 49.63  ? 4063 ASN A ND2   1 
ATOM   18500 N  N     . THR A 1 4064 ? 142.028 137.846 148.317 1.00 32.52  ? 4064 THR A N     1 
ATOM   18501 C  CA    . THR A 1 4064 ? 141.649 138.247 149.663 1.00 33.56  ? 4064 THR A CA    1 
ATOM   18502 C  C     . THR A 1 4064 ? 141.512 139.761 149.703 1.00 33.34  ? 4064 THR A C     1 
ATOM   18503 O  O     . THR A 1 4064 ? 142.427 140.481 149.291 1.00 35.46  ? 4064 THR A O     1 
ATOM   18504 C  CB    . THR A 1 4064 ? 142.682 137.782 150.694 1.00 29.36  ? 4064 THR A CB    1 
ATOM   18505 O  OG1   . THR A 1 4064 ? 142.939 136.383 150.521 1.00 33.22  ? 4064 THR A OG1   1 
ATOM   18506 C  CG2   . THR A 1 4064 ? 142.171 138.024 152.104 1.00 25.93  ? 4064 THR A CG2   1 
ATOM   18507 N  N     . GLN A 1 4065 ? 140.372 140.240 150.190 1.00 30.55  ? 4065 GLN A N     1 
ATOM   18508 C  CA    . GLN A 1 4065 ? 140.169 141.676 150.309 1.00 37.42  ? 4065 GLN A CA    1 
ATOM   18509 C  C     . GLN A 1 4065 ? 140.953 142.215 151.497 1.00 35.30  ? 4065 GLN A C     1 
ATOM   18510 O  O     . GLN A 1 4065 ? 140.871 141.679 152.606 1.00 34.65  ? 4065 GLN A O     1 
ATOM   18511 C  CB    . GLN A 1 4065 ? 138.683 141.994 150.456 1.00 31.67  ? 4065 GLN A CB    1 
ATOM   18512 C  CG    . GLN A 1 4065 ? 137.951 142.151 149.130 1.00 37.92  ? 4065 GLN A CG    1 
ATOM   18513 C  CD    . GLN A 1 4065 ? 138.787 142.848 148.069 1.00 46.39  ? 4065 GLN A CD    1 
ATOM   18514 O  OE1   . GLN A 1 4065 ? 139.336 143.927 148.299 1.00 44.76  ? 4065 GLN A OE1   1 
ATOM   18515 N  NE2   . GLN A 1 4065 ? 138.890 142.228 146.899 1.00 38.31  ? 4065 GLN A NE2   1 
ATOM   18516 N  N     . ILE A 1 4066 ? 141.717 143.279 151.264 1.00 26.89  ? 4066 ILE A N     1 
ATOM   18517 C  CA    . ILE A 1 4066 ? 142.578 143.865 152.281 1.00 23.32  ? 4066 ILE A CA    1 
ATOM   18518 C  C     . ILE A 1 4066 ? 142.296 145.357 152.373 1.00 27.28  ? 4066 ILE A C     1 
ATOM   18519 O  O     . ILE A 1 4066 ? 142.132 146.037 151.354 1.00 29.53  ? 4066 ILE A O     1 
ATOM   18520 C  CB    . ILE A 1 4066 ? 144.071 143.601 151.987 1.00 22.31  ? 4066 ILE A CB    1 
ATOM   18521 C  CG1   . ILE A 1 4066 ? 144.945 144.181 153.099 1.00 20.76  ? 4066 ILE A CG1   1 
ATOM   18522 C  CG2   . ILE A 1 4066 ? 144.470 144.152 150.624 1.00 21.24  ? 4066 ILE A CG2   1 
ATOM   18523 C  CD1   . ILE A 1 4066 ? 146.414 143.984 152.877 1.00 18.12  ? 4066 ILE A CD1   1 
ATOM   18524 N  N     . THR A 1 4067 ? 142.217 145.858 153.602 1.00 24.93  ? 4067 THR A N     1 
ATOM   18525 C  CA    . THR A 1 4067 ? 142.064 147.281 153.867 1.00 20.59  ? 4067 THR A CA    1 
ATOM   18526 C  C     . THR A 1 4067 ? 143.420 147.849 154.263 1.00 20.32  ? 4067 THR A C     1 
ATOM   18527 O  O     . THR A 1 4067 ? 144.005 147.422 155.263 1.00 22.15  ? 4067 THR A O     1 
ATOM   18528 C  CB    . THR A 1 4067 ? 141.037 147.531 154.970 1.00 25.89  ? 4067 THR A CB    1 
ATOM   18529 O  OG1   . THR A 1 4067 ? 139.729 147.191 154.496 1.00 35.69  ? 4067 THR A OG1   1 
ATOM   18530 C  CG2   . THR A 1 4067 ? 141.054 148.991 155.390 1.00 20.13  ? 4067 THR A CG2   1 
ATOM   18531 N  N     . SER A 1 4068 ? 143.916 148.801 153.481 1.00 22.74  ? 4068 SER A N     1 
ATOM   18532 C  CA    . SER A 1 4068 ? 145.204 149.433 153.730 1.00 16.19  ? 4068 SER A CA    1 
ATOM   18533 C  C     . SER A 1 4068 ? 144.983 150.833 154.284 1.00 14.31  ? 4068 SER A C     1 
ATOM   18534 O  O     . SER A 1 4068 ? 144.221 151.619 153.712 1.00 19.21  ? 4068 SER A O     1 
ATOM   18535 C  CB    . SER A 1 4068 ? 146.039 149.494 152.451 1.00 20.53  ? 4068 SER A CB    1 
ATOM   18536 O  OG    . SER A 1 4068 ? 146.123 148.220 151.838 1.00 26.14  ? 4068 SER A OG    1 
ATOM   18537 N  N     . ILE A 1 4069 ? 145.644 151.137 155.397 1.00 14.64  ? 4069 ILE A N     1 
ATOM   18538 C  CA    . ILE A 1 4069 ? 145.502 152.419 156.075 1.00 13.50  ? 4069 ILE A CA    1 
ATOM   18539 C  C     . ILE A 1 4069 ? 146.890 152.951 156.399 1.00 16.04  ? 4069 ILE A C     1 
ATOM   18540 O  O     . ILE A 1 4069 ? 147.741 152.212 156.905 1.00 14.56  ? 4069 ILE A O     1 
ATOM   18541 C  CB    . ILE A 1 4069 ? 144.653 152.296 157.354 1.00 16.03  ? 4069 ILE A CB    1 
ATOM   18542 C  CG1   . ILE A 1 4069 ? 143.219 151.900 157.001 1.00 17.30  ? 4069 ILE A CG1   1 
ATOM   18543 C  CG2   . ILE A 1 4069 ? 144.670 153.597 158.139 1.00 15.56  ? 4069 ILE A CG2   1 
ATOM   18544 C  CD1   . ILE A 1 4069 ? 142.518 151.129 158.082 1.00 18.23  ? 4069 ILE A CD1   1 
ATOM   18545 N  N     . ALA A 1 4070 ? 147.116 154.228 156.107 1.00 14.75  ? 4070 ALA A N     1 
ATOM   18546 C  CA    . ALA A 1 4070 ? 148.384 154.880 156.401 1.00 10.94  ? 4070 ALA A CA    1 
ATOM   18547 C  C     . ALA A 1 4070 ? 148.285 155.588 157.746 1.00 15.41  ? 4070 ALA A C     1 
ATOM   18548 O  O     . ALA A 1 4070 ? 147.359 156.373 157.976 1.00 22.37  ? 4070 ALA A O     1 
ATOM   18549 C  CB    . ALA A 1 4070 ? 148.751 155.864 155.294 1.00 11.82  ? 4070 ALA A CB    1 
ATOM   18550 N  N     . ILE A 1 4071 ? 149.236 155.312 158.625 1.00 13.60  ? 4071 ILE A N     1 
ATOM   18551 C  CA    . ILE A 1 4071 ? 149.225 155.851 159.979 1.00 14.69  ? 4071 ILE A CA    1 
ATOM   18552 C  C     . ILE A 1 4071 ? 149.760 157.277 159.964 1.00 21.38  ? 4071 ILE A C     1 
ATOM   18553 O  O     . ILE A 1 4071 ? 150.593 157.643 159.127 1.00 18.62  ? 4071 ILE A O     1 
ATOM   18554 C  CB    . ILE A 1 4071 ? 150.045 154.931 160.909 1.00 10.41  ? 4071 ILE A CB    1 
ATOM   18555 C  CG1   . ILE A 1 4071 ? 149.397 153.549 160.984 1.00 13.52  ? 4071 ILE A CG1   1 
ATOM   18556 C  CG2   . ILE A 1 4071 ? 150.181 155.514 162.304 1.00 11.09  ? 4071 ILE A CG2   1 
ATOM   18557 C  CD1   . ILE A 1 4071 ? 147.966 153.572 161.462 1.00 12.56  ? 4071 ILE A CD1   1 
ATOM   18558 N  N     . GLY A 1 4072 ? 149.277 158.098 160.896 1.00 21.63  ? 4072 GLY A N     1 
ATOM   18559 C  CA    . GLY A 1 4072 ? 149.780 159.449 161.033 1.00 15.22  ? 4072 GLY A CA    1 
ATOM   18560 C  C     . GLY A 1 4072 ? 148.754 160.492 161.424 1.00 18.13  ? 4072 GLY A C     1 
ATOM   18561 O  O     . GLY A 1 4072 ? 149.108 161.521 162.007 1.00 24.43  ? 4072 GLY A O     1 
ATOM   18562 N  N     . SER A 1 4073 ? 147.484 160.246 161.122 1.00 26.27  ? 4073 SER A N     1 
ATOM   18563 C  CA    . SER A 1 4073 ? 146.414 161.175 161.445 1.00 24.47  ? 4073 SER A CA    1 
ATOM   18564 C  C     . SER A 1 4073 ? 145.430 160.522 162.407 1.00 29.65  ? 4073 SER A C     1 
ATOM   18565 O  O     . SER A 1 4073 ? 145.370 159.295 162.531 1.00 30.13  ? 4073 SER A O     1 
ATOM   18566 C  CB    . SER A 1 4073 ? 145.680 161.644 160.182 1.00 14.95  ? 4073 SER A CB    1 
ATOM   18567 O  OG    . SER A 1 4073 ? 145.126 160.549 159.475 1.00 20.66  ? 4073 SER A OG    1 
ATOM   18568 N  N     . ALA A 1 4074 ? 144.662 161.365 163.104 1.00 26.70  ? 4074 ALA A N     1 
ATOM   18569 C  CA    . ALA A 1 4074 ? 143.639 160.856 164.013 1.00 31.05  ? 4074 ALA A CA    1 
ATOM   18570 C  C     . ALA A 1 4074 ? 142.582 160.062 163.258 1.00 26.68  ? 4074 ALA A C     1 
ATOM   18571 O  O     . ALA A 1 4074 ? 142.146 158.995 163.714 1.00 29.94  ? 4074 ALA A O     1 
ATOM   18572 C  CB    . ALA A 1 4074 ? 142.999 162.011 164.782 1.00 26.90  ? 4074 ALA A CB    1 
ATOM   18573 N  N     . GLU A 1 4075 ? 142.153 160.572 162.101 1.00 25.49  ? 4075 GLU A N     1 
ATOM   18574 C  CA    . GLU A 1 4075 ? 141.264 159.803 161.240 1.00 28.64  ? 4075 GLU A CA    1 
ATOM   18575 C  C     . GLU A 1 4075 ? 141.900 158.483 160.838 1.00 29.16  ? 4075 GLU A C     1 
ATOM   18576 O  O     . GLU A 1 4075 ? 141.198 157.477 160.692 1.00 27.27  ? 4075 GLU A O     1 
ATOM   18577 C  CB    . GLU A 1 4075 ? 140.894 160.619 160.000 1.00 28.03  ? 4075 GLU A CB    1 
ATOM   18578 C  CG    . GLU A 1 4075 ? 140.463 162.050 160.293 1.00 37.32  ? 4075 GLU A CG    1 
ATOM   18579 C  CD    . GLU A 1 4075 ? 141.601 163.046 160.177 1.00 42.54  ? 4075 GLU A CD    1 
ATOM   18580 O  OE1   . GLU A 1 4075 ? 142.721 162.726 160.622 1.00 44.59  ? 4075 GLU A OE1   1 
ATOM   18581 O  OE2   . GLU A 1 4075 ? 141.375 164.150 159.640 1.00 34.67  ? 4075 GLU A OE2   1 
ATOM   18582 N  N     . GLY A 1 4076 ? 143.223 158.463 160.671 1.00 30.96  ? 4076 GLY A N     1 
ATOM   18583 C  CA    . GLY A 1 4076 ? 143.905 157.212 160.388 1.00 24.11  ? 4076 GLY A CA    1 
ATOM   18584 C  C     . GLY A 1 4076 ? 143.777 156.209 161.518 1.00 20.88  ? 4076 GLY A C     1 
ATOM   18585 O  O     . GLY A 1 4076 ? 143.532 155.026 161.282 1.00 28.16  ? 4076 GLY A O     1 
ATOM   18586 N  N     . PHE A 1 4077 ? 143.938 156.668 162.762 1.00 23.20  ? 4077 PHE A N     1 
ATOM   18587 C  CA    . PHE A 1 4077 ? 143.778 155.774 163.906 1.00 17.52  ? 4077 PHE A CA    1 
ATOM   18588 C  C     . PHE A 1 4077 ? 142.347 155.264 164.015 1.00 21.25  ? 4077 PHE A C     1 
ATOM   18589 O  O     . PHE A 1 4077 ? 142.124 154.080 164.300 1.00 25.36  ? 4077 PHE A O     1 
ATOM   18590 C  CB    . PHE A 1 4077 ? 144.187 156.485 165.195 1.00 14.28  ? 4077 PHE A CB    1 
ATOM   18591 C  CG    . PHE A 1 4077 ? 145.633 156.881 165.237 1.00 19.44  ? 4077 PHE A CG    1 
ATOM   18592 C  CD1   . PHE A 1 4077 ? 146.625 155.962 164.945 1.00 19.05  ? 4077 PHE A CD1   1 
ATOM   18593 C  CD2   . PHE A 1 4077 ? 146.000 158.172 165.568 1.00 20.62  ? 4077 PHE A CD2   1 
ATOM   18594 C  CE1   . PHE A 1 4077 ? 147.955 156.324 164.985 1.00 16.56  ? 4077 PHE A CE1   1 
ATOM   18595 C  CE2   . PHE A 1 4077 ? 147.328 158.540 165.607 1.00 20.23  ? 4077 PHE A CE2   1 
ATOM   18596 C  CZ    . PHE A 1 4077 ? 148.306 157.614 165.316 1.00 17.21  ? 4077 PHE A CZ    1 
ATOM   18597 N  N     . ASN A 1 4078 ? 141.365 156.143 163.803 1.00 19.32  ? 4078 ASN A N     1 
ATOM   18598 C  CA    . ASN A 1 4078 ? 139.972 155.709 163.853 1.00 18.31  ? 4078 ASN A CA    1 
ATOM   18599 C  C     . ASN A 1 4078 ? 139.678 154.679 162.769 1.00 21.13  ? 4078 ASN A C     1 
ATOM   18600 O  O     . ASN A 1 4078 ? 139.014 153.664 163.024 1.00 23.29  ? 4078 ASN A O     1 
ATOM   18601 C  CB    . ASN A 1 4078 ? 139.044 156.916 163.720 1.00 23.01  ? 4078 ASN A CB    1 
ATOM   18602 C  CG    . ASN A 1 4078 ? 138.904 157.687 165.017 1.00 27.68  ? 4078 ASN A CG    1 
ATOM   18603 O  OD1   . ASN A 1 4078 ? 139.780 158.468 165.386 1.00 27.34  ? 4078 ASN A OD1   1 
ATOM   18604 N  ND2   . ASN A 1 4078 ? 137.797 157.468 165.718 1.00 34.87  ? 4078 ASN A ND2   1 
ATOM   18605 N  N     . GLN A 1 4079 ? 140.175 154.919 161.552 1.00 23.72  ? 4079 GLN A N     1 
ATOM   18606 C  CA    . GLN A 1 4079 ? 139.988 153.965 160.467 1.00 20.62  ? 4079 GLN A CA    1 
ATOM   18607 C  C     . GLN A 1 4079 ? 140.665 152.639 160.776 1.00 19.34  ? 4079 GLN A C     1 
ATOM   18608 O  O     . GLN A 1 4079 ? 140.115 151.574 160.484 1.00 25.92  ? 4079 GLN A O     1 
ATOM   18609 C  CB    . GLN A 1 4079 ? 140.527 154.545 159.160 1.00 22.14  ? 4079 GLN A CB    1 
ATOM   18610 C  CG    . GLN A 1 4079 ? 139.841 154.010 157.917 1.00 27.59  ? 4079 GLN A CG    1 
ATOM   18611 C  CD    . GLN A 1 4079 ? 140.572 154.384 156.645 1.00 37.93  ? 4079 GLN A CD    1 
ATOM   18612 O  OE1   . GLN A 1 4079 ? 141.183 155.449 156.556 1.00 33.07  ? 4079 GLN A OE1   1 
ATOM   18613 N  NE2   . GLN A 1 4079 ? 140.514 153.507 155.651 1.00 36.15  ? 4079 GLN A NE2   1 
ATOM   18614 N  N     . ALA A 1 4080 ? 141.867 152.683 161.355 1.00 17.76  ? 4080 ALA A N     1 
ATOM   18615 C  CA    . ALA A 1 4080 ? 142.568 151.453 161.703 1.00 19.29  ? 4080 ALA A CA    1 
ATOM   18616 C  C     . ALA A 1 4080 ? 141.793 150.652 162.738 1.00 21.32  ? 4080 ALA A C     1 
ATOM   18617 O  O     . ALA A 1 4080 ? 141.646 149.431 162.606 1.00 26.75  ? 4080 ALA A O     1 
ATOM   18618 C  CB    . ALA A 1 4080 ? 143.972 151.776 162.213 1.00 14.92  ? 4080 ALA A CB    1 
ATOM   18619 N  N     . ASP A 1 4081 ? 141.283 151.323 163.773 1.00 21.96  ? 4081 ASP A N     1 
ATOM   18620 C  CA    . ASP A 1 4081 ? 140.504 150.627 164.792 1.00 21.60  ? 4081 ASP A CA    1 
ATOM   18621 C  C     . ASP A 1 4081 ? 139.252 150.003 164.190 1.00 19.95  ? 4081 ASP A C     1 
ATOM   18622 O  O     . ASP A 1 4081 ? 138.937 148.836 164.453 1.00 22.73  ? 4081 ASP A O     1 
ATOM   18623 C  CB    . ASP A 1 4081 ? 140.136 151.589 165.921 1.00 26.02  ? 4081 ASP A CB    1 
ATOM   18624 C  CG    . ASP A 1 4081 ? 141.337 152.014 166.738 1.00 38.52  ? 4081 ASP A CG    1 
ATOM   18625 O  OD1   . ASP A 1 4081 ? 142.300 151.225 166.837 1.00 38.36  ? 4081 ASP A OD1   1 
ATOM   18626 O  OD2   . ASP A 1 4081 ? 141.318 153.137 167.285 1.00 39.28  ? 4081 ASP A OD2   1 
ATOM   18627 N  N     . LYS A 1 4082 ? 138.532 150.766 163.362 1.00 23.70  ? 4082 LYS A N     1 
ATOM   18628 C  CA    . LYS A 1 4082 ? 137.314 150.245 162.751 1.00 24.00  ? 4082 LYS A CA    1 
ATOM   18629 C  C     . LYS A 1 4082 ? 137.614 149.061 161.838 1.00 21.45  ? 4082 LYS A C     1 
ATOM   18630 O  O     . LYS A 1 4082 ? 136.902 148.048 161.865 1.00 24.16  ? 4082 LYS A O     1 
ATOM   18631 C  CB    . LYS A 1 4082 ? 136.609 151.360 161.978 1.00 21.07  ? 4082 LYS A CB    1 
ATOM   18632 C  CG    . LYS A 1 4082 ? 135.259 150.976 161.404 1.00 33.65  ? 4082 LYS A CG    1 
ATOM   18633 C  CD    . LYS A 1 4082 ? 134.668 152.122 160.600 1.00 37.17  ? 4082 LYS A CD    1 
ATOM   18634 C  CE    . LYS A 1 4082 ? 134.167 153.233 161.507 1.00 44.30  ? 4082 LYS A CE    1 
ATOM   18635 N  NZ    . LYS A 1 4082 ? 133.480 154.310 160.740 1.00 39.01  ? 4082 LYS A NZ    1 
ATOM   18636 N  N     . ALA A 1 4083 ? 138.674 149.164 161.033 1.00 21.23  ? 4083 ALA A N     1 
ATOM   18637 C  CA    . ALA A 1 4083 ? 139.023 148.090 160.112 1.00 23.84  ? 4083 ALA A CA    1 
ATOM   18638 C  C     . ALA A 1 4083 ? 139.434 146.830 160.858 1.00 22.84  ? 4083 ALA A C     1 
ATOM   18639 O  O     . ALA A 1 4083 ? 139.038 145.723 160.478 1.00 21.92  ? 4083 ALA A O     1 
ATOM   18640 C  CB    . ALA A 1 4083 ? 140.141 148.547 159.176 1.00 19.59  ? 4083 ALA A CB    1 
ATOM   18641 N  N     . ILE A 1 4084 ? 140.230 146.974 161.920 1.00 21.33  ? 4084 ILE A N     1 
ATOM   18642 C  CA    . ILE A 1 4084 ? 140.637 145.807 162.698 1.00 19.74  ? 4084 ILE A CA    1 
ATOM   18643 C  C     . ILE A 1 4084 ? 139.427 145.162 163.360 1.00 22.02  ? 4084 ILE A C     1 
ATOM   18644 O  O     . ILE A 1 4084 ? 139.284 143.932 163.360 1.00 21.78  ? 4084 ILE A O     1 
ATOM   18645 C  CB    . ILE A 1 4084 ? 141.712 146.197 163.729 1.00 19.18  ? 4084 ILE A CB    1 
ATOM   18646 C  CG1   . ILE A 1 4084 ? 143.022 146.550 163.023 1.00 17.51  ? 4084 ILE A CG1   1 
ATOM   18647 C  CG2   . ILE A 1 4084 ? 141.936 145.070 164.724 1.00 17.53  ? 4084 ILE A CG2   1 
ATOM   18648 C  CD1   . ILE A 1 4084 ? 144.065 147.143 163.938 1.00 13.20  ? 4084 ILE A CD1   1 
ATOM   18649 N  N     . ASN A 1 4085 ? 138.534 145.978 163.927 1.00 24.52  ? 4085 ASN A N     1 
ATOM   18650 C  CA    . ASN A 1 4085 ? 137.350 145.434 164.582 1.00 18.46  ? 4085 ASN A CA    1 
ATOM   18651 C  C     . ASN A 1 4085 ? 136.460 144.695 163.592 1.00 19.05  ? 4085 ASN A C     1 
ATOM   18652 O  O     . ASN A 1 4085 ? 135.875 143.658 163.926 1.00 22.27  ? 4085 ASN A O     1 
ATOM   18653 C  CB    . ASN A 1 4085 ? 136.573 146.554 165.273 1.00 20.00  ? 4085 ASN A CB    1 
ATOM   18654 C  CG    . ASN A 1 4085 ? 137.264 147.050 166.525 1.00 25.91  ? 4085 ASN A CG    1 
ATOM   18655 O  OD1   . ASN A 1 4085 ? 138.268 146.487 166.956 1.00 24.27  ? 4085 ASN A OD1   1 
ATOM   18656 N  ND2   . ASN A 1 4085 ? 136.730 148.112 167.115 1.00 26.62  ? 4085 ASN A ND2   1 
ATOM   18657 N  N     . THR A 1 4086 ? 136.338 145.215 162.370 1.00 21.76  ? 4086 THR A N     1 
ATOM   18658 C  CA    . THR A 1 4086 ? 135.540 144.526 161.361 1.00 22.21  ? 4086 THR A CA    1 
ATOM   18659 C  C     . THR A 1 4086 ? 136.217 143.240 160.898 1.00 25.75  ? 4086 THR A C     1 
ATOM   18660 O  O     . THR A 1 4086 ? 135.552 142.211 160.721 1.00 27.21  ? 4086 THR A O     1 
ATOM   18661 C  CB    . THR A 1 4086 ? 135.282 145.451 160.173 1.00 20.05  ? 4086 THR A CB    1 
ATOM   18662 O  OG1   . THR A 1 4086 ? 134.711 146.679 160.638 1.00 29.35  ? 4086 THR A OG1   1 
ATOM   18663 C  CG2   . THR A 1 4086 ? 134.327 144.799 159.189 1.00 21.94  ? 4086 THR A CG2   1 
ATOM   18664 N  N     . ALA A 1 4087 ? 137.537 143.275 160.703 1.00 23.65  ? 4087 ALA A N     1 
ATOM   18665 C  CA    . ALA A 1 4087 ? 138.238 142.148 160.101 1.00 19.67  ? 4087 ALA A CA    1 
ATOM   18666 C  C     . ALA A 1 4087 ? 138.449 140.993 161.071 1.00 21.19  ? 4087 ALA A C     1 
ATOM   18667 O  O     . ALA A 1 4087 ? 138.522 139.839 160.635 1.00 18.59  ? 4087 ALA A O     1 
ATOM   18668 C  CB    . ALA A 1 4087 ? 139.583 142.607 159.539 1.00 21.59  ? 4087 ALA A CB    1 
ATOM   18669 N  N     . VAL A 1 4088 ? 138.565 141.266 162.374 1.00 20.50  ? 4088 VAL A N     1 
ATOM   18670 C  CA    . VAL A 1 4088 ? 138.732 140.171 163.325 1.00 21.12  ? 4088 VAL A CA    1 
ATOM   18671 C  C     . VAL A 1 4088 ? 137.497 139.284 163.368 1.00 25.43  ? 4088 VAL A C     1 
ATOM   18672 O  O     . VAL A 1 4088 ? 137.582 138.125 163.788 1.00 30.12  ? 4088 VAL A O     1 
ATOM   18673 C  CB    . VAL A 1 4088 ? 139.076 140.698 164.734 1.00 18.51  ? 4088 VAL A CB    1 
ATOM   18674 C  CG1   . VAL A 1 4088 ? 140.445 141.351 164.735 1.00 16.32  ? 4088 VAL A CG1   1 
ATOM   18675 C  CG2   . VAL A 1 4088 ? 138.010 141.659 165.226 1.00 25.85  ? 4088 VAL A CG2   1 
ATOM   18676 N  N     . LYS A 1 4089 ? 136.346 139.800 162.942 1.00 24.04  ? 4089 LYS A N     1 
ATOM   18677 C  CA    . LYS A 1 4089 ? 135.126 139.011 162.831 1.00 25.10  ? 4089 LYS A CA    1 
ATOM   18678 C  C     . LYS A 1 4089 ? 134.875 138.506 161.418 1.00 23.81  ? 4089 LYS A C     1 
ATOM   18679 O  O     . LYS A 1 4089 ? 134.492 137.345 161.241 1.00 26.97  ? 4089 LYS A O     1 
ATOM   18680 C  CB    . LYS A 1 4089 ? 133.921 139.833 163.297 1.00 24.53  ? 4089 LYS A CB    1 
ATOM   18681 C  CG    . LYS A 1 4089 ? 133.675 139.781 164.792 1.00 27.45  ? 4089 LYS A CG    1 
ATOM   18682 C  CD    . LYS A 1 4089 ? 133.117 141.099 165.301 1.00 36.66  ? 4089 LYS A CD    1 
ATOM   18683 C  CE    . LYS A 1 4089 ? 133.099 141.141 166.820 1.00 43.47  ? 4089 LYS A CE    1 
ATOM   18684 N  NZ    . LYS A 1 4089 ? 132.283 142.275 167.332 1.00 55.03  ? 4089 LYS A NZ    1 
ATOM   18685 N  N     . SER A 1 4090 ? 135.080 139.349 160.404 1.00 22.60  ? 4090 SER A N     1 
ATOM   18686 C  CA    . SER A 1 4090 ? 134.818 138.938 159.029 1.00 22.06  ? 4090 SER A CA    1 
ATOM   18687 C  C     . SER A 1 4090 ? 135.890 138.001 158.489 1.00 20.87  ? 4090 SER A C     1 
ATOM   18688 O  O     . SER A 1 4090 ? 135.583 137.119 157.680 1.00 27.22  ? 4090 SER A O     1 
ATOM   18689 C  CB    . SER A 1 4090 ? 134.700 140.165 158.125 1.00 29.10  ? 4090 SER A CB    1 
ATOM   18690 O  OG    . SER A 1 4090 ? 135.908 140.904 158.110 1.00 28.83  ? 4090 SER A OG    1 
ATOM   18691 N  N     . GLY A 1 4091 ? 137.136 138.169 158.916 1.00 23.58  ? 4091 GLY A N     1 
ATOM   18692 C  CA    . GLY A 1 4091 ? 138.232 137.377 158.405 1.00 20.29  ? 4091 GLY A CA    1 
ATOM   18693 C  C     . GLY A 1 4091 ? 139.043 138.023 157.304 1.00 23.28  ? 4091 GLY A C     1 
ATOM   18694 O  O     . GLY A 1 4091 ? 139.855 137.335 156.677 1.00 20.37  ? 4091 GLY A O     1 
ATOM   18695 N  N     . ARG A 1 4092 ? 138.849 139.313 157.048 1.00 25.53  ? 4092 ARG A N     1 
ATOM   18696 C  CA    . ARG A 1 4092 ? 139.600 140.011 156.019 1.00 20.07  ? 4092 ARG A CA    1 
ATOM   18697 C  C     . ARG A 1 4092 ? 140.995 140.356 156.535 1.00 17.11  ? 4092 ARG A C     1 
ATOM   18698 O  O     . ARG A 1 4092 ? 141.382 140.002 157.651 1.00 14.01  ? 4092 ARG A O     1 
ATOM   18699 C  CB    . ARG A 1 4092 ? 138.846 141.261 155.571 1.00 26.15  ? 4092 ARG A CB    1 
ATOM   18700 C  CG    . ARG A 1 4092 ? 137.521 140.970 154.885 1.00 30.27  ? 4092 ARG A CG    1 
ATOM   18701 C  CD    . ARG A 1 4092 ? 136.797 142.248 154.477 1.00 42.75  ? 4092 ARG A CD    1 
ATOM   18702 N  NE    . ARG A 1 4092 ? 137.503 142.986 153.436 1.00 44.78  ? 4092 ARG A NE    1 
ATOM   18703 C  CZ    . ARG A 1 4092 ? 138.120 144.145 153.622 1.00 47.15  ? 4092 ARG A CZ    1 
ATOM   18704 N  NH1   . ARG A 1 4092 ? 138.159 144.724 154.811 1.00 45.96  ? 4092 ARG A NH1   1 
ATOM   18705 N  NH2   . ARG A 1 4092 ? 138.713 144.738 152.590 1.00 38.91  ? 4092 ARG A NH2   1 
ATOM   18706 N  N     . TRP A 1 4093 ? 141.764 141.060 155.710 1.00 24.41  ? 4093 TRP A N     1 
ATOM   18707 C  CA    . TRP A 1 4093 ? 143.126 141.446 156.047 1.00 15.84  ? 4093 TRP A CA    1 
ATOM   18708 C  C     . TRP A 1 4093 ? 143.213 142.953 156.242 1.00 18.43  ? 4093 TRP A C     1 
ATOM   18709 O  O     . TRP A 1 4093 ? 142.550 143.721 155.539 1.00 21.51  ? 4093 TRP A O     1 
ATOM   18710 C  CB    . TRP A 1 4093 ? 144.104 141.011 154.956 1.00 13.45  ? 4093 TRP A CB    1 
ATOM   18711 C  CG    . TRP A 1 4093 ? 144.319 139.536 154.888 1.00 14.20  ? 4093 TRP A CG    1 
ATOM   18712 C  CD1   . TRP A 1 4093 ? 143.641 138.575 155.577 1.00 14.71  ? 4093 TRP A CD1   1 
ATOM   18713 C  CD2   . TRP A 1 4093 ? 145.278 138.850 154.080 1.00 15.24  ? 4093 TRP A CD2   1 
ATOM   18714 N  NE1   . TRP A 1 4093 ? 144.120 137.332 155.249 1.00 15.75  ? 4093 TRP A NE1   1 
ATOM   18715 C  CE2   . TRP A 1 4093 ? 145.126 137.474 154.331 1.00 16.95  ? 4093 TRP A CE2   1 
ATOM   18716 C  CE3   . TRP A 1 4093 ? 146.251 139.265 153.168 1.00 16.86  ? 4093 TRP A CE3   1 
ATOM   18717 C  CZ2   . TRP A 1 4093 ? 145.910 136.512 153.704 1.00 18.41  ? 4093 TRP A CZ2   1 
ATOM   18718 C  CZ3   . TRP A 1 4093 ? 147.027 138.310 152.549 1.00 13.55  ? 4093 TRP A CZ3   1 
ATOM   18719 C  CH2   . TRP A 1 4093 ? 146.852 136.950 152.819 1.00 14.17  ? 4093 TRP A CH2   1 
ATOM   18720 N  N     . VAL A 1 4094 ? 144.031 143.371 157.203 1.00 18.51  ? 4094 VAL A N     1 
ATOM   18721 C  CA    . VAL A 1 4094 ? 144.259 144.785 157.476 1.00 14.17  ? 4094 VAL A CA    1 
ATOM   18722 C  C     . VAL A 1 4094 ? 145.754 145.052 157.417 1.00 16.46  ? 4094 VAL A C     1 
ATOM   18723 O  O     . VAL A 1 4094 ? 146.536 144.365 158.082 1.00 13.39  ? 4094 VAL A O     1 
ATOM   18724 C  CB    . VAL A 1 4094 ? 143.691 145.208 158.844 1.00 11.14  ? 4094 VAL A CB    1 
ATOM   18725 C  CG1   . VAL A 1 4094 ? 144.044 146.655 159.136 1.00 14.41  ? 4094 VAL A CG1   1 
ATOM   18726 C  CG2   . VAL A 1 4094 ? 142.190 145.015 158.875 1.00 17.78  ? 4094 VAL A CG2   1 
ATOM   18727 N  N     . MET A 1 4095 ? 146.150 146.045 156.624 1.00 15.56  ? 4095 MET A N     1 
ATOM   18728 C  CA    . MET A 1 4095 ? 147.531 146.500 156.558 1.00 13.37  ? 4095 MET A CA    1 
ATOM   18729 C  C     . MET A 1 4095 ? 147.606 147.936 157.050 1.00 14.94  ? 4095 MET A C     1 
ATOM   18730 O  O     . MET A 1 4095 ? 146.790 148.777 156.656 1.00 15.75  ? 4095 MET A O     1 
ATOM   18731 C  CB    . MET A 1 4095 ? 148.090 146.402 155.138 1.00 14.96  ? 4095 MET A CB    1 
ATOM   18732 C  CG    . MET A 1 4095 ? 149.547 146.820 155.031 1.00 15.02  ? 4095 MET A CG    1 
ATOM   18733 S  SD    . MET A 1 4095 ? 150.207 146.677 153.363 1.00 32.49  ? 4095 MET A SD    1 
ATOM   18734 C  CE    . MET A 1 4095 ? 149.374 148.030 152.547 1.00 22.93  ? 4095 MET A CE    1 
ATOM   18735 N  N     . LEU A 1 4096 ? 148.571 148.206 157.924 1.00 11.04  ? 4096 LEU A N     1 
ATOM   18736 C  CA    . LEU A 1 4096 ? 148.829 149.544 158.437 1.00 10.68  ? 4096 LEU A CA    1 
ATOM   18737 C  C     . LEU A 1 4096 ? 150.248 149.943 158.058 1.00 13.58  ? 4096 LEU A C     1 
ATOM   18738 O  O     . LEU A 1 4096 ? 151.206 149.222 158.366 1.00 13.27  ? 4096 LEU A O     1 
ATOM   18739 C  CB    . LEU A 1 4096 ? 148.622 149.603 159.952 1.00 11.65  ? 4096 LEU A CB    1 
ATOM   18740 C  CG    . LEU A 1 4096 ? 147.303 149.004 160.446 1.00 7.42   ? 4096 LEU A CG    1 
ATOM   18741 C  CD1   . LEU A 1 4096 ? 147.245 148.985 161.961 1.00 7.11   ? 4096 LEU A CD1   1 
ATOM   18742 C  CD2   . LEU A 1 4096 ? 146.120 149.767 159.875 1.00 9.09   ? 4096 LEU A CD2   1 
ATOM   18743 N  N     . LYS A 1 4097 ? 150.374 151.090 157.398 1.00 15.02  ? 4097 LYS A N     1 
ATOM   18744 C  CA    . LYS A 1 4097 ? 151.637 151.554 156.847 1.00 9.44   ? 4097 LYS A CA    1 
ATOM   18745 C  C     . LYS A 1 4097 ? 152.247 152.639 157.723 1.00 9.12   ? 4097 LYS A C     1 
ATOM   18746 O  O     . LYS A 1 4097 ? 151.540 153.464 158.307 1.00 11.72  ? 4097 LYS A O     1 
ATOM   18747 C  CB    . LYS A 1 4097 ? 151.449 152.088 155.426 1.00 9.48   ? 4097 LYS A CB    1 
ATOM   18748 C  CG    . LYS A 1 4097 ? 150.563 151.232 154.541 1.00 8.35   ? 4097 LYS A CG    1 
ATOM   18749 C  CD    . LYS A 1 4097 ? 150.640 151.692 153.097 1.00 10.50  ? 4097 LYS A CD    1 
ATOM   18750 C  CE    . LYS A 1 4097 ? 149.292 151.589 152.405 1.00 22.98  ? 4097 LYS A CE    1 
ATOM   18751 N  NZ    . LYS A 1 4097 ? 148.271 152.471 153.031 1.00 19.84  ? 4097 LYS A NZ    1 
ATOM   18752 N  N     . ASN A 1 4098 ? 153.579 152.627 157.800 1.00 8.95   ? 4098 ASN A N     1 
ATOM   18753 C  CA    . ASN A 1 4098 ? 154.348 153.639 158.524 1.00 8.66   ? 4098 ASN A CA    1 
ATOM   18754 C  C     . ASN A 1 4098 ? 153.920 153.730 159.986 1.00 10.64  ? 4098 ASN A C     1 
ATOM   18755 O  O     . ASN A 1 4098 ? 153.768 154.820 160.542 1.00 15.57  ? 4098 ASN A O     1 
ATOM   18756 C  CB    . ASN A 1 4098 ? 154.241 155.004 157.840 1.00 12.54  ? 4098 ASN A CB    1 
ATOM   18757 C  CG    . ASN A 1 4098 ? 154.378 154.914 156.334 1.00 10.76  ? 4098 ASN A CG    1 
ATOM   18758 O  OD1   . ASN A 1 4098 ? 153.531 155.408 155.591 1.00 8.73   ? 4098 ASN A OD1   1 
ATOM   18759 N  ND2   . ASN A 1 4098 ? 155.450 154.285 155.874 1.00 10.55  ? 4098 ASN A ND2   1 
ATOM   18760 N  N     . VAL A 1 4099 ? 153.727 152.571 160.620 1.00 12.55  ? 4099 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4099 ? 153.343 152.534 162.026 1.00 10.02  ? 4099 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4099 ? 154.449 153.014 162.950 1.00 9.30   ? 4099 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4099 ? 154.189 153.271 164.130 1.00 11.76  ? 4099 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4099 ? 152.909 151.112 162.435 1.00 7.29   ? 4099 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4099 ? 151.703 150.676 161.628 1.00 9.53   ? 4099 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4099 ? 154.054 150.135 162.250 1.00 8.58   ? 4099 VAL A CG2   1 
ATOM   18767 N  N     . HIS A 1 4100 ? 155.679 153.140 162.447 1.00 10.62  ? 4100 HIS A N     1 
ATOM   18768 C  CA    . HIS A 1 4100 ? 156.773 153.666 163.253 1.00 10.23  ? 4100 HIS A CA    1 
ATOM   18769 C  C     . HIS A 1 4100 ? 156.631 155.155 163.536 1.00 11.45  ? 4100 HIS A C     1 
ATOM   18770 O  O     . HIS A 1 4100 ? 157.353 155.675 164.393 1.00 14.00  ? 4100 HIS A O     1 
ATOM   18771 C  CB    . HIS A 1 4100 ? 158.111 153.395 162.564 1.00 11.41  ? 4100 HIS A CB    1 
ATOM   18772 C  CG    . HIS A 1 4100 ? 158.286 154.129 161.271 1.00 12.05  ? 4100 HIS A CG    1 
ATOM   18773 N  ND1   . HIS A 1 4100 ? 157.769 153.671 160.079 1.00 10.78  ? 4100 HIS A ND1   1 
ATOM   18774 C  CD2   . HIS A 1 4100 ? 158.923 155.288 160.984 1.00 12.48  ? 4100 HIS A CD2   1 
ATOM   18775 C  CE1   . HIS A 1 4100 ? 158.080 154.516 159.113 1.00 10.66  ? 4100 HIS A CE1   1 
ATOM   18776 N  NE2   . HIS A 1 4100 ? 158.780 155.507 159.635 1.00 13.71  ? 4100 HIS A NE2   1 
ATOM   18777 N  N     . LEU A 1 4101 ? 155.728 155.848 162.844 1.00 11.02  ? 4101 LEU A N     1 
ATOM   18778 C  CA    . LEU A 1 4101 ? 155.494 157.262 163.096 1.00 9.43   ? 4101 LEU A CA    1 
ATOM   18779 C  C     . LEU A 1 4101 ? 154.559 157.507 164.272 1.00 10.80  ? 4101 LEU A C     1 
ATOM   18780 O  O     . LEU A 1 4101 ? 154.384 158.662 164.672 1.00 16.40  ? 4101 LEU A O     1 
ATOM   18781 C  CB    . LEU A 1 4101 ? 154.932 157.934 161.841 1.00 11.31  ? 4101 LEU A CB    1 
ATOM   18782 C  CG    . LEU A 1 4101 ? 155.782 157.805 160.577 1.00 10.73  ? 4101 LEU A CG    1 
ATOM   18783 C  CD1   . LEU A 1 4101 ? 155.007 158.277 159.361 1.00 11.71  ? 4101 LEU A CD1   1 
ATOM   18784 C  CD2   . LEU A 1 4101 ? 157.076 158.584 160.723 1.00 9.61   ? 4101 LEU A CD2   1 
ATOM   18785 N  N     . ALA A 1 4102 ? 153.957 156.459 164.829 1.00 11.67  ? 4102 ALA A N     1 
ATOM   18786 C  CA    . ALA A 1 4102 ? 153.107 156.560 166.013 1.00 10.61  ? 4102 ALA A CA    1 
ATOM   18787 C  C     . ALA A 1 4102 ? 153.546 155.509 167.024 1.00 13.29  ? 4102 ALA A C     1 
ATOM   18788 O  O     . ALA A 1 4102 ? 152.854 154.508 167.242 1.00 11.24  ? 4102 ALA A O     1 
ATOM   18789 C  CB    . ALA A 1 4102 ? 151.632 156.392 165.649 1.00 11.54  ? 4102 ALA A CB    1 
ATOM   18790 N  N     . PRO A 1 4103 ? 154.709 155.702 167.651 1.00 16.25  ? 4103 PRO A N     1 
ATOM   18791 C  CA    . PRO A 1 4103 ? 155.195 154.695 168.609 1.00 16.71  ? 4103 PRO A CA    1 
ATOM   18792 C  C     . PRO A 1 4103 ? 154.271 154.485 169.793 1.00 18.48  ? 4103 PRO A C     1 
ATOM   18793 O  O     . PRO A 1 4103 ? 154.154 153.355 170.281 1.00 20.65  ? 4103 PRO A O     1 
ATOM   18794 C  CB    . PRO A 1 4103 ? 156.555 155.258 169.044 1.00 17.66  ? 4103 PRO A CB    1 
ATOM   18795 C  CG    . PRO A 1 4103 ? 156.445 156.723 168.815 1.00 18.24  ? 4103 PRO A CG    1 
ATOM   18796 C  CD    . PRO A 1 4103 ? 155.580 156.888 167.604 1.00 16.63  ? 4103 PRO A CD    1 
ATOM   18797 N  N     . GLY A 1 4104 ? 153.613 155.541 170.276 1.00 19.83  ? 4104 GLY A N     1 
ATOM   18798 C  CA    . GLY A 1 4104 ? 152.708 155.379 171.401 1.00 17.81  ? 4104 GLY A CA    1 
ATOM   18799 C  C     . GLY A 1 4104 ? 151.510 154.509 171.074 1.00 17.77  ? 4104 GLY A C     1 
ATOM   18800 O  O     . GLY A 1 4104 ? 151.178 153.592 171.827 1.00 22.45  ? 4104 GLY A O     1 
ATOM   18801 N  N     . TRP A 1 4105 ? 150.865 154.765 169.932 1.00 17.42  ? 4105 TRP A N     1 
ATOM   18802 C  CA    . TRP A 1 4105 ? 149.664 154.032 169.545 1.00 16.24  ? 4105 TRP A CA    1 
ATOM   18803 C  C     . TRP A 1 4105 ? 149.933 152.548 169.330 1.00 17.37  ? 4105 TRP A C     1 
ATOM   18804 O  O     . TRP A 1 4105 ? 149.021 151.728 169.504 1.00 18.04  ? 4105 TRP A O     1 
ATOM   18805 C  CB    . TRP A 1 4105 ? 149.074 154.658 168.278 1.00 15.83  ? 4105 TRP A CB    1 
ATOM   18806 C  CG    . TRP A 1 4105 ? 147.878 153.950 167.730 1.00 16.74  ? 4105 TRP A CG    1 
ATOM   18807 C  CD1   . TRP A 1 4105 ? 146.589 154.070 168.156 1.00 18.45  ? 4105 TRP A CD1   1 
ATOM   18808 C  CD2   . TRP A 1 4105 ? 147.857 153.015 166.647 1.00 17.25  ? 4105 TRP A CD2   1 
ATOM   18809 N  NE1   . TRP A 1 4105 ? 145.766 153.267 167.406 1.00 17.65  ? 4105 TRP A NE1   1 
ATOM   18810 C  CE2   . TRP A 1 4105 ? 146.521 152.607 166.473 1.00 14.92  ? 4105 TRP A CE2   1 
ATOM   18811 C  CE3   . TRP A 1 4105 ? 148.839 152.480 165.808 1.00 18.38  ? 4105 TRP A CE3   1 
ATOM   18812 C  CZ2   . TRP A 1 4105 ? 146.142 151.691 165.499 1.00 16.28  ? 4105 TRP A CZ2   1 
ATOM   18813 C  CZ3   . TRP A 1 4105 ? 148.461 151.571 164.841 1.00 18.09  ? 4105 TRP A CZ3   1 
ATOM   18814 C  CH2   . TRP A 1 4105 ? 147.124 151.186 164.694 1.00 17.33  ? 4105 TRP A CH2   1 
ATOM   18815 N  N     . LEU A 1 4106 ? 151.165 152.189 168.965 1.00 18.61  ? 4106 LEU A N     1 
ATOM   18816 C  CA    . LEU A 1 4106 ? 151.508 150.787 168.755 1.00 16.40  ? 4106 LEU A CA    1 
ATOM   18817 C  C     . LEU A 1 4106 ? 151.365 149.983 170.040 1.00 20.42  ? 4106 LEU A C     1 
ATOM   18818 O  O     . LEU A 1 4106 ? 151.034 148.794 170.000 1.00 24.19  ? 4106 LEU A O     1 
ATOM   18819 C  CB    . LEU A 1 4106 ? 152.930 150.679 168.205 1.00 15.97  ? 4106 LEU A CB    1 
ATOM   18820 C  CG    . LEU A 1 4106 ? 153.086 150.852 166.693 1.00 11.49  ? 4106 LEU A CG    1 
ATOM   18821 C  CD1   . LEU A 1 4106 ? 154.536 150.682 166.281 1.00 11.68  ? 4106 LEU A CD1   1 
ATOM   18822 C  CD2   . LEU A 1 4106 ? 152.199 149.875 165.945 1.00 12.11  ? 4106 LEU A CD2   1 
ATOM   18823 N  N     . MET A 1 4107 ? 151.596 150.616 171.193 1.00 20.23  ? 4107 MET A N     1 
ATOM   18824 C  CA    . MET A 1 4107 ? 151.445 149.907 172.460 1.00 17.71  ? 4107 MET A CA    1 
ATOM   18825 C  C     . MET A 1 4107 ? 149.988 149.543 172.723 1.00 16.71  ? 4107 MET A C     1 
ATOM   18826 O  O     . MET A 1 4107 ? 149.682 148.389 173.055 1.00 18.89  ? 4107 MET A O     1 
ATOM   18827 C  CB    . MET A 1 4107 ? 152.013 150.747 173.602 1.00 23.16  ? 4107 MET A CB    1 
ATOM   18828 C  CG    . MET A 1 4107 ? 153.520 150.935 173.531 1.00 29.76  ? 4107 MET A CG    1 
ATOM   18829 S  SD    . MET A 1 4107 ? 154.168 151.995 174.836 1.00 75.47  ? 4107 MET A SD    1 
ATOM   18830 C  CE    . MET A 1 4107 ? 153.958 150.937 176.265 1.00 57.00  ? 4107 MET A CE    1 
ATOM   18831 N  N     . GLN A 1 4108 ? 149.071 150.506 172.580 1.00 17.60  ? 4108 GLN A N     1 
ATOM   18832 C  CA    . GLN A 1 4108 ? 147.657 150.176 172.731 1.00 21.89  ? 4108 GLN A CA    1 
ATOM   18833 C  C     . GLN A 1 4108 ? 147.217 149.164 171.684 1.00 18.66  ? 4108 GLN A C     1 
ATOM   18834 O  O     . GLN A 1 4108 ? 146.362 148.315 171.958 1.00 19.68  ? 4108 GLN A O     1 
ATOM   18835 C  CB    . GLN A 1 4108 ? 146.778 151.428 172.666 1.00 25.13  ? 4108 GLN A CB    1 
ATOM   18836 C  CG    . GLN A 1 4108 ? 146.947 152.406 173.825 1.00 35.96  ? 4108 GLN A CG    1 
ATOM   18837 C  CD    . GLN A 1 4108 ? 148.128 153.327 173.658 1.00 38.25  ? 4108 GLN A CD    1 
ATOM   18838 O  OE1   . GLN A 1 4108 ? 148.652 153.481 172.560 1.00 38.57  ? 4108 GLN A OE1   1 
ATOM   18839 N  NE2   . GLN A 1 4108 ? 148.554 153.952 174.749 1.00 41.47  ? 4108 GLN A NE2   1 
ATOM   18840 N  N     . LEU A 1 4109 ? 147.797 149.225 170.483 1.00 19.77  ? 4109 LEU A N     1 
ATOM   18841 C  CA    . LEU A 1 4109 ? 147.484 148.215 169.476 1.00 17.79  ? 4109 LEU A CA    1 
ATOM   18842 C  C     . LEU A 1 4109 ? 147.922 146.827 169.935 1.00 17.52  ? 4109 LEU A C     1 
ATOM   18843 O  O     . LEU A 1 4109 ? 147.200 145.843 169.740 1.00 18.93  ? 4109 LEU A O     1 
ATOM   18844 C  CB    . LEU A 1 4109 ? 148.142 148.577 168.145 1.00 18.53  ? 4109 LEU A CB    1 
ATOM   18845 C  CG    . LEU A 1 4109 ? 148.185 147.468 167.093 1.00 16.59  ? 4109 LEU A CG    1 
ATOM   18846 C  CD1   . LEU A 1 4109 ? 146.793 147.189 166.560 1.00 13.47  ? 4109 LEU A CD1   1 
ATOM   18847 C  CD2   . LEU A 1 4109 ? 149.128 147.834 165.963 1.00 14.28  ? 4109 LEU A CD2   1 
ATOM   18848 N  N     . GLU A 1 4110 ? 149.104 146.731 170.547 1.00 17.02  ? 4110 GLU A N     1 
ATOM   18849 C  CA    . GLU A 1 4110 ? 149.589 145.446 171.040 1.00 17.93  ? 4110 GLU A CA    1 
ATOM   18850 C  C     . GLU A 1 4110 ? 148.699 144.904 172.152 1.00 22.49  ? 4110 GLU A C     1 
ATOM   18851 O  O     . GLU A 1 4110 ? 148.372 143.711 172.171 1.00 24.50  ? 4110 GLU A O     1 
ATOM   18852 C  CB    . GLU A 1 4110 ? 151.033 145.587 171.522 1.00 20.30  ? 4110 GLU A CB    1 
ATOM   18853 C  CG    . GLU A 1 4110 ? 151.784 144.273 171.673 1.00 21.19  ? 4110 GLU A CG    1 
ATOM   18854 C  CD    . GLU A 1 4110 ? 151.634 143.667 173.055 1.00 35.59  ? 4110 GLU A CD    1 
ATOM   18855 O  OE1   . GLU A 1 4110 ? 151.805 144.404 174.048 1.00 32.42  ? 4110 GLU A OE1   1 
ATOM   18856 O  OE2   . GLU A 1 4110 ? 151.349 142.454 173.149 1.00 37.14  ? 4110 GLU A OE2   1 
ATOM   18857 N  N     . LYS A 1 4111 ? 148.301 145.766 173.092 1.00 23.63  ? 4111 LYS A N     1 
ATOM   18858 C  CA    . LYS A 1 4111 ? 147.392 145.324 174.150 1.00 18.39  ? 4111 LYS A CA    1 
ATOM   18859 C  C     . LYS A 1 4111 ? 146.036 144.909 173.588 1.00 21.65  ? 4111 LYS A C     1 
ATOM   18860 O  O     . LYS A 1 4111 ? 145.427 143.946 174.070 1.00 26.10  ? 4111 LYS A O     1 
ATOM   18861 C  CB    . LYS A 1 4111 ? 147.226 146.404 175.222 1.00 16.07  ? 4111 LYS A CB    1 
ATOM   18862 C  CG    . LYS A 1 4111 ? 148.358 146.469 176.249 1.00 28.70  ? 4111 LYS A CG    1 
ATOM   18863 C  CD    . LYS A 1 4111 ? 149.634 147.050 175.687 1.00 33.42  ? 4111 LYS A CD    1 
ATOM   18864 C  CE    . LYS A 1 4111 ? 150.707 147.188 176.747 1.00 34.17  ? 4111 LYS A CE    1 
ATOM   18865 N  NZ    . LYS A 1 4111 ? 151.997 147.651 176.160 1.00 36.46  ? 4111 LYS A NZ    1 
ATOM   18866 N  N     . LYS A 1 4112 ? 145.539 145.625 172.577 1.00 19.05  ? 4112 LYS A N     1 
ATOM   18867 C  CA    . LYS A 1 4112 ? 144.276 145.244 171.954 1.00 16.54  ? 4112 LYS A CA    1 
ATOM   18868 C  C     . LYS A 1 4112 ? 144.394 143.894 171.256 1.00 23.83  ? 4112 LYS A C     1 
ATOM   18869 O  O     . LYS A 1 4112 ? 143.470 143.074 171.309 1.00 26.37  ? 4112 LYS A O     1 
ATOM   18870 C  CB    . LYS A 1 4112 ? 143.834 146.329 170.972 1.00 16.05  ? 4112 LYS A CB    1 
ATOM   18871 C  CG    . LYS A 1 4112 ? 142.919 145.844 169.862 1.00 27.63  ? 4112 LYS A CG    1 
ATOM   18872 C  CD    . LYS A 1 4112 ? 142.592 146.965 168.894 1.00 22.45  ? 4112 LYS A CD    1 
ATOM   18873 C  CE    . LYS A 1 4112 ? 141.378 146.626 168.049 1.00 22.62  ? 4112 LYS A CE    1 
ATOM   18874 N  NZ    . LYS A 1 4112 ? 140.307 145.984 168.857 1.00 32.53  ? 4112 LYS A NZ    1 
ATOM   18875 N  N     . LEU A 1 4113 ? 145.529 143.647 170.599 1.00 26.17  ? 4113 LEU A N     1 
ATOM   18876 C  CA    . LEU A 1 4113 ? 145.738 142.377 169.913 1.00 20.74  ? 4113 LEU A CA    1 
ATOM   18877 C  C     . LEU A 1 4113 ? 145.872 141.223 170.897 1.00 23.26  ? 4113 LEU A C     1 
ATOM   18878 O  O     . LEU A 1 4113 ? 145.408 140.110 170.622 1.00 23.59  ? 4113 LEU A O     1 
ATOM   18879 C  CB    . LEU A 1 4113 ? 146.980 142.460 169.028 1.00 18.38  ? 4113 LEU A CB    1 
ATOM   18880 C  CG    . LEU A 1 4113 ? 146.851 143.209 167.704 1.00 17.68  ? 4113 LEU A CG    1 
ATOM   18881 C  CD1   . LEU A 1 4113 ? 148.229 143.482 167.129 1.00 15.97  ? 4113 LEU A CD1   1 
ATOM   18882 C  CD2   . LEU A 1 4113 ? 146.002 142.418 166.724 1.00 17.64  ? 4113 LEU A CD2   1 
ATOM   18883 N  N     . HIS A 1 4114 ? 146.518 141.464 172.042 1.00 26.48  ? 4114 HIS A N     1 
ATOM   18884 C  CA    . HIS A 1 4114 ? 146.787 140.381 172.985 1.00 26.19  ? 4114 HIS A CA    1 
ATOM   18885 C  C     . HIS A 1 4114 ? 145.496 139.765 173.513 1.00 27.51  ? 4114 HIS A C     1 
ATOM   18886 O  O     . HIS A 1 4114 ? 145.375 138.538 173.600 1.00 23.02  ? 4114 HIS A O     1 
ATOM   18887 C  CB    . HIS A 1 4114 ? 147.644 140.896 174.140 1.00 26.33  ? 4114 HIS A CB    1 
ATOM   18888 C  CG    . HIS A 1 4114 ? 147.987 139.847 175.152 1.00 29.95  ? 4114 HIS A CG    1 
ATOM   18889 N  ND1   . HIS A 1 4114 ? 148.795 138.769 174.861 1.00 30.80  ? 4114 HIS A ND1   1 
ATOM   18890 C  CD2   . HIS A 1 4114 ? 147.627 139.708 176.449 1.00 24.34  ? 4114 HIS A CD2   1 
ATOM   18891 C  CE1   . HIS A 1 4114 ? 148.921 138.013 175.937 1.00 25.95  ? 4114 HIS A CE1   1 
ATOM   18892 N  NE2   . HIS A 1 4114 ? 148.222 138.561 176.914 1.00 23.70  ? 4114 HIS A NE2   1 
ATOM   18893 N  N     . SER A 1 4115 ? 144.521 140.600 173.867 1.00 31.69  ? 4115 SER A N     1 
ATOM   18894 C  CA    . SER A 1 4115 ? 143.231 140.122 174.363 1.00 35.55  ? 4115 SER A CA    1 
ATOM   18895 C  C     . SER A 1 4115 ? 142.226 140.088 173.211 1.00 32.94  ? 4115 SER A C     1 
ATOM   18896 O  O     . SER A 1 4115 ? 141.285 140.878 173.130 1.00 34.79  ? 4115 SER A O     1 
ATOM   18897 C  CB    . SER A 1 4115 ? 142.745 141.000 175.509 1.00 39.96  ? 4115 SER A CB    1 
ATOM   18898 O  OG    . SER A 1 4115 ? 142.528 142.329 175.069 1.00 30.69  ? 4115 SER A OG    1 
ATOM   18899 N  N     . LEU A 1 4116 ? 142.446 139.136 172.308 1.00 29.98  ? 4116 LEU A N     1 
ATOM   18900 C  CA    . LEU A 1 4116 ? 141.647 139.052 171.095 1.00 27.81  ? 4116 LEU A CA    1 
ATOM   18901 C  C     . LEU A 1 4116 ? 141.780 137.656 170.504 1.00 33.06  ? 4116 LEU A C     1 
ATOM   18902 O  O     . LEU A 1 4116 ? 142.875 137.089 170.481 1.00 43.86  ? 4116 LEU A O     1 
ATOM   18903 C  CB    . LEU A 1 4116 ? 142.092 140.112 170.081 1.00 31.41  ? 4116 LEU A CB    1 
ATOM   18904 C  CG    . LEU A 1 4116 ? 141.140 140.494 168.951 1.00 33.64  ? 4116 LEU A CG    1 
ATOM   18905 C  CD1   . LEU A 1 4116 ? 139.809 140.959 169.510 1.00 28.94  ? 4116 LEU A CD1   1 
ATOM   18906 C  CD2   . LEU A 1 4116 ? 141.773 141.581 168.104 1.00 28.91  ? 4116 LEU A CD2   1 
ATOM   18907 N  N     . GLN A 1 4117 ? 140.661 137.112 170.028 1.00 32.98  ? 4117 GLN A N     1 
ATOM   18908 C  CA    . GLN A 1 4117 ? 140.618 135.802 169.379 1.00 33.66  ? 4117 GLN A CA    1 
ATOM   18909 C  C     . GLN A 1 4117 ? 139.918 135.983 168.039 1.00 34.34  ? 4117 GLN A C     1 
ATOM   18910 O  O     . GLN A 1 4117 ? 138.712 135.731 167.911 1.00 35.48  ? 4117 GLN A O     1 
ATOM   18911 C  CB    . GLN A 1 4117 ? 139.910 134.767 170.255 1.00 32.87  ? 4117 GLN A CB    1 
ATOM   18912 C  CG    . GLN A 1 4117 ? 139.894 133.353 169.683 1.00 46.03  ? 4117 GLN A CG    1 
ATOM   18913 C  CD    . GLN A 1 4117 ? 141.269 132.866 169.262 1.00 49.13  ? 4117 GLN A CD    1 
ATOM   18914 O  OE1   . GLN A 1 4117 ? 141.433 132.291 168.185 1.00 41.94  ? 4117 GLN A OE1   1 
ATOM   18915 N  NE2   . GLN A 1 4117 ? 142.263 133.078 170.118 1.00 49.93  ? 4117 GLN A NE2   1 
ATOM   18916 N  N     . PRO A 1 4118 ? 140.644 136.421 167.020 1.00 34.61  ? 4118 PRO A N     1 
ATOM   18917 C  CA    . PRO A 1 4118 ? 140.016 136.824 165.760 1.00 32.53  ? 4118 PRO A CA    1 
ATOM   18918 C  C     . PRO A 1 4118 ? 139.642 135.620 164.901 1.00 30.70  ? 4118 PRO A C     1 
ATOM   18919 O  O     . PRO A 1 4118 ? 139.789 134.465 165.296 1.00 31.10  ? 4118 PRO A O     1 
ATOM   18920 C  CB    . PRO A 1 4118 ? 141.101 137.670 165.095 1.00 24.41  ? 4118 PRO A CB    1 
ATOM   18921 C  CG    . PRO A 1 4118 ? 142.373 137.097 165.600 1.00 22.79  ? 4118 PRO A CG    1 
ATOM   18922 C  CD    . PRO A 1 4118 ? 142.107 136.592 166.992 1.00 27.86  ? 4118 PRO A CD    1 
ATOM   18923 N  N     . HIS A 1 4119 ? 139.145 135.922 163.704 1.00 25.43  ? 4119 HIS A N     1 
ATOM   18924 C  CA    . HIS A 1 4119 ? 138.772 134.894 162.746 1.00 24.68  ? 4119 HIS A CA    1 
ATOM   18925 C  C     . HIS A 1 4119 ? 140.008 134.121 162.294 1.00 27.60  ? 4119 HIS A C     1 
ATOM   18926 O  O     . HIS A 1 4119 ? 141.145 134.579 162.430 1.00 34.06  ? 4119 HIS A O     1 
ATOM   18927 C  CB    . HIS A 1 4119 ? 138.070 135.525 161.543 1.00 26.73  ? 4119 HIS A CB    1 
ATOM   18928 C  CG    . HIS A 1 4119 ? 137.286 134.555 160.715 1.00 28.35  ? 4119 HIS A CG    1 
ATOM   18929 N  ND1   . HIS A 1 4119 ? 137.594 134.281 159.400 1.00 29.73  ? 4119 HIS A ND1   1 
ATOM   18930 C  CD2   . HIS A 1 4119 ? 136.198 133.806 161.011 1.00 32.21  ? 4119 HIS A CD2   1 
ATOM   18931 C  CE1   . HIS A 1 4119 ? 136.734 133.398 158.923 1.00 30.21  ? 4119 HIS A CE1   1 
ATOM   18932 N  NE2   . HIS A 1 4119 ? 135.877 133.094 159.881 1.00 42.94  ? 4119 HIS A NE2   1 
ATOM   18933 N  N     . ALA A 1 4120 ? 139.771 132.924 161.754 1.00 24.50  ? 4120 ALA A N     1 
ATOM   18934 C  CA    . ALA A 1 4120 ? 140.878 132.060 161.357 1.00 22.02  ? 4120 ALA A CA    1 
ATOM   18935 C  C     . ALA A 1 4120 ? 141.707 132.690 160.245 1.00 30.30  ? 4120 ALA A C     1 
ATOM   18936 O  O     . ALA A 1 4120 ? 142.941 132.609 160.260 1.00 37.65  ? 4120 ALA A O     1 
ATOM   18937 C  CB    . ALA A 1 4120 ? 140.348 130.695 160.921 1.00 26.05  ? 4120 ALA A CB    1 
ATOM   18938 N  N     . CYS A 1 4121 ? 141.052 133.322 159.276 1.00 28.54  ? 4121 CYS A N     1 
ATOM   18939 C  CA    . CYS A 1 4121 ? 141.731 133.880 158.116 1.00 23.52  ? 4121 CYS A CA    1 
ATOM   18940 C  C     . CYS A 1 4121 ? 142.170 135.326 158.312 1.00 24.39  ? 4121 CYS A C     1 
ATOM   18941 O  O     . CYS A 1 4121 ? 142.752 135.907 157.391 1.00 25.45  ? 4121 CYS A O     1 
ATOM   18942 C  CB    . CYS A 1 4121 ? 140.828 133.782 156.883 1.00 26.55  ? 4121 CYS A CB    1 
ATOM   18943 S  SG    . CYS A 1 4121 ? 140.454 132.093 156.364 1.00 49.02  ? 4121 CYS A SG    1 
ATOM   18944 N  N     . PHE A 1 4122 ? 141.908 135.918 159.474 1.00 21.76  ? 4122 PHE A N     1 
ATOM   18945 C  CA    . PHE A 1 4122 ? 142.296 137.302 159.708 1.00 17.66  ? 4122 PHE A CA    1 
ATOM   18946 C  C     . PHE A 1 4122 ? 143.811 137.444 159.737 1.00 17.81  ? 4122 PHE A C     1 
ATOM   18947 O  O     . PHE A 1 4122 ? 144.518 136.627 160.334 1.00 23.63  ? 4122 PHE A O     1 
ATOM   18948 C  CB    . PHE A 1 4122 ? 141.711 137.810 161.023 1.00 15.34  ? 4122 PHE A CB    1 
ATOM   18949 C  CG    . PHE A 1 4122 ? 142.309 139.109 161.487 1.00 13.62  ? 4122 PHE A CG    1 
ATOM   18950 C  CD1   . PHE A 1 4122 ? 142.081 140.281 160.789 1.00 15.66  ? 4122 PHE A CD1   1 
ATOM   18951 C  CD2   . PHE A 1 4122 ? 143.114 139.153 162.612 1.00 11.68  ? 4122 PHE A CD2   1 
ATOM   18952 C  CE1   . PHE A 1 4122 ? 142.633 141.475 161.212 1.00 13.09  ? 4122 PHE A CE1   1 
ATOM   18953 C  CE2   . PHE A 1 4122 ? 143.670 140.342 163.039 1.00 8.66   ? 4122 PHE A CE2   1 
ATOM   18954 C  CZ    . PHE A 1 4122 ? 143.429 141.504 162.337 1.00 10.99  ? 4122 PHE A CZ    1 
ATOM   18955 N  N     . ARG A 1 4123 ? 144.307 138.494 159.088 1.00 13.71  ? 4123 ARG A N     1 
ATOM   18956 C  CA    . ARG A 1 4123 ? 145.723 138.825 159.113 1.00 10.12  ? 4123 ARG A CA    1 
ATOM   18957 C  C     . ARG A 1 4123 ? 145.889 140.324 159.301 1.00 9.48   ? 4123 ARG A C     1 
ATOM   18958 O  O     . ARG A 1 4123 ? 145.124 141.120 158.745 1.00 14.94  ? 4123 ARG A O     1 
ATOM   18959 C  CB    . ARG A 1 4123 ? 146.435 138.370 157.834 1.00 12.12  ? 4123 ARG A CB    1 
ATOM   18960 C  CG    . ARG A 1 4123 ? 146.515 136.865 157.677 1.00 13.88  ? 4123 ARG A CG    1 
ATOM   18961 C  CD    . ARG A 1 4123 ? 147.375 136.248 158.767 1.00 18.70  ? 4123 ARG A CD    1 
ATOM   18962 N  NE    . ARG A 1 4123 ? 147.450 134.797 158.648 1.00 20.96  ? 4123 ARG A NE    1 
ATOM   18963 C  CZ    . ARG A 1 4123 ? 146.517 133.961 159.080 1.00 18.36  ? 4123 ARG A CZ    1 
ATOM   18964 N  NH1   . ARG A 1 4123 ? 145.428 134.398 159.690 1.00 20.56  ? 4123 ARG A NH1   1 
ATOM   18965 N  NH2   . ARG A 1 4123 ? 146.682 132.655 158.900 1.00 20.21  ? 4123 ARG A NH2   1 
ATOM   18966 N  N     . LEU A 1 4124 ? 146.885 140.696 160.098 1.00 8.01   ? 4124 LEU A N     1 
ATOM   18967 C  CA    . LEU A 1 4124 ? 147.234 142.088 160.341 1.00 8.75   ? 4124 LEU A CA    1 
ATOM   18968 C  C     . LEU A 1 4124 ? 148.700 142.284 159.991 1.00 10.49  ? 4124 LEU A C     1 
ATOM   18969 O  O     . LEU A 1 4124 ? 149.575 141.674 160.610 1.00 11.61  ? 4124 LEU A O     1 
ATOM   18970 C  CB    . LEU A 1 4124 ? 146.973 142.483 161.795 1.00 7.14   ? 4124 LEU A CB    1 
ATOM   18971 C  CG    . LEU A 1 4124 ? 147.340 143.924 162.154 1.00 7.31   ? 4124 LEU A CG    1 
ATOM   18972 C  CD1   . LEU A 1 4124 ? 146.444 144.901 161.417 1.00 8.96   ? 4124 LEU A CD1   1 
ATOM   18973 C  CD2   . LEU A 1 4124 ? 147.262 144.142 163.652 1.00 7.64   ? 4124 LEU A CD2   1 
ATOM   18974 N  N     . PHE A 1 4125 ? 148.962 143.131 159.004 1.00 12.90  ? 4125 PHE A N     1 
ATOM   18975 C  CA    . PHE A 1 4125 ? 150.309 143.465 158.574 1.00 8.70   ? 4125 PHE A CA    1 
ATOM   18976 C  C     . PHE A 1 4125 ? 150.638 144.881 159.020 1.00 9.09   ? 4125 PHE A C     1 
ATOM   18977 O  O     . PHE A 1 4125 ? 149.807 145.786 158.902 1.00 11.56  ? 4125 PHE A O     1 
ATOM   18978 C  CB    . PHE A 1 4125 ? 150.450 143.348 157.053 1.00 8.17   ? 4125 PHE A CB    1 
ATOM   18979 C  CG    . PHE A 1 4125 ? 150.063 142.001 156.505 1.00 8.53   ? 4125 PHE A CG    1 
ATOM   18980 C  CD1   . PHE A 1 4125 ? 148.736 141.688 156.263 1.00 11.13  ? 4125 PHE A CD1   1 
ATOM   18981 C  CD2   . PHE A 1 4125 ? 151.030 141.052 156.221 1.00 9.64   ? 4125 PHE A CD2   1 
ATOM   18982 C  CE1   . PHE A 1 4125 ? 148.382 140.453 155.761 1.00 9.16   ? 4125 PHE A CE1   1 
ATOM   18983 C  CE2   . PHE A 1 4125 ? 150.680 139.819 155.710 1.00 10.21  ? 4125 PHE A CE2   1 
ATOM   18984 C  CZ    . PHE A 1 4125 ? 149.354 139.519 155.484 1.00 10.42  ? 4125 PHE A CZ    1 
ATOM   18985 N  N     . LEU A 1 4126 ? 151.842 145.065 159.554 1.00 9.39   ? 4126 LEU A N     1 
ATOM   18986 C  CA    . LEU A 1 4126 ? 152.313 146.372 160.006 1.00 9.17   ? 4126 LEU A CA    1 
ATOM   18987 C  C     . LEU A 1 4126 ? 153.636 146.647 159.302 1.00 11.00  ? 4126 LEU A C     1 
ATOM   18988 O  O     . LEU A 1 4126 ? 154.661 146.059 159.655 1.00 11.03  ? 4126 LEU A O     1 
ATOM   18989 C  CB    . LEU A 1 4126 ? 152.473 146.413 161.524 1.00 9.22   ? 4126 LEU A CB    1 
ATOM   18990 C  CG    . LEU A 1 4126 ? 151.286 145.952 162.371 1.00 6.39   ? 4126 LEU A CG    1 
ATOM   18991 C  CD1   . LEU A 1 4126 ? 151.617 146.026 163.849 1.00 6.79   ? 4126 LEU A CD1   1 
ATOM   18992 C  CD2   . LEU A 1 4126 ? 150.055 146.772 162.059 1.00 5.83   ? 4126 LEU A CD2   1 
ATOM   18993 N  N     . THR A 1 4127 ? 153.617 147.520 158.298 1.00 14.54  ? 4127 THR A N     1 
ATOM   18994 C  CA    . THR A 1 4127 ? 154.839 147.880 157.591 1.00 12.01  ? 4127 THR A CA    1 
ATOM   18995 C  C     . THR A 1 4127 ? 155.489 149.063 158.293 1.00 10.71  ? 4127 THR A C     1 
ATOM   18996 O  O     . THR A 1 4127 ? 154.810 150.037 158.634 1.00 12.00  ? 4127 THR A O     1 
ATOM   18997 C  CB    . THR A 1 4127 ? 154.559 148.215 156.126 1.00 10.74  ? 4127 THR A CB    1 
ATOM   18998 O  OG1   . THR A 1 4127 ? 153.679 149.340 156.050 1.00 13.74  ? 4127 THR A OG1   1 
ATOM   18999 C  CG2   . THR A 1 4127 ? 153.916 147.033 155.423 1.00 15.69  ? 4127 THR A CG2   1 
ATOM   19000 N  N     . MET A 1 4128 ? 156.798 148.976 158.515 1.00 10.59  ? 4128 MET A N     1 
ATOM   19001 C  CA    . MET A 1 4128 ? 157.488 149.987 159.298 1.00 9.38   ? 4128 MET A CA    1 
ATOM   19002 C  C     . MET A 1 4128 ? 158.934 150.083 158.842 1.00 14.48  ? 4128 MET A C     1 
ATOM   19003 O  O     . MET A 1 4128 ? 159.448 149.207 158.141 1.00 20.87  ? 4128 MET A O     1 
ATOM   19004 C  CB    . MET A 1 4128 ? 157.435 149.665 160.795 1.00 13.04  ? 4128 MET A CB    1 
ATOM   19005 C  CG    . MET A 1 4128 ? 158.176 148.389 161.163 1.00 17.36  ? 4128 MET A CG    1 
ATOM   19006 S  SD    . MET A 1 4128 ? 158.037 147.938 162.901 1.00 42.03  ? 4128 MET A SD    1 
ATOM   19007 C  CE    . MET A 1 4128 ? 156.345 147.361 162.967 1.00 16.02  ? 4128 MET A CE    1 
ATOM   19008 N  N     . GLU A 1 4129 ? 159.583 151.166 159.247 1.00 14.48  ? 4129 GLU A N     1 
ATOM   19009 C  CA    . GLU A 1 4129 ? 161.015 151.317 159.064 1.00 13.53  ? 4129 GLU A CA    1 
ATOM   19010 C  C     . GLU A 1 4129 ? 161.748 150.808 160.300 1.00 18.82  ? 4129 GLU A C     1 
ATOM   19011 O  O     . GLU A 1 4129 ? 161.199 150.759 161.402 1.00 25.55  ? 4129 GLU A O     1 
ATOM   19012 C  CB    . GLU A 1 4129 ? 161.376 152.777 158.797 1.00 13.80  ? 4129 GLU A CB    1 
ATOM   19013 C  CG    . GLU A 1 4129 ? 161.499 153.119 157.325 1.00 22.64  ? 4129 GLU A CG    1 
ATOM   19014 C  CD    . GLU A 1 4129 ? 161.991 154.532 157.095 1.00 34.04  ? 4129 GLU A CD    1 
ATOM   19015 O  OE1   . GLU A 1 4129 ? 162.276 155.231 158.088 1.00 26.52  ? 4129 GLU A OE1   1 
ATOM   19016 O  OE2   . GLU A 1 4129 ? 162.092 154.942 155.920 1.00 34.40  ? 4129 GLU A OE2   1 
ATOM   19017 N  N     . ILE A 1 4130 ? 163.006 150.426 160.103 1.00 17.19  ? 4130 ILE A N     1 
ATOM   19018 C  CA    . ILE A 1 4130 ? 163.813 149.900 161.196 1.00 14.75  ? 4130 ILE A CA    1 
ATOM   19019 C  C     . ILE A 1 4130 ? 164.336 151.061 162.028 1.00 15.86  ? 4130 ILE A C     1 
ATOM   19020 O  O     . ILE A 1 4130 ? 165.390 151.633 161.728 1.00 20.26  ? 4130 ILE A O     1 
ATOM   19021 C  CB    . ILE A 1 4130 ? 164.967 149.027 160.673 1.00 12.65  ? 4130 ILE A CB    1 
ATOM   19022 C  CG1   . ILE A 1 4130 ? 164.434 147.958 159.721 1.00 13.14  ? 4130 ILE A CG1   1 
ATOM   19023 C  CG2   . ILE A 1 4130 ? 165.712 148.382 161.829 1.00 13.00  ? 4130 ILE A CG2   1 
ATOM   19024 C  CD1   . ILE A 1 4130 ? 165.490 146.997 159.232 1.00 12.69  ? 4130 ILE A CD1   1 
ATOM   19025 N  N     . ASN A 1 4131 ? 163.596 151.424 163.070 1.00 14.57  ? 4131 ASN A N     1 
ATOM   19026 C  CA    . ASN A 1 4131 ? 163.999 152.470 163.995 1.00 16.30  ? 4131 ASN A CA    1 
ATOM   19027 C  C     . ASN A 1 4131 ? 163.701 152.041 165.426 1.00 16.69  ? 4131 ASN A C     1 
ATOM   19028 O  O     . ASN A 1 4131 ? 162.830 151.194 165.655 1.00 15.75  ? 4131 ASN A O     1 
ATOM   19029 C  CB    . ASN A 1 4131 ? 163.339 153.820 163.633 1.00 17.22  ? 4131 ASN A CB    1 
ATOM   19030 C  CG    . ASN A 1 4131 ? 161.899 153.973 164.129 1.00 21.22  ? 4131 ASN A CG    1 
ATOM   19031 O  OD1   . ASN A 1 4131 ? 161.298 153.072 164.705 1.00 26.18  ? 4131 ASN A OD1   1 
ATOM   19032 N  ND2   . ASN A 1 4131 ? 161.340 155.148 163.881 1.00 23.29  ? 4131 ASN A ND2   1 
ATOM   19033 N  N     . PRO A 1 4132 ? 164.445 152.570 166.403 1.00 14.14  ? 4132 PRO A N     1 
ATOM   19034 C  CA    . PRO A 1 4132 ? 164.285 152.096 167.788 1.00 14.34  ? 4132 PRO A CA    1 
ATOM   19035 C  C     . PRO A 1 4132 ? 163.001 152.546 168.465 1.00 18.08  ? 4132 PRO A C     1 
ATOM   19036 O  O     . PRO A 1 4132 ? 162.707 152.055 169.562 1.00 22.92  ? 4132 PRO A O     1 
ATOM   19037 C  CB    . PRO A 1 4132 ? 165.514 152.673 168.501 1.00 14.28  ? 4132 PRO A CB    1 
ATOM   19038 C  CG    . PRO A 1 4132 ? 165.930 153.829 167.664 1.00 12.86  ? 4132 PRO A CG    1 
ATOM   19039 C  CD    . PRO A 1 4132 ? 165.616 153.449 166.255 1.00 9.63   ? 4132 PRO A CD    1 
ATOM   19040 N  N     . LYS A 1 4133 ? 162.230 153.456 167.865 1.00 17.79  ? 4133 LYS A N     1 
ATOM   19041 C  CA    . LYS A 1 4133 ? 161.007 153.921 168.510 1.00 18.56  ? 4133 LYS A CA    1 
ATOM   19042 C  C     . LYS A 1 4133 ? 159.921 152.854 168.551 1.00 21.19  ? 4133 LYS A C     1 
ATOM   19043 O  O     . LYS A 1 4133 ? 158.983 152.979 169.345 1.00 22.85  ? 4133 LYS A O     1 
ATOM   19044 C  CB    . LYS A 1 4133 ? 160.474 155.172 167.809 1.00 24.68  ? 4133 LYS A CB    1 
ATOM   19045 C  CG    . LYS A 1 4133 ? 161.363 156.395 167.954 1.00 31.89  ? 4133 LYS A CG    1 
ATOM   19046 C  CD    . LYS A 1 4133 ? 160.696 157.635 167.379 1.00 25.30  ? 4133 LYS A CD    1 
ATOM   19047 C  CE    . LYS A 1 4133 ? 160.690 157.614 165.861 1.00 36.56  ? 4133 LYS A CE    1 
ATOM   19048 N  NZ    . LYS A 1 4133 ? 160.140 158.871 165.286 1.00 42.82  ? 4133 LYS A NZ    1 
ATOM   19049 N  N     . VAL A 1 4134 ? 160.018 151.820 167.721 1.00 18.23  ? 4134 VAL A N     1 
ATOM   19050 C  CA    . VAL A 1 4134 ? 159.000 150.763 167.733 1.00 15.28  ? 4134 VAL A CA    1 
ATOM   19051 C  C     . VAL A 1 4134 ? 159.053 150.033 169.070 1.00 14.97  ? 4134 VAL A C     1 
ATOM   19052 O  O     . VAL A 1 4134 ? 160.150 149.648 169.521 1.00 14.84  ? 4134 VAL A O     1 
ATOM   19053 C  CB    . VAL A 1 4134 ? 159.217 149.789 166.563 1.00 15.11  ? 4134 VAL A CB    1 
ATOM   19054 C  CG1   . VAL A 1 4134 ? 158.099 148.762 166.509 1.00 13.17  ? 4134 VAL A CG1   1 
ATOM   19055 C  CG2   . VAL A 1 4134 ? 159.303 150.550 165.253 1.00 17.85  ? 4134 VAL A CG2   1 
ATOM   19056 N  N     . PRO A 1 4135 ? 157.923 149.831 169.748 1.00 15.44  ? 4135 PRO A N     1 
ATOM   19057 C  CA    . PRO A 1 4135 ? 157.956 149.175 171.061 1.00 14.96  ? 4135 PRO A CA    1 
ATOM   19058 C  C     . PRO A 1 4135 ? 158.515 147.762 170.978 1.00 14.88  ? 4135 PRO A C     1 
ATOM   19059 O  O     . PRO A 1 4135 ? 158.262 147.026 170.022 1.00 15.98  ? 4135 PRO A O     1 
ATOM   19060 C  CB    . PRO A 1 4135 ? 156.485 149.171 171.491 1.00 14.82  ? 4135 PRO A CB    1 
ATOM   19061 C  CG    . PRO A 1 4135 ? 155.852 150.264 170.703 1.00 15.26  ? 4135 PRO A CG    1 
ATOM   19062 C  CD    . PRO A 1 4135 ? 156.573 150.296 169.394 1.00 13.18  ? 4135 PRO A CD    1 
ATOM   19063 N  N     . VAL A 1 4136 ? 159.281 147.388 172.004 1.00 15.05  ? 4136 VAL A N     1 
ATOM   19064 C  CA    . VAL A 1 4136 ? 159.872 146.054 172.053 1.00 13.22  ? 4136 VAL A CA    1 
ATOM   19065 C  C     . VAL A 1 4136 ? 158.788 144.997 172.223 1.00 12.01  ? 4136 VAL A C     1 
ATOM   19066 O  O     . VAL A 1 4136 ? 158.867 143.906 171.643 1.00 16.12  ? 4136 VAL A O     1 
ATOM   19067 C  CB    . VAL A 1 4136 ? 160.923 145.985 173.176 1.00 9.29   ? 4136 VAL A CB    1 
ATOM   19068 C  CG1   . VAL A 1 4136 ? 161.254 144.543 173.524 1.00 13.85  ? 4136 VAL A CG1   1 
ATOM   19069 C  CG2   . VAL A 1 4136 ? 162.179 146.734 172.770 1.00 8.10   ? 4136 VAL A CG2   1 
ATOM   19070 N  N     . ASN A 1 4137 ? 157.757 145.305 173.011 1.00 13.04  ? 4137 ASN A N     1 
ATOM   19071 C  CA    . ASN A 1 4137 ? 156.694 144.337 173.258 1.00 13.75  ? 4137 ASN A CA    1 
ATOM   19072 C  C     . ASN A 1 4137 ? 155.935 144.025 171.973 1.00 13.90  ? 4137 ASN A C     1 
ATOM   19073 O  O     . ASN A 1 4137 ? 155.557 142.873 171.729 1.00 13.58  ? 4137 ASN A O     1 
ATOM   19074 C  CB    . ASN A 1 4137 ? 155.757 144.873 174.344 1.00 21.84  ? 4137 ASN A CB    1 
ATOM   19075 C  CG    . ASN A 1 4137 ? 154.747 143.841 174.820 1.00 36.95  ? 4137 ASN A CG    1 
ATOM   19076 O  OD1   . ASN A 1 4137 ? 154.707 142.712 174.333 1.00 37.61  ? 4137 ASN A OD1   1 
ATOM   19077 N  ND2   . ASN A 1 4137 ? 153.929 144.228 175.791 1.00 32.56  ? 4137 ASN A ND2   1 
ATOM   19078 N  N     . LEU A 1 4138 ? 155.711 145.038 171.131 1.00 13.36  ? 4138 LEU A N     1 
ATOM   19079 C  CA    . LEU A 1 4138 ? 155.091 144.800 169.831 1.00 12.01  ? 4138 LEU A CA    1 
ATOM   19080 C  C     . LEU A 1 4138 ? 155.969 143.918 168.952 1.00 10.85  ? 4138 LEU A C     1 
ATOM   19081 O  O     . LEU A 1 4138 ? 155.465 143.046 168.234 1.00 11.36  ? 4138 LEU A O     1 
ATOM   19082 C  CB    . LEU A 1 4138 ? 154.806 146.125 169.127 1.00 11.91  ? 4138 LEU A CB    1 
ATOM   19083 C  CG    . LEU A 1 4138 ? 154.134 145.985 167.759 1.00 12.71  ? 4138 LEU A CG    1 
ATOM   19084 C  CD1   . LEU A 1 4138 ? 152.629 145.830 167.903 1.00 15.48  ? 4138 LEU A CD1   1 
ATOM   19085 C  CD2   . LEU A 1 4138 ? 154.481 147.148 166.854 1.00 11.29  ? 4138 LEU A CD2   1 
ATOM   19086 N  N     . LEU A 1 4139 ? 157.285 144.141 168.982 1.00 10.69  ? 4139 LEU A N     1 
ATOM   19087 C  CA    . LEU A 1 4139 ? 158.196 143.298 168.214 1.00 9.12   ? 4139 LEU A CA    1 
ATOM   19088 C  C     . LEU A 1 4139 ? 158.131 141.852 168.685 1.00 8.54   ? 4139 LEU A C     1 
ATOM   19089 O  O     . LEU A 1 4139 ? 158.141 140.923 167.869 1.00 10.52  ? 4139 LEU A O     1 
ATOM   19090 C  CB    . LEU A 1 4139 ? 159.625 143.829 168.324 1.00 12.49  ? 4139 LEU A CB    1 
ATOM   19091 C  CG    . LEU A 1 4139 ? 159.936 145.175 167.670 1.00 11.06  ? 4139 LEU A CG    1 
ATOM   19092 C  CD1   . LEU A 1 4139 ? 161.355 145.600 167.997 1.00 8.11   ? 4139 LEU A CD1   1 
ATOM   19093 C  CD2   . LEU A 1 4139 ? 159.733 145.102 166.168 1.00 11.90  ? 4139 LEU A CD2   1 
ATOM   19094 N  N     . ARG A 1 4140 ? 158.067 141.643 170.001 1.00 8.61   ? 4140 ARG A N     1 
ATOM   19095 C  CA    . ARG A 1 4140 ? 157.965 140.288 170.530 1.00 8.97   ? 4140 ARG A CA    1 
ATOM   19096 C  C     . ARG A 1 4140 ? 156.617 139.658 170.206 1.00 8.81   ? 4140 ARG A C     1 
ATOM   19097 O  O     . ARG A 1 4140 ? 156.529 138.435 170.045 1.00 8.61   ? 4140 ARG A O     1 
ATOM   19098 C  CB    . ARG A 1 4140 ? 158.191 140.297 172.041 1.00 9.76   ? 4140 ARG A CB    1 
ATOM   19099 C  CG    . ARG A 1 4140 ? 159.615 140.610 172.458 1.00 11.44  ? 4140 ARG A CG    1 
ATOM   19100 C  CD    . ARG A 1 4140 ? 159.756 140.601 173.970 1.00 12.45  ? 4140 ARG A CD    1 
ATOM   19101 N  NE    . ARG A 1 4140 ? 160.494 139.434 174.440 1.00 14.68  ? 4140 ARG A NE    1 
ATOM   19102 C  CZ    . ARG A 1 4140 ? 159.971 138.466 175.180 1.00 19.04  ? 4140 ARG A CZ    1 
ATOM   19103 N  NH1   . ARG A 1 4140 ? 158.702 138.488 175.552 1.00 20.80  ? 4140 ARG A NH1   1 
ATOM   19104 N  NH2   . ARG A 1 4140 ? 160.741 137.447 175.552 1.00 21.02  ? 4140 ARG A NH2   1 
ATOM   19105 N  N     . ALA A 1 4141 ? 155.563 140.469 170.104 1.00 8.79   ? 4141 ALA A N     1 
ATOM   19106 C  CA    . ALA A 1 4141 ? 154.221 139.935 169.903 1.00 7.86   ? 4141 ALA A CA    1 
ATOM   19107 C  C     . ALA A 1 4141 ? 153.991 139.423 168.488 1.00 11.31  ? 4141 ALA A C     1 
ATOM   19108 O  O     . ALA A 1 4141 ? 153.091 138.602 168.282 1.00 17.91  ? 4141 ALA A O     1 
ATOM   19109 C  CB    . ALA A 1 4141 ? 153.180 141.002 170.239 1.00 11.98  ? 4141 ALA A CB    1 
ATOM   19110 N  N     . GLY A 1 4142 ? 154.778 139.879 167.510 1.00 11.19  ? 4142 GLY A N     1 
ATOM   19111 C  CA    . GLY A 1 4142 ? 154.565 139.509 166.130 1.00 8.44   ? 4142 GLY A CA    1 
ATOM   19112 C  C     . GLY A 1 4142 ? 155.829 138.948 165.503 1.00 7.82   ? 4142 GLY A C     1 
ATOM   19113 O  O     . GLY A 1 4142 ? 156.919 139.022 166.072 1.00 10.58  ? 4142 GLY A O     1 
ATOM   19114 N  N     . ARG A 1 4143 ? 155.657 138.381 164.312 1.00 9.18   ? 4143 ARG A N     1 
ATOM   19115 C  CA    . ARG A 1 4143 ? 156.767 137.827 163.550 1.00 8.86   ? 4143 ARG A CA    1 
ATOM   19116 C  C     . ARG A 1 4143 ? 157.343 138.894 162.630 1.00 8.42   ? 4143 ARG A C     1 
ATOM   19117 O  O     . ARG A 1 4143 ? 156.601 139.566 161.904 1.00 8.32   ? 4143 ARG A O     1 
ATOM   19118 C  CB    . ARG A 1 4143 ? 156.324 136.608 162.741 1.00 7.33   ? 4143 ARG A CB    1 
ATOM   19119 C  CG    . ARG A 1 4143 ? 157.463 135.941 161.991 1.00 13.79  ? 4143 ARG A CG    1 
ATOM   19120 C  CD    . ARG A 1 4143 ? 157.173 134.486 161.685 1.00 17.31  ? 4143 ARG A CD    1 
ATOM   19121 N  NE    . ARG A 1 4143 ? 158.186 133.914 160.806 1.00 17.37  ? 4143 ARG A NE    1 
ATOM   19122 C  CZ    . ARG A 1 4143 ? 158.089 132.729 160.221 1.00 27.31  ? 4143 ARG A CZ    1 
ATOM   19123 N  NH1   . ARG A 1 4143 ? 157.040 131.947 160.413 1.00 27.62  ? 4143 ARG A NH1   1 
ATOM   19124 N  NH2   . ARG A 1 4143 ? 159.069 132.319 159.420 1.00 20.62  ? 4143 ARG A NH2   1 
ATOM   19125 N  N     . ILE A 1 4144 ? 158.666 139.033 162.653 1.00 6.96   ? 4144 ILE A N     1 
ATOM   19126 C  CA    . ILE A 1 4144 ? 159.375 140.115 161.980 1.00 6.35   ? 4144 ILE A CA    1 
ATOM   19127 C  C     . ILE A 1 4144 ? 159.963 139.608 160.673 1.00 8.06   ? 4144 ILE A C     1 
ATOM   19128 O  O     . ILE A 1 4144 ? 160.546 138.518 160.618 1.00 8.51   ? 4144 ILE A O     1 
ATOM   19129 C  CB    . ILE A 1 4144 ? 160.475 140.697 162.888 1.00 6.42   ? 4144 ILE A CB    1 
ATOM   19130 C  CG1   . ILE A 1 4144 ? 159.879 141.147 164.222 1.00 8.35   ? 4144 ILE A CG1   1 
ATOM   19131 C  CG2   . ILE A 1 4144 ? 161.193 141.846 162.201 1.00 7.32   ? 4144 ILE A CG2   1 
ATOM   19132 C  CD1   . ILE A 1 4144 ? 160.912 141.436 165.280 1.00 9.48   ? 4144 ILE A CD1   1 
ATOM   19133 N  N     . PHE A 1 4145 ? 159.798 140.396 159.613 1.00 9.60   ? 4145 PHE A N     1 
ATOM   19134 C  CA    . PHE A 1 4145 ? 160.420 140.148 158.321 1.00 6.29   ? 4145 PHE A CA    1 
ATOM   19135 C  C     . PHE A 1 4145 ? 161.167 141.403 157.900 1.00 9.44   ? 4145 PHE A C     1 
ATOM   19136 O  O     . PHE A 1 4145 ? 160.579 142.488 157.842 1.00 11.28  ? 4145 PHE A O     1 
ATOM   19137 C  CB    . PHE A 1 4145 ? 159.380 139.769 157.264 1.00 7.66   ? 4145 PHE A CB    1 
ATOM   19138 C  CG    . PHE A 1 4145 ? 158.631 138.512 157.582 1.00 12.34  ? 4145 PHE A CG    1 
ATOM   19139 C  CD1   . PHE A 1 4145 ? 159.165 137.276 157.270 1.00 11.31  ? 4145 PHE A CD1   1 
ATOM   19140 C  CD2   . PHE A 1 4145 ? 157.400 138.565 158.211 1.00 11.87  ? 4145 PHE A CD2   1 
ATOM   19141 C  CE1   . PHE A 1 4145 ? 158.481 136.119 157.566 1.00 11.91  ? 4145 PHE A CE1   1 
ATOM   19142 C  CE2   . PHE A 1 4145 ? 156.714 137.410 158.511 1.00 11.31  ? 4145 PHE A CE2   1 
ATOM   19143 C  CZ    . PHE A 1 4145 ? 157.254 136.187 158.188 1.00 15.51  ? 4145 PHE A CZ    1 
ATOM   19144 N  N     . VAL A 1 4146 ? 162.453 141.252 157.603 1.00 7.21   ? 4146 VAL A N     1 
ATOM   19145 C  CA    . VAL A 1 4146 ? 163.312 142.365 157.224 1.00 6.93   ? 4146 VAL A CA    1 
ATOM   19146 C  C     . VAL A 1 4146 ? 163.402 142.416 155.706 1.00 7.66   ? 4146 VAL A C     1 
ATOM   19147 O  O     . VAL A 1 4146 ? 163.709 141.407 155.059 1.00 16.70  ? 4146 VAL A O     1 
ATOM   19148 C  CB    . VAL A 1 4146 ? 164.707 142.233 157.858 1.00 6.88   ? 4146 VAL A CB    1 
ATOM   19149 C  CG1   . VAL A 1 4146 ? 165.704 143.130 157.148 1.00 8.20   ? 4146 VAL A CG1   1 
ATOM   19150 C  CG2   . VAL A 1 4146 ? 164.644 142.575 159.334 1.00 6.46   ? 4146 VAL A CG2   1 
ATOM   19151 N  N     . PHE A 1 4147 ? 163.125 143.584 155.138 1.00 7.98   ? 4147 PHE A N     1 
ATOM   19152 C  CA    . PHE A 1 4147 ? 163.203 143.795 153.698 1.00 9.93   ? 4147 PHE A CA    1 
ATOM   19153 C  C     . PHE A 1 4147 ? 164.362 144.735 153.399 1.00 8.81   ? 4147 PHE A C     1 
ATOM   19154 O  O     . PHE A 1 4147 ? 164.407 145.858 153.913 1.00 9.90   ? 4147 PHE A O     1 
ATOM   19155 C  CB    . PHE A 1 4147 ? 161.888 144.350 153.152 1.00 11.18  ? 4147 PHE A CB    1 
ATOM   19156 C  CG    . PHE A 1 4147 ? 160.766 143.353 153.160 1.00 15.02  ? 4147 PHE A CG    1 
ATOM   19157 C  CD1   . PHE A 1 4147 ? 159.974 143.191 154.283 1.00 14.08  ? 4147 PHE A CD1   1 
ATOM   19158 C  CD2   . PHE A 1 4147 ? 160.520 142.560 152.055 1.00 21.16  ? 4147 PHE A CD2   1 
ATOM   19159 C  CE1   . PHE A 1 4147 ? 158.948 142.271 154.296 1.00 13.88  ? 4147 PHE A CE1   1 
ATOM   19160 C  CE2   . PHE A 1 4147 ? 159.496 141.635 152.064 1.00 25.86  ? 4147 PHE A CE2   1 
ATOM   19161 C  CZ    . PHE A 1 4147 ? 158.708 141.492 153.186 1.00 20.01  ? 4147 PHE A CZ    1 
ATOM   19162 N  N     . GLU A 1 4148 ? 165.289 144.275 152.569 1.00 9.20   ? 4148 GLU A N     1 
ATOM   19163 C  CA    . GLU A 1 4148 ? 166.517 145.001 152.281 1.00 7.79   ? 4148 GLU A CA    1 
ATOM   19164 C  C     . GLU A 1 4148 ? 166.975 144.606 150.889 1.00 12.50  ? 4148 GLU A C     1 
ATOM   19165 O  O     . GLU A 1 4148 ? 166.386 143.715 150.263 1.00 15.97  ? 4148 GLU A O     1 
ATOM   19166 C  CB    . GLU A 1 4148 ? 167.598 144.697 153.327 1.00 9.85   ? 4148 GLU A CB    1 
ATOM   19167 C  CG    . GLU A 1 4148 ? 167.767 143.227 153.653 1.00 11.41  ? 4148 GLU A CG    1 
ATOM   19168 C  CD    . GLU A 1 4148 ? 168.855 142.988 154.679 1.00 14.18  ? 4148 GLU A CD    1 
ATOM   19169 O  OE1   . GLU A 1 4148 ? 169.545 143.958 155.052 1.00 10.18  ? 4148 GLU A OE1   1 
ATOM   19170 O  OE2   . GLU A 1 4148 ? 169.019 141.830 155.113 1.00 24.58  ? 4148 GLU A OE2   1 
ATOM   19171 N  N     . PRO A 1 4149 ? 168.007 145.263 150.359 1.00 14.99  ? 4149 PRO A N     1 
ATOM   19172 C  CA    . PRO A 1 4149 ? 168.559 144.846 149.064 1.00 11.77  ? 4149 PRO A CA    1 
ATOM   19173 C  C     . PRO A 1 4149 ? 169.001 143.395 149.096 1.00 10.97  ? 4149 PRO A C     1 
ATOM   19174 O  O     . PRO A 1 4149 ? 169.520 142.916 150.116 1.00 17.01  ? 4149 PRO A O     1 
ATOM   19175 C  CB    . PRO A 1 4149 ? 169.755 145.788 148.871 1.00 12.79  ? 4149 PRO A CB    1 
ATOM   19176 C  CG    . PRO A 1 4149 ? 169.377 147.008 149.605 1.00 13.59  ? 4149 PRO A CG    1 
ATOM   19177 C  CD    . PRO A 1 4149 ? 168.551 146.569 150.781 1.00 12.93  ? 4149 PRO A CD    1 
ATOM   19178 N  N     . PRO A 1 4150 ? 168.800 142.661 148.003 1.00 11.00  ? 4150 PRO A N     1 
ATOM   19179 C  CA    . PRO A 1 4150 ? 169.207 141.262 147.982 1.00 12.62  ? 4150 PRO A CA    1 
ATOM   19180 C  C     . PRO A 1 4150 ? 170.707 141.136 148.148 1.00 14.28  ? 4150 PRO A C     1 
ATOM   19181 O  O     . PRO A 1 4150 ? 171.474 142.032 147.746 1.00 17.36  ? 4150 PRO A O     1 
ATOM   19182 C  CB    . PRO A 1 4150 ? 168.749 140.783 146.597 1.00 9.75   ? 4150 PRO A CB    1 
ATOM   19183 C  CG    . PRO A 1 4150 ? 167.646 141.712 146.228 1.00 10.80  ? 4150 PRO A CG    1 
ATOM   19184 C  CD    . PRO A 1 4150 ? 168.050 143.038 146.794 1.00 14.80  ? 4150 PRO A CD    1 
ATOM   19185 N  N     . PRO A 1 4151 ? 171.175 140.038 148.746 1.00 12.11  ? 4151 PRO A N     1 
ATOM   19186 C  CA    . PRO A 1 4151 ? 172.606 139.931 149.078 1.00 13.69  ? 4151 PRO A CA    1 
ATOM   19187 C  C     . PRO A 1 4151 ? 173.540 140.016 147.883 1.00 17.68  ? 4151 PRO A C     1 
ATOM   19188 O  O     . PRO A 1 4151 ? 174.679 140.472 148.041 1.00 23.68  ? 4151 PRO A O     1 
ATOM   19189 C  CB    . PRO A 1 4151 ? 172.700 138.561 149.767 1.00 9.25   ? 4151 PRO A CB    1 
ATOM   19190 C  CG    . PRO A 1 4151 ? 171.468 137.828 149.357 1.00 12.79  ? 4151 PRO A CG    1 
ATOM   19191 C  CD    . PRO A 1 4151 ? 170.412 138.870 149.211 1.00 10.78  ? 4151 PRO A CD    1 
ATOM   19192 N  N     . GLY A 1 4152 ? 173.110 139.592 146.697 1.00 12.77  ? 4152 GLY A N     1 
ATOM   19193 C  CA    . GLY A 1 4152 ? 173.999 139.583 145.556 1.00 11.04  ? 4152 GLY A CA    1 
ATOM   19194 C  C     . GLY A 1 4152 ? 173.254 139.711 144.245 1.00 8.87   ? 4152 GLY A C     1 
ATOM   19195 O  O     . GLY A 1 4152 ? 172.036 139.892 144.210 1.00 12.65  ? 4152 GLY A O     1 
ATOM   19196 N  N     . VAL A 1 4153 ? 174.017 139.616 143.154 1.00 7.69   ? 4153 VAL A N     1 
ATOM   19197 C  CA    . VAL A 1 4153 ? 173.442 139.735 141.817 1.00 7.91   ? 4153 VAL A CA    1 
ATOM   19198 C  C     . VAL A 1 4153 ? 172.478 138.588 141.544 1.00 7.16   ? 4153 VAL A C     1 
ATOM   19199 O  O     . VAL A 1 4153 ? 171.380 138.792 141.010 1.00 7.21   ? 4153 VAL A O     1 
ATOM   19200 C  CB    . VAL A 1 4153 ? 174.563 139.797 140.762 1.00 5.56   ? 4153 VAL A CB    1 
ATOM   19201 C  CG1   . VAL A 1 4153 ? 174.003 139.580 139.366 1.00 4.80   ? 4153 VAL A CG1   1 
ATOM   19202 C  CG2   . VAL A 1 4153 ? 175.294 141.124 140.846 1.00 7.52   ? 4153 VAL A CG2   1 
ATOM   19203 N  N     . LYS A 1 4154 ? 172.872 137.365 141.904 1.00 6.50   ? 4154 LYS A N     1 
ATOM   19204 C  CA    . LYS A 1 4154 ? 172.022 136.204 141.659 1.00 5.42   ? 4154 LYS A CA    1 
ATOM   19205 C  C     . LYS A 1 4154 ? 170.714 136.310 142.431 1.00 5.77   ? 4154 LYS A C     1 
ATOM   19206 O  O     . LYS A 1 4154 ? 169.631 136.081 141.878 1.00 6.11   ? 4154 LYS A O     1 
ATOM   19207 C  CB    . LYS A 1 4154 ? 172.773 134.926 142.035 1.00 5.28   ? 4154 LYS A CB    1 
ATOM   19208 C  CG    . LYS A 1 4154 ? 171.987 133.647 141.820 1.00 5.95   ? 4154 LYS A CG    1 
ATOM   19209 C  CD    . LYS A 1 4154 ? 172.759 132.442 142.324 1.00 8.42   ? 4154 LYS A CD    1 
ATOM   19210 C  CE    . LYS A 1 4154 ? 171.897 131.195 142.326 1.00 13.59  ? 4154 LYS A CE    1 
ATOM   19211 N  NZ    . LYS A 1 4154 ? 172.606 130.033 142.927 1.00 16.53  ? 4154 LYS A NZ    1 
ATOM   19212 N  N     . ALA A 1 4155 ? 170.797 136.667 143.714 1.00 6.42   ? 4155 ALA A N     1 
ATOM   19213 C  CA    . ALA A 1 4155 ? 169.592 136.823 144.521 1.00 6.12   ? 4155 ALA A CA    1 
ATOM   19214 C  C     . ALA A 1 4155 ? 168.717 137.951 143.994 1.00 5.93   ? 4155 ALA A C     1 
ATOM   19215 O  O     . ALA A 1 4155 ? 167.487 137.829 143.963 1.00 9.37   ? 4155 ALA A O     1 
ATOM   19216 C  CB    . ALA A 1 4155 ? 169.968 137.072 145.981 1.00 6.43   ? 4155 ALA A CB    1 
ATOM   19217 N  N     . ASN A 1 4156 ? 169.335 139.059 143.578 1.00 6.13   ? 4156 ASN A N     1 
ATOM   19218 C  CA    . ASN A 1 4156 ? 168.568 140.179 143.044 1.00 5.40   ? 4156 ASN A CA    1 
ATOM   19219 C  C     . ASN A 1 4156 ? 167.818 139.776 141.783 1.00 5.99   ? 4156 ASN A C     1 
ATOM   19220 O  O     . ASN A 1 4156 ? 166.634 140.097 141.625 1.00 6.13   ? 4156 ASN A O     1 
ATOM   19221 C  CB    . ASN A 1 4156 ? 169.501 141.363 142.776 1.00 5.54   ? 4156 ASN A CB    1 
ATOM   19222 C  CG    . ASN A 1 4156 ? 168.762 142.612 142.326 1.00 6.88   ? 4156 ASN A CG    1 
ATOM   19223 O  OD1   . ASN A 1 4156 ? 168.090 142.622 141.296 1.00 10.29  ? 4156 ASN A OD1   1 
ATOM   19224 N  ND2   . ASN A 1 4156 ? 168.884 143.677 143.108 1.00 5.00   ? 4156 ASN A ND2   1 
ATOM   19225 N  N     . MET A 1 4157 ? 168.484 139.055 140.879 1.00 5.92   ? 4157 MET A N     1 
ATOM   19226 C  CA    . MET A 1 4157 ? 167.829 138.650 139.641 1.00 4.79   ? 4157 MET A CA    1 
ATOM   19227 C  C     . MET A 1 4157 ? 166.735 137.624 139.909 1.00 6.69   ? 4157 MET A C     1 
ATOM   19228 O  O     . MET A 1 4157 ? 165.681 137.650 139.262 1.00 9.65   ? 4157 MET A O     1 
ATOM   19229 C  CB    . MET A 1 4157 ? 168.860 138.100 138.657 1.00 4.18   ? 4157 MET A CB    1 
ATOM   19230 C  CG    . MET A 1 4157 ? 169.751 139.171 138.054 1.00 4.12   ? 4157 MET A CG    1 
ATOM   19231 S  SD    . MET A 1 4157 ? 170.526 138.690 136.504 1.00 7.50   ? 4157 MET A SD    1 
ATOM   19232 C  CE    . MET A 1 4157 ? 169.101 138.113 135.594 1.00 7.72   ? 4157 MET A CE    1 
ATOM   19233 N  N     . LEU A 1 4158 ? 166.963 136.714 140.861 1.00 8.22   ? 4158 LEU A N     1 
ATOM   19234 C  CA    . LEU A 1 4158 ? 165.925 135.753 141.222 1.00 5.64   ? 4158 LEU A CA    1 
ATOM   19235 C  C     . LEU A 1 4158 ? 164.701 136.455 141.793 1.00 6.50   ? 4158 LEU A C     1 
ATOM   19236 O  O     . LEU A 1 4158 ? 163.563 136.113 141.449 1.00 10.61  ? 4158 LEU A O     1 
ATOM   19237 C  CB    . LEU A 1 4158 ? 166.472 134.733 142.219 1.00 6.13   ? 4158 LEU A CB    1 
ATOM   19238 C  CG    . LEU A 1 4158 ? 167.382 133.644 141.649 1.00 7.29   ? 4158 LEU A CG    1 
ATOM   19239 C  CD1   . LEU A 1 4158 ? 167.914 132.758 142.760 1.00 11.08  ? 4158 LEU A CD1   1 
ATOM   19240 C  CD2   . LEU A 1 4158 ? 166.647 132.817 140.609 1.00 4.64   ? 4158 LEU A CD2   1 
ATOM   19241 N  N     . ARG A 1 4159 ? 164.913 137.446 142.663 1.00 6.47   ? 4159 ARG A N     1 
ATOM   19242 C  CA    . ARG A 1 4159 ? 163.791 138.205 143.204 1.00 7.97   ? 4159 ARG A CA    1 
ATOM   19243 C  C     . ARG A 1 4159 ? 163.058 138.963 142.105 1.00 9.54   ? 4159 ARG A C     1 
ATOM   19244 O  O     . ARG A 1 4159 ? 161.823 139.012 142.092 1.00 11.37  ? 4159 ARG A O     1 
ATOM   19245 C  CB    . ARG A 1 4159 ? 164.279 139.172 144.281 1.00 7.37   ? 4159 ARG A CB    1 
ATOM   19246 C  CG    . ARG A 1 4159 ? 163.176 140.026 144.884 1.00 9.18   ? 4159 ARG A CG    1 
ATOM   19247 C  CD    . ARG A 1 4159 ? 163.733 141.049 145.854 1.00 18.24  ? 4159 ARG A CD    1 
ATOM   19248 N  NE    . ARG A 1 4159 ? 164.592 140.442 146.863 1.00 29.13  ? 4159 ARG A NE    1 
ATOM   19249 C  CZ    . ARG A 1 4159 ? 164.740 140.905 148.096 1.00 25.78  ? 4159 ARG A CZ    1 
ATOM   19250 N  NH1   . ARG A 1 4159 ? 164.096 141.984 148.511 1.00 19.20  ? 4159 ARG A NH1   1 
ATOM   19251 N  NH2   . ARG A 1 4159 ? 165.557 140.273 148.933 1.00 19.17  ? 4159 ARG A NH2   1 
ATOM   19252 N  N     . THR A 1 4160 ? 163.806 139.562 141.176 1.00 9.42   ? 4160 THR A N     1 
ATOM   19253 C  CA    . THR A 1 4160 ? 163.178 140.295 140.082 1.00 7.21   ? 4160 THR A CA    1 
ATOM   19254 C  C     . THR A 1 4160 ? 162.323 139.373 139.223 1.00 10.89  ? 4160 THR A C     1 
ATOM   19255 O  O     . THR A 1 4160 ? 161.195 139.722 138.856 1.00 14.26  ? 4160 THR A O     1 
ATOM   19256 C  CB    . THR A 1 4160 ? 164.248 140.984 139.233 1.00 7.56   ? 4160 THR A CB    1 
ATOM   19257 O  OG1   . THR A 1 4160 ? 164.772 142.111 139.944 1.00 9.69   ? 4160 THR A OG1   1 
ATOM   19258 C  CG2   . THR A 1 4160 ? 163.665 141.456 137.912 1.00 7.90   ? 4160 THR A CG2   1 
ATOM   19259 N  N     . PHE A 1 4161 ? 162.838 138.184 138.904 1.00 12.30  ? 4161 PHE A N     1 
ATOM   19260 C  CA    . PHE A 1 4161 ? 162.075 137.251 138.082 1.00 12.18  ? 4161 PHE A CA    1 
ATOM   19261 C  C     . PHE A 1 4161 ? 160.880 136.681 138.833 1.00 12.12  ? 4161 PHE A C     1 
ATOM   19262 O  O     . PHE A 1 4161 ? 159.849 136.388 138.217 1.00 18.17  ? 4161 PHE A O     1 
ATOM   19263 C  CB    . PHE A 1 4161 ? 162.982 136.130 137.580 1.00 11.06  ? 4161 PHE A CB    1 
ATOM   19264 C  CG    . PHE A 1 4161 ? 163.717 136.472 136.318 1.00 15.35  ? 4161 PHE A CG    1 
ATOM   19265 C  CD1   . PHE A 1 4161 ? 163.023 136.750 135.154 1.00 12.42  ? 4161 PHE A CD1   1 
ATOM   19266 C  CD2   . PHE A 1 4161 ? 165.099 136.524 136.296 1.00 20.04  ? 4161 PHE A CD2   1 
ATOM   19267 C  CE1   . PHE A 1 4161 ? 163.694 137.069 133.990 1.00 13.83  ? 4161 PHE A CE1   1 
ATOM   19268 C  CE2   . PHE A 1 4161 ? 165.775 136.843 135.135 1.00 15.13  ? 4161 PHE A CE2   1 
ATOM   19269 C  CZ    . PHE A 1 4161 ? 165.072 137.115 133.982 1.00 12.24  ? 4161 PHE A CZ    1 
ATOM   19270 N  N     . SER A 1 4162 ? 160.991 136.516 140.152 1.00 10.64  ? 4162 SER A N     1 
ATOM   19271 C  CA    . SER A 1 4162 ? 159.856 136.028 140.926 1.00 13.15  ? 4162 SER A CA    1 
ATOM   19272 C  C     . SER A 1 4162 ? 158.764 137.083 141.055 1.00 15.79  ? 4162 SER A C     1 
ATOM   19273 O  O     . SER A 1 4162 ? 157.576 136.743 141.055 1.00 19.51  ? 4162 SER A O     1 
ATOM   19274 C  CB    . SER A 1 4162 ? 160.321 135.574 142.309 1.00 12.73  ? 4162 SER A CB    1 
ATOM   19275 O  OG    . SER A 1 4162 ? 160.466 136.678 143.184 1.00 20.57  ? 4162 SER A OG    1 
ATOM   19276 N  N     . SER A 1 4163 ? 159.142 138.359 141.170 1.00 16.37  ? 4163 SER A N     1 
ATOM   19277 C  CA    . SER A 1 4163 ? 158.146 139.413 141.338 1.00 13.36  ? 4163 SER A CA    1 
ATOM   19278 C  C     . SER A 1 4163 ? 157.322 139.614 140.071 1.00 16.48  ? 4163 SER A C     1 
ATOM   19279 O  O     . SER A 1 4163 ? 156.098 139.777 140.140 1.00 28.63  ? 4163 SER A O     1 
ATOM   19280 C  CB    . SER A 1 4163 ? 158.827 140.717 141.748 1.00 16.07  ? 4163 SER A CB    1 
ATOM   19281 O  OG    . SER A 1 4163 ? 159.428 141.354 140.634 1.00 20.36  ? 4163 SER A OG    1 
ATOM   19282 N  N     . ILE A 1 4164 ? 157.968 139.612 138.913 1.00 15.33  ? 4164 ILE A N     1 
ATOM   19283 C  CA    . ILE A 1 4164 ? 157.248 139.824 137.652 1.00 17.85  ? 4164 ILE A CA    1 
ATOM   19284 C  C     . ILE A 1 4164 ? 156.436 138.577 137.319 1.00 18.90  ? 4164 ILE A C     1 
ATOM   19285 O  O     . ILE A 1 4164 ? 156.969 137.456 137.396 1.00 21.23  ? 4164 ILE A O     1 
ATOM   19286 C  CB    . ILE A 1 4164 ? 158.229 140.161 136.529 1.00 18.72  ? 4164 ILE A CB    1 
ATOM   19287 C  CG1   . ILE A 1 4164 ? 159.071 141.380 136.906 1.00 14.06  ? 4164 ILE A CG1   1 
ATOM   19288 C  CG2   . ILE A 1 4164 ? 157.490 140.407 135.224 1.00 22.03  ? 4164 ILE A CG2   1 
ATOM   19289 C  CD1   . ILE A 1 4164 ? 160.116 141.733 135.880 1.00 17.46  ? 4164 ILE A CD1   1 
ATOM   19290 N  N     . PRO A 1 4165 ? 155.160 138.712 136.956 1.00 24.87  ? 4165 PRO A N     1 
ATOM   19291 C  CA    . PRO A 1 4165 ? 154.365 137.532 136.595 1.00 21.97  ? 4165 PRO A CA    1 
ATOM   19292 C  C     . PRO A 1 4165 ? 154.920 136.829 135.366 1.00 20.71  ? 4165 PRO A C     1 
ATOM   19293 O  O     . PRO A 1 4165 ? 155.509 137.448 134.478 1.00 24.84  ? 4165 PRO A O     1 
ATOM   19294 C  CB    . PRO A 1 4165 ? 152.972 138.112 136.323 1.00 19.40  ? 4165 PRO A CB    1 
ATOM   19295 C  CG    . PRO A 1 4165 ? 152.953 139.417 137.045 1.00 19.99  ? 4165 PRO A CG    1 
ATOM   19296 C  CD    . PRO A 1 4165 ? 154.350 139.941 136.975 1.00 23.35  ? 4165 PRO A CD    1 
ATOM   19297 N  N     . VAL A 1 4166 ? 154.728 135.509 135.330 1.00 24.39  ? 4166 VAL A N     1 
ATOM   19298 C  CA    . VAL A 1 4166 ? 155.219 134.711 134.210 1.00 28.14  ? 4166 VAL A CA    1 
ATOM   19299 C  C     . VAL A 1 4166 ? 154.496 135.089 132.923 1.00 30.01  ? 4166 VAL A C     1 
ATOM   19300 O  O     . VAL A 1 4166 ? 155.105 135.147 131.848 1.00 33.06  ? 4166 VAL A O     1 
ATOM   19301 C  CB    . VAL A 1 4166 ? 155.074 133.210 134.522 1.00 26.72  ? 4166 VAL A CB    1 
ATOM   19302 C  CG1   . VAL A 1 4166 ? 155.761 132.375 133.454 1.00 23.70  ? 4166 VAL A CG1   1 
ATOM   19303 C  CG2   . VAL A 1 4166 ? 155.643 132.897 135.895 1.00 27.54  ? 4166 VAL A CG2   1 
ATOM   19304 N  N     . SER A 1 4167 ? 153.189 135.346 133.008 1.00 31.79  ? 4167 SER A N     1 
ATOM   19305 C  CA    . SER A 1 4167 ? 152.422 135.695 131.816 1.00 30.36  ? 4167 SER A CA    1 
ATOM   19306 C  C     . SER A 1 4167 ? 152.882 137.015 131.212 1.00 32.02  ? 4167 SER A C     1 
ATOM   19307 O  O     . SER A 1 4167 ? 152.731 137.227 130.003 1.00 36.69  ? 4167 SER A O     1 
ATOM   19308 C  CB    . SER A 1 4167 ? 150.933 135.762 132.150 1.00 28.02  ? 4167 SER A CB    1 
ATOM   19309 O  OG    . SER A 1 4167 ? 150.671 136.783 133.095 1.00 29.05  ? 4167 SER A OG    1 
ATOM   19310 N  N     . ARG A 1 4168 ? 153.433 137.913 132.029 1.00 29.30  ? 4168 ARG A N     1 
ATOM   19311 C  CA    . ARG A 1 4168 ? 153.912 139.190 131.511 1.00 23.94  ? 4168 ARG A CA    1 
ATOM   19312 C  C     . ARG A 1 4168 ? 155.141 139.000 130.632 1.00 29.67  ? 4168 ARG A C     1 
ATOM   19313 O  O     . ARG A 1 4168 ? 155.237 139.583 129.545 1.00 34.91  ? 4168 ARG A O     1 
ATOM   19314 C  CB    . ARG A 1 4168 ? 154.217 140.142 132.666 1.00 20.73  ? 4168 ARG A CB    1 
ATOM   19315 C  CG    . ARG A 1 4168 ? 154.908 141.422 132.239 1.00 25.17  ? 4168 ARG A CG    1 
ATOM   19316 C  CD    . ARG A 1 4168 ? 154.907 142.452 133.351 1.00 26.92  ? 4168 ARG A CD    1 
ATOM   19317 N  NE    . ARG A 1 4168 ? 154.789 143.808 132.829 1.00 19.81  ? 4168 ARG A NE    1 
ATOM   19318 C  CZ    . ARG A 1 4168 ? 154.887 144.904 133.568 1.00 18.81  ? 4168 ARG A CZ    1 
ATOM   19319 N  NH1   . ARG A 1 4168 ? 155.121 144.843 134.868 1.00 22.69  ? 4168 ARG A NH1   1 
ATOM   19320 N  NH2   . ARG A 1 4168 ? 154.752 146.092 132.986 1.00 21.47  ? 4168 ARG A NH2   1 
ATOM   19321 N  N     . ILE A 1 4169 ? 156.097 138.189 131.088 1.00 29.69  ? 4169 ILE A N     1 
ATOM   19322 C  CA    . ILE A 1 4169 ? 157.323 137.980 130.325 1.00 27.01  ? 4169 ILE A CA    1 
ATOM   19323 C  C     . ILE A 1 4169 ? 157.041 137.179 129.060 1.00 29.67  ? 4169 ILE A C     1 
ATOM   19324 O  O     . ILE A 1 4169 ? 157.582 137.475 127.989 1.00 32.08  ? 4169 ILE A O     1 
ATOM   19325 C  CB    . ILE A 1 4169 ? 158.387 137.299 131.205 1.00 24.77  ? 4169 ILE A CB    1 
ATOM   19326 C  CG1   . ILE A 1 4169 ? 158.499 138.018 132.550 1.00 20.12  ? 4169 ILE A CG1   1 
ATOM   19327 C  CG2   . ILE A 1 4169 ? 159.729 137.280 130.497 1.00 22.84  ? 4169 ILE A CG2   1 
ATOM   19328 C  CD1   . ILE A 1 4169 ? 159.610 137.498 133.429 1.00 22.60  ? 4169 ILE A CD1   1 
ATOM   19329 N  N     . CYS A 1 4170 ? 156.196 136.157 129.160 1.00 30.61  ? 4170 CYS A N     1 
ATOM   19330 C  CA    . CYS A 1 4170 ? 155.839 135.324 128.014 1.00 35.71  ? 4170 CYS A CA    1 
ATOM   19331 C  C     . CYS A 1 4170 ? 154.631 135.948 127.329 1.00 40.48  ? 4170 CYS A C     1 
ATOM   19332 O  O     . CYS A 1 4170 ? 153.487 135.723 127.731 1.00 47.81  ? 4170 CYS A O     1 
ATOM   19333 C  CB    . CYS A 1 4170 ? 155.559 133.893 128.455 1.00 44.96  ? 4170 CYS A CB    1 
ATOM   19334 S  SG    . CYS A 1 4170 ? 156.778 133.218 129.607 1.00 62.40  ? 4170 CYS A SG    1 
ATOM   19335 N  N     . LYS A 1 4171 ? 154.884 136.731 126.284 1.00 44.62  ? 4171 LYS A N     1 
ATOM   19336 C  CA    . LYS A 1 4171 ? 153.832 137.419 125.548 1.00 39.49  ? 4171 LYS A CA    1 
ATOM   19337 C  C     . LYS A 1 4171 ? 154.114 137.262 124.058 1.00 50.82  ? 4171 LYS A C     1 
ATOM   19338 O  O     . LYS A 1 4171 ? 154.926 136.428 123.645 1.00 61.72  ? 4171 LYS A O     1 
ATOM   19339 C  CB    . LYS A 1 4171 ? 153.726 138.887 125.976 1.00 36.55  ? 4171 LYS A CB    1 
ATOM   19340 C  CG    . LYS A 1 4171 ? 152.603 139.153 126.965 1.00 33.99  ? 4171 LYS A CG    1 
ATOM   19341 C  CD    . LYS A 1 4171 ? 152.257 140.628 127.035 1.00 40.58  ? 4171 LYS A CD    1 
ATOM   19342 C  CE    . LYS A 1 4171 ? 151.499 141.075 125.798 1.00 44.44  ? 4171 LYS A CE    1 
ATOM   19343 N  NZ    . LYS A 1 4171 ? 150.789 142.365 126.022 1.00 40.52  ? 4171 LYS A NZ    1 
ATOM   19344 N  N     . SER A 1 4172 ? 153.424 138.065 123.248 1.00 51.15  ? 4172 SER A N     1 
ATOM   19345 C  CA    . SER A 1 4172 ? 153.454 137.898 121.795 1.00 52.54  ? 4172 SER A CA    1 
ATOM   19346 C  C     . SER A 1 4172 ? 154.859 137.899 121.200 1.00 49.32  ? 4172 SER A C     1 
ATOM   19347 O  O     . SER A 1 4172 ? 155.162 136.993 120.407 1.00 59.15  ? 4172 SER A O     1 
ATOM   19348 C  CB    . SER A 1 4172 ? 152.575 138.978 121.147 1.00 58.95  ? 4172 SER A CB    1 
ATOM   19349 O  OG    . SER A 1 4172 ? 151.247 138.917 121.637 1.00 54.90  ? 4172 SER A OG    1 
ATOM   19350 N  N     . PRO A 1 4173 ? 155.760 138.846 121.522 1.00 44.57  ? 4173 PRO A N     1 
ATOM   19351 C  CA    . PRO A 1 4173 ? 157.118 138.750 120.971 1.00 44.00  ? 4173 PRO A CA    1 
ATOM   19352 C  C     . PRO A 1 4173 ? 158.035 137.897 121.835 1.00 45.98  ? 4173 PRO A C     1 
ATOM   19353 O  O     . PRO A 1 4173 ? 158.102 138.084 123.054 1.00 47.42  ? 4173 PRO A O     1 
ATOM   19354 C  CB    . PRO A 1 4173 ? 157.580 140.211 120.925 1.00 34.50  ? 4173 PRO A CB    1 
ATOM   19355 C  CG    . PRO A 1 4173 ? 156.842 140.868 122.035 1.00 39.37  ? 4173 PRO A CG    1 
ATOM   19356 C  CD    . PRO A 1 4173 ? 155.574 140.091 122.291 1.00 42.68  ? 4173 PRO A CD    1 
ATOM   19357 N  N     . ASN A 1 4174 ? 158.740 136.949 121.213 1.00 41.03  ? 4174 ASN A N     1 
ATOM   19358 C  CA    . ASN A 1 4174 ? 159.664 136.100 121.957 1.00 41.25  ? 4174 ASN A CA    1 
ATOM   19359 C  C     . ASN A 1 4174 ? 160.857 136.877 122.496 1.00 37.37  ? 4174 ASN A C     1 
ATOM   19360 O  O     . ASN A 1 4174 ? 161.508 136.414 123.439 1.00 36.50  ? 4174 ASN A O     1 
ATOM   19361 C  CB    . ASN A 1 4174 ? 160.155 134.950 121.076 1.00 37.37  ? 4174 ASN A CB    1 
ATOM   19362 C  CG    . ASN A 1 4174 ? 159.050 133.978 120.715 1.00 47.05  ? 4174 ASN A CG    1 
ATOM   19363 O  OD1   . ASN A 1 4174 ? 157.926 134.086 121.204 1.00 46.49  ? 4174 ASN A OD1   1 
ATOM   19364 N  ND2   . ASN A 1 4174 ? 159.367 133.017 119.855 1.00 47.43  ? 4174 ASN A ND2   1 
ATOM   19365 N  N     . GLU A 1 4175 ? 161.155 138.043 121.921 1.00 34.33  ? 4175 GLU A N     1 
ATOM   19366 C  CA    . GLU A 1 4175 ? 162.292 138.840 122.363 1.00 26.82  ? 4175 GLU A CA    1 
ATOM   19367 C  C     . GLU A 1 4175 ? 162.022 139.536 123.691 1.00 24.13  ? 4175 GLU A C     1 
ATOM   19368 O  O     . GLU A 1 4175 ? 162.964 140.021 124.333 1.00 23.16  ? 4175 GLU A O     1 
ATOM   19369 C  CB    . GLU A 1 4175 ? 162.639 139.867 121.284 1.00 29.82  ? 4175 GLU A CB    1 
ATOM   19370 C  CG    . GLU A 1 4175 ? 163.323 139.275 120.057 1.00 32.18  ? 4175 GLU A CG    1 
ATOM   19371 C  CD    . GLU A 1 4175 ? 162.377 138.490 119.163 1.00 42.74  ? 4175 GLU A CD    1 
ATOM   19372 O  OE1   . GLU A 1 4175 ? 161.149 138.563 119.374 1.00 46.31  ? 4175 GLU A OE1   1 
ATOM   19373 O  OE2   . GLU A 1 4175 ? 162.864 137.792 118.250 1.00 46.62  ? 4175 GLU A OE2   1 
ATOM   19374 N  N     . ARG A 1 4176 ? 160.757 139.586 124.113 1.00 23.21  ? 4176 ARG A N     1 
ATOM   19375 C  CA    . ARG A 1 4176 ? 160.398 140.241 125.365 1.00 17.73  ? 4176 ARG A CA    1 
ATOM   19376 C  C     . ARG A 1 4176 ? 161.075 139.567 126.551 1.00 17.87  ? 4176 ARG A C     1 
ATOM   19377 O  O     . ARG A 1 4176 ? 161.466 140.229 127.517 1.00 18.86  ? 4176 ARG A O     1 
ATOM   19378 C  CB    . ARG A 1 4176 ? 158.877 140.235 125.530 1.00 23.40  ? 4176 ARG A CB    1 
ATOM   19379 C  CG    . ARG A 1 4176 ? 158.381 140.780 126.855 1.00 26.27  ? 4176 ARG A CG    1 
ATOM   19380 C  CD    . ARG A 1 4176 ? 156.868 140.692 126.948 1.00 26.09  ? 4176 ARG A CD    1 
ATOM   19381 N  NE    . ARG A 1 4176 ? 156.213 141.149 125.729 1.00 33.05  ? 4176 ARG A NE    1 
ATOM   19382 C  CZ    . ARG A 1 4176 ? 155.417 142.207 125.658 1.00 33.73  ? 4176 ARG A CZ    1 
ATOM   19383 N  NH1   . ARG A 1 4176 ? 155.159 142.950 126.722 1.00 31.49  ? 4176 ARG A NH1   1 
ATOM   19384 N  NH2   . ARG A 1 4176 ? 154.864 142.527 124.492 1.00 33.45  ? 4176 ARG A NH2   1 
ATOM   19385 N  N     . ALA A 1 4177 ? 161.224 138.242 126.491 1.00 24.73  ? 4177 ALA A N     1 
ATOM   19386 C  CA    . ALA A 1 4177 ? 161.882 137.520 127.575 1.00 18.66  ? 4177 ALA A CA    1 
ATOM   19387 C  C     . ALA A 1 4177 ? 163.336 137.949 127.721 1.00 15.39  ? 4177 ALA A C     1 
ATOM   19388 O  O     . ALA A 1 4177 ? 163.825 138.169 128.835 1.00 16.93  ? 4177 ALA A O     1 
ATOM   19389 C  CB    . ALA A 1 4177 ? 161.783 136.014 127.333 1.00 19.77  ? 4177 ALA A CB    1 
ATOM   19390 N  N     . ARG A 1 4178 ? 164.045 138.084 126.599 1.00 14.53  ? 4178 ARG A N     1 
ATOM   19391 C  CA    . ARG A 1 4178 ? 165.442 138.499 126.663 1.00 11.24  ? 4178 ARG A CA    1 
ATOM   19392 C  C     . ARG A 1 4178 ? 165.556 139.955 127.096 1.00 11.84  ? 4178 ARG A C     1 
ATOM   19393 O  O     . ARG A 1 4178 ? 166.493 140.330 127.810 1.00 13.51  ? 4178 ARG A O     1 
ATOM   19394 C  CB    . ARG A 1 4178 ? 166.124 138.276 125.315 1.00 11.84  ? 4178 ARG A CB    1 
ATOM   19395 C  CG    . ARG A 1 4178 ? 167.639 138.210 125.406 1.00 10.33  ? 4178 ARG A CG    1 
ATOM   19396 C  CD    . ARG A 1 4178 ? 168.270 138.112 124.034 1.00 16.00  ? 4178 ARG A CD    1 
ATOM   19397 N  NE    . ARG A 1 4178 ? 169.544 137.407 124.050 1.00 23.60  ? 4178 ARG A NE    1 
ATOM   19398 C  CZ    . ARG A 1 4178 ? 169.670 136.087 124.062 1.00 27.38  ? 4178 ARG A CZ    1 
ATOM   19399 N  NH1   . ARG A 1 4178 ? 168.614 135.291 124.050 1.00 23.85  ? 4178 ARG A NH1   1 
ATOM   19400 N  NH2   . ARG A 1 4178 ? 170.887 135.552 124.080 1.00 33.32  ? 4178 ARG A NH2   1 
ATOM   19401 N  N     . LEU A 1 4179 ? 164.606 140.793 126.674 1.00 15.14  ? 4179 LEU A N     1 
ATOM   19402 C  CA    . LEU A 1 4179 ? 164.597 142.177 127.141 1.00 10.16  ? 4179 LEU A CA    1 
ATOM   19403 C  C     . LEU A 1 4179 ? 164.406 142.244 128.651 1.00 9.86   ? 4179 LEU A C     1 
ATOM   19404 O  O     . LEU A 1 4179 ? 165.073 143.020 129.343 1.00 12.62  ? 4179 LEU A O     1 
ATOM   19405 C  CB    . LEU A 1 4179 ? 163.507 142.974 126.423 1.00 10.92  ? 4179 LEU A CB    1 
ATOM   19406 C  CG    . LEU A 1 4179 ? 163.699 143.188 124.923 1.00 12.30  ? 4179 LEU A CG    1 
ATOM   19407 C  CD1   . LEU A 1 4179 ? 162.781 144.285 124.416 1.00 13.91  ? 4179 LEU A CD1   1 
ATOM   19408 C  CD2   . LEU A 1 4179 ? 165.145 143.521 124.622 1.00 9.87   ? 4179 LEU A CD2   1 
ATOM   19409 N  N     . TYR A 1 4180 ? 163.496 141.426 129.181 1.00 12.99  ? 4180 TYR A N     1 
ATOM   19410 C  CA    . TYR A 1 4180 ? 163.286 141.389 130.625 1.00 10.73  ? 4180 TYR A CA    1 
ATOM   19411 C  C     . TYR A 1 4180 ? 164.512 140.853 131.353 1.00 9.42   ? 4180 TYR A C     1 
ATOM   19412 O  O     . TYR A 1 4180 ? 164.840 141.316 132.450 1.00 8.03   ? 4180 TYR A O     1 
ATOM   19413 C  CB    . TYR A 1 4180 ? 162.052 140.553 130.958 1.00 10.63  ? 4180 TYR A CB    1 
ATOM   19414 C  CG    . TYR A 1 4180 ? 160.777 141.358 131.012 1.00 13.90  ? 4180 TYR A CG    1 
ATOM   19415 C  CD1   . TYR A 1 4180 ? 160.217 141.891 129.860 1.00 15.09  ? 4180 TYR A CD1   1 
ATOM   19416 C  CD2   . TYR A 1 4180 ? 160.134 141.588 132.219 1.00 19.33  ? 4180 TYR A CD2   1 
ATOM   19417 C  CE1   . TYR A 1 4180 ? 159.053 142.630 129.909 1.00 18.01  ? 4180 TYR A CE1   1 
ATOM   19418 C  CE2   . TYR A 1 4180 ? 158.971 142.323 132.278 1.00 19.46  ? 4180 TYR A CE2   1 
ATOM   19419 C  CZ    . TYR A 1 4180 ? 158.434 142.842 131.121 1.00 22.31  ? 4180 TYR A CZ    1 
ATOM   19420 O  OH    . TYR A 1 4180 ? 157.274 143.574 131.181 1.00 27.60  ? 4180 TYR A OH    1 
ATOM   19421 N  N     . PHE A 1 4181 ? 165.194 139.866 130.770 1.00 10.57  ? 4181 PHE A N     1 
ATOM   19422 C  CA    . PHE A 1 4181 ? 166.420 139.363 131.382 1.00 8.31   ? 4181 PHE A CA    1 
ATOM   19423 C  C     . PHE A 1 4181 ? 167.493 140.445 131.428 1.00 8.78   ? 4181 PHE A C     1 
ATOM   19424 O  O     . PHE A 1 4181 ? 168.203 140.595 132.430 1.00 8.39   ? 4181 PHE A O     1 
ATOM   19425 C  CB    . PHE A 1 4181 ? 166.929 138.137 130.625 1.00 9.90   ? 4181 PHE A CB    1 
ATOM   19426 C  CG    . PHE A 1 4181 ? 168.279 137.670 131.081 1.00 10.65  ? 4181 PHE A CG    1 
ATOM   19427 C  CD1   . PHE A 1 4181 ? 168.402 136.827 132.169 1.00 9.62   ? 4181 PHE A CD1   1 
ATOM   19428 C  CD2   . PHE A 1 4181 ? 169.427 138.085 130.430 1.00 13.02  ? 4181 PHE A CD2   1 
ATOM   19429 C  CE1   . PHE A 1 4181 ? 169.642 136.403 132.593 1.00 11.80  ? 4181 PHE A CE1   1 
ATOM   19430 C  CE2   . PHE A 1 4181 ? 170.668 137.666 130.852 1.00 11.75  ? 4181 PHE A CE2   1 
ATOM   19431 C  CZ    . PHE A 1 4181 ? 170.775 136.825 131.934 1.00 13.05  ? 4181 PHE A CZ    1 
ATOM   19432 N  N     . LEU A 1 4182 ? 167.637 141.199 130.336 1.00 11.94  ? 4182 LEU A N     1 
ATOM   19433 C  CA    . LEU A 1 4182 ? 168.581 142.311 130.317 1.00 7.94   ? 4182 LEU A CA    1 
ATOM   19434 C  C     . LEU A 1 4182 ? 168.210 143.354 131.362 1.00 5.61   ? 4182 LEU A C     1 
ATOM   19435 O  O     . LEU A 1 4182 ? 169.079 143.909 132.042 1.00 6.66   ? 4182 LEU A O     1 
ATOM   19436 C  CB    . LEU A 1 4182 ? 168.624 142.939 128.924 1.00 6.62   ? 4182 LEU A CB    1 
ATOM   19437 C  CG    . LEU A 1 4182 ? 169.403 142.189 127.845 1.00 7.93   ? 4182 LEU A CG    1 
ATOM   19438 C  CD1   . LEU A 1 4182 ? 169.115 142.789 126.482 1.00 13.15  ? 4182 LEU A CD1   1 
ATOM   19439 C  CD2   . LEU A 1 4182 ? 170.891 142.224 128.143 1.00 10.68  ? 4182 LEU A CD2   1 
ATOM   19440 N  N     . LEU A 1 4183 ? 166.913 143.631 131.497 1.00 5.51   ? 4183 LEU A N     1 
ATOM   19441 C  CA    . LEU A 1 4183 ? 166.443 144.569 132.510 1.00 4.93   ? 4183 LEU A CA    1 
ATOM   19442 C  C     . LEU A 1 4183 ? 166.801 144.089 133.911 1.00 5.70   ? 4183 LEU A C     1 
ATOM   19443 O  O     . LEU A 1 4183 ? 167.252 144.873 134.753 1.00 6.03   ? 4183 LEU A O     1 
ATOM   19444 C  CB    . LEU A 1 4183 ? 164.932 144.747 132.371 1.00 6.70   ? 4183 LEU A CB    1 
ATOM   19445 C  CG    . LEU A 1 4183 ? 164.302 146.007 132.951 1.00 8.22   ? 4183 LEU A CG    1 
ATOM   19446 C  CD1   . LEU A 1 4183 ? 165.153 147.202 132.603 1.00 8.06   ? 4183 LEU A CD1   1 
ATOM   19447 C  CD2   . LEU A 1 4183 ? 162.898 146.173 132.412 1.00 7.19   ? 4183 LEU A CD2   1 
ATOM   19448 N  N     . ALA A 1 4184 ? 166.598 142.797 134.177 1.00 6.05   ? 4184 ALA A N     1 
ATOM   19449 C  CA    . ALA A 1 4184 ? 166.917 142.242 135.488 1.00 4.66   ? 4184 ALA A CA    1 
ATOM   19450 C  C     . ALA A 1 4184 ? 168.410 142.310 135.772 1.00 4.68   ? 4184 ALA A C     1 
ATOM   19451 O  O     . ALA A 1 4184 ? 168.822 142.664 136.882 1.00 5.46   ? 4184 ALA A O     1 
ATOM   19452 C  CB    . ALA A 1 4184 ? 166.420 140.800 135.582 1.00 6.42   ? 4184 ALA A CB    1 
ATOM   19453 N  N     . TRP A 1 4185 ? 169.238 141.972 134.781 1.00 4.36   ? 4185 TRP A N     1 
ATOM   19454 C  CA    . TRP A 1 4185 ? 170.684 142.063 134.961 1.00 3.23   ? 4185 TRP A CA    1 
ATOM   19455 C  C     . TRP A 1 4185 ? 171.110 143.499 135.234 1.00 4.15   ? 4185 TRP A C     1 
ATOM   19456 O  O     . TRP A 1 4185 ? 171.927 143.757 136.126 1.00 5.92   ? 4185 TRP A O     1 
ATOM   19457 C  CB    . TRP A 1 4185 ? 171.407 141.517 133.730 1.00 4.45   ? 4185 TRP A CB    1 
ATOM   19458 C  CG    . TRP A 1 4185 ? 172.897 141.660 133.810 1.00 4.78   ? 4185 TRP A CG    1 
ATOM   19459 C  CD1   . TRP A 1 4185 ? 173.655 142.643 133.248 1.00 3.32   ? 4185 TRP A CD1   1 
ATOM   19460 C  CD2   . TRP A 1 4185 ? 173.810 140.790 134.488 1.00 5.38   ? 4185 TRP A CD2   1 
ATOM   19461 N  NE1   . TRP A 1 4185 ? 174.981 142.443 133.536 1.00 4.09   ? 4185 TRP A NE1   1 
ATOM   19462 C  CE2   . TRP A 1 4185 ? 175.103 141.311 134.296 1.00 5.34   ? 4185 TRP A CE2   1 
ATOM   19463 C  CE3   . TRP A 1 4185 ? 173.659 139.621 135.239 1.00 4.29   ? 4185 TRP A CE3   1 
ATOM   19464 C  CZ2   . TRP A 1 4185 ? 176.238 140.704 134.827 1.00 5.69   ? 4185 TRP A CZ2   1 
ATOM   19465 C  CZ3   . TRP A 1 4185 ? 174.786 139.022 135.765 1.00 4.79   ? 4185 TRP A CZ3   1 
ATOM   19466 C  CH2   . TRP A 1 4185 ? 176.058 139.564 135.558 1.00 5.90   ? 4185 TRP A CH2   1 
ATOM   19467 N  N     . PHE A 1 4186 ? 170.560 144.446 134.473 1.00 4.05   ? 4186 PHE A N     1 
ATOM   19468 C  CA    . PHE A 1 4186 ? 170.886 145.854 134.661 1.00 3.35   ? 4186 PHE A CA    1 
ATOM   19469 C  C     . PHE A 1 4186 ? 170.517 146.302 136.072 1.00 3.80   ? 4186 PHE A C     1 
ATOM   19470 O  O     . PHE A 1 4186 ? 171.340 146.880 136.796 1.00 4.70   ? 4186 PHE A O     1 
ATOM   19471 C  CB    . PHE A 1 4186 ? 170.134 146.675 133.610 1.00 4.69   ? 4186 PHE A CB    1 
ATOM   19472 C  CG    . PHE A 1 4186 ? 170.362 148.157 133.690 1.00 5.85   ? 4186 PHE A CG    1 
ATOM   19473 C  CD1   . PHE A 1 4186 ? 171.520 148.719 133.182 1.00 6.59   ? 4186 PHE A CD1   1 
ATOM   19474 C  CD2   . PHE A 1 4186 ? 169.422 148.987 134.276 1.00 4.08   ? 4186 PHE A CD2   1 
ATOM   19475 C  CE1   . PHE A 1 4186 ? 171.728 150.084 133.239 1.00 7.88   ? 4186 PHE A CE1   1 
ATOM   19476 C  CE2   . PHE A 1 4186 ? 169.631 150.349 134.349 1.00 3.65   ? 4186 PHE A CE2   1 
ATOM   19477 C  CZ    . PHE A 1 4186 ? 170.784 150.898 133.831 1.00 6.42   ? 4186 PHE A CZ    1 
ATOM   19478 N  N     . HIS A 1 4187 ? 169.282 146.010 136.485 1.00 4.42   ? 4187 HIS A N     1 
ATOM   19479 C  CA    . HIS A 1 4187 ? 168.819 146.397 137.810 1.00 3.30   ? 4187 HIS A CA    1 
ATOM   19480 C  C     . HIS A 1 4187 ? 169.687 145.786 138.899 1.00 4.33   ? 4187 HIS A C     1 
ATOM   19481 O  O     . HIS A 1 4187 ? 170.046 146.473 139.862 1.00 5.71   ? 4187 HIS A O     1 
ATOM   19482 C  CB    . HIS A 1 4187 ? 167.359 145.976 137.984 1.00 4.19   ? 4187 HIS A CB    1 
ATOM   19483 C  CG    . HIS A 1 4187 ? 166.741 146.439 139.265 1.00 5.08   ? 4187 HIS A CG    1 
ATOM   19484 N  ND1   . HIS A 1 4187 ? 166.481 147.766 139.526 1.00 6.27   ? 4187 HIS A ND1   1 
ATOM   19485 C  CD2   . HIS A 1 4187 ? 166.325 145.752 140.354 1.00 5.39   ? 4187 HIS A CD2   1 
ATOM   19486 C  CE1   . HIS A 1 4187 ? 165.934 147.878 140.723 1.00 6.72   ? 4187 HIS A CE1   1 
ATOM   19487 N  NE2   . HIS A 1 4187 ? 165.828 146.670 141.246 1.00 6.89   ? 4187 HIS A NE2   1 
ATOM   19488 N  N     . ALA A 1 4188 ? 170.051 144.510 138.754 1.00 4.55   ? 4188 ALA A N     1 
ATOM   19489 C  CA    . ALA A 1 4188 ? 170.903 143.862 139.743 1.00 4.36   ? 4188 ALA A CA    1 
ATOM   19490 C  C     . ALA A 1 4188 ? 172.270 144.528 139.818 1.00 4.76   ? 4188 ALA A C     1 
ATOM   19491 O  O     . ALA A 1 4188 ? 172.794 144.760 140.912 1.00 8.28   ? 4188 ALA A O     1 
ATOM   19492 C  CB    . ALA A 1 4188 ? 171.043 142.375 139.419 1.00 4.58   ? 4188 ALA A CB    1 
ATOM   19493 N  N     . ILE A 1 4189 ? 172.862 144.853 138.665 1.00 4.30   ? 4189 ILE A N     1 
ATOM   19494 C  CA    . ILE A 1 4189 ? 174.195 145.455 138.666 1.00 3.63   ? 4189 ILE A CA    1 
ATOM   19495 C  C     . ILE A 1 4189 ? 174.181 146.806 139.367 1.00 4.27   ? 4189 ILE A C     1 
ATOM   19496 O  O     . ILE A 1 4189 ? 175.017 147.077 140.241 1.00 5.47   ? 4189 ILE A O     1 
ATOM   19497 C  CB    . ILE A 1 4189 ? 174.740 145.572 137.229 1.00 4.58   ? 4189 ILE A CB    1 
ATOM   19498 C  CG1   . ILE A 1 4189 ? 174.914 144.188 136.599 1.00 4.47   ? 4189 ILE A CG1   1 
ATOM   19499 C  CG2   . ILE A 1 4189 ? 176.052 146.338 137.215 1.00 5.25   ? 4189 ILE A CG2   1 
ATOM   19500 C  CD1   . ILE A 1 4189 ? 175.699 143.219 137.446 1.00 3.89   ? 4189 ILE A CD1   1 
ATOM   19501 N  N     . ILE A 1 4190 ? 173.238 147.677 139.002 1.00 4.25   ? 4190 ILE A N     1 
ATOM   19502 C  CA    . ILE A 1 4190 ? 173.206 149.002 139.626 1.00 4.52   ? 4190 ILE A CA    1 
ATOM   19503 C  C     . ILE A 1 4190 ? 172.808 148.932 141.098 1.00 4.25   ? 4190 ILE A C     1 
ATOM   19504 O  O     . ILE A 1 4190 ? 173.337 149.687 141.922 1.00 5.00   ? 4190 ILE A O     1 
ATOM   19505 C  CB    . ILE A 1 4190 ? 172.338 149.987 138.816 1.00 3.86   ? 4190 ILE A CB    1 
ATOM   19506 C  CG1   . ILE A 1 4190 ? 172.984 150.270 137.456 1.00 6.97   ? 4190 ILE A CG1   1 
ATOM   19507 C  CG2   . ILE A 1 4190 ? 172.119 151.267 139.570 1.00 9.06   ? 4190 ILE A CG2   1 
ATOM   19508 C  CD1   . ILE A 1 4190 ? 172.639 149.385 136.365 1.00 7.65   ? 4190 ILE A CD1   1 
ATOM   19509 N  N     . GLN A 1 4191 ? 171.899 148.033 141.468 1.00 5.06   ? 4191 GLN A N     1 
ATOM   19510 C  CA    . GLN A 1 4191 ? 171.581 147.916 142.886 1.00 4.16   ? 4191 GLN A CA    1 
ATOM   19511 C  C     . GLN A 1 4191 ? 172.734 147.348 143.700 1.00 4.40   ? 4191 GLN A C     1 
ATOM   19512 O  O     . GLN A 1 4191 ? 172.916 147.743 144.858 1.00 4.20   ? 4191 GLN A O     1 
ATOM   19513 C  CB    . GLN A 1 4191 ? 170.331 147.057 143.090 1.00 3.50   ? 4191 GLN A CB    1 
ATOM   19514 C  CG    . GLN A 1 4191 ? 169.038 147.843 142.998 1.00 4.82   ? 4191 GLN A CG    1 
ATOM   19515 C  CD    . GLN A 1 4191 ? 167.917 147.222 143.803 1.00 9.29   ? 4191 GLN A CD    1 
ATOM   19516 O  OE1   . GLN A 1 4191 ? 167.768 146.004 143.845 1.00 15.17  ? 4191 GLN A OE1   1 
ATOM   19517 N  NE2   . GLN A 1 4191 ? 167.120 148.064 144.450 1.00 11.26  ? 4191 GLN A NE2   1 
ATOM   19518 N  N     . GLU A 1 4192 ? 173.523 146.441 143.125 1.00 4.51   ? 4192 GLU A N     1 
ATOM   19519 C  CA    . GLU A 1 4192 ? 174.661 145.872 143.831 1.00 5.75   ? 4192 GLU A CA    1 
ATOM   19520 C  C     . GLU A 1 4192 ? 175.845 146.825 143.901 1.00 7.30   ? 4192 GLU A C     1 
ATOM   19521 O  O     . GLU A 1 4192 ? 176.648 146.723 144.834 1.00 9.56   ? 4192 GLU A O     1 
ATOM   19522 C  CB    . GLU A 1 4192 ? 175.082 144.562 143.165 1.00 6.15   ? 4192 GLU A CB    1 
ATOM   19523 C  CG    . GLU A 1 4192 ? 175.739 143.568 144.103 1.00 14.66  ? 4192 GLU A CG    1 
ATOM   19524 C  CD    . GLU A 1 4192 ? 174.778 143.023 145.138 1.00 24.18  ? 4192 GLU A CD    1 
ATOM   19525 O  OE1   . GLU A 1 4192 ? 175.242 142.609 146.221 1.00 22.99  ? 4192 GLU A OE1   1 
ATOM   19526 O  OE2   . GLU A 1 4192 ? 173.559 143.006 144.868 1.00 25.72  ? 4192 GLU A OE2   1 
ATOM   19527 N  N     . ARG A 1 4193 ? 175.981 147.739 142.937 1.00 7.00   ? 4193 ARG A N     1 
ATOM   19528 C  CA    . ARG A 1 4193 ? 177.029 148.749 143.029 1.00 6.12   ? 4193 ARG A CA    1 
ATOM   19529 C  C     . ARG A 1 4193 ? 176.777 149.760 144.140 1.00 6.93   ? 4193 ARG A C     1 
ATOM   19530 O  O     . ARG A 1 4193 ? 177.710 150.465 144.537 1.00 8.86   ? 4193 ARG A O     1 
ATOM   19531 C  CB    . ARG A 1 4193 ? 177.188 149.489 141.700 1.00 6.20   ? 4193 ARG A CB    1 
ATOM   19532 C  CG    . ARG A 1 4193 ? 177.871 148.680 140.617 1.00 7.36   ? 4193 ARG A CG    1 
ATOM   19533 C  CD    . ARG A 1 4193 ? 177.989 149.479 139.333 1.00 7.11   ? 4193 ARG A CD    1 
ATOM   19534 N  NE    . ARG A 1 4193 ? 178.957 150.561 139.459 1.00 6.31   ? 4193 ARG A NE    1 
ATOM   19535 C  CZ    . ARG A 1 4193 ? 180.150 150.571 138.882 1.00 5.79   ? 4193 ARG A CZ    1 
ATOM   19536 N  NH1   . ARG A 1 4193 ? 180.555 149.573 138.117 1.00 5.00   ? 4193 ARG A NH1   1 
ATOM   19537 N  NH2   . ARG A 1 4193 ? 180.958 151.608 139.081 1.00 8.12   ? 4193 ARG A NH2   1 
ATOM   19538 N  N     . LEU A 1 4194 ? 175.545 149.849 144.646 1.00 6.97   ? 4194 LEU A N     1 
ATOM   19539 C  CA    . LEU A 1 4194 ? 175.248 150.772 145.735 1.00 6.45   ? 4194 LEU A CA    1 
ATOM   19540 C  C     . LEU A 1 4194 ? 175.972 150.404 147.024 1.00 8.13   ? 4194 LEU A C     1 
ATOM   19541 O  O     . LEU A 1 4194 ? 176.175 151.277 147.873 1.00 8.90   ? 4194 LEU A O     1 
ATOM   19542 C  CB    . LEU A 1 4194 ? 173.741 150.823 145.985 1.00 5.52   ? 4194 LEU A CB    1 
ATOM   19543 C  CG    . LEU A 1 4194 ? 172.899 151.559 144.942 1.00 6.43   ? 4194 LEU A CG    1 
ATOM   19544 C  CD1   . LEU A 1 4194 ? 171.427 151.231 145.113 1.00 7.10   ? 4194 LEU A CD1   1 
ATOM   19545 C  CD2   . LEU A 1 4194 ? 173.127 153.056 145.036 1.00 9.66   ? 4194 LEU A CD2   1 
ATOM   19546 N  N     . ARG A 1 4195 ? 176.356 149.136 147.190 1.00 8.61   ? 4195 ARG A N     1 
ATOM   19547 C  CA    . ARG A 1 4195 ? 177.086 148.733 148.387 1.00 8.98   ? 4195 ARG A CA    1 
ATOM   19548 C  C     . ARG A 1 4195 ? 178.441 149.421 148.464 1.00 9.61   ? 4195 ARG A C     1 
ATOM   19549 O  O     . ARG A 1 4195 ? 178.887 149.816 149.548 1.00 10.90  ? 4195 ARG A O     1 
ATOM   19550 C  CB    . ARG A 1 4195 ? 177.252 147.215 148.412 1.00 7.97   ? 4195 ARG A CB    1 
ATOM   19551 C  CG    . ARG A 1 4195 ? 175.973 146.453 148.125 1.00 12.41  ? 4195 ARG A CG    1 
ATOM   19552 C  CD    . ARG A 1 4195 ? 176.162 144.960 148.328 1.00 20.27  ? 4195 ARG A CD    1 
ATOM   19553 N  NE    . ARG A 1 4195 ? 174.895 144.239 148.305 1.00 25.54  ? 4195 ARG A NE    1 
ATOM   19554 C  CZ    . ARG A 1 4195 ? 174.026 144.215 149.306 1.00 21.91  ? 4195 ARG A CZ    1 
ATOM   19555 N  NH1   . ARG A 1 4195 ? 174.257 144.857 150.439 1.00 18.38  ? 4195 ARG A NH1   1 
ATOM   19556 N  NH2   . ARG A 1 4195 ? 172.896 143.528 149.167 1.00 15.52  ? 4195 ARG A NH2   1 
ATOM   19557 N  N     . TYR A 1 4196 ? 179.114 149.567 147.325 1.00 8.85   ? 4196 TYR A N     1 
ATOM   19558 C  CA    . TYR A 1 4196 ? 180.404 150.252 147.261 1.00 10.54  ? 4196 TYR A CA    1 
ATOM   19559 C  C     . TYR A 1 4196 ? 180.151 151.724 146.937 1.00 13.86  ? 4196 TYR A C     1 
ATOM   19560 O  O     . TYR A 1 4196 ? 180.425 152.221 145.845 1.00 15.11  ? 4196 TYR A O     1 
ATOM   19561 C  CB    . TYR A 1 4196 ? 181.305 149.577 146.236 1.00 8.17   ? 4196 TYR A CB    1 
ATOM   19562 C  CG    . TYR A 1 4196 ? 181.220 148.069 146.293 1.00 10.63  ? 4196 TYR A CG    1 
ATOM   19563 C  CD1   . TYR A 1 4196 ? 180.325 147.376 145.490 1.00 10.48  ? 4196 TYR A CD1   1 
ATOM   19564 C  CD2   . TYR A 1 4196 ? 182.010 147.339 147.170 1.00 12.36  ? 4196 TYR A CD2   1 
ATOM   19565 C  CE1   . TYR A 1 4196 ? 180.230 146.002 145.545 1.00 11.20  ? 4196 TYR A CE1   1 
ATOM   19566 C  CE2   . TYR A 1 4196 ? 181.922 145.962 147.231 1.00 11.75  ? 4196 TYR A CE2   1 
ATOM   19567 C  CZ    . TYR A 1 4196 ? 181.030 145.299 146.416 1.00 12.44  ? 4196 TYR A CZ    1 
ATOM   19568 O  OH    . TYR A 1 4196 ? 180.934 143.930 146.467 1.00 14.02  ? 4196 TYR A OH    1 
ATOM   19569 N  N     . ALA A 1 4197 ? 179.607 152.418 147.938 1.00 14.74  ? 4197 ALA A N     1 
ATOM   19570 C  CA    . ALA A 1 4197 ? 179.017 153.737 147.714 1.00 12.79  ? 4197 ALA A CA    1 
ATOM   19571 C  C     . ALA A 1 4197 ? 179.990 154.760 147.143 1.00 22.19  ? 4197 ALA A C     1 
ATOM   19572 O  O     . ALA A 1 4197 ? 179.618 155.451 146.180 1.00 29.49  ? 4197 ALA A O     1 
ATOM   19573 C  CB    . ALA A 1 4197 ? 178.383 154.238 149.016 1.00 22.78  ? 4197 ALA A CB    1 
ATOM   19574 N  N     . PRO A 1 4198 ? 181.205 154.941 147.674 1.00 22.30  ? 4198 PRO A N     1 
ATOM   19575 C  CA    . PRO A 1 4198 ? 182.102 155.942 147.070 1.00 14.61  ? 4198 PRO A CA    1 
ATOM   19576 C  C     . PRO A 1 4198 ? 182.492 155.635 145.633 1.00 12.11  ? 4198 PRO A C     1 
ATOM   19577 O  O     . PRO A 1 4198 ? 182.664 156.568 144.841 1.00 17.19  ? 4198 PRO A O     1 
ATOM   19578 C  CB    . PRO A 1 4198 ? 183.323 155.928 147.999 1.00 18.38  ? 4198 PRO A CB    1 
ATOM   19579 C  CG    . PRO A 1 4198 ? 182.830 155.356 149.277 1.00 20.92  ? 4198 PRO A CG    1 
ATOM   19580 C  CD    . PRO A 1 4198 ? 181.802 154.349 148.885 1.00 16.62  ? 4198 PRO A CD    1 
ATOM   19581 N  N     . LEU A 1 4199 ? 182.631 154.361 145.266 1.00 12.72  ? 4199 LEU A N     1 
ATOM   19582 C  CA    . LEU A 1 4199 ? 183.156 153.983 143.957 1.00 9.24   ? 4199 LEU A CA    1 
ATOM   19583 C  C     . LEU A 1 4199 ? 182.080 153.497 142.995 1.00 12.99  ? 4199 LEU A C     1 
ATOM   19584 O  O     . LEU A 1 4199 ? 182.067 153.906 141.831 1.00 20.40  ? 4199 LEU A O     1 
ATOM   19585 C  CB    . LEU A 1 4199 ? 184.232 152.903 144.109 1.00 8.27   ? 4199 LEU A CB    1 
ATOM   19586 C  CG    . LEU A 1 4199 ? 185.662 153.381 144.350 1.00 9.43   ? 4199 LEU A CG    1 
ATOM   19587 C  CD1   . LEU A 1 4199 ? 185.850 153.855 145.784 1.00 12.36  ? 4199 LEU A CD1   1 
ATOM   19588 C  CD2   . LEU A 1 4199 ? 186.640 152.271 144.012 1.00 9.01   ? 4199 LEU A CD2   1 
ATOM   19589 N  N     . GLY A 1 4200 ? 181.186 152.616 143.451 1.00 13.08  ? 4200 GLY A N     1 
ATOM   19590 C  CA    . GLY A 1 4200 ? 180.133 152.129 142.575 1.00 10.20  ? 4200 GLY A CA    1 
ATOM   19591 C  C     . GLY A 1 4200 ? 179.232 153.244 142.083 1.00 11.34  ? 4200 GLY A C     1 
ATOM   19592 O  O     . GLY A 1 4200 ? 178.750 153.214 140.949 1.00 10.59  ? 4200 GLY A O     1 
ATOM   19593 N  N     . TRP A 1 4201 ? 178.992 154.236 142.930 1.00 10.92  ? 4201 TRP A N     1 
ATOM   19594 C  CA    . TRP A 1 4201 ? 178.282 155.451 142.556 1.00 9.75   ? 4201 TRP A CA    1 
ATOM   19595 C  C     . TRP A 1 4201 ? 178.977 156.602 143.274 1.00 16.29  ? 4201 TRP A C     1 
ATOM   19596 O  O     . TRP A 1 4201 ? 180.105 156.465 143.759 1.00 25.48  ? 4201 TRP A O     1 
ATOM   19597 C  CB    . TRP A 1 4201 ? 176.787 155.325 142.883 1.00 10.64  ? 4201 TRP A CB    1 
ATOM   19598 C  CG    . TRP A 1 4201 ? 176.066 154.400 141.955 1.00 9.96   ? 4201 TRP A CG    1 
ATOM   19599 C  CD1   . TRP A 1 4201 ? 175.560 153.169 142.252 1.00 6.38   ? 4201 TRP A CD1   1 
ATOM   19600 C  CD2   . TRP A 1 4201 ? 175.779 154.629 140.572 1.00 11.56  ? 4201 TRP A CD2   1 
ATOM   19601 N  NE1   . TRP A 1 4201 ? 174.973 152.619 141.139 1.00 5.92   ? 4201 TRP A NE1   1 
ATOM   19602 C  CE2   . TRP A 1 4201 ? 175.095 153.496 140.094 1.00 8.69   ? 4201 TRP A CE2   1 
ATOM   19603 C  CE3   . TRP A 1 4201 ? 176.033 155.683 139.691 1.00 10.16  ? 4201 TRP A CE3   1 
ATOM   19604 C  CZ2   . TRP A 1 4201 ? 174.662 153.390 138.776 1.00 9.66   ? 4201 TRP A CZ2   1 
ATOM   19605 C  CZ3   . TRP A 1 4201 ? 175.602 155.574 138.386 1.00 10.31  ? 4201 TRP A CZ3   1 
ATOM   19606 C  CH2   . TRP A 1 4201 ? 174.924 154.437 137.941 1.00 9.71   ? 4201 TRP A CH2   1 
ATOM   19607 N  N     . SER A 1 4202 ? 178.330 157.764 143.325 1.00 16.91  ? 4202 SER A N     1 
ATOM   19608 C  CA    . SER A 1 4202 ? 178.828 158.864 144.136 1.00 15.83  ? 4202 SER A CA    1 
ATOM   19609 C  C     . SER A 1 4202 ? 178.009 159.096 145.394 1.00 22.00  ? 4202 SER A C     1 
ATOM   19610 O  O     . SER A 1 4202 ? 178.517 159.710 146.338 1.00 29.37  ? 4202 SER A O     1 
ATOM   19611 C  CB    . SER A 1 4202 ? 178.871 160.164 143.321 1.00 14.91  ? 4202 SER A CB    1 
ATOM   19612 O  OG    . SER A 1 4202 ? 179.789 160.059 142.249 1.00 24.74  ? 4202 SER A OG    1 
ATOM   19613 N  N     . LYS A 1 4203 ? 176.769 158.618 145.433 1.00 19.64  ? 4203 LYS A N     1 
ATOM   19614 C  CA    . LYS A 1 4203 ? 175.927 158.737 146.611 1.00 18.47  ? 4203 LYS A CA    1 
ATOM   19615 C  C     . LYS A 1 4203 ? 174.924 157.594 146.610 1.00 17.65  ? 4203 LYS A C     1 
ATOM   19616 O  O     . LYS A 1 4203 ? 174.720 156.922 145.596 1.00 18.82  ? 4203 LYS A O     1 
ATOM   19617 C  CB    . LYS A 1 4203 ? 175.210 160.090 146.659 1.00 19.86  ? 4203 LYS A CB    1 
ATOM   19618 C  CG    . LYS A 1 4203 ? 174.521 160.472 145.366 1.00 15.63  ? 4203 LYS A CG    1 
ATOM   19619 C  CD    . LYS A 1 4203 ? 173.850 161.826 145.488 1.00 23.01  ? 4203 LYS A CD    1 
ATOM   19620 C  CE    . LYS A 1 4203 ? 174.874 162.928 145.700 1.00 28.22  ? 4203 LYS A CE    1 
ATOM   19621 N  NZ    . LYS A 1 4203 ? 175.798 163.063 144.541 1.00 25.71  ? 4203 LYS A NZ    1 
ATOM   19622 N  N     . LYS A 1 4204 ? 174.300 157.379 147.767 1.00 18.78  ? 4204 LYS A N     1 
ATOM   19623 C  CA    . LYS A 1 4204 ? 173.345 156.287 147.944 1.00 18.29  ? 4204 LYS A CA    1 
ATOM   19624 C  C     . LYS A 1 4204 ? 172.035 156.651 147.253 1.00 16.58  ? 4204 LYS A C     1 
ATOM   19625 O  O     . LYS A 1 4204 ? 171.065 157.098 147.869 1.00 21.16  ? 4204 LYS A O     1 
ATOM   19626 C  CB    . LYS A 1 4204 ? 173.135 155.994 149.424 1.00 19.32  ? 4204 LYS A CB    1 
ATOM   19627 C  CG    . LYS A 1 4204 ? 174.379 155.512 150.144 1.00 18.82  ? 4204 LYS A CG    1 
ATOM   19628 C  CD    . LYS A 1 4204 ? 174.836 154.173 149.596 1.00 16.93  ? 4204 LYS A CD    1 
ATOM   19629 C  CE    . LYS A 1 4204 ? 173.881 153.061 149.995 1.00 25.76  ? 4204 LYS A CE    1 
ATOM   19630 N  NZ    . LYS A 1 4204 ? 174.351 151.728 149.532 1.00 28.94  ? 4204 LYS A NZ    1 
ATOM   19631 N  N     . TYR A 1 4205 ? 172.014 156.454 145.938 1.00 12.79  ? 4205 TYR A N     1 
ATOM   19632 C  CA    . TYR A 1 4205 ? 170.784 156.626 145.181 1.00 13.17  ? 4205 TYR A CA    1 
ATOM   19633 C  C     . TYR A 1 4205 ? 169.769 155.560 145.570 1.00 16.27  ? 4205 TYR A C     1 
ATOM   19634 O  O     . TYR A 1 4205 ? 170.121 154.438 145.942 1.00 20.69  ? 4205 TYR A O     1 
ATOM   19635 C  CB    . TYR A 1 4205 ? 171.053 156.556 143.681 1.00 12.64  ? 4205 TYR A CB    1 
ATOM   19636 C  CG    . TYR A 1 4205 ? 171.874 157.698 143.139 1.00 10.82  ? 4205 TYR A CG    1 
ATOM   19637 C  CD1   . TYR A 1 4205 ? 171.403 159.001 143.193 1.00 10.43  ? 4205 TYR A CD1   1 
ATOM   19638 C  CD2   . TYR A 1 4205 ? 173.113 157.472 142.565 1.00 10.42  ? 4205 TYR A CD2   1 
ATOM   19639 C  CE1   . TYR A 1 4205 ? 172.147 160.047 142.694 1.00 10.76  ? 4205 TYR A CE1   1 
ATOM   19640 C  CE2   . TYR A 1 4205 ? 173.862 158.511 142.065 1.00 13.91  ? 4205 TYR A CE2   1 
ATOM   19641 C  CZ    . TYR A 1 4205 ? 173.376 159.797 142.132 1.00 13.39  ? 4205 TYR A CZ    1 
ATOM   19642 O  OH    . TYR A 1 4205 ? 174.122 160.839 141.633 1.00 13.59  ? 4205 TYR A OH    1 
ATOM   19643 N  N     . GLU A 1 4206 ? 168.494 155.923 145.477 1.00 17.25  ? 4206 GLU A N     1 
ATOM   19644 C  CA    . GLU A 1 4206 ? 167.417 155.021 145.879 1.00 12.61  ? 4206 GLU A CA    1 
ATOM   19645 C  C     . GLU A 1 4206 ? 166.887 154.249 144.671 1.00 14.40  ? 4206 GLU A C     1 
ATOM   19646 O  O     . GLU A 1 4206 ? 165.702 154.270 144.343 1.00 15.34  ? 4206 GLU A O     1 
ATOM   19647 C  CB    . GLU A 1 4206 ? 166.309 155.803 146.573 1.00 16.28  ? 4206 GLU A CB    1 
ATOM   19648 C  CG    . GLU A 1 4206 ? 166.738 156.414 147.893 1.00 23.25  ? 4206 GLU A CG    1 
ATOM   19649 C  CD    . GLU A 1 4206 ? 167.052 155.370 148.938 1.00 29.21  ? 4206 GLU A CD    1 
ATOM   19650 O  OE1   . GLU A 1 4206 ? 166.422 154.296 148.908 1.00 29.13  ? 4206 GLU A OE1   1 
ATOM   19651 O  OE2   . GLU A 1 4206 ? 167.930 155.619 149.790 1.00 32.61  ? 4206 GLU A OE2   1 
ATOM   19652 N  N     . PHE A 1 4207 ? 167.803 153.551 144.006 1.00 14.20  ? 4207 PHE A N     1 
ATOM   19653 C  CA    . PHE A 1 4207 ? 167.450 152.681 142.888 1.00 8.04   ? 4207 PHE A CA    1 
ATOM   19654 C  C     . PHE A 1 4207 ? 166.683 151.489 143.435 1.00 12.98  ? 4207 PHE A C     1 
ATOM   19655 O  O     . PHE A 1 4207 ? 167.270 150.546 143.970 1.00 16.59  ? 4207 PHE A O     1 
ATOM   19656 C  CB    . PHE A 1 4207 ? 168.701 152.236 142.141 1.00 7.94   ? 4207 PHE A CB    1 
ATOM   19657 C  CG    . PHE A 1 4207 ? 169.406 153.344 141.416 1.00 9.71   ? 4207 PHE A CG    1 
ATOM   19658 C  CD1   . PHE A 1 4207 ? 168.711 154.181 140.563 1.00 9.63   ? 4207 PHE A CD1   1 
ATOM   19659 C  CD2   . PHE A 1 4207 ? 170.761 153.550 141.589 1.00 8.82   ? 4207 PHE A CD2   1 
ATOM   19660 C  CE1   . PHE A 1 4207 ? 169.358 155.196 139.890 1.00 11.15  ? 4207 PHE A CE1   1 
ATOM   19661 C  CE2   . PHE A 1 4207 ? 171.414 154.561 140.915 1.00 10.62  ? 4207 PHE A CE2   1 
ATOM   19662 C  CZ    . PHE A 1 4207 ? 170.710 155.387 140.069 1.00 11.70  ? 4207 PHE A CZ    1 
ATOM   19663 N  N     . GLY A 1 4208 ? 165.361 151.525 143.306 1.00 12.58  ? 4208 GLY A N     1 
ATOM   19664 C  CA    . GLY A 1 4208 ? 164.532 150.524 143.943 1.00 11.18  ? 4208 GLY A CA    1 
ATOM   19665 C  C     . GLY A 1 4208 ? 163.576 149.796 143.025 1.00 9.74   ? 4208 GLY A C     1 
ATOM   19666 O  O     . GLY A 1 4208 ? 163.762 149.759 141.806 1.00 9.80   ? 4208 GLY A O     1 
ATOM   19667 N  N     . GLU A 1 4209 ? 162.534 149.216 143.620 1.00 12.43  ? 4209 GLU A N     1 
ATOM   19668 C  CA    . GLU A 1 4209 ? 161.627 148.344 142.883 1.00 17.81  ? 4209 GLU A CA    1 
ATOM   19669 C  C     . GLU A 1 4209 ? 160.685 149.145 141.989 1.00 14.56  ? 4209 GLU A C     1 
ATOM   19670 O  O     . GLU A 1 4209 ? 160.228 148.639 140.956 1.00 15.20  ? 4209 GLU A O     1 
ATOM   19671 C  CB    . GLU A 1 4209 ? 160.868 147.473 143.888 1.00 25.62  ? 4209 GLU A CB    1 
ATOM   19672 C  CG    . GLU A 1 4209 ? 160.043 146.329 143.323 1.00 34.82  ? 4209 GLU A CG    1 
ATOM   19673 C  CD    . GLU A 1 4209 ? 158.672 146.752 142.861 1.00 46.72  ? 4209 GLU A CD    1 
ATOM   19674 O  OE1   . GLU A 1 4209 ? 158.126 147.727 143.416 1.00 42.96  ? 4209 GLU A OE1   1 
ATOM   19675 O  OE2   . GLU A 1 4209 ? 158.128 146.080 141.961 1.00 48.62  ? 4209 GLU A OE2   1 
ATOM   19676 N  N     . SER A 1 4210 ? 160.398 150.397 142.360 1.00 12.95  ? 4210 SER A N     1 
ATOM   19677 C  CA    . SER A 1 4210 ? 159.567 151.252 141.517 1.00 11.63  ? 4210 SER A CA    1 
ATOM   19678 C  C     . SER A 1 4210 ? 160.256 151.563 140.195 1.00 9.58   ? 4210 SER A C     1 
ATOM   19679 O  O     . SER A 1 4210 ? 159.605 151.627 139.146 1.00 7.52   ? 4210 SER A O     1 
ATOM   19680 C  CB    . SER A 1 4210 ? 159.221 152.542 142.260 1.00 10.87  ? 4210 SER A CB    1 
ATOM   19681 O  OG    . SER A 1 4210 ? 160.361 153.077 142.906 1.00 15.92  ? 4210 SER A OG    1 
ATOM   19682 N  N     . ASP A 1 4211 ? 161.575 151.772 140.226 1.00 11.83  ? 4211 ASP A N     1 
ATOM   19683 C  CA    . ASP A 1 4211 ? 162.322 151.960 138.988 1.00 7.50   ? 4211 ASP A CA    1 
ATOM   19684 C  C     . ASP A 1 4211 ? 162.233 150.723 138.106 1.00 8.93   ? 4211 ASP A C     1 
ATOM   19685 O  O     . ASP A 1 4211 ? 162.109 150.832 136.881 1.00 12.88  ? 4211 ASP A O     1 
ATOM   19686 C  CB    . ASP A 1 4211 ? 163.781 152.293 139.296 1.00 8.91   ? 4211 ASP A CB    1 
ATOM   19687 C  CG    . ASP A 1 4211 ? 163.947 153.661 139.924 1.00 15.91  ? 4211 ASP A CG    1 
ATOM   19688 O  OD1   . ASP A 1 4211 ? 163.119 154.552 139.641 1.00 23.32  ? 4211 ASP A OD1   1 
ATOM   19689 O  OD2   . ASP A 1 4211 ? 164.907 153.847 140.699 1.00 16.99  ? 4211 ASP A OD2   1 
ATOM   19690 N  N     . LEU A 1 4212 ? 162.299 149.536 138.712 1.00 8.34   ? 4212 LEU A N     1 
ATOM   19691 C  CA    . LEU A 1 4212 ? 162.161 148.306 137.941 1.00 6.66   ? 4212 LEU A CA    1 
ATOM   19692 C  C     . LEU A 1 4212 ? 160.778 148.205 137.308 1.00 7.14   ? 4212 LEU A C     1 
ATOM   19693 O  O     . LEU A 1 4212 ? 160.654 147.826 136.138 1.00 10.69  ? 4212 LEU A O     1 
ATOM   19694 C  CB    . LEU A 1 4212 ? 162.441 147.095 138.830 1.00 8.85   ? 4212 LEU A CB    1 
ATOM   19695 C  CG    . LEU A 1 4212 ? 162.233 145.722 138.191 1.00 8.29   ? 4212 LEU A CG    1 
ATOM   19696 C  CD1   . LEU A 1 4212 ? 163.346 145.420 137.204 1.00 6.73   ? 4212 LEU A CD1   1 
ATOM   19697 C  CD2   . LEU A 1 4212 ? 162.156 144.646 139.257 1.00 10.09  ? 4212 LEU A CD2   1 
ATOM   19698 N  N     . ARG A 1 4213 ? 159.726 148.545 138.061 1.00 7.29   ? 4213 ARG A N     1 
ATOM   19699 C  CA    . ARG A 1 4213 ? 158.385 148.536 137.481 1.00 8.01   ? 4213 ARG A CA    1 
ATOM   19700 C  C     . ARG A 1 4213 ? 158.266 149.525 136.330 1.00 9.42   ? 4213 ARG A C     1 
ATOM   19701 O  O     . ARG A 1 4213 ? 157.663 149.214 135.296 1.00 14.61  ? 4213 ARG A O     1 
ATOM   19702 C  CB    . ARG A 1 4213 ? 157.325 148.843 138.538 1.00 14.04  ? 4213 ARG A CB    1 
ATOM   19703 C  CG    . ARG A 1 4213 ? 157.150 147.787 139.603 1.00 19.00  ? 4213 ARG A CG    1 
ATOM   19704 C  CD    . ARG A 1 4213 ? 156.046 148.191 140.568 1.00 38.57  ? 4213 ARG A CD    1 
ATOM   19705 N  NE    . ARG A 1 4213 ? 155.890 147.248 141.668 1.00 44.77  ? 4213 ARG A NE    1 
ATOM   19706 C  CZ    . ARG A 1 4213 ? 155.101 146.183 141.635 1.00 45.94  ? 4213 ARG A CZ    1 
ATOM   19707 N  NH1   . ARG A 1 4213 ? 154.375 145.893 140.567 1.00 58.38  ? 4213 ARG A NH1   1 
ATOM   19708 N  NH2   . ARG A 1 4213 ? 155.036 145.390 142.700 1.00 47.13  ? 4213 ARG A NH2   1 
ATOM   19709 N  N     . SER A 1 4214 ? 158.814 150.731 136.497 1.00 9.31   ? 4214 SER A N     1 
ATOM   19710 C  CA    . SER A 1 4214 ? 158.734 151.728 135.436 1.00 6.62   ? 4214 SER A CA    1 
ATOM   19711 C  C     . SER A 1 4214 ? 159.478 151.268 134.190 1.00 6.52   ? 4214 SER A C     1 
ATOM   19712 O  O     . SER A 1 4214 ? 158.994 151.445 133.067 1.00 8.45   ? 4214 SER A O     1 
ATOM   19713 C  CB    . SER A 1 4214 ? 159.282 153.066 135.930 1.00 7.26   ? 4214 SER A CB    1 
ATOM   19714 O  OG    . SER A 1 4214 ? 158.613 153.485 137.105 1.00 7.70   ? 4214 SER A OG    1 
ATOM   19715 N  N     . ALA A 1 4215 ? 160.657 150.669 134.370 1.00 8.09   ? 4215 ALA A N     1 
ATOM   19716 C  CA    . ALA A 1 4215 ? 161.411 150.161 133.230 1.00 6.57   ? 4215 ALA A CA    1 
ATOM   19717 C  C     . ALA A 1 4215 ? 160.669 149.025 132.537 1.00 7.54   ? 4215 ALA A C     1 
ATOM   19718 O  O     . ALA A 1 4215 ? 160.656 148.948 131.304 1.00 11.68  ? 4215 ALA A O     1 
ATOM   19719 C  CB    . ALA A 1 4215 ? 162.797 149.706 133.681 1.00 7.16   ? 4215 ALA A CB    1 
ATOM   19720 N  N     . CYS A 1 4216 ? 160.052 148.130 133.312 1.00 8.54   ? 4216 CYS A N     1 
ATOM   19721 C  CA    . CYS A 1 4216 ? 159.280 147.045 132.715 1.00 9.29   ? 4216 CYS A CA    1 
ATOM   19722 C  C     . CYS A 1 4216 ? 158.090 147.583 131.932 1.00 12.71  ? 4216 CYS A C     1 
ATOM   19723 O  O     . CYS A 1 4216 ? 157.790 147.100 130.834 1.00 15.08  ? 4216 CYS A O     1 
ATOM   19724 C  CB    . CYS A 1 4216 ? 158.815 146.075 133.800 1.00 13.50  ? 4216 CYS A CB    1 
ATOM   19725 S  SG    . CYS A 1 4216 ? 160.134 145.085 134.532 1.00 19.30  ? 4216 CYS A SG    1 
ATOM   19726 N  N     . ASP A 1 4217 ? 157.401 148.586 132.482 1.00 13.73  ? 4217 ASP A N     1 
ATOM   19727 C  CA    . ASP A 1 4217 ? 156.281 149.198 131.775 1.00 11.77  ? 4217 ASP A CA    1 
ATOM   19728 C  C     . ASP A 1 4217 ? 156.742 149.863 130.485 1.00 12.16  ? 4217 ASP A C     1 
ATOM   19729 O  O     . ASP A 1 4217 ? 156.074 149.757 129.449 1.00 16.27  ? 4217 ASP A O     1 
ATOM   19730 C  CB    . ASP A 1 4217 ? 155.582 150.212 132.678 1.00 11.66  ? 4217 ASP A CB    1 
ATOM   19731 C  CG    . ASP A 1 4217 ? 154.805 149.556 133.801 1.00 27.55  ? 4217 ASP A CG    1 
ATOM   19732 O  OD1   . ASP A 1 4217 ? 154.727 150.151 134.896 1.00 34.91  ? 4217 ASP A OD1   1 
ATOM   19733 O  OD2   . ASP A 1 4217 ? 154.271 148.447 133.590 1.00 29.33  ? 4217 ASP A OD2   1 
ATOM   19734 N  N     . THR A 1 4218 ? 157.880 150.560 130.530 1.00 9.97   ? 4218 THR A N     1 
ATOM   19735 C  CA    . THR A 1 4218 ? 158.419 151.187 129.328 1.00 8.78   ? 4218 THR A CA    1 
ATOM   19736 C  C     . THR A 1 4218 ? 158.767 150.145 128.273 1.00 11.06  ? 4218 THR A C     1 
ATOM   19737 O  O     . THR A 1 4218 ? 158.455 150.318 127.086 1.00 15.00  ? 4218 THR A O     1 
ATOM   19738 C  CB    . THR A 1 4218 ? 159.650 152.021 129.684 1.00 7.75   ? 4218 THR A CB    1 
ATOM   19739 O  OG1   . THR A 1 4218 ? 159.254 153.147 130.478 1.00 8.82   ? 4218 THR A OG1   1 
ATOM   19740 C  CG2   . THR A 1 4218 ? 160.354 152.510 128.429 1.00 9.29   ? 4218 THR A CG2   1 
ATOM   19741 N  N     . VAL A 1 4219 ? 159.411 149.053 128.689 1.00 12.81  ? 4219 VAL A N     1 
ATOM   19742 C  CA    . VAL A 1 4219 ? 159.771 147.993 127.753 1.00 13.47  ? 4219 VAL A CA    1 
ATOM   19743 C  C     . VAL A 1 4219 ? 158.519 147.407 127.119 1.00 17.31  ? 4219 VAL A C     1 
ATOM   19744 O  O     . VAL A 1 4219 ? 158.447 147.225 125.899 1.00 24.53  ? 4219 VAL A O     1 
ATOM   19745 C  CB    . VAL A 1 4219 ? 160.607 146.912 128.462 1.00 10.22  ? 4219 VAL A CB    1 
ATOM   19746 C  CG1   . VAL A 1 4219 ? 160.620 145.628 127.648 1.00 13.78  ? 4219 VAL A CG1   1 
ATOM   19747 C  CG2   . VAL A 1 4219 ? 162.021 147.407 128.699 1.00 10.88  ? 4219 VAL A CG2   1 
ATOM   19748 N  N     . ASP A 1 4220 ? 157.505 147.120 127.940 1.00 16.50  ? 4220 ASP A N     1 
ATOM   19749 C  CA    . ASP A 1 4220 ? 156.258 146.569 127.420 1.00 17.69  ? 4220 ASP A CA    1 
ATOM   19750 C  C     . ASP A 1 4220 ? 155.618 147.513 126.412 1.00 20.97  ? 4220 ASP A C     1 
ATOM   19751 O  O     . ASP A 1 4220 ? 155.244 147.099 125.309 1.00 29.43  ? 4220 ASP A O     1 
ATOM   19752 C  CB    . ASP A 1 4220 ? 155.294 146.285 128.572 1.00 22.75  ? 4220 ASP A CB    1 
ATOM   19753 C  CG    . ASP A 1 4220 ? 155.513 144.925 129.192 1.00 33.22  ? 4220 ASP A CG    1 
ATOM   19754 O  OD1   . ASP A 1 4220 ? 156.264 144.118 128.608 1.00 43.67  ? 4220 ASP A OD1   1 
ATOM   19755 O  OD2   . ASP A 1 4220 ? 154.935 144.664 130.267 1.00 33.41  ? 4220 ASP A OD2   1 
ATOM   19756 N  N     . THR A 1 4221 ? 155.497 148.794 126.770 1.00 17.24  ? 4221 THR A N     1 
ATOM   19757 C  CA    . THR A 1 4221 ? 154.830 149.753 125.895 1.00 19.89  ? 4221 THR A CA    1 
ATOM   19758 C  C     . THR A 1 4221 ? 155.557 149.883 124.564 1.00 17.79  ? 4221 THR A C     1 
ATOM   19759 O  O     . THR A 1 4221 ? 154.937 149.815 123.496 1.00 24.04  ? 4221 THR A O     1 
ATOM   19760 C  CB    . THR A 1 4221 ? 154.730 151.114 126.586 1.00 17.28  ? 4221 THR A CB    1 
ATOM   19761 O  OG1   . THR A 1 4221 ? 153.892 151.007 127.743 1.00 28.69  ? 4221 THR A OG1   1 
ATOM   19762 C  CG2   . THR A 1 4221 ? 154.144 152.149 125.640 1.00 13.84  ? 4221 THR A CG2   1 
ATOM   19763 N  N     . TRP A 1 4222 ? 156.880 150.051 124.603 1.00 16.19  ? 4222 TRP A N     1 
ATOM   19764 C  CA    . TRP A 1 4222 ? 157.606 150.291 123.362 1.00 15.94  ? 4222 TRP A CA    1 
ATOM   19765 C  C     . TRP A 1 4222 ? 157.719 149.030 122.514 1.00 19.72  ? 4222 TRP A C     1 
ATOM   19766 O  O     . TRP A 1 4222 ? 157.681 149.115 121.281 1.00 24.92  ? 4222 TRP A O     1 
ATOM   19767 C  CB    . TRP A 1 4222 ? 158.980 150.882 123.667 1.00 11.69  ? 4222 TRP A CB    1 
ATOM   19768 C  CG    . TRP A 1 4222 ? 158.887 152.341 123.958 1.00 10.01  ? 4222 TRP A CG    1 
ATOM   19769 C  CD1   . TRP A 1 4222 ? 158.829 152.929 125.185 1.00 10.26  ? 4222 TRP A CD1   1 
ATOM   19770 C  CD2   . TRP A 1 4222 ? 158.802 153.402 123.000 1.00 13.12  ? 4222 TRP A CD2   1 
ATOM   19771 N  NE1   . TRP A 1 4222 ? 158.727 154.292 125.052 1.00 12.95  ? 4222 TRP A NE1   1 
ATOM   19772 C  CE2   . TRP A 1 4222 ? 158.709 154.608 123.720 1.00 12.02  ? 4222 TRP A CE2   1 
ATOM   19773 C  CE3   . TRP A 1 4222 ? 158.803 153.450 121.603 1.00 14.04  ? 4222 TRP A CE3   1 
ATOM   19774 C  CZ2   . TRP A 1 4222 ? 158.618 155.846 123.092 1.00 13.85  ? 4222 TRP A CZ2   1 
ATOM   19775 C  CZ3   . TRP A 1 4222 ? 158.714 154.680 120.982 1.00 11.14  ? 4222 TRP A CZ3   1 
ATOM   19776 C  CH2   . TRP A 1 4222 ? 158.623 155.861 121.725 1.00 13.78  ? 4222 TRP A CH2   1 
ATOM   19777 N  N     . LEU A 1 4223 ? 157.843 147.857 123.140 1.00 20.09  ? 4223 LEU A N     1 
ATOM   19778 C  CA    . LEU A 1 4223 ? 157.838 146.618 122.374 1.00 22.11  ? 4223 LEU A CA    1 
ATOM   19779 C  C     . LEU A 1 4223 ? 156.489 146.391 121.707 1.00 27.18  ? 4223 LEU A C     1 
ATOM   19780 O  O     . LEU A 1 4223 ? 156.430 145.990 120.539 1.00 31.45  ? 4223 LEU A O     1 
ATOM   19781 C  CB    . LEU A 1 4223 ? 158.193 145.441 123.280 1.00 22.65  ? 4223 LEU A CB    1 
ATOM   19782 C  CG    . LEU A 1 4223 ? 158.798 144.230 122.575 1.00 28.36  ? 4223 LEU A CG    1 
ATOM   19783 C  CD1   . LEU A 1 4223 ? 159.875 144.673 121.602 1.00 30.64  ? 4223 LEU A CD1   1 
ATOM   19784 C  CD2   . LEU A 1 4223 ? 159.355 143.251 123.584 1.00 25.45  ? 4223 LEU A CD2   1 
ATOM   19785 N  N     . ASP A 1 4224 ? 155.393 146.643 122.429 1.00 25.28  ? 4224 ASP A N     1 
ATOM   19786 C  CA    . ASP A 1 4224 ? 154.070 146.495 121.835 1.00 23.54  ? 4224 ASP A CA    1 
ATOM   19787 C  C     . ASP A 1 4224 ? 153.864 147.488 120.700 1.00 33.40  ? 4224 ASP A C     1 
ATOM   19788 O  O     . ASP A 1 4224 ? 153.239 147.160 119.685 1.00 40.82  ? 4224 ASP A O     1 
ATOM   19789 C  CB    . ASP A 1 4224 ? 152.993 146.668 122.906 1.00 31.49  ? 4224 ASP A CB    1 
ATOM   19790 C  CG    . ASP A 1 4224 ? 152.997 145.544 123.922 1.00 42.00  ? 4224 ASP A CG    1 
ATOM   19791 O  OD1   . ASP A 1 4224 ? 153.693 144.534 123.689 1.00 47.27  ? 4224 ASP A OD1   1 
ATOM   19792 O  OD2   . ASP A 1 4224 ? 152.306 145.670 124.955 1.00 40.40  ? 4224 ASP A OD2   1 
ATOM   19793 N  N     . ASP A 1 4225 ? 154.370 148.713 120.857 1.00 33.70  ? 4225 ASP A N     1 
ATOM   19794 C  CA    . ASP A 1 4225 ? 154.274 149.692 119.780 1.00 29.31  ? 4225 ASP A CA    1 
ATOM   19795 C  C     . ASP A 1 4225 ? 155.052 149.234 118.552 1.00 31.66  ? 4225 ASP A C     1 
ATOM   19796 O  O     . ASP A 1 4225 ? 154.560 149.326 117.422 1.00 43.11  ? 4225 ASP A O     1 
ATOM   19797 C  CB    . ASP A 1 4225 ? 154.778 151.053 120.261 1.00 30.22  ? 4225 ASP A CB    1 
ATOM   19798 C  CG    . ASP A 1 4225 ? 154.743 152.104 119.170 1.00 44.68  ? 4225 ASP A CG    1 
ATOM   19799 O  OD1   . ASP A 1 4225 ? 153.667 152.301 118.570 1.00 46.00  ? 4225 ASP A OD1   1 
ATOM   19800 O  OD2   . ASP A 1 4225 ? 155.791 152.732 118.911 1.00 48.67  ? 4225 ASP A OD2   1 
ATOM   19801 N  N     . THR A 1 4226 ? 156.270 148.730 118.755 1.00 31.40  ? 4226 THR A N     1 
ATOM   19802 C  CA    . THR A 1 4226 ? 157.081 148.303 117.619 1.00 32.41  ? 4226 THR A CA    1 
ATOM   19803 C  C     . THR A 1 4226 ? 156.567 146.994 117.031 1.00 35.78  ? 4226 THR A C     1 
ATOM   19804 O  O     . THR A 1 4226 ? 156.543 146.823 115.806 1.00 40.88  ? 4226 THR A O     1 
ATOM   19805 C  CB    . THR A 1 4226 ? 158.545 148.175 118.043 1.00 35.09  ? 4226 THR A CB    1 
ATOM   19806 O  OG1   . THR A 1 4226 ? 159.115 149.482 118.185 1.00 38.06  ? 4226 THR A OG1   1 
ATOM   19807 C  CG2   . THR A 1 4226 ? 159.346 147.397 117.012 1.00 33.08  ? 4226 THR A CG2   1 
ATOM   19808 N  N     . ALA A 1 4227 ? 156.127 146.070 117.881 1.00 38.53  ? 4227 ALA A N     1 
ATOM   19809 C  CA    . ALA A 1 4227 ? 155.643 144.761 117.447 1.00 36.85  ? 4227 ALA A CA    1 
ATOM   19810 C  C     . ALA A 1 4227 ? 154.124 144.739 117.570 1.00 50.42  ? 4227 ALA A C     1 
ATOM   19811 O  O     . ALA A 1 4227 ? 153.582 144.580 118.667 1.00 54.69  ? 4227 ALA A O     1 
ATOM   19812 C  CB    . ALA A 1 4227 ? 156.283 143.648 118.269 1.00 38.56  ? 4227 ALA A CB    1 
ATOM   19813 N  N     . LYS A 1 4228 ? 153.434 144.886 116.438 1.00 50.78  ? 4228 LYS A N     1 
ATOM   19814 C  CA    . LYS A 1 4228 ? 151.971 144.857 116.408 1.00 51.24  ? 4228 LYS A CA    1 
ATOM   19815 C  C     . LYS A 1 4228 ? 151.484 143.408 116.482 1.00 49.08  ? 4228 LYS A C     1 
ATOM   19816 O  O     . LYS A 1 4228 ? 150.827 142.881 115.582 1.00 51.88  ? 4228 LYS A O     1 
ATOM   19817 C  CB    . LYS A 1 4228 ? 151.442 145.553 115.162 1.00 51.57  ? 4228 LYS A CB    1 
ATOM   19818 C  CG    . LYS A 1 4228 ? 151.820 147.018 115.031 1.00 50.26  ? 4228 LYS A CG    1 
ATOM   19819 C  CD    . LYS A 1 4228 ? 151.179 147.849 116.128 1.00 53.00  ? 4228 LYS A CD    1 
ATOM   19820 C  CE    . LYS A 1 4228 ? 151.410 149.335 115.904 1.00 50.16  ? 4228 LYS A CE    1 
ATOM   19821 N  NZ    . LYS A 1 4228 ? 152.830 149.726 116.088 1.00 43.99  ? 4228 LYS A NZ    1 
ATOM   19822 N  N     . GLY A 1 4229 ? 151.823 142.759 117.594 1.00 49.26  ? 4229 GLY A N     1 
ATOM   19823 C  CA    . GLY A 1 4229 ? 151.400 141.398 117.837 1.00 50.14  ? 4229 GLY A CA    1 
ATOM   19824 C  C     . GLY A 1 4229 ? 152.184 140.334 117.103 1.00 51.83  ? 4229 GLY A C     1 
ATOM   19825 O  O     . GLY A 1 4229 ? 151.834 139.152 117.209 1.00 56.86  ? 4229 GLY A O     1 
ATOM   19826 N  N     . ARG A 1 4230 ? 153.223 140.706 116.361 1.00 49.24  ? 4230 ARG A N     1 
ATOM   19827 C  CA    . ARG A 1 4230 ? 154.022 139.720 115.648 1.00 46.92  ? 4230 ARG A CA    1 
ATOM   19828 C  C     . ARG A 1 4230 ? 154.747 138.811 116.631 1.00 55.31  ? 4230 ARG A C     1 
ATOM   19829 O  O     . ARG A 1 4230 ? 155.250 139.260 117.664 1.00 57.44  ? 4230 ARG A O     1 
ATOM   19830 C  CB    . ARG A 1 4230 ? 155.028 140.410 114.729 1.00 50.55  ? 4230 ARG A CB    1 
ATOM   19831 C  CG    . ARG A 1 4230 ? 154.403 141.358 113.723 1.00 49.03  ? 4230 ARG A CG    1 
ATOM   19832 C  CD    . ARG A 1 4230 ? 155.343 141.614 112.559 1.00 52.42  ? 4230 ARG A CD    1 
ATOM   19833 N  NE    . ARG A 1 4230 ? 156.683 141.977 113.005 1.00 57.11  ? 4230 ARG A NE    1 
ATOM   19834 C  CZ    . ARG A 1 4230 ? 157.425 142.925 112.451 1.00 69.50  ? 4230 ARG A CZ    1 
ATOM   19835 N  NH1   . ARG A 1 4230 ? 156.987 143.633 111.422 1.00 70.06  ? 4230 ARG A NH1   1 
ATOM   19836 N  NH2   . ARG A 1 4230 ? 158.638 143.170 112.940 1.00 65.00  ? 4230 ARG A NH2   1 
ATOM   19837 N  N     . GLN A 1 4231 ? 154.792 137.518 116.302 1.00 57.00  ? 4231 GLN A N     1 
ATOM   19838 C  CA    . GLN A 1 4231 ? 155.422 136.547 117.190 1.00 52.85  ? 4231 GLN A CA    1 
ATOM   19839 C  C     . GLN A 1 4231 ? 156.913 136.813 117.354 1.00 54.55  ? 4231 GLN A C     1 
ATOM   19840 O  O     . GLN A 1 4231 ? 157.441 136.698 118.465 1.00 52.01  ? 4231 GLN A O     1 
ATOM   19841 C  CB    . GLN A 1 4231 ? 155.190 135.130 116.666 1.00 51.60  ? 4231 GLN A CB    1 
ATOM   19842 C  CG    . GLN A 1 4231 ? 155.743 134.035 117.563 1.00 55.75  ? 4231 GLN A CG    1 
ATOM   19843 C  CD    . GLN A 1 4231 ? 155.026 133.953 118.896 1.00 66.80  ? 4231 GLN A CD    1 
ATOM   19844 O  OE1   . GLN A 1 4231 ? 153.802 134.070 118.966 1.00 65.17  ? 4231 GLN A OE1   1 
ATOM   19845 N  NE2   . GLN A 1 4231 ? 155.787 133.748 119.965 1.00 65.26  ? 4231 GLN A NE2   1 
ATOM   19846 N  N     . ASN A 1 4232 ? 157.603 137.165 116.273 1.00 50.36  ? 4232 ASN A N     1 
ATOM   19847 C  CA    . ASN A 1 4232 ? 159.037 137.404 116.302 1.00 46.21  ? 4232 ASN A CA    1 
ATOM   19848 C  C     . ASN A 1 4232 ? 159.357 138.713 115.599 1.00 47.79  ? 4232 ASN A C     1 
ATOM   19849 O  O     . ASN A 1 4232 ? 158.728 139.059 114.595 1.00 52.58  ? 4232 ASN A O     1 
ATOM   19850 C  CB    . ASN A 1 4232 ? 159.803 136.256 115.635 1.00 43.81  ? 4232 ASN A CB    1 
ATOM   19851 C  CG    . ASN A 1 4232 ? 159.769 134.982 116.452 1.00 45.83  ? 4232 ASN A CG    1 
ATOM   19852 O  OD1   . ASN A 1 4232 ? 159.747 135.019 117.681 1.00 51.96  ? 4232 ASN A OD1   1 
ATOM   19853 N  ND2   . ASN A 1 4232 ? 159.764 133.842 115.770 1.00 48.85  ? 4232 ASN A ND2   1 
ATOM   19854 N  N     . ILE A 1 4233 ? 160.338 139.438 116.131 1.00 44.08  ? 4233 ILE A N     1 
ATOM   19855 C  CA    . ILE A 1 4233 ? 160.847 140.658 115.518 1.00 40.30  ? 4233 ILE A CA    1 
ATOM   19856 C  C     . ILE A 1 4233 ? 162.365 140.579 115.497 1.00 38.37  ? 4233 ILE A C     1 
ATOM   19857 O  O     . ILE A 1 4233 ? 162.966 139.890 116.330 1.00 41.10  ? 4233 ILE A O     1 
ATOM   19858 C  CB    . ILE A 1 4233 ? 160.385 141.923 116.266 1.00 46.05  ? 4233 ILE A CB    1 
ATOM   19859 C  CG1   . ILE A 1 4233 ? 160.918 141.924 117.698 1.00 40.75  ? 4233 ILE A CG1   1 
ATOM   19860 C  CG2   . ILE A 1 4233 ? 158.869 142.030 116.259 1.00 44.52  ? 4233 ILE A CG2   1 
ATOM   19861 C  CD1   . ILE A 1 4233 ? 160.707 143.228 118.415 1.00 35.00  ? 4233 ILE A CD1   1 
ATOM   19862 N  N     . SER A 1 4234 ? 162.981 141.273 114.549 1.00 35.05  ? 4234 SER A N     1 
ATOM   19863 C  CA    . SER A 1 4234 ? 164.432 141.279 114.472 1.00 32.37  ? 4234 SER A CA    1 
ATOM   19864 C  C     . SER A 1 4234 ? 165.009 142.092 115.628 1.00 35.42  ? 4234 SER A C     1 
ATOM   19865 O  O     . SER A 1 4234 ? 164.396 143.073 116.064 1.00 35.57  ? 4234 SER A O     1 
ATOM   19866 C  CB    . SER A 1 4234 ? 164.898 141.859 113.136 1.00 35.56  ? 4234 SER A CB    1 
ATOM   19867 O  OG    . SER A 1 4234 ? 166.312 141.947 113.085 1.00 37.36  ? 4234 SER A OG    1 
ATOM   19868 N  N     . PRO A 1 4235 ? 166.173 141.707 116.157 1.00 34.84  ? 4235 PRO A N     1 
ATOM   19869 C  CA    . PRO A 1 4235 ? 166.799 142.521 117.211 1.00 32.83  ? 4235 PRO A CA    1 
ATOM   19870 C  C     . PRO A 1 4235 ? 167.103 143.941 116.774 1.00 30.04  ? 4235 PRO A C     1 
ATOM   19871 O  O     . PRO A 1 4235 ? 167.087 144.854 117.608 1.00 26.36  ? 4235 PRO A O     1 
ATOM   19872 C  CB    . PRO A 1 4235 ? 168.080 141.741 117.536 1.00 29.78  ? 4235 PRO A CB    1 
ATOM   19873 C  CG    . PRO A 1 4235 ? 167.781 140.341 117.127 1.00 31.12  ? 4235 PRO A CG    1 
ATOM   19874 C  CD    . PRO A 1 4235 ? 166.901 140.450 115.921 1.00 33.02  ? 4235 PRO A CD    1 
ATOM   19875 N  N     . ASP A 1 4236 ? 167.386 144.157 115.488 1.00 31.75  ? 4236 ASP A N     1 
ATOM   19876 C  CA    . ASP A 1 4236 ? 167.659 145.506 115.009 1.00 29.08  ? 4236 ASP A CA    1 
ATOM   19877 C  C     . ASP A 1 4236 ? 166.399 146.360 114.978 1.00 31.41  ? 4236 ASP A C     1 
ATOM   19878 O  O     . ASP A 1 4236 ? 166.486 147.592 115.013 1.00 33.18  ? 4236 ASP A O     1 
ATOM   19879 C  CB    . ASP A 1 4236 ? 168.298 145.447 113.623 1.00 32.53  ? 4236 ASP A CB    1 
ATOM   19880 C  CG    . ASP A 1 4236 ? 169.647 144.759 113.637 1.00 41.39  ? 4236 ASP A CG    1 
ATOM   19881 O  OD1   . ASP A 1 4236 ? 169.678 143.516 113.751 1.00 37.60  ? 4236 ASP A OD1   1 
ATOM   19882 O  OD2   . ASP A 1 4236 ? 170.676 145.460 113.535 1.00 48.22  ? 4236 ASP A OD2   1 
ATOM   19883 N  N     . LYS A 1 4237 ? 165.225 145.730 114.912 1.00 30.66  ? 4237 LYS A N     1 
ATOM   19884 C  CA    . LYS A 1 4237 ? 163.964 146.458 114.915 1.00 24.99  ? 4237 LYS A CA    1 
ATOM   19885 C  C     . LYS A 1 4237 ? 163.507 146.856 116.312 1.00 29.28  ? 4237 LYS A C     1 
ATOM   19886 O  O     . LYS A 1 4237 ? 162.573 147.655 116.433 1.00 40.60  ? 4237 LYS A O     1 
ATOM   19887 C  CB    . LYS A 1 4237 ? 162.874 145.621 114.241 1.00 31.36  ? 4237 LYS A CB    1 
ATOM   19888 C  CG    . LYS A 1 4237 ? 163.102 145.372 112.759 1.00 34.21  ? 4237 LYS A CG    1 
ATOM   19889 C  CD    . LYS A 1 4237 ? 163.642 146.608 112.061 1.00 33.00  ? 4237 LYS A CD    1 
ATOM   19890 C  CE    . LYS A 1 4237 ? 163.386 146.547 110.566 1.00 31.91  ? 4237 LYS A CE    1 
ATOM   19891 N  NZ    . LYS A 1 4237 ? 161.955 146.271 110.265 1.00 31.92  ? 4237 LYS A NZ    1 
ATOM   19892 N  N     . ILE A 1 4238 ? 164.127 146.321 117.356 1.00 25.30  ? 4238 ILE A N     1 
ATOM   19893 C  CA    . ILE A 1 4238 ? 163.754 146.684 118.728 1.00 18.57  ? 4238 ILE A CA    1 
ATOM   19894 C  C     . ILE A 1 4238 ? 164.096 148.151 118.967 1.00 17.30  ? 4238 ILE A C     1 
ATOM   19895 O  O     . ILE A 1 4238 ? 165.210 148.587 118.625 1.00 19.78  ? 4238 ILE A O     1 
ATOM   19896 C  CB    . ILE A 1 4238 ? 164.474 145.780 119.730 1.00 18.98  ? 4238 ILE A CB    1 
ATOM   19897 C  CG1   . ILE A 1 4238 ? 164.159 144.311 119.446 1.00 24.54  ? 4238 ILE A CG1   1 
ATOM   19898 C  CG2   . ILE A 1 4238 ? 164.088 146.141 121.156 1.00 16.90  ? 4238 ILE A CG2   1 
ATOM   19899 C  CD1   . ILE A 1 4238 ? 164.726 143.355 120.473 1.00 19.71  ? 4238 ILE A CD1   1 
ATOM   19900 N  N     . PRO A 1 4239 ? 163.192 148.948 119.540 1.00 18.28  ? 4239 PRO A N     1 
ATOM   19901 C  CA    . PRO A 1 4239 ? 163.514 150.357 119.800 1.00 16.02  ? 4239 PRO A CA    1 
ATOM   19902 C  C     . PRO A 1 4239 ? 164.533 150.521 120.916 1.00 12.21  ? 4239 PRO A C     1 
ATOM   19903 O  O     . PRO A 1 4239 ? 164.185 150.899 122.038 1.00 12.51  ? 4239 PRO A O     1 
ATOM   19904 C  CB    . PRO A 1 4239 ? 162.157 150.961 120.180 1.00 18.94  ? 4239 PRO A CB    1 
ATOM   19905 C  CG    . PRO A 1 4239 ? 161.373 149.812 120.710 1.00 16.49  ? 4239 PRO A CG    1 
ATOM   19906 C  CD    . PRO A 1 4239 ? 161.806 148.617 119.914 1.00 19.37  ? 4239 PRO A CD    1 
ATOM   19907 N  N     . TRP A 1 4240 ? 165.800 150.230 120.610 1.00 13.92  ? 4240 TRP A N     1 
ATOM   19908 C  CA    . TRP A 1 4240 ? 166.852 150.327 121.617 1.00 11.28  ? 4240 TRP A CA    1 
ATOM   19909 C  C     . TRP A 1 4240 ? 167.060 151.764 122.075 1.00 9.66   ? 4240 TRP A C     1 
ATOM   19910 O  O     . TRP A 1 4240 ? 167.251 152.017 123.270 1.00 8.52   ? 4240 TRP A O     1 
ATOM   19911 C  CB    . TRP A 1 4240 ? 168.155 149.753 121.064 1.00 12.06  ? 4240 TRP A CB    1 
ATOM   19912 C  CG    . TRP A 1 4240 ? 168.090 148.291 120.781 1.00 13.79  ? 4240 TRP A CG    1 
ATOM   19913 C  CD1   . TRP A 1 4240 ? 168.068 147.694 119.558 1.00 14.76  ? 4240 TRP A CD1   1 
ATOM   19914 C  CD2   . TRP A 1 4240 ? 168.053 147.234 121.745 1.00 17.22  ? 4240 TRP A CD2   1 
ATOM   19915 N  NE1   . TRP A 1 4240 ? 168.012 146.330 119.697 1.00 19.62  ? 4240 TRP A NE1   1 
ATOM   19916 C  CE2   . TRP A 1 4240 ? 168.003 146.022 121.032 1.00 16.52  ? 4240 TRP A CE2   1 
ATOM   19917 C  CE3   . TRP A 1 4240 ? 168.055 147.195 123.142 1.00 16.31  ? 4240 TRP A CE3   1 
ATOM   19918 C  CZ2   . TRP A 1 4240 ? 167.954 144.786 121.667 1.00 17.61  ? 4240 TRP A CZ2   1 
ATOM   19919 C  CZ3   . TRP A 1 4240 ? 168.007 145.967 123.769 1.00 11.78  ? 4240 TRP A CZ3   1 
ATOM   19920 C  CH2   . TRP A 1 4240 ? 167.959 144.781 123.033 1.00 15.24  ? 4240 TRP A CH2   1 
ATOM   19921 N  N     . SER A 1 4241 ? 167.038 152.714 121.138 1.00 12.55  ? 4241 SER A N     1 
ATOM   19922 C  CA    . SER A 1 4241 ? 167.288 154.109 121.487 1.00 9.10   ? 4241 SER A CA    1 
ATOM   19923 C  C     . SER A 1 4241 ? 166.225 154.641 122.437 1.00 8.83   ? 4241 SER A C     1 
ATOM   19924 O  O     . SER A 1 4241 ? 166.541 155.350 123.399 1.00 8.08   ? 4241 SER A O     1 
ATOM   19925 C  CB    . SER A 1 4241 ? 167.350 154.961 120.222 1.00 12.32  ? 4241 SER A CB    1 
ATOM   19926 O  OG    . SER A 1 4241 ? 166.131 154.888 119.503 1.00 31.13  ? 4241 SER A OG    1 
ATOM   19927 N  N     . ALA A 1 4242 ? 164.958 154.307 122.184 1.00 10.35  ? 4242 ALA A N     1 
ATOM   19928 C  CA    . ALA A 1 4242 ? 163.879 154.769 123.051 1.00 7.41   ? 4242 ALA A CA    1 
ATOM   19929 C  C     . ALA A 1 4242 ? 164.060 154.252 124.472 1.00 8.10   ? 4242 ALA A C     1 
ATOM   19930 O  O     . ALA A 1 4242 ? 163.967 155.016 125.441 1.00 9.29   ? 4242 ALA A O     1 
ATOM   19931 C  CB    . ALA A 1 4242 ? 162.531 154.323 122.487 1.00 7.49   ? 4242 ALA A CB    1 
ATOM   19932 N  N     . LEU A 1 4243 ? 164.331 152.953 124.611 1.00 9.47   ? 4243 LEU A N     1 
ATOM   19933 C  CA    . LEU A 1 4243 ? 164.505 152.367 125.935 1.00 8.23   ? 4243 LEU A CA    1 
ATOM   19934 C  C     . LEU A 1 4243 ? 165.711 152.962 126.645 1.00 8.65   ? 4243 LEU A C     1 
ATOM   19935 O  O     . LEU A 1 4243 ? 165.634 153.310 127.830 1.00 11.72  ? 4243 LEU A O     1 
ATOM   19936 C  CB    . LEU A 1 4243 ? 164.646 150.850 125.818 1.00 7.55   ? 4243 LEU A CB    1 
ATOM   19937 C  CG    . LEU A 1 4243 ? 163.441 150.114 125.233 1.00 7.96   ? 4243 LEU A CG    1 
ATOM   19938 C  CD1   . LEU A 1 4243 ? 163.820 148.697 124.833 1.00 17.54  ? 4243 LEU A CD1   1 
ATOM   19939 C  CD2   . LEU A 1 4243 ? 162.284 150.112 126.211 1.00 9.02   ? 4243 LEU A CD2   1 
ATOM   19940 N  N     . LYS A 1 4244 ? 166.832 153.097 125.933 1.00 8.17   ? 4244 LYS A N     1 
ATOM   19941 C  CA    . LYS A 1 4244 ? 168.040 153.636 126.546 1.00 6.80   ? 4244 LYS A CA    1 
ATOM   19942 C  C     . LYS A 1 4244 ? 167.828 155.069 127.012 1.00 7.44   ? 4244 LYS A C     1 
ATOM   19943 O  O     . LYS A 1 4244 ? 168.208 155.432 128.129 1.00 10.77  ? 4244 LYS A O     1 
ATOM   19944 C  CB    . LYS A 1 4244 ? 169.209 153.557 125.565 1.00 8.66   ? 4244 LYS A CB    1 
ATOM   19945 C  CG    . LYS A 1 4244 ? 169.797 152.170 125.413 1.00 8.75   ? 4244 LYS A CG    1 
ATOM   19946 C  CD    . LYS A 1 4244 ? 171.151 152.222 124.731 1.00 8.99   ? 4244 LYS A CD    1 
ATOM   19947 C  CE    . LYS A 1 4244 ? 171.043 152.812 123.339 1.00 8.62   ? 4244 LYS A CE    1 
ATOM   19948 N  NZ    . LYS A 1 4244 ? 172.344 152.773 122.622 1.00 19.39  ? 4244 LYS A NZ    1 
ATOM   19949 N  N     . THR A 1 4245 ? 167.207 155.900 126.170 1.00 7.13   ? 4245 THR A N     1 
ATOM   19950 C  CA    . THR A 1 4245 ? 166.981 157.291 126.545 1.00 6.26   ? 4245 THR A CA    1 
ATOM   19951 C  C     . THR A 1 4245 ? 166.007 157.402 127.710 1.00 7.91   ? 4245 THR A C     1 
ATOM   19952 O  O     . THR A 1 4245 ? 166.238 158.179 128.644 1.00 7.98   ? 4245 THR A O     1 
ATOM   19953 C  CB    . THR A 1 4245 ? 166.471 158.083 125.343 1.00 7.79   ? 4245 THR A CB    1 
ATOM   19954 O  OG1   . THR A 1 4245 ? 167.290 157.804 124.202 1.00 9.43   ? 4245 THR A OG1   1 
ATOM   19955 C  CG2   . THR A 1 4245 ? 166.513 159.574 125.632 1.00 8.22   ? 4245 THR A CG2   1 
ATOM   19956 N  N     . LEU A 1 4246 ? 164.917 156.630 127.685 1.00 6.46   ? 4246 LEU A N     1 
ATOM   19957 C  CA    . LEU A 1 4246 ? 163.940 156.725 128.762 1.00 6.26   ? 4246 LEU A CA    1 
ATOM   19958 C  C     . LEU A 1 4246 ? 164.504 156.215 130.081 1.00 7.20   ? 4246 LEU A C     1 
ATOM   19959 O  O     . LEU A 1 4246 ? 164.142 156.730 131.144 1.00 13.14  ? 4246 LEU A O     1 
ATOM   19960 C  CB    . LEU A 1 4246 ? 162.666 155.968 128.390 1.00 7.97   ? 4246 LEU A CB    1 
ATOM   19961 C  CG    . LEU A 1 4246 ? 161.696 156.742 127.494 1.00 6.24   ? 4246 LEU A CG    1 
ATOM   19962 C  CD1   . LEU A 1 4246 ? 160.407 155.977 127.313 1.00 8.31   ? 4246 LEU A CD1   1 
ATOM   19963 C  CD2   . LEU A 1 4246 ? 161.418 158.121 128.067 1.00 5.47   ? 4246 LEU A CD2   1 
ATOM   19964 N  N     . MET A 1 4247 ? 165.384 155.213 130.042 1.00 6.93   ? 4247 MET A N     1 
ATOM   19965 C  CA    . MET A 1 4247 ? 166.005 154.748 131.275 1.00 6.17   ? 4247 MET A CA    1 
ATOM   19966 C  C     . MET A 1 4247 ? 167.108 155.681 131.757 1.00 8.45   ? 4247 MET A C     1 
ATOM   19967 O  O     . MET A 1 4247 ? 167.315 155.807 132.969 1.00 11.27  ? 4247 MET A O     1 
ATOM   19968 C  CB    . MET A 1 4247 ? 166.551 153.334 131.089 1.00 8.56   ? 4247 MET A CB    1 
ATOM   19969 C  CG    . MET A 1 4247 ? 165.475 152.287 130.878 1.00 8.77   ? 4247 MET A CG    1 
ATOM   19970 S  SD    . MET A 1 4247 ? 166.170 150.657 130.584 1.00 34.77  ? 4247 MET A SD    1 
ATOM   19971 C  CE    . MET A 1 4247 ? 166.808 150.300 132.214 1.00 17.06  ? 4247 MET A CE    1 
ATOM   19972 N  N     . ALA A 1 4248 ? 167.825 156.336 130.843 1.00 8.34   ? 4248 ALA A N     1 
ATOM   19973 C  CA    . ALA A 1 4248 ? 168.904 157.232 131.230 1.00 5.90   ? 4248 ALA A CA    1 
ATOM   19974 C  C     . ALA A 1 4248 ? 168.424 158.622 131.614 1.00 8.34   ? 4248 ALA A C     1 
ATOM   19975 O  O     . ALA A 1 4248 ? 169.190 159.374 132.225 1.00 13.58  ? 4248 ALA A O     1 
ATOM   19976 C  CB    . ALA A 1 4248 ? 169.922 157.348 130.094 1.00 5.90   ? 4248 ALA A CB    1 
ATOM   19977 N  N     . GLN A 1 4249 ? 167.189 158.984 131.279 1.00 8.75   ? 4249 GLN A N     1 
ATOM   19978 C  CA    . GLN A 1 4249 ? 166.694 160.324 131.548 1.00 6.46   ? 4249 GLN A CA    1 
ATOM   19979 C  C     . GLN A 1 4249 ? 165.488 160.367 132.472 1.00 8.04   ? 4249 GLN A C     1 
ATOM   19980 O  O     . GLN A 1 4249 ? 165.337 161.342 133.209 1.00 11.57  ? 4249 GLN A O     1 
ATOM   19981 C  CB    . GLN A 1 4249 ? 166.332 161.032 130.233 1.00 6.73   ? 4249 GLN A CB    1 
ATOM   19982 C  CG    . GLN A 1 4249 ? 167.458 161.055 129.214 1.00 6.07   ? 4249 GLN A CG    1 
ATOM   19983 C  CD    . GLN A 1 4249 ? 168.244 162.345 129.239 1.00 8.63   ? 4249 GLN A CD    1 
ATOM   19984 O  OE1   . GLN A 1 4249 ? 167.760 163.390 128.806 1.00 9.40   ? 4249 GLN A OE1   1 
ATOM   19985 N  NE2   . GLN A 1 4249 ? 169.468 162.280 129.747 1.00 9.30   ? 4249 GLN A NE2   1 
ATOM   19986 N  N     . SER A 1 4250 ? 164.633 159.347 132.460 1.00 8.00   ? 4250 SER A N     1 
ATOM   19987 C  CA    . SER A 1 4250 ? 163.379 159.384 133.204 1.00 5.87   ? 4250 SER A CA    1 
ATOM   19988 C  C     . SER A 1 4250 ? 163.304 158.342 134.308 1.00 8.21   ? 4250 SER A C     1 
ATOM   19989 O  O     . SER A 1 4250 ? 162.979 158.684 135.450 1.00 12.57  ? 4250 SER A O     1 
ATOM   19990 C  CB    . SER A 1 4250 ? 162.194 159.210 132.241 1.00 6.06   ? 4250 SER A CB    1 
ATOM   19991 O  OG    . SER A 1 4250 ? 162.334 160.045 131.107 1.00 8.77   ? 4250 SER A OG    1 
ATOM   19992 N  N     . ILE A 1 4251 ? 163.592 157.077 134.007 1.00 7.79   ? 4251 ILE A N     1 
ATOM   19993 C  CA    . ILE A 1 4251 ? 163.373 156.013 134.983 1.00 8.74   ? 4251 ILE A CA    1 
ATOM   19994 C  C     . ILE A 1 4251 ? 164.508 155.965 135.998 1.00 9.31   ? 4251 ILE A C     1 
ATOM   19995 O  O     . ILE A 1 4251 ? 164.303 156.186 137.196 1.00 10.35  ? 4251 ILE A O     1 
ATOM   19996 C  CB    . ILE A 1 4251 ? 163.198 154.658 134.275 1.00 7.97   ? 4251 ILE A CB    1 
ATOM   19997 C  CG1   . ILE A 1 4251 ? 162.119 154.753 133.196 1.00 5.18   ? 4251 ILE A CG1   1 
ATOM   19998 C  CG2   . ILE A 1 4251 ? 162.863 153.575 135.283 1.00 6.20   ? 4251 ILE A CG2   1 
ATOM   19999 C  CD1   . ILE A 1 4251 ? 162.240 153.699 132.124 1.00 5.13   ? 4251 ILE A CD1   1 
ATOM   20000 N  N     . TYR A 1 4252 ? 165.723 155.676 135.535 1.00 9.87   ? 4252 TYR A N     1 
ATOM   20001 C  CA    . TYR A 1 4252 ? 166.870 155.565 136.426 1.00 7.36   ? 4252 TYR A CA    1 
ATOM   20002 C  C     . TYR A 1 4252 ? 167.697 156.838 136.498 1.00 8.64   ? 4252 TYR A C     1 
ATOM   20003 O  O     . TYR A 1 4252 ? 168.288 157.120 137.545 1.00 9.31   ? 4252 TYR A O     1 
ATOM   20004 C  CB    . TYR A 1 4252 ? 167.771 154.405 135.992 1.00 5.70   ? 4252 TYR A CB    1 
ATOM   20005 C  CG    . TYR A 1 4252 ? 167.232 153.043 136.355 1.00 5.58   ? 4252 TYR A CG    1 
ATOM   20006 C  CD1   . TYR A 1 4252 ? 167.530 152.459 137.578 1.00 7.06   ? 4252 TYR A CD1   1 
ATOM   20007 C  CD2   . TYR A 1 4252 ? 166.427 152.338 135.474 1.00 5.87   ? 4252 TYR A CD2   1 
ATOM   20008 C  CE1   . TYR A 1 4252 ? 167.039 151.213 137.912 1.00 5.74   ? 4252 TYR A CE1   1 
ATOM   20009 C  CE2   . TYR A 1 4252 ? 165.933 151.093 135.799 1.00 5.31   ? 4252 TYR A CE2   1 
ATOM   20010 C  CZ    . TYR A 1 4252 ? 166.242 150.535 137.018 1.00 5.97   ? 4252 TYR A CZ    1 
ATOM   20011 O  OH    . TYR A 1 4252 ? 165.749 149.294 137.342 1.00 7.38   ? 4252 TYR A OH    1 
ATOM   20012 N  N     . GLY A 1 4253 ? 167.752 157.612 135.416 1.00 9.30   ? 4253 GLY A N     1 
ATOM   20013 C  CA    . GLY A 1 4253 ? 168.484 158.862 135.432 1.00 7.22   ? 4253 GLY A CA    1 
ATOM   20014 C  C     . GLY A 1 4253 ? 167.808 159.986 136.179 1.00 9.71   ? 4253 GLY A C     1 
ATOM   20015 O  O     . GLY A 1 4253 ? 168.446 161.011 136.436 1.00 12.78  ? 4253 GLY A O     1 
ATOM   20016 N  N     . GLY A 1 4254 ? 166.532 159.819 136.532 1.00 8.13   ? 4254 GLY A N     1 
ATOM   20017 C  CA    . GLY A 1 4254 ? 165.850 160.842 137.305 1.00 6.99   ? 4254 GLY A CA    1 
ATOM   20018 C  C     . GLY A 1 4254 ? 166.447 161.021 138.687 1.00 8.95   ? 4254 GLY A C     1 
ATOM   20019 O  O     . GLY A 1 4254 ? 166.525 162.141 139.199 1.00 11.09  ? 4254 GLY A O     1 
ATOM   20020 N  N     . ARG A 1 4255 ? 166.876 159.924 139.310 1.00 8.17   ? 4255 ARG A N     1 
ATOM   20021 C  CA    . ARG A 1 4255 ? 167.502 160.006 140.623 1.00 9.27   ? 4255 ARG A CA    1 
ATOM   20022 C  C     . ARG A 1 4255 ? 168.928 160.536 140.550 1.00 10.41  ? 4255 ARG A C     1 
ATOM   20023 O  O     . ARG A 1 4255 ? 169.431 161.080 141.539 1.00 14.60  ? 4255 ARG A O     1 
ATOM   20024 C  CB    . ARG A 1 4255 ? 167.493 158.634 141.295 1.00 10.65  ? 4255 ARG A CB    1 
ATOM   20025 C  CG    . ARG A 1 4255 ? 166.144 157.949 141.276 1.00 10.48  ? 4255 ARG A CG    1 
ATOM   20026 C  CD    . ARG A 1 4255 ? 166.174 156.658 142.071 1.00 12.12  ? 4255 ARG A CD    1 
ATOM   20027 N  NE    . ARG A 1 4255 ? 164.841 156.092 142.232 1.00 14.03  ? 4255 ARG A NE    1 
ATOM   20028 C  CZ    . ARG A 1 4255 ? 163.943 156.530 143.104 1.00 14.23  ? 4255 ARG A CZ    1 
ATOM   20029 N  NH1   . ARG A 1 4255 ? 164.207 157.536 143.920 1.00 11.74  ? 4255 ARG A NH1   1 
ATOM   20030 N  NH2   . ARG A 1 4255 ? 162.752 155.943 143.158 1.00 22.04  ? 4255 ARG A NH2   1 
ATOM   20031 N  N     . VAL A 1 4256 ? 169.588 160.392 139.404 1.00 8.00   ? 4256 VAL A N     1 
ATOM   20032 C  CA    . VAL A 1 4256 ? 170.997 160.753 139.294 1.00 11.45  ? 4256 VAL A CA    1 
ATOM   20033 C  C     . VAL A 1 4256 ? 171.126 162.270 139.248 1.00 14.77  ? 4256 VAL A C     1 
ATOM   20034 O  O     . VAL A 1 4256 ? 170.540 162.934 138.385 1.00 18.04  ? 4256 VAL A O     1 
ATOM   20035 C  CB    . VAL A 1 4256 ? 171.633 160.103 138.060 1.00 10.21  ? 4256 VAL A CB    1 
ATOM   20036 C  CG1   . VAL A 1 4256 ? 172.972 160.746 137.761 1.00 12.88  ? 4256 VAL A CG1   1 
ATOM   20037 C  CG2   . VAL A 1 4256 ? 171.795 158.610 138.276 1.00 11.76  ? 4256 VAL A CG2   1 
ATOM   20038 N  N     . ASP A 1 4257 ? 171.907 162.824 140.176 1.00 12.32  ? 4257 ASP A N     1 
ATOM   20039 C  CA    . ASP A 1 4257 ? 172.121 164.262 140.273 1.00 13.90  ? 4257 ASP A CA    1 
ATOM   20040 C  C     . ASP A 1 4257 ? 173.578 164.646 140.035 1.00 18.33  ? 4257 ASP A C     1 
ATOM   20041 O  O     . ASP A 1 4257 ? 173.998 165.739 140.424 1.00 21.97  ? 4257 ASP A O     1 
ATOM   20042 C  CB    . ASP A 1 4257 ? 171.645 164.780 141.632 1.00 14.56  ? 4257 ASP A CB    1 
ATOM   20043 C  CG    . ASP A 1 4257 ? 172.244 164.016 142.798 1.00 26.40  ? 4257 ASP A CG    1 
ATOM   20044 O  OD1   . ASP A 1 4257 ? 173.486 163.920 142.884 1.00 26.33  ? 4257 ASP A OD1   1 
ATOM   20045 O  OD2   . ASP A 1 4257 ? 171.468 163.511 143.636 1.00 31.02  ? 4257 ASP A OD2   1 
ATOM   20046 N  N     . ASN A 1 4258 ? 174.354 163.771 139.402 1.00 18.66  ? 4258 ASN A N     1 
ATOM   20047 C  CA    . ASN A 1 4258 ? 175.767 164.007 139.153 1.00 15.15  ? 4258 ASN A CA    1 
ATOM   20048 C  C     . ASN A 1 4258 ? 176.076 163.717 137.692 1.00 18.16  ? 4258 ASN A C     1 
ATOM   20049 O  O     . ASN A 1 4258 ? 175.477 162.830 137.079 1.00 18.57  ? 4258 ASN A O     1 
ATOM   20050 C  CB    . ASN A 1 4258 ? 176.646 163.134 140.063 1.00 15.17  ? 4258 ASN A CB    1 
ATOM   20051 C  CG    . ASN A 1 4258 ? 178.117 163.497 139.985 1.00 21.51  ? 4258 ASN A CG    1 
ATOM   20052 O  OD1   . ASN A 1 4258 ? 178.513 164.388 139.234 1.00 35.04  ? 4258 ASN A OD1   1 
ATOM   20053 N  ND2   . ASN A 1 4258 ? 178.936 162.804 140.765 1.00 18.92  ? 4258 ASN A ND2   1 
ATOM   20054 N  N     . GLU A 1 4259 ? 177.014 164.486 137.135 1.00 17.14  ? 4259 GLU A N     1 
ATOM   20055 C  CA    . GLU A 1 4259 ? 177.408 164.285 135.745 1.00 17.41  ? 4259 GLU A CA    1 
ATOM   20056 C  C     . GLU A 1 4259 ? 178.108 162.944 135.554 1.00 15.54  ? 4259 GLU A C     1 
ATOM   20057 O  O     . GLU A 1 4259 ? 177.863 162.243 134.566 1.00 19.42  ? 4259 GLU A O     1 
ATOM   20058 C  CB    . GLU A 1 4259 ? 178.301 165.442 135.288 1.00 21.07  ? 4259 GLU A CB    1 
ATOM   20059 C  CG    . GLU A 1 4259 ? 178.595 165.481 133.792 1.00 34.80  ? 4259 GLU A CG    1 
ATOM   20060 C  CD    . GLU A 1 4259 ? 179.749 164.581 133.388 1.00 46.24  ? 4259 GLU A CD    1 
ATOM   20061 O  OE1   . GLU A 1 4259 ? 180.648 164.356 134.223 1.00 34.90  ? 4259 GLU A OE1   1 
ATOM   20062 O  OE2   . GLU A 1 4259 ? 179.756 164.098 132.236 1.00 56.47  ? 4259 GLU A OE2   1 
ATOM   20063 N  N     . PHE A 1 4260 ? 178.977 162.566 136.492 1.00 11.42  ? 4260 PHE A N     1 
ATOM   20064 C  CA    . PHE A 1 4260 ? 179.725 161.321 136.364 1.00 14.47  ? 4260 PHE A CA    1 
ATOM   20065 C  C     . PHE A 1 4260 ? 178.866 160.096 136.657 1.00 12.28  ? 4260 PHE A C     1 
ATOM   20066 O  O     . PHE A 1 4260 ? 179.042 159.053 136.018 1.00 9.68   ? 4260 PHE A O     1 
ATOM   20067 C  CB    . PHE A 1 4260 ? 180.948 161.367 137.279 1.00 12.34  ? 4260 PHE A CB    1 
ATOM   20068 C  CG    . PHE A 1 4260 ? 181.727 162.644 137.164 1.00 10.22  ? 4260 PHE A CG    1 
ATOM   20069 C  CD1   . PHE A 1 4260 ? 182.623 162.829 136.125 1.00 11.52  ? 4260 PHE A CD1   1 
ATOM   20070 C  CD2   . PHE A 1 4260 ? 181.539 163.673 138.070 1.00 14.93  ? 4260 PHE A CD2   1 
ATOM   20071 C  CE1   . PHE A 1 4260 ? 183.331 164.004 136.004 1.00 12.59  ? 4260 PHE A CE1   1 
ATOM   20072 C  CE2   . PHE A 1 4260 ? 182.245 164.853 137.953 1.00 12.89  ? 4260 PHE A CE2   1 
ATOM   20073 C  CZ    . PHE A 1 4260 ? 183.141 165.019 136.918 1.00 13.29  ? 4260 PHE A CZ    1 
ATOM   20074 N  N     . ASP A 1 4261 ? 177.928 160.201 137.600 1.00 13.76  ? 4261 ASP A N     1 
ATOM   20075 C  CA    . ASP A 1 4261 ? 176.973 159.118 137.805 1.00 10.11  ? 4261 ASP A CA    1 
ATOM   20076 C  C     . ASP A 1 4261 ? 176.088 158.934 136.579 1.00 11.80  ? 4261 ASP A C     1 
ATOM   20077 O  O     . ASP A 1 4261 ? 175.776 157.801 136.190 1.00 14.74  ? 4261 ASP A O     1 
ATOM   20078 C  CB    . ASP A 1 4261 ? 176.132 159.394 139.048 1.00 13.10  ? 4261 ASP A CB    1 
ATOM   20079 C  CG    . ASP A 1 4261 ? 176.951 159.361 140.322 1.00 16.82  ? 4261 ASP A CG    1 
ATOM   20080 O  OD1   . ASP A 1 4261 ? 178.100 158.874 140.280 1.00 16.57  ? 4261 ASP A OD1   1 
ATOM   20081 O  OD2   . ASP A 1 4261 ? 176.454 159.836 141.361 1.00 20.60  ? 4261 ASP A OD2   1 
ATOM   20082 N  N     . GLN A 1 4262 ? 175.676 160.040 135.954 1.00 10.31  ? 4262 GLN A N     1 
ATOM   20083 C  CA    . GLN A 1 4262 ? 174.930 159.951 134.704 1.00 8.94   ? 4262 GLN A CA    1 
ATOM   20084 C  C     . GLN A 1 4262 ? 175.770 159.305 133.614 1.00 8.75   ? 4262 GLN A C     1 
ATOM   20085 O  O     . GLN A 1 4262 ? 175.263 158.509 132.815 1.00 11.36  ? 4262 GLN A O     1 
ATOM   20086 C  CB    . GLN A 1 4262 ? 174.469 161.341 134.270 1.00 11.59  ? 4262 GLN A CB    1 
ATOM   20087 C  CG    . GLN A 1 4262 ? 173.585 161.340 133.038 1.00 7.58   ? 4262 GLN A CG    1 
ATOM   20088 C  CD    . GLN A 1 4262 ? 172.206 160.789 133.319 1.00 7.43   ? 4262 GLN A CD    1 
ATOM   20089 O  OE1   . GLN A 1 4262 ? 171.498 161.280 134.197 1.00 10.81  ? 4262 GLN A OE1   1 
ATOM   20090 N  NE2   . GLN A 1 4262 ? 171.815 159.763 132.576 1.00 6.62   ? 4262 GLN A NE2   1 
ATOM   20091 N  N     . ARG A 1 4263 ? 177.059 159.640 133.565 1.00 8.84   ? 4263 ARG A N     1 
ATOM   20092 C  CA    . ARG A 1 4263 ? 177.952 159.027 132.590 1.00 7.59   ? 4263 ARG A CA    1 
ATOM   20093 C  C     . ARG A 1 4263 ? 178.058 157.523 132.810 1.00 9.77   ? 4263 ARG A C     1 
ATOM   20094 O  O     . ARG A 1 4263 ? 178.084 156.751 131.850 1.00 9.63   ? 4263 ARG A O     1 
ATOM   20095 C  CB    . ARG A 1 4263 ? 179.328 159.687 132.665 1.00 8.82   ? 4263 ARG A CB    1 
ATOM   20096 C  CG    . ARG A 1 4263 ? 180.336 159.160 131.669 1.00 11.72  ? 4263 ARG A CG    1 
ATOM   20097 C  CD    . ARG A 1 4263 ? 181.632 159.940 131.763 1.00 12.39  ? 4263 ARG A CD    1 
ATOM   20098 N  NE    . ARG A 1 4263 ? 182.260 159.799 133.070 1.00 15.74  ? 4263 ARG A NE    1 
ATOM   20099 C  CZ    . ARG A 1 4263 ? 183.353 160.445 133.449 1.00 18.12  ? 4263 ARG A CZ    1 
ATOM   20100 N  NH1   . ARG A 1 4263 ? 183.962 161.302 132.646 1.00 17.69  ? 4263 ARG A NH1   1 
ATOM   20101 N  NH2   . ARG A 1 4263 ? 183.851 160.223 134.662 1.00 15.14  ? 4263 ARG A NH2   1 
ATOM   20102 N  N     . LEU A 1 4264 ? 178.122 157.091 134.071 1.00 9.02   ? 4264 LEU A N     1 
ATOM   20103 C  CA    . LEU A 1 4264 ? 178.199 155.661 134.366 1.00 6.65   ? 4264 LEU A CA    1 
ATOM   20104 C  C     . LEU A 1 4264 ? 176.893 154.948 134.018 1.00 10.19  ? 4264 LEU A C     1 
ATOM   20105 O  O     . LEU A 1 4264 ? 176.902 153.808 133.530 1.00 12.01  ? 4264 LEU A O     1 
ATOM   20106 C  CB    . LEU A 1 4264 ? 178.553 155.461 135.838 1.00 8.19   ? 4264 LEU A CB    1 
ATOM   20107 C  CG    . LEU A 1 4264 ? 178.588 154.037 136.389 1.00 11.34  ? 4264 LEU A CG    1 
ATOM   20108 C  CD1   . LEU A 1 4264 ? 179.516 153.163 135.564 1.00 11.81  ? 4264 LEU A CD1   1 
ATOM   20109 C  CD2   . LEU A 1 4264 ? 179.019 154.059 137.839 1.00 8.38   ? 4264 LEU A CD2   1 
ATOM   20110 N  N     . LEU A 1 4265 ? 175.757 155.600 134.268 1.00 8.52   ? 4265 LEU A N     1 
ATOM   20111 C  CA    . LEU A 1 4265 ? 174.479 155.015 133.877 1.00 6.12   ? 4265 LEU A CA    1 
ATOM   20112 C  C     . LEU A 1 4265 ? 174.383 154.873 132.362 1.00 8.43   ? 4265 LEU A C     1 
ATOM   20113 O  O     . LEU A 1 4265 ? 173.905 153.850 131.854 1.00 9.86   ? 4265 LEU A O     1 
ATOM   20114 C  CB    . LEU A 1 4265 ? 173.328 155.861 134.416 1.00 7.22   ? 4265 LEU A CB    1 
ATOM   20115 C  CG    . LEU A 1 4265 ? 171.916 155.344 134.142 1.00 7.47   ? 4265 LEU A CG    1 
ATOM   20116 C  CD1   . LEU A 1 4265 ? 171.553 154.227 135.105 1.00 5.94   ? 4265 LEU A CD1   1 
ATOM   20117 C  CD2   . LEU A 1 4265 ? 170.918 156.476 134.236 1.00 9.37   ? 4265 LEU A CD2   1 
ATOM   20118 N  N     . ASN A 1 4266 ? 174.830 155.894 131.626 1.00 10.07  ? 4266 ASN A N     1 
ATOM   20119 C  CA    . ASN A 1 4266 ? 174.854 155.813 130.169 1.00 9.72   ? 4266 ASN A CA    1 
ATOM   20120 C  C     . ASN A 1 4266 ? 175.805 154.722 129.697 1.00 9.42   ? 4266 ASN A C     1 
ATOM   20121 O  O     . ASN A 1 4266 ? 175.503 153.993 128.747 1.00 10.97  ? 4266 ASN A O     1 
ATOM   20122 C  CB    . ASN A 1 4266 ? 175.252 157.164 129.577 1.00 10.17  ? 4266 ASN A CB    1 
ATOM   20123 C  CG    . ASN A 1 4266 ? 174.240 158.251 129.875 1.00 10.76  ? 4266 ASN A CG    1 
ATOM   20124 O  OD1   . ASN A 1 4266 ? 173.169 157.986 130.418 1.00 10.72  ? 4266 ASN A OD1   1 
ATOM   20125 N  ND2   . ASN A 1 4266 ? 174.579 159.486 129.526 1.00 13.16  ? 4266 ASN A ND2   1 
ATOM   20126 N  N     . THR A 1 4267 ? 176.976 154.624 130.331 1.00 12.26  ? 4267 THR A N     1 
ATOM   20127 C  CA    . THR A 1 4267 ? 177.858 153.472 130.168 1.00 11.89  ? 4267 THR A CA    1 
ATOM   20128 C  C     . THR A 1 4267 ? 177.085 152.165 130.185 1.00 13.64  ? 4267 THR A C     1 
ATOM   20129 O  O     . THR A 1 4267 ? 177.097 151.406 129.207 1.00 14.07  ? 4267 THR A O     1 
ATOM   20130 C  CB    . THR A 1 4267 ? 178.901 153.473 131.289 1.00 15.43  ? 4267 THR A CB    1 
ATOM   20131 O  OG1   . THR A 1 4267 ? 179.722 154.648 131.214 1.00 18.92  ? 4267 THR A OG1   1 
ATOM   20132 C  CG2   . THR A 1 4267 ? 179.703 152.179 131.347 1.00 18.58  ? 4267 THR A CG2   1 
ATOM   20133 N  N     . PHE A 1 4268 ? 176.414 151.886 131.300 1.00 12.77  ? 4268 PHE A N     1 
ATOM   20134 C  CA    . PHE A 1 4268 ? 175.776 150.585 131.463 1.00 10.73  ? 4268 PHE A CA    1 
ATOM   20135 C  C     . PHE A 1 4268 ? 174.658 150.387 130.448 1.00 10.26  ? 4268 PHE A C     1 
ATOM   20136 O  O     . PHE A 1 4268 ? 174.517 149.301 129.872 1.00 11.64  ? 4268 PHE A O     1 
ATOM   20137 C  CB    . PHE A 1 4268 ? 175.260 150.441 132.892 1.00 10.32  ? 4268 PHE A CB    1 
ATOM   20138 C  CG    . PHE A 1 4268 ? 176.289 149.914 133.843 1.00 11.84  ? 4268 PHE A CG    1 
ATOM   20139 C  CD1   . PHE A 1 4268 ? 177.043 148.803 133.520 1.00 14.23  ? 4268 PHE A CD1   1 
ATOM   20140 C  CD2   . PHE A 1 4268 ? 176.526 150.551 135.047 1.00 15.77  ? 4268 PHE A CD2   1 
ATOM   20141 C  CE1   . PHE A 1 4268 ? 178.000 148.323 134.389 1.00 20.84  ? 4268 PHE A CE1   1 
ATOM   20142 C  CE2   . PHE A 1 4268 ? 177.481 150.077 135.918 1.00 15.32  ? 4268 PHE A CE2   1 
ATOM   20143 C  CZ    . PHE A 1 4268 ? 178.219 148.962 135.589 1.00 17.20  ? 4268 PHE A CZ    1 
ATOM   20144 N  N     . LEU A 1 4269 ? 173.866 151.433 130.199 1.00 11.80  ? 4269 LEU A N     1 
ATOM   20145 C  CA    . LEU A 1 4269 ? 172.736 151.298 129.285 1.00 11.00  ? 4269 LEU A CA    1 
ATOM   20146 C  C     . LEU A 1 4269 ? 173.193 151.065 127.850 1.00 10.22  ? 4269 LEU A C     1 
ATOM   20147 O  O     . LEU A 1 4269 ? 172.621 150.230 127.142 1.00 13.99  ? 4269 LEU A O     1 
ATOM   20148 C  CB    . LEU A 1 4269 ? 171.841 152.531 129.376 1.00 9.27   ? 4269 LEU A CB    1 
ATOM   20149 C  CG    . LEU A 1 4269 ? 170.865 152.486 130.551 1.00 8.05   ? 4269 LEU A CG    1 
ATOM   20150 C  CD1   . LEU A 1 4269 ? 170.423 153.881 130.936 1.00 7.02   ? 4269 LEU A CD1   1 
ATOM   20151 C  CD2   . LEU A 1 4269 ? 169.672 151.612 130.216 1.00 8.19   ? 4269 LEU A CD2   1 
ATOM   20152 N  N     . GLU A 1 4270 ? 174.216 151.794 127.397 1.00 10.85  ? 4270 GLU A N     1 
ATOM   20153 C  CA    . GLU A 1 4270 ? 174.727 151.579 126.048 1.00 11.60  ? 4270 GLU A CA    1 
ATOM   20154 C  C     . GLU A 1 4270 ? 175.400 150.220 125.923 1.00 12.98  ? 4270 GLU A C     1 
ATOM   20155 O  O     . GLU A 1 4270 ? 175.299 149.567 124.879 1.00 12.54  ? 4270 GLU A O     1 
ATOM   20156 C  CB    . GLU A 1 4270 ? 175.698 152.694 125.662 1.00 10.79  ? 4270 GLU A CB    1 
ATOM   20157 C  CG    . GLU A 1 4270 ? 175.087 154.085 125.650 1.00 17.91  ? 4270 GLU A CG    1 
ATOM   20158 C  CD    . GLU A 1 4270 ? 174.364 154.392 124.355 1.00 30.10  ? 4270 GLU A CD    1 
ATOM   20159 O  OE1   . GLU A 1 4270 ? 174.591 153.672 123.360 1.00 30.78  ? 4270 GLU A OE1   1 
ATOM   20160 O  OE2   . GLU A 1 4270 ? 173.570 155.356 124.331 1.00 33.33  ? 4270 GLU A OE2   1 
ATOM   20161 N  N     . ARG A 1 4271 ? 176.097 149.777 126.973 1.00 17.47  ? 4271 ARG A N     1 
ATOM   20162 C  CA    . ARG A 1 4271 ? 176.789 148.496 126.900 1.00 12.65  ? 4271 ARG A CA    1 
ATOM   20163 C  C     . ARG A 1 4271 ? 175.810 147.329 126.881 1.00 13.23  ? 4271 ARG A C     1 
ATOM   20164 O  O     . ARG A 1 4271 ? 176.047 146.327 126.197 1.00 17.00  ? 4271 ARG A O     1 
ATOM   20165 C  CB    . ARG A 1 4271 ? 177.762 148.362 128.069 1.00 15.45  ? 4271 ARG A CB    1 
ATOM   20166 C  CG    . ARG A 1 4271 ? 179.032 147.606 127.733 1.00 22.94  ? 4271 ARG A CG    1 
ATOM   20167 C  CD    . ARG A 1 4271 ? 179.988 147.598 128.911 1.00 29.58  ? 4271 ARG A CD    1 
ATOM   20168 N  NE    . ARG A 1 4271 ? 179.284 147.445 130.179 1.00 31.95  ? 4271 ARG A NE    1 
ATOM   20169 C  CZ    . ARG A 1 4271 ? 178.800 146.299 130.635 1.00 24.84  ? 4271 ARG A CZ    1 
ATOM   20170 N  NH1   . ARG A 1 4271 ? 178.924 145.174 129.948 1.00 18.57  ? 4271 ARG A NH1   1 
ATOM   20171 N  NH2   . ARG A 1 4271 ? 178.173 146.280 131.806 1.00 24.87  ? 4271 ARG A NH2   1 
ATOM   20172 N  N     . LEU A 1 4272 ? 174.706 147.437 127.619 1.00 11.71  ? 4272 LEU A N     1 
ATOM   20173 C  CA    . LEU A 1 4272 ? 173.802 146.302 127.768 1.00 9.22   ? 4272 LEU A CA    1 
ATOM   20174 C  C     . LEU A 1 4272 ? 172.686 146.286 126.727 1.00 10.21  ? 4272 LEU A C     1 
ATOM   20175 O  O     . LEU A 1 4272 ? 172.390 145.234 126.153 1.00 12.12  ? 4272 LEU A O     1 
ATOM   20176 C  CB    . LEU A 1 4272 ? 173.205 146.295 129.178 1.00 8.74   ? 4272 LEU A CB    1 
ATOM   20177 C  CG    . LEU A 1 4272 ? 174.121 145.755 130.276 1.00 8.83   ? 4272 LEU A CG    1 
ATOM   20178 C  CD1   . LEU A 1 4272 ? 173.378 145.667 131.595 1.00 8.19   ? 4272 LEU A CD1   1 
ATOM   20179 C  CD2   . LEU A 1 4272 ? 174.687 144.402 129.881 1.00 11.34  ? 4272 LEU A CD2   1 
ATOM   20180 N  N     . PHE A 1 4273 ? 172.054 147.431 126.474 1.00 13.04  ? 4273 PHE A N     1 
ATOM   20181 C  CA    . PHE A 1 4273 ? 170.863 147.484 125.625 1.00 12.99  ? 4273 PHE A CA    1 
ATOM   20182 C  C     . PHE A 1 4273 ? 171.281 147.799 124.194 1.00 15.46  ? 4273 PHE A C     1 
ATOM   20183 O  O     . PHE A 1 4273 ? 171.431 148.958 123.805 1.00 14.71  ? 4273 PHE A O     1 
ATOM   20184 C  CB    . PHE A 1 4273 ? 169.870 148.505 126.163 1.00 9.15   ? 4273 PHE A CB    1 
ATOM   20185 C  CG    . PHE A 1 4273 ? 169.190 148.074 127.430 1.00 12.89  ? 4273 PHE A CG    1 
ATOM   20186 C  CD1   . PHE A 1 4273 ? 169.796 148.272 128.658 1.00 14.67  ? 4273 PHE A CD1   1 
ATOM   20187 C  CD2   . PHE A 1 4273 ? 167.952 147.457 127.392 1.00 14.69  ? 4273 PHE A CD2   1 
ATOM   20188 C  CE1   . PHE A 1 4273 ? 169.176 147.873 129.824 1.00 12.29  ? 4273 PHE A CE1   1 
ATOM   20189 C  CE2   . PHE A 1 4273 ? 167.328 147.055 128.556 1.00 10.73  ? 4273 PHE A CE2   1 
ATOM   20190 C  CZ    . PHE A 1 4273 ? 167.941 147.264 129.773 1.00 7.99   ? 4273 PHE A CZ    1 
ATOM   20191 N  N     . THR A 1 4274 ? 171.461 146.749 123.399 1.00 16.34  ? 4274 THR A N     1 
ATOM   20192 C  CA    . THR A 1 4274 ? 171.842 146.889 122.000 1.00 14.75  ? 4274 THR A CA    1 
ATOM   20193 C  C     . THR A 1 4274 ? 171.483 145.601 121.274 1.00 17.55  ? 4274 THR A C     1 
ATOM   20194 O  O     . THR A 1 4274 ? 171.158 144.586 121.893 1.00 22.11  ? 4274 THR A O     1 
ATOM   20195 C  CB    . THR A 1 4274 ? 173.334 147.203 121.849 1.00 17.26  ? 4274 THR A CB    1 
ATOM   20196 O  OG1   . THR A 1 4274 ? 173.676 147.249 120.459 1.00 23.26  ? 4274 THR A OG1   1 
ATOM   20197 C  CG2   . THR A 1 4274 ? 174.173 146.140 122.538 1.00 14.85  ? 4274 THR A CG2   1 
ATOM   20198 N  N     . THR A 1 4275 ? 171.535 145.661 119.941 1.00 21.80  ? 4275 THR A N     1 
ATOM   20199 C  CA    . THR A 1 4275 ? 171.293 144.466 119.139 1.00 22.11  ? 4275 THR A CA    1 
ATOM   20200 C  C     . THR A 1 4275 ? 172.330 143.386 119.419 1.00 21.70  ? 4275 THR A C     1 
ATOM   20201 O  O     . THR A 1 4275 ? 172.021 142.191 119.344 1.00 22.45  ? 4275 THR A O     1 
ATOM   20202 C  CB    . THR A 1 4275 ? 171.287 144.818 117.651 1.00 20.36  ? 4275 THR A CB    1 
ATOM   20203 O  OG1   . THR A 1 4275 ? 172.622 145.106 117.221 1.00 29.96  ? 4275 THR A OG1   1 
ATOM   20204 C  CG2   . THR A 1 4275 ? 170.416 146.034 117.397 1.00 23.02  ? 4275 THR A CG2   1 
ATOM   20205 N  N     . ARG A 1 4276 ? 173.558 143.785 119.763 1.00 19.62  ? 4276 ARG A N     1 
ATOM   20206 C  CA    . ARG A 1 4276 ? 174.612 142.814 120.028 1.00 25.27  ? 4276 ARG A CA    1 
ATOM   20207 C  C     . ARG A 1 4276 ? 174.297 141.939 121.230 1.00 26.91  ? 4276 ARG A C     1 
ATOM   20208 O  O     . ARG A 1 4276 ? 174.913 140.880 121.392 1.00 29.35  ? 4276 ARG A O     1 
ATOM   20209 C  CB    . ARG A 1 4276 ? 175.948 143.530 120.240 1.00 23.55  ? 4276 ARG A CB    1 
ATOM   20210 C  CG    . ARG A 1 4276 ? 176.442 144.315 119.034 1.00 30.21  ? 4276 ARG A CG    1 
ATOM   20211 C  CD    . ARG A 1 4276 ? 176.999 143.408 117.941 1.00 41.21  ? 4276 ARG A CD    1 
ATOM   20212 N  NE    . ARG A 1 4276 ? 175.948 142.708 117.212 1.00 43.78  ? 4276 ARG A NE    1 
ATOM   20213 C  CZ    . ARG A 1 4276 ? 175.193 143.258 116.271 1.00 42.71  ? 4276 ARG A CZ    1 
ATOM   20214 N  NH1   . ARG A 1 4276 ? 175.360 144.516 115.898 1.00 45.16  ? 4276 ARG A NH1   1 
ATOM   20215 N  NH2   . ARG A 1 4276 ? 174.245 142.528 115.692 1.00 38.95  ? 4276 ARG A NH2   1 
ATOM   20216 N  N     . SER A 1 4277 ? 173.349 142.352 122.072 1.00 23.66  ? 4277 SER A N     1 
ATOM   20217 C  CA    . SER A 1 4277 ? 172.918 141.528 123.190 1.00 20.36  ? 4277 SER A CA    1 
ATOM   20218 C  C     . SER A 1 4277 ? 172.172 140.280 122.745 1.00 23.28  ? 4277 SER A C     1 
ATOM   20219 O  O     . SER A 1 4277 ? 171.996 139.365 123.555 1.00 29.53  ? 4277 SER A O     1 
ATOM   20220 C  CB    . SER A 1 4277 ? 172.035 142.347 124.131 1.00 20.17  ? 4277 SER A CB    1 
ATOM   20221 O  OG    . SER A 1 4277 ? 172.788 143.344 124.799 1.00 25.60  ? 4277 SER A OG    1 
ATOM   20222 N  N     . PHE A 1 4278 ? 171.730 140.219 121.491 1.00 23.23  ? 4278 PHE A N     1 
ATOM   20223 C  CA    . PHE A 1 4278 ? 171.031 139.050 120.978 1.00 21.76  ? 4278 PHE A CA    1 
ATOM   20224 C  C     . PHE A 1 4278 ? 171.954 138.071 120.267 1.00 32.43  ? 4278 PHE A C     1 
ATOM   20225 O  O     . PHE A 1 4278 ? 171.475 137.069 119.726 1.00 36.19  ? 4278 PHE A O     1 
ATOM   20226 C  CB    . PHE A 1 4278 ? 169.902 139.483 120.041 1.00 21.80  ? 4278 PHE A CB    1 
ATOM   20227 C  CG    . PHE A 1 4278 ? 168.638 139.845 120.757 1.00 23.71  ? 4278 PHE A CG    1 
ATOM   20228 C  CD1   . PHE A 1 4278 ? 168.533 141.044 121.440 1.00 22.28  ? 4278 PHE A CD1   1 
ATOM   20229 C  CD2   . PHE A 1 4278 ? 167.559 138.982 120.761 1.00 20.74  ? 4278 PHE A CD2   1 
ATOM   20230 C  CE1   . PHE A 1 4278 ? 167.375 141.376 122.108 1.00 16.71  ? 4278 PHE A CE1   1 
ATOM   20231 C  CE2   . PHE A 1 4278 ? 166.400 139.310 121.428 1.00 17.83  ? 4278 PHE A CE2   1 
ATOM   20232 C  CZ    . PHE A 1 4278 ? 166.307 140.508 122.102 1.00 17.35  ? 4278 PHE A CZ    1 
ATOM   20233 N  N     . ASP A 1 4279 ? 173.256 138.334 120.255 1.00 34.10  ? 4279 ASP A N     1 
ATOM   20234 C  CA    . ASP A 1 4279 ? 174.214 137.415 119.668 1.00 34.47  ? 4279 ASP A CA    1 
ATOM   20235 C  C     . ASP A 1 4279 ? 174.643 136.368 120.693 1.00 35.72  ? 4279 ASP A C     1 
ATOM   20236 O  O     . ASP A 1 4279 ? 174.534 136.565 121.906 1.00 34.03  ? 4279 ASP A O     1 
ATOM   20237 C  CB    . ASP A 1 4279 ? 175.431 138.177 119.146 1.00 38.96  ? 4279 ASP A CB    1 
ATOM   20238 C  CG    . ASP A 1 4279 ? 175.066 139.196 118.085 1.00 43.99  ? 4279 ASP A CG    1 
ATOM   20239 O  OD1   . ASP A 1 4279 ? 173.884 139.237 117.683 1.00 39.79  ? 4279 ASP A OD1   1 
ATOM   20240 O  OD2   . ASP A 1 4279 ? 175.957 139.958 117.655 1.00 43.71  ? 4279 ASP A OD2   1 
ATOM   20241 N  N     . SER A 1 4280 ? 175.135 135.237 120.187 1.00 39.43  ? 4280 SER A N     1 
ATOM   20242 C  CA    . SER A 1 4280 ? 175.556 134.147 121.059 1.00 42.76  ? 4280 SER A CA    1 
ATOM   20243 C  C     . SER A 1 4280 ? 176.902 134.407 121.720 1.00 38.13  ? 4280 SER A C     1 
ATOM   20244 O  O     . SER A 1 4280 ? 177.242 133.723 122.691 1.00 34.60  ? 4280 SER A O     1 
ATOM   20245 C  CB    . SER A 1 4280 ? 175.612 132.836 120.273 1.00 44.66  ? 4280 SER A CB    1 
ATOM   20246 O  OG    . SER A 1 4280 ? 176.360 132.987 119.079 1.00 46.77  ? 4280 SER A OG    1 
ATOM   20247 N  N     . GLU A 1 4281 ? 177.669 135.374 121.223 1.00 37.82  ? 4281 GLU A N     1 
ATOM   20248 C  CA    . GLU A 1 4281 ? 178.977 135.706 121.768 1.00 39.18  ? 4281 GLU A CA    1 
ATOM   20249 C  C     . GLU A 1 4281 ? 178.934 136.885 122.732 1.00 41.02  ? 4281 GLU A C     1 
ATOM   20250 O  O     . GLU A 1 4281 ? 179.991 137.364 123.155 1.00 44.91  ? 4281 GLU A O     1 
ATOM   20251 C  CB    . GLU A 1 4281 ? 179.958 135.991 120.627 1.00 52.62  ? 4281 GLU A CB    1 
ATOM   20252 C  CG    . GLU A 1 4281 ? 179.498 137.078 119.663 1.00 60.07  ? 4281 GLU A CG    1 
ATOM   20253 C  CD    . GLU A 1 4281 ? 179.957 138.466 120.069 1.00 65.30  ? 4281 GLU A CD    1 
ATOM   20254 O  OE1   . GLU A 1 4281 ? 180.965 138.574 120.798 1.00 67.36  ? 4281 GLU A OE1   1 
ATOM   20255 O  OE2   . GLU A 1 4281 ? 179.305 139.451 119.662 1.00 59.19  ? 4281 GLU A OE2   1 
ATOM   20256 N  N     . PHE A 1 4282 ? 177.744 137.361 123.086 1.00 37.41  ? 4282 PHE A N     1 
ATOM   20257 C  CA    . PHE A 1 4282 ? 177.626 138.518 123.963 1.00 30.29  ? 4282 PHE A CA    1 
ATOM   20258 C  C     . PHE A 1 4282 ? 178.127 138.195 125.365 1.00 28.16  ? 4282 PHE A C     1 
ATOM   20259 O  O     . PHE A 1 4282 ? 177.880 137.109 125.898 1.00 30.68  ? 4282 PHE A O     1 
ATOM   20260 C  CB    . PHE A 1 4282 ? 176.176 138.992 124.026 1.00 25.84  ? 4282 PHE A CB    1 
ATOM   20261 C  CG    . PHE A 1 4282 ? 176.003 140.316 124.709 1.00 24.30  ? 4282 PHE A CG    1 
ATOM   20262 C  CD1   . PHE A 1 4282 ? 176.512 141.471 124.144 1.00 18.18  ? 4282 PHE A CD1   1 
ATOM   20263 C  CD2   . PHE A 1 4282 ? 175.335 140.405 125.917 1.00 21.08  ? 4282 PHE A CD2   1 
ATOM   20264 C  CE1   . PHE A 1 4282 ? 176.356 142.689 124.770 1.00 18.11  ? 4282 PHE A CE1   1 
ATOM   20265 C  CE2   . PHE A 1 4282 ? 175.177 141.620 126.548 1.00 18.01  ? 4282 PHE A CE2   1 
ATOM   20266 C  CZ    . PHE A 1 4282 ? 175.687 142.764 125.973 1.00 20.67  ? 4282 PHE A CZ    1 
ATOM   20267 N  N     . LYS A 1 4283 ? 178.835 139.148 125.962 1.00 24.10  ? 4283 LYS A N     1 
ATOM   20268 C  CA    . LYS A 1 4283 ? 179.353 139.025 127.318 1.00 22.80  ? 4283 LYS A CA    1 
ATOM   20269 C  C     . LYS A 1 4283 ? 178.649 140.038 128.210 1.00 19.96  ? 4283 LYS A C     1 
ATOM   20270 O  O     . LYS A 1 4283 ? 178.667 141.240 127.923 1.00 23.84  ? 4283 LYS A O     1 
ATOM   20271 C  CB    . LYS A 1 4283 ? 180.865 139.248 127.351 1.00 25.35  ? 4283 LYS A CB    1 
ATOM   20272 C  CG    . LYS A 1 4283 ? 181.644 138.423 126.345 1.00 32.46  ? 4283 LYS A CG    1 
ATOM   20273 C  CD    . LYS A 1 4283 ? 183.138 138.510 126.613 1.00 30.62  ? 4283 LYS A CD    1 
ATOM   20274 C  CE    . LYS A 1 4283 ? 183.941 137.897 125.479 1.00 29.17  ? 4283 LYS A CE    1 
ATOM   20275 N  NZ    . LYS A 1 4283 ? 183.934 136.411 125.533 1.00 31.34  ? 4283 LYS A NZ    1 
ATOM   20276 N  N     . LEU A 1 4284 ? 178.028 139.553 129.287 1.00 17.05  ? 4284 LEU A N     1 
ATOM   20277 C  CA    . LEU A 1 4284 ? 177.411 140.461 130.248 1.00 17.89  ? 4284 LEU A CA    1 
ATOM   20278 C  C     . LEU A 1 4284 ? 178.469 141.218 131.040 1.00 17.26  ? 4284 LEU A C     1 
ATOM   20279 O  O     . LEU A 1 4284 ? 178.316 142.415 131.311 1.00 15.26  ? 4284 LEU A O     1 
ATOM   20280 C  CB    . LEU A 1 4284 ? 176.488 139.686 131.187 1.00 10.08  ? 4284 LEU A CB    1 
ATOM   20281 C  CG    . LEU A 1 4284 ? 175.100 139.369 130.633 1.00 9.90   ? 4284 LEU A CG    1 
ATOM   20282 C  CD1   . LEU A 1 4284 ? 174.386 138.369 131.525 1.00 13.07  ? 4284 LEU A CD1   1 
ATOM   20283 C  CD2   . LEU A 1 4284 ? 174.281 140.636 130.474 1.00 9.11   ? 4284 LEU A CD2   1 
ATOM   20284 N  N     . ALA A 1 4285 ? 179.543 140.534 131.422 1.00 18.76  ? 4285 ALA A N     1 
ATOM   20285 C  CA    . ALA A 1 4285 ? 180.671 141.145 132.105 1.00 19.83  ? 4285 ALA A CA    1 
ATOM   20286 C  C     . ALA A 1 4285 ? 181.949 140.518 131.572 1.00 31.12  ? 4285 ALA A C     1 
ATOM   20287 O  O     . ALA A 1 4285 ? 181.925 139.462 130.938 1.00 32.72  ? 4285 ALA A O     1 
ATOM   20288 C  CB    . ALA A 1 4285 ? 180.577 140.974 133.626 1.00 17.47  ? 4285 ALA A CB    1 
ATOM   20289 N  N     . CYS A 1 4286 ? 183.071 141.184 131.826 1.00 41.54  ? 4286 CYS A N     1 
ATOM   20290 C  CA    . CYS A 1 4286 ? 184.367 140.734 131.342 1.00 43.90  ? 4286 CYS A CA    1 
ATOM   20291 C  C     . CYS A 1 4286 ? 185.358 140.639 132.492 1.00 52.66  ? 4286 CYS A C     1 
ATOM   20292 O  O     . CYS A 1 4286 ? 185.264 141.382 133.475 1.00 50.78  ? 4286 CYS A O     1 
ATOM   20293 C  CB    . CYS A 1 4286 ? 184.915 141.675 130.261 1.00 42.48  ? 4286 CYS A CB    1 
ATOM   20294 S  SG    . CYS A 1 4286 ? 183.740 142.072 128.946 1.00 64.09  ? 4286 CYS A SG    1 
ATOM   20295 N  N     . LYS A 1 4287 ? 186.310 139.719 132.343 1.00 57.49  ? 4287 LYS A N     1 
ATOM   20296 C  CA    . LYS A 1 4287 ? 187.402 139.467 133.291 1.00 58.11  ? 4287 LYS A CA    1 
ATOM   20297 C  C     . LYS A 1 4287 ? 186.929 139.555 134.744 1.00 55.24  ? 4287 LYS A C     1 
ATOM   20298 O  O     . LYS A 1 4287 ? 187.445 140.319 135.560 1.00 52.14  ? 4287 LYS A O     1 
ATOM   20299 C  CB    . LYS A 1 4287 ? 188.591 140.399 133.028 1.00 61.60  ? 4287 LYS A CB    1 
ATOM   20300 C  CG    . LYS A 1 4287 ? 188.300 141.896 133.038 1.00 55.97  ? 4287 LYS A CG    1 
ATOM   20301 C  CD    . LYS A 1 4287 ? 189.362 142.668 132.274 1.00 61.24  ? 4287 LYS A CD    1 
ATOM   20302 C  CE    . LYS A 1 4287 ? 189.377 142.270 130.806 1.00 59.93  ? 4287 LYS A CE    1 
ATOM   20303 N  NZ    . LYS A 1 4287 ? 190.398 143.028 130.033 1.00 58.18  ? 4287 LYS A NZ    1 
ATOM   20304 N  N     . VAL A 1 4288 ? 185.924 138.736 135.056 1.00 52.35  ? 4288 VAL A N     1 
ATOM   20305 C  CA    . VAL A 1 4288 ? 185.385 138.711 136.412 1.00 45.66  ? 4288 VAL A CA    1 
ATOM   20306 C  C     . VAL A 1 4288 ? 186.413 138.154 137.390 1.00 51.93  ? 4288 VAL A C     1 
ATOM   20307 O  O     . VAL A 1 4288 ? 186.584 138.679 138.496 1.00 55.42  ? 4288 VAL A O     1 
ATOM   20308 C  CB    . VAL A 1 4288 ? 184.062 137.925 136.448 1.00 35.69  ? 4288 VAL A CB    1 
ATOM   20309 C  CG1   . VAL A 1 4288 ? 182.949 138.756 135.834 1.00 32.06  ? 4288 VAL A CG1   1 
ATOM   20310 C  CG2   . VAL A 1 4288 ? 184.200 136.608 135.708 1.00 51.48  ? 4288 VAL A CG2   1 
ATOM   20311 N  N     . ASP A 1 4289 ? 187.111 137.087 137.007 1.00 58.61  ? 4289 ASP A N     1 
ATOM   20312 C  CA    . ASP A 1 4289 ? 188.211 136.562 137.810 1.00 67.86  ? 4289 ASP A CA    1 
ATOM   20313 C  C     . ASP A 1 4289 ? 189.147 135.795 136.890 1.00 79.09  ? 4289 ASP A C     1 
ATOM   20314 O  O     . ASP A 1 4289 ? 188.747 134.794 136.287 1.00 77.99  ? 4289 ASP A O     1 
ATOM   20315 C  CB    . ASP A 1 4289 ? 187.707 135.667 138.949 1.00 65.40  ? 4289 ASP A CB    1 
ATOM   20316 C  CG    . ASP A 1 4289 ? 186.756 134.587 138.473 1.00 73.34  ? 4289 ASP A CG    1 
ATOM   20317 O  OD1   . ASP A 1 4289 ? 186.190 134.730 137.371 1.00 73.44  ? 4289 ASP A OD1   1 
ATOM   20318 O  OD2   . ASP A 1 4289 ? 186.576 133.590 139.204 1.00 77.75  ? 4289 ASP A OD2   1 
ATOM   20319 N  N     . GLY A 1 4290 ? 190.385 136.267 136.777 1.00 80.64  ? 4290 GLY A N     1 
ATOM   20320 C  CA    . GLY A 1 4290 ? 191.334 135.658 135.868 1.00 87.11  ? 4290 GLY A CA    1 
ATOM   20321 C  C     . GLY A 1 4290 ? 191.079 136.050 134.429 1.00 88.22  ? 4290 GLY A C     1 
ATOM   20322 O  O     . GLY A 1 4290 ? 191.308 137.199 134.043 1.00 85.74  ? 4290 GLY A O     1 
ATOM   20323 N  N     . HIS A 1 4291 ? 190.599 135.102 133.623 1.00 90.60  ? 4291 HIS A N     1 
ATOM   20324 C  CA    . HIS A 1 4291 ? 190.310 135.360 132.220 1.00 96.03  ? 4291 HIS A CA    1 
ATOM   20325 C  C     . HIS A 1 4291 ? 188.898 134.983 131.795 1.00 93.72  ? 4291 HIS A C     1 
ATOM   20326 O  O     . HIS A 1 4291 ? 188.505 135.326 130.674 1.00 90.65  ? 4291 HIS A O     1 
ATOM   20327 C  CB    . HIS A 1 4291 ? 191.311 134.619 131.320 1.00 98.30  ? 4291 HIS A CB    1 
ATOM   20328 C  CG    . HIS A 1 4291 ? 191.096 133.139 131.268 1.00 101.26 ? 4291 HIS A CG    1 
ATOM   20329 N  ND1   . HIS A 1 4291 ? 191.470 132.296 132.291 1.00 99.88  ? 4291 HIS A ND1   1 
ATOM   20330 C  CD2   . HIS A 1 4291 ? 190.543 132.352 130.315 1.00 101.14 ? 4291 HIS A CD2   1 
ATOM   20331 C  CE1   . HIS A 1 4291 ? 191.158 131.053 131.971 1.00 98.85  ? 4291 HIS A CE1   1 
ATOM   20332 N  NE2   . HIS A 1 4291 ? 190.595 131.059 130.777 1.00 101.82 ? 4291 HIS A NE2   1 
ATOM   20333 N  N     . LYS A 1 4292 ? 188.128 134.294 132.634 1.00 87.31  ? 4292 LYS A N     1 
ATOM   20334 C  CA    . LYS A 1 4292 ? 186.765 133.944 132.269 1.00 74.88  ? 4292 LYS A CA    1 
ATOM   20335 C  C     . LYS A 1 4292 ? 185.845 135.154 132.411 1.00 64.04  ? 4292 LYS A C     1 
ATOM   20336 O  O     . LYS A 1 4292 ? 186.191 136.167 133.026 1.00 62.82  ? 4292 LYS A O     1 
ATOM   20337 C  CB    . LYS A 1 4292 ? 186.252 132.790 133.129 1.00 71.69  ? 4292 LYS A CB    1 
ATOM   20338 C  CG    . LYS A 1 4292 ? 186.083 133.136 134.595 1.00 70.37  ? 4292 LYS A CG    1 
ATOM   20339 C  CD    . LYS A 1 4292 ? 185.621 131.931 135.396 1.00 75.54  ? 4292 LYS A CD    1 
ATOM   20340 C  CE    . LYS A 1 4292 ? 184.190 131.557 135.049 1.00 74.47  ? 4292 LYS A CE    1 
ATOM   20341 N  NZ    . LYS A 1 4292 ? 183.225 132.612 135.468 1.00 67.97  ? 4292 LYS A NZ    1 
ATOM   20342 N  N     . ASP A 1 4293 ? 184.654 135.037 131.831 1.00 52.56  ? 4293 ASP A N     1 
ATOM   20343 C  CA    . ASP A 1 4293 ? 183.706 136.139 131.818 1.00 45.46  ? 4293 ASP A CA    1 
ATOM   20344 C  C     . ASP A 1 4293 ? 182.287 135.591 131.842 1.00 40.75  ? 4293 ASP A C     1 
ATOM   20345 O  O     . ASP A 1 4293 ? 182.040 134.434 131.492 1.00 49.42  ? 4293 ASP A O     1 
ATOM   20346 C  CB    . ASP A 1 4293 ? 183.922 137.042 130.596 1.00 44.91  ? 4293 ASP A CB    1 
ATOM   20347 C  CG    . ASP A 1 4293 ? 183.993 136.262 129.297 1.00 46.72  ? 4293 ASP A CG    1 
ATOM   20348 O  OD1   . ASP A 1 4293 ? 183.042 135.516 128.987 1.00 45.22  ? 4293 ASP A OD1   1 
ATOM   20349 O  OD2   . ASP A 1 4293 ? 185.010 136.396 128.584 1.00 54.00  ? 4293 ASP A OD2   1 
ATOM   20350 N  N     . ILE A 1 4294 ? 181.356 136.440 132.264 1.00 29.72  ? 4294 ILE A N     1 
ATOM   20351 C  CA    . ILE A 1 4294 ? 179.946 136.071 132.310 1.00 23.86  ? 4294 ILE A CA    1 
ATOM   20352 C  C     . ILE A 1 4294 ? 179.399 136.063 130.889 1.00 22.40  ? 4294 ILE A C     1 
ATOM   20353 O  O     . ILE A 1 4294 ? 179.593 137.021 130.131 1.00 25.69  ? 4294 ILE A O     1 
ATOM   20354 C  CB    . ILE A 1 4294 ? 179.158 137.039 133.205 1.00 24.81  ? 4294 ILE A CB    1 
ATOM   20355 C  CG1   . ILE A 1 4294 ? 179.731 137.048 134.624 1.00 19.19  ? 4294 ILE A CG1   1 
ATOM   20356 C  CG2   . ILE A 1 4294 ? 177.688 136.657 133.236 1.00 19.39  ? 4294 ILE A CG2   1 
ATOM   20357 C  CD1   . ILE A 1 4294 ? 179.670 135.713 135.319 1.00 21.84  ? 4294 ILE A CD1   1 
ATOM   20358 N  N     . GLN A 1 4295 ? 178.717 134.984 130.524 1.00 28.90  ? 4295 GLN A N     1 
ATOM   20359 C  CA    . GLN A 1 4295 ? 178.219 134.796 129.170 1.00 27.23  ? 4295 GLN A CA    1 
ATOM   20360 C  C     . GLN A 1 4295 ? 176.722 135.063 129.100 1.00 25.00  ? 4295 GLN A C     1 
ATOM   20361 O  O     . GLN A 1 4295 ? 175.966 134.681 129.998 1.00 28.32  ? 4295 GLN A O     1 
ATOM   20362 C  CB    . GLN A 1 4295 ? 178.514 133.379 128.673 1.00 31.48  ? 4295 GLN A CB    1 
ATOM   20363 C  CG    . GLN A 1 4295 ? 179.811 133.259 127.897 1.00 36.41  ? 4295 GLN A CG    1 
ATOM   20364 C  CD    . GLN A 1 4295 ? 179.745 133.953 126.553 1.00 40.11  ? 4295 GLN A CD    1 
ATOM   20365 O  OE1   . GLN A 1 4295 ? 180.582 134.798 126.235 1.00 35.87  ? 4295 GLN A OE1   1 
ATOM   20366 N  NE2   . GLN A 1 4295 ? 178.744 133.600 125.755 1.00 31.72  ? 4295 GLN A NE2   1 
ATOM   20367 N  N     . MET A 1 4296 ? 176.306 135.724 128.030 1.00 24.65  ? 4296 MET A N     1 
ATOM   20368 C  CA    . MET A 1 4296 ? 174.889 135.957 127.787 1.00 20.41  ? 4296 MET A CA    1 
ATOM   20369 C  C     . MET A 1 4296 ? 174.197 134.630 127.499 1.00 24.81  ? 4296 MET A C     1 
ATOM   20370 O  O     . MET A 1 4296 ? 174.650 133.880 126.627 1.00 31.05  ? 4296 MET A O     1 
ATOM   20371 C  CB    . MET A 1 4296 ? 174.720 136.910 126.607 1.00 23.77  ? 4296 MET A CB    1 
ATOM   20372 C  CG    . MET A 1 4296 ? 173.310 137.415 126.356 1.00 26.03  ? 4296 MET A CG    1 
ATOM   20373 S  SD    . MET A 1 4296 ? 172.524 138.162 127.790 1.00 25.93  ? 4296 MET A SD    1 
ATOM   20374 C  CE    . MET A 1 4296 ? 170.815 138.120 127.269 1.00 20.02  ? 4296 MET A CE    1 
ATOM   20375 N  N     . PRO A 1 4297 ? 173.117 134.297 128.205 1.00 24.04  ? 4297 PRO A N     1 
ATOM   20376 C  CA    . PRO A 1 4297 ? 172.399 133.054 127.904 1.00 25.12  ? 4297 PRO A CA    1 
ATOM   20377 C  C     . PRO A 1 4297 ? 171.860 133.052 126.482 1.00 29.46  ? 4297 PRO A C     1 
ATOM   20378 O  O     . PRO A 1 4297 ? 171.443 134.081 125.947 1.00 33.16  ? 4297 PRO A O     1 
ATOM   20379 C  CB    . PRO A 1 4297 ? 171.261 133.036 128.933 1.00 19.00  ? 4297 PRO A CB    1 
ATOM   20380 C  CG    . PRO A 1 4297 ? 171.648 134.024 129.970 1.00 18.44  ? 4297 PRO A CG    1 
ATOM   20381 C  CD    . PRO A 1 4297 ? 172.498 135.046 129.309 1.00 18.67  ? 4297 PRO A CD    1 
ATOM   20382 N  N     . ASP A 1 4298 ? 171.874 131.872 125.870 1.00 30.53  ? 4298 ASP A N     1 
ATOM   20383 C  CA    . ASP A 1 4298 ? 171.407 131.695 124.503 1.00 36.41  ? 4298 ASP A CA    1 
ATOM   20384 C  C     . ASP A 1 4298 ? 169.911 131.430 124.411 1.00 40.82  ? 4298 ASP A C     1 
ATOM   20385 O  O     . ASP A 1 4298 ? 169.391 131.272 123.302 1.00 41.00  ? 4298 ASP A O     1 
ATOM   20386 C  CB    . ASP A 1 4298 ? 172.181 130.557 123.827 1.00 38.97  ? 4298 ASP A CB    1 
ATOM   20387 C  CG    . ASP A 1 4298 ? 171.964 129.210 124.503 1.00 52.32  ? 4298 ASP A CG    1 
ATOM   20388 O  OD1   . ASP A 1 4298 ? 171.247 129.148 125.525 1.00 51.11  ? 4298 ASP A OD1   1 
ATOM   20389 O  OD2   . ASP A 1 4298 ? 172.510 128.205 124.003 1.00 57.92  ? 4298 ASP A OD2   1 
ATOM   20390 N  N     . GLY A 1 4299 ? 169.211 131.383 125.542 1.00 34.16  ? 4299 GLY A N     1 
ATOM   20391 C  CA    . GLY A 1 4299 ? 167.816 131.005 125.529 1.00 34.25  ? 4299 GLY A CA    1 
ATOM   20392 C  C     . GLY A 1 4299 ? 166.911 132.086 124.972 1.00 36.44  ? 4299 GLY A C     1 
ATOM   20393 O  O     . GLY A 1 4299 ? 167.295 133.242 124.793 1.00 44.43  ? 4299 GLY A O     1 
ATOM   20394 N  N     . ILE A 1 4300 ? 165.673 131.684 124.689 1.00 26.32  ? 4300 ILE A N     1 
ATOM   20395 C  CA    . ILE A 1 4300 ? 164.642 132.583 124.188 1.00 26.23  ? 4300 ILE A CA    1 
ATOM   20396 C  C     . ILE A 1 4300 ? 163.366 132.524 125.011 1.00 30.17  ? 4300 ILE A C     1 
ATOM   20397 O  O     . ILE A 1 4300 ? 162.371 133.151 124.632 1.00 30.13  ? 4300 ILE A O     1 
ATOM   20398 C  CB    . ILE A 1 4300 ? 164.328 132.309 122.703 1.00 26.94  ? 4300 ILE A CB    1 
ATOM   20399 C  CG1   . ILE A 1 4300 ? 163.783 130.892 122.523 1.00 37.29  ? 4300 ILE A CG1   1 
ATOM   20400 C  CG2   . ILE A 1 4300 ? 165.564 132.523 121.844 1.00 28.38  ? 4300 ILE A CG2   1 
ATOM   20401 C  CD1   . ILE A 1 4300 ? 163.235 130.621 121.141 1.00 40.65  ? 4300 ILE A CD1   1 
ATOM   20402 N  N     . ARG A 1 4301 ? 163.359 131.793 126.122 1.00 32.87  ? 4301 ARG A N     1 
ATOM   20403 C  CA    . ARG A 1 4301 ? 162.191 131.666 126.977 1.00 29.69  ? 4301 ARG A CA    1 
ATOM   20404 C  C     . ARG A 1 4301 ? 162.551 132.040 128.409 1.00 25.08  ? 4301 ARG A C     1 
ATOM   20405 O  O     . ARG A 1 4301 ? 163.710 131.955 128.823 1.00 25.53  ? 4301 ARG A O     1 
ATOM   20406 C  CB    . ARG A 1 4301 ? 161.618 130.245 126.928 1.00 32.53  ? 4301 ARG A CB    1 
ATOM   20407 C  CG    . ARG A 1 4301 ? 160.998 129.879 125.591 1.00 39.93  ? 4301 ARG A CG    1 
ATOM   20408 C  CD    . ARG A 1 4301 ? 160.274 128.547 125.664 1.00 47.18  ? 4301 ARG A CD    1 
ATOM   20409 N  NE    . ARG A 1 4301 ? 161.188 127.447 125.947 1.00 51.71  ? 4301 ARG A NE    1 
ATOM   20410 C  CZ    . ARG A 1 4301 ? 161.842 126.760 125.021 1.00 61.11  ? 4301 ARG A CZ    1 
ATOM   20411 N  NH1   . ARG A 1 4301 ? 161.706 127.032 123.733 1.00 66.42  ? 4301 ARG A NH1   1 
ATOM   20412 N  NH2   . ARG A 1 4301 ? 162.653 125.776 125.396 1.00 59.82  ? 4301 ARG A NH2   1 
ATOM   20413 N  N     . ARG A 1 4302 ? 161.531 132.458 129.163 1.00 22.04  ? 4302 ARG A N     1 
ATOM   20414 C  CA    . ARG A 1 4302 ? 161.755 132.953 130.519 1.00 20.42  ? 4302 ARG A CA    1 
ATOM   20415 C  C     . ARG A 1 4302 ? 162.339 131.875 131.424 1.00 22.66  ? 4302 ARG A C     1 
ATOM   20416 O  O     . ARG A 1 4302 ? 163.254 132.145 132.214 1.00 24.74  ? 4302 ARG A O     1 
ATOM   20417 C  CB    . ARG A 1 4302 ? 160.448 133.482 131.106 1.00 21.76  ? 4302 ARG A CB    1 
ATOM   20418 C  CG    . ARG A 1 4302 ? 160.529 133.779 132.592 1.00 19.75  ? 4302 ARG A CG    1 
ATOM   20419 C  CD    . ARG A 1 4302 ? 159.162 133.743 133.245 1.00 25.02  ? 4302 ARG A CD    1 
ATOM   20420 N  NE    . ARG A 1 4302 ? 159.253 133.880 134.693 1.00 30.56  ? 4302 ARG A NE    1 
ATOM   20421 C  CZ    . ARG A 1 4302 ? 159.598 132.899 135.517 1.00 30.64  ? 4302 ARG A CZ    1 
ATOM   20422 N  NH1   . ARG A 1 4302 ? 159.877 131.686 135.069 1.00 25.22  ? 4302 ARG A NH1   1 
ATOM   20423 N  NH2   . ARG A 1 4302 ? 159.663 133.141 136.823 1.00 21.70  ? 4302 ARG A NH2   1 
ATOM   20424 N  N     . GLU A 1 4303 ? 161.815 130.650 131.333 1.00 24.45  ? 4303 GLU A N     1 
ATOM   20425 C  CA    . GLU A 1 4303 ? 162.279 129.588 132.218 1.00 21.89  ? 4303 GLU A CA    1 
ATOM   20426 C  C     . GLU A 1 4303 ? 163.751 129.280 131.979 1.00 21.46  ? 4303 GLU A C     1 
ATOM   20427 O  O     . GLU A 1 4303 ? 164.482 128.951 132.918 1.00 24.04  ? 4303 GLU A O     1 
ATOM   20428 C  CB    . GLU A 1 4303 ? 161.412 128.337 132.044 1.00 26.42  ? 4303 GLU A CB    1 
ATOM   20429 C  CG    . GLU A 1 4303 ? 161.776 127.444 130.867 1.00 33.60  ? 4303 GLU A CG    1 
ATOM   20430 C  CD    . GLU A 1 4303 ? 161.122 127.880 129.571 1.00 44.36  ? 4303 GLU A CD    1 
ATOM   20431 O  OE1   . GLU A 1 4303 ? 161.497 127.345 128.507 1.00 44.10  ? 4303 GLU A OE1   1 
ATOM   20432 O  OE2   . GLU A 1 4303 ? 160.233 128.756 129.616 1.00 41.09  ? 4303 GLU A OE2   1 
ATOM   20433 N  N     . GLU A 1 4304 ? 164.213 129.419 130.736 1.00 24.20  ? 4304 GLU A N     1 
ATOM   20434 C  CA    . GLU A 1 4304 ? 165.621 129.186 130.440 1.00 24.18  ? 4304 GLU A CA    1 
ATOM   20435 C  C     . GLU A 1 4304 ? 166.504 130.264 131.060 1.00 22.51  ? 4304 GLU A C     1 
ATOM   20436 O  O     . GLU A 1 4304 ? 167.583 129.968 131.585 1.00 24.64  ? 4304 GLU A O     1 
ATOM   20437 C  CB    . GLU A 1 4304 ? 165.818 129.102 128.927 1.00 21.20  ? 4304 GLU A CB    1 
ATOM   20438 C  CG    . GLU A 1 4304 ? 165.152 127.873 128.320 1.00 36.17  ? 4304 GLU A CG    1 
ATOM   20439 C  CD    . GLU A 1 4304 ? 165.316 127.781 126.818 1.00 52.87  ? 4304 GLU A CD    1 
ATOM   20440 O  OE1   . GLU A 1 4304 ? 165.841 128.734 126.214 1.00 49.46  ? 4304 GLU A OE1   1 
ATOM   20441 O  OE2   . GLU A 1 4304 ? 164.921 126.747 126.240 1.00 65.00  ? 4304 GLU A OE2   1 
ATOM   20442 N  N     . PHE A 1 4305 ? 166.055 131.522 131.026 1.00 22.64  ? 4305 PHE A N     1 
ATOM   20443 C  CA    . PHE A 1 4305 ? 166.797 132.587 131.695 1.00 18.27  ? 4305 PHE A CA    1 
ATOM   20444 C  C     . PHE A 1 4305 ? 166.843 132.372 133.203 1.00 18.54  ? 4305 PHE A C     1 
ATOM   20445 O  O     . PHE A 1 4305 ? 167.891 132.566 133.832 1.00 17.50  ? 4305 PHE A O     1 
ATOM   20446 C  CB    . PHE A 1 4305 ? 166.182 133.946 131.364 1.00 14.36  ? 4305 PHE A CB    1 
ATOM   20447 C  CG    . PHE A 1 4305 ? 166.377 134.366 129.938 1.00 15.74  ? 4305 PHE A CG    1 
ATOM   20448 C  CD1   . PHE A 1 4305 ? 167.649 134.468 129.402 1.00 15.56  ? 4305 PHE A CD1   1 
ATOM   20449 C  CD2   . PHE A 1 4305 ? 165.291 134.654 129.130 1.00 18.52  ? 4305 PHE A CD2   1 
ATOM   20450 C  CE1   . PHE A 1 4305 ? 167.834 134.853 128.090 1.00 15.04  ? 4305 PHE A CE1   1 
ATOM   20451 C  CE2   . PHE A 1 4305 ? 165.471 135.036 127.816 1.00 18.17  ? 4305 PHE A CE2   1 
ATOM   20452 C  CZ    . PHE A 1 4305 ? 166.745 135.136 127.296 1.00 16.04  ? 4305 PHE A CZ    1 
ATOM   20453 N  N     . VAL A 1 4306 ? 165.719 131.974 133.803 1.00 17.09  ? 4306 VAL A N     1 
ATOM   20454 C  CA    . VAL A 1 4306 ? 165.708 131.711 135.241 1.00 18.66  ? 4306 VAL A CA    1 
ATOM   20455 C  C     . VAL A 1 4306 ? 166.638 130.551 135.574 1.00 19.81  ? 4306 VAL A C     1 
ATOM   20456 O  O     . VAL A 1 4306 ? 167.364 130.582 136.576 1.00 19.20  ? 4306 VAL A O     1 
ATOM   20457 C  CB    . VAL A 1 4306 ? 164.270 131.448 135.727 1.00 20.52  ? 4306 VAL A CB    1 
ATOM   20458 C  CG1   . VAL A 1 4306 ? 164.267 131.073 137.201 1.00 16.24  ? 4306 VAL A CG1   1 
ATOM   20459 C  CG2   . VAL A 1 4306 ? 163.397 132.667 135.482 1.00 19.24  ? 4306 VAL A CG2   1 
ATOM   20460 N  N     . GLN A 1 4307 ? 166.637 129.514 134.734 1.00 21.88  ? 4307 GLN A N     1 
ATOM   20461 C  CA    . GLN A 1 4307 ? 167.509 128.366 134.947 1.00 20.71  ? 4307 GLN A CA    1 
ATOM   20462 C  C     . GLN A 1 4307 ? 168.977 128.761 134.821 1.00 20.15  ? 4307 GLN A C     1 
ATOM   20463 O  O     . GLN A 1 4307 ? 169.835 128.226 135.532 1.00 24.30  ? 4307 GLN A O     1 
ATOM   20464 C  CB    . GLN A 1 4307 ? 167.129 127.263 133.954 1.00 28.49  ? 4307 GLN A CB    1 
ATOM   20465 C  CG    . GLN A 1 4307 ? 167.797 125.910 134.143 1.00 41.01  ? 4307 GLN A CG    1 
ATOM   20466 C  CD    . GLN A 1 4307 ? 169.144 125.808 133.464 1.00 48.46  ? 4307 GLN A CD    1 
ATOM   20467 O  OE1   . GLN A 1 4307 ? 169.393 126.455 132.447 1.00 50.89  ? 4307 GLN A OE1   1 
ATOM   20468 N  NE2   . GLN A 1 4307 ? 170.009 124.961 134.003 1.00 44.19  ? 4307 GLN A NE2   1 
ATOM   20469 N  N     . TRP A 1 4308 ? 169.285 129.696 133.919 1.00 19.32  ? 4308 TRP A N     1 
ATOM   20470 C  CA    . TRP A 1 4308 ? 170.637 130.243 133.848 1.00 18.24  ? 4308 TRP A CA    1 
ATOM   20471 C  C     . TRP A 1 4308 ? 170.995 131.006 135.118 1.00 13.77  ? 4308 TRP A C     1 
ATOM   20472 O  O     . TRP A 1 4308 ? 172.123 130.908 135.614 1.00 14.16  ? 4308 TRP A O     1 
ATOM   20473 C  CB    . TRP A 1 4308 ? 170.775 131.156 132.630 1.00 15.80  ? 4308 TRP A CB    1 
ATOM   20474 C  CG    . TRP A 1 4308 ? 172.121 131.816 132.520 1.00 16.28  ? 4308 TRP A CG    1 
ATOM   20475 C  CD1   . TRP A 1 4308 ? 173.209 131.348 131.847 1.00 14.54  ? 4308 TRP A CD1   1 
ATOM   20476 C  CD2   . TRP A 1 4308 ? 172.517 133.067 133.101 1.00 16.06  ? 4308 TRP A CD2   1 
ATOM   20477 N  NE1   . TRP A 1 4308 ? 174.257 132.227 131.971 1.00 16.21  ? 4308 TRP A NE1   1 
ATOM   20478 C  CE2   . TRP A 1 4308 ? 173.857 133.290 132.736 1.00 14.18  ? 4308 TRP A CE2   1 
ATOM   20479 C  CE3   . TRP A 1 4308 ? 171.866 134.018 133.892 1.00 12.65  ? 4308 TRP A CE3   1 
ATOM   20480 C  CZ2   . TRP A 1 4308 ? 174.560 134.424 133.135 1.00 12.44  ? 4308 TRP A CZ2   1 
ATOM   20481 C  CZ3   . TRP A 1 4308 ? 172.566 135.141 134.290 1.00 9.32   ? 4308 TRP A CZ3   1 
ATOM   20482 C  CH2   . TRP A 1 4308 ? 173.897 135.335 133.910 1.00 12.03  ? 4308 TRP A CH2   1 
ATOM   20483 N  N     . VAL A 1 4309 ? 170.051 131.788 135.646 1.00 14.01  ? 4309 VAL A N     1 
ATOM   20484 C  CA    . VAL A 1 4309 ? 170.315 132.550 136.864 1.00 12.90  ? 4309 VAL A CA    1 
ATOM   20485 C  C     . VAL A 1 4309 ? 170.566 131.609 138.034 1.00 16.83  ? 4309 VAL A C     1 
ATOM   20486 O  O     . VAL A 1 4309 ? 171.392 131.888 138.912 1.00 20.29  ? 4309 VAL A O     1 
ATOM   20487 C  CB    . VAL A 1 4309 ? 169.153 133.520 137.155 1.00 15.18  ? 4309 VAL A CB    1 
ATOM   20488 C  CG1   . VAL A 1 4309 ? 169.371 134.238 138.479 1.00 7.12   ? 4309 VAL A CG1   1 
ATOM   20489 C  CG2   . VAL A 1 4309 ? 169.007 134.527 136.031 1.00 10.08  ? 4309 VAL A CG2   1 
ATOM   20490 N  N     . GLU A 1 4310 ? 169.862 130.476 138.062 1.00 18.96  ? 4310 GLU A N     1 
ATOM   20491 C  CA    . GLU A 1 4310 ? 170.019 129.530 139.162 1.00 15.09  ? 4310 GLU A CA    1 
ATOM   20492 C  C     . GLU A 1 4310 ? 171.411 128.908 139.190 1.00 17.63  ? 4310 GLU A C     1 
ATOM   20493 O  O     . GLU A 1 4310 ? 171.919 128.583 140.269 1.00 22.45  ? 4310 GLU A O     1 
ATOM   20494 C  CB    . GLU A 1 4310 ? 168.946 128.447 139.072 1.00 16.04  ? 4310 GLU A CB    1 
ATOM   20495 C  CG    . GLU A 1 4310 ? 167.539 128.967 139.314 1.00 21.29  ? 4310 GLU A CG    1 
ATOM   20496 C  CD    . GLU A 1 4310 ? 166.485 127.887 139.200 1.00 38.95  ? 4310 GLU A CD    1 
ATOM   20497 O  OE1   . GLU A 1 4310 ? 166.832 126.752 138.809 1.00 48.55  ? 4310 GLU A OE1   1 
ATOM   20498 O  OE2   . GLU A 1 4310 ? 165.307 128.173 139.500 1.00 36.19  ? 4310 GLU A OE2   1 
ATOM   20499 N  N     . LEU A 1 4311 ? 172.044 128.732 138.030 1.00 17.16  ? 4311 LEU A N     1 
ATOM   20500 C  CA    . LEU A 1 4311 ? 173.373 128.137 137.963 1.00 20.50  ? 4311 LEU A CA    1 
ATOM   20501 C  C     . LEU A 1 4311 ? 174.494 129.165 138.016 1.00 24.16  ? 4311 LEU A C     1 
ATOM   20502 O  O     . LEU A 1 4311 ? 175.586 128.898 137.501 1.00 26.36  ? 4311 LEU A O     1 
ATOM   20503 C  CB    . LEU A 1 4311 ? 173.528 127.289 136.699 1.00 19.70  ? 4311 LEU A CB    1 
ATOM   20504 C  CG    . LEU A 1 4311 ? 172.401 126.387 136.210 1.00 28.68  ? 4311 LEU A CG    1 
ATOM   20505 C  CD1   . LEU A 1 4311 ? 172.929 125.540 135.070 1.00 29.26  ? 4311 LEU A CD1   1 
ATOM   20506 C  CD2   . LEU A 1 4311 ? 171.883 125.510 137.336 1.00 24.77  ? 4311 LEU A CD2   1 
ATOM   20507 N  N     . LEU A 1 4312 ? 174.259 130.328 138.613 1.00 17.14  ? 4312 LEU A N     1 
ATOM   20508 C  CA    . LEU A 1 4312 ? 175.340 131.282 138.779 1.00 18.09  ? 4312 LEU A CA    1 
ATOM   20509 C  C     . LEU A 1 4312 ? 176.371 130.731 139.765 1.00 22.87  ? 4312 LEU A C     1 
ATOM   20510 O  O     . LEU A 1 4312 ? 176.018 130.044 140.727 1.00 28.11  ? 4312 LEU A O     1 
ATOM   20511 C  CB    . LEU A 1 4312 ? 174.804 132.629 139.254 1.00 16.46  ? 4312 LEU A CB    1 
ATOM   20512 C  CG    . LEU A 1 4312 ? 174.296 133.528 138.122 1.00 14.27  ? 4312 LEU A CG    1 
ATOM   20513 C  CD1   . LEU A 1 4312 ? 173.894 134.898 138.638 1.00 12.39  ? 4312 LEU A CD1   1 
ATOM   20514 C  CD2   . LEU A 1 4312 ? 175.340 133.659 137.022 1.00 13.95  ? 4312 LEU A CD2   1 
ATOM   20515 N  N     . PRO A 1 4313 ? 177.657 131.019 139.543 1.00 18.81  ? 4313 PRO A N     1 
ATOM   20516 C  CA    . PRO A 1 4313 ? 178.713 130.310 140.286 1.00 25.21  ? 4313 PRO A CA    1 
ATOM   20517 C  C     . PRO A 1 4313 ? 178.707 130.547 141.787 1.00 33.22  ? 4313 PRO A C     1 
ATOM   20518 O  O     . PRO A 1 4313 ? 179.387 129.807 142.508 1.00 39.15  ? 4313 PRO A O     1 
ATOM   20519 C  CB    . PRO A 1 4313 ? 180.006 130.840 139.648 1.00 24.32  ? 4313 PRO A CB    1 
ATOM   20520 C  CG    . PRO A 1 4313 ? 179.583 131.383 138.318 1.00 27.01  ? 4313 PRO A CG    1 
ATOM   20521 C  CD    . PRO A 1 4313 ? 178.214 131.932 138.534 1.00 21.74  ? 4313 PRO A CD    1 
ATOM   20522 N  N     . ASP A 1 4314 ? 177.972 131.546 142.278 1.00 31.38  ? 4314 ASP A N     1 
ATOM   20523 C  CA    . ASP A 1 4314 ? 177.966 131.903 143.698 1.00 35.06  ? 4314 ASP A CA    1 
ATOM   20524 C  C     . ASP A 1 4314 ? 179.378 132.274 144.155 1.00 35.56  ? 4314 ASP A C     1 
ATOM   20525 O  O     . ASP A 1 4314 ? 179.803 131.992 145.276 1.00 33.86  ? 4314 ASP A O     1 
ATOM   20526 C  CB    . ASP A 1 4314 ? 177.368 130.774 144.548 1.00 40.46  ? 4314 ASP A CB    1 
ATOM   20527 C  CG    . ASP A 1 4314 ? 177.204 131.155 146.010 1.00 58.87  ? 4314 ASP A CG    1 
ATOM   20528 O  OD1   . ASP A 1 4314 ? 176.282 131.938 146.322 1.00 61.11  ? 4314 ASP A OD1   1 
ATOM   20529 O  OD2   . ASP A 1 4314 ? 177.988 130.662 146.848 1.00 59.45  ? 4314 ASP A OD2   1 
ATOM   20530 N  N     . THR A 1 4315 ? 180.115 132.917 143.252 1.00 33.81  ? 4315 THR A N     1 
ATOM   20531 C  CA    . THR A 1 4315 ? 181.445 133.447 143.523 1.00 20.25  ? 4315 THR A CA    1 
ATOM   20532 C  C     . THR A 1 4315 ? 181.507 134.906 143.104 1.00 21.20  ? 4315 THR A C     1 
ATOM   20533 O  O     . THR A 1 4315 ? 182.454 135.344 142.443 1.00 28.32  ? 4315 THR A O     1 
ATOM   20534 C  CB    . THR A 1 4315 ? 182.529 132.638 142.808 1.00 25.87  ? 4315 THR A CB    1 
ATOM   20535 O  OG1   . THR A 1 4315 ? 182.409 132.820 141.391 1.00 36.02  ? 4315 THR A OG1   1 
ATOM   20536 C  CG2   . THR A 1 4315 ? 182.406 131.158 143.133 1.00 28.88  ? 4315 THR A CG2   1 
ATOM   20537 N  N     . GLN A 1 4316 ? 180.486 135.674 143.476 1.00 18.13  ? 4316 GLN A N     1 
ATOM   20538 C  CA    . GLN A 1 4316 ? 180.371 137.049 143.012 1.00 13.31  ? 4316 GLN A CA    1 
ATOM   20539 C  C     . GLN A 1 4316 ? 181.484 137.918 143.580 1.00 14.53  ? 4316 GLN A C     1 
ATOM   20540 O  O     . GLN A 1 4316 ? 181.815 137.846 144.766 1.00 18.31  ? 4316 GLN A O     1 
ATOM   20541 C  CB    . GLN A 1 4316 ? 179.013 137.630 143.396 1.00 13.03  ? 4316 GLN A CB    1 
ATOM   20542 C  CG    . GLN A 1 4316 ? 178.699 138.946 142.710 1.00 13.15  ? 4316 GLN A CG    1 
ATOM   20543 C  CD    . GLN A 1 4316 ? 177.630 139.738 143.428 1.00 15.15  ? 4316 GLN A CD    1 
ATOM   20544 O  OE1   . GLN A 1 4316 ? 176.488 139.297 143.544 1.00 16.94  ? 4316 GLN A OE1   1 
ATOM   20545 N  NE2   . GLN A 1 4316 ? 177.995 140.916 143.918 1.00 15.36  ? 4316 GLN A NE2   1 
ATOM   20546 N  N     . THR A 1 4317 ? 182.052 138.745 142.718 1.00 16.11  ? 4317 THR A N     1 
ATOM   20547 C  CA    . THR A 1 4317 ? 183.093 139.704 143.041 1.00 13.70  ? 4317 THR A CA    1 
ATOM   20548 C  C     . THR A 1 4317 ? 182.687 141.048 142.465 1.00 13.55  ? 4317 THR A C     1 
ATOM   20549 O  O     . THR A 1 4317 ? 181.847 141.112 141.561 1.00 14.79  ? 4317 THR A O     1 
ATOM   20550 C  CB    . THR A 1 4317 ? 184.450 139.271 142.464 1.00 14.04  ? 4317 THR A CB    1 
ATOM   20551 O  OG1   . THR A 1 4317 ? 184.298 138.938 141.080 1.00 17.08  ? 4317 THR A OG1   1 
ATOM   20552 C  CG2   . THR A 1 4317 ? 184.989 138.066 143.212 1.00 14.81  ? 4317 THR A CG2   1 
ATOM   20553 N  N     . PRO A 1 4318 ? 183.248 142.147 142.975 1.00 16.30  ? 4318 PRO A N     1 
ATOM   20554 C  CA    . PRO A 1 4318 ? 182.929 143.460 142.393 1.00 11.85  ? 4318 PRO A CA    1 
ATOM   20555 C  C     . PRO A 1 4318 ? 183.282 143.570 140.920 1.00 11.64  ? 4318 PRO A C     1 
ATOM   20556 O  O     . PRO A 1 4318 ? 182.756 144.459 140.239 1.00 14.31  ? 4318 PRO A O     1 
ATOM   20557 C  CB    . PRO A 1 4318 ? 183.751 144.439 143.245 1.00 13.20  ? 4318 PRO A CB    1 
ATOM   20558 C  CG    . PRO A 1 4318 ? 184.676 143.591 144.066 1.00 15.38  ? 4318 PRO A CG    1 
ATOM   20559 C  CD    . PRO A 1 4318 ? 184.011 142.274 144.225 1.00 12.52  ? 4318 PRO A CD    1 
ATOM   20560 N  N     . SER A 1 4319 ? 184.152 142.697 140.406 1.00 12.07  ? 4319 SER A N     1 
ATOM   20561 C  CA    . SER A 1 4319 ? 184.408 142.655 138.971 1.00 11.89  ? 4319 SER A CA    1 
ATOM   20562 C  C     . SER A 1 4319 ? 183.167 142.272 138.176 1.00 12.26  ? 4319 SER A C     1 
ATOM   20563 O  O     . SER A 1 4319 ? 183.067 142.631 136.998 1.00 16.77  ? 4319 SER A O     1 
ATOM   20564 C  CB    . SER A 1 4319 ? 185.542 141.679 138.668 1.00 18.61  ? 4319 SER A CB    1 
ATOM   20565 O  OG    . SER A 1 4319 ? 185.304 140.421 139.273 1.00 25.91  ? 4319 SER A OG    1 
ATOM   20566 N  N     . TRP A 1 4320 ? 182.225 141.546 138.787 1.00 11.20  ? 4320 TRP A N     1 
ATOM   20567 C  CA    . TRP A 1 4320 ? 180.936 141.316 138.141 1.00 10.19  ? 4320 TRP A CA    1 
ATOM   20568 C  C     . TRP A 1 4320 ? 180.237 142.629 137.836 1.00 8.91   ? 4320 TRP A C     1 
ATOM   20569 O  O     . TRP A 1 4320 ? 179.498 142.731 136.850 1.00 9.52   ? 4320 TRP A O     1 
ATOM   20570 C  CB    . TRP A 1 4320 ? 180.033 140.464 139.034 1.00 12.41  ? 4320 TRP A CB    1 
ATOM   20571 C  CG    . TRP A 1 4320 ? 180.351 139.006 139.074 1.00 11.02  ? 4320 TRP A CG    1 
ATOM   20572 C  CD1   . TRP A 1 4320 ? 181.577 138.429 138.957 1.00 12.49  ? 4320 TRP A CD1   1 
ATOM   20573 C  CD2   . TRP A 1 4320 ? 179.420 137.936 139.262 1.00 13.05  ? 4320 TRP A CD2   1 
ATOM   20574 N  NE1   . TRP A 1 4320 ? 181.469 137.064 139.054 1.00 16.76  ? 4320 TRP A NE1   1 
ATOM   20575 C  CE2   . TRP A 1 4320 ? 180.153 136.736 139.242 1.00 16.24  ? 4320 TRP A CE2   1 
ATOM   20576 C  CE3   . TRP A 1 4320 ? 178.034 137.878 139.442 1.00 13.00  ? 4320 TRP A CE3   1 
ATOM   20577 C  CZ2   . TRP A 1 4320 ? 179.549 135.490 139.394 1.00 17.67  ? 4320 TRP A CZ2   1 
ATOM   20578 C  CZ3   . TRP A 1 4320 ? 177.437 136.642 139.595 1.00 11.49  ? 4320 TRP A CZ3   1 
ATOM   20579 C  CH2   . TRP A 1 4320 ? 178.193 135.465 139.569 1.00 13.05  ? 4320 TRP A CH2   1 
ATOM   20580 N  N     . LEU A 1 4321 ? 180.455 143.637 138.673 1.00 7.76   ? 4321 LEU A N     1 
ATOM   20581 C  CA    . LEU A 1 4321 ? 179.800 144.930 138.569 1.00 6.69   ? 4321 LEU A CA    1 
ATOM   20582 C  C     . LEU A 1 4321 ? 180.569 145.910 137.696 1.00 8.54   ? 4321 LEU A C     1 
ATOM   20583 O  O     . LEU A 1 4321 ? 180.074 147.012 137.440 1.00 11.07  ? 4321 LEU A O     1 
ATOM   20584 C  CB    . LEU A 1 4321 ? 179.627 145.523 139.969 1.00 9.45   ? 4321 LEU A CB    1 
ATOM   20585 C  CG    . LEU A 1 4321 ? 178.712 144.743 140.912 1.00 6.76   ? 4321 LEU A CG    1 
ATOM   20586 C  CD1   . LEU A 1 4321 ? 178.736 145.347 142.305 1.00 7.03   ? 4321 LEU A CD1   1 
ATOM   20587 C  CD2   . LEU A 1 4321 ? 177.304 144.694 140.370 1.00 6.76   ? 4321 LEU A CD2   1 
ATOM   20588 N  N     . GLY A 1 4322 ? 181.760 145.537 137.233 1.00 9.08   ? 4322 GLY A N     1 
ATOM   20589 C  CA    . GLY A 1 4322 ? 182.646 146.442 136.539 1.00 9.09   ? 4322 GLY A CA    1 
ATOM   20590 C  C     . GLY A 1 4322 ? 183.660 147.127 137.429 1.00 11.95  ? 4322 GLY A C     1 
ATOM   20591 O  O     . GLY A 1 4322 ? 184.600 147.739 136.911 1.00 14.80  ? 4322 GLY A O     1 
ATOM   20592 N  N     . LEU A 1 4323 ? 183.497 147.041 138.744 1.00 10.70  ? 4323 LEU A N     1 
ATOM   20593 C  CA    . LEU A 1 4323 ? 184.414 147.644 139.694 1.00 9.30   ? 4323 LEU A CA    1 
ATOM   20594 C  C     . LEU A 1 4323 ? 185.660 146.780 139.869 1.00 12.65  ? 4323 LEU A C     1 
ATOM   20595 O  O     . LEU A 1 4323 ? 185.657 145.594 139.531 1.00 13.63  ? 4323 LEU A O     1 
ATOM   20596 C  CB    . LEU A 1 4323 ? 183.715 147.838 141.036 1.00 8.92   ? 4323 LEU A CB    1 
ATOM   20597 C  CG    . LEU A 1 4323 ? 182.626 148.908 141.095 1.00 10.00  ? 4323 LEU A CG    1 
ATOM   20598 C  CD1   . LEU A 1 4323 ? 181.570 148.536 142.117 1.00 7.49   ? 4323 LEU A CD1   1 
ATOM   20599 C  CD2   . LEU A 1 4323 ? 183.230 150.262 141.418 1.00 8.92   ? 4323 LEU A CD2   1 
ATOM   20600 N  N     . PRO A 1 4324 ? 186.748 147.355 140.382 1.00 14.73  ? 4324 PRO A N     1 
ATOM   20601 C  CA    . PRO A 1 4324 ? 187.924 146.537 140.701 1.00 11.18  ? 4324 PRO A CA    1 
ATOM   20602 C  C     . PRO A 1 4324 ? 187.618 145.543 141.811 1.00 15.22  ? 4324 PRO A C     1 
ATOM   20603 O  O     . PRO A 1 4324 ? 186.743 145.762 142.651 1.00 18.35  ? 4324 PRO A O     1 
ATOM   20604 C  CB    . PRO A 1 4324 ? 188.968 147.569 141.143 1.00 10.02  ? 4324 PRO A CB    1 
ATOM   20605 C  CG    . PRO A 1 4324 ? 188.179 148.774 141.525 1.00 10.65  ? 4324 PRO A CG    1 
ATOM   20606 C  CD    . PRO A 1 4324 ? 187.002 148.787 140.607 1.00 11.83  ? 4324 PRO A CD    1 
ATOM   20607 N  N     . ASN A 1 4325 ? 188.354 144.429 141.802 1.00 15.77  ? 4325 ASN A N     1 
ATOM   20608 C  CA    . ASN A 1 4325 ? 188.104 143.358 142.761 1.00 13.65  ? 4325 ASN A CA    1 
ATOM   20609 C  C     . ASN A 1 4325 ? 188.416 143.762 144.196 1.00 17.40  ? 4325 ASN A C     1 
ATOM   20610 O  O     . ASN A 1 4325 ? 187.848 143.176 145.124 1.00 24.85  ? 4325 ASN A O     1 
ATOM   20611 C  CB    . ASN A 1 4325 ? 188.916 142.117 142.390 1.00 20.15  ? 4325 ASN A CB    1 
ATOM   20612 C  CG    . ASN A 1 4325 ? 188.209 141.239 141.380 1.00 19.95  ? 4325 ASN A CG    1 
ATOM   20613 O  OD1   . ASN A 1 4325 ? 187.015 140.974 141.501 1.00 14.15  ? 4325 ASN A OD1   1 
ATOM   20614 N  ND2   . ASN A 1 4325 ? 188.946 140.775 140.379 1.00 27.75  ? 4325 ASN A ND2   1 
ATOM   20615 N  N     . ASN A 1 4326 ? 189.292 144.742 144.405 1.00 17.84  ? 4326 ASN A N     1 
ATOM   20616 C  CA    . ASN A 1 4326 ? 189.678 145.131 145.756 1.00 17.23  ? 4326 ASN A CA    1 
ATOM   20617 C  C     . ASN A 1 4326 ? 188.679 146.071 146.417 1.00 16.24  ? 4326 ASN A C     1 
ATOM   20618 O  O     . ASN A 1 4326 ? 188.866 146.418 147.589 1.00 18.70  ? 4326 ASN A O     1 
ATOM   20619 C  CB    . ASN A 1 4326 ? 191.069 145.774 145.744 1.00 16.65  ? 4326 ASN A CB    1 
ATOM   20620 C  CG    . ASN A 1 4326 ? 191.197 146.881 144.714 1.00 19.77  ? 4326 ASN A CG    1 
ATOM   20621 O  OD1   . ASN A 1 4326 ? 190.388 147.806 144.669 1.00 20.89  ? 4326 ASN A OD1   1 
ATOM   20622 N  ND2   . ASN A 1 4326 ? 192.223 146.789 143.878 1.00 27.04  ? 4326 ASN A ND2   1 
ATOM   20623 N  N     . ALA A 1 4327 ? 187.624 146.478 145.705 1.00 14.61  ? 4327 ALA A N     1 
ATOM   20624 C  CA    . ALA A 1 4327 ? 186.652 147.406 146.274 1.00 18.26  ? 4327 ALA A CA    1 
ATOM   20625 C  C     . ALA A 1 4327 ? 186.008 146.851 147.537 1.00 22.30  ? 4327 ALA A C     1 
ATOM   20626 O  O     . ALA A 1 4327 ? 185.676 147.614 148.452 1.00 21.46  ? 4327 ALA A O     1 
ATOM   20627 C  CB    . ALA A 1 4327 ? 185.578 147.742 145.240 1.00 11.96  ? 4327 ALA A CB    1 
ATOM   20628 N  N     . GLU A 1 4328 ? 185.826 145.536 147.611 1.00 23.40  ? 4328 GLU A N     1 
ATOM   20629 C  CA    . GLU A 1 4328 ? 185.239 144.910 148.785 1.00 18.47  ? 4328 GLU A CA    1 
ATOM   20630 C  C     . GLU A 1 4328 ? 186.256 144.612 149.877 1.00 18.15  ? 4328 GLU A C     1 
ATOM   20631 O  O     . GLU A 1 4328 ? 185.851 144.315 151.007 1.00 18.07  ? 4328 GLU A O     1 
ATOM   20632 C  CB    . GLU A 1 4328 ? 184.531 143.610 148.388 1.00 15.86  ? 4328 GLU A CB    1 
ATOM   20633 C  CG    . GLU A 1 4328 ? 185.437 142.598 147.707 1.00 18.62  ? 4328 GLU A CG    1 
ATOM   20634 C  CD    . GLU A 1 4328 ? 184.728 141.294 147.399 1.00 34.52  ? 4328 GLU A CD    1 
ATOM   20635 O  OE1   . GLU A 1 4328 ? 183.503 141.212 147.626 1.00 31.08  ? 4328 GLU A OE1   1 
ATOM   20636 O  OE2   . GLU A 1 4328 ? 185.397 140.348 146.931 1.00 35.09  ? 4328 GLU A OE2   1 
ATOM   20637 N  N     . ARG A 1 4329 ? 187.556 144.722 149.580 1.00 21.12  ? 4329 ARG A N     1 
ATOM   20638 C  CA    . ARG A 1 4329 ? 188.573 144.213 150.497 1.00 17.28  ? 4329 ARG A CA    1 
ATOM   20639 C  C     . ARG A 1 4329 ? 188.475 144.873 151.865 1.00 17.04  ? 4329 ARG A C     1 
ATOM   20640 O  O     . ARG A 1 4329 ? 188.572 144.197 152.896 1.00 20.44  ? 4329 ARG A O     1 
ATOM   20641 C  CB    . ARG A 1 4329 ? 189.967 144.415 149.905 1.00 18.39  ? 4329 ARG A CB    1 
ATOM   20642 C  CG    . ARG A 1 4329 ? 191.086 144.282 150.923 1.00 19.19  ? 4329 ARG A CG    1 
ATOM   20643 C  CD    . ARG A 1 4329 ? 192.429 144.072 150.256 1.00 22.58  ? 4329 ARG A CD    1 
ATOM   20644 N  NE    . ARG A 1 4329 ? 192.477 142.822 149.509 1.00 30.38  ? 4329 ARG A NE    1 
ATOM   20645 C  CZ    . ARG A 1 4329 ? 193.372 141.865 149.708 1.00 30.85  ? 4329 ARG A CZ    1 
ATOM   20646 N  NH1   . ARG A 1 4329 ? 194.303 141.972 150.642 1.00 32.66  ? 4329 ARG A NH1   1 
ATOM   20647 N  NH2   . ARG A 1 4329 ? 193.333 140.773 148.950 1.00 29.40  ? 4329 ARG A NH2   1 
ATOM   20648 N  N     . VAL A 1 4330 ? 188.284 146.191 151.900 1.00 17.98  ? 4330 VAL A N     1 
ATOM   20649 C  CA    . VAL A 1 4330 ? 188.075 146.865 153.177 1.00 16.86  ? 4330 VAL A CA    1 
ATOM   20650 C  C     . VAL A 1 4330 ? 186.747 146.437 153.789 1.00 15.77  ? 4330 VAL A C     1 
ATOM   20651 O  O     . VAL A 1 4330 ? 186.684 146.042 154.960 1.00 21.16  ? 4330 VAL A O     1 
ATOM   20652 C  CB    . VAL A 1 4330 ? 188.155 148.391 152.999 1.00 16.67  ? 4330 VAL A CB    1 
ATOM   20653 C  CG1   . VAL A 1 4330 ? 187.467 149.100 154.154 1.00 18.54  ? 4330 VAL A CG1   1 
ATOM   20654 C  CG2   . VAL A 1 4330 ? 189.603 148.832 152.893 1.00 12.85  ? 4330 VAL A CG2   1 
ATOM   20655 N  N     . LEU A 1 4331 ? 185.674 146.472 152.995 1.00 14.62  ? 4331 LEU A N     1 
ATOM   20656 C  CA    . LEU A 1 4331 ? 184.345 146.199 153.534 1.00 15.36  ? 4331 LEU A CA    1 
ATOM   20657 C  C     . LEU A 1 4331 ? 184.260 144.781 154.079 1.00 14.62  ? 4331 LEU A C     1 
ATOM   20658 O  O     . LEU A 1 4331 ? 183.906 144.571 155.246 1.00 15.86  ? 4331 LEU A O     1 
ATOM   20659 C  CB    . LEU A 1 4331 ? 183.279 146.429 152.460 1.00 17.57  ? 4331 LEU A CB    1 
ATOM   20660 C  CG    . LEU A 1 4331 ? 182.773 147.855 152.212 1.00 17.02  ? 4331 LEU A CG    1 
ATOM   20661 C  CD1   . LEU A 1 4331 ? 182.065 148.392 153.448 1.00 16.72  ? 4331 LEU A CD1   1 
ATOM   20662 C  CD2   . LEU A 1 4331 ? 183.884 148.801 151.773 1.00 16.29  ? 4331 LEU A CD2   1 
ATOM   20663 N  N     . LEU A 1 4332 ? 184.637 143.796 153.260 1.00 15.93  ? 4332 LEU A N     1 
ATOM   20664 C  CA    . LEU A 1 4332 ? 184.654 142.412 153.714 1.00 14.64  ? 4332 LEU A CA    1 
ATOM   20665 C  C     . LEU A 1 4332 ? 185.573 142.220 154.909 1.00 15.36  ? 4332 LEU A C     1 
ATOM   20666 O  O     . LEU A 1 4332 ? 185.392 141.262 155.669 1.00 17.93  ? 4332 LEU A O     1 
ATOM   20667 C  CB    . LEU A 1 4332 ? 185.079 141.486 152.574 1.00 9.78   ? 4332 LEU A CB    1 
ATOM   20668 C  CG    . LEU A 1 4332 ? 184.049 141.218 151.478 1.00 8.40   ? 4332 LEU A CG    1 
ATOM   20669 C  CD1   . LEU A 1 4332 ? 184.511 140.075 150.597 1.00 15.32  ? 4332 LEU A CD1   1 
ATOM   20670 C  CD2   . LEU A 1 4332 ? 182.692 140.910 152.083 1.00 10.66  ? 4332 LEU A CD2   1 
ATOM   20671 N  N     . THR A 1 4333 ? 186.554 143.104 155.094 1.00 13.34  ? 4333 THR A N     1 
ATOM   20672 C  CA    . THR A 1 4333 ? 187.336 143.078 156.322 1.00 13.34  ? 4333 THR A CA    1 
ATOM   20673 C  C     . THR A 1 4333 ? 186.495 143.559 157.496 1.00 14.84  ? 4333 THR A C     1 
ATOM   20674 O  O     . THR A 1 4333 ? 186.302 142.831 158.478 1.00 21.03  ? 4333 THR A O     1 
ATOM   20675 C  CB    . THR A 1 4333 ? 188.593 143.936 156.168 1.00 14.52  ? 4333 THR A CB    1 
ATOM   20676 O  OG1   . THR A 1 4333 ? 189.378 143.446 155.075 1.00 20.52  ? 4333 THR A OG1   1 
ATOM   20677 C  CG2   . THR A 1 4333 ? 189.426 143.892 157.439 1.00 14.27  ? 4333 THR A CG2   1 
ATOM   20678 N  N     . THR A 1 4334 ? 185.944 144.772 157.385 1.00 14.13  ? 4334 THR A N     1 
ATOM   20679 C  CA    . THR A 1 4334 ? 185.247 145.380 158.513 1.00 16.07  ? 4334 THR A CA    1 
ATOM   20680 C  C     . THR A 1 4334 ? 184.113 144.490 158.998 1.00 14.17  ? 4334 THR A C     1 
ATOM   20681 O  O     . THR A 1 4334 ? 184.054 144.129 160.180 1.00 16.65  ? 4334 THR A O     1 
ATOM   20682 C  CB    . THR A 1 4334 ? 184.719 146.761 158.120 1.00 18.71  ? 4334 THR A CB    1 
ATOM   20683 O  OG1   . THR A 1 4334 ? 185.810 147.684 158.027 1.00 21.60  ? 4334 THR A OG1   1 
ATOM   20684 C  CG2   . THR A 1 4334 ? 183.722 147.266 159.148 1.00 21.08  ? 4334 THR A CG2   1 
ATOM   20685 N  N     . GLN A 1 4335 ? 183.231 144.084 158.080 1.00 16.15  ? 4335 GLN A N     1 
ATOM   20686 C  CA    . GLN A 1 4335 ? 182.137 143.192 158.441 1.00 18.20  ? 4335 GLN A CA    1 
ATOM   20687 C  C     . GLN A 1 4335 ? 182.658 141.960 159.164 1.00 15.90  ? 4335 GLN A C     1 
ATOM   20688 O  O     . GLN A 1 4335 ? 182.118 141.570 160.207 1.00 18.72  ? 4335 GLN A O     1 
ATOM   20689 C  CB    . GLN A 1 4335 ? 181.351 142.792 157.193 1.00 17.46  ? 4335 GLN A CB    1 
ATOM   20690 C  CG    . GLN A 1 4335 ? 180.411 143.869 156.683 1.00 24.34  ? 4335 GLN A CG    1 
ATOM   20691 C  CD    . GLN A 1 4335 ? 179.597 143.414 155.489 1.00 33.54  ? 4335 GLN A CD    1 
ATOM   20692 O  OE1   . GLN A 1 4335 ? 180.146 143.077 154.440 1.00 30.11  ? 4335 GLN A OE1   1 
ATOM   20693 N  NE2   . GLN A 1 4335 ? 178.278 143.401 155.643 1.00 30.49  ? 4335 GLN A NE2   1 
ATOM   20694 N  N     . GLY A 1 4336 ? 183.737 141.363 158.651 1.00 13.88  ? 4336 GLY A N     1 
ATOM   20695 C  CA    . GLY A 1 4336 ? 184.316 140.216 159.329 1.00 11.44  ? 4336 GLY A CA    1 
ATOM   20696 C  C     . GLY A 1 4336 ? 184.662 140.532 160.769 1.00 12.39  ? 4336 GLY A C     1 
ATOM   20697 O  O     . GLY A 1 4336 ? 184.205 139.854 161.694 1.00 21.40  ? 4336 GLY A O     1 
ATOM   20698 N  N     . VAL A 1 4337 ? 185.412 141.617 160.980 1.00 12.22  ? 4337 VAL A N     1 
ATOM   20699 C  CA    . VAL A 1 4337 ? 185.707 142.050 162.340 1.00 14.29  ? 4337 VAL A CA    1 
ATOM   20700 C  C     . VAL A 1 4337 ? 184.411 142.298 163.093 1.00 13.89  ? 4337 VAL A C     1 
ATOM   20701 O  O     . VAL A 1 4337 ? 184.238 141.844 164.232 1.00 15.97  ? 4337 VAL A O     1 
ATOM   20702 C  CB    . VAL A 1 4337 ? 186.606 143.301 162.322 1.00 11.75  ? 4337 VAL A CB    1 
ATOM   20703 C  CG1   . VAL A 1 4337 ? 186.527 144.033 163.649 1.00 8.46   ? 4337 VAL A CG1   1 
ATOM   20704 C  CG2   . VAL A 1 4337 ? 188.040 142.916 162.008 1.00 10.55  ? 4337 VAL A CG2   1 
ATOM   20705 N  N     . ASP A 1 4338 ? 183.459 142.970 162.440 1.00 12.76  ? 4338 ASP A N     1 
ATOM   20706 C  CA    . ASP A 1 4338 ? 182.168 143.228 163.062 1.00 13.62  ? 4338 ASP A CA    1 
ATOM   20707 C  C     . ASP A 1 4338 ? 181.528 141.930 163.526 1.00 16.16  ? 4338 ASP A C     1 
ATOM   20708 O  O     . ASP A 1 4338 ? 181.022 141.847 164.653 1.00 19.12  ? 4338 ASP A O     1 
ATOM   20709 C  CB    . ASP A 1 4338 ? 181.260 143.966 162.077 1.00 18.72  ? 4338 ASP A CB    1 
ATOM   20710 C  CG    . ASP A 1 4338 ? 180.258 144.867 162.766 1.00 37.25  ? 4338 ASP A CG    1 
ATOM   20711 O  OD1   . ASP A 1 4338 ? 180.684 145.770 163.516 1.00 44.80  ? 4338 ASP A OD1   1 
ATOM   20712 O  OD2   . ASP A 1 4338 ? 179.045 144.685 162.543 1.00 36.78  ? 4338 ASP A OD2   1 
ATOM   20713 N  N     . MET A 1 4339 ? 181.598 140.887 162.692 1.00 14.34  ? 4339 MET A N     1 
ATOM   20714 C  CA    . MET A 1 4339 ? 181.032 139.599 163.073 1.00 11.52  ? 4339 MET A CA    1 
ATOM   20715 C  C     . MET A 1 4339 ? 181.629 139.125 164.388 1.00 16.83  ? 4339 MET A C     1 
ATOM   20716 O  O     . MET A 1 4339 ? 180.900 138.776 165.326 1.00 17.67  ? 4339 MET A O     1 
ATOM   20717 C  CB    . MET A 1 4339 ? 181.264 138.572 161.962 1.00 11.43  ? 4339 MET A CB    1 
ATOM   20718 C  CG    . MET A 1 4339 ? 180.539 137.251 162.175 1.00 15.03  ? 4339 MET A CG    1 
ATOM   20719 S  SD    . MET A 1 4339 ? 181.349 135.845 161.388 1.00 24.61  ? 4339 MET A SD    1 
ATOM   20720 C  CE    . MET A 1 4339 ? 182.912 135.813 162.255 1.00 14.86  ? 4339 MET A CE    1 
ATOM   20721 N  N     . ILE A 1 4340 ? 182.961 139.187 164.500 1.00 17.73  ? 4340 ILE A N     1 
ATOM   20722 C  CA    . ILE A 1 4340 ? 183.623 138.790 165.740 1.00 16.29  ? 4340 ILE A CA    1 
ATOM   20723 C  C     . ILE A 1 4340 ? 183.036 139.564 166.907 1.00 15.41  ? 4340 ILE A C     1 
ATOM   20724 O  O     . ILE A 1 4340 ? 182.641 138.984 167.927 1.00 16.31  ? 4340 ILE A O     1 
ATOM   20725 C  CB    . ILE A 1 4340 ? 185.143 139.008 165.636 1.00 18.61  ? 4340 ILE A CB    1 
ATOM   20726 C  CG1   . ILE A 1 4340 ? 185.728 138.199 164.481 1.00 16.62  ? 4340 ILE A CG1   1 
ATOM   20727 C  CG2   . ILE A 1 4340 ? 185.824 138.638 166.942 1.00 23.35  ? 4340 ILE A CG2   1 
ATOM   20728 C  CD1   . ILE A 1 4340 ? 185.536 136.720 164.637 1.00 19.46  ? 4340 ILE A CD1   1 
ATOM   20729 N  N     . SER A 1 4341 ? 182.905 140.883 166.739 1.00 13.84  ? 4341 SER A N     1 
ATOM   20730 C  CA    . SER A 1 4341 ? 182.375 141.712 167.813 1.00 13.03  ? 4341 SER A CA    1 
ATOM   20731 C  C     . SER A 1 4341 ? 181.002 141.219 168.238 1.00 13.73  ? 4341 SER A C     1 
ATOM   20732 O  O     . SER A 1 4341 ? 180.729 141.061 169.434 1.00 15.32  ? 4341 SER A O     1 
ATOM   20733 C  CB    . SER A 1 4341 ? 182.318 143.172 167.365 1.00 18.99  ? 4341 SER A CB    1 
ATOM   20734 O  OG    . SER A 1 4341 ? 183.602 143.637 166.992 1.00 19.40  ? 4341 SER A OG    1 
ATOM   20735 N  N     . LYS A 1 4342 ? 180.139 140.918 167.265 1.00 15.96  ? 4342 LYS A N     1 
ATOM   20736 C  CA    . LYS A 1 4342 ? 178.819 140.407 167.608 1.00 15.21  ? 4342 LYS A CA    1 
ATOM   20737 C  C     . LYS A 1 4342 ? 178.931 139.072 168.328 1.00 16.21  ? 4342 LYS A C     1 
ATOM   20738 O  O     . LYS A 1 4342 ? 178.292 138.864 169.367 1.00 22.08  ? 4342 LYS A O     1 
ATOM   20739 C  CB    . LYS A 1 4342 ? 177.959 140.291 166.352 1.00 16.16  ? 4342 LYS A CB    1 
ATOM   20740 C  CG    . LYS A 1 4342 ? 177.611 141.635 165.742 1.00 12.49  ? 4342 LYS A CG    1 
ATOM   20741 C  CD    . LYS A 1 4342 ? 176.958 141.483 164.386 1.00 15.39  ? 4342 LYS A CD    1 
ATOM   20742 C  CE    . LYS A 1 4342 ? 176.799 142.832 163.709 1.00 18.73  ? 4342 LYS A CE    1 
ATOM   20743 N  NZ    . LYS A 1 4342 ? 176.154 143.834 164.598 1.00 18.16  ? 4342 LYS A NZ    1 
ATOM   20744 N  N     . MET A 1 4343 ? 179.786 138.176 167.825 1.00 17.24  ? 4343 MET A N     1 
ATOM   20745 C  CA    . MET A 1 4343 ? 180.000 136.907 168.507 1.00 14.67  ? 4343 MET A CA    1 
ATOM   20746 C  C     . MET A 1 4343 ? 180.586 137.104 169.894 1.00 19.95  ? 4343 MET A C     1 
ATOM   20747 O  O     . MET A 1 4343 ? 180.448 136.220 170.746 1.00 32.49  ? 4343 MET A O     1 
ATOM   20748 C  CB    . MET A 1 4343 ? 180.913 136.002 167.682 1.00 18.86  ? 4343 MET A CB    1 
ATOM   20749 C  CG    . MET A 1 4343 ? 180.253 135.349 166.487 1.00 15.71  ? 4343 MET A CG    1 
ATOM   20750 S  SD    . MET A 1 4343 ? 181.391 134.235 165.646 1.00 38.32  ? 4343 MET A SD    1 
ATOM   20751 C  CE    . MET A 1 4343 ? 181.009 132.686 166.459 1.00 23.79  ? 4343 MET A CE    1 
ATOM   20752 N  N     . LEU A 1 4344 ? 181.233 138.241 170.143 1.00 17.60  ? 4344 LEU A N     1 
ATOM   20753 C  CA    . LEU A 1 4344 ? 181.722 138.537 171.478 1.00 18.74  ? 4344 LEU A CA    1 
ATOM   20754 C  C     . LEU A 1 4344 ? 180.682 139.247 172.329 1.00 20.18  ? 4344 LEU A C     1 
ATOM   20755 O  O     . LEU A 1 4344 ? 180.732 139.144 173.560 1.00 29.39  ? 4344 LEU A O     1 
ATOM   20756 C  CB    . LEU A 1 4344 ? 182.994 139.385 171.400 1.00 22.53  ? 4344 LEU A CB    1 
ATOM   20757 C  CG    . LEU A 1 4344 ? 183.894 139.350 172.634 1.00 28.23  ? 4344 LEU A CG    1 
ATOM   20758 C  CD1   . LEU A 1 4344 ? 184.143 137.914 173.057 1.00 27.97  ? 4344 LEU A CD1   1 
ATOM   20759 C  CD2   . LEU A 1 4344 ? 185.205 140.061 172.359 1.00 30.70  ? 4344 LEU A CD2   1 
ATOM   20760 N  N     . LYS A 1 4345 ? 179.736 139.949 171.704 1.00 19.42  ? 4345 LYS A N     1 
ATOM   20761 C  CA    . LYS A 1 4345 ? 178.702 140.648 172.454 1.00 17.95  ? 4345 LYS A CA    1 
ATOM   20762 C  C     . LYS A 1 4345 ? 177.661 139.694 173.021 1.00 21.53  ? 4345 LYS A C     1 
ATOM   20763 O  O     . LYS A 1 4345 ? 177.011 140.022 174.020 1.00 25.20  ? 4345 LYS A O     1 
ATOM   20764 C  CB    . LYS A 1 4345 ? 178.033 141.693 171.557 1.00 16.70  ? 4345 LYS A CB    1 
ATOM   20765 C  CG    . LYS A 1 4345 ? 176.975 142.543 172.237 1.00 20.63  ? 4345 LYS A CG    1 
ATOM   20766 C  CD    . LYS A 1 4345 ? 177.585 143.452 173.284 1.00 25.90  ? 4345 LYS A CD    1 
ATOM   20767 C  CE    . LYS A 1 4345 ? 176.518 144.287 173.969 1.00 26.90  ? 4345 LYS A CE    1 
ATOM   20768 N  NZ    . LYS A 1 4345 ? 175.888 145.253 173.030 1.00 33.73  ? 4345 LYS A NZ    1 
ATOM   20769 N  N     . MET A 1 4346 ? 177.510 138.515 172.422 1.00 22.14  ? 4346 MET A N     1 
ATOM   20770 C  CA    . MET A 1 4346 ? 176.509 137.535 172.819 1.00 25.16  ? 4346 MET A CA    1 
ATOM   20771 C  C     . MET A 1 4346 ? 177.116 136.402 173.642 1.00 28.30  ? 4346 MET A C     1 
ATOM   20772 O  O     . MET A 1 4346 ? 176.568 135.299 173.693 1.00 25.21  ? 4346 MET A O     1 
ATOM   20773 C  CB    . MET A 1 4346 ? 175.801 136.988 171.582 1.00 19.47  ? 4346 MET A CB    1 
ATOM   20774 C  CG    . MET A 1 4346 ? 174.792 137.950 170.985 1.00 22.42  ? 4346 MET A CG    1 
ATOM   20775 S  SD    . MET A 1 4346 ? 173.909 137.259 169.579 1.00 45.48  ? 4346 MET A SD    1 
ATOM   20776 C  CE    . MET A 1 4346 ? 175.199 137.280 168.340 1.00 23.58  ? 4346 MET A CE    1 
ATOM   20777 N  N     . GLN A 1 4347 ? 178.245 136.666 174.292 1.00 35.82  ? 4347 GLN A N     1 
ATOM   20778 C  CA    . GLN A 1 4347 ? 178.936 135.652 175.078 1.00 41.72  ? 4347 GLN A CA    1 
ATOM   20779 C  C     . GLN A 1 4347 ? 178.513 135.712 176.543 1.00 43.54  ? 4347 GLN A C     1 
ATOM   20780 O  O     . GLN A 1 4347 ? 177.835 134.813 177.042 1.00 41.51  ? 4347 GLN A O     1 
ATOM   20781 C  CB    . GLN A 1 4347 ? 180.451 135.827 174.959 1.00 38.95  ? 4347 GLN A CB    1 
ATOM   20782 C  CG    . GLN A 1 4347 ? 181.256 134.637 175.441 1.00 45.29  ? 4347 GLN A CG    1 
ATOM   20783 C  CD    . GLN A 1 4347 ? 181.210 133.475 174.469 1.00 50.39  ? 4347 GLN A CD    1 
ATOM   20784 O  OE1   . GLN A 1 4347 ? 181.262 133.666 173.254 1.00 38.88  ? 4347 GLN A OE1   1 
ATOM   20785 N  NE2   . GLN A 1 4347 ? 181.113 132.262 175.000 1.00 57.07  ? 4347 GLN A NE2   1 
ATOM   20786 N  N     . PRO A 1 4374 ? 190.143 163.766 188.280 1.00 49.23  ? 4374 PRO A N     1 
ATOM   20787 C  CA    . PRO A 1 4374 ? 189.838 162.417 187.793 1.00 57.53  ? 4374 PRO A CA    1 
ATOM   20788 C  C     . PRO A 1 4374 ? 190.801 161.957 186.702 1.00 57.46  ? 4374 PRO A C     1 
ATOM   20789 O  O     . PRO A 1 4374 ? 191.657 162.729 186.271 1.00 52.31  ? 4374 PRO A O     1 
ATOM   20790 C  CB    . PRO A 1 4374 ? 188.411 162.551 187.239 1.00 52.56  ? 4374 PRO A CB    1 
ATOM   20791 C  CG    . PRO A 1 4374 ? 187.943 163.957 187.595 1.00 51.17  ? 4374 PRO A CG    1 
ATOM   20792 C  CD    . PRO A 1 4374 ? 188.920 164.529 188.567 1.00 47.14  ? 4374 PRO A CD    1 
ATOM   20793 N  N     . ALA A 1 4375 ? 190.657 160.701 186.272 1.00 58.87  ? 4375 ALA A N     1 
ATOM   20794 C  CA    . ALA A 1 4375 ? 191.535 160.164 185.237 1.00 61.86  ? 4375 ALA A CA    1 
ATOM   20795 C  C     . ALA A 1 4375 ? 191.339 160.889 183.912 1.00 57.73  ? 4375 ALA A C     1 
ATOM   20796 O  O     . ALA A 1 4375 ? 192.311 161.143 183.185 1.00 51.54  ? 4375 ALA A O     1 
ATOM   20797 C  CB    . ALA A 1 4375 ? 191.292 158.665 185.070 1.00 56.37  ? 4375 ALA A CB    1 
ATOM   20798 N  N     . TRP A 1 4376 ? 190.088 161.220 183.576 1.00 52.99  ? 4376 TRP A N     1 
ATOM   20799 C  CA    . TRP A 1 4376 ? 189.826 161.915 182.321 1.00 51.05  ? 4376 TRP A CA    1 
ATOM   20800 C  C     . TRP A 1 4376 ? 190.500 163.280 182.311 1.00 49.29  ? 4376 TRP A C     1 
ATOM   20801 O  O     . TRP A 1 4376 ? 191.015 163.716 181.276 1.00 44.52  ? 4376 TRP A O     1 
ATOM   20802 C  CB    . TRP A 1 4376 ? 188.319 162.032 182.080 1.00 44.53  ? 4376 TRP A CB    1 
ATOM   20803 C  CG    . TRP A 1 4376 ? 187.591 163.001 182.964 1.00 52.14  ? 4376 TRP A CG    1 
ATOM   20804 C  CD1   . TRP A 1 4376 ? 186.852 162.701 184.070 1.00 59.57  ? 4376 TRP A CD1   1 
ATOM   20805 C  CD2   . TRP A 1 4376 ? 187.468 164.416 182.772 1.00 53.52  ? 4376 TRP A CD2   1 
ATOM   20806 N  NE1   . TRP A 1 4376 ? 186.311 163.846 184.603 1.00 58.77  ? 4376 TRP A NE1   1 
ATOM   20807 C  CE2   . TRP A 1 4376 ? 186.672 164.912 183.821 1.00 54.42  ? 4376 TRP A CE2   1 
ATOM   20808 C  CE3   . TRP A 1 4376 ? 187.970 165.313 181.825 1.00 51.89  ? 4376 TRP A CE3   1 
ATOM   20809 C  CZ2   . TRP A 1 4376 ? 186.364 166.264 183.948 1.00 49.13  ? 4376 TRP A CZ2   1 
ATOM   20810 C  CZ3   . TRP A 1 4376 ? 187.667 166.653 181.955 1.00 45.75  ? 4376 TRP A CZ3   1 
ATOM   20811 C  CH2   . TRP A 1 4376 ? 186.868 167.116 183.006 1.00 47.08  ? 4376 TRP A CH2   1 
ATOM   20812 N  N     . MET A 1 4377 ? 190.535 163.951 183.465 1.00 45.85  ? 4377 MET A N     1 
ATOM   20813 C  CA    . MET A 1 4377 ? 191.258 165.213 183.574 1.00 44.35  ? 4377 MET A CA    1 
ATOM   20814 C  C     . MET A 1 4377 ? 192.722 165.043 183.186 1.00 41.67  ? 4377 MET A C     1 
ATOM   20815 O  O     . MET A 1 4377 ? 193.256 165.814 182.381 1.00 41.64  ? 4377 MET A O     1 
ATOM   20816 C  CB    . MET A 1 4377 ? 191.150 165.753 185.001 1.00 48.77  ? 4377 MET A CB    1 
ATOM   20817 C  CG    . MET A 1 4377 ? 191.404 167.243 185.132 1.00 43.54  ? 4377 MET A CG    1 
ATOM   20818 S  SD    . MET A 1 4377 ? 190.447 168.031 186.442 1.00 61.97  ? 4377 MET A SD    1 
ATOM   20819 C  CE    . MET A 1 4377 ? 188.825 168.102 185.696 1.00 52.77  ? 4377 MET A CE    1 
ATOM   20820 N  N     . ARG A 1 4378 ? 193.384 164.026 183.741 1.00 47.02  ? 4378 ARG A N     1 
ATOM   20821 C  CA    . ARG A 1 4378 ? 194.813 163.846 183.503 1.00 45.30  ? 4378 ARG A CA    1 
ATOM   20822 C  C     . ARG A 1 4378 ? 195.094 163.458 182.056 1.00 45.07  ? 4378 ARG A C     1 
ATOM   20823 O  O     . ARG A 1 4378 ? 196.022 163.990 181.427 1.00 45.66  ? 4378 ARG A O     1 
ATOM   20824 C  CB    . ARG A 1 4378 ? 195.371 162.795 184.462 1.00 48.31  ? 4378 ARG A CB    1 
ATOM   20825 C  CG    . ARG A 1 4378 ? 195.102 163.092 185.926 1.00 51.15  ? 4378 ARG A CG    1 
ATOM   20826 C  CD    . ARG A 1 4378 ? 195.436 161.897 186.805 1.00 59.23  ? 4378 ARG A CD    1 
ATOM   20827 N  NE    . ARG A 1 4378 ? 196.622 162.133 187.621 1.00 62.07  ? 4378 ARG A NE    1 
ATOM   20828 C  CZ    . ARG A 1 4378 ? 196.627 162.823 188.753 1.00 61.63  ? 4378 ARG A CZ    1 
ATOM   20829 N  NH1   . ARG A 1 4378 ? 195.521 163.360 189.241 1.00 62.04  ? 4378 ARG A NH1   1 
ATOM   20830 N  NH2   . ARG A 1 4378 ? 197.771 162.976 189.414 1.00 54.06  ? 4378 ARG A NH2   1 
ATOM   20831 N  N     . THR A 1 4379 ? 194.309 162.524 181.508 1.00 37.78  ? 4379 THR A N     1 
ATOM   20832 C  CA    . THR A 1 4379 ? 194.553 162.115 180.128 1.00 38.29  ? 4379 THR A CA    1 
ATOM   20833 C  C     . THR A 1 4379 ? 194.265 163.256 179.159 1.00 42.90  ? 4379 THR A C     1 
ATOM   20834 O  O     . THR A 1 4379 ? 194.995 163.437 178.177 1.00 41.82  ? 4379 THR A O     1 
ATOM   20835 C  CB    . THR A 1 4379 ? 193.739 160.865 179.773 1.00 43.43  ? 4379 THR A CB    1 
ATOM   20836 O  OG1   . THR A 1 4379 ? 194.014 160.483 178.419 1.00 49.76  ? 4379 THR A OG1   1 
ATOM   20837 C  CG2   . THR A 1 4379 ? 192.253 161.105 179.920 1.00 41.60  ? 4379 THR A CG2   1 
ATOM   20838 N  N     . LEU A 1 4380 ? 193.228 164.059 179.428 1.00 39.55  ? 4380 LEU A N     1 
ATOM   20839 C  CA    . LEU A 1 4380 ? 192.957 165.219 178.590 1.00 34.48  ? 4380 LEU A CA    1 
ATOM   20840 C  C     . LEU A 1 4380 ? 194.067 166.254 178.705 1.00 32.50  ? 4380 LEU A C     1 
ATOM   20841 O  O     . LEU A 1 4380 ? 194.430 166.888 177.712 1.00 37.74  ? 4380 LEU A O     1 
ATOM   20842 C  CB    . LEU A 1 4380 ? 191.608 165.833 178.960 1.00 37.25  ? 4380 LEU A CB    1 
ATOM   20843 C  CG    . LEU A 1 4380 ? 191.077 166.918 178.021 1.00 34.27  ? 4380 LEU A CG    1 
ATOM   20844 C  CD1   . LEU A 1 4380 ? 190.949 166.388 176.605 1.00 30.52  ? 4380 LEU A CD1   1 
ATOM   20845 C  CD2   . LEU A 1 4380 ? 189.742 167.444 178.516 1.00 31.86  ? 4380 LEU A CD2   1 
ATOM   20846 N  N     . HIS A 1 4381 ? 194.612 166.443 179.909 1.00 29.25  ? 4381 HIS A N     1 
ATOM   20847 C  CA    . HIS A 1 4381 ? 195.723 167.373 180.080 1.00 33.23  ? 4381 HIS A CA    1 
ATOM   20848 C  C     . HIS A 1 4381 ? 196.920 166.946 179.243 1.00 36.47  ? 4381 HIS A C     1 
ATOM   20849 O  O     . HIS A 1 4381 ? 197.514 167.758 178.521 1.00 35.50  ? 4381 HIS A O     1 
ATOM   20850 C  CB    . HIS A 1 4381 ? 196.104 167.460 181.559 1.00 30.70  ? 4381 HIS A CB    1 
ATOM   20851 C  CG    . HIS A 1 4381 ? 197.220 168.416 181.845 1.00 31.63  ? 4381 HIS A CG    1 
ATOM   20852 N  ND1   . HIS A 1 4381 ? 198.539 168.125 181.575 1.00 36.32  ? 4381 HIS A ND1   1 
ATOM   20853 C  CD2   . HIS A 1 4381 ? 197.213 169.655 182.391 1.00 33.93  ? 4381 HIS A CD2   1 
ATOM   20854 C  CE1   . HIS A 1 4381 ? 199.297 169.146 181.935 1.00 34.77  ? 4381 HIS A CE1   1 
ATOM   20855 N  NE2   . HIS A 1 4381 ? 198.517 170.087 182.434 1.00 34.72  ? 4381 HIS A NE2   1 
ATOM   20856 N  N     . THR A 1 4382 ? 197.281 165.663 179.322 1.00 39.94  ? 4382 THR A N     1 
ATOM   20857 C  CA    . THR A 1 4382 ? 198.413 165.170 178.543 1.00 39.54  ? 4382 THR A CA    1 
ATOM   20858 C  C     . THR A 1 4382 ? 198.147 165.292 177.047 1.00 36.57  ? 4382 THR A C     1 
ATOM   20859 O  O     . THR A 1 4382 ? 199.023 165.724 176.284 1.00 36.78  ? 4382 THR A O     1 
ATOM   20860 C  CB    . THR A 1 4382 ? 198.718 163.720 178.918 1.00 45.34  ? 4382 THR A CB    1 
ATOM   20861 O  OG1   . THR A 1 4382 ? 198.881 163.618 180.338 1.00 45.39  ? 4382 THR A OG1   1 
ATOM   20862 C  CG2   . THR A 1 4382 ? 199.992 163.248 178.231 1.00 39.86  ? 4382 THR A CG2   1 
ATOM   20863 N  N     . THR A 1 4383 ? 196.936 164.931 176.613 1.00 31.67  ? 4383 THR A N     1 
ATOM   20864 C  CA    . THR A 1 4383 ? 196.601 164.999 175.195 1.00 34.30  ? 4383 THR A CA    1 
ATOM   20865 C  C     . THR A 1 4383 ? 196.652 166.432 174.681 1.00 34.32  ? 4383 THR A C     1 
ATOM   20866 O  O     . THR A 1 4383 ? 197.180 166.690 173.593 1.00 35.19  ? 4383 THR A O     1 
ATOM   20867 C  CB    . THR A 1 4383 ? 195.215 164.397 174.961 1.00 32.33  ? 4383 THR A CB    1 
ATOM   20868 O  OG1   . THR A 1 4383 ? 195.192 163.046 175.435 1.00 45.61  ? 4383 THR A OG1   1 
ATOM   20869 C  CG2   . THR A 1 4383 ? 194.880 164.405 173.489 1.00 27.09  ? 4383 THR A CG2   1 
ATOM   20870 N  N     . ALA A 1 4384 ? 196.117 167.379 175.453 1.00 34.92  ? 4384 ALA A N     1 
ATOM   20871 C  CA    . ALA A 1 4384 ? 196.099 168.770 175.020 1.00 31.61  ? 4384 ALA A CA    1 
ATOM   20872 C  C     . ALA A 1 4384 ? 197.499 169.368 175.013 1.00 31.33  ? 4384 ALA A C     1 
ATOM   20873 O  O     . ALA A 1 4384 ? 197.831 170.164 174.127 1.00 33.81  ? 4384 ALA A O     1 
ATOM   20874 C  CB    . ALA A 1 4384 ? 195.165 169.584 175.912 1.00 35.39  ? 4384 ALA A CB    1 
ATOM   20875 N  N     . SER A 1 4385 ? 198.336 169.007 175.990 1.00 32.94  ? 4385 SER A N     1 
ATOM   20876 C  CA    . SER A 1 4385 ? 199.719 169.474 175.970 1.00 33.02  ? 4385 SER A CA    1 
ATOM   20877 C  C     . SER A 1 4385 ? 200.462 168.934 174.753 1.00 37.77  ? 4385 SER A C     1 
ATOM   20878 O  O     . SER A 1 4385 ? 201.196 169.673 174.082 1.00 38.83  ? 4385 SER A O     1 
ATOM   20879 C  CB    . SER A 1 4385 ? 200.429 169.070 177.261 1.00 30.97  ? 4385 SER A CB    1 
ATOM   20880 O  OG    . SER A 1 4385 ? 199.702 169.509 178.395 1.00 37.91  ? 4385 SER A OG    1 
ATOM   20881 N  N     . ASN A 1 4386 ? 200.266 167.651 174.439 1.00 34.72  ? 4386 ASN A N     1 
ATOM   20882 C  CA    . ASN A 1 4386 ? 200.884 167.092 173.242 1.00 37.09  ? 4386 ASN A CA    1 
ATOM   20883 C  C     . ASN A 1 4386 ? 200.394 167.807 171.989 1.00 40.01  ? 4386 ASN A C     1 
ATOM   20884 O  O     . ASN A 1 4386 ? 201.194 168.159 171.115 1.00 41.88  ? 4386 ASN A O     1 
ATOM   20885 C  CB    . ASN A 1 4386 ? 200.601 165.594 173.156 1.00 37.67  ? 4386 ASN A CB    1 
ATOM   20886 C  CG    . ASN A 1 4386 ? 201.551 164.773 174.002 1.00 47.01  ? 4386 ASN A CG    1 
ATOM   20887 O  OD1   . ASN A 1 4386 ? 201.133 163.876 174.734 1.00 49.61  ? 4386 ASN A OD1   1 
ATOM   20888 N  ND2   . ASN A 1 4386 ? 202.840 165.077 173.907 1.00 54.13  ? 4386 ASN A ND2   1 
ATOM   20889 N  N     . TRP A 1 4387 ? 199.085 168.052 171.898 1.00 38.42  ? 4387 TRP A N     1 
ATOM   20890 C  CA    . TRP A 1 4387 ? 198.536 168.763 170.748 1.00 30.07  ? 4387 TRP A CA    1 
ATOM   20891 C  C     . TRP A 1 4387 ? 199.151 170.148 170.613 1.00 27.69  ? 4387 TRP A C     1 
ATOM   20892 O  O     . TRP A 1 4387 ? 199.545 170.556 169.515 1.00 29.47  ? 4387 TRP A O     1 
ATOM   20893 C  CB    . TRP A 1 4387 ? 197.020 168.865 170.881 1.00 25.15  ? 4387 TRP A CB    1 
ATOM   20894 C  CG    . TRP A 1 4387 ? 196.302 167.616 170.510 1.00 22.58  ? 4387 TRP A CG    1 
ATOM   20895 C  CD1   . TRP A 1 4387 ? 196.794 166.570 169.789 1.00 22.98  ? 4387 TRP A CD1   1 
ATOM   20896 C  CD2   . TRP A 1 4387 ? 194.971 167.257 170.885 1.00 24.57  ? 4387 TRP A CD2   1 
ATOM   20897 N  NE1   . TRP A 1 4387 ? 195.838 165.591 169.667 1.00 28.37  ? 4387 TRP A NE1   1 
ATOM   20898 C  CE2   . TRP A 1 4387 ? 194.711 165.988 170.336 1.00 25.40  ? 4387 TRP A CE2   1 
ATOM   20899 C  CE3   . TRP A 1 4387 ? 193.969 167.890 171.625 1.00 29.12  ? 4387 TRP A CE3   1 
ATOM   20900 C  CZ2   . TRP A 1 4387 ? 193.491 165.342 170.501 1.00 21.65  ? 4387 TRP A CZ2   1 
ATOM   20901 C  CZ3   . TRP A 1 4387 ? 192.762 167.247 171.790 1.00 31.49  ? 4387 TRP A CZ3   1 
ATOM   20902 C  CH2   . TRP A 1 4387 ? 192.534 165.984 171.237 1.00 29.58  ? 4387 TRP A CH2   1 
ATOM   20903 N  N     . LEU A 1 4388 ? 199.256 170.882 171.722 1.00 30.15  ? 4388 LEU A N     1 
ATOM   20904 C  CA    . LEU A 1 4388 ? 199.896 172.191 171.684 1.00 31.13  ? 4388 LEU A CA    1 
ATOM   20905 C  C     . LEU A 1 4388 ? 201.349 172.084 171.246 1.00 36.02  ? 4388 LEU A C     1 
ATOM   20906 O  O     . LEU A 1 4388 ? 201.888 173.022 170.649 1.00 33.69  ? 4388 LEU A O     1 
ATOM   20907 C  CB    . LEU A 1 4388 ? 199.799 172.864 173.052 1.00 26.78  ? 4388 LEU A CB    1 
ATOM   20908 C  CG    . LEU A 1 4388 ? 198.486 173.591 173.346 1.00 21.87  ? 4388 LEU A CG    1 
ATOM   20909 C  CD1   . LEU A 1 4388 ? 198.458 174.097 174.778 1.00 23.54  ? 4388 LEU A CD1   1 
ATOM   20910 C  CD2   . LEU A 1 4388 ? 198.276 174.732 172.366 1.00 20.73  ? 4388 LEU A CD2   1 
ATOM   20911 N  N     . HIS A 1 4389 ? 201.999 170.955 171.537 1.00 40.31  ? 4389 HIS A N     1 
ATOM   20912 C  CA    . HIS A 1 4389 ? 203.376 170.772 171.086 1.00 36.73  ? 4389 HIS A CA    1 
ATOM   20913 C  C     . HIS A 1 4389 ? 203.453 170.529 169.581 1.00 32.46  ? 4389 HIS A C     1 
ATOM   20914 O  O     . HIS A 1 4389 ? 204.298 171.119 168.898 1.00 37.69  ? 4389 HIS A O     1 
ATOM   20915 C  CB    . HIS A 1 4389 ? 204.033 169.628 171.855 1.00 46.68  ? 4389 HIS A CB    1 
ATOM   20916 C  CG    . HIS A 1 4389 ? 204.669 170.056 173.141 1.00 56.15  ? 4389 HIS A CG    1 
ATOM   20917 N  ND1   . HIS A 1 4389 ? 205.500 171.153 173.229 1.00 51.27  ? 4389 HIS A ND1   1 
ATOM   20918 C  CD2   . HIS A 1 4389 ? 204.591 169.542 174.390 1.00 58.25  ? 4389 HIS A CD2   1 
ATOM   20919 C  CE1   . HIS A 1 4389 ? 205.910 171.292 174.476 1.00 57.69  ? 4389 HIS A CE1   1 
ATOM   20920 N  NE2   . HIS A 1 4389 ? 205.374 170.328 175.202 1.00 59.44  ? 4389 HIS A NE2   1 
ATOM   20921 N  N     . LEU A 1 4390 ? 202.589 169.664 169.041 1.00 30.46  ? 4390 LEU A N     1 
ATOM   20922 C  CA    . LEU A 1 4390 ? 202.646 169.368 167.608 1.00 25.28  ? 4390 LEU A CA    1 
ATOM   20923 C  C     . LEU A 1 4390 ? 202.209 170.559 166.762 1.00 28.53  ? 4390 LEU A C     1 
ATOM   20924 O  O     . LEU A 1 4390 ? 202.884 170.918 165.790 1.00 32.95  ? 4390 LEU A O     1 
ATOM   20925 C  CB    . LEU A 1 4390 ? 201.806 168.134 167.267 1.00 24.87  ? 4390 LEU A CB    1 
ATOM   20926 C  CG    . LEU A 1 4390 ? 202.345 166.725 167.555 1.00 36.16  ? 4390 LEU A CG    1 
ATOM   20927 C  CD1   . LEU A 1 4390 ? 202.391 166.370 169.026 1.00 29.61  ? 4390 LEU A CD1   1 
ATOM   20928 C  CD2   . LEU A 1 4390 ? 201.528 165.695 166.787 1.00 36.82  ? 4390 LEU A CD2   1 
ATOM   20929 N  N     . ILE A 1 4391 ? 201.083 171.175 167.099 1.00 27.43  ? 4391 ILE A N     1 
ATOM   20930 C  CA    . ILE A 1 4391 ? 200.576 172.288 166.286 1.00 24.74  ? 4391 ILE A CA    1 
ATOM   20931 C  C     . ILE A 1 4391 ? 201.536 173.467 166.389 1.00 28.49  ? 4391 ILE A C     1 
ATOM   20932 O  O     . ILE A 1 4391 ? 201.974 173.807 167.503 1.00 29.83  ? 4391 ILE A O     1 
ATOM   20933 C  CB    . ILE A 1 4391 ? 199.166 172.678 166.735 1.00 22.73  ? 4391 ILE A CB    1 
ATOM   20934 C  CG1   . ILE A 1 4391 ? 198.285 171.437 166.871 1.00 22.72  ? 4391 ILE A CG1   1 
ATOM   20935 C  CG2   . ILE A 1 4391 ? 198.540 173.648 165.753 1.00 24.36  ? 4391 ILE A CG2   1 
ATOM   20936 C  CD1   . ILE A 1 4391 ? 196.893 171.731 167.374 1.00 21.70  ? 4391 ILE A CD1   1 
ATOM   20937 N  N     . PRO A 1 4392 ? 201.898 174.106 165.275 1.00 23.58  ? 4392 PRO A N     1 
ATOM   20938 C  CA    . PRO A 1 4392 ? 202.855 175.218 165.336 1.00 25.14  ? 4392 PRO A CA    1 
ATOM   20939 C  C     . PRO A 1 4392 ? 202.341 176.367 166.190 1.00 26.01  ? 4392 PRO A C     1 
ATOM   20940 O  O     . PRO A 1 4392 ? 201.138 176.611 166.291 1.00 29.94  ? 4392 PRO A O     1 
ATOM   20941 C  CB    . PRO A 1 4392 ? 203.004 175.636 163.869 1.00 21.53  ? 4392 PRO A CB    1 
ATOM   20942 C  CG    . PRO A 1 4392 ? 202.659 174.409 163.099 1.00 22.29  ? 4392 PRO A CG    1 
ATOM   20943 C  CD    . PRO A 1 4392 ? 201.581 173.729 163.888 1.00 18.57  ? 4392 PRO A CD    1 
ATOM   20944 N  N     . GLN A 1 4393 ? 203.284 177.074 166.817 1.00 23.69  ? 4393 GLN A N     1 
ATOM   20945 C  CA    . GLN A 1 4393 ? 202.920 178.104 167.783 1.00 27.31  ? 4393 GLN A CA    1 
ATOM   20946 C  C     . GLN A 1 4393 ? 202.294 179.321 167.109 1.00 28.58  ? 4393 GLN A C     1 
ATOM   20947 O  O     . GLN A 1 4393 ? 201.328 179.891 167.628 1.00 32.81  ? 4393 GLN A O     1 
ATOM   20948 C  CB    . GLN A 1 4393 ? 204.147 178.511 168.600 1.00 30.22  ? 4393 GLN A CB    1 
ATOM   20949 C  CG    . GLN A 1 4393 ? 204.683 177.404 169.497 1.00 38.45  ? 4393 GLN A CG    1 
ATOM   20950 C  CD    . GLN A 1 4393 ? 206.170 177.538 169.772 1.00 55.10  ? 4393 GLN A CD    1 
ATOM   20951 O  OE1   . GLN A 1 4393 ? 207.002 177.248 168.914 1.00 52.03  ? 4393 GLN A OE1   1 
ATOM   20952 N  NE2   . GLN A 1 4393 ? 206.509 177.979 170.978 1.00 56.57  ? 4393 GLN A NE2   1 
ATOM   20953 N  N     . THR A 1 4394 ? 202.823 179.739 165.961 1.00 28.97  ? 4394 THR A N     1 
ATOM   20954 C  CA    . THR A 1 4394 ? 202.359 180.965 165.328 1.00 27.18  ? 4394 THR A CA    1 
ATOM   20955 C  C     . THR A 1 4394 ? 202.394 180.833 163.813 1.00 25.53  ? 4394 THR A C     1 
ATOM   20956 O  O     . THR A 1 4394 ? 203.109 180.001 163.251 1.00 26.13  ? 4394 THR A O     1 
ATOM   20957 C  CB    . THR A 1 4394 ? 203.196 182.177 165.759 1.00 31.55  ? 4394 THR A CB    1 
ATOM   20958 O  OG1   . THR A 1 4394 ? 202.602 183.376 165.246 1.00 33.11  ? 4394 THR A OG1   1 
ATOM   20959 C  CG2   . THR A 1 4394 ? 204.620 182.058 165.235 1.00 22.79  ? 4394 THR A CG2   1 
ATOM   20960 N  N     . LEU A 1 4395 ? 201.592 181.674 163.162 1.00 25.30  ? 4395 LEU A N     1 
ATOM   20961 C  CA    . LEU A 1 4395 ? 201.587 181.831 161.714 1.00 20.61  ? 4395 LEU A CA    1 
ATOM   20962 C  C     . LEU A 1 4395 ? 201.627 183.318 161.399 1.00 22.85  ? 4395 LEU A C     1 
ATOM   20963 O  O     . LEU A 1 4395 ? 200.859 184.095 161.975 1.00 25.87  ? 4395 LEU A O     1 
ATOM   20964 C  CB    . LEU A 1 4395 ? 200.350 181.180 161.084 1.00 19.17  ? 4395 LEU A CB    1 
ATOM   20965 C  CG    . LEU A 1 4395 ? 200.186 181.326 159.570 1.00 20.07  ? 4395 LEU A CG    1 
ATOM   20966 C  CD1   . LEU A 1 4395 ? 201.441 180.878 158.842 1.00 18.79  ? 4395 LEU A CD1   1 
ATOM   20967 C  CD2   . LEU A 1 4395 ? 198.976 180.544 159.085 1.00 12.36  ? 4395 LEU A CD2   1 
ATOM   20968 N  N     . SER A 1 4396 ? 202.516 183.710 160.491 1.00 25.67  ? 4396 SER A N     1 
ATOM   20969 C  CA    . SER A 1 4396 ? 202.749 185.118 160.196 1.00 27.08  ? 4396 SER A CA    1 
ATOM   20970 C  C     . SER A 1 4396 ? 201.907 185.561 159.006 1.00 25.73  ? 4396 SER A C     1 
ATOM   20971 O  O     . SER A 1 4396 ? 201.904 184.905 157.960 1.00 31.42  ? 4396 SER A O     1 
ATOM   20972 C  CB    . SER A 1 4396 ? 204.231 185.368 159.913 1.00 29.66  ? 4396 SER A CB    1 
ATOM   20973 O  OG    . SER A 1 4396 ? 205.028 185.031 161.034 1.00 32.16  ? 4396 SER A OG    1 
ATOM   20974 N  N     . HIS A 1 4397 ? 201.200 186.676 159.171 1.00 28.70  ? 4397 HIS A N     1 
ATOM   20975 C  CA    . HIS A 1 4397 ? 200.402 187.234 158.089 1.00 28.40  ? 4397 HIS A CA    1 
ATOM   20976 C  C     . HIS A 1 4397 ? 201.296 187.750 156.967 1.00 26.75  ? 4397 HIS A C     1 
ATOM   20977 O  O     . HIS A 1 4397 ? 202.434 188.171 157.190 1.00 32.09  ? 4397 HIS A O     1 
ATOM   20978 C  CB    . HIS A 1 4397 ? 199.517 188.368 158.605 1.00 24.00  ? 4397 HIS A CB    1 
ATOM   20979 C  CG    . HIS A 1 4397 ? 198.221 187.907 159.195 1.00 27.48  ? 4397 HIS A CG    1 
ATOM   20980 N  ND1   . HIS A 1 4397 ? 197.452 188.704 160.015 1.00 25.57  ? 4397 HIS A ND1   1 
ATOM   20981 C  CD2   . HIS A 1 4397 ? 197.558 186.732 159.084 1.00 29.44  ? 4397 HIS A CD2   1 
ATOM   20982 C  CE1   . HIS A 1 4397 ? 196.372 188.040 160.384 1.00 23.84  ? 4397 HIS A CE1   1 
ATOM   20983 N  NE2   . HIS A 1 4397 ? 196.412 186.841 159.833 1.00 27.64  ? 4397 HIS A NE2   1 
ATOM   20984 N  N     . LEU A 1 4398 ? 200.767 187.709 155.748 1.00 27.40  ? 4398 LEU A N     1 
ATOM   20985 C  CA    . LEU A 1 4398 ? 201.501 188.215 154.597 1.00 27.78  ? 4398 LEU A CA    1 
ATOM   20986 C  C     . LEU A 1 4398 ? 201.531 189.738 154.611 1.00 38.01  ? 4398 LEU A C     1 
ATOM   20987 O  O     . LEU A 1 4398 ? 200.510 190.394 154.836 1.00 42.84  ? 4398 LEU A O     1 
ATOM   20988 C  CB    . LEU A 1 4398 ? 200.864 187.716 153.302 1.00 26.06  ? 4398 LEU A CB    1 
ATOM   20989 C  CG    . LEU A 1 4398 ? 200.912 186.210 153.044 1.00 23.61  ? 4398 LEU A CG    1 
ATOM   20990 C  CD1   . LEU A 1 4398 ? 200.584 185.904 151.592 1.00 25.21  ? 4398 LEU A CD1   1 
ATOM   20991 C  CD2   . LEU A 1 4398 ? 202.270 185.650 153.418 1.00 25.04  ? 4398 LEU A CD2   1 
ATOM   20992 N  N     . LYS A 1 4399 ? 202.712 190.301 154.367 1.00 41.06  ? 4399 LYS A N     1 
ATOM   20993 C  CA    . LYS A 1 4399 ? 202.851 191.750 154.326 1.00 44.48  ? 4399 LYS A CA    1 
ATOM   20994 C  C     . LYS A 1 4399 ? 202.176 192.305 153.078 1.00 46.83  ? 4399 LYS A C     1 
ATOM   20995 O  O     . LYS A 1 4399 ? 202.371 191.792 151.972 1.00 44.92  ? 4399 LYS A O     1 
ATOM   20996 C  CB    . LYS A 1 4399 ? 204.326 192.145 154.351 1.00 46.81  ? 4399 LYS A CB    1 
ATOM   20997 C  CG    . LYS A 1 4399 ? 205.054 191.756 155.627 1.00 48.95  ? 4399 LYS A CG    1 
ATOM   20998 C  CD    . LYS A 1 4399 ? 206.494 192.242 155.606 1.00 53.48  ? 4399 LYS A CD    1 
ATOM   20999 C  CE    . LYS A 1 4399 ? 207.328 191.463 154.600 1.00 50.42  ? 4399 LYS A CE    1 
ATOM   21000 N  NZ    . LYS A 1 4399 ? 207.482 190.033 154.987 1.00 40.80  ? 4399 LYS A NZ    1 
ATOM   21001 N  N     . ARG A 1 4400 ? 201.384 193.358 153.257 1.00 49.96  ? 4400 ARG A N     1 
ATOM   21002 C  CA    . ARG A 1 4400 ? 200.666 193.982 152.157 1.00 41.22  ? 4400 ARG A CA    1 
ATOM   21003 C  C     . ARG A 1 4400 ? 201.526 195.056 151.506 1.00 49.54  ? 4400 ARG A C     1 
ATOM   21004 O  O     . ARG A 1 4400 ? 202.184 195.844 152.191 1.00 55.30  ? 4400 ARG A O     1 
ATOM   21005 C  CB    . ARG A 1 4400 ? 199.352 194.591 152.648 1.00 46.24  ? 4400 ARG A CB    1 
ATOM   21006 C  CG    . ARG A 1 4400 ? 198.191 193.615 152.682 1.00 44.45  ? 4400 ARG A CG    1 
ATOM   21007 C  CD    . ARG A 1 4400 ? 196.859 194.339 152.577 1.00 43.86  ? 4400 ARG A CD    1 
ATOM   21008 N  NE    . ARG A 1 4400 ? 195.789 193.450 152.142 1.00 45.69  ? 4400 ARG A NE    1 
ATOM   21009 C  CZ    . ARG A 1 4400 ? 194.638 193.859 151.627 1.00 45.04  ? 4400 ARG A CZ    1 
ATOM   21010 N  NH1   . ARG A 1 4400 ? 194.371 195.145 151.465 1.00 43.63  ? 4400 ARG A NH1   1 
ATOM   21011 N  NH2   . ARG A 1 4400 ? 193.731 192.956 151.267 1.00 41.64  ? 4400 ARG A NH2   1 
ATOM   21012 N  N     . THR A 1 4401 ? 201.515 195.081 150.176 1.00 53.00  ? 4401 THR A N     1 
ATOM   21013 C  CA    . THR A 1 4401 ? 202.293 196.033 149.400 1.00 53.07  ? 4401 THR A CA    1 
ATOM   21014 C  C     . THR A 1 4401 ? 201.438 196.505 148.228 1.00 57.06  ? 4401 THR A C     1 
ATOM   21015 O  O     . THR A 1 4401 ? 200.518 195.809 147.791 1.00 62.79  ? 4401 THR A O     1 
ATOM   21016 C  CB    . THR A 1 4401 ? 203.612 195.399 148.924 1.00 52.68  ? 4401 THR A CB    1 
ATOM   21017 O  OG1   . THR A 1 4401 ? 204.358 194.957 150.065 1.00 55.24  ? 4401 THR A OG1   1 
ATOM   21018 C  CG2   . THR A 1 4401 ? 204.468 196.403 148.183 1.00 51.22  ? 4401 THR A CG2   1 
ATOM   21019 N  N     . VAL A 1 4402 ? 201.738 197.710 147.732 1.00 57.05  ? 4402 VAL A N     1 
ATOM   21020 C  CA    . VAL A 1 4402 ? 200.882 198.339 146.728 1.00 59.13  ? 4402 VAL A CA    1 
ATOM   21021 C  C     . VAL A 1 4402 ? 200.822 197.503 145.452 1.00 61.58  ? 4402 VAL A C     1 
ATOM   21022 O  O     . VAL A 1 4402 ? 199.764 197.395 144.819 1.00 62.33  ? 4402 VAL A O     1 
ATOM   21023 C  CB    . VAL A 1 4402 ? 201.344 199.784 146.453 1.00 58.28  ? 4402 VAL A CB    1 
ATOM   21024 C  CG1   . VAL A 1 4402 ? 201.214 200.621 147.714 1.00 56.41  ? 4402 VAL A CG1   1 
ATOM   21025 C  CG2   . VAL A 1 4402 ? 202.776 199.815 145.957 1.00 56.05  ? 4402 VAL A CG2   1 
ATOM   21026 N  N     . GLU A 1 4403 ? 201.943 196.899 145.048 1.00 58.98  ? 4403 GLU A N     1 
ATOM   21027 C  CA    . GLU A 1 4403 ? 201.902 196.032 143.876 1.00 57.03  ? 4403 GLU A CA    1 
ATOM   21028 C  C     . GLU A 1 4403 ? 201.495 194.603 144.212 1.00 51.85  ? 4403 GLU A C     1 
ATOM   21029 O  O     . GLU A 1 4403 ? 201.242 193.815 143.294 1.00 54.09  ? 4403 GLU A O     1 
ATOM   21030 C  CB    . GLU A 1 4403 ? 203.251 196.020 143.146 1.00 52.91  ? 4403 GLU A CB    1 
ATOM   21031 C  CG    . GLU A 1 4403 ? 204.388 195.337 143.886 1.00 58.23  ? 4403 GLU A CG    1 
ATOM   21032 C  CD    . GLU A 1 4403 ? 205.101 196.260 144.848 1.00 67.69  ? 4403 GLU A CD    1 
ATOM   21033 O  OE1   . GLU A 1 4403 ? 204.550 197.332 145.163 1.00 69.27  ? 4403 GLU A OE1   1 
ATOM   21034 O  OE2   . GLU A 1 4403 ? 206.214 195.911 145.293 1.00 74.59  ? 4403 GLU A OE2   1 
ATOM   21035 N  N     . ASN A 1 4404 ? 201.430 194.247 145.496 1.00 47.68  ? 4404 ASN A N     1 
ATOM   21036 C  CA    . ASN A 1 4404 ? 200.962 192.918 145.873 1.00 42.87  ? 4404 ASN A CA    1 
ATOM   21037 C  C     . ASN A 1 4404 ? 199.448 192.792 145.773 1.00 41.37  ? 4404 ASN A C     1 
ATOM   21038 O  O     . ASN A 1 4404 ? 198.939 191.700 145.498 1.00 40.03  ? 4404 ASN A O     1 
ATOM   21039 C  CB    . ASN A 1 4404 ? 201.412 192.577 147.295 1.00 41.84  ? 4404 ASN A CB    1 
ATOM   21040 C  CG    . ASN A 1 4404 ? 202.878 192.213 147.372 1.00 49.99  ? 4404 ASN A CG    1 
ATOM   21041 O  OD1   . ASN A 1 4404 ? 203.541 192.038 146.349 1.00 56.50  ? 4404 ASN A OD1   1 
ATOM   21042 N  ND2   . ASN A 1 4404 ? 203.392 192.083 148.589 1.00 43.85  ? 4404 ASN A ND2   1 
ATOM   21043 N  N     . ILE A 1 4405 ? 198.720 193.890 145.989 1.00 46.60  ? 4405 ILE A N     1 
ATOM   21044 C  CA    . ILE A 1 4405 ? 197.261 193.831 146.044 1.00 43.24  ? 4405 ILE A CA    1 
ATOM   21045 C  C     . ILE A 1 4405 ? 196.686 193.420 144.694 1.00 38.48  ? 4405 ILE A C     1 
ATOM   21046 O  O     . ILE A 1 4405 ? 195.717 192.655 144.622 1.00 44.15  ? 4405 ILE A O     1 
ATOM   21047 C  CB    . ILE A 1 4405 ? 196.695 195.183 146.518 1.00 51.02  ? 4405 ILE A CB    1 
ATOM   21048 C  CG1   . ILE A 1 4405 ? 197.141 195.478 147.952 1.00 49.86  ? 4405 ILE A CG1   1 
ATOM   21049 C  CG2   . ILE A 1 4405 ? 195.177 195.197 146.423 1.00 52.72  ? 4405 ILE A CG2   1 
ATOM   21050 C  CD1   . ILE A 1 4405 ? 197.112 194.273 148.870 1.00 45.01  ? 4405 ILE A CD1   1 
ATOM   21051 N  N     . LYS A 1 4406 ? 197.276 193.911 143.603 1.00 39.74  ? 4406 LYS A N     1 
ATOM   21052 C  CA    . LYS A 1 4406 ? 196.754 193.616 142.275 1.00 42.65  ? 4406 LYS A CA    1 
ATOM   21053 C  C     . LYS A 1 4406 ? 196.987 192.168 141.854 1.00 44.95  ? 4406 LYS A C     1 
ATOM   21054 O  O     . LYS A 1 4406 ? 196.405 191.727 140.858 1.00 42.91  ? 4406 LYS A O     1 
ATOM   21055 C  CB    . LYS A 1 4406 ? 197.378 194.561 141.247 1.00 46.52  ? 4406 LYS A CB    1 
ATOM   21056 C  CG    . LYS A 1 4406 ? 197.132 196.035 141.529 1.00 52.91  ? 4406 LYS A CG    1 
ATOM   21057 C  CD    . LYS A 1 4406 ? 197.973 196.917 140.621 1.00 66.40  ? 4406 LYS A CD    1 
ATOM   21058 C  CE    . LYS A 1 4406 ? 198.319 198.235 141.294 1.00 68.79  ? 4406 LYS A CE    1 
ATOM   21059 N  NZ    . LYS A 1 4406 ? 198.637 198.055 142.737 1.00 65.62  ? 4406 LYS A NZ    1 
ATOM   21060 N  N     . ASP A 1 4407 ? 197.815 191.427 142.576 1.00 41.26  ? 4407 ASP A N     1 
ATOM   21061 C  CA    . ASP A 1 4407 ? 198.105 190.043 142.211 1.00 29.92  ? 4407 ASP A CA    1 
ATOM   21062 C  C     . ASP A 1 4407 ? 197.028 189.113 142.755 1.00 31.77  ? 4407 ASP A C     1 
ATOM   21063 O  O     . ASP A 1 4407 ? 196.842 189.046 143.977 1.00 28.58  ? 4407 ASP A O     1 
ATOM   21064 C  CB    . ASP A 1 4407 ? 199.476 189.642 142.744 1.00 31.47  ? 4407 ASP A CB    1 
ATOM   21065 C  CG    . ASP A 1 4407 ? 199.811 188.191 142.466 1.00 34.09  ? 4407 ASP A CG    1 
ATOM   21066 O  OD1   . ASP A 1 4407 ? 199.366 187.660 141.428 1.00 34.23  ? 4407 ASP A OD1   1 
ATOM   21067 O  OD2   . ASP A 1 4407 ? 200.522 187.580 143.290 1.00 38.36  ? 4407 ASP A OD2   1 
ATOM   21068 N  N     . PRO A 1 4408 ? 196.293 188.392 141.901 1.00 30.84  ? 4408 PRO A N     1 
ATOM   21069 C  CA    . PRO A 1 4408 ? 195.291 187.450 142.430 1.00 28.50  ? 4408 PRO A CA    1 
ATOM   21070 C  C     . PRO A 1 4408 ? 195.893 186.337 143.267 1.00 23.70  ? 4408 PRO A C     1 
ATOM   21071 O  O     . PRO A 1 4408 ? 195.276 185.901 144.250 1.00 24.92  ? 4408 PRO A O     1 
ATOM   21072 C  CB    . PRO A 1 4408 ? 194.614 186.914 141.159 1.00 25.42  ? 4408 PRO A CB    1 
ATOM   21073 C  CG    . PRO A 1 4408 ? 195.619 187.120 140.077 1.00 22.30  ? 4408 PRO A CG    1 
ATOM   21074 C  CD    . PRO A 1 4408 ? 196.357 188.373 140.431 1.00 28.51  ? 4408 PRO A CD    1 
ATOM   21075 N  N     . LEU A 1 4409 ? 197.087 185.862 142.904 1.00 25.78  ? 4409 LEU A N     1 
ATOM   21076 C  CA    . LEU A 1 4409 ? 197.749 184.835 143.701 1.00 24.20  ? 4409 LEU A CA    1 
ATOM   21077 C  C     . LEU A 1 4409 ? 198.042 185.340 145.105 1.00 22.04  ? 4409 LEU A C     1 
ATOM   21078 O  O     . LEU A 1 4409 ? 197.827 184.623 146.092 1.00 22.16  ? 4409 LEU A O     1 
ATOM   21079 C  CB    . LEU A 1 4409 ? 199.040 184.390 143.017 1.00 20.84  ? 4409 LEU A CB    1 
ATOM   21080 C  CG    . LEU A 1 4409 ? 198.936 183.319 141.932 1.00 19.85  ? 4409 LEU A CG    1 
ATOM   21081 C  CD1   . LEU A 1 4409 ? 200.317 182.980 141.406 1.00 20.91  ? 4409 LEU A CD1   1 
ATOM   21082 C  CD2   . LEU A 1 4409 ? 198.240 182.079 142.462 1.00 20.56  ? 4409 LEU A CD2   1 
ATOM   21083 N  N     . PHE A 1 4410 ? 198.532 186.577 145.215 1.00 23.44  ? 4410 PHE A N     1 
ATOM   21084 C  CA    . PHE A 1 4410 ? 198.814 187.134 146.530 1.00 21.37  ? 4410 PHE A CA    1 
ATOM   21085 C  C     . PHE A 1 4410 ? 197.536 187.303 147.337 1.00 21.23  ? 4410 PHE A C     1 
ATOM   21086 O  O     . PHE A 1 4410 ? 197.534 187.079 148.548 1.00 26.79  ? 4410 PHE A O     1 
ATOM   21087 C  CB    . PHE A 1 4410 ? 199.548 188.469 146.410 1.00 25.20  ? 4410 PHE A CB    1 
ATOM   21088 C  CG    . PHE A 1 4410 ? 199.746 189.162 147.729 1.00 29.81  ? 4410 PHE A CG    1 
ATOM   21089 C  CD1   . PHE A 1 4410 ? 200.817 188.830 148.541 1.00 34.90  ? 4410 PHE A CD1   1 
ATOM   21090 C  CD2   . PHE A 1 4410 ? 198.857 190.129 148.167 1.00 30.13  ? 4410 PHE A CD2   1 
ATOM   21091 C  CE1   . PHE A 1 4410 ? 201.002 189.454 149.758 1.00 34.22  ? 4410 PHE A CE1   1 
ATOM   21092 C  CE2   . PHE A 1 4410 ? 199.037 190.755 149.382 1.00 33.84  ? 4410 PHE A CE2   1 
ATOM   21093 C  CZ    . PHE A 1 4410 ? 200.111 190.418 150.178 1.00 37.12  ? 4410 PHE A CZ    1 
ATOM   21094 N  N     . ARG A 1 4411 ? 196.442 187.716 146.692 1.00 19.72  ? 4411 ARG A N     1 
ATOM   21095 C  CA    . ARG A 1 4411 ? 195.180 187.847 147.414 1.00 17.94  ? 4411 ARG A CA    1 
ATOM   21096 C  C     . ARG A 1 4411 ? 194.705 186.502 147.946 1.00 17.91  ? 4411 ARG A C     1 
ATOM   21097 O  O     . ARG A 1 4411 ? 194.289 186.395 149.109 1.00 19.71  ? 4411 ARG A O     1 
ATOM   21098 C  CB    . ARG A 1 4411 ? 194.109 188.469 146.518 1.00 21.55  ? 4411 ARG A CB    1 
ATOM   21099 C  CG    . ARG A 1 4411 ? 194.356 189.919 146.146 1.00 24.06  ? 4411 ARG A CG    1 
ATOM   21100 C  CD    . ARG A 1 4411 ? 193.239 190.438 145.259 1.00 23.16  ? 4411 ARG A CD    1 
ATOM   21101 N  NE    . ARG A 1 4411 ? 193.443 191.825 144.861 1.00 39.92  ? 4411 ARG A NE    1 
ATOM   21102 C  CZ    . ARG A 1 4411 ? 192.641 192.493 144.045 1.00 41.93  ? 4411 ARG A CZ    1 
ATOM   21103 N  NH1   . ARG A 1 4411 ? 191.573 191.926 143.509 1.00 35.11  ? 4411 ARG A NH1   1 
ATOM   21104 N  NH2   . ARG A 1 4411 ? 192.916 193.763 143.760 1.00 43.87  ? 4411 ARG A NH2   1 
ATOM   21105 N  N     . PHE A 1 4412 ? 194.766 185.459 147.113 1.00 18.75  ? 4412 PHE A N     1 
ATOM   21106 C  CA    . PHE A 1 4412 ? 194.341 184.139 147.565 1.00 16.25  ? 4412 PHE A CA    1 
ATOM   21107 C  C     . PHE A 1 4412 ? 195.202 183.660 148.725 1.00 16.85  ? 4412 PHE A C     1 
ATOM   21108 O  O     . PHE A 1 4412 ? 194.688 183.156 149.732 1.00 17.57  ? 4412 PHE A O     1 
ATOM   21109 C  CB    . PHE A 1 4412 ? 194.397 183.132 146.418 1.00 16.64  ? 4412 PHE A CB    1 
ATOM   21110 C  CG    . PHE A 1 4412 ? 194.358 181.704 146.879 1.00 15.78  ? 4412 PHE A CG    1 
ATOM   21111 C  CD1   . PHE A 1 4412 ? 193.160 181.124 147.260 1.00 18.73  ? 4412 PHE A CD1   1 
ATOM   21112 C  CD2   . PHE A 1 4412 ? 195.516 180.951 146.962 1.00 16.36  ? 4412 PHE A CD2   1 
ATOM   21113 C  CE1   . PHE A 1 4412 ? 193.116 179.819 147.697 1.00 17.30  ? 4412 PHE A CE1   1 
ATOM   21114 C  CE2   . PHE A 1 4412 ? 195.476 179.647 147.403 1.00 18.44  ? 4412 PHE A CE2   1 
ATOM   21115 C  CZ    . PHE A 1 4412 ? 194.274 179.080 147.771 1.00 19.87  ? 4412 PHE A CZ    1 
ATOM   21116 N  N     . PHE A 1 4413 ? 196.523 183.811 148.602 1.00 18.05  ? 4413 PHE A N     1 
ATOM   21117 C  CA    . PHE A 1 4413 ? 197.407 183.335 149.659 1.00 15.74  ? 4413 PHE A CA    1 
ATOM   21118 C  C     . PHE A 1 4413 ? 197.264 184.165 150.927 1.00 17.59  ? 4413 PHE A C     1 
ATOM   21119 O  O     . PHE A 1 4413 ? 197.370 183.622 152.029 1.00 23.20  ? 4413 PHE A O     1 
ATOM   21120 C  CB    . PHE A 1 4413 ? 198.854 183.327 149.170 1.00 17.47  ? 4413 PHE A CB    1 
ATOM   21121 C  CG    . PHE A 1 4413 ? 199.190 182.139 148.315 1.00 20.84  ? 4413 PHE A CG    1 
ATOM   21122 C  CD1   . PHE A 1 4413 ? 198.887 180.858 148.742 1.00 20.71  ? 4413 PHE A CD1   1 
ATOM   21123 C  CD2   . PHE A 1 4413 ? 199.802 182.302 147.086 1.00 23.24  ? 4413 PHE A CD2   1 
ATOM   21124 C  CE1   . PHE A 1 4413 ? 199.189 179.763 147.960 1.00 21.47  ? 4413 PHE A CE1   1 
ATOM   21125 C  CE2   . PHE A 1 4413 ? 200.107 181.210 146.300 1.00 24.61  ? 4413 PHE A CE2   1 
ATOM   21126 C  CZ    . PHE A 1 4413 ? 199.800 179.939 146.738 1.00 26.18  ? 4413 PHE A CZ    1 
ATOM   21127 N  N     . GLU A 1 4414 ? 197.008 185.468 150.798 1.00 17.93  ? 4414 GLU A N     1 
ATOM   21128 C  CA    . GLU A 1 4414 ? 196.757 186.295 151.971 1.00 18.10  ? 4414 GLU A CA    1 
ATOM   21129 C  C     . GLU A 1 4414 ? 195.499 185.851 152.699 1.00 18.89  ? 4414 GLU A C     1 
ATOM   21130 O  O     . GLU A 1 4414 ? 195.494 185.751 153.930 1.00 19.36  ? 4414 GLU A O     1 
ATOM   21131 C  CB    . GLU A 1 4414 ? 196.640 187.764 151.567 1.00 17.19  ? 4414 GLU A CB    1 
ATOM   21132 C  CG    . GLU A 1 4414 ? 196.455 188.704 152.746 1.00 27.83  ? 4414 GLU A CG    1 
ATOM   21133 C  CD    . GLU A 1 4414 ? 196.387 190.159 152.332 1.00 46.18  ? 4414 GLU A CD    1 
ATOM   21134 O  OE1   . GLU A 1 4414 ? 196.461 190.438 151.118 1.00 56.59  ? 4414 GLU A OE1   1 
ATOM   21135 O  OE2   . GLU A 1 4414 ? 196.254 191.024 153.223 1.00 47.09  ? 4414 GLU A OE2   1 
ATOM   21136 N  N     . ARG A 1 4415 ? 194.418 185.587 151.959 1.00 16.30  ? 4415 ARG A N     1 
ATOM   21137 C  CA    . ARG A 1 4415 ? 193.200 185.111 152.608 1.00 15.80  ? 4415 ARG A CA    1 
ATOM   21138 C  C     . ARG A 1 4415 ? 193.425 183.755 153.266 1.00 19.07  ? 4415 ARG A C     1 
ATOM   21139 O  O     . ARG A 1 4415 ? 192.947 183.509 154.382 1.00 21.45  ? 4415 ARG A O     1 
ATOM   21140 C  CB    . ARG A 1 4415 ? 192.053 185.038 151.602 1.00 16.76  ? 4415 ARG A CB    1 
ATOM   21141 C  CG    . ARG A 1 4415 ? 190.723 184.670 152.234 1.00 15.34  ? 4415 ARG A CG    1 
ATOM   21142 C  CD    . ARG A 1 4415 ? 189.570 184.849 151.266 1.00 19.35  ? 4415 ARG A CD    1 
ATOM   21143 N  NE    . ARG A 1 4415 ? 189.571 183.845 150.211 1.00 18.57  ? 4415 ARG A NE    1 
ATOM   21144 C  CZ    . ARG A 1 4415 ? 188.726 183.835 149.190 1.00 21.61  ? 4415 ARG A CZ    1 
ATOM   21145 N  NH1   . ARG A 1 4415 ? 187.802 184.770 149.050 1.00 26.00  ? 4415 ARG A NH1   1 
ATOM   21146 N  NH2   . ARG A 1 4415 ? 188.811 182.864 148.286 1.00 26.57  ? 4415 ARG A NH2   1 
ATOM   21147 N  N     . GLU A 1 4416 ? 194.160 182.867 152.592 1.00 16.73  ? 4416 GLU A N     1 
ATOM   21148 C  CA    . GLU A 1 4416 ? 194.471 181.564 153.170 1.00 14.56  ? 4416 GLU A CA    1 
ATOM   21149 C  C     . GLU A 1 4416 ? 195.252 181.715 154.467 1.00 17.57  ? 4416 GLU A C     1 
ATOM   21150 O  O     . GLU A 1 4416 ? 194.948 181.059 155.470 1.00 21.73  ? 4416 GLU A O     1 
ATOM   21151 C  CB    . GLU A 1 4416 ? 195.263 180.726 152.166 1.00 18.51  ? 4416 GLU A CB    1 
ATOM   21152 C  CG    . GLU A 1 4416 ? 194.417 180.069 151.093 1.00 26.71  ? 4416 GLU A CG    1 
ATOM   21153 C  CD    . GLU A 1 4416 ? 193.613 178.900 151.617 1.00 27.31  ? 4416 GLU A CD    1 
ATOM   21154 O  OE1   . GLU A 1 4416 ? 192.384 178.876 151.402 1.00 26.42  ? 4416 GLU A OE1   1 
ATOM   21155 O  OE2   . GLU A 1 4416 ? 194.213 178.001 152.241 1.00 30.67  ? 4416 GLU A OE2   1 
ATOM   21156 N  N     . VAL A 1 4417 ? 196.259 182.589 154.468 1.00 16.75  ? 4417 VAL A N     1 
ATOM   21157 C  CA    . VAL A 1 4417 ? 197.085 182.780 155.653 1.00 14.55  ? 4417 VAL A CA    1 
ATOM   21158 C  C     . VAL A 1 4417 ? 196.274 183.407 156.779 1.00 15.89  ? 4417 VAL A C     1 
ATOM   21159 O  O     . VAL A 1 4417 ? 196.433 183.040 157.945 1.00 18.25  ? 4417 VAL A O     1 
ATOM   21160 C  CB    . VAL A 1 4417 ? 198.330 183.617 155.304 1.00 16.60  ? 4417 VAL A CB    1 
ATOM   21161 C  CG1   . VAL A 1 4417 ? 199.037 184.079 156.567 1.00 20.76  ? 4417 VAL A CG1   1 
ATOM   21162 C  CG2   . VAL A 1 4417 ? 199.278 182.808 154.439 1.00 13.21  ? 4417 VAL A CG2   1 
ATOM   21163 N  N     . LYS A 1 4418 ? 195.393 184.356 156.457 1.00 15.55  ? 4418 LYS A N     1 
ATOM   21164 C  CA    . LYS A 1 4418 ? 194.574 184.975 157.495 1.00 13.65  ? 4418 LYS A CA    1 
ATOM   21165 C  C     . LYS A 1 4418 ? 193.629 183.963 158.131 1.00 15.97  ? 4418 LYS A C     1 
ATOM   21166 O  O     . LYS A 1 4418 ? 193.504 183.902 159.361 1.00 18.07  ? 4418 LYS A O     1 
ATOM   21167 C  CB    . LYS A 1 4418 ? 193.790 186.158 156.927 1.00 18.40  ? 4418 LYS A CB    1 
ATOM   21168 C  CG    . LYS A 1 4418 ? 194.648 187.336 156.501 1.00 19.52  ? 4418 LYS A CG    1 
ATOM   21169 C  CD    . LYS A 1 4418 ? 193.784 188.522 156.107 1.00 23.06  ? 4418 LYS A CD    1 
ATOM   21170 C  CE    . LYS A 1 4418 ? 193.118 188.294 154.762 1.00 25.65  ? 4418 LYS A CE    1 
ATOM   21171 N  NZ    . LYS A 1 4418 ? 192.356 189.488 154.309 1.00 27.73  ? 4418 LYS A NZ    1 
ATOM   21172 N  N     . MET A 1 4419 ? 192.952 183.156 157.307 1.00 18.77  ? 4419 MET A N     1 
ATOM   21173 C  CA    . MET A 1 4419 ? 192.064 182.137 157.861 1.00 15.39  ? 4419 MET A CA    1 
ATOM   21174 C  C     . MET A 1 4419 ? 192.838 181.115 158.682 1.00 16.36  ? 4419 MET A C     1 
ATOM   21175 O  O     . MET A 1 4419 ? 192.400 180.727 159.774 1.00 16.00  ? 4419 MET A O     1 
ATOM   21176 C  CB    . MET A 1 4419 ? 191.278 181.450 156.744 1.00 16.02  ? 4419 MET A CB    1 
ATOM   21177 C  CG    . MET A 1 4419 ? 190.391 182.386 155.945 1.00 20.64  ? 4419 MET A CG    1 
ATOM   21178 S  SD    . MET A 1 4419 ? 189.602 181.589 154.535 1.00 55.22  ? 4419 MET A SD    1 
ATOM   21179 C  CE    . MET A 1 4419 ? 190.957 180.613 153.895 1.00 26.56  ? 4419 MET A CE    1 
ATOM   21180 N  N     . GLY A 1 4420 ? 193.997 180.680 158.182 1.00 16.90  ? 4420 GLY A N     1 
ATOM   21181 C  CA    . GLY A 1 4420 ? 194.804 179.733 158.929 1.00 13.56  ? 4420 GLY A CA    1 
ATOM   21182 C  C     . GLY A 1 4420 ? 195.290 180.293 160.250 1.00 14.07  ? 4420 GLY A C     1 
ATOM   21183 O  O     . GLY A 1 4420 ? 195.275 179.601 161.266 1.00 20.44  ? 4420 GLY A O     1 
ATOM   21184 N  N     . ALA A 1 4421 ? 195.716 181.557 160.257 1.00 10.56  ? 4421 ALA A N     1 
ATOM   21185 C  CA    . ALA A 1 4421 ? 196.191 182.178 161.488 1.00 12.16  ? 4421 ALA A CA    1 
ATOM   21186 C  C     . ALA A 1 4421 ? 195.062 182.347 162.494 1.00 13.57  ? 4421 ALA A C     1 
ATOM   21187 O  O     . ALA A 1 4421 ? 195.254 182.109 163.692 1.00 17.52  ? 4421 ALA A O     1 
ATOM   21188 C  CB    . ALA A 1 4421 ? 196.840 183.526 161.178 1.00 12.14  ? 4421 ALA A CB    1 
ATOM   21189 N  N     . LYS A 1 4422 ? 193.880 182.760 162.033 1.00 13.01  ? 4422 LYS A N     1 
ATOM   21190 C  CA    . LYS A 1 4422 ? 192.754 182.914 162.948 1.00 12.75  ? 4422 LYS A CA    1 
ATOM   21191 C  C     . LYS A 1 4422 ? 192.348 181.574 163.548 1.00 17.28  ? 4422 LYS A C     1 
ATOM   21192 O  O     . LYS A 1 4422 ? 192.141 181.464 164.765 1.00 17.48  ? 4422 LYS A O     1 
ATOM   21193 C  CB    . LYS A 1 4422 ? 191.576 183.566 162.226 1.00 12.90  ? 4422 LYS A CB    1 
ATOM   21194 C  CG    . LYS A 1 4422 ? 190.373 183.823 163.113 1.00 20.21  ? 4422 LYS A CG    1 
ATOM   21195 C  CD    . LYS A 1 4422 ? 189.285 184.572 162.365 1.00 25.79  ? 4422 LYS A CD    1 
ATOM   21196 C  CE    . LYS A 1 4422 ? 188.026 184.699 163.206 1.00 44.93  ? 4422 LYS A CE    1 
ATOM   21197 N  NZ    . LYS A 1 4422 ? 188.246 185.555 164.405 1.00 43.86  ? 4422 LYS A NZ    1 
ATOM   21198 N  N     . LEU A 1 4423 ? 192.250 180.534 162.714 1.00 17.35  ? 4423 LEU A N     1 
ATOM   21199 C  CA    . LEU A 1 4423 ? 191.902 179.214 163.226 1.00 13.20  ? 4423 LEU A CA    1 
ATOM   21200 C  C     . LEU A 1 4423 ? 192.984 178.674 164.153 1.00 14.11  ? 4423 LEU A C     1 
ATOM   21201 O  O     . LEU A 1 4423 ? 192.679 178.033 165.163 1.00 18.89  ? 4423 LEU A O     1 
ATOM   21202 C  CB    . LEU A 1 4423 ? 191.648 178.249 162.070 1.00 17.65  ? 4423 LEU A CB    1 
ATOM   21203 C  CG    . LEU A 1 4423 ? 191.042 176.905 162.474 1.00 18.79  ? 4423 LEU A CG    1 
ATOM   21204 C  CD1   . LEU A 1 4423 ? 189.805 177.115 163.322 1.00 16.21  ? 4423 LEU A CD1   1 
ATOM   21205 C  CD2   . LEU A 1 4423 ? 190.704 176.085 161.241 1.00 20.10  ? 4423 LEU A CD2   1 
ATOM   21206 N  N     . LEU A 1 4424 ? 194.254 178.917 163.823 1.00 13.50  ? 4424 LEU A N     1 
ATOM   21207 C  CA    . LEU A 1 4424 ? 195.346 178.462 164.673 1.00 14.69  ? 4424 LEU A CA    1 
ATOM   21208 C  C     . LEU A 1 4424 ? 195.293 179.133 166.036 1.00 17.15  ? 4424 LEU A C     1 
ATOM   21209 O  O     . LEU A 1 4424 ? 195.453 178.472 167.068 1.00 20.37  ? 4424 LEU A O     1 
ATOM   21210 C  CB    . LEU A 1 4424 ? 196.683 178.737 163.986 1.00 13.31  ? 4424 LEU A CB    1 
ATOM   21211 C  CG    . LEU A 1 4424 ? 197.942 178.616 164.840 1.00 18.30  ? 4424 LEU A CG    1 
ATOM   21212 C  CD1   . LEU A 1 4424 ? 198.132 177.182 165.281 1.00 19.64  ? 4424 LEU A CD1   1 
ATOM   21213 C  CD2   . LEU A 1 4424 ? 199.157 179.108 164.076 1.00 19.57  ? 4424 LEU A CD2   1 
ATOM   21214 N  N     . GLN A 1 4425 ? 195.057 180.446 166.059 1.00 17.68  ? 4425 GLN A N     1 
ATOM   21215 C  CA    . GLN A 1 4425 ? 194.941 181.153 167.327 1.00 16.89  ? 4425 GLN A CA    1 
ATOM   21216 C  C     . GLN A 1 4425 ? 193.758 180.638 168.136 1.00 17.14  ? 4425 GLN A C     1 
ATOM   21217 O  O     . GLN A 1 4425 ? 193.876 180.420 169.347 1.00 16.60  ? 4425 GLN A O     1 
ATOM   21218 C  CB    . GLN A 1 4425 ? 194.817 182.655 167.075 1.00 17.17  ? 4425 GLN A CB    1 
ATOM   21219 C  CG    . GLN A 1 4425 ? 194.887 183.506 168.328 1.00 18.78  ? 4425 GLN A CG    1 
ATOM   21220 C  CD    . GLN A 1 4425 ? 194.275 184.876 168.131 1.00 25.38  ? 4425 GLN A CD    1 
ATOM   21221 O  OE1   . GLN A 1 4425 ? 193.074 185.004 167.900 1.00 32.75  ? 4425 GLN A OE1   1 
ATOM   21222 N  NE2   . GLN A 1 4425 ? 195.101 185.911 168.222 1.00 25.08  ? 4425 GLN A NE2   1 
ATOM   21223 N  N     . ASP A 1 4426 ? 192.615 180.417 167.481 1.00 18.04  ? 4426 ASP A N     1 
ATOM   21224 C  CA    . ASP A 1 4426 ? 191.441 179.922 168.196 1.00 20.73  ? 4426 ASP A CA    1 
ATOM   21225 C  C     . ASP A 1 4426 ? 191.691 178.538 168.785 1.00 21.22  ? 4426 ASP A C     1 
ATOM   21226 O  O     . ASP A 1 4426 ? 191.372 178.279 169.952 1.00 23.20  ? 4426 ASP A O     1 
ATOM   21227 C  CB    . ASP A 1 4426 ? 190.231 179.899 167.262 1.00 18.78  ? 4426 ASP A CB    1 
ATOM   21228 C  CG    . ASP A 1 4426 ? 189.768 181.287 166.874 1.00 30.88  ? 4426 ASP A CG    1 
ATOM   21229 O  OD1   . ASP A 1 4426 ? 190.260 182.268 167.469 1.00 31.75  ? 4426 ASP A OD1   1 
ATOM   21230 O  OD2   . ASP A 1 4426 ? 188.909 181.399 165.974 1.00 39.11  ? 4426 ASP A OD2   1 
ATOM   21231 N  N     . VAL A 1 4427 ? 192.274 177.637 167.992 1.00 17.23  ? 4427 VAL A N     1 
ATOM   21232 C  CA    . VAL A 1 4427 ? 192.505 176.271 168.452 1.00 16.23  ? 4427 VAL A CA    1 
ATOM   21233 C  C     . VAL A 1 4427 ? 193.536 176.249 169.573 1.00 19.59  ? 4427 VAL A C     1 
ATOM   21234 O  O     . VAL A 1 4427 ? 193.368 175.538 170.572 1.00 21.49  ? 4427 VAL A O     1 
ATOM   21235 C  CB    . VAL A 1 4427 ? 192.925 175.377 167.271 1.00 18.42  ? 4427 VAL A CB    1 
ATOM   21236 C  CG1   . VAL A 1 4427 ? 193.490 174.056 167.769 1.00 17.34  ? 4427 VAL A CG1   1 
ATOM   21237 C  CG2   . VAL A 1 4427 ? 191.744 175.136 166.347 1.00 18.28  ? 4427 VAL A CG2   1 
ATOM   21238 N  N     . ARG A 1 4428 ? 194.616 177.021 169.431 1.00 19.24  ? 4428 ARG A N     1 
ATOM   21239 C  CA    . ARG A 1 4428 ? 195.631 177.067 170.477 1.00 18.00  ? 4428 ARG A CA    1 
ATOM   21240 C  C     . ARG A 1 4428 ? 195.075 177.659 171.765 1.00 19.57  ? 4428 ARG A C     1 
ATOM   21241 O  O     . ARG A 1 4428 ? 195.388 177.175 172.857 1.00 22.09  ? 4428 ARG A O     1 
ATOM   21242 C  CB    . ARG A 1 4428 ? 196.845 177.859 169.994 1.00 18.83  ? 4428 ARG A CB    1 
ATOM   21243 C  CG    . ARG A 1 4428 ? 197.694 177.122 168.973 1.00 17.80  ? 4428 ARG A CG    1 
ATOM   21244 C  CD    . ARG A 1 4428 ? 199.061 177.764 168.825 1.00 21.16  ? 4428 ARG A CD    1 
ATOM   21245 N  NE    . ARG A 1 4428 ? 199.911 177.520 169.984 1.00 22.73  ? 4428 ARG A NE    1 
ATOM   21246 C  CZ    . ARG A 1 4428 ? 200.595 176.403 170.190 1.00 24.94  ? 4428 ARG A CZ    1 
ATOM   21247 N  NH1   . ARG A 1 4428 ? 200.557 175.400 169.329 1.00 27.65  ? 4428 ARG A NH1   1 
ATOM   21248 N  NH2   . ARG A 1 4428 ? 201.335 176.290 171.289 1.00 23.12  ? 4428 ARG A NH2   1 
ATOM   21249 N  N     . GLN A 1 4429 ? 194.249 178.705 171.663 1.00 19.82  ? 4429 GLN A N     1 
ATOM   21250 C  CA    . GLN A 1 4429 ? 193.646 179.278 172.861 1.00 20.07  ? 4429 GLN A CA    1 
ATOM   21251 C  C     . GLN A 1 4429 ? 192.704 178.288 173.533 1.00 21.43  ? 4429 GLN A C     1 
ATOM   21252 O  O     . GLN A 1 4429 ? 192.694 178.168 174.764 1.00 23.54  ? 4429 GLN A O     1 
ATOM   21253 C  CB    . GLN A 1 4429 ? 192.910 180.570 172.510 1.00 22.55  ? 4429 GLN A CB    1 
ATOM   21254 C  CG    . GLN A 1 4429 ? 192.579 181.438 173.709 1.00 23.11  ? 4429 GLN A CG    1 
ATOM   21255 C  CD    . GLN A 1 4429 ? 193.772 181.655 174.616 1.00 31.09  ? 4429 GLN A CD    1 
ATOM   21256 O  OE1   . GLN A 1 4429 ? 193.713 181.383 175.814 1.00 30.31  ? 4429 GLN A OE1   1 
ATOM   21257 N  NE2   . GLN A 1 4429 ? 194.866 182.148 174.047 1.00 29.23  ? 4429 GLN A NE2   1 
ATOM   21258 N  N     . ASP A 1 4430 ? 191.905 177.567 172.742 1.00 19.49  ? 4430 ASP A N     1 
ATOM   21259 C  CA    . ASP A 1 4430 ? 191.012 176.567 173.319 1.00 19.99  ? 4430 ASP A CA    1 
ATOM   21260 C  C     . ASP A 1 4430 ? 191.798 175.459 174.007 1.00 23.13  ? 4430 ASP A C     1 
ATOM   21261 O  O     . ASP A 1 4430 ? 191.428 175.009 175.098 1.00 25.30  ? 4430 ASP A O     1 
ATOM   21262 C  CB    . ASP A 1 4430 ? 190.101 175.990 172.237 1.00 24.74  ? 4430 ASP A CB    1 
ATOM   21263 C  CG    . ASP A 1 4430 ? 189.096 177.000 171.722 1.00 30.26  ? 4430 ASP A CG    1 
ATOM   21264 O  OD1   . ASP A 1 4430 ? 189.095 178.148 172.214 1.00 32.72  ? 4430 ASP A OD1   1 
ATOM   21265 O  OD2   . ASP A 1 4430 ? 188.304 176.646 170.826 1.00 34.74  ? 4430 ASP A OD2   1 
ATOM   21266 N  N     . LEU A 1 4431 ? 192.891 175.010 173.387 1.00 23.59  ? 4431 LEU A N     1 
ATOM   21267 C  CA    . LEU A 1 4431 ? 193.720 173.977 173.999 1.00 20.01  ? 4431 LEU A CA    1 
ATOM   21268 C  C     . LEU A 1 4431 ? 194.371 174.478 175.282 1.00 22.79  ? 4431 LEU A C     1 
ATOM   21269 O  O     . LEU A 1 4431 ? 194.476 173.733 176.264 1.00 28.48  ? 4431 LEU A O     1 
ATOM   21270 C  CB    . LEU A 1 4431 ? 194.780 173.504 173.007 1.00 22.94  ? 4431 LEU A CB    1 
ATOM   21271 C  CG    . LEU A 1 4431 ? 194.295 172.518 171.944 1.00 18.04  ? 4431 LEU A CG    1 
ATOM   21272 C  CD1   . LEU A 1 4431 ? 195.430 172.144 171.011 1.00 19.61  ? 4431 LEU A CD1   1 
ATOM   21273 C  CD2   . LEU A 1 4431 ? 193.697 171.286 172.595 1.00 15.25  ? 4431 LEU A CD2   1 
ATOM   21274 N  N     . ALA A 1 4432 ? 194.819 175.735 175.292 1.00 21.11  ? 4432 ALA A N     1 
ATOM   21275 C  CA    . ALA A 1 4432 ? 195.400 176.306 176.501 1.00 24.65  ? 4432 ALA A CA    1 
ATOM   21276 C  C     . ALA A 1 4432 ? 194.374 176.385 177.623 1.00 29.34  ? 4432 ALA A C     1 
ATOM   21277 O  O     . ALA A 1 4432 ? 194.686 176.087 178.782 1.00 29.46  ? 4432 ALA A O     1 
ATOM   21278 C  CB    . ALA A 1 4432 ? 195.977 177.689 176.202 1.00 25.69  ? 4432 ALA A CB    1 
ATOM   21279 N  N     . ASP A 1 4433 ? 193.142 176.788 177.299 1.00 29.83  ? 4433 ASP A N     1 
ATOM   21280 C  CA    . ASP A 1 4433 ? 192.091 176.826 178.312 1.00 27.68  ? 4433 ASP A CA    1 
ATOM   21281 C  C     . ASP A 1 4433 ? 191.760 175.428 178.821 1.00 26.30  ? 4433 ASP A C     1 
ATOM   21282 O  O     . ASP A 1 4433 ? 191.496 175.243 180.014 1.00 29.48  ? 4433 ASP A O     1 
ATOM   21283 C  CB    . ASP A 1 4433 ? 190.842 177.509 177.757 1.00 27.81  ? 4433 ASP A CB    1 
ATOM   21284 C  CG    . ASP A 1 4433 ? 191.127 178.897 177.221 1.00 33.94  ? 4433 ASP A CG    1 
ATOM   21285 O  OD1   . ASP A 1 4433 ? 192.305 179.310 177.231 1.00 34.10  ? 4433 ASP A OD1   1 
ATOM   21286 O  OD2   . ASP A 1 4433 ? 190.172 179.575 176.787 1.00 36.74  ? 4433 ASP A OD2   1 
ATOM   21287 N  N     . VAL A 1 4434 ? 191.764 174.432 177.932 1.00 26.69  ? 4434 VAL A N     1 
ATOM   21288 C  CA    . VAL A 1 4434 ? 191.537 173.055 178.364 1.00 25.73  ? 4434 VAL A CA    1 
ATOM   21289 C  C     . VAL A 1 4434 ? 192.641 172.608 179.315 1.00 27.58  ? 4434 VAL A C     1 
ATOM   21290 O  O     . VAL A 1 4434 ? 192.378 171.960 180.336 1.00 27.69  ? 4434 VAL A O     1 
ATOM   21291 C  CB    . VAL A 1 4434 ? 191.423 172.120 177.145 1.00 25.09  ? 4434 VAL A CB    1 
ATOM   21292 C  CG1   . VAL A 1 4434 ? 191.517 170.668 177.575 1.00 31.58  ? 4434 VAL A CG1   1 
ATOM   21293 C  CG2   . VAL A 1 4434 ? 190.117 172.363 176.419 1.00 24.43  ? 4434 VAL A CG2   1 
ATOM   21294 N  N     . VAL A 1 4435 ? 193.892 172.949 178.997 1.00 28.16  ? 4435 VAL A N     1 
ATOM   21295 C  CA    . VAL A 1 4435 ? 195.007 172.594 179.871 1.00 28.99  ? 4435 VAL A CA    1 
ATOM   21296 C  C     . VAL A 1 4435 ? 194.853 173.264 181.230 1.00 34.42  ? 4435 VAL A C     1 
ATOM   21297 O  O     . VAL A 1 4435 ? 195.052 172.634 182.276 1.00 39.37  ? 4435 VAL A O     1 
ATOM   21298 C  CB    . VAL A 1 4435 ? 196.348 172.962 179.208 1.00 33.41  ? 4435 VAL A CB    1 
ATOM   21299 C  CG1   . VAL A 1 4435 ? 197.468 172.974 180.238 1.00 37.91  ? 4435 VAL A CG1   1 
ATOM   21300 C  CG2   . VAL A 1 4435 ? 196.669 171.995 178.086 1.00 34.30  ? 4435 VAL A CG2   1 
ATOM   21301 N  N     . GLN A 1 4436 ? 194.493 174.550 181.238 1.00 33.98  ? 4436 GLN A N     1 
ATOM   21302 C  CA    . GLN A 1 4436 ? 194.316 175.263 182.500 1.00 30.50  ? 4436 GLN A CA    1 
ATOM   21303 C  C     . GLN A 1 4436 ? 193.187 174.658 183.325 1.00 28.77  ? 4436 GLN A C     1 
ATOM   21304 O  O     . GLN A 1 4436 ? 193.294 174.550 184.552 1.00 38.81  ? 4436 GLN A O     1 
ATOM   21305 C  CB    . GLN A 1 4436 ? 194.054 176.746 182.240 1.00 32.11  ? 4436 GLN A CB    1 
ATOM   21306 C  CG    . GLN A 1 4436 ? 195.207 177.476 181.576 1.00 38.92  ? 4436 GLN A CG    1 
ATOM   21307 C  CD    . GLN A 1 4436 ? 196.432 177.560 182.463 1.00 53.88  ? 4436 GLN A CD    1 
ATOM   21308 O  OE1   . GLN A 1 4436 ? 196.324 177.756 183.674 1.00 53.15  ? 4436 GLN A OE1   1 
ATOM   21309 N  NE2   . GLN A 1 4436 ? 197.608 177.411 181.864 1.00 54.82  ? 4436 GLN A NE2   1 
ATOM   21310 N  N     . VAL A 1 4437 ? 192.092 174.266 182.671 1.00 26.56  ? 4437 VAL A N     1 
ATOM   21311 C  CA    . VAL A 1 4437 ? 190.995 173.613 183.381 1.00 28.93  ? 4437 VAL A CA    1 
ATOM   21312 C  C     . VAL A 1 4437 ? 191.461 172.291 183.975 1.00 30.60  ? 4437 VAL A C     1 
ATOM   21313 O  O     . VAL A 1 4437 ? 191.156 171.968 185.130 1.00 31.69  ? 4437 VAL A O     1 
ATOM   21314 C  CB    . VAL A 1 4437 ? 189.790 173.417 182.443 1.00 25.75  ? 4437 VAL A CB    1 
ATOM   21315 C  CG1   . VAL A 1 4437 ? 188.885 172.317 182.967 1.00 24.08  ? 4437 VAL A CG1   1 
ATOM   21316 C  CG2   . VAL A 1 4437 ? 189.018 174.714 182.295 1.00 23.40  ? 4437 VAL A CG2   1 
ATOM   21317 N  N     . CYS A 1 4438 ? 192.214 171.508 183.200 1.00 34.22  ? 4438 CYS A N     1 
ATOM   21318 C  CA    . CYS A 1 4438 ? 192.711 170.231 183.692 1.00 32.98  ? 4438 CYS A CA    1 
ATOM   21319 C  C     . CYS A 1 4438 ? 193.725 170.396 184.816 1.00 35.68  ? 4438 CYS A C     1 
ATOM   21320 O  O     . CYS A 1 4438 ? 193.910 169.464 185.606 1.00 43.44  ? 4438 CYS A O     1 
ATOM   21321 C  CB    . CYS A 1 4438 ? 193.322 169.428 182.546 1.00 32.84  ? 4438 CYS A CB    1 
ATOM   21322 S  SG    . CYS A 1 4438 ? 192.122 168.852 181.327 1.00 41.97  ? 4438 CYS A SG    1 
ATOM   21323 N  N     . GLU A 1 4439 ? 194.381 171.549 184.907 1.00 40.57  ? 4439 GLU A N     1 
ATOM   21324 C  CA    . GLU A 1 4439 ? 195.269 171.838 186.024 1.00 38.14  ? 4439 GLU A CA    1 
ATOM   21325 C  C     . GLU A 1 4439 ? 194.521 172.330 187.255 1.00 37.74  ? 4439 GLU A C     1 
ATOM   21326 O  O     . GLU A 1 4439 ? 195.146 172.516 188.305 1.00 45.75  ? 4439 GLU A O     1 
ATOM   21327 C  CB    . GLU A 1 4439 ? 196.318 172.873 185.612 1.00 39.16  ? 4439 GLU A CB    1 
ATOM   21328 C  CG    . GLU A 1 4439 ? 197.308 172.378 184.574 1.00 39.96  ? 4439 GLU A CG    1 
ATOM   21329 C  CD    . GLU A 1 4439 ? 198.317 173.439 184.180 1.00 58.03  ? 4439 GLU A CD    1 
ATOM   21330 O  OE1   . GLU A 1 4439 ? 198.168 174.597 184.623 1.00 60.57  ? 4439 GLU A OE1   1 
ATOM   21331 O  OE2   . GLU A 1 4439 ? 199.260 173.114 183.427 1.00 57.08  ? 4439 GLU A OE2   1 
ATOM   21332 N  N     . GLY A 1 4440 ? 193.212 172.542 187.154 1.00 35.21  ? 4440 GLY A N     1 
ATOM   21333 C  CA    . GLY A 1 4440 ? 192.429 173.026 188.270 1.00 32.06  ? 4440 GLY A CA    1 
ATOM   21334 C  C     . GLY A 1 4440 ? 192.567 174.502 188.555 1.00 39.66  ? 4440 GLY A C     1 
ATOM   21335 O  O     . GLY A 1 4440 ? 192.137 174.952 189.623 1.00 44.06  ? 4440 GLY A O     1 
ATOM   21336 N  N     . LYS A 1 4441 ? 193.150 175.272 187.637 1.00 38.82  ? 4441 LYS A N     1 
ATOM   21337 C  CA    . LYS A 1 4441 ? 193.388 176.692 187.870 1.00 42.66  ? 4441 LYS A CA    1 
ATOM   21338 C  C     . LYS A 1 4441 ? 192.173 177.544 187.509 1.00 46.18  ? 4441 LYS A C     1 
ATOM   21339 O  O     . LYS A 1 4441 ? 191.644 178.269 188.358 1.00 51.98  ? 4441 LYS A O     1 
ATOM   21340 C  CB    . LYS A 1 4441 ? 194.622 177.151 187.087 1.00 39.06  ? 4441 LYS A CB    1 
ATOM   21341 C  CG    . LYS A 1 4441 ? 195.939 176.673 187.678 1.00 50.72  ? 4441 LYS A CG    1 
ATOM   21342 C  CD    . LYS A 1 4441 ? 197.121 177.154 186.852 1.00 59.59  ? 4441 LYS A CD    1 
ATOM   21343 C  CE    . LYS A 1 4441 ? 198.431 176.605 187.391 1.00 57.26  ? 4441 LYS A CE    1 
ATOM   21344 N  NZ    . LYS A 1 4441 ? 199.561 176.853 186.454 1.00 57.44  ? 4441 LYS A NZ    1 
ATOM   21345 N  N     . LYS A 1 4442 ? 191.721 177.468 186.262 1.00 35.17  ? 4442 LYS A N     1 
ATOM   21346 C  CA    . LYS A 1 4442 ? 190.638 178.316 185.788 1.00 33.12  ? 4442 LYS A CA    1 
ATOM   21347 C  C     . LYS A 1 4442 ? 189.310 177.568 185.826 1.00 32.77  ? 4442 LYS A C     1 
ATOM   21348 O  O     . LYS A 1 4442 ? 189.256 176.345 185.671 1.00 26.12  ? 4442 LYS A O     1 
ATOM   21349 C  CB    . LYS A 1 4442 ? 190.918 178.828 184.372 1.00 28.92  ? 4442 LYS A CB    1 
ATOM   21350 C  CG    . LYS A 1 4442 ? 190.556 177.867 183.257 1.00 26.52  ? 4442 LYS A CG    1 
ATOM   21351 C  CD    . LYS A 1 4442 ? 190.842 178.482 181.899 1.00 25.66  ? 4442 LYS A CD    1 
ATOM   21352 C  CE    . LYS A 1 4442 ? 189.958 179.688 181.643 1.00 29.03  ? 4442 LYS A CE    1 
ATOM   21353 N  NZ    . LYS A 1 4442 ? 190.211 180.287 180.305 1.00 33.00  ? 4442 LYS A NZ    1 
ATOM   21354 N  N     . LYS A 1 4443 ? 188.238 178.323 186.051 1.00 35.42  ? 4443 LYS A N     1 
ATOM   21355 C  CA    . LYS A 1 4443 ? 186.912 177.745 186.204 1.00 28.12  ? 4443 LYS A CA    1 
ATOM   21356 C  C     . LYS A 1 4443 ? 186.308 177.403 184.849 1.00 25.52  ? 4443 LYS A C     1 
ATOM   21357 O  O     . LYS A 1 4443 ? 186.476 178.138 183.872 1.00 29.37  ? 4443 LYS A O     1 
ATOM   21358 C  CB    . LYS A 1 4443 ? 185.996 178.711 186.955 1.00 27.15  ? 4443 LYS A CB    1 
ATOM   21359 C  CG    . LYS A 1 4443 ? 186.369 178.906 188.414 1.00 38.58  ? 4443 LYS A CG    1 
ATOM   21360 C  CD    . LYS A 1 4443 ? 185.470 179.929 189.086 1.00 50.28  ? 4443 LYS A CD    1 
ATOM   21361 C  CE    . LYS A 1 4443 ? 184.061 179.386 189.271 1.00 53.45  ? 4443 LYS A CE    1 
ATOM   21362 N  NZ    . LYS A 1 4443 ? 184.024 178.273 190.260 1.00 38.53  ? 4443 LYS A NZ    1 
ATOM   21363 N  N     . GLN A 1 4444 ? 185.601 176.277 184.799 1.00 22.62  ? 4444 GLN A N     1 
ATOM   21364 C  CA    . GLN A 1 4444 ? 184.957 175.848 183.566 1.00 18.44  ? 4444 GLN A CA    1 
ATOM   21365 C  C     . GLN A 1 4444 ? 183.794 176.765 183.212 1.00 19.05  ? 4444 GLN A C     1 
ATOM   21366 O  O     . GLN A 1 4444 ? 183.054 177.226 184.084 1.00 23.10  ? 4444 GLN A O     1 
ATOM   21367 C  CB    . GLN A 1 4444 ? 184.461 174.410 183.699 1.00 23.83  ? 4444 GLN A CB    1 
ATOM   21368 C  CG    . GLN A 1 4444 ? 185.415 173.369 183.148 1.00 28.64  ? 4444 GLN A CG    1 
ATOM   21369 C  CD    . GLN A 1 4444 ? 184.886 171.958 183.299 1.00 39.85  ? 4444 GLN A CD    1 
ATOM   21370 O  OE1   . GLN A 1 4444 ? 184.131 171.472 182.457 1.00 30.80  ? 4444 GLN A OE1   1 
ATOM   21371 N  NE2   . GLN A 1 4444 ? 185.279 171.290 184.378 1.00 38.75  ? 4444 GLN A NE2   1 
ATOM   21372 N  N     . THR A 1 4445 ? 183.636 177.025 181.919 1.00 16.74  ? 4445 THR A N     1 
ATOM   21373 C  CA    . THR A 1 4445 ? 182.519 177.783 181.378 1.00 11.94  ? 4445 THR A CA    1 
ATOM   21374 C  C     . THR A 1 4445 ? 181.646 176.859 180.535 1.00 12.54  ? 4445 THR A C     1 
ATOM   21375 O  O     . THR A 1 4445 ? 181.938 175.672 180.372 1.00 12.54  ? 4445 THR A O     1 
ATOM   21376 C  CB    . THR A 1 4445 ? 183.021 178.973 180.557 1.00 12.15  ? 4445 THR A CB    1 
ATOM   21377 O  OG1   . THR A 1 4445 ? 183.826 178.502 179.470 1.00 13.77  ? 4445 THR A OG1   1 
ATOM   21378 C  CG2   . THR A 1 4445 ? 183.854 179.902 181.423 1.00 11.24  ? 4445 THR A CG2   1 
ATOM   21379 N  N     . ASN A 1 4446 ? 180.557 177.415 180.000 1.00 13.37  ? 4446 ASN A N     1 
ATOM   21380 C  CA    . ASN A 1 4446 ? 179.677 176.632 179.137 1.00 11.48  ? 4446 ASN A CA    1 
ATOM   21381 C  C     . ASN A 1 4446 ? 180.407 176.181 177.878 1.00 11.80  ? 4446 ASN A C     1 
ATOM   21382 O  O     . ASN A 1 4446 ? 180.360 175.002 177.502 1.00 17.93  ? 4446 ASN A O     1 
ATOM   21383 C  CB    . ASN A 1 4446 ? 178.436 177.448 178.773 1.00 9.29   ? 4446 ASN A CB    1 
ATOM   21384 C  CG    . ASN A 1 4446 ? 177.283 177.210 179.723 1.00 8.36   ? 4446 ASN A CG    1 
ATOM   21385 O  OD1   . ASN A 1 4446 ? 176.958 176.070 180.050 1.00 12.01  ? 4446 ASN A OD1   1 
ATOM   21386 N  ND2   . ASN A 1 4446 ? 176.650 178.289 180.164 1.00 8.11   ? 4446 ASN A ND2   1 
ATOM   21387 N  N     . TYR A 1 4447 ? 181.094 177.113 177.213 1.00 12.29  ? 4447 TYR A N     1 
ATOM   21388 C  CA    . TYR A 1 4447 ? 181.865 176.758 176.028 1.00 16.97  ? 4447 TYR A CA    1 
ATOM   21389 C  C     . TYR A 1 4447 ? 182.975 175.779 176.375 1.00 16.49  ? 4447 TYR A C     1 
ATOM   21390 O  O     . TYR A 1 4447 ? 183.226 174.822 175.632 1.00 18.03  ? 4447 TYR A O     1 
ATOM   21391 C  CB    . TYR A 1 4447 ? 182.446 178.014 175.379 1.00 19.42  ? 4447 TYR A CB    1 
ATOM   21392 C  CG    . TYR A 1 4447 ? 183.413 177.715 174.258 1.00 19.21  ? 4447 TYR A CG    1 
ATOM   21393 C  CD1   . TYR A 1 4447 ? 182.975 177.135 173.076 1.00 20.62  ? 4447 TYR A CD1   1 
ATOM   21394 C  CD2   . TYR A 1 4447 ? 184.765 177.999 174.386 1.00 21.12  ? 4447 TYR A CD2   1 
ATOM   21395 C  CE1   . TYR A 1 4447 ? 183.853 176.854 172.050 1.00 27.40  ? 4447 TYR A CE1   1 
ATOM   21396 C  CE2   . TYR A 1 4447 ? 185.652 177.721 173.365 1.00 27.85  ? 4447 TYR A CE2   1 
ATOM   21397 C  CZ    . TYR A 1 4447 ? 185.189 177.149 172.199 1.00 32.34  ? 4447 TYR A CZ    1 
ATOM   21398 O  OH    . TYR A 1 4447 ? 186.064 176.869 171.176 1.00 32.63  ? 4447 TYR A OH    1 
ATOM   21399 N  N     . LEU A 1 4448 ? 183.655 176.005 177.500 1.00 15.47  ? 4448 LEU A N     1 
ATOM   21400 C  CA    . LEU A 1 4448 ? 184.698 175.084 177.932 1.00 13.99  ? 4448 LEU A CA    1 
ATOM   21401 C  C     . LEU A 1 4448 ? 184.123 173.709 178.238 1.00 16.88  ? 4448 LEU A C     1 
ATOM   21402 O  O     . LEU A 1 4448 ? 184.735 172.689 177.911 1.00 21.86  ? 4448 LEU A O     1 
ATOM   21403 C  CB    . LEU A 1 4448 ? 185.427 175.651 179.148 1.00 13.81  ? 4448 LEU A CB    1 
ATOM   21404 C  CG    . LEU A 1 4448 ? 186.542 176.640 178.816 1.00 14.90  ? 4448 LEU A CG    1 
ATOM   21405 C  CD1   . LEU A 1 4448 ? 187.203 177.163 180.081 1.00 16.63  ? 4448 LEU A CD1   1 
ATOM   21406 C  CD2   . LEU A 1 4448 ? 187.563 175.986 177.903 1.00 18.72  ? 4448 LEU A CD2   1 
ATOM   21407 N  N     . ARG A 1 4449 ? 182.944 173.662 178.862 1.00 18.28  ? 4449 ARG A N     1 
ATOM   21408 C  CA    . ARG A 1 4449 ? 182.308 172.380 179.148 1.00 13.98  ? 4449 ARG A CA    1 
ATOM   21409 C  C     . ARG A 1 4449 ? 181.997 171.626 177.862 1.00 14.87  ? 4449 ARG A C     1 
ATOM   21410 O  O     . ARG A 1 4449 ? 182.290 170.431 177.742 1.00 22.68  ? 4449 ARG A O     1 
ATOM   21411 C  CB    . ARG A 1 4449 ? 181.034 172.600 179.962 1.00 13.37  ? 4449 ARG A CB    1 
ATOM   21412 C  CG    . ARG A 1 4449 ? 181.259 172.682 181.458 1.00 17.27  ? 4449 ARG A CG    1 
ATOM   21413 C  CD    . ARG A 1 4449 ? 179.942 172.672 182.209 1.00 16.71  ? 4449 ARG A CD    1 
ATOM   21414 N  NE    . ARG A 1 4449 ? 179.336 173.997 182.241 1.00 15.32  ? 4449 ARG A NE    1 
ATOM   21415 C  CZ    . ARG A 1 4449 ? 179.720 174.979 183.045 1.00 18.53  ? 4449 ARG A CZ    1 
ATOM   21416 N  NH1   . ARG A 1 4449 ? 180.714 174.821 183.903 1.00 23.59  ? 4449 ARG A NH1   1 
ATOM   21417 N  NH2   . ARG A 1 4449 ? 179.094 176.150 182.982 1.00 12.15  ? 4449 ARG A NH2   1 
ATOM   21418 N  N     . THR A 1 4450 ? 181.405 172.316 176.882 1.00 14.12  ? 4450 THR A N     1 
ATOM   21419 C  CA    . THR A 1 4450 ? 181.076 171.665 175.617 1.00 17.02  ? 4450 THR A CA    1 
ATOM   21420 C  C     . THR A 1 4450 ? 182.331 171.191 174.893 1.00 17.89  ? 4450 THR A C     1 
ATOM   21421 O  O     . THR A 1 4450 ? 182.375 170.065 174.378 1.00 20.30  ? 4450 THR A O     1 
ATOM   21422 C  CB    . THR A 1 4450 ? 180.275 172.620 174.730 1.00 14.72  ? 4450 THR A CB    1 
ATOM   21423 O  OG1   . THR A 1 4450 ? 179.128 173.088 175.447 1.00 16.56  ? 4450 THR A OG1   1 
ATOM   21424 C  CG2   . THR A 1 4450 ? 179.819 171.918 173.463 1.00 14.22  ? 4450 THR A CG2   1 
ATOM   21425 N  N     . LEU A 1 4451 ? 183.365 172.034 174.852 1.00 17.55  ? 4451 LEU A N     1 
ATOM   21426 C  CA    . LEU A 1 4451 ? 184.598 171.671 174.163 1.00 15.88  ? 4451 LEU A CA    1 
ATOM   21427 C  C     . LEU A 1 4451 ? 185.286 170.493 174.841 1.00 18.49  ? 4451 LEU A C     1 
ATOM   21428 O  O     . LEU A 1 4451 ? 185.793 169.591 174.166 1.00 25.96  ? 4451 LEU A O     1 
ATOM   21429 C  CB    . LEU A 1 4451 ? 185.525 172.884 174.099 1.00 15.88  ? 4451 LEU A CB    1 
ATOM   21430 C  CG    . LEU A 1 4451 ? 186.991 172.669 173.727 1.00 16.47  ? 4451 LEU A CG    1 
ATOM   21431 C  CD1   . LEU A 1 4451 ? 187.131 172.388 172.246 1.00 17.47  ? 4451 LEU A CD1   1 
ATOM   21432 C  CD2   . LEU A 1 4451 ? 187.800 173.890 174.114 1.00 20.86  ? 4451 LEU A CD2   1 
ATOM   21433 N  N     . ILE A 1 4452 ? 185.306 170.478 176.175 1.00 15.44  ? 4452 ILE A N     1 
ATOM   21434 C  CA    . ILE A 1 4452 ? 185.929 169.379 176.902 1.00 20.85  ? 4452 ILE A CA    1 
ATOM   21435 C  C     . ILE A 1 4452 ? 185.146 168.089 176.699 1.00 20.00  ? 4452 ILE A C     1 
ATOM   21436 O  O     . ILE A 1 4452 ? 185.734 167.014 176.533 1.00 24.92  ? 4452 ILE A O     1 
ATOM   21437 C  CB    . ILE A 1 4452 ? 186.062 169.741 178.393 1.00 25.63  ? 4452 ILE A CB    1 
ATOM   21438 C  CG1   . ILE A 1 4452 ? 187.225 170.710 178.597 1.00 20.00  ? 4452 ILE A CG1   1 
ATOM   21439 C  CG2   . ILE A 1 4452 ? 186.259 168.495 179.240 1.00 20.73  ? 4452 ILE A CG2   1 
ATOM   21440 C  CD1   . ILE A 1 4452 ? 187.200 171.409 179.928 1.00 17.85  ? 4452 ILE A CD1   1 
ATOM   21441 N  N     . ASN A 1 4453 ? 183.813 168.169 176.709 1.00 19.23  ? 4453 ASN A N     1 
ATOM   21442 C  CA    . ASN A 1 4453 ? 183.008 166.980 176.448 1.00 22.31  ? 4453 ASN A CA    1 
ATOM   21443 C  C     . ASN A 1 4453 ? 183.283 166.431 175.055 1.00 25.29  ? 4453 ASN A C     1 
ATOM   21444 O  O     . ASN A 1 4453 ? 183.447 165.217 174.878 1.00 28.37  ? 4453 ASN A O     1 
ATOM   21445 C  CB    . ASN A 1 4453 ? 181.524 167.303 176.614 1.00 21.94  ? 4453 ASN A CB    1 
ATOM   21446 C  CG    . ASN A 1 4453 ? 181.060 167.185 178.051 1.00 37.17  ? 4453 ASN A CG    1 
ATOM   21447 O  OD1   . ASN A 1 4453 ? 181.577 166.373 178.819 1.00 39.31  ? 4453 ASN A OD1   1 
ATOM   21448 N  ND2   . ASN A 1 4453 ? 180.076 167.995 178.423 1.00 39.04  ? 4453 ASN A ND2   1 
ATOM   21449 N  N     . GLU A 1 4454 ? 183.352 167.314 174.055 1.00 23.99  ? 4454 GLU A N     1 
ATOM   21450 C  CA    . GLU A 1 4454 ? 183.639 166.871 172.695 1.00 22.67  ? 4454 GLU A CA    1 
ATOM   21451 C  C     . GLU A 1 4454 ? 185.026 166.247 172.594 1.00 23.65  ? 4454 GLU A C     1 
ATOM   21452 O  O     . GLU A 1 4454 ? 185.202 165.209 171.946 1.00 30.05  ? 4454 GLU A O     1 
ATOM   21453 C  CB    . GLU A 1 4454 ? 183.503 168.046 171.726 1.00 25.51  ? 4454 GLU A CB    1 
ATOM   21454 C  CG    . GLU A 1 4454 ? 182.060 168.425 171.417 1.00 31.55  ? 4454 GLU A CG    1 
ATOM   21455 C  CD    . GLU A 1 4454 ? 181.945 169.425 170.282 1.00 37.98  ? 4454 GLU A CD    1 
ATOM   21456 O  OE1   . GLU A 1 4454 ? 181.554 169.021 169.167 1.00 43.54  ? 4454 GLU A OE1   1 
ATOM   21457 O  OE2   . GLU A 1 4454 ? 182.243 170.617 170.507 1.00 38.40  ? 4454 GLU A OE2   1 
ATOM   21458 N  N     . LEU A 1 4455 ? 186.024 166.865 173.230 1.00 23.38  ? 4455 LEU A N     1 
ATOM   21459 C  CA    . LEU A 1 4455 ? 187.384 166.339 173.169 1.00 20.40  ? 4455 LEU A CA    1 
ATOM   21460 C  C     . LEU A 1 4455 ? 187.493 164.982 173.854 1.00 23.77  ? 4455 LEU A C     1 
ATOM   21461 O  O     . LEU A 1 4455 ? 188.147 164.070 173.334 1.00 28.61  ? 4455 LEU A O     1 
ATOM   21462 C  CB    . LEU A 1 4455 ? 188.359 167.334 173.799 1.00 20.84  ? 4455 LEU A CB    1 
ATOM   21463 C  CG    . LEU A 1 4455 ? 188.700 168.573 172.971 1.00 22.45  ? 4455 LEU A CG    1 
ATOM   21464 C  CD1   . LEU A 1 4455 ? 189.900 169.291 173.559 1.00 27.37  ? 4455 LEU A CD1   1 
ATOM   21465 C  CD2   . LEU A 1 4455 ? 188.958 168.194 171.523 1.00 28.08  ? 4455 LEU A CD2   1 
ATOM   21466 N  N     . VAL A 1 4456 ? 186.868 164.832 175.023 1.00 27.09  ? 4456 VAL A N     1 
ATOM   21467 C  CA    . VAL A 1 4456 ? 186.930 163.563 175.741 1.00 26.64  ? 4456 VAL A CA    1 
ATOM   21468 C  C     . VAL A 1 4456 ? 186.203 162.474 174.964 1.00 28.27  ? 4456 VAL A C     1 
ATOM   21469 O  O     . VAL A 1 4456 ? 186.703 161.351 174.829 1.00 29.19  ? 4456 VAL A O     1 
ATOM   21470 C  CB    . VAL A 1 4456 ? 186.359 163.730 177.161 1.00 23.30  ? 4456 VAL A CB    1 
ATOM   21471 C  CG1   . VAL A 1 4456 ? 186.002 162.379 177.759 1.00 25.45  ? 4456 VAL A CG1   1 
ATOM   21472 C  CG2   . VAL A 1 4456 ? 187.355 164.459 178.046 1.00 27.87  ? 4456 VAL A CG2   1 
ATOM   21473 N  N     . LYS A 1 4457 ? 185.021 162.786 174.430 1.00 27.04  ? 4457 LYS A N     1 
ATOM   21474 C  CA    . LYS A 1 4457 ? 184.271 161.797 173.669 1.00 28.34  ? 4457 LYS A CA    1 
ATOM   21475 C  C     . LYS A 1 4457 ? 184.842 161.562 172.276 1.00 29.70  ? 4457 LYS A C     1 
ATOM   21476 O  O     . LYS A 1 4457 ? 184.398 160.633 171.594 1.00 37.24  ? 4457 LYS A O     1 
ATOM   21477 C  CB    . LYS A 1 4457 ? 182.805 162.218 173.573 1.00 27.50  ? 4457 LYS A CB    1 
ATOM   21478 C  CG    . LYS A 1 4457 ? 182.067 162.200 174.900 1.00 27.66  ? 4457 LYS A CG    1 
ATOM   21479 C  CD    . LYS A 1 4457 ? 180.660 161.650 174.744 1.00 29.72  ? 4457 LYS A CD    1 
ATOM   21480 C  CE    . LYS A 1 4457 ? 179.957 162.257 173.541 1.00 26.96  ? 4457 LYS A CE    1 
ATOM   21481 N  NZ    . LYS A 1 4457 ? 178.477 162.143 173.645 1.00 29.30  ? 4457 LYS A NZ    1 
ATOM   21482 N  N     . GLY A 1 4458 ? 185.804 162.372 171.840 1.00 27.40  ? 4458 GLY A N     1 
ATOM   21483 C  CA    . GLY A 1 4458 ? 186.474 162.157 170.576 1.00 24.56  ? 4458 GLY A CA    1 
ATOM   21484 C  C     . GLY A 1 4458 ? 185.848 162.818 169.368 1.00 26.37  ? 4458 GLY A C     1 
ATOM   21485 O  O     . GLY A 1 4458 ? 186.345 162.620 168.254 1.00 28.85  ? 4458 GLY A O     1 
ATOM   21486 N  N     . ILE A 1 4459 ? 184.781 163.588 169.544 1.00 23.51  ? 4459 ILE A N     1 
ATOM   21487 C  CA    . ILE A 1 4459 ? 184.133 164.282 168.436 1.00 27.66  ? 4459 ILE A CA    1 
ATOM   21488 C  C     . ILE A 1 4459 ? 184.858 165.595 168.177 1.00 29.12  ? 4459 ILE A C     1 
ATOM   21489 O  O     . ILE A 1 4459 ? 185.186 166.332 169.114 1.00 32.59  ? 4459 ILE A O     1 
ATOM   21490 C  CB    . ILE A 1 4459 ? 182.639 164.520 168.723 1.00 25.82  ? 4459 ILE A CB    1 
ATOM   21491 C  CG1   . ILE A 1 4459 ? 181.881 163.193 168.835 1.00 25.53  ? 4459 ILE A CG1   1 
ATOM   21492 C  CG2   . ILE A 1 4459 ? 182.015 165.403 167.652 1.00 27.11  ? 4459 ILE A CG2   1 
ATOM   21493 C  CD1   . ILE A 1 4459 ? 181.832 162.612 170.221 1.00 29.44  ? 4459 ILE A CD1   1 
ATOM   21494 N  N     . LEU A 1 4460 ? 185.123 165.876 166.906 1.00 22.56  ? 4460 LEU A N     1 
ATOM   21495 C  CA    . LEU A 1 4460 ? 185.743 167.137 166.527 1.00 23.39  ? 4460 LEU A CA    1 
ATOM   21496 C  C     . LEU A 1 4460 ? 184.815 168.296 166.880 1.00 29.88  ? 4460 LEU A C     1 
ATOM   21497 O  O     . LEU A 1 4460 ? 183.629 168.262 166.523 1.00 35.61  ? 4460 LEU A O     1 
ATOM   21498 C  CB    . LEU A 1 4460 ? 186.056 167.141 165.033 1.00 27.19  ? 4460 LEU A CB    1 
ATOM   21499 C  CG    . LEU A 1 4460 ? 186.349 168.481 164.357 1.00 26.67  ? 4460 LEU A CG    1 
ATOM   21500 C  CD1   . LEU A 1 4460 ? 187.695 169.029 164.793 1.00 23.48  ? 4460 LEU A CD1   1 
ATOM   21501 C  CD2   . LEU A 1 4460 ? 186.293 168.325 162.849 1.00 23.59  ? 4460 LEU A CD2   1 
ATOM   21502 N  N     . PRO A 1 4461 ? 185.300 169.319 167.582 1.00 27.97  ? 4461 PRO A N     1 
ATOM   21503 C  CA    . PRO A 1 4461 ? 184.431 170.445 167.941 1.00 25.89  ? 4461 PRO A CA    1 
ATOM   21504 C  C     . PRO A 1 4461 ? 183.874 171.136 166.706 1.00 28.77  ? 4461 PRO A C     1 
ATOM   21505 O  O     . PRO A 1 4461 ? 184.562 171.297 165.696 1.00 34.17  ? 4461 PRO A O     1 
ATOM   21506 C  CB    . PRO A 1 4461 ? 185.360 171.372 168.732 1.00 24.02  ? 4461 PRO A CB    1 
ATOM   21507 C  CG    . PRO A 1 4461 ? 186.439 170.484 169.235 1.00 25.48  ? 4461 PRO A CG    1 
ATOM   21508 C  CD    . PRO A 1 4461 ? 186.641 169.448 168.175 1.00 30.73  ? 4461 PRO A CD    1 
ATOM   21509 N  N     . ARG A 1 4462 ? 182.609 171.549 166.798 1.00 30.07  ? 4462 ARG A N     1 
ATOM   21510 C  CA    . ARG A 1 4462 ? 181.982 172.259 165.691 1.00 36.16  ? 4462 ARG A CA    1 
ATOM   21511 C  C     . ARG A 1 4462 ? 182.553 173.658 165.512 1.00 36.05  ? 4462 ARG A C     1 
ATOM   21512 O  O     . ARG A 1 4462 ? 182.428 174.231 164.425 1.00 39.33  ? 4462 ARG A O     1 
ATOM   21513 C  CB    . ARG A 1 4462 ? 180.469 172.331 165.899 1.00 33.13  ? 4462 ARG A CB    1 
ATOM   21514 C  CG    . ARG A 1 4462 ? 179.808 170.977 166.090 1.00 35.29  ? 4462 ARG A CG    1 
ATOM   21515 C  CD    . ARG A 1 4462 ? 179.845 170.162 164.808 1.00 46.81  ? 4462 ARG A CD    1 
ATOM   21516 N  NE    . ARG A 1 4462 ? 180.909 169.165 164.830 1.00 56.54  ? 4462 ARG A NE    1 
ATOM   21517 C  CZ    . ARG A 1 4462 ? 181.685 168.873 163.796 1.00 43.50  ? 4462 ARG A CZ    1 
ATOM   21518 N  NH1   . ARG A 1 4462 ? 181.546 169.487 162.632 1.00 40.22  ? 4462 ARG A NH1   1 
ATOM   21519 N  NH2   . ARG A 1 4462 ? 182.626 167.942 163.932 1.00 30.14  ? 4462 ARG A NH2   1 
ATOM   21520 N  N     . SER A 1 4463 ? 183.177 174.215 166.549 1.00 28.80  ? 4463 SER A N     1 
ATOM   21521 C  CA    . SER A 1 4463 ? 183.782 175.536 166.467 1.00 22.58  ? 4463 SER A CA    1 
ATOM   21522 C  C     . SER A 1 4463 ? 185.170 175.516 165.842 1.00 25.49  ? 4463 SER A C     1 
ATOM   21523 O  O     . SER A 1 4463 ? 185.717 176.587 165.560 1.00 27.50  ? 4463 SER A O     1 
ATOM   21524 C  CB    . SER A 1 4463 ? 183.854 176.163 167.860 1.00 30.23  ? 4463 SER A CB    1 
ATOM   21525 O  OG    . SER A 1 4463 ? 184.739 175.440 168.698 1.00 35.03  ? 4463 SER A OG    1 
ATOM   21526 N  N     . TRP A 1 4464 ? 185.750 174.337 165.621 1.00 24.69  ? 4464 TRP A N     1 
ATOM   21527 C  CA    . TRP A 1 4464 ? 187.054 174.218 164.982 1.00 20.25  ? 4464 TRP A CA    1 
ATOM   21528 C  C     . TRP A 1 4464 ? 186.969 173.871 163.504 1.00 25.17  ? 4464 TRP A C     1 
ATOM   21529 O  O     . TRP A 1 4464 ? 187.871 174.233 162.743 1.00 28.22  ? 4464 TRP A O     1 
ATOM   21530 C  CB    . TRP A 1 4464 ? 187.898 173.150 165.687 1.00 24.10  ? 4464 TRP A CB    1 
ATOM   21531 C  CG    . TRP A 1 4464 ? 188.399 173.549 167.037 1.00 23.08  ? 4464 TRP A CG    1 
ATOM   21532 C  CD1   . TRP A 1 4464 ? 188.145 174.714 167.696 1.00 25.97  ? 4464 TRP A CD1   1 
ATOM   21533 C  CD2   . TRP A 1 4464 ? 189.249 172.779 167.895 1.00 20.03  ? 4464 TRP A CD2   1 
ATOM   21534 N  NE1   . TRP A 1 4464 ? 188.782 174.718 168.912 1.00 22.61  ? 4464 TRP A NE1   1 
ATOM   21535 C  CE2   . TRP A 1 4464 ? 189.467 173.541 169.058 1.00 23.05  ? 4464 TRP A CE2   1 
ATOM   21536 C  CE3   . TRP A 1 4464 ? 189.846 171.520 167.792 1.00 21.58  ? 4464 TRP A CE3   1 
ATOM   21537 C  CZ2   . TRP A 1 4464 ? 190.256 173.085 170.112 1.00 21.29  ? 4464 TRP A CZ2   1 
ATOM   21538 C  CZ3   . TRP A 1 4464 ? 190.628 171.070 168.838 1.00 20.75  ? 4464 TRP A CZ3   1 
ATOM   21539 C  CH2   . TRP A 1 4464 ? 190.826 171.850 169.982 1.00 17.32  ? 4464 TRP A CH2   1 
ATOM   21540 N  N     . SER A 1 4465 ? 185.910 173.181 163.081 1.00 28.64  ? 4465 SER A N     1 
ATOM   21541 C  CA    . SER A 1 4465 ? 185.786 172.708 161.703 1.00 28.15  ? 4465 SER A CA    1 
ATOM   21542 C  C     . SER A 1 4465 ? 185.277 173.850 160.828 1.00 23.71  ? 4465 SER A C     1 
ATOM   21543 O  O     . SER A 1 4465 ? 184.092 173.956 160.503 1.00 27.12  ? 4465 SER A O     1 
ATOM   21544 C  CB    . SER A 1 4465 ? 184.865 171.496 161.634 1.00 36.40  ? 4465 SER A CB    1 
ATOM   21545 O  OG    . SER A 1 4465 ? 183.511 171.891 161.503 1.00 41.99  ? 4465 SER A OG    1 
ATOM   21546 N  N     . HIS A 1 4466 ? 186.204 174.722 160.439 1.00 22.24  ? 4466 HIS A N     1 
ATOM   21547 C  CA    . HIS A 1 4466 ? 185.899 175.832 159.549 1.00 22.10  ? 4466 HIS A CA    1 
ATOM   21548 C  C     . HIS A 1 4466 ? 186.310 175.570 158.107 1.00 25.06  ? 4466 HIS A C     1 
ATOM   21549 O  O     . HIS A 1 4466 ? 186.161 176.460 157.264 1.00 33.34  ? 4466 HIS A O     1 
ATOM   21550 C  CB    . HIS A 1 4466 ? 186.560 177.115 160.059 1.00 19.56  ? 4466 HIS A CB    1 
ATOM   21551 C  CG    . HIS A 1 4466 ? 186.021 177.583 161.374 1.00 23.05  ? 4466 HIS A CG    1 
ATOM   21552 N  ND1   . HIS A 1 4466 ? 184.793 178.194 161.499 1.00 32.83  ? 4466 HIS A ND1   1 
ATOM   21553 C  CD2   . HIS A 1 4466 ? 186.540 177.526 162.623 1.00 24.79  ? 4466 HIS A CD2   1 
ATOM   21554 C  CE1   . HIS A 1 4466 ? 184.579 178.495 162.767 1.00 31.39  ? 4466 HIS A CE1   1 
ATOM   21555 N  NE2   . HIS A 1 4466 ? 185.625 178.100 163.470 1.00 30.36  ? 4466 HIS A NE2   1 
ATOM   21556 N  N     . TYR A 1 4467 ? 186.822 174.380 157.802 1.00 22.84  ? 4467 TYR A N     1 
ATOM   21557 C  CA    . TYR A 1 4467 ? 187.059 173.971 156.427 1.00 16.82  ? 4467 TYR A CA    1 
ATOM   21558 C  C     . TYR A 1 4467 ? 186.416 172.610 156.211 1.00 17.91  ? 4467 TYR A C     1 
ATOM   21559 O  O     . TYR A 1 4467 ? 186.045 171.920 157.163 1.00 18.69  ? 4467 TYR A O     1 
ATOM   21560 C  CB    . TYR A 1 4467 ? 188.555 173.933 156.079 1.00 18.24  ? 4467 TYR A CB    1 
ATOM   21561 C  CG    . TYR A 1 4467 ? 189.423 173.136 157.027 1.00 19.13  ? 4467 TYR A CG    1 
ATOM   21562 C  CD1   . TYR A 1 4467 ? 190.007 173.734 158.134 1.00 17.21  ? 4467 TYR A CD1   1 
ATOM   21563 C  CD2   . TYR A 1 4467 ? 189.680 171.792 156.799 1.00 18.77  ? 4467 TYR A CD2   1 
ATOM   21564 C  CE1   . TYR A 1 4467 ? 190.810 173.014 158.995 1.00 17.38  ? 4467 TYR A CE1   1 
ATOM   21565 C  CE2   . TYR A 1 4467 ? 190.480 171.064 157.654 1.00 18.19  ? 4467 TYR A CE2   1 
ATOM   21566 C  CZ    . TYR A 1 4467 ? 191.043 171.679 158.750 1.00 21.02  ? 4467 TYR A CZ    1 
ATOM   21567 O  OH    . TYR A 1 4467 ? 191.842 170.954 159.604 1.00 22.52  ? 4467 TYR A OH    1 
ATOM   21568 N  N     . THR A 1 4468 ? 186.269 172.237 154.941 1.00 17.82  ? 4468 THR A N     1 
ATOM   21569 C  CA    . THR A 1 4468 ? 185.565 171.007 154.604 1.00 17.66  ? 4468 THR A CA    1 
ATOM   21570 C  C     . THR A 1 4468 ? 186.325 169.792 155.118 1.00 22.00  ? 4468 THR A C     1 
ATOM   21571 O  O     . THR A 1 4468 ? 187.531 169.652 154.893 1.00 25.58  ? 4468 THR A O     1 
ATOM   21572 C  CB    . THR A 1 4468 ? 185.368 170.904 153.094 1.00 15.06  ? 4468 THR A CB    1 
ATOM   21573 O  OG1   . THR A 1 4468 ? 184.673 172.064 152.621 1.00 18.66  ? 4468 THR A OG1   1 
ATOM   21574 C  CG2   . THR A 1 4468 ? 184.558 169.669 152.758 1.00 15.95  ? 4468 THR A CG2   1 
ATOM   21575 N  N     . VAL A 1 4469 ? 185.608 168.910 155.808 1.00 20.15  ? 4469 VAL A N     1 
ATOM   21576 C  CA    . VAL A 1 4469 ? 186.191 167.748 156.472 1.00 15.82  ? 4469 VAL A CA    1 
ATOM   21577 C  C     . VAL A 1 4469 ? 185.333 166.526 156.164 1.00 20.18  ? 4469 VAL A C     1 
ATOM   21578 O  O     . VAL A 1 4469 ? 184.103 166.646 156.071 1.00 24.12  ? 4469 VAL A O     1 
ATOM   21579 C  CB    . VAL A 1 4469 ? 186.304 167.987 157.989 1.00 19.81  ? 4469 VAL A CB    1 
ATOM   21580 C  CG1   . VAL A 1 4469 ? 186.804 166.753 158.703 1.00 21.02  ? 4469 VAL A CG1   1 
ATOM   21581 C  CG2   . VAL A 1 4469 ? 187.230 169.159 158.280 1.00 30.01  ? 4469 VAL A CG2   1 
ATOM   21582 N  N     . PRO A 1 4470 ? 185.926 165.344 155.982 1.00 20.76  ? 4470 PRO A N     1 
ATOM   21583 C  CA    . PRO A 1 4470 ? 185.117 164.122 155.922 1.00 16.39  ? 4470 PRO A CA    1 
ATOM   21584 C  C     . PRO A 1 4470 ? 184.318 163.937 157.203 1.00 22.70  ? 4470 PRO A C     1 
ATOM   21585 O  O     . PRO A 1 4470 ? 184.760 164.297 158.297 1.00 27.70  ? 4470 PRO A O     1 
ATOM   21586 C  CB    . PRO A 1 4470 ? 186.160 163.013 155.746 1.00 17.09  ? 4470 PRO A CB    1 
ATOM   21587 C  CG    . PRO A 1 4470 ? 187.322 163.687 155.121 1.00 17.33  ? 4470 PRO A CG    1 
ATOM   21588 C  CD    . PRO A 1 4470 ? 187.335 165.096 155.635 1.00 18.58  ? 4470 PRO A CD    1 
ATOM   21589 N  N     . ALA A 1 4471 ? 183.122 163.364 157.052 1.00 19.07  ? 4471 ALA A N     1 
ATOM   21590 C  CA    . ALA A 1 4471 ? 182.169 163.316 158.157 1.00 26.16  ? 4471 ALA A CA    1 
ATOM   21591 C  C     . ALA A 1 4471 ? 182.714 162.530 159.344 1.00 25.69  ? 4471 ALA A C     1 
ATOM   21592 O  O     . ALA A 1 4471 ? 182.522 162.926 160.500 1.00 25.47  ? 4471 ALA A O     1 
ATOM   21593 C  CB    . ALA A 1 4471 ? 180.847 162.717 157.681 1.00 29.13  ? 4471 ALA A CB    1 
ATOM   21594 N  N     . GLY A 1 4472 ? 183.390 161.417 159.084 1.00 20.94  ? 4472 GLY A N     1 
ATOM   21595 C  CA    . GLY A 1 4472 ? 183.829 160.529 160.137 1.00 27.68  ? 4472 GLY A CA    1 
ATOM   21596 C  C     . GLY A 1 4472 ? 185.194 160.808 160.726 1.00 32.45  ? 4472 GLY A C     1 
ATOM   21597 O  O     . GLY A 1 4472 ? 185.685 159.990 161.510 1.00 33.04  ? 4472 GLY A O     1 
ATOM   21598 N  N     . MET A 1 4473 ? 185.828 161.925 160.379 1.00 30.92  ? 4473 MET A N     1 
ATOM   21599 C  CA    . MET A 1 4473 ? 187.172 162.195 160.871 1.00 30.58  ? 4473 MET A CA    1 
ATOM   21600 C  C     . MET A 1 4473 ? 187.140 162.531 162.358 1.00 28.95  ? 4473 MET A C     1 
ATOM   21601 O  O     . MET A 1 4473 ? 186.319 163.336 162.808 1.00 23.92  ? 4473 MET A O     1 
ATOM   21602 C  CB    . MET A 1 4473 ? 187.816 163.331 160.077 1.00 28.21  ? 4473 MET A CB    1 
ATOM   21603 C  CG    . MET A 1 4473 ? 188.999 163.977 160.779 1.00 25.08  ? 4473 MET A CG    1 
ATOM   21604 S  SD    . MET A 1 4473 ? 189.761 165.318 159.850 1.00 35.07  ? 4473 MET A SD    1 
ATOM   21605 C  CE    . MET A 1 4473 ? 189.780 164.628 158.202 1.00 22.87  ? 4473 MET A CE    1 
ATOM   21606 N  N     . THR A 1 4474 ? 188.038 161.908 163.118 1.00 29.20  ? 4474 THR A N     1 
ATOM   21607 C  CA    . THR A 1 4474 ? 188.115 162.104 164.556 1.00 25.29  ? 4474 THR A CA    1 
ATOM   21608 C  C     . THR A 1 4474 ? 189.028 163.284 164.882 1.00 24.45  ? 4474 THR A C     1 
ATOM   21609 O  O     . THR A 1 4474 ? 189.556 163.962 163.998 1.00 29.63  ? 4474 THR A O     1 
ATOM   21610 C  CB    . THR A 1 4474 ? 188.599 160.829 165.243 1.00 25.56  ? 4474 THR A CB    1 
ATOM   21611 O  OG1   . THR A 1 4474 ? 189.959 160.571 164.875 1.00 28.82  ? 4474 THR A OG1   1 
ATOM   21612 C  CG2   . THR A 1 4474 ? 187.736 159.647 164.834 1.00 23.35  ? 4474 THR A CG2   1 
ATOM   21613 N  N     . VAL A 1 4475 ? 189.217 163.533 166.179 1.00 24.01  ? 4475 VAL A N     1 
ATOM   21614 C  CA    . VAL A 1 4475 ? 189.968 164.709 166.606 1.00 21.88  ? 4475 VAL A CA    1 
ATOM   21615 C  C     . VAL A 1 4475 ? 191.456 164.540 166.315 1.00 19.64  ? 4475 VAL A C     1 
ATOM   21616 O  O     . VAL A 1 4475 ? 192.139 165.500 165.947 1.00 24.01  ? 4475 VAL A O     1 
ATOM   21617 C  CB    . VAL A 1 4475 ? 189.711 164.997 168.096 1.00 25.47  ? 4475 VAL A CB    1 
ATOM   21618 C  CG1   . VAL A 1 4475 ? 190.563 166.155 168.560 1.00 28.06  ? 4475 VAL A CG1   1 
ATOM   21619 C  CG2   . VAL A 1 4475 ? 188.249 165.286 168.335 1.00 26.74  ? 4475 VAL A CG2   1 
ATOM   21620 N  N     . ILE A 1 4476 ? 191.986 163.327 166.490 1.00 20.56  ? 4476 ILE A N     1 
ATOM   21621 C  CA    . ILE A 1 4476 ? 193.402 163.084 166.220 1.00 21.93  ? 4476 ILE A CA    1 
ATOM   21622 C  C     . ILE A 1 4476 ? 193.720 163.350 164.753 1.00 18.34  ? 4476 ILE A C     1 
ATOM   21623 O  O     . ILE A 1 4476 ? 194.700 164.033 164.420 1.00 18.07  ? 4476 ILE A O     1 
ATOM   21624 C  CB    . ILE A 1 4476 ? 193.783 161.647 166.621 1.00 23.51  ? 4476 ILE A CB    1 
ATOM   21625 C  CG1   . ILE A 1 4476 ? 193.512 161.406 168.106 1.00 19.80  ? 4476 ILE A CG1   1 
ATOM   21626 C  CG2   . ILE A 1 4476 ? 195.243 161.370 166.300 1.00 23.13  ? 4476 ILE A CG2   1 
ATOM   21627 C  CD1   . ILE A 1 4476 ? 194.306 162.299 169.020 1.00 25.34  ? 4476 ILE A CD1   1 
ATOM   21628 N  N     . GLN A 1 4477 ? 192.890 162.814 163.856 1.00 18.11  ? 4477 GLN A N     1 
ATOM   21629 C  CA    . GLN A 1 4477 ? 193.097 163.026 162.429 1.00 20.86  ? 4477 GLN A CA    1 
ATOM   21630 C  C     . GLN A 1 4477 ? 192.979 164.499 162.070 1.00 23.82  ? 4477 GLN A C     1 
ATOM   21631 O  O     . GLN A 1 4477 ? 193.767 165.016 161.268 1.00 24.95  ? 4477 GLN A O     1 
ATOM   21632 C  CB    . GLN A 1 4477 ? 192.095 162.196 161.628 1.00 18.90  ? 4477 GLN A CB    1 
ATOM   21633 C  CG    . GLN A 1 4477 ? 191.999 160.747 162.070 1.00 19.47  ? 4477 GLN A CG    1 
ATOM   21634 C  CD    . GLN A 1 4477 ? 190.934 159.978 161.316 1.00 23.12  ? 4477 GLN A CD    1 
ATOM   21635 O  OE1   . GLN A 1 4477 ? 189.758 160.334 161.345 1.00 20.87  ? 4477 GLN A OE1   1 
ATOM   21636 N  NE2   . GLN A 1 4477 ? 191.343 158.916 160.632 1.00 27.59  ? 4477 GLN A NE2   1 
ATOM   21637 N  N     . TRP A 1 4478 ? 191.999 165.193 162.655 1.00 19.13  ? 4478 TRP A N     1 
ATOM   21638 C  CA    . TRP A 1 4478 ? 191.835 166.611 162.364 1.00 13.40  ? 4478 TRP A CA    1 
ATOM   21639 C  C     . TRP A 1 4478 ? 193.028 167.416 162.854 1.00 16.38  ? 4478 TRP A C     1 
ATOM   21640 O  O     . TRP A 1 4478 ? 193.463 168.355 162.185 1.00 20.25  ? 4478 TRP A O     1 
ATOM   21641 C  CB    . TRP A 1 4478 ? 190.546 167.145 162.985 1.00 14.28  ? 4478 TRP A CB    1 
ATOM   21642 C  CG    . TRP A 1 4478 ? 190.241 168.549 162.550 1.00 16.83  ? 4478 TRP A CG    1 
ATOM   21643 C  CD1   . TRP A 1 4478 ? 189.446 168.927 161.509 1.00 12.21  ? 4478 TRP A CD1   1 
ATOM   21644 C  CD2   . TRP A 1 4478 ? 190.741 169.761 163.132 1.00 17.24  ? 4478 TRP A CD2   1 
ATOM   21645 N  NE1   . TRP A 1 4478 ? 189.411 170.295 161.411 1.00 17.49  ? 4478 TRP A NE1   1 
ATOM   21646 C  CE2   . TRP A 1 4478 ? 190.199 170.831 162.395 1.00 19.06  ? 4478 TRP A CE2   1 
ATOM   21647 C  CE3   . TRP A 1 4478 ? 191.590 170.044 164.206 1.00 13.00  ? 4478 TRP A CE3   1 
ATOM   21648 C  CZ2   . TRP A 1 4478 ? 190.478 172.162 162.697 1.00 14.85  ? 4478 TRP A CZ2   1 
ATOM   21649 C  CZ3   . TRP A 1 4478 ? 191.867 171.364 164.503 1.00 16.32  ? 4478 TRP A CZ3   1 
ATOM   21650 C  CH2   . TRP A 1 4478 ? 191.312 172.407 163.752 1.00 18.99  ? 4478 TRP A CH2   1 
ATOM   21651 N  N     . VAL A 1 4479 ? 193.561 167.075 164.027 1.00 15.26  ? 4479 VAL A N     1 
ATOM   21652 C  CA    . VAL A 1 4479 ? 194.714 167.798 164.552 1.00 17.00  ? 4479 VAL A CA    1 
ATOM   21653 C  C     . VAL A 1 4479 ? 195.931 167.575 163.664 1.00 18.47  ? 4479 VAL A C     1 
ATOM   21654 O  O     . VAL A 1 4479 ? 196.679 168.516 163.369 1.00 23.06  ? 4479 VAL A O     1 
ATOM   21655 C  CB    . VAL A 1 4479 ? 194.984 167.390 166.011 1.00 16.24  ? 4479 VAL A CB    1 
ATOM   21656 C  CG1   . VAL A 1 4479 ? 196.392 167.785 166.426 1.00 19.73  ? 4479 VAL A CG1   1 
ATOM   21657 C  CG2   . VAL A 1 4479 ? 193.960 168.027 166.932 1.00 15.63  ? 4479 VAL A CG2   1 
ATOM   21658 N  N     . SER A 1 4480 ? 196.149 166.335 163.217 1.00 16.12  ? 4480 SER A N     1 
ATOM   21659 C  CA    . SER A 1 4480 ? 197.270 166.075 162.314 1.00 15.92  ? 4480 SER A CA    1 
ATOM   21660 C  C     . SER A 1 4480 ? 197.110 166.830 160.998 1.00 18.78  ? 4480 SER A C     1 
ATOM   21661 O  O     . SER A 1 4480 ? 198.067 167.440 160.498 1.00 20.91  ? 4480 SER A O     1 
ATOM   21662 C  CB    . SER A 1 4480 ? 197.404 164.574 162.061 1.00 18.39  ? 4480 SER A CB    1 
ATOM   21663 O  OG    . SER A 1 4480 ? 197.673 163.875 163.264 1.00 25.07  ? 4480 SER A OG    1 
ATOM   21664 N  N     . ASP A 1 4481 ? 195.903 166.809 160.426 1.00 17.54  ? 4481 ASP A N     1 
ATOM   21665 C  CA    . ASP A 1 4481 ? 195.653 167.528 159.181 1.00 17.92  ? 4481 ASP A CA    1 
ATOM   21666 C  C     . ASP A 1 4481 ? 195.838 169.029 159.363 1.00 20.79  ? 4481 ASP A C     1 
ATOM   21667 O  O     . ASP A 1 4481 ? 196.392 169.706 158.489 1.00 22.19  ? 4481 ASP A O     1 
ATOM   21668 C  CB    . ASP A 1 4481 ? 194.244 167.218 158.677 1.00 19.94  ? 4481 ASP A CB    1 
ATOM   21669 C  CG    . ASP A 1 4481 ? 194.148 167.229 157.167 1.00 32.10  ? 4481 ASP A CG    1 
ATOM   21670 O  OD1   . ASP A 1 4481 ? 193.015 167.236 156.644 1.00 29.00  ? 4481 ASP A OD1   1 
ATOM   21671 O  OD2   . ASP A 1 4481 ? 195.205 167.229 156.503 1.00 42.47  ? 4481 ASP A OD2   1 
ATOM   21672 N  N     . PHE A 1 4482 ? 195.371 169.566 160.490 1.00 17.92  ? 4482 PHE A N     1 
ATOM   21673 C  CA    . PHE A 1 4482 ? 195.515 170.987 160.770 1.00 15.06  ? 4482 PHE A CA    1 
ATOM   21674 C  C     . PHE A 1 4482 ? 196.979 171.369 160.924 1.00 18.27  ? 4482 PHE A C     1 
ATOM   21675 O  O     . PHE A 1 4482 ? 197.398 172.432 160.456 1.00 21.63  ? 4482 PHE A O     1 
ATOM   21676 C  CB    . PHE A 1 4482 ? 194.724 171.346 162.028 1.00 16.87  ? 4482 PHE A CB    1 
ATOM   21677 C  CG    . PHE A 1 4482 ? 194.685 172.815 162.325 1.00 15.95  ? 4482 PHE A CG    1 
ATOM   21678 C  CD1   . PHE A 1 4482 ? 194.020 173.687 161.481 1.00 16.15  ? 4482 PHE A CD1   1 
ATOM   21679 C  CD2   . PHE A 1 4482 ? 195.308 173.324 163.451 1.00 15.27  ? 4482 PHE A CD2   1 
ATOM   21680 C  CE1   . PHE A 1 4482 ? 193.982 175.036 161.752 1.00 14.88  ? 4482 PHE A CE1   1 
ATOM   21681 C  CE2   . PHE A 1 4482 ? 195.272 174.674 163.726 1.00 14.73  ? 4482 PHE A CE2   1 
ATOM   21682 C  CZ    . PHE A 1 4482 ? 194.608 175.530 162.876 1.00 18.06  ? 4482 PHE A CZ    1 
ATOM   21683 N  N     . SER A 1 4483 ? 197.771 170.519 161.581 1.00 18.20  ? 4483 SER A N     1 
ATOM   21684 C  CA    . SER A 1 4483 ? 199.201 170.780 161.686 1.00 20.34  ? 4483 SER A CA    1 
ATOM   21685 C  C     . SER A 1 4483 ? 199.858 170.783 160.312 1.00 19.59  ? 4483 SER A C     1 
ATOM   21686 O  O     . SER A 1 4483 ? 200.692 171.648 160.017 1.00 21.94  ? 4483 SER A O     1 
ATOM   21687 C  CB    . SER A 1 4483 ? 199.860 169.745 162.597 1.00 25.06  ? 4483 SER A CB    1 
ATOM   21688 O  OG    . SER A 1 4483 ? 199.127 169.583 163.798 1.00 26.26  ? 4483 SER A OG    1 
ATOM   21689 N  N     . GLU A 1 4484 ? 199.486 169.829 159.454 1.00 22.57  ? 4484 GLU A N     1 
ATOM   21690 C  CA    . GLU A 1 4484 ? 200.028 169.809 158.097 1.00 18.77  ? 4484 GLU A CA    1 
ATOM   21691 C  C     . GLU A 1 4484 ? 199.670 171.082 157.339 1.00 19.31  ? 4484 GLU A C     1 
ATOM   21692 O  O     . GLU A 1 4484 ? 200.523 171.685 156.673 1.00 19.91  ? 4484 GLU A O     1 
ATOM   21693 C  CB    . GLU A 1 4484 ? 199.512 168.580 157.349 1.00 19.52  ? 4484 GLU A CB    1 
ATOM   21694 C  CG    . GLU A 1 4484 ? 200.437 167.376 157.406 1.00 28.35  ? 4484 GLU A CG    1 
ATOM   21695 C  CD    . GLU A 1 4484 ? 201.851 167.703 156.973 1.00 34.08  ? 4484 GLU A CD    1 
ATOM   21696 O  OE1   . GLU A 1 4484 ? 202.018 168.320 155.901 1.00 37.14  ? 4484 GLU A OE1   1 
ATOM   21697 O  OE2   . GLU A 1 4484 ? 202.795 167.342 157.705 1.00 30.49  ? 4484 GLU A OE2   1 
ATOM   21698 N  N     . ARG A 1 4485 ? 198.410 171.511 157.438 1.00 19.39  ? 4485 ARG A N     1 
ATOM   21699 C  CA    . ARG A 1 4485 ? 197.969 172.712 156.737 1.00 18.47  ? 4485 ARG A CA    1 
ATOM   21700 C  C     . ARG A 1 4485 ? 198.671 173.957 157.265 1.00 18.84  ? 4485 ARG A C     1 
ATOM   21701 O  O     . ARG A 1 4485 ? 199.044 174.842 156.487 1.00 21.48  ? 4485 ARG A O     1 
ATOM   21702 C  CB    . ARG A 1 4485 ? 196.453 172.859 156.857 1.00 17.05  ? 4485 ARG A CB    1 
ATOM   21703 C  CG    . ARG A 1 4485 ? 195.674 171.751 156.174 1.00 15.84  ? 4485 ARG A CG    1 
ATOM   21704 C  CD    . ARG A 1 4485 ? 194.185 171.887 156.420 1.00 14.91  ? 4485 ARG A CD    1 
ATOM   21705 N  NE    . ARG A 1 4485 ? 193.435 170.800 155.804 1.00 17.01  ? 4485 ARG A NE    1 
ATOM   21706 C  CZ    . ARG A 1 4485 ? 192.471 170.968 154.911 1.00 18.76  ? 4485 ARG A CZ    1 
ATOM   21707 N  NH1   . ARG A 1 4485 ? 192.107 172.172 154.504 1.00 18.82  ? 4485 ARG A NH1   1 
ATOM   21708 N  NH2   . ARG A 1 4485 ? 191.857 169.900 154.411 1.00 18.92  ? 4485 ARG A NH2   1 
ATOM   21709 N  N     . ILE A 1 4486 ? 198.856 174.048 158.583 1.00 18.25  ? 4486 ILE A N     1 
ATOM   21710 C  CA    . ILE A 1 4486 ? 199.519 175.213 159.158 1.00 15.80  ? 4486 ILE A CA    1 
ATOM   21711 C  C     . ILE A 1 4486 ? 200.989 175.240 158.762 1.00 20.31  ? 4486 ILE A C     1 
ATOM   21712 O  O     . ILE A 1 4486 ? 201.552 176.309 158.508 1.00 24.24  ? 4486 ILE A O     1 
ATOM   21713 C  CB    . ILE A 1 4486 ? 199.335 175.240 160.686 1.00 18.65  ? 4486 ILE A CB    1 
ATOM   21714 C  CG1   . ILE A 1 4486 ? 197.864 175.457 161.043 1.00 17.25  ? 4486 ILE A CG1   1 
ATOM   21715 C  CG2   . ILE A 1 4486 ? 200.177 176.341 161.310 1.00 17.52  ? 4486 ILE A CG2   1 
ATOM   21716 C  CD1   . ILE A 1 4486 ? 197.272 176.719 160.463 1.00 15.53  ? 4486 ILE A CD1   1 
ATOM   21717 N  N     . LYS A 1 4487 ? 201.636 174.073 158.694 1.00 17.24  ? 4487 LYS A N     1 
ATOM   21718 C  CA    . LYS A 1 4487 ? 203.016 174.035 158.219 1.00 16.35  ? 4487 LYS A CA    1 
ATOM   21719 C  C     . LYS A 1 4487 ? 203.110 174.460 156.757 1.00 18.73  ? 4487 LYS A C     1 
ATOM   21720 O  O     . LYS A 1 4487 ? 204.040 175.181 156.370 1.00 20.77  ? 4487 LYS A O     1 
ATOM   21721 C  CB    . LYS A 1 4487 ? 203.610 172.642 158.426 1.00 17.97  ? 4487 LYS A CB    1 
ATOM   21722 C  CG    . LYS A 1 4487 ? 203.786 172.267 159.891 1.00 25.15  ? 4487 LYS A CG    1 
ATOM   21723 C  CD    . LYS A 1 4487 ? 204.524 170.950 160.057 1.00 23.81  ? 4487 LYS A CD    1 
ATOM   21724 C  CE    . LYS A 1 4487 ? 203.634 169.773 159.695 1.00 33.16  ? 4487 LYS A CE    1 
ATOM   21725 N  NZ    . LYS A 1 4487 ? 204.300 168.467 159.955 1.00 30.79  ? 4487 LYS A NZ    1 
ATOM   21726 N  N     . GLN A 1 4488 ? 202.155 174.029 155.928 1.00 17.77  ? 4488 GLN A N     1 
ATOM   21727 C  CA    . GLN A 1 4488 ? 202.140 174.477 154.538 1.00 17.84  ? 4488 GLN A CA    1 
ATOM   21728 C  C     . GLN A 1 4488 ? 201.947 175.986 154.447 1.00 20.30  ? 4488 GLN A C     1 
ATOM   21729 O  O     . GLN A 1 4488 ? 202.588 176.657 153.629 1.00 20.08  ? 4488 GLN A O     1 
ATOM   21730 C  CB    . GLN A 1 4488 ? 201.045 173.754 153.756 1.00 20.77  ? 4488 GLN A CB    1 
ATOM   21731 C  CG    . GLN A 1 4488 ? 200.838 174.304 152.354 1.00 24.25  ? 4488 GLN A CG    1 
ATOM   21732 C  CD    . GLN A 1 4488 ? 199.611 173.740 151.673 1.00 21.65  ? 4488 GLN A CD    1 
ATOM   21733 O  OE1   . GLN A 1 4488 ? 199.700 173.148 150.600 1.00 20.02  ? 4488 GLN A OE1   1 
ATOM   21734 N  NE2   . GLN A 1 4488 ? 198.453 173.927 152.293 1.00 23.48  ? 4488 GLN A NE2   1 
ATOM   21735 N  N     . LEU A 1 4489 ? 201.060 176.538 155.278 1.00 21.29  ? 4489 LEU A N     1 
ATOM   21736 C  CA    . LEU A 1 4489 ? 200.849 177.982 155.285 1.00 17.21  ? 4489 LEU A CA    1 
ATOM   21737 C  C     . LEU A 1 4489 ? 202.092 178.723 155.762 1.00 17.01  ? 4489 LEU A C     1 
ATOM   21738 O  O     . LEU A 1 4489 ? 202.401 179.810 155.264 1.00 18.29  ? 4489 LEU A O     1 
ATOM   21739 C  CB    . LEU A 1 4489 ? 199.642 178.330 156.153 1.00 16.21  ? 4489 LEU A CB    1 
ATOM   21740 C  CG    . LEU A 1 4489 ? 198.284 177.974 155.548 1.00 16.74  ? 4489 LEU A CG    1 
ATOM   21741 C  CD1   . LEU A 1 4489 ? 197.155 178.497 156.416 1.00 13.56  ? 4489 LEU A CD1   1 
ATOM   21742 C  CD2   . LEU A 1 4489 ? 198.171 178.521 154.136 1.00 13.79  ? 4489 LEU A CD2   1 
ATOM   21743 N  N     . GLN A 1 4490 ? 202.809 178.158 156.735 1.00 18.99  ? 4490 GLN A N     1 
ATOM   21744 C  CA    . GLN A 1 4490 ? 204.066 178.754 157.176 1.00 16.71  ? 4490 GLN A CA    1 
ATOM   21745 C  C     . GLN A 1 4490 ? 205.091 178.760 156.052 1.00 18.77  ? 4490 GLN A C     1 
ATOM   21746 O  O     . GLN A 1 4490 ? 205.817 179.743 155.868 1.00 23.35  ? 4490 GLN A O     1 
ATOM   21747 C  CB    . GLN A 1 4490 ? 204.611 177.997 158.387 1.00 13.21  ? 4490 GLN A CB    1 
ATOM   21748 C  CG    . GLN A 1 4490 ? 203.836 178.225 159.669 1.00 14.56  ? 4490 GLN A CG    1 
ATOM   21749 C  CD    . GLN A 1 4490 ? 204.464 177.524 160.855 1.00 18.97  ? 4490 GLN A CD    1 
ATOM   21750 O  OE1   . GLN A 1 4490 ? 204.736 176.326 160.809 1.00 20.99  ? 4490 GLN A OE1   1 
ATOM   21751 N  NE2   . GLN A 1 4490 ? 204.694 178.270 161.928 1.00 22.48  ? 4490 GLN A NE2   1 
ATOM   21752 N  N     . ASN A 1 4491 ? 205.166 177.665 155.292 1.00 21.60  ? 4491 ASN A N     1 
ATOM   21753 C  CA    . ASN A 1 4491 ? 206.065 177.625 154.143 1.00 19.85  ? 4491 ASN A CA    1 
ATOM   21754 C  C     . ASN A 1 4491 ? 205.673 178.668 153.104 1.00 20.27  ? 4491 ASN A C     1 
ATOM   21755 O  O     . ASN A 1 4491 ? 206.539 179.330 152.519 1.00 25.41  ? 4491 ASN A O     1 
ATOM   21756 C  CB    . ASN A 1 4491 ? 206.066 176.226 153.527 1.00 21.31  ? 4491 ASN A CB    1 
ATOM   21757 C  CG    . ASN A 1 4491 ? 206.853 175.228 154.351 1.00 29.32  ? 4491 ASN A CG    1 
ATOM   21758 O  OD1   . ASN A 1 4491 ? 206.329 174.192 154.758 1.00 27.23  ? 4491 ASN A OD1   1 
ATOM   21759 N  ND2   . ASN A 1 4491 ? 208.120 175.537 154.601 1.00 34.33  ? 4491 ASN A ND2   1 
ATOM   21760 N  N     . ILE A 1 4492 ? 204.371 178.827 152.862 1.00 21.93  ? 4492 ILE A N     1 
ATOM   21761 C  CA    . ILE A 1 4492 ? 203.898 179.825 151.905 1.00 23.85  ? 4492 ILE A CA    1 
ATOM   21762 C  C     . ILE A 1 4492 ? 204.264 181.229 152.372 1.00 25.98  ? 4492 ILE A C     1 
ATOM   21763 O  O     . ILE A 1 4492 ? 204.709 182.068 151.579 1.00 35.24  ? 4492 ILE A O     1 
ATOM   21764 C  CB    . ILE A 1 4492 ? 202.380 179.676 151.690 1.00 22.62  ? 4492 ILE A CB    1 
ATOM   21765 C  CG1   . ILE A 1 4492 ? 202.081 178.437 150.845 1.00 20.94  ? 4492 ILE A CG1   1 
ATOM   21766 C  CG2   . ILE A 1 4492 ? 201.803 180.922 151.035 1.00 19.48  ? 4492 ILE A CG2   1 
ATOM   21767 C  CD1   . ILE A 1 4492 ? 200.614 178.088 150.778 1.00 19.73  ? 4492 ILE A CD1   1 
ATOM   21768 N  N     . SER A 1 4493 ? 204.078 181.507 153.664 1.00 22.01  ? 4493 SER A N     1 
ATOM   21769 C  CA    . SER A 1 4493 ? 204.421 182.819 154.202 1.00 20.57  ? 4493 SER A CA    1 
ATOM   21770 C  C     . SER A 1 4493 ? 205.918 183.080 154.113 1.00 27.68  ? 4493 SER A C     1 
ATOM   21771 O  O     . SER A 1 4493 ? 206.342 184.197 153.794 1.00 35.11  ? 4493 SER A O     1 
ATOM   21772 C  CB    . SER A 1 4493 ? 203.943 182.932 155.650 1.00 21.62  ? 4493 SER A CB    1 
ATOM   21773 O  OG    . SER A 1 4493 ? 202.546 183.152 155.710 1.00 28.07  ? 4493 SER A OG    1 
ATOM   21774 N  N     . LEU A 1 4494 ? 206.734 182.066 154.404 1.00 27.69  ? 4494 LEU A N     1 
ATOM   21775 C  CA    . LEU A 1 4494 ? 208.179 182.225 154.287 1.00 27.84  ? 4494 LEU A CA    1 
ATOM   21776 C  C     . LEU A 1 4494 ? 208.586 182.489 152.844 1.00 33.40  ? 4494 LEU A C     1 
ATOM   21777 O  O     . LEU A 1 4494 ? 209.456 183.325 152.580 1.00 41.72  ? 4494 LEU A O     1 
ATOM   21778 C  CB    . LEU A 1 4494 ? 208.891 180.988 154.830 1.00 29.18  ? 4494 LEU A CB    1 
ATOM   21779 C  CG    . LEU A 1 4494 ? 210.419 181.052 154.827 1.00 38.62  ? 4494 LEU A CG    1 
ATOM   21780 C  CD1   . LEU A 1 4494 ? 210.905 182.175 155.727 1.00 34.40  ? 4494 LEU A CD1   1 
ATOM   21781 C  CD2   . LEU A 1 4494 ? 211.018 179.720 155.252 1.00 40.96  ? 4494 LEU A CD2   1 
ATOM   21782 N  N     . ALA A 1 4495 ? 207.968 181.782 151.895 1.00 33.19  ? 4495 ALA A N     1 
ATOM   21783 C  CA    . ALA A 1 4495 ? 208.260 182.022 150.486 1.00 35.27  ? 4495 ALA A CA    1 
ATOM   21784 C  C     . ALA A 1 4495 ? 207.860 183.433 150.073 1.00 40.34  ? 4495 ALA A C     1 
ATOM   21785 O  O     . ALA A 1 4495 ? 208.590 184.102 149.331 1.00 45.10  ? 4495 ALA A O     1 
ATOM   21786 C  CB    . ALA A 1 4495 ? 207.548 180.985 149.619 1.00 28.99  ? 4495 ALA A CB    1 
ATOM   21787 N  N     . ALA A 1 4496 ? 206.701 183.901 150.541 1.00 37.39  ? 4496 ALA A N     1 
ATOM   21788 C  CA    . ALA A 1 4496 ? 206.254 185.249 150.205 1.00 36.44  ? 4496 ALA A CA    1 
ATOM   21789 C  C     . ALA A 1 4496 ? 207.185 186.307 150.784 1.00 40.75  ? 4496 ALA A C     1 
ATOM   21790 O  O     . ALA A 1 4496 ? 207.518 187.286 150.106 1.00 45.47  ? 4496 ALA A O     1 
ATOM   21791 C  CB    . ALA A 1 4496 ? 204.826 185.466 150.701 1.00 31.61  ? 4496 ALA A CB    1 
ATOM   21792 N  N     . ALA A 1 4497 ? 207.612 186.131 152.036 1.00 43.07  ? 4497 ALA A N     1 
ATOM   21793 C  CA    . ALA A 1 4497 ? 208.489 187.115 152.662 1.00 42.69  ? 4497 ALA A CA    1 
ATOM   21794 C  C     . ALA A 1 4497 ? 209.875 187.113 152.027 1.00 49.52  ? 4497 ALA A C     1 
ATOM   21795 O  O     . ALA A 1 4497 ? 210.432 188.178 151.739 1.00 49.80  ? 4497 ALA A O     1 
ATOM   21796 C  CB    . ALA A 1 4497 ? 208.585 186.851 154.163 1.00 33.71  ? 4497 ALA A CB    1 
ATOM   21797 N  N     . SER A 1 4498 ? 210.448 185.927 151.804 1.00 49.77  ? 4498 SER A N     1 
ATOM   21798 C  CA    . SER A 1 4498 ? 211.779 185.842 151.211 1.00 51.83  ? 4498 SER A CA    1 
ATOM   21799 C  C     . SER A 1 4498 ? 211.787 186.368 149.781 1.00 51.04  ? 4498 SER A C     1 
ATOM   21800 O  O     . SER A 1 4498 ? 212.730 187.055 149.372 1.00 56.63  ? 4498 SER A O     1 
ATOM   21801 C  CB    . SER A 1 4498 ? 212.279 184.399 151.254 1.00 57.52  ? 4498 SER A CB    1 
ATOM   21802 O  OG    . SER A 1 4498 ? 212.313 183.908 152.583 1.00 57.63  ? 4498 SER A OG    1 
ATOM   21803 N  N     . GLY A 1 4499 ? 210.752 186.052 149.008 1.00 54.64  ? 4499 GLY A N     1 
ATOM   21804 C  CA    . GLY A 1 4499 ? 210.666 186.503 147.633 1.00 55.99  ? 4499 GLY A CA    1 
ATOM   21805 C  C     . GLY A 1 4499 ? 209.681 187.637 147.445 1.00 55.53  ? 4499 GLY A C     1 
ATOM   21806 O  O     . GLY A 1 4499 ? 209.994 188.797 147.729 1.00 59.53  ? 4499 GLY A O     1 
ATOM   21807 N  N     . GLY A 1 4500 ? 208.490 187.313 146.963 1.00 56.47  ? 4500 GLY A N     1 
ATOM   21808 C  CA    . GLY A 1 4500 ? 207.479 188.327 146.753 1.00 56.96  ? 4500 GLY A CA    1 
ATOM   21809 C  C     . GLY A 1 4500 ? 206.274 187.742 146.058 1.00 65.17  ? 4500 GLY A C     1 
ATOM   21810 O  O     . GLY A 1 4500 ? 206.062 186.528 146.068 1.00 60.05  ? 4500 GLY A O     1 
ATOM   21811 N  N     . ALA A 1 4501 ? 205.477 188.626 145.453 1.00 67.38  ? 4501 ALA A N     1 
ATOM   21812 C  CA    . ALA A 1 4501 ? 204.315 188.173 144.697 1.00 65.95  ? 4501 ALA A CA    1 
ATOM   21813 C  C     . ALA A 1 4501 ? 204.722 187.313 143.509 1.00 62.86  ? 4501 ALA A C     1 
ATOM   21814 O  O     . ALA A 1 4501 ? 203.991 186.390 143.132 1.00 60.28  ? 4501 ALA A O     1 
ATOM   21815 C  CB    . ALA A 1 4501 ? 203.489 189.372 144.230 1.00 60.74  ? 4501 ALA A CB    1 
ATOM   21816 N  N     . LYS A 1 4502 ? 205.877 187.600 142.905 1.00 58.54  ? 4502 LYS A N     1 
ATOM   21817 C  CA    . LYS A 1 4502 ? 206.356 186.773 141.802 1.00 60.35  ? 4502 LYS A CA    1 
ATOM   21818 C  C     . LYS A 1 4502 ? 206.832 185.410 142.289 1.00 62.16  ? 4502 LYS A C     1 
ATOM   21819 O  O     . LYS A 1 4502 ? 206.762 184.428 141.542 1.00 57.85  ? 4502 LYS A O     1 
ATOM   21820 C  CB    . LYS A 1 4502 ? 207.474 187.497 141.050 1.00 61.52  ? 4502 LYS A CB    1 
ATOM   21821 C  CG    . LYS A 1 4502 ? 208.738 187.722 141.866 1.00 68.81  ? 4502 LYS A CG    1 
ATOM   21822 C  CD    . LYS A 1 4502 ? 209.785 188.482 141.067 1.00 73.94  ? 4502 LYS A CD    1 
ATOM   21823 C  CE    . LYS A 1 4502 ? 211.054 188.689 141.878 1.00 77.29  ? 4502 LYS A CE    1 
ATOM   21824 N  NZ    . LYS A 1 4502 ? 212.089 189.436 141.112 1.00 74.64  ? 4502 LYS A NZ    1 
ATOM   21825 N  N     . GLU A 1 4503 ? 207.320 185.331 143.529 1.00 58.11  ? 4503 GLU A N     1 
ATOM   21826 C  CA    . GLU A 1 4503 ? 207.780 184.056 144.068 1.00 56.38  ? 4503 GLU A CA    1 
ATOM   21827 C  C     . GLU A 1 4503 ? 206.613 183.119 144.356 1.00 54.28  ? 4503 GLU A C     1 
ATOM   21828 O  O     . GLU A 1 4503 ? 206.767 181.894 144.278 1.00 54.62  ? 4503 GLU A O     1 
ATOM   21829 C  CB    . GLU A 1 4503 ? 208.609 184.301 145.332 1.00 63.41  ? 4503 GLU A CB    1 
ATOM   21830 C  CG    . GLU A 1 4503 ? 208.814 183.089 146.227 1.00 56.51  ? 4503 GLU A CG    1 
ATOM   21831 C  CD    . GLU A 1 4503 ? 209.786 182.086 145.636 1.00 72.09  ? 4503 GLU A CD    1 
ATOM   21832 O  OE1   . GLU A 1 4503 ? 210.764 182.517 144.988 1.00 71.81  ? 4503 GLU A OE1   1 
ATOM   21833 O  OE2   . GLU A 1 4503 ? 209.577 180.869 145.822 1.00 69.22  ? 4503 GLU A OE2   1 
ATOM   21834 N  N     . LEU A 1 4504 ? 205.438 183.673 144.666 1.00 53.12  ? 4504 LEU A N     1 
ATOM   21835 C  CA    . LEU A 1 4504 ? 204.275 182.853 144.988 1.00 44.63  ? 4504 LEU A CA    1 
ATOM   21836 C  C     . LEU A 1 4504 ? 203.815 182.002 143.813 1.00 38.50  ? 4504 LEU A C     1 
ATOM   21837 O  O     . LEU A 1 4504 ? 203.077 181.033 144.016 1.00 41.38  ? 4504 LEU A O     1 
ATOM   21838 C  CB    . LEU A 1 4504 ? 203.123 183.739 145.462 1.00 42.79  ? 4504 LEU A CB    1 
ATOM   21839 C  CG    . LEU A 1 4504 ? 203.332 184.480 146.781 1.00 43.59  ? 4504 LEU A CG    1 
ATOM   21840 C  CD1   . LEU A 1 4504 ? 202.172 185.422 147.050 1.00 38.70  ? 4504 LEU A CD1   1 
ATOM   21841 C  CD2   . LEU A 1 4504 ? 203.498 183.488 147.921 1.00 37.81  ? 4504 LEU A CD2   1 
ATOM   21842 N  N     . LYS A 1 4505 ? 204.223 182.343 142.592 1.00 37.53  ? 4505 LYS A N     1 
ATOM   21843 C  CA    . LYS A 1 4505 ? 203.820 181.562 141.430 1.00 33.64  ? 4505 LYS A CA    1 
ATOM   21844 C  C     . LYS A 1 4505 ? 204.596 180.255 141.321 1.00 33.31  ? 4505 LYS A C     1 
ATOM   21845 O  O     . LYS A 1 4505 ? 204.048 179.253 140.848 1.00 40.00  ? 4505 LYS A O     1 
ATOM   21846 C  CB    . LYS A 1 4505 ? 203.995 182.396 140.159 1.00 31.26  ? 4505 LYS A CB    1 
ATOM   21847 C  CG    . LYS A 1 4505 ? 203.445 181.756 138.897 1.00 26.93  ? 4505 LYS A CG    1 
ATOM   21848 C  CD    . LYS A 1 4505 ? 204.545 181.076 138.108 1.00 32.90  ? 4505 LYS A CD    1 
ATOM   21849 C  CE    . LYS A 1 4505 ? 204.010 180.423 136.854 1.00 31.50  ? 4505 LYS A CE    1 
ATOM   21850 N  NZ    . LYS A 1 4505 ? 205.090 179.682 136.156 1.00 32.45  ? 4505 LYS A NZ    1 
ATOM   21851 N  N     . ASN A 1 4506 ? 205.854 180.239 141.751 1.00 34.12  ? 4506 ASN A N     1 
ATOM   21852 C  CA    . ASN A 1 4506 ? 206.724 179.086 141.569 1.00 29.76  ? 4506 ASN A CA    1 
ATOM   21853 C  C     . ASN A 1 4506 ? 206.642 178.076 142.706 1.00 30.64  ? 4506 ASN A C     1 
ATOM   21854 O  O     . ASN A 1 4506 ? 207.346 177.063 142.661 1.00 33.06  ? 4506 ASN A O     1 
ATOM   21855 C  CB    . ASN A 1 4506 ? 208.176 179.545 141.401 1.00 37.31  ? 4506 ASN A CB    1 
ATOM   21856 C  CG    . ASN A 1 4506 ? 208.385 180.363 140.144 1.00 43.33  ? 4506 ASN A CG    1 
ATOM   21857 O  OD1   . ASN A 1 4506 ? 208.650 181.563 140.206 1.00 49.17  ? 4506 ASN A OD1   1 
ATOM   21858 N  ND2   . ASN A 1 4506 ? 208.267 179.714 138.992 1.00 39.76  ? 4506 ASN A ND2   1 
ATOM   21859 N  N     . ILE A 1 4507 ? 205.819 178.315 143.709 1.00 31.71  ? 4507 ILE A N     1 
ATOM   21860 C  CA    . ILE A 1 4507 ? 205.688 177.383 144.822 1.00 32.07  ? 4507 ILE A CA    1 
ATOM   21861 C  C     . ILE A 1 4507 ? 204.687 176.301 144.446 1.00 32.37  ? 4507 ILE A C     1 
ATOM   21862 O  O     . ILE A 1 4507 ? 203.737 176.532 143.691 1.00 34.75  ? 4507 ILE A O     1 
ATOM   21863 C  CB    . ILE A 1 4507 ? 205.274 178.106 146.120 1.00 32.99  ? 4507 ILE A CB    1 
ATOM   21864 C  CG1   . ILE A 1 4507 ? 203.852 178.656 146.003 1.00 32.71  ? 4507 ILE A CG1   1 
ATOM   21865 C  CG2   . ILE A 1 4507 ? 206.257 179.220 146.445 1.00 36.13  ? 4507 ILE A CG2   1 
ATOM   21866 C  CD1   . ILE A 1 4507 ? 203.268 179.115 147.318 1.00 33.39  ? 4507 ILE A CD1   1 
ATOM   21867 N  N     . HIS A 1 4508 ? 204.912 175.100 144.967 1.00 30.76  ? 4508 HIS A N     1 
ATOM   21868 C  CA    . HIS A 1 4508 ? 204.001 173.979 144.783 1.00 20.47  ? 4508 HIS A CA    1 
ATOM   21869 C  C     . HIS A 1 4508 ? 203.146 173.845 146.035 1.00 25.46  ? 4508 HIS A C     1 
ATOM   21870 O  O     . HIS A 1 4508 ? 203.678 173.720 147.143 1.00 38.55  ? 4508 HIS A O     1 
ATOM   21871 C  CB    . HIS A 1 4508 ? 204.763 172.684 144.511 1.00 22.29  ? 4508 HIS A CB    1 
ATOM   21872 C  CG    . HIS A 1 4508 ? 205.870 172.829 143.515 1.00 27.69  ? 4508 HIS A CG    1 
ATOM   21873 N  ND1   . HIS A 1 4508 ? 205.658 173.270 142.226 1.00 31.68  ? 4508 HIS A ND1   1 
ATOM   21874 C  CD2   . HIS A 1 4508 ? 207.196 172.576 143.613 1.00 25.93  ? 4508 HIS A CD2   1 
ATOM   21875 C  CE1   . HIS A 1 4508 ? 206.808 173.293 141.577 1.00 30.41  ? 4508 HIS A CE1   1 
ATOM   21876 N  NE2   . HIS A 1 4508 ? 207.757 172.875 142.395 1.00 31.98  ? 4508 HIS A NE2   1 
ATOM   21877 N  N     . VAL A 1 4509 ? 201.830 173.873 145.860 1.00 22.97  ? 4509 VAL A N     1 
ATOM   21878 C  CA    . VAL A 1 4509 ? 200.904 173.792 146.977 1.00 23.14  ? 4509 VAL A CA    1 
ATOM   21879 C  C     . VAL A 1 4509 ? 200.198 172.445 146.942 1.00 21.06  ? 4509 VAL A C     1 
ATOM   21880 O  O     . VAL A 1 4509 ? 200.102 171.783 145.904 1.00 20.93  ? 4509 VAL A O     1 
ATOM   21881 C  CB    . VAL A 1 4509 ? 199.877 174.943 146.965 1.00 19.44  ? 4509 VAL A CB    1 
ATOM   21882 C  CG1   . VAL A 1 4509 ? 200.580 176.283 147.096 1.00 23.43  ? 4509 VAL A CG1   1 
ATOM   21883 C  CG2   . VAL A 1 4509 ? 199.034 174.890 145.704 1.00 19.52  ? 4509 VAL A CG2   1 
ATOM   21884 N  N     . CYS A 1 4510 ? 199.701 172.038 148.105 1.00 20.01  ? 4510 CYS A N     1 
ATOM   21885 C  CA    . CYS A 1 4510 ? 198.865 170.852 148.234 1.00 15.69  ? 4510 CYS A CA    1 
ATOM   21886 C  C     . CYS A 1 4510 ? 197.413 171.314 148.248 1.00 19.04  ? 4510 CYS A C     1 
ATOM   21887 O  O     . CYS A 1 4510 ? 196.998 172.050 149.150 1.00 15.34  ? 4510 CYS A O     1 
ATOM   21888 C  CB    . CYS A 1 4510 ? 199.216 170.071 149.498 1.00 17.56  ? 4510 CYS A CB    1 
ATOM   21889 S  SG    . CYS A 1 4510 ? 198.226 168.581 149.760 1.00 28.36  ? 4510 CYS A SG    1 
ATOM   21890 N  N     . LEU A 1 4511 ? 196.646 170.888 147.242 1.00 18.53  ? 4511 LEU A N     1 
ATOM   21891 C  CA    . LEU A 1 4511 ? 195.259 171.326 147.132 1.00 13.26  ? 4511 LEU A CA    1 
ATOM   21892 C  C     . LEU A 1 4511 ? 194.424 170.853 148.314 1.00 14.40  ? 4511 LEU A C     1 
ATOM   21893 O  O     . LEU A 1 4511 ? 193.482 171.540 148.721 1.00 19.71  ? 4511 LEU A O     1 
ATOM   21894 C  CB    . LEU A 1 4511 ? 194.654 170.826 145.821 1.00 12.92  ? 4511 LEU A CB    1 
ATOM   21895 C  CG    . LEU A 1 4511 ? 194.929 171.672 144.577 1.00 14.69  ? 4511 LEU A CG    1 
ATOM   21896 C  CD1   . LEU A 1 4511 ? 194.077 171.200 143.411 1.00 18.99  ? 4511 LEU A CD1   1 
ATOM   21897 C  CD2   . LEU A 1 4511 ? 194.688 173.145 144.860 1.00 16.84  ? 4511 LEU A CD2   1 
ATOM   21898 N  N     . GLY A 1 4512 ? 194.752 169.689 148.877 1.00 13.84  ? 4512 GLY A N     1 
ATOM   21899 C  CA    . GLY A 1 4512 ? 194.037 169.206 150.043 1.00 14.63  ? 4512 GLY A CA    1 
ATOM   21900 C  C     . GLY A 1 4512 ? 194.352 169.963 151.314 1.00 20.17  ? 4512 GLY A C     1 
ATOM   21901 O  O     . GLY A 1 4512 ? 193.554 169.931 152.255 1.00 22.78  ? 4512 GLY A O     1 
ATOM   21902 N  N     . GLY A 1 4513 ? 195.494 170.641 151.363 1.00 17.33  ? 4513 GLY A N     1 
ATOM   21903 C  CA    . GLY A 1 4513 ? 195.889 171.443 152.498 1.00 13.72  ? 4513 GLY A CA    1 
ATOM   21904 C  C     . GLY A 1 4513 ? 195.424 172.881 152.460 1.00 19.29  ? 4513 GLY A C     1 
ATOM   21905 O  O     . GLY A 1 4513 ? 195.794 173.662 153.343 1.00 26.80  ? 4513 GLY A O     1 
ATOM   21906 N  N     . LEU A 1 4514 ? 194.631 173.260 151.464 1.00 18.71  ? 4514 LEU A N     1 
ATOM   21907 C  CA    . LEU A 1 4514 ? 194.097 174.608 151.348 1.00 16.34  ? 4514 LEU A CA    1 
ATOM   21908 C  C     . LEU A 1 4514 ? 192.634 174.618 151.766 1.00 18.36  ? 4514 LEU A C     1 
ATOM   21909 O  O     . LEU A 1 4514 ? 191.892 173.673 151.481 1.00 25.63  ? 4514 LEU A O     1 
ATOM   21910 C  CB    . LEU A 1 4514 ? 194.236 175.132 149.919 1.00 17.12  ? 4514 LEU A CB    1 
ATOM   21911 C  CG    . LEU A 1 4514 ? 195.659 175.303 149.388 1.00 15.50  ? 4514 LEU A CG    1 
ATOM   21912 C  CD1   . LEU A 1 4514 ? 195.635 175.716 147.928 1.00 16.31  ? 4514 LEU A CD1   1 
ATOM   21913 C  CD2   . LEU A 1 4514 ? 196.420 176.318 150.220 1.00 16.80  ? 4514 LEU A CD2   1 
ATOM   21914 N  N     . PHE A 1 4515 ? 192.227 175.688 152.452 1.00 18.39  ? 4515 PHE A N     1 
ATOM   21915 C  CA    . PHE A 1 4515 ? 190.844 175.785 152.909 1.00 23.26  ? 4515 PHE A CA    1 
ATOM   21916 C  C     . PHE A 1 4515 ? 189.879 175.827 151.732 1.00 23.80  ? 4515 PHE A C     1 
ATOM   21917 O  O     . PHE A 1 4515 ? 188.824 175.184 151.758 1.00 33.46  ? 4515 PHE A O     1 
ATOM   21918 C  CB    . PHE A 1 4515 ? 190.667 177.018 153.794 1.00 23.54  ? 4515 PHE A CB    1 
ATOM   21919 C  CG    . PHE A 1 4515 ? 191.541 177.018 155.015 1.00 26.20  ? 4515 PHE A CG    1 
ATOM   21920 C  CD1   . PHE A 1 4515 ? 192.805 177.580 154.977 1.00 23.57  ? 4515 PHE A CD1   1 
ATOM   21921 C  CD2   . PHE A 1 4515 ? 191.107 176.443 156.195 1.00 22.64  ? 4515 PHE A CD2   1 
ATOM   21922 C  CE1   . PHE A 1 4515 ? 193.613 177.577 156.094 1.00 27.05  ? 4515 PHE A CE1   1 
ATOM   21923 C  CE2   . PHE A 1 4515 ? 191.913 176.437 157.315 1.00 23.15  ? 4515 PHE A CE2   1 
ATOM   21924 C  CZ    . PHE A 1 4515 ? 193.166 177.003 157.265 1.00 24.55  ? 4515 PHE A CZ    1 
ATOM   21925 N  N     . VAL A 1 4516 ? 190.222 176.582 150.694 1.00 23.15  ? 4516 VAL A N     1 
ATOM   21926 C  CA    . VAL A 1 4516 ? 189.412 176.682 149.482 1.00 21.69  ? 4516 VAL A CA    1 
ATOM   21927 C  C     . VAL A 1 4516 ? 190.293 176.460 148.253 1.00 20.75  ? 4516 VAL A C     1 
ATOM   21928 O  O     . VAL A 1 4516 ? 190.878 177.410 147.715 1.00 23.31  ? 4516 VAL A O     1 
ATOM   21929 C  CB    . VAL A 1 4516 ? 188.645 178.016 149.445 1.00 19.23  ? 4516 VAL A CB    1 
ATOM   21930 C  CG1   . VAL A 1 4516 ? 187.627 178.054 150.563 1.00 21.71  ? 4516 VAL A CG1   1 
ATOM   21931 C  CG2   . VAL A 1 4516 ? 189.588 179.189 149.666 1.00 18.89  ? 4516 VAL A CG2   1 
ATOM   21932 N  N     . PRO A 1 4517 ? 190.425 175.217 147.781 1.00 18.96  ? 4517 PRO A N     1 
ATOM   21933 C  CA    . PRO A 1 4517 ? 191.283 174.970 146.611 1.00 18.30  ? 4517 PRO A CA    1 
ATOM   21934 C  C     . PRO A 1 4517 ? 190.697 175.483 145.306 1.00 19.39  ? 4517 PRO A C     1 
ATOM   21935 O  O     . PRO A 1 4517 ? 191.457 175.834 144.393 1.00 21.46  ? 4517 PRO A O     1 
ATOM   21936 C  CB    . PRO A 1 4517 ? 191.432 173.444 146.604 1.00 20.28  ? 4517 PRO A CB    1 
ATOM   21937 C  CG    . PRO A 1 4517 ? 190.208 172.945 147.287 1.00 23.73  ? 4517 PRO A CG    1 
ATOM   21938 C  CD    . PRO A 1 4517 ? 189.831 173.978 148.312 1.00 19.48  ? 4517 PRO A CD    1 
ATOM   21939 N  N     . GLU A 1 4518 ? 189.368 175.530 145.183 1.00 19.74  ? 4518 GLU A N     1 
ATOM   21940 C  CA    . GLU A 1 4518 ? 188.769 176.104 143.984 1.00 18.08  ? 4518 GLU A CA    1 
ATOM   21941 C  C     . GLU A 1 4518 ? 189.133 177.575 143.843 1.00 23.37  ? 4518 GLU A C     1 
ATOM   21942 O  O     . GLU A 1 4518 ? 189.291 178.074 142.721 1.00 24.13  ? 4518 GLU A O     1 
ATOM   21943 C  CB    . GLU A 1 4518 ? 187.250 175.913 144.008 1.00 21.87  ? 4518 GLU A CB    1 
ATOM   21944 C  CG    . GLU A 1 4518 ? 186.514 176.728 145.061 1.00 29.68  ? 4518 GLU A CG    1 
ATOM   21945 C  CD    . GLU A 1 4518 ? 186.484 176.051 146.420 1.00 35.42  ? 4518 GLU A CD    1 
ATOM   21946 O  OE1   . GLU A 1 4518 ? 187.269 175.107 146.640 1.00 31.57  ? 4518 GLU A OE1   1 
ATOM   21947 O  OE2   . GLU A 1 4518 ? 185.672 176.468 147.272 1.00 37.52  ? 4518 GLU A OE2   1 
ATOM   21948 N  N     . ALA A 1 4519 ? 189.301 178.274 144.967 1.00 21.60  ? 4519 ALA A N     1 
ATOM   21949 C  CA    . ALA A 1 4519 ? 189.804 179.640 144.914 1.00 19.15  ? 4519 ALA A CA    1 
ATOM   21950 C  C     . ALA A 1 4519 ? 191.229 179.676 144.382 1.00 20.26  ? 4519 ALA A C     1 
ATOM   21951 O  O     . ALA A 1 4519 ? 191.605 180.610 143.670 1.00 27.11  ? 4519 ALA A O     1 
ATOM   21952 C  CB    . ALA A 1 4519 ? 189.727 180.287 146.295 1.00 15.63  ? 4519 ALA A CB    1 
ATOM   21953 N  N     . TYR A 1 4520 ? 192.040 178.668 144.715 1.00 17.37  ? 4520 TYR A N     1 
ATOM   21954 C  CA    . TYR A 1 4520 ? 193.385 178.599 144.151 1.00 16.55  ? 4520 TYR A CA    1 
ATOM   21955 C  C     . TYR A 1 4520 ? 193.343 178.394 142.644 1.00 17.94  ? 4520 TYR A C     1 
ATOM   21956 O  O     . TYR A 1 4520 ? 194.116 179.014 141.903 1.00 21.36  ? 4520 TYR A O     1 
ATOM   21957 C  CB    . TYR A 1 4520 ? 194.190 177.478 144.802 1.00 15.19  ? 4520 TYR A CB    1 
ATOM   21958 C  CG    . TYR A 1 4520 ? 195.573 177.336 144.210 1.00 16.44  ? 4520 TYR A CG    1 
ATOM   21959 C  CD1   . TYR A 1 4520 ? 196.549 178.293 144.444 1.00 17.30  ? 4520 TYR A CD1   1 
ATOM   21960 C  CD2   . TYR A 1 4520 ? 195.896 176.258 143.399 1.00 16.25  ? 4520 TYR A CD2   1 
ATOM   21961 C  CE1   . TYR A 1 4520 ? 197.810 178.173 143.900 1.00 18.06  ? 4520 TYR A CE1   1 
ATOM   21962 C  CE2   . TYR A 1 4520 ? 197.154 176.130 142.852 1.00 13.93  ? 4520 TYR A CE2   1 
ATOM   21963 C  CZ    . TYR A 1 4520 ? 198.107 177.090 143.104 1.00 15.80  ? 4520 TYR A CZ    1 
ATOM   21964 O  OH    . TYR A 1 4520 ? 199.363 176.966 142.559 1.00 19.41  ? 4520 TYR A OH    1 
ATOM   21965 N  N     . ILE A 1 4521 ? 192.463 177.508 142.172 1.00 16.17  ? 4521 ILE A N     1 
ATOM   21966 C  CA    . ILE A 1 4521 ? 192.340 177.295 140.732 1.00 12.99  ? 4521 ILE A CA    1 
ATOM   21967 C  C     . ILE A 1 4521 ? 191.916 178.584 140.042 1.00 15.66  ? 4521 ILE A C     1 
ATOM   21968 O  O     . ILE A 1 4521 ? 192.467 178.964 138.999 1.00 21.36  ? 4521 ILE A O     1 
ATOM   21969 C  CB    . ILE A 1 4521 ? 191.360 176.144 140.439 1.00 14.35  ? 4521 ILE A CB    1 
ATOM   21970 C  CG1   . ILE A 1 4521 ? 191.655 174.944 141.340 1.00 18.55  ? 4521 ILE A CG1   1 
ATOM   21971 C  CG2   . ILE A 1 4521 ? 191.431 175.742 138.977 1.00 12.56  ? 4521 ILE A CG2   1 
ATOM   21972 C  CD1   . ILE A 1 4521 ? 192.909 174.192 140.965 1.00 16.52  ? 4521 ILE A CD1   1 
ATOM   21973 N  N     . THR A 1 4522 ? 190.937 179.283 140.622 1.00 19.38  ? 4522 THR A N     1 
ATOM   21974 C  CA    . THR A 1 4522 ? 190.489 180.548 140.051 1.00 16.55  ? 4522 THR A CA    1 
ATOM   21975 C  C     . THR A 1 4522 ? 191.603 181.587 140.060 1.00 17.84  ? 4522 THR A C     1 
ATOM   21976 O  O     . THR A 1 4522 ? 191.748 182.358 139.107 1.00 21.21  ? 4522 THR A O     1 
ATOM   21977 C  CB    . THR A 1 4522 ? 189.268 181.064 140.812 1.00 17.74  ? 4522 THR A CB    1 
ATOM   21978 O  OG1   . THR A 1 4522 ? 188.283 180.027 140.897 1.00 25.38  ? 4522 THR A OG1   1 
ATOM   21979 C  CG2   . THR A 1 4522 ? 188.669 182.272 140.110 1.00 16.02  ? 4522 THR A CG2   1 
ATOM   21980 N  N     . ALA A 1 4523 ? 192.396 181.630 141.133 1.00 18.40  ? 4523 ALA A N     1 
ATOM   21981 C  CA    . ALA A 1 4523 ? 193.489 182.592 141.218 1.00 16.27  ? 4523 ALA A CA    1 
ATOM   21982 C  C     . ALA A 1 4523 ? 194.559 182.313 140.172 1.00 16.74  ? 4523 ALA A C     1 
ATOM   21983 O  O     . ALA A 1 4523 ? 195.094 183.245 139.564 1.00 21.80  ? 4523 ALA A O     1 
ATOM   21984 C  CB    . ALA A 1 4523 ? 194.094 182.576 142.621 1.00 22.95  ? 4523 ALA A CB    1 
ATOM   21985 N  N     . THR A 1 4524 ? 194.895 181.039 139.956 1.00 16.90  ? 4524 THR A N     1 
ATOM   21986 C  CA    . THR A 1 4524 ? 195.863 180.702 138.915 1.00 14.46  ? 4524 THR A CA    1 
ATOM   21987 C  C     . THR A 1 4524 ? 195.328 181.060 137.534 1.00 15.56  ? 4524 THR A C     1 
ATOM   21988 O  O     . THR A 1 4524 ? 196.064 181.586 136.688 1.00 20.73  ? 4524 THR A O     1 
ATOM   21989 C  CB    . THR A 1 4524 ? 196.220 179.217 138.983 1.00 12.25  ? 4524 THR A CB    1 
ATOM   21990 O  OG1   . THR A 1 4524 ? 195.031 178.432 138.837 1.00 16.45  ? 4524 THR A OG1   1 
ATOM   21991 C  CG2   . THR A 1 4524 ? 196.878 178.890 140.309 1.00 13.24  ? 4524 THR A CG2   1 
ATOM   21992 N  N     . ARG A 1 4525 ? 194.044 180.787 137.294 1.00 14.63  ? 4525 ARG A N     1 
ATOM   21993 C  CA    . ARG A 1 4525 ? 193.428 181.165 136.026 1.00 15.92  ? 4525 ARG A CA    1 
ATOM   21994 C  C     . ARG A 1 4525 ? 193.471 182.677 135.825 1.00 16.69  ? 4525 ARG A C     1 
ATOM   21995 O  O     . ARG A 1 4525 ? 193.785 183.159 134.730 1.00 15.71  ? 4525 ARG A O     1 
ATOM   21996 C  CB    . ARG A 1 4525 ? 191.992 180.644 135.987 1.00 13.66  ? 4525 ARG A CB    1 
ATOM   21997 C  CG    . ARG A 1 4525 ? 191.311 180.709 134.638 1.00 13.78  ? 4525 ARG A CG    1 
ATOM   21998 C  CD    . ARG A 1 4525 ? 189.805 180.625 134.814 1.00 13.57  ? 4525 ARG A CD    1 
ATOM   21999 N  NE    . ARG A 1 4525 ? 189.114 180.314 133.571 1.00 18.11  ? 4525 ARG A NE    1 
ATOM   22000 C  CZ    . ARG A 1 4525 ? 188.157 179.405 133.458 1.00 19.09  ? 4525 ARG A CZ    1 
ATOM   22001 N  NH1   . ARG A 1 4525 ? 187.763 178.685 134.496 1.00 14.26  ? 4525 ARG A NH1   1 
ATOM   22002 N  NH2   . ARG A 1 4525 ? 187.580 179.213 132.276 1.00 19.98  ? 4525 ARG A NH2   1 
ATOM   22003 N  N     . GLN A 1 4526 ? 193.174 183.437 136.881 1.00 17.69  ? 4526 GLN A N     1 
ATOM   22004 C  CA    . GLN A 1 4526 ? 193.223 184.893 136.811 1.00 17.38  ? 4526 GLN A CA    1 
ATOM   22005 C  C     . GLN A 1 4526 ? 194.637 185.391 136.548 1.00 16.96  ? 4526 GLN A C     1 
ATOM   22006 O  O     . GLN A 1 4526 ? 194.836 186.335 135.776 1.00 21.17  ? 4526 GLN A O     1 
ATOM   22007 C  CB    . GLN A 1 4526 ? 192.685 185.490 138.112 1.00 17.83  ? 4526 GLN A CB    1 
ATOM   22008 C  CG    . GLN A 1 4526 ? 191.203 185.804 138.097 1.00 21.56  ? 4526 GLN A CG    1 
ATOM   22009 C  CD    . GLN A 1 4526 ? 190.821 186.832 139.140 1.00 23.79  ? 4526 GLN A CD    1 
ATOM   22010 O  OE1   . GLN A 1 4526 ? 190.667 186.508 140.316 1.00 35.27  ? 4526 GLN A OE1   1 
ATOM   22011 N  NE2   . GLN A 1 4526 ? 190.673 188.080 138.718 1.00 19.58  ? 4526 GLN A NE2   1 
ATOM   22012 N  N     . TYR A 1 4527 ? 195.629 184.779 137.197 1.00 15.24  ? 4527 TYR A N     1 
ATOM   22013 C  CA    . TYR A 1 4527 ? 197.015 185.181 136.984 1.00 16.30  ? 4527 TYR A CA    1 
ATOM   22014 C  C     . TYR A 1 4527 ? 197.436 184.946 135.541 1.00 16.01  ? 4527 TYR A C     1 
ATOM   22015 O  O     . TYR A 1 4527 ? 198.064 185.811 134.919 1.00 14.93  ? 4527 TYR A O     1 
ATOM   22016 C  CB    . TYR A 1 4527 ? 197.929 184.420 137.946 1.00 15.47  ? 4527 TYR A CB    1 
ATOM   22017 C  CG    . TYR A 1 4527 ? 199.402 184.716 137.781 1.00 16.22  ? 4527 TYR A CG    1 
ATOM   22018 C  CD1   . TYR A 1 4527 ? 199.991 185.783 138.444 1.00 17.84  ? 4527 TYR A CD1   1 
ATOM   22019 C  CD2   . TYR A 1 4527 ? 200.206 183.923 136.973 1.00 15.74  ? 4527 TYR A CD2   1 
ATOM   22020 C  CE1   . TYR A 1 4527 ? 201.336 186.058 138.301 1.00 20.97  ? 4527 TYR A CE1   1 
ATOM   22021 C  CE2   . TYR A 1 4527 ? 201.552 184.191 136.824 1.00 19.80  ? 4527 TYR A CE2   1 
ATOM   22022 C  CZ    . TYR A 1 4527 ? 202.111 185.260 137.491 1.00 20.82  ? 4527 TYR A CZ    1 
ATOM   22023 O  OH    . TYR A 1 4527 ? 203.452 185.532 137.348 1.00 18.01  ? 4527 TYR A OH    1 
ATOM   22024 N  N     . VAL A 1 4528 ? 197.086 183.783 134.987 1.00 15.55  ? 4528 VAL A N     1 
ATOM   22025 C  CA    . VAL A 1 4528 ? 197.427 183.501 133.596 1.00 13.68  ? 4528 VAL A CA    1 
ATOM   22026 C  C     . VAL A 1 4528 ? 196.709 184.465 132.661 1.00 15.46  ? 4528 VAL A C     1 
ATOM   22027 O  O     . VAL A 1 4528 ? 197.295 184.964 131.693 1.00 18.99  ? 4528 VAL A O     1 
ATOM   22028 C  CB    . VAL A 1 4528 ? 197.115 182.035 133.251 1.00 16.92  ? 4528 VAL A CB    1 
ATOM   22029 C  CG1   . VAL A 1 4528 ? 197.258 181.801 131.756 1.00 15.75  ? 4528 VAL A CG1   1 
ATOM   22030 C  CG2   . VAL A 1 4528 ? 198.033 181.109 134.024 1.00 18.05  ? 4528 VAL A CG2   1 
ATOM   22031 N  N     . ALA A 1 4529 ? 195.430 184.743 132.929 1.00 16.14  ? 4529 ALA A N     1 
ATOM   22032 C  CA    . ALA A 1 4529 ? 194.677 185.654 132.072 1.00 14.89  ? 4529 ALA A CA    1 
ATOM   22033 C  C     . ALA A 1 4529 ? 195.265 187.060 132.099 1.00 19.49  ? 4529 ALA A C     1 
ATOM   22034 O  O     . ALA A 1 4529 ? 195.378 187.712 131.055 1.00 29.18  ? 4529 ALA A O     1 
ATOM   22035 C  CB    . ALA A 1 4529 ? 193.210 185.678 132.496 1.00 18.26  ? 4529 ALA A CB    1 
ATOM   22036 N  N     . GLN A 1 4530 ? 195.643 187.545 133.282 1.00 20.17  ? 4530 GLN A N     1 
ATOM   22037 C  CA    . GLN A 1 4530 ? 196.193 188.893 133.386 1.00 19.14  ? 4530 GLN A CA    1 
ATOM   22038 C  C     . GLN A 1 4530 ? 197.585 188.975 132.774 1.00 19.35  ? 4530 GLN A C     1 
ATOM   22039 O  O     . GLN A 1 4530 ? 197.941 189.991 132.166 1.00 24.98  ? 4530 GLN A O     1 
ATOM   22040 C  CB    . GLN A 1 4530 ? 196.224 189.335 134.848 1.00 20.86  ? 4530 GLN A CB    1 
ATOM   22041 C  CG    . GLN A 1 4530 ? 194.921 189.931 135.344 1.00 21.36  ? 4530 GLN A CG    1 
ATOM   22042 C  CD    . GLN A 1 4530 ? 194.880 190.063 136.851 1.00 27.83  ? 4530 GLN A CD    1 
ATOM   22043 O  OE1   . GLN A 1 4530 ? 195.915 190.198 137.502 1.00 23.94  ? 4530 GLN A OE1   1 
ATOM   22044 N  NE2   . GLN A 1 4530 ? 193.679 190.019 137.417 1.00 29.39  ? 4530 GLN A NE2   1 
ATOM   22045 N  N     . ALA A 1 4531 ? 198.390 187.922 132.932 1.00 23.52  ? 4531 ALA A N     1 
ATOM   22046 C  CA    . ALA A 1 4531 ? 199.750 187.946 132.405 1.00 21.90  ? 4531 ALA A CA    1 
ATOM   22047 C  C     . ALA A 1 4531 ? 199.758 188.052 130.885 1.00 21.14  ? 4531 ALA A C     1 
ATOM   22048 O  O     . ALA A 1 4531 ? 200.570 188.787 130.312 1.00 27.54  ? 4531 ALA A O     1 
ATOM   22049 C  CB    . ALA A 1 4531 ? 200.510 186.700 132.860 1.00 21.42  ? 4531 ALA A CB    1 
ATOM   22050 N  N     . ASN A 1 4532 ? 198.866 187.326 130.215 1.00 20.43  ? 4532 ASN A N     1 
ATOM   22051 C  CA    . ASN A 1 4532 ? 198.798 187.316 128.761 1.00 23.85  ? 4532 ASN A CA    1 
ATOM   22052 C  C     . ASN A 1 4532 ? 197.742 188.267 128.210 1.00 26.75  ? 4532 ASN A C     1 
ATOM   22053 O  O     . ASN A 1 4532 ? 197.533 188.303 126.993 1.00 27.86  ? 4532 ASN A O     1 
ATOM   22054 C  CB    . ASN A 1 4532 ? 198.535 185.897 128.257 1.00 25.50  ? 4532 ASN A CB    1 
ATOM   22055 C  CG    . ASN A 1 4532 ? 199.674 184.947 128.566 1.00 31.24  ? 4532 ASN A CG    1 
ATOM   22056 O  OD1   . ASN A 1 4532 ? 200.484 184.627 127.697 1.00 37.34  ? 4532 ASN A OD1   1 
ATOM   22057 N  ND2   . ASN A 1 4532 ? 199.737 184.482 129.808 1.00 31.02  ? 4532 ASN A ND2   1 
ATOM   22058 N  N     . SER A 1 4533 ? 197.071 189.028 129.077 1.00 26.73  ? 4533 SER A N     1 
ATOM   22059 C  CA    . SER A 1 4533 ? 196.026 189.972 128.674 1.00 26.31  ? 4533 SER A CA    1 
ATOM   22060 C  C     . SER A 1 4533 ? 194.891 189.266 127.935 1.00 28.17  ? 4533 SER A C     1 
ATOM   22061 O  O     . SER A 1 4533 ? 194.267 189.827 127.033 1.00 29.78  ? 4533 SER A O     1 
ATOM   22062 C  CB    . SER A 1 4533 ? 196.599 191.112 127.829 1.00 35.47  ? 4533 SER A CB    1 
ATOM   22063 O  OG    . SER A 1 4533 ? 197.509 191.896 128.580 1.00 43.03  ? 4533 SER A OG    1 
ATOM   22064 N  N     . TRP A 1 4534 ? 194.621 188.023 128.322 1.00 26.75  ? 4534 TRP A N     1 
ATOM   22065 C  CA    . TRP A 1 4534 ? 193.535 187.258 127.737 1.00 25.42  ? 4534 TRP A CA    1 
ATOM   22066 C  C     . TRP A 1 4534 ? 192.251 187.477 128.530 1.00 32.90  ? 4534 TRP A C     1 
ATOM   22067 O  O     . TRP A 1 4534 ? 192.251 188.044 129.626 1.00 36.11  ? 4534 TRP A O     1 
ATOM   22068 C  CB    . TRP A 1 4534 ? 193.890 185.773 127.683 1.00 29.72  ? 4534 TRP A CB    1 
ATOM   22069 C  CG    . TRP A 1 4534 ? 195.007 185.445 126.748 1.00 33.09  ? 4534 TRP A CG    1 
ATOM   22070 C  CD1   . TRP A 1 4534 ? 195.395 186.158 125.651 1.00 30.24  ? 4534 TRP A CD1   1 
ATOM   22071 C  CD2   . TRP A 1 4534 ? 195.880 184.313 126.821 1.00 30.09  ? 4534 TRP A CD2   1 
ATOM   22072 N  NE1   . TRP A 1 4534 ? 196.458 185.540 125.039 1.00 34.35  ? 4534 TRP A NE1   1 
ATOM   22073 C  CE2   . TRP A 1 4534 ? 196.775 184.405 125.737 1.00 33.71  ? 4534 TRP A CE2   1 
ATOM   22074 C  CE3   . TRP A 1 4534 ? 195.995 183.232 127.700 1.00 27.79  ? 4534 TRP A CE3   1 
ATOM   22075 C  CZ2   . TRP A 1 4534 ? 197.770 183.459 125.509 1.00 33.59  ? 4534 TRP A CZ2   1 
ATOM   22076 C  CZ3   . TRP A 1 4534 ? 196.981 182.293 127.471 1.00 31.14  ? 4534 TRP A CZ3   1 
ATOM   22077 C  CH2   . TRP A 1 4534 ? 197.856 182.412 126.385 1.00 35.47  ? 4534 TRP A CH2   1 
ATOM   22078 N  N     . SER A 1 4535 ? 191.139 187.015 127.971 1.00 30.72  ? 4535 SER A N     1 
ATOM   22079 C  CA    . SER A 1 4535 ? 189.856 187.050 128.651 1.00 27.97  ? 4535 SER A CA    1 
ATOM   22080 C  C     . SER A 1 4535 ? 189.746 185.849 129.580 1.00 30.03  ? 4535 SER A C     1 
ATOM   22081 O  O     . SER A 1 4535 ? 190.218 184.753 129.268 1.00 32.48  ? 4535 SER A O     1 
ATOM   22082 C  CB    . SER A 1 4535 ? 188.700 187.051 127.651 1.00 35.49  ? 4535 SER A CB    1 
ATOM   22083 O  OG    . SER A 1 4535 ? 187.468 187.285 128.308 1.00 33.49  ? 4535 SER A OG    1 
ATOM   22084 N  N     . LEU A 1 4536 ? 189.120 186.070 130.736 1.00 25.92  ? 4536 LEU A N     1 
ATOM   22085 C  CA    . LEU A 1 4536 ? 189.131 185.055 131.783 1.00 22.30  ? 4536 LEU A CA    1 
ATOM   22086 C  C     . LEU A 1 4536 ? 188.300 183.839 131.389 1.00 25.95  ? 4536 LEU A C     1 
ATOM   22087 O  O     . LEU A 1 4536 ? 188.634 182.706 131.754 1.00 22.44  ? 4536 LEU A O     1 
ATOM   22088 C  CB    . LEU A 1 4536 ? 188.613 185.658 133.086 1.00 18.02  ? 4536 LEU A CB    1 
ATOM   22089 C  CG    . LEU A 1 4536 ? 188.733 184.822 134.355 1.00 14.10  ? 4536 LEU A CG    1 
ATOM   22090 C  CD1   . LEU A 1 4536 ? 190.052 184.080 134.374 1.00 11.91  ? 4536 LEU A CD1   1 
ATOM   22091 C  CD2   . LEU A 1 4536 ? 188.606 185.712 135.568 1.00 18.12  ? 4536 LEU A CD2   1 
ATOM   22092 N  N     . GLU A 1 4537 ? 187.221 184.052 130.636 1.00 30.32  ? 4537 GLU A N     1 
ATOM   22093 C  CA    . GLU A 1 4537 ? 186.280 182.982 130.330 1.00 27.91  ? 4537 GLU A CA    1 
ATOM   22094 C  C     . GLU A 1 4537 ? 186.740 182.078 129.194 1.00 29.32  ? 4537 GLU A C     1 
ATOM   22095 O  O     . GLU A 1 4537 ? 186.138 181.017 128.994 1.00 28.11  ? 4537 GLU A O     1 
ATOM   22096 C  CB    . GLU A 1 4537 ? 184.915 183.579 129.988 1.00 23.53  ? 4537 GLU A CB    1 
ATOM   22097 C  CG    . GLU A 1 4537 ? 184.745 183.905 128.519 1.00 27.01  ? 4537 GLU A CG    1 
ATOM   22098 C  CD    . GLU A 1 4537 ? 185.169 185.319 128.193 1.00 34.43  ? 4537 GLU A CD    1 
ATOM   22099 O  OE1   . GLU A 1 4537 ? 185.674 186.011 129.101 1.00 32.44  ? 4537 GLU A OE1   1 
ATOM   22100 O  OE2   . GLU A 1 4537 ? 185.002 185.738 127.029 1.00 37.50  ? 4537 GLU A OE2   1 
ATOM   22101 N  N     . GLU A 1 4538 ? 187.778 182.459 128.449 1.00 31.00  ? 4538 GLU A N     1 
ATOM   22102 C  CA    . GLU A 1 4538 ? 188.245 181.674 127.314 1.00 33.40  ? 4538 GLU A CA    1 
ATOM   22103 C  C     . GLU A 1 4538 ? 189.506 180.880 127.634 1.00 33.21  ? 4538 GLU A C     1 
ATOM   22104 O  O     . GLU A 1 4538 ? 190.306 180.606 126.734 1.00 38.16  ? 4538 GLU A O     1 
ATOM   22105 C  CB    . GLU A 1 4538 ? 188.478 182.578 126.104 1.00 36.52  ? 4538 GLU A CB    1 
ATOM   22106 C  CG    . GLU A 1 4538 ? 187.205 183.186 125.541 1.00 47.04  ? 4538 GLU A CG    1 
ATOM   22107 C  CD    . GLU A 1 4538 ? 187.466 184.091 124.355 1.00 62.68  ? 4538 GLU A CD    1 
ATOM   22108 O  OE1   . GLU A 1 4538 ? 188.650 184.344 124.048 1.00 66.63  ? 4538 GLU A OE1   1 
ATOM   22109 O  OE2   . GLU A 1 4538 ? 186.487 184.546 123.727 1.00 60.51  ? 4538 GLU A OE2   1 
ATOM   22110 N  N     . LEU A 1 4539 ? 189.696 180.499 128.893 1.00 29.99  ? 4539 LEU A N     1 
ATOM   22111 C  CA    . LEU A 1 4539 ? 190.862 179.740 129.321 1.00 25.13  ? 4539 LEU A CA    1 
ATOM   22112 C  C     . LEU A 1 4539 ? 190.433 178.356 129.788 1.00 27.88  ? 4539 LEU A C     1 
ATOM   22113 O  O     . LEU A 1 4539 ? 189.472 178.222 130.552 1.00 33.58  ? 4539 LEU A O     1 
ATOM   22114 C  CB    . LEU A 1 4539 ? 191.608 180.466 130.442 1.00 22.61  ? 4539 LEU A CB    1 
ATOM   22115 C  CG    . LEU A 1 4539 ? 192.311 181.764 130.043 1.00 24.93  ? 4539 LEU A CG    1 
ATOM   22116 C  CD1   . LEU A 1 4539 ? 193.271 182.206 131.131 1.00 19.96  ? 4539 LEU A CD1   1 
ATOM   22117 C  CD2   . LEU A 1 4539 ? 193.037 181.591 128.721 1.00 26.23  ? 4539 LEU A CD2   1 
ATOM   22118 N  N     . CYS A 1 4540 ? 191.147 177.335 129.324 1.00 27.49  ? 4540 CYS A N     1 
ATOM   22119 C  CA    . CYS A 1 4540 ? 190.923 175.961 129.738 1.00 28.10  ? 4540 CYS A CA    1 
ATOM   22120 C  C     . CYS A 1 4540 ? 192.193 175.405 130.369 1.00 22.57  ? 4540 CYS A C     1 
ATOM   22121 O  O     . CYS A 1 4540 ? 193.285 175.959 130.215 1.00 30.10  ? 4540 CYS A O     1 
ATOM   22122 C  CB    . CYS A 1 4540 ? 190.475 175.084 128.560 1.00 29.71  ? 4540 CYS A CB    1 
ATOM   22123 S  SG    . CYS A 1 4540 ? 191.686 174.902 127.239 1.00 55.07  ? 4540 CYS A SG    1 
ATOM   22124 N  N     . LEU A 1 4541 ? 192.035 174.301 131.090 1.00 17.05  ? 4541 LEU A N     1 
ATOM   22125 C  CA    . LEU A 1 4541 ? 193.093 173.741 131.916 1.00 19.48  ? 4541 LEU A CA    1 
ATOM   22126 C  C     . LEU A 1 4541 ? 193.632 172.457 131.300 1.00 20.02  ? 4541 LEU A C     1 
ATOM   22127 O  O     . LEU A 1 4541 ? 192.862 171.596 130.864 1.00 25.13  ? 4541 LEU A O     1 
ATOM   22128 C  CB    . LEU A 1 4541 ? 192.579 173.464 133.331 1.00 15.83  ? 4541 LEU A CB    1 
ATOM   22129 C  CG    . LEU A 1 4541 ? 193.636 173.164 134.392 1.00 15.12  ? 4541 LEU A CG    1 
ATOM   22130 C  CD1   . LEU A 1 4541 ? 194.665 174.279 134.426 1.00 15.88  ? 4541 LEU A CD1   1 
ATOM   22131 C  CD2   . LEU A 1 4541 ? 192.988 172.988 135.751 1.00 13.44  ? 4541 LEU A CD2   1 
ATOM   22132 N  N     . GLU A 1 4542 ? 194.957 172.334 131.268 1.00 17.63  ? 4542 GLU A N     1 
ATOM   22133 C  CA    . GLU A 1 4542 ? 195.634 171.127 130.823 1.00 18.70  ? 4542 GLU A CA    1 
ATOM   22134 C  C     . GLU A 1 4542 ? 196.509 170.607 131.953 1.00 22.02  ? 4542 GLU A C     1 
ATOM   22135 O  O     . GLU A 1 4542 ? 197.099 171.388 132.705 1.00 23.54  ? 4542 GLU A O     1 
ATOM   22136 C  CB    . GLU A 1 4542 ? 196.478 171.390 129.574 1.00 16.54  ? 4542 GLU A CB    1 
ATOM   22137 C  CG    . GLU A 1 4542 ? 195.659 171.695 128.332 1.00 25.45  ? 4542 GLU A CG    1 
ATOM   22138 C  CD    . GLU A 1 4542 ? 196.517 171.867 127.096 1.00 39.22  ? 4542 GLU A CD    1 
ATOM   22139 O  OE1   . GLU A 1 4542 ? 197.750 171.990 127.239 1.00 48.96  ? 4542 GLU A OE1   1 
ATOM   22140 O  OE2   . GLU A 1 4542 ? 195.958 171.880 125.981 1.00 38.44  ? 4542 GLU A OE2   1 
ATOM   22141 N  N     . VAL A 1 4543 ? 196.589 169.286 132.073 1.00 16.90  ? 4543 VAL A N     1 
ATOM   22142 C  CA    . VAL A 1 4543 ? 197.240 168.629 133.200 1.00 19.01  ? 4543 VAL A CA    1 
ATOM   22143 C  C     . VAL A 1 4543 ? 198.429 167.832 132.689 1.00 25.67  ? 4543 VAL A C     1 
ATOM   22144 O  O     . VAL A 1 4543 ? 198.299 167.048 131.742 1.00 34.47  ? 4543 VAL A O     1 
ATOM   22145 C  CB    . VAL A 1 4543 ? 196.253 167.728 133.958 1.00 23.44  ? 4543 VAL A CB    1 
ATOM   22146 C  CG1   . VAL A 1 4543 ? 196.962 166.968 135.057 1.00 26.01  ? 4543 VAL A CG1   1 
ATOM   22147 C  CG2   . VAL A 1 4543 ? 195.135 168.569 134.536 1.00 25.52  ? 4543 VAL A CG2   1 
ATOM   22148 N  N     . ASN A 1 4544 ? 199.587 168.036 133.313 1.00 22.67  ? 4544 ASN A N     1 
ATOM   22149 C  CA    . ASN A 1 4544 ? 200.800 167.302 132.966 1.00 24.18  ? 4544 ASN A CA    1 
ATOM   22150 C  C     . ASN A 1 4544 ? 201.417 166.735 134.236 1.00 28.73  ? 4544 ASN A C     1 
ATOM   22151 O  O     . ASN A 1 4544 ? 201.823 167.493 135.119 1.00 34.48  ? 4544 ASN A O     1 
ATOM   22152 C  CB    . ASN A 1 4544 ? 201.791 168.207 132.232 1.00 24.80  ? 4544 ASN A CB    1 
ATOM   22153 C  CG    . ASN A 1 4544 ? 203.113 167.528 131.963 1.00 26.59  ? 4544 ASN A CG    1 
ATOM   22154 O  OD1   . ASN A 1 4544 ? 204.174 168.087 132.233 1.00 39.33  ? 4544 ASN A OD1   1 
ATOM   22155 N  ND2   . ASN A 1 4544 ? 203.059 166.316 131.428 1.00 26.18  ? 4544 ASN A ND2   1 
ATOM   22156 N  N     . VAL A 1 4545 ? 201.497 165.413 134.329 1.00 25.07  ? 4545 VAL A N     1 
ATOM   22157 C  CA    . VAL A 1 4545 ? 202.008 164.758 135.529 1.00 24.81  ? 4545 VAL A CA    1 
ATOM   22158 C  C     . VAL A 1 4545 ? 203.490 164.463 135.338 1.00 29.66  ? 4545 VAL A C     1 
ATOM   22159 O  O     . VAL A 1 4545 ? 203.873 163.729 134.421 1.00 29.71  ? 4545 VAL A O     1 
ATOM   22160 C  CB    . VAL A 1 4545 ? 201.224 163.475 135.839 1.00 24.79  ? 4545 VAL A CB    1 
ATOM   22161 C  CG1   . VAL A 1 4545 ? 201.822 162.771 137.045 1.00 24.88  ? 4545 VAL A CG1   1 
ATOM   22162 C  CG2   . VAL A 1 4545 ? 199.761 163.799 136.083 1.00 18.52  ? 4545 VAL A CG2   1 
ATOM   22163 N  N     . THR A 1 4546 ? 204.326 165.039 136.204 1.00 40.50  ? 4546 THR A N     1 
ATOM   22164 C  CA    . THR A 1 4546 ? 205.767 164.832 136.165 1.00 42.20  ? 4546 THR A CA    1 
ATOM   22165 C  C     . THR A 1 4546 ? 206.292 164.652 137.582 1.00 46.32  ? 4546 THR A C     1 
ATOM   22166 O  O     . THR A 1 4546 ? 205.565 164.814 138.566 1.00 47.83  ? 4546 THR A O     1 
ATOM   22167 C  CB    . THR A 1 4546 ? 206.504 165.999 135.490 1.00 52.82  ? 4546 THR A CB    1 
ATOM   22168 O  OG1   . THR A 1 4546 ? 206.362 167.183 136.286 1.00 46.35  ? 4546 THR A OG1   1 
ATOM   22169 C  CG2   . THR A 1 4546 ? 205.975 166.255 134.087 1.00 46.83  ? 4546 THR A CG2   1 
ATOM   22170 N  N     . THR A 1 4547 ? 207.575 164.311 137.675 1.00 57.57  ? 4547 THR A N     1 
ATOM   22171 C  CA    . THR A 1 4547 ? 208.245 164.220 138.964 1.00 63.47  ? 4547 THR A CA    1 
ATOM   22172 C  C     . THR A 1 4547 ? 208.444 165.612 139.557 1.00 60.27  ? 4547 THR A C     1 
ATOM   22173 O  O     . THR A 1 4547 ? 208.614 166.600 138.837 1.00 61.27  ? 4547 THR A O     1 
ATOM   22174 C  CB    . THR A 1 4547 ? 209.593 163.512 138.817 1.00 62.37  ? 4547 THR A CB    1 
ATOM   22175 O  OG1   . THR A 1 4547 ? 209.447 162.379 137.952 1.00 61.08  ? 4547 THR A OG1   1 
ATOM   22176 C  CG2   . THR A 1 4547 ? 210.103 163.038 140.169 1.00 58.93  ? 4547 THR A CG2   1 
ATOM   22177 N  N     . SER A 1 4548 ? 208.412 165.683 140.890 1.00 51.38  ? 4548 SER A N     1 
ATOM   22178 C  CA    . SER A 1 4548 ? 208.507 166.975 141.564 1.00 63.02  ? 4548 SER A CA    1 
ATOM   22179 C  C     . SER A 1 4548 ? 209.848 167.649 141.300 1.00 70.51  ? 4548 SER A C     1 
ATOM   22180 O  O     . SER A 1 4548 ? 209.902 168.852 141.018 1.00 67.04  ? 4548 SER A O     1 
ATOM   22181 C  CB    . SER A 1 4548 ? 208.280 166.803 143.065 1.00 61.42  ? 4548 SER A CB    1 
ATOM   22182 O  OG    . SER A 1 4548 ? 208.257 168.058 143.722 1.00 51.88  ? 4548 SER A OG    1 
ATOM   22183 N  N     . GLN A 1 4549 ? 210.944 166.894 141.390 1.00 75.90  ? 4549 GLN A N     1 
ATOM   22184 C  CA    . GLN A 1 4549 ? 212.259 167.483 141.162 1.00 80.12  ? 4549 GLN A CA    1 
ATOM   22185 C  C     . GLN A 1 4549 ? 212.511 167.745 139.681 1.00 77.17  ? 4549 GLN A C     1 
ATOM   22186 O  O     . GLN A 1 4549 ? 213.041 168.801 139.318 1.00 76.67  ? 4549 GLN A O     1 
ATOM   22187 C  CB    . GLN A 1 4549 ? 213.349 166.580 141.737 1.00 76.26  ? 4549 GLN A CB    1 
ATOM   22188 C  CG    . GLN A 1 4549 ? 214.728 167.220 141.748 1.00 85.33  ? 4549 GLN A CG    1 
ATOM   22189 C  CD    . GLN A 1 4549 ? 214.715 168.619 142.333 1.00 82.82  ? 4549 GLN A CD    1 
ATOM   22190 O  OE1   . GLN A 1 4549 ? 215.004 169.596 141.642 1.00 83.17  ? 4549 GLN A OE1   1 
ATOM   22191 N  NE2   . GLN A 1 4549 ? 214.381 168.723 143.614 1.00 76.06  ? 4549 GLN A NE2   1 
ATOM   22192 N  N     . GLY A 1 4550 ? 212.141 166.804 138.818 1.00 72.37  ? 4550 GLY A N     1 
ATOM   22193 C  CA    . GLY A 1 4550 ? 212.364 166.961 137.394 1.00 79.77  ? 4550 GLY A CA    1 
ATOM   22194 C  C     . GLY A 1 4550 ? 211.206 167.611 136.666 1.00 83.14  ? 4550 GLY A C     1 
ATOM   22195 O  O     . GLY A 1 4550 ? 210.520 166.958 135.875 1.00 81.94  ? 4550 GLY A O     1 
ATOM   22196 N  N     . ALA A 1 4551 ? 210.979 168.898 136.919 1.00 84.16  ? 4551 ALA A N     1 
ATOM   22197 C  CA    . ALA A 1 4551 ? 209.889 169.614 136.275 1.00 77.41  ? 4551 ALA A CA    1 
ATOM   22198 C  C     . ALA A 1 4551 ? 210.278 171.073 136.096 1.00 77.41  ? 4551 ALA A C     1 
ATOM   22199 O  O     . ALA A 1 4551 ? 211.111 171.612 136.829 1.00 71.56  ? 4551 ALA A O     1 
ATOM   22200 C  CB    . ALA A 1 4551 ? 208.590 169.504 137.080 1.00 69.13  ? 4551 ALA A CB    1 
ATOM   22201 N  N     . THR A 1 4552 ? 209.658 171.707 135.101 1.00 77.26  ? 4552 THR A N     1 
ATOM   22202 C  CA    . THR A 1 4552 ? 209.848 173.123 134.817 1.00 73.99  ? 4552 THR A CA    1 
ATOM   22203 C  C     . THR A 1 4552 ? 208.485 173.770 134.631 1.00 59.47  ? 4552 THR A C     1 
ATOM   22204 O  O     . THR A 1 4552 ? 207.623 173.217 133.940 1.00 58.48  ? 4552 THR A O     1 
ATOM   22205 C  CB    . THR A 1 4552 ? 210.710 173.335 133.566 1.00 80.73  ? 4552 THR A CB    1 
ATOM   22206 O  OG1   . THR A 1 4552 ? 210.121 172.648 132.455 1.00 84.76  ? 4552 THR A OG1   1 
ATOM   22207 C  CG2   . THR A 1 4552 ? 212.122 172.814 133.790 1.00 69.73  ? 4552 THR A CG2   1 
ATOM   22208 N  N     . LEU A 1 4553 ? 208.292 174.934 135.244 1.00 47.05  ? 4553 LEU A N     1 
ATOM   22209 C  CA    . LEU A 1 4553 ? 207.031 175.663 135.177 1.00 46.14  ? 4553 LEU A CA    1 
ATOM   22210 C  C     . LEU A 1 4553 ? 207.211 176.891 134.296 1.00 42.12  ? 4553 LEU A C     1 
ATOM   22211 O  O     . LEU A 1 4553 ? 208.037 177.759 134.598 1.00 44.77  ? 4553 LEU A O     1 
ATOM   22212 C  CB    . LEU A 1 4553 ? 206.558 176.070 136.572 1.00 40.99  ? 4553 LEU A CB    1 
ATOM   22213 C  CG    . LEU A 1 4553 ? 206.322 174.950 137.586 1.00 38.24  ? 4553 LEU A CG    1 
ATOM   22214 C  CD1   . LEU A 1 4553 ? 205.711 175.509 138.859 1.00 34.24  ? 4553 LEU A CD1   1 
ATOM   22215 C  CD2   . LEU A 1 4553 ? 205.434 173.866 136.997 1.00 33.02  ? 4553 LEU A CD2   1 
ATOM   22216 N  N     . ASP A 1 4554 ? 206.438 176.964 133.216 1.00 36.63  ? 4554 ASP A N     1 
ATOM   22217 C  CA    . ASP A 1 4554 ? 206.464 178.127 132.341 1.00 40.47  ? 4554 ASP A CA    1 
ATOM   22218 C  C     . ASP A 1 4554 ? 205.516 179.190 132.895 1.00 40.21  ? 4554 ASP A C     1 
ATOM   22219 O  O     . ASP A 1 4554 ? 205.021 179.088 134.021 1.00 37.66  ? 4554 ASP A O     1 
ATOM   22220 C  CB    . ASP A 1 4554 ? 206.138 177.721 130.903 1.00 45.36  ? 4554 ASP A CB    1 
ATOM   22221 C  CG    . ASP A 1 4554 ? 204.739 177.143 130.748 1.00 45.71  ? 4554 ASP A CG    1 
ATOM   22222 O  OD1   . ASP A 1 4554 ? 204.017 177.007 131.755 1.00 43.31  ? 4554 ASP A OD1   1 
ATOM   22223 O  OD2   . ASP A 1 4554 ? 204.360 176.819 129.604 1.00 52.93  ? 4554 ASP A OD2   1 
ATOM   22224 N  N     . ALA A 1 4555 ? 205.241 180.224 132.100 1.00 41.00  ? 4555 ALA A N     1 
ATOM   22225 C  CA    . ALA A 1 4555 ? 204.429 181.342 132.565 1.00 39.41  ? 4555 ALA A CA    1 
ATOM   22226 C  C     . ALA A 1 4555 ? 202.987 180.953 132.865 1.00 36.70  ? 4555 ALA A C     1 
ATOM   22227 O  O     . ALA A 1 4555 ? 202.275 181.739 133.497 1.00 37.25  ? 4555 ALA A O     1 
ATOM   22228 C  CB    . ALA A 1 4555 ? 204.451 182.469 131.532 1.00 33.40  ? 4555 ALA A CB    1 
ATOM   22229 N  N     . CYS A 1 4556 ? 202.540 179.774 132.434 1.00 34.98  ? 4556 CYS A N     1 
ATOM   22230 C  CA    . CYS A 1 4556 ? 201.163 179.351 132.636 1.00 30.45  ? 4556 CYS A CA    1 
ATOM   22231 C  C     . CYS A 1 4556 ? 201.025 178.104 133.498 1.00 30.70  ? 4556 CYS A C     1 
ATOM   22232 O  O     . CYS A 1 4556 ? 199.895 177.691 133.779 1.00 31.64  ? 4556 CYS A O     1 
ATOM   22233 C  CB    . CYS A 1 4556 ? 200.483 179.108 131.282 1.00 33.70  ? 4556 CYS A CB    1 
ATOM   22234 S  SG    . CYS A 1 4556 ? 200.492 180.539 130.176 1.00 52.04  ? 4556 CYS A SG    1 
ATOM   22235 N  N     . SER A 1 4557 ? 202.127 177.499 133.933 1.00 28.50  ? 4557 SER A N     1 
ATOM   22236 C  CA    . SER A 1 4557 ? 202.088 176.247 134.675 1.00 24.19  ? 4557 SER A CA    1 
ATOM   22237 C  C     . SER A 1 4557 ? 202.181 176.502 136.173 1.00 27.53  ? 4557 SER A C     1 
ATOM   22238 O  O     . SER A 1 4557 ? 202.999 177.304 136.631 1.00 27.70  ? 4557 SER A O     1 
ATOM   22239 C  CB    . SER A 1 4557 ? 203.223 175.319 134.241 1.00 30.71  ? 4557 SER A CB    1 
ATOM   22240 O  OG    . SER A 1 4557 ? 203.008 174.827 132.931 1.00 36.43  ? 4557 SER A OG    1 
ATOM   22241 N  N     . PHE A 1 4558 ? 201.334 175.811 136.930 1.00 24.37  ? 4558 PHE A N     1 
ATOM   22242 C  CA    . PHE A 1 4558 ? 201.347 175.849 138.384 1.00 20.29  ? 4558 PHE A CA    1 
ATOM   22243 C  C     . PHE A 1 4558 ? 201.499 174.436 138.926 1.00 22.05  ? 4558 PHE A C     1 
ATOM   22244 O  O     . PHE A 1 4558 ? 200.900 173.492 138.401 1.00 25.07  ? 4558 PHE A O     1 
ATOM   22245 C  CB    . PHE A 1 4558 ? 200.075 176.495 138.935 1.00 15.07  ? 4558 PHE A CB    1 
ATOM   22246 C  CG    . PHE A 1 4558 ? 199.925 177.941 138.567 1.00 17.36  ? 4558 PHE A CG    1 
ATOM   22247 C  CD1   . PHE A 1 4558 ? 199.398 178.307 137.342 1.00 17.65  ? 4558 PHE A CD1   1 
ATOM   22248 C  CD2   . PHE A 1 4558 ? 200.321 178.935 139.443 1.00 19.24  ? 4558 PHE A CD2   1 
ATOM   22249 C  CE1   . PHE A 1 4558 ? 199.264 179.636 137.002 1.00 16.43  ? 4558 PHE A CE1   1 
ATOM   22250 C  CE2   . PHE A 1 4558 ? 200.187 180.264 139.108 1.00 19.69  ? 4558 PHE A CE2   1 
ATOM   22251 C  CZ    . PHE A 1 4558 ? 199.658 180.615 137.886 1.00 19.22  ? 4558 PHE A CZ    1 
ATOM   22252 N  N     . GLY A 1 4559 ? 202.305 174.297 139.976 1.00 21.98  ? 4559 GLY A N     1 
ATOM   22253 C  CA    . GLY A 1 4559 ? 202.595 172.994 140.549 1.00 16.26  ? 4559 GLY A CA    1 
ATOM   22254 C  C     . GLY A 1 4559 ? 201.656 172.647 141.693 1.00 18.04  ? 4559 GLY A C     1 
ATOM   22255 O  O     . GLY A 1 4559 ? 201.344 173.484 142.537 1.00 22.35  ? 4559 GLY A O     1 
ATOM   22256 N  N     . VAL A 1 4560 ? 201.210 171.394 141.703 1.00 20.43  ? 4560 VAL A N     1 
ATOM   22257 C  CA    . VAL A 1 4560 ? 200.288 170.877 142.705 1.00 14.81  ? 4560 VAL A CA    1 
ATOM   22258 C  C     . VAL A 1 4560 ? 200.820 169.533 143.185 1.00 22.77  ? 4560 VAL A C     1 
ATOM   22259 O  O     . VAL A 1 4560 ? 201.259 168.710 142.375 1.00 25.40  ? 4560 VAL A O     1 
ATOM   22260 C  CB    . VAL A 1 4560 ? 198.860 170.731 142.142 1.00 13.15  ? 4560 VAL A CB    1 
ATOM   22261 C  CG1   . VAL A 1 4560 ? 197.982 169.938 143.093 1.00 19.80  ? 4560 VAL A CG1   1 
ATOM   22262 C  CG2   . VAL A 1 4560 ? 198.254 172.096 141.868 1.00 16.69  ? 4560 VAL A CG2   1 
ATOM   22263 N  N     . THR A 1 4561 ? 200.796 169.319 144.498 1.00 19.94  ? 4561 THR A N     1 
ATOM   22264 C  CA    . THR A 1 4561 ? 201.225 168.066 145.096 1.00 17.15  ? 4561 THR A CA    1 
ATOM   22265 C  C     . THR A 1 4561 ? 200.094 167.477 145.928 1.00 19.49  ? 4561 THR A C     1 
ATOM   22266 O  O     . THR A 1 4561 ? 199.155 168.174 146.323 1.00 23.25  ? 4561 THR A O     1 
ATOM   22267 C  CB    . THR A 1 4561 ? 202.472 168.255 145.972 1.00 17.71  ? 4561 THR A CB    1 
ATOM   22268 O  OG1   . THR A 1 4561 ? 202.155 169.096 147.087 1.00 23.48  ? 4561 THR A OG1   1 
ATOM   22269 C  CG2   . THR A 1 4561 ? 203.599 168.887 145.172 1.00 21.99  ? 4561 THR A CG2   1 
ATOM   22270 N  N     . GLY A 1 4562 ? 200.190 166.175 146.186 1.00 18.95  ? 4562 GLY A N     1 
ATOM   22271 C  CA    . GLY A 1 4562 ? 199.228 165.486 147.017 1.00 12.87  ? 4562 GLY A CA    1 
ATOM   22272 C  C     . GLY A 1 4562 ? 198.048 164.877 146.293 1.00 14.28  ? 4562 GLY A C     1 
ATOM   22273 O  O     . GLY A 1 4562 ? 197.215 164.233 146.941 1.00 19.92  ? 4562 GLY A O     1 
ATOM   22274 N  N     . LEU A 1 4563 ? 197.940 165.064 144.981 1.00 16.61  ? 4563 LEU A N     1 
ATOM   22275 C  CA    . LEU A 1 4563 ? 196.856 164.448 144.229 1.00 12.73  ? 4563 LEU A CA    1 
ATOM   22276 C  C     . LEU A 1 4563 ? 197.044 162.938 144.166 1.00 14.01  ? 4563 LEU A C     1 
ATOM   22277 O  O     . LEU A 1 4563 ? 198.152 162.442 143.945 1.00 14.87  ? 4563 LEU A O     1 
ATOM   22278 C  CB    . LEU A 1 4563 ? 196.788 165.028 142.817 1.00 12.05  ? 4563 LEU A CB    1 
ATOM   22279 C  CG    . LEU A 1 4563 ? 196.485 166.522 142.680 1.00 13.33  ? 4563 LEU A CG    1 
ATOM   22280 C  CD1   . LEU A 1 4563 ? 196.026 166.840 141.269 1.00 17.45  ? 4563 LEU A CD1   1 
ATOM   22281 C  CD2   . LEU A 1 4563 ? 195.443 166.961 143.692 1.00 16.46  ? 4563 LEU A CD2   1 
ATOM   22282 N  N     . LYS A 1 4564 ? 195.951 162.205 144.362 1.00 15.53  ? 4564 LYS A N     1 
ATOM   22283 C  CA    . LYS A 1 4564 ? 195.965 160.749 144.360 1.00 14.48  ? 4564 LYS A CA    1 
ATOM   22284 C  C     . LYS A 1 4564 ? 195.021 160.237 143.283 1.00 15.15  ? 4564 LYS A C     1 
ATOM   22285 O  O     . LYS A 1 4564 ? 193.847 160.612 143.257 1.00 17.38  ? 4564 LYS A O     1 
ATOM   22286 C  CB    . LYS A 1 4564 ? 195.556 160.195 145.727 1.00 14.43  ? 4564 LYS A CB    1 
ATOM   22287 C  CG    . LYS A 1 4564 ? 196.385 160.720 146.887 1.00 12.06  ? 4564 LYS A CG    1 
ATOM   22288 C  CD    . LYS A 1 4564 ? 197.748 160.059 146.935 1.00 15.57  ? 4564 LYS A CD    1 
ATOM   22289 C  CE    . LYS A 1 4564 ? 198.471 160.376 148.232 1.00 20.29  ? 4564 LYS A CE    1 
ATOM   22290 N  NZ    . LYS A 1 4564 ? 198.736 161.832 148.381 1.00 14.62  ? 4564 LYS A NZ    1 
ATOM   22291 N  N     . LEU A 1 4565 ? 195.530 159.377 142.407 1.00 12.76  ? 4565 LEU A N     1 
ATOM   22292 C  CA    . LEU A 1 4565 ? 194.733 158.790 141.337 1.00 11.95  ? 4565 LEU A CA    1 
ATOM   22293 C  C     . LEU A 1 4565 ? 194.166 157.459 141.816 1.00 13.74  ? 4565 LEU A C     1 
ATOM   22294 O  O     . LEU A 1 4565 ? 194.923 156.557 142.186 1.00 20.22  ? 4565 LEU A O     1 
ATOM   22295 C  CB    . LEU A 1 4565 ? 195.584 158.598 140.085 1.00 11.87  ? 4565 LEU A CB    1 
ATOM   22296 C  CG    . LEU A 1 4565 ? 194.886 158.129 138.811 1.00 12.12  ? 4565 LEU A CG    1 
ATOM   22297 C  CD1   . LEU A 1 4565 ? 193.738 159.054 138.455 1.00 12.04  ? 4565 LEU A CD1   1 
ATOM   22298 C  CD2   . LEU A 1 4565 ? 195.889 158.059 137.677 1.00 15.57  ? 4565 LEU A CD2   1 
ATOM   22299 N  N     . GLN A 1 4566 ? 192.841 157.335 141.809 1.00 12.82  ? 4566 GLN A N     1 
ATOM   22300 C  CA    . GLN A 1 4566 ? 192.172 156.162 142.354 1.00 11.67  ? 4566 GLN A CA    1 
ATOM   22301 C  C     . GLN A 1 4566 ? 191.961 155.131 141.252 1.00 12.18  ? 4566 GLN A C     1 
ATOM   22302 O  O     . GLN A 1 4566 ? 191.297 155.414 140.250 1.00 12.07  ? 4566 GLN A O     1 
ATOM   22303 C  CB    . GLN A 1 4566 ? 190.838 156.554 142.984 1.00 12.09  ? 4566 GLN A CB    1 
ATOM   22304 C  CG    . GLN A 1 4566 ? 190.936 157.697 143.978 1.00 13.14  ? 4566 GLN A CG    1 
ATOM   22305 C  CD    . GLN A 1 4566 ? 191.749 157.336 145.203 1.00 14.43  ? 4566 GLN A CD    1 
ATOM   22306 O  OE1   . GLN A 1 4566 ? 192.776 157.951 145.483 1.00 13.44  ? 4566 GLN A OE1   1 
ATOM   22307 N  NE2   . GLN A 1 4566 ? 191.289 156.336 145.944 1.00 21.21  ? 4566 GLN A NE2   1 
ATOM   22308 N  N     . GLY A 1 4567 ? 192.523 153.940 141.441 1.00 18.45  ? 4567 GLY A N     1 
ATOM   22309 C  CA    . GLY A 1 4567 ? 192.301 152.854 140.509 1.00 16.95  ? 4567 GLY A CA    1 
ATOM   22310 C  C     . GLY A 1 4567 ? 193.016 152.979 139.186 1.00 16.00  ? 4567 GLY A C     1 
ATOM   22311 O  O     . GLY A 1 4567 ? 192.642 152.298 138.228 1.00 21.17  ? 4567 GLY A O     1 
ATOM   22312 N  N     . ALA A 1 4568 ? 194.038 153.825 139.099 1.00 14.41  ? 4568 ALA A N     1 
ATOM   22313 C  CA    . ALA A 1 4568 ? 194.784 153.975 137.859 1.00 15.08  ? 4568 ALA A CA    1 
ATOM   22314 C  C     . ALA A 1 4568 ? 196.188 154.463 138.178 1.00 17.71  ? 4568 ALA A C     1 
ATOM   22315 O  O     . ALA A 1 4568 ? 196.444 155.027 139.244 1.00 21.32  ? 4568 ALA A O     1 
ATOM   22316 C  CB    . ALA A 1 4568 ? 194.084 154.934 136.892 1.00 14.28  ? 4568 ALA A CB    1 
ATOM   22317 N  N     . THR A 1 4569 ? 197.093 154.234 137.233 1.00 19.07  ? 4569 THR A N     1 
ATOM   22318 C  CA    . THR A 1 4569 ? 198.478 154.667 137.328 1.00 21.86  ? 4569 THR A CA    1 
ATOM   22319 C  C     . THR A 1 4569 ? 198.811 155.549 136.134 1.00 21.02  ? 4569 THR A C     1 
ATOM   22320 O  O     . THR A 1 4569 ? 198.297 155.339 135.031 1.00 24.93  ? 4569 THR A O     1 
ATOM   22321 C  CB    . THR A 1 4569 ? 199.441 153.476 137.377 1.00 22.44  ? 4569 THR A CB    1 
ATOM   22322 O  OG1   . THR A 1 4569 ? 199.169 152.593 136.283 1.00 25.74  ? 4569 THR A OG1   1 
ATOM   22323 C  CG2   . THR A 1 4569 ? 199.287 152.720 138.685 1.00 20.61  ? 4569 THR A CG2   1 
ATOM   22324 N  N     . CYS A 1 4570 ? 199.669 156.538 136.360 1.00 25.11  ? 4570 CYS A N     1 
ATOM   22325 C  CA    . CYS A 1 4570 ? 200.054 157.499 135.335 1.00 25.22  ? 4570 CYS A CA    1 
ATOM   22326 C  C     . CYS A 1 4570 ? 201.508 157.265 134.950 1.00 32.05  ? 4570 CYS A C     1 
ATOM   22327 O  O     . CYS A 1 4570 ? 202.403 157.370 135.795 1.00 34.40  ? 4570 CYS A O     1 
ATOM   22328 C  CB    . CYS A 1 4570 ? 199.850 158.932 135.826 1.00 26.51  ? 4570 CYS A CB    1 
ATOM   22329 S  SG    . CYS A 1 4570 ? 199.863 160.177 134.521 1.00 37.05  ? 4570 CYS A SG    1 
ATOM   22330 N  N     . ASN A 1 4571 ? 201.736 156.947 133.679 1.00 35.34  ? 4571 ASN A N     1 
ATOM   22331 C  CA    . ASN A 1 4571 ? 203.073 156.816 133.120 1.00 32.21  ? 4571 ASN A CA    1 
ATOM   22332 C  C     . ASN A 1 4571 ? 203.144 157.638 131.844 1.00 32.77  ? 4571 ASN A C     1 
ATOM   22333 O  O     . ASN A 1 4571 ? 202.303 157.477 130.954 1.00 34.70  ? 4571 ASN A O     1 
ATOM   22334 C  CB    . ASN A 1 4571 ? 203.419 155.352 132.832 1.00 35.52  ? 4571 ASN A CB    1 
ATOM   22335 C  CG    . ASN A 1 4571 ? 204.880 155.159 132.475 1.00 46.51  ? 4571 ASN A CG    1 
ATOM   22336 O  OD1   . ASN A 1 4571 ? 205.766 155.728 133.111 1.00 50.97  ? 4571 ASN A OD1   1 
ATOM   22337 N  ND2   . ASN A 1 4571 ? 205.138 154.352 131.453 1.00 39.98  ? 4571 ASN A ND2   1 
ATOM   22338 N  N     . ASN A 1 4572 ? 204.146 158.515 131.761 1.00 32.39  ? 4572 ASN A N     1 
ATOM   22339 C  CA    . ASN A 1 4572 ? 204.327 159.400 130.610 1.00 35.95  ? 4572 ASN A CA    1 
ATOM   22340 C  C     . ASN A 1 4572 ? 203.052 160.188 130.320 1.00 33.97  ? 4572 ASN A C     1 
ATOM   22341 O  O     . ASN A 1 4572 ? 202.651 160.364 129.167 1.00 31.17  ? 4572 ASN A O     1 
ATOM   22342 C  CB    . ASN A 1 4572 ? 204.780 158.617 129.377 1.00 42.59  ? 4572 ASN A CB    1 
ATOM   22343 C  CG    . ASN A 1 4572 ? 205.578 159.465 128.409 1.00 46.95  ? 4572 ASN A CG    1 
ATOM   22344 O  OD1   . ASN A 1 4572 ? 205.515 160.693 128.444 1.00 55.78  ? 4572 ASN A OD1   1 
ATOM   22345 N  ND2   . ASN A 1 4572 ? 206.336 158.813 127.536 1.00 51.31  ? 4572 ASN A ND2   1 
ATOM   22346 N  N     . ASN A 1 4573 ? 202.407 160.658 131.389 1.00 35.14  ? 4573 ASN A N     1 
ATOM   22347 C  CA    . ASN A 1 4573 ? 201.169 161.432 131.306 1.00 29.90  ? 4573 ASN A CA    1 
ATOM   22348 C  C     . ASN A 1 4573 ? 200.056 160.649 130.615 1.00 33.32  ? 4573 ASN A C     1 
ATOM   22349 O  O     . ASN A 1 4573 ? 199.197 161.227 129.945 1.00 33.27  ? 4573 ASN A O     1 
ATOM   22350 C  CB    . ASN A 1 4573 ? 201.400 162.775 130.605 1.00 28.76  ? 4573 ASN A CB    1 
ATOM   22351 C  CG    . ASN A 1 4573 ? 200.521 163.877 131.153 1.00 28.38  ? 4573 ASN A CG    1 
ATOM   22352 O  OD1   . ASN A 1 4573 ? 200.494 164.121 132.358 1.00 32.84  ? 4573 ASN A OD1   1 
ATOM   22353 N  ND2   . ASN A 1 4573 ? 199.800 164.555 130.270 1.00 27.64  ? 4573 ASN A ND2   1 
ATOM   22354 N  N     . LYS A 1 4574 ? 200.063 159.326 130.772 1.00 36.12  ? 4574 LYS A N     1 
ATOM   22355 C  CA    . LYS A 1 4574 ? 199.029 158.460 130.223 1.00 28.36  ? 4574 LYS A CA    1 
ATOM   22356 C  C     . LYS A 1 4574 ? 198.531 157.519 131.309 1.00 30.51  ? 4574 LYS A C     1 
ATOM   22357 O  O     . LYS A 1 4574 ? 199.321 156.997 132.098 1.00 29.77  ? 4574 LYS A O     1 
ATOM   22358 C  CB    . LYS A 1 4574 ? 199.548 157.663 129.024 1.00 29.72  ? 4574 LYS A CB    1 
ATOM   22359 C  CG    . LYS A 1 4574 ? 199.889 158.524 127.820 1.00 32.38  ? 4574 LYS A CG    1 
ATOM   22360 C  CD    . LYS A 1 4574 ? 200.309 157.680 126.633 1.00 35.77  ? 4574 LYS A CD    1 
ATOM   22361 C  CE    . LYS A 1 4574 ? 200.715 158.553 125.459 1.00 40.05  ? 4574 LYS A CE    1 
ATOM   22362 N  NZ    . LYS A 1 4574 ? 199.690 159.589 125.164 1.00 44.92  ? 4574 LYS A NZ    1 
ATOM   22363 N  N     . LEU A 1 4575 ? 197.219 157.302 131.341 1.00 31.90  ? 4575 LEU A N     1 
ATOM   22364 C  CA    . LEU A 1 4575 ? 196.578 156.552 132.412 1.00 22.22  ? 4575 LEU A CA    1 
ATOM   22365 C  C     . LEU A 1 4575 ? 196.352 155.103 132.007 1.00 24.13  ? 4575 LEU A C     1 
ATOM   22366 O  O     . LEU A 1 4575 ? 195.945 154.816 130.878 1.00 28.95  ? 4575 LEU A O     1 
ATOM   22367 C  CB    . LEU A 1 4575 ? 195.242 157.188 132.800 1.00 22.51  ? 4575 LEU A CB    1 
ATOM   22368 C  CG    . LEU A 1 4575 ? 195.267 158.630 133.308 1.00 23.17  ? 4575 LEU A CG    1 
ATOM   22369 C  CD1   . LEU A 1 4575 ? 193.988 158.932 134.062 1.00 25.29  ? 4575 LEU A CD1   1 
ATOM   22370 C  CD2   . LEU A 1 4575 ? 196.478 158.882 134.184 1.00 20.92  ? 4575 LEU A CD2   1 
ATOM   22371 N  N     . SER A 1 4576 ? 196.617 154.193 132.943 1.00 26.36  ? 4576 SER A N     1 
ATOM   22372 C  CA    . SER A 1 4576 ? 196.364 152.771 132.759 1.00 22.46  ? 4576 SER A CA    1 
ATOM   22373 C  C     . SER A 1 4576 ? 195.670 152.223 133.995 1.00 22.86  ? 4576 SER A C     1 
ATOM   22374 O  O     . SER A 1 4576 ? 196.002 152.602 135.121 1.00 29.35  ? 4576 SER A O     1 
ATOM   22375 C  CB    . SER A 1 4576 ? 197.661 151.997 132.501 1.00 24.52  ? 4576 SER A CB    1 
ATOM   22376 O  OG    . SER A 1 4576 ? 198.321 152.473 131.342 1.00 33.85  ? 4576 SER A OG    1 
ATOM   22377 N  N     . LEU A 1 4577 ? 194.710 151.327 133.783 1.00 23.84  ? 4577 LEU A N     1 
ATOM   22378 C  CA    . LEU A 1 4577 ? 193.984 150.735 134.898 1.00 19.33  ? 4577 LEU A CA    1 
ATOM   22379 C  C     . LEU A 1 4577 ? 194.921 149.905 135.766 1.00 19.42  ? 4577 LEU A C     1 
ATOM   22380 O  O     . LEU A 1 4577 ? 195.784 149.181 135.263 1.00 26.35  ? 4577 LEU A O     1 
ATOM   22381 C  CB    . LEU A 1 4577 ? 192.839 149.865 134.385 1.00 19.37  ? 4577 LEU A CB    1 
ATOM   22382 C  CG    . LEU A 1 4577 ? 191.654 150.599 133.762 1.00 17.23  ? 4577 LEU A CG    1 
ATOM   22383 C  CD1   . LEU A 1 4577 ? 190.670 149.604 133.184 1.00 17.52  ? 4577 LEU A CD1   1 
ATOM   22384 C  CD2   . LEU A 1 4577 ? 190.979 151.494 134.784 1.00 17.41  ? 4577 LEU A CD2   1 
ATOM   22385 N  N     . SER A 1 4578 ? 194.745 150.012 137.081 1.00 17.15  ? 4578 SER A N     1 
ATOM   22386 C  CA    . SER A 1 4578 ? 195.585 149.303 138.033 1.00 21.81  ? 4578 SER A CA    1 
ATOM   22387 C  C     . SER A 1 4578 ? 194.717 148.703 139.128 1.00 27.47  ? 4578 SER A C     1 
ATOM   22388 O  O     . SER A 1 4578 ? 193.595 149.149 139.378 1.00 31.38  ? 4578 SER A O     1 
ATOM   22389 C  CB    . SER A 1 4578 ? 196.644 150.223 138.651 1.00 22.10  ? 4578 SER A CB    1 
ATOM   22390 O  OG    . SER A 1 4578 ? 196.073 151.068 139.633 1.00 21.49  ? 4578 SER A OG    1 
ATOM   22391 N  N     . ASN A 1 4579 ? 195.254 147.677 139.782 1.00 28.16  ? 4579 ASN A N     1 
ATOM   22392 C  CA    . ASN A 1 4579 ? 194.576 147.022 140.890 1.00 25.16  ? 4579 ASN A CA    1 
ATOM   22393 C  C     . ASN A 1 4579 ? 194.913 147.643 142.239 1.00 24.23  ? 4579 ASN A C     1 
ATOM   22394 O  O     . ASN A 1 4579 ? 194.453 147.140 143.268 1.00 30.53  ? 4579 ASN A O     1 
ATOM   22395 C  CB    . ASN A 1 4579 ? 194.914 145.529 140.906 1.00 27.66  ? 4579 ASN A CB    1 
ATOM   22396 C  CG    . ASN A 1 4579 ? 194.236 144.770 139.784 1.00 37.39  ? 4579 ASN A CG    1 
ATOM   22397 O  OD1   . ASN A 1 4579 ? 194.891 144.087 138.997 1.00 40.94  ? 4579 ASN A OD1   1 
ATOM   22398 N  ND2   . ASN A 1 4579 ? 192.916 144.892 139.700 1.00 35.88  ? 4579 ASN A ND2   1 
ATOM   22399 N  N     . ALA A 1 4580 ? 195.707 148.709 142.258 1.00 23.09  ? 4580 ALA A N     1 
ATOM   22400 C  CA    . ALA A 1 4580 ? 196.002 149.418 143.492 1.00 18.70  ? 4580 ALA A CA    1 
ATOM   22401 C  C     . ALA A 1 4580 ? 194.862 150.363 143.849 1.00 23.06  ? 4580 ALA A C     1 
ATOM   22402 O  O     . ALA A 1 4580 ? 194.155 150.877 142.977 1.00 28.62  ? 4580 ALA A O     1 
ATOM   22403 C  CB    . ALA A 1 4580 ? 197.309 150.200 143.363 1.00 18.72  ? 4580 ALA A CB    1 
ATOM   22404 N  N     . ILE A 1 4581 ? 194.681 150.583 145.152 1.00 23.89  ? 4581 ILE A N     1 
ATOM   22405 C  CA    . ILE A 1 4581 ? 193.610 151.459 145.619 1.00 24.99  ? 4581 ILE A CA    1 
ATOM   22406 C  C     . ILE A 1 4581 ? 193.856 152.892 145.162 1.00 28.33  ? 4581 ILE A C     1 
ATOM   22407 O  O     . ILE A 1 4581 ? 192.949 153.571 144.667 1.00 24.54  ? 4581 ILE A O     1 
ATOM   22408 C  CB    . ILE A 1 4581 ? 193.472 151.369 147.149 1.00 28.88  ? 4581 ILE A CB    1 
ATOM   22409 C  CG1   . ILE A 1 4581 ? 192.854 150.028 147.550 1.00 26.96  ? 4581 ILE A CG1   1 
ATOM   22410 C  CG2   . ILE A 1 4581 ? 192.642 152.526 147.684 1.00 28.41  ? 4581 ILE A CG2   1 
ATOM   22411 C  CD1   . ILE A 1 4581 ? 191.419 149.864 147.109 1.00 20.98  ? 4581 ILE A CD1   1 
ATOM   22412 N  N     . SER A 1 4582 ? 195.088 153.371 145.316 1.00 28.14  ? 4582 SER A N     1 
ATOM   22413 C  CA    . SER A 1 4582 ? 195.429 154.730 144.929 1.00 20.58  ? 4582 SER A CA    1 
ATOM   22414 C  C     . SER A 1 4582 ? 196.907 154.800 144.581 1.00 25.50  ? 4582 SER A C     1 
ATOM   22415 O  O     . SER A 1 4582 ? 197.723 154.037 145.104 1.00 34.06  ? 4582 SER A O     1 
ATOM   22416 C  CB    . SER A 1 4582 ? 195.102 155.734 146.040 1.00 24.72  ? 4582 SER A CB    1 
ATOM   22417 O  OG    . SER A 1 4582 ? 195.853 155.465 147.210 1.00 31.73  ? 4582 SER A OG    1 
ATOM   22418 N  N     . THR A 1 4583 ? 197.238 155.728 143.688 1.00 22.85  ? 4583 THR A N     1 
ATOM   22419 C  CA    . THR A 1 4583 ? 198.607 155.981 143.267 1.00 21.78  ? 4583 THR A CA    1 
ATOM   22420 C  C     . THR A 1 4583 ? 198.914 157.455 143.481 1.00 23.30  ? 4583 THR A C     1 
ATOM   22421 O  O     . THR A 1 4583 ? 198.133 158.321 143.076 1.00 20.47  ? 4583 THR A O     1 
ATOM   22422 C  CB    . THR A 1 4583 ? 198.813 155.596 141.797 1.00 19.77  ? 4583 THR A CB    1 
ATOM   22423 O  OG1   . THR A 1 4583 ? 198.844 154.169 141.677 1.00 20.00  ? 4583 THR A OG1   1 
ATOM   22424 C  CG2   . THR A 1 4583 ? 200.117 156.169 141.268 1.00 20.25  ? 4583 THR A CG2   1 
ATOM   22425 N  N     . ALA A 1 4584 ? 200.045 157.738 144.121 1.00 29.81  ? 4584 ALA A N     1 
ATOM   22426 C  CA    . ALA A 1 4584 ? 200.416 159.111 144.433 1.00 23.91  ? 4584 ALA A CA    1 
ATOM   22427 C  C     . ALA A 1 4584 ? 201.046 159.769 143.211 1.00 24.98  ? 4584 ALA A C     1 
ATOM   22428 O  O     . ALA A 1 4584 ? 202.108 159.340 142.746 1.00 26.19  ? 4584 ALA A O     1 
ATOM   22429 C  CB    . ALA A 1 4584 ? 201.376 159.145 145.620 1.00 23.75  ? 4584 ALA A CB    1 
ATOM   22430 N  N     . LEU A 1 4585 ? 200.395 160.803 142.694 1.00 23.61  ? 4585 LEU A N     1 
ATOM   22431 C  CA    . LEU A 1 4585 ? 200.966 161.583 141.604 1.00 21.42  ? 4585 LEU A CA    1 
ATOM   22432 C  C     . LEU A 1 4585 ? 202.050 162.498 142.158 1.00 28.00  ? 4585 LEU A C     1 
ATOM   22433 O  O     . LEU A 1 4585 ? 201.761 163.318 143.037 1.00 33.28  ? 4585 LEU A O     1 
ATOM   22434 C  CB    . LEU A 1 4585 ? 199.887 162.402 140.910 1.00 21.54  ? 4585 LEU A CB    1 
ATOM   22435 C  CG    . LEU A 1 4585 ? 198.751 161.613 140.259 1.00 16.25  ? 4585 LEU A CG    1 
ATOM   22436 C  CD1   . LEU A 1 4585 ? 197.695 162.549 139.702 1.00 10.91  ? 4585 LEU A CD1   1 
ATOM   22437 C  CD2   . LEU A 1 4585 ? 199.294 160.713 139.166 1.00 20.60  ? 4585 LEU A CD2   1 
ATOM   22438 N  N     . PRO A 1 4586 ? 203.297 162.390 141.689 1.00 28.66  ? 4586 PRO A N     1 
ATOM   22439 C  CA    . PRO A 1 4586 ? 204.385 163.178 142.287 1.00 32.37  ? 4586 PRO A CA    1 
ATOM   22440 C  C     . PRO A 1 4586 ? 204.156 164.679 142.204 1.00 32.42  ? 4586 PRO A C     1 
ATOM   22441 O  O     . PRO A 1 4586 ? 204.102 165.361 143.231 1.00 34.90  ? 4586 PRO A O     1 
ATOM   22442 C  CB    . PRO A 1 4586 ? 205.618 162.754 141.475 1.00 34.14  ? 4586 PRO A CB    1 
ATOM   22443 C  CG    . PRO A 1 4586 ? 205.079 162.114 140.237 1.00 33.84  ? 4586 PRO A CG    1 
ATOM   22444 C  CD    . PRO A 1 4586 ? 203.768 161.513 140.606 1.00 26.79  ? 4586 PRO A CD    1 
ATOM   22445 N  N     . LEU A 1 4587 ? 204.009 165.201 140.990 1.00 32.38  ? 4587 LEU A N     1 
ATOM   22446 C  CA    . LEU A 1 4587 ? 203.740 166.615 140.786 1.00 27.16  ? 4587 LEU A CA    1 
ATOM   22447 C  C     . LEU A 1 4587 ? 202.819 166.779 139.589 1.00 29.61  ? 4587 LEU A C     1 
ATOM   22448 O  O     . LEU A 1 4587 ? 202.999 166.119 138.561 1.00 35.03  ? 4587 LEU A O     1 
ATOM   22449 C  CB    . LEU A 1 4587 ? 205.032 167.411 140.569 1.00 34.52  ? 4587 LEU A CB    1 
ATOM   22450 C  CG    . LEU A 1 4587 ? 204.875 168.913 140.330 1.00 32.28  ? 4587 LEU A CG    1 
ATOM   22451 C  CD1   . LEU A 1 4587 ? 204.461 169.621 141.607 1.00 29.86  ? 4587 LEU A CD1   1 
ATOM   22452 C  CD2   . LEU A 1 4587 ? 206.160 169.502 139.785 1.00 30.58  ? 4587 LEU A CD2   1 
ATOM   22453 N  N     . THR A 1 4588 ? 201.829 167.654 139.730 1.00 24.59  ? 4588 THR A N     1 
ATOM   22454 C  CA    . THR A 1 4588 ? 200.865 167.932 138.678 1.00 21.78  ? 4588 THR A CA    1 
ATOM   22455 C  C     . THR A 1 4588 ? 201.024 169.377 138.234 1.00 26.69  ? 4588 THR A C     1 
ATOM   22456 O  O     . THR A 1 4588 ? 200.999 170.291 139.062 1.00 25.35  ? 4588 THR A O     1 
ATOM   22457 C  CB    . THR A 1 4588 ? 199.436 167.677 139.163 1.00 21.28  ? 4588 THR A CB    1 
ATOM   22458 O  OG1   . THR A 1 4588 ? 199.285 166.295 139.508 1.00 30.19  ? 4588 THR A OG1   1 
ATOM   22459 C  CG2   . THR A 1 4588 ? 198.438 168.034 138.086 1.00 23.04  ? 4588 THR A CG2   1 
ATOM   22460 N  N     . GLN A 1 4589 ? 201.192 169.582 136.933 1.00 28.57  ? 4589 GLN A N     1 
ATOM   22461 C  CA    . GLN A 1 4589 ? 201.298 170.910 136.350 1.00 23.92  ? 4589 GLN A CA    1 
ATOM   22462 C  C     . GLN A 1 4589 ? 199.950 171.257 135.735 1.00 22.02  ? 4589 GLN A C     1 
ATOM   22463 O  O     . GLN A 1 4589 ? 199.504 170.597 134.789 1.00 31.02  ? 4589 GLN A O     1 
ATOM   22464 C  CB    . GLN A 1 4589 ? 202.408 170.960 135.305 1.00 27.13  ? 4589 GLN A CB    1 
ATOM   22465 C  CG    . GLN A 1 4589 ? 203.788 170.640 135.844 1.00 33.43  ? 4589 GLN A CG    1 
ATOM   22466 C  CD    . GLN A 1 4589 ? 204.861 170.747 134.782 1.00 46.45  ? 4589 GLN A CD    1 
ATOM   22467 O  OE1   . GLN A 1 4589 ? 205.539 169.769 134.467 1.00 53.00  ? 4589 GLN A OE1   1 
ATOM   22468 N  NE2   . GLN A 1 4589 ? 205.019 171.937 134.218 1.00 42.92  ? 4589 GLN A NE2   1 
ATOM   22469 N  N     . LEU A 1 4590 ? 199.298 172.271 136.296 1.00 22.43  ? 4590 LEU A N     1 
ATOM   22470 C  CA    . LEU A 1 4590 ? 198.084 172.840 135.728 1.00 18.41  ? 4590 LEU A CA    1 
ATOM   22471 C  C     . LEU A 1 4590 ? 198.477 174.021 134.853 1.00 22.79  ? 4590 LEU A C     1 
ATOM   22472 O  O     . LEU A 1 4590 ? 199.060 174.993 135.344 1.00 27.12  ? 4590 LEU A O     1 
ATOM   22473 C  CB    . LEU A 1 4590 ? 197.122 173.280 136.830 1.00 19.51  ? 4590 LEU A CB    1 
ATOM   22474 C  CG    . LEU A 1 4590 ? 196.878 172.310 137.984 1.00 19.85  ? 4590 LEU A CG    1 
ATOM   22475 C  CD1   . LEU A 1 4590 ? 195.881 172.899 138.963 1.00 19.26  ? 4590 LEU A CD1   1 
ATOM   22476 C  CD2   . LEU A 1 4590 ? 196.382 170.978 137.460 1.00 20.62  ? 4590 LEU A CD2   1 
ATOM   22477 N  N     . ARG A 1 4591 ? 198.175 173.932 133.563 1.00 22.38  ? 4591 ARG A N     1 
ATOM   22478 C  CA    . ARG A 1 4591 ? 198.596 174.924 132.585 1.00 18.73  ? 4591 ARG A CA    1 
ATOM   22479 C  C     . ARG A 1 4591 ? 197.367 175.483 131.883 1.00 22.47  ? 4591 ARG A C     1 
ATOM   22480 O  O     . ARG A 1 4591 ? 196.585 174.732 131.292 1.00 25.36  ? 4591 ARG A O     1 
ATOM   22481 C  CB    . ARG A 1 4591 ? 199.583 174.296 131.595 1.00 19.25  ? 4591 ARG A CB    1 
ATOM   22482 C  CG    . ARG A 1 4591 ? 200.180 175.221 130.550 1.00 26.98  ? 4591 ARG A CG    1 
ATOM   22483 C  CD    . ARG A 1 4591 ? 201.184 174.442 129.702 1.00 39.29  ? 4591 ARG A CD    1 
ATOM   22484 N  NE    . ARG A 1 4591 ? 201.843 175.257 128.689 1.00 53.52  ? 4591 ARG A NE    1 
ATOM   22485 C  CZ    . ARG A 1 4591 ? 201.395 175.434 127.454 1.00 57.95  ? 4591 ARG A CZ    1 
ATOM   22486 N  NH1   . ARG A 1 4591 ? 200.330 174.791 127.007 1.00 49.74  ? 4591 ARG A NH1   1 
ATOM   22487 N  NH2   . ARG A 1 4591 ? 202.049 176.255 126.638 1.00 57.00  ? 4591 ARG A NH2   1 
ATOM   22488 N  N     . TRP A 1 4592 ? 197.187 176.797 131.976 1.00 21.33  ? 4592 TRP A N     1 
ATOM   22489 C  CA    . TRP A 1 4592 ? 196.017 177.463 131.422 1.00 20.47  ? 4592 TRP A CA    1 
ATOM   22490 C  C     . TRP A 1 4592 ? 196.325 177.898 129.995 1.00 24.72  ? 4592 TRP A C     1 
ATOM   22491 O  O     . TRP A 1 4592 ? 197.338 178.560 129.748 1.00 33.13  ? 4592 TRP A O     1 
ATOM   22492 C  CB    . TRP A 1 4592 ? 195.622 178.663 132.282 1.00 19.77  ? 4592 TRP A CB    1 
ATOM   22493 C  CG    . TRP A 1 4592 ? 195.041 178.284 133.606 1.00 16.20  ? 4592 TRP A CG    1 
ATOM   22494 C  CD1   . TRP A 1 4592 ? 195.677 178.301 134.811 1.00 15.38  ? 4592 TRP A CD1   1 
ATOM   22495 C  CD2   . TRP A 1 4592 ? 193.707 177.834 133.862 1.00 16.11  ? 4592 TRP A CD2   1 
ATOM   22496 N  NE1   . TRP A 1 4592 ? 194.823 177.886 135.802 1.00 16.36  ? 4592 TRP A NE1   1 
ATOM   22497 C  CE2   . TRP A 1 4592 ? 193.606 177.594 135.245 1.00 14.76  ? 4592 TRP A CE2   1 
ATOM   22498 C  CE3   . TRP A 1 4592 ? 192.588 177.609 133.057 1.00 17.33  ? 4592 TRP A CE3   1 
ATOM   22499 C  CZ2   . TRP A 1 4592 ? 192.433 177.141 135.839 1.00 13.25  ? 4592 TRP A CZ2   1 
ATOM   22500 C  CZ3   . TRP A 1 4592 ? 191.424 177.161 133.649 1.00 14.27  ? 4592 TRP A CZ3   1 
ATOM   22501 C  CH2   . TRP A 1 4592 ? 191.356 176.931 135.026 1.00 12.73  ? 4592 TRP A CH2   1 
ATOM   22502 N  N     . VAL A 1 4593 ? 195.456 177.520 129.059 1.00 26.53  ? 4593 VAL A N     1 
ATOM   22503 C  CA    . VAL A 1 4593 ? 195.656 177.798 127.645 1.00 33.81  ? 4593 VAL A CA    1 
ATOM   22504 C  C     . VAL A 1 4593 ? 194.365 178.356 127.063 1.00 34.54  ? 4593 VAL A C     1 
ATOM   22505 O  O     . VAL A 1 4593 ? 193.308 178.327 127.690 1.00 32.61  ? 4593 VAL A O     1 
ATOM   22506 C  CB    . VAL A 1 4593 ? 196.107 176.550 126.860 1.00 30.68  ? 4593 VAL A CB    1 
ATOM   22507 C  CG1   . VAL A 1 4593 ? 197.510 176.168 127.256 1.00 27.61  ? 4593 VAL A CG1   1 
ATOM   22508 C  CG2   . VAL A 1 4593 ? 195.157 175.398 127.113 1.00 26.53  ? 4593 VAL A CG2   1 
ATOM   22509 N  N     . LYS A 1 4594 ? 194.472 178.880 125.846 1.00 37.38  ? 4594 LYS A N     1 
ATOM   22510 C  CA    . LYS A 1 4594 ? 193.300 179.398 125.156 1.00 37.94  ? 4594 LYS A CA    1 
ATOM   22511 C  C     . LYS A 1 4594 ? 192.439 178.251 124.645 1.00 37.95  ? 4594 LYS A C     1 
ATOM   22512 O  O     . LYS A 1 4594 ? 192.949 177.245 124.142 1.00 39.58  ? 4594 LYS A O     1 
ATOM   22513 C  CB    . LYS A 1 4594 ? 193.722 180.301 123.997 1.00 39.44  ? 4594 LYS A CB    1 
ATOM   22514 C  CG    . LYS A 1 4594 ? 194.570 181.489 124.418 1.00 37.35  ? 4594 LYS A CG    1 
ATOM   22515 C  CD    . LYS A 1 4594 ? 194.441 182.642 123.438 1.00 37.89  ? 4594 LYS A CD    1 
ATOM   22516 C  CE    . LYS A 1 4594 ? 192.993 183.063 123.271 1.00 41.20  ? 4594 LYS A CE    1 
ATOM   22517 N  NZ    . LYS A 1 4594 ? 192.353 183.362 124.581 1.00 43.43  ? 4594 LYS A NZ    1 
ATOM   22518 N  N     . GLN A 1 4595 ? 191.125 178.403 124.784 1.00 39.68  ? 4595 GLN A N     1 
ATOM   22519 C  CA    . GLN A 1 4595 ? 190.198 177.384 124.314 1.00 50.43  ? 4595 GLN A CA    1 
ATOM   22520 C  C     . GLN A 1 4595 ? 190.234 177.294 122.794 1.00 57.64  ? 4595 GLN A C     1 
ATOM   22521 O  O     . GLN A 1 4595 ? 190.252 178.311 122.095 1.00 58.30  ? 4595 GLN A O     1 
ATOM   22522 C  CB    . GLN A 1 4595 ? 188.781 177.699 124.794 1.00 52.72  ? 4595 GLN A CB    1 
ATOM   22523 C  CG    . GLN A 1 4595 ? 187.741 176.658 124.419 1.00 65.73  ? 4595 GLN A CG    1 
ATOM   22524 C  CD    . GLN A 1 4595 ? 188.024 175.303 125.033 1.00 69.94  ? 4595 GLN A CD    1 
ATOM   22525 O  OE1   . GLN A 1 4595 ? 188.474 174.381 124.352 1.00 67.81  ? 4595 GLN A OE1   1 
ATOM   22526 N  NE2   . GLN A 1 4595 ? 187.756 175.172 126.327 1.00 62.99  ? 4595 GLN A NE2   1 
ATOM   22527 N  N     . THR A 1 4596 ? 190.248 176.062 122.279 1.00 64.57  ? 4596 THR A N     1 
ATOM   22528 C  CA    . THR A 1 4596 ? 190.302 175.826 120.844 1.00 71.10  ? 4596 THR A CA    1 
ATOM   22529 C  C     . THR A 1 4596 ? 188.995 175.320 120.256 1.00 79.01  ? 4596 THR A C     1 
ATOM   22530 O  O     . THR A 1 4596 ? 188.797 175.450 119.043 1.00 81.53  ? 4596 THR A O     1 
ATOM   22531 C  CB    . THR A 1 4596 ? 191.414 174.821 120.505 1.00 71.74  ? 4596 THR A CB    1 
ATOM   22532 O  OG1   . THR A 1 4596 ? 191.077 173.534 121.037 1.00 78.12  ? 4596 THR A OG1   1 
ATOM   22533 C  CG2   . THR A 1 4596 ? 192.740 175.278 121.091 1.00 58.40  ? 4596 THR A CG2   1 
ATOM   22534 N  N     . ASN A 1 4597 ? 188.108 174.753 121.077 1.00 80.85  ? 4597 ASN A N     1 
ATOM   22535 C  CA    . ASN A 1 4597 ? 186.803 174.264 120.625 1.00 84.90  ? 4597 ASN A CA    1 
ATOM   22536 C  C     . ASN A 1 4597 ? 186.949 173.239 119.503 1.00 83.52  ? 4597 ASN A C     1 
ATOM   22537 O  O     . ASN A 1 4597 ? 186.172 173.223 118.546 1.00 82.01  ? 4597 ASN A O     1 
ATOM   22538 C  CB    . ASN A 1 4597 ? 185.901 175.421 120.193 1.00 85.61  ? 4597 ASN A CB    1 
ATOM   22539 C  CG    . ASN A 1 4597 ? 185.548 176.344 121.341 1.00 86.43  ? 4597 ASN A CG    1 
ATOM   22540 O  OD1   . ASN A 1 4597 ? 185.965 177.502 121.373 1.00 84.77  ? 4597 ASN A OD1   1 
ATOM   22541 N  ND2   . ASN A 1 4597 ? 184.775 175.835 122.293 1.00 88.13  ? 4597 ASN A ND2   1 
ATOM   22542 N  N     . THR A 1 4598 ? 187.953 172.374 119.622 1.00 84.56  ? 4598 THR A N     1 
ATOM   22543 C  CA    . THR A 1 4598 ? 188.242 171.344 118.629 1.00 83.80  ? 4598 THR A CA    1 
ATOM   22544 C  C     . THR A 1 4598 ? 187.917 169.951 119.162 1.00 87.56  ? 4598 THR A C     1 
ATOM   22545 O  O     . THR A 1 4598 ? 188.622 168.981 118.877 1.00 81.77  ? 4598 THR A O     1 
ATOM   22546 C  CB    . THR A 1 4598 ? 189.699 171.415 118.182 1.00 78.89  ? 4598 THR A CB    1 
ATOM   22547 O  OG1   . THR A 1 4598 ? 190.558 171.351 119.327 1.00 75.33  ? 4598 THR A OG1   1 
ATOM   22548 C  CG2   . THR A 1 4598 ? 189.962 172.709 117.428 1.00 77.79  ? 4598 THR A CG2   1 
ATOM   22549 N  N     . GLU A 1 4599 ? 186.845 169.850 119.941 1.00 95.26  ? 4599 GLU A N     1 
ATOM   22550 C  CA    . GLU A 1 4599 ? 186.359 168.587 120.514 1.00 94.81  ? 4599 GLU A CA    1 
ATOM   22551 C  C     . GLU A 1 4599 ? 187.474 167.982 121.372 1.00 92.59  ? 4599 GLU A C     1 
ATOM   22552 O  O     . GLU A 1 4599 ? 188.268 168.708 121.984 1.00 95.21  ? 4599 GLU A O     1 
ATOM   22553 C  CB    . GLU A 1 4599 ? 185.850 167.681 119.407 1.00 88.92  ? 4599 GLU A CB    1 
ATOM   22554 C  CG    . GLU A 1 4599 ? 184.807 168.322 118.508 1.00 96.25  ? 4599 GLU A CG    1 
ATOM   22555 C  CD    . GLU A 1 4599 ? 184.779 167.709 117.122 1.00 97.19  ? 4599 GLU A CD    1 
ATOM   22556 O  OE1   . GLU A 1 4599 ? 184.805 166.464 117.021 1.00 94.38  ? 4599 GLU A OE1   1 
ATOM   22557 O  OE2   . GLU A 1 4599 ? 184.731 168.471 116.134 1.00 93.03  ? 4599 GLU A OE2   1 
ATOM   22558 N  N     . LYS A 1 4600 ? 187.542 166.654 121.428 1.00 78.98  ? 4600 LYS A N     1 
ATOM   22559 C  CA    . LYS A 1 4600 ? 188.584 165.972 122.179 1.00 71.91  ? 4600 LYS A CA    1 
ATOM   22560 C  C     . LYS A 1 4600 ? 188.830 164.607 121.554 1.00 66.56  ? 4600 LYS A C     1 
ATOM   22561 O  O     . LYS A 1 4600 ? 187.980 164.064 120.843 1.00 60.23  ? 4600 LYS A O     1 
ATOM   22562 C  CB    . LYS A 1 4600 ? 188.213 165.829 123.661 1.00 63.77  ? 4600 LYS A CB    1 
ATOM   22563 C  CG    . LYS A 1 4600 ? 187.014 164.937 123.921 1.00 65.20  ? 4600 LYS A CG    1 
ATOM   22564 C  CD    . LYS A 1 4600 ? 186.735 164.815 125.409 1.00 64.06  ? 4600 LYS A CD    1 
ATOM   22565 C  CE    . LYS A 1 4600 ? 186.161 166.106 125.972 1.00 65.04  ? 4600 LYS A CE    1 
ATOM   22566 N  NZ    . LYS A 1 4600 ? 184.812 166.404 125.416 1.00 79.83  ? 4600 LYS A NZ    1 
ATOM   22567 N  N     . LYS A 1 4601 ? 190.009 164.059 121.832 1.00 65.13  ? 4601 LYS A N     1 
ATOM   22568 C  CA    . LYS A 1 4601 ? 190.387 162.768 121.279 1.00 57.31  ? 4601 LYS A CA    1 
ATOM   22569 C  C     . LYS A 1 4601 ? 189.546 161.653 121.891 1.00 54.40  ? 4601 LYS A C     1 
ATOM   22570 O  O     . LYS A 1 4601 ? 189.050 161.763 123.016 1.00 49.22  ? 4601 LYS A O     1 
ATOM   22571 C  CB    . LYS A 1 4601 ? 191.873 162.502 121.521 1.00 55.12  ? 4601 LYS A CB    1 
ATOM   22572 C  CG    . LYS A 1 4601 ? 192.797 163.413 120.729 1.00 63.12  ? 4601 LYS A CG    1 
ATOM   22573 C  CD    . LYS A 1 4601 ? 194.258 163.156 121.062 1.00 65.15  ? 4601 LYS A CD    1 
ATOM   22574 C  CE    . LYS A 1 4601 ? 194.726 161.818 120.518 1.00 61.82  ? 4601 LYS A CE    1 
ATOM   22575 N  NZ    . LYS A 1 4601 ? 194.767 161.812 119.029 1.00 53.54  ? 4601 LYS A NZ    1 
ATOM   22576 N  N     . ALA A 1 4602 ? 189.378 160.571 121.127 1.00 52.82  ? 4602 ALA A N     1 
ATOM   22577 C  CA    . ALA A 1 4602 ? 188.603 159.435 121.615 1.00 50.91  ? 4602 ALA A CA    1 
ATOM   22578 C  C     . ALA A 1 4602 ? 189.270 158.771 122.811 1.00 43.77  ? 4602 ALA A C     1 
ATOM   22579 O  O     . ALA A 1 4602 ? 188.587 158.155 123.638 1.00 33.79  ? 4602 ALA A O     1 
ATOM   22580 C  CB    . ALA A 1 4602 ? 188.392 158.419 120.492 1.00 43.78  ? 4602 ALA A CB    1 
ATOM   22581 N  N     . SER A 1 4603 ? 190.593 158.881 122.921 1.00 43.71  ? 4603 SER A N     1 
ATOM   22582 C  CA    . SER A 1 4603 ? 191.317 158.318 124.051 1.00 45.04  ? 4603 SER A CA    1 
ATOM   22583 C  C     . SER A 1 4603 ? 191.359 159.251 125.253 1.00 40.24  ? 4603 SER A C     1 
ATOM   22584 O  O     . SER A 1 4603 ? 191.942 158.885 126.279 1.00 41.60  ? 4603 SER A O     1 
ATOM   22585 C  CB    . SER A 1 4603 ? 192.744 157.958 123.631 1.00 42.54  ? 4603 SER A CB    1 
ATOM   22586 O  OG    . SER A 1 4603 ? 193.306 158.974 122.819 1.00 42.94  ? 4603 SER A OG    1 
ATOM   22587 N  N     . VAL A 1 4604 ? 190.768 160.435 125.158 1.00 37.25  ? 4604 VAL A N     1 
ATOM   22588 C  CA    . VAL A 1 4604 ? 190.790 161.384 126.264 1.00 34.20  ? 4604 VAL A CA    1 
ATOM   22589 C  C     . VAL A 1 4604 ? 189.651 161.063 127.222 1.00 32.10  ? 4604 VAL A C     1 
ATOM   22590 O  O     . VAL A 1 4604 ? 188.493 160.923 126.811 1.00 41.59  ? 4604 VAL A O     1 
ATOM   22591 C  CB    . VAL A 1 4604 ? 190.697 162.828 125.747 1.00 38.43  ? 4604 VAL A CB    1 
ATOM   22592 C  CG1   . VAL A 1 4604 ? 190.200 163.755 126.843 1.00 28.94  ? 4604 VAL A CG1   1 
ATOM   22593 C  CG2   . VAL A 1 4604 ? 192.051 163.288 125.233 1.00 40.25  ? 4604 VAL A CG2   1 
ATOM   22594 N  N     . VAL A 1 4605 ? 189.983 160.943 128.502 1.00 21.98  ? 4605 VAL A N     1 
ATOM   22595 C  CA    . VAL A 1 4605 ? 189.020 160.663 129.559 1.00 17.79  ? 4605 VAL A CA    1 
ATOM   22596 C  C     . VAL A 1 4605 ? 188.968 161.858 130.503 1.00 18.02  ? 4605 VAL A C     1 
ATOM   22597 O  O     . VAL A 1 4605 ? 189.998 162.472 130.809 1.00 21.54  ? 4605 VAL A O     1 
ATOM   22598 C  CB    . VAL A 1 4605 ? 189.369 159.359 130.309 1.00 18.40  ? 4605 VAL A CB    1 
ATOM   22599 C  CG1   . VAL A 1 4605 ? 190.582 159.543 131.212 1.00 17.40  ? 4605 VAL A CG1   1 
ATOM   22600 C  CG2   . VAL A 1 4605 ? 188.181 158.874 131.109 1.00 17.94  ? 4605 VAL A CG2   1 
ATOM   22601 N  N     . THR A 1 4606 ? 187.762 162.211 130.933 1.00 14.10  ? 4606 THR A N     1 
ATOM   22602 C  CA    . THR A 1 4606 ? 187.555 163.298 131.880 1.00 12.87  ? 4606 THR A CA    1 
ATOM   22603 C  C     . THR A 1 4606 ? 187.329 162.704 133.264 1.00 19.20  ? 4606 THR A C     1 
ATOM   22604 O  O     . THR A 1 4606 ? 186.387 161.931 133.467 1.00 21.42  ? 4606 THR A O     1 
ATOM   22605 C  CB    . THR A 1 4606 ? 186.372 164.175 131.470 1.00 16.96  ? 4606 THR A CB    1 
ATOM   22606 O  OG1   . THR A 1 4606 ? 186.672 164.835 130.235 1.00 30.87  ? 4606 THR A OG1   1 
ATOM   22607 C  CG2   . THR A 1 4606 ? 186.094 165.220 132.535 1.00 12.44  ? 4606 THR A CG2   1 
ATOM   22608 N  N     . LEU A 1 4607 ? 188.192 163.066 134.208 1.00 14.96  ? 4607 LEU A N     1 
ATOM   22609 C  CA    . LEU A 1 4607 ? 188.159 162.533 135.554 1.00 11.27  ? 4607 LEU A CA    1 
ATOM   22610 C  C     . LEU A 1 4607 ? 187.833 163.632 136.548 1.00 13.71  ? 4607 LEU A C     1 
ATOM   22611 O  O     . LEU A 1 4607 ? 188.422 164.719 136.481 1.00 15.92  ? 4607 LEU A O     1 
ATOM   22612 C  CB    . LEU A 1 4607 ? 189.504 161.897 135.915 1.00 8.48   ? 4607 LEU A CB    1 
ATOM   22613 C  CG    . LEU A 1 4607 ? 189.895 160.613 135.187 1.00 11.40  ? 4607 LEU A CG    1 
ATOM   22614 C  CD1   . LEU A 1 4607 ? 191.021 159.930 135.930 1.00 11.26  ? 4607 LEU A CD1   1 
ATOM   22615 C  CD2   . LEU A 1 4607 ? 188.704 159.684 135.044 1.00 11.97  ? 4607 LEU A CD2   1 
ATOM   22616 N  N     . PRO A 1 4608 ? 186.903 163.392 137.467 1.00 14.00  ? 4608 PRO A N     1 
ATOM   22617 C  CA    . PRO A 1 4608 ? 186.665 164.357 138.544 1.00 11.35  ? 4608 PRO A CA    1 
ATOM   22618 C  C     . PRO A 1 4608 ? 187.834 164.401 139.514 1.00 11.16  ? 4608 PRO A C     1 
ATOM   22619 O  O     . PRO A 1 4608 ? 188.564 163.423 139.689 1.00 13.10  ? 4608 PRO A O     1 
ATOM   22620 C  CB    . PRO A 1 4608 ? 185.402 163.820 139.224 1.00 10.04  ? 4608 PRO A CB    1 
ATOM   22621 C  CG    . PRO A 1 4608 ? 185.403 162.365 138.924 1.00 8.30   ? 4608 PRO A CG    1 
ATOM   22622 C  CD    . PRO A 1 4608 ? 186.059 162.192 137.589 1.00 7.51   ? 4608 PRO A CD    1 
ATOM   22623 N  N     . VAL A 1 4609 ? 188.006 165.553 140.151 1.00 11.53  ? 4609 VAL A N     1 
ATOM   22624 C  CA    . VAL A 1 4609 ? 189.005 165.725 141.202 1.00 11.80  ? 4609 VAL A CA    1 
ATOM   22625 C  C     . VAL A 1 4609 ? 188.232 166.053 142.473 1.00 11.73  ? 4609 VAL A C     1 
ATOM   22626 O  O     . VAL A 1 4609 ? 187.835 167.198 142.707 1.00 14.55  ? 4609 VAL A O     1 
ATOM   22627 C  CB    . VAL A 1 4609 ? 190.033 166.807 140.869 1.00 7.80   ? 4609 VAL A CB    1 
ATOM   22628 C  CG1   . VAL A 1 4609 ? 191.102 166.866 141.945 1.00 7.47   ? 4609 VAL A CG1   1 
ATOM   22629 C  CG2   . VAL A 1 4609 ? 190.657 166.538 139.514 1.00 7.37   ? 4609 VAL A CG2   1 
ATOM   22630 N  N     . TYR A 1 4610 ? 188.006 165.041 143.301 1.00 12.03  ? 4610 TYR A N     1 
ATOM   22631 C  CA    . TYR A 1 4610 ? 187.257 165.224 144.530 1.00 9.91   ? 4610 TYR A CA    1 
ATOM   22632 C  C     . TYR A 1 4610 ? 188.171 165.715 145.647 1.00 10.30  ? 4610 TYR A C     1 
ATOM   22633 O  O     . TYR A 1 4610 ? 189.384 165.491 145.642 1.00 13.10  ? 4610 TYR A O     1 
ATOM   22634 C  CB    . TYR A 1 4610 ? 186.570 163.922 144.936 1.00 8.43   ? 4610 TYR A CB    1 
ATOM   22635 C  CG    . TYR A 1 4610 ? 185.520 163.466 143.953 1.00 9.35   ? 4610 TYR A CG    1 
ATOM   22636 C  CD1   . TYR A 1 4610 ? 184.350 164.190 143.776 1.00 9.17   ? 4610 TYR A CD1   1 
ATOM   22637 C  CD2   . TYR A 1 4610 ? 185.703 162.321 143.195 1.00 9.24   ? 4610 TYR A CD2   1 
ATOM   22638 C  CE1   . TYR A 1 4610 ? 183.389 163.780 142.878 1.00 9.39   ? 4610 TYR A CE1   1 
ATOM   22639 C  CE2   . TYR A 1 4610 ? 184.747 161.904 142.295 1.00 8.86   ? 4610 TYR A CE2   1 
ATOM   22640 C  CZ    . TYR A 1 4610 ? 183.593 162.636 142.141 1.00 12.31  ? 4610 TYR A CZ    1 
ATOM   22641 O  OH    . TYR A 1 4610 ? 182.638 162.221 141.243 1.00 19.82  ? 4610 TYR A OH    1 
ATOM   22642 N  N     . LEU A 1 4611 ? 187.564 166.404 146.613 1.00 12.31  ? 4611 LEU A N     1 
ATOM   22643 C  CA    . LEU A 1 4611 ? 188.335 166.968 147.714 1.00 10.96  ? 4611 LEU A CA    1 
ATOM   22644 C  C     . LEU A 1 4611 ? 188.882 165.878 148.627 1.00 14.55  ? 4611 LEU A C     1 
ATOM   22645 O  O     . LEU A 1 4611 ? 190.019 165.973 149.102 1.00 19.48  ? 4611 LEU A O     1 
ATOM   22646 C  CB    . LEU A 1 4611 ? 187.472 167.952 148.501 1.00 13.07  ? 4611 LEU A CB    1 
ATOM   22647 C  CG    . LEU A 1 4611 ? 188.164 168.736 149.612 1.00 14.43  ? 4611 LEU A CG    1 
ATOM   22648 C  CD1   . LEU A 1 4611 ? 189.399 169.442 149.075 1.00 17.30  ? 4611 LEU A CD1   1 
ATOM   22649 C  CD2   . LEU A 1 4611 ? 187.199 169.735 150.208 1.00 15.95  ? 4611 LEU A CD2   1 
ATOM   22650 N  N     . ASN A 1 4612 ? 188.095 164.837 148.881 1.00 16.36  ? 4612 ASN A N     1 
ATOM   22651 C  CA    . ASN A 1 4612 ? 188.501 163.762 149.777 1.00 11.95  ? 4612 ASN A CA    1 
ATOM   22652 C  C     . ASN A 1 4612 ? 187.901 162.454 149.271 1.00 10.67  ? 4612 ASN A C     1 
ATOM   22653 O  O     . ASN A 1 4612 ? 187.275 162.407 148.208 1.00 9.33   ? 4612 ASN A O     1 
ATOM   22654 C  CB    . ASN A 1 4612 ? 188.085 164.080 151.219 1.00 10.44  ? 4612 ASN A CB    1 
ATOM   22655 C  CG    . ASN A 1 4612 ? 186.679 164.635 151.311 1.00 13.64  ? 4612 ASN A CG    1 
ATOM   22656 O  OD1   . ASN A 1 4612 ? 185.848 164.404 150.434 1.00 14.37  ? 4612 ASN A OD1   1 
ATOM   22657 N  ND2   . ASN A 1 4612 ? 186.409 165.382 152.371 1.00 18.19  ? 4612 ASN A ND2   1 
ATOM   22658 N  N     . PHE A 1 4613 ? 188.098 161.383 150.044 1.00 11.17  ? 4613 PHE A N     1 
ATOM   22659 C  CA    . PHE A 1 4613 ? 187.634 160.061 149.640 1.00 8.40   ? 4613 PHE A CA    1 
ATOM   22660 C  C     . PHE A 1 4613 ? 186.116 159.953 149.615 1.00 9.40   ? 4613 PHE A C     1 
ATOM   22661 O  O     . PHE A 1 4613 ? 185.584 159.063 148.943 1.00 11.36  ? 4613 PHE A O     1 
ATOM   22662 C  CB    . PHE A 1 4613 ? 188.225 158.995 150.567 1.00 10.30  ? 4613 PHE A CB    1 
ATOM   22663 C  CG    . PHE A 1 4613 ? 187.595 158.953 151.932 1.00 13.65  ? 4613 PHE A CG    1 
ATOM   22664 C  CD1   . PHE A 1 4613 ? 186.516 158.125 152.193 1.00 11.74  ? 4613 PHE A CD1   1 
ATOM   22665 C  CD2   . PHE A 1 4613 ? 188.087 159.744 152.956 1.00 12.20  ? 4613 PHE A CD2   1 
ATOM   22666 C  CE1   . PHE A 1 4613 ? 185.940 158.090 153.444 1.00 15.23  ? 4613 PHE A CE1   1 
ATOM   22667 C  CE2   . PHE A 1 4613 ? 187.516 159.713 154.209 1.00 14.00  ? 4613 PHE A CE2   1 
ATOM   22668 C  CZ    . PHE A 1 4613 ? 186.441 158.884 154.454 1.00 21.94  ? 4613 PHE A CZ    1 
ATOM   22669 N  N     . THR A 1 4614 ? 185.409 160.831 150.329 1.00 8.69   ? 4614 THR A N     1 
ATOM   22670 C  CA    . THR A 1 4614 ? 183.953 160.780 150.342 1.00 8.13   ? 4614 THR A CA    1 
ATOM   22671 C  C     . THR A 1 4614 ? 183.346 161.121 148.988 1.00 9.61   ? 4614 THR A C     1 
ATOM   22672 O  O     . THR A 1 4614 ? 182.187 160.773 148.742 1.00 17.03  ? 4614 THR A O     1 
ATOM   22673 C  CB    . THR A 1 4614 ? 183.401 161.728 151.407 1.00 8.29   ? 4614 THR A CB    1 
ATOM   22674 O  OG1   . THR A 1 4614 ? 183.840 163.063 151.132 1.00 12.21  ? 4614 THR A OG1   1 
ATOM   22675 C  CG2   . THR A 1 4614 ? 183.886 161.318 152.785 1.00 8.78   ? 4614 THR A CG2   1 
ATOM   22676 N  N     . ARG A 1 4615 ? 184.101 161.792 148.115 1.00 7.60   ? 4615 ARG A N     1 
ATOM   22677 C  CA    . ARG A 1 4615 ? 183.641 162.166 146.777 1.00 8.74   ? 4615 ARG A CA    1 
ATOM   22678 C  C     . ARG A 1 4615 ? 182.387 163.034 146.833 1.00 14.39  ? 4615 ARG A C     1 
ATOM   22679 O  O     . ARG A 1 4615 ? 181.535 162.971 145.944 1.00 25.68  ? 4615 ARG A O     1 
ATOM   22680 C  CB    . ARG A 1 4615 ? 183.396 160.930 145.906 1.00 7.22   ? 4615 ARG A CB    1 
ATOM   22681 C  CG    . ARG A 1 4615 ? 184.609 160.031 145.748 1.00 6.42   ? 4615 ARG A CG    1 
ATOM   22682 C  CD    . ARG A 1 4615 ? 184.506 159.187 144.495 1.00 5.42   ? 4615 ARG A CD    1 
ATOM   22683 N  NE    . ARG A 1 4615 ? 185.588 158.216 144.401 1.00 6.45   ? 4615 ARG A NE    1 
ATOM   22684 C  CZ    . ARG A 1 4615 ? 185.842 157.480 143.328 1.00 6.20   ? 4615 ARG A CZ    1 
ATOM   22685 N  NH1   . ARG A 1 4615 ? 185.101 157.570 142.237 1.00 4.02   ? 4615 ARG A NH1   1 
ATOM   22686 N  NH2   . ARG A 1 4615 ? 186.865 156.630 143.352 1.00 7.74   ? 4615 ARG A NH2   1 
ATOM   22687 N  N     . ALA A 1 4616 ? 182.268 163.853 147.876 1.00 11.85  ? 4616 ALA A N     1 
ATOM   22688 C  CA    . ALA A 1 4616 ? 181.093 164.696 148.052 1.00 17.65  ? 4616 ALA A CA    1 
ATOM   22689 C  C     . ALA A 1 4616 ? 181.264 166.081 147.446 1.00 26.85  ? 4616 ALA A C     1 
ATOM   22690 O  O     . ALA A 1 4616 ? 180.269 166.709 147.067 1.00 30.47  ? 4616 ALA A O     1 
ATOM   22691 C  CB    . ALA A 1 4616 ? 180.757 164.827 149.539 1.00 16.95  ? 4616 ALA A CB    1 
ATOM   22692 N  N     . ASP A 1 4617 ? 182.495 166.572 147.347 1.00 28.60  ? 4617 ASP A N     1 
ATOM   22693 C  CA    . ASP A 1 4617 ? 182.780 167.890 146.796 1.00 20.61  ? 4617 ASP A CA    1 
ATOM   22694 C  C     . ASP A 1 4617 ? 183.687 167.745 145.584 1.00 15.75  ? 4617 ASP A C     1 
ATOM   22695 O  O     . ASP A 1 4617 ? 184.741 167.108 145.665 1.00 14.55  ? 4617 ASP A O     1 
ATOM   22696 C  CB    . ASP A 1 4617 ? 183.430 168.795 147.842 1.00 24.30  ? 4617 ASP A CB    1 
ATOM   22697 C  CG    . ASP A 1 4617 ? 182.472 169.181 148.948 1.00 41.69  ? 4617 ASP A CG    1 
ATOM   22698 O  OD1   . ASP A 1 4617 ? 181.253 169.252 148.684 1.00 44.74  ? 4617 ASP A OD1   1 
ATOM   22699 O  OD2   . ASP A 1 4617 ? 182.936 169.411 150.082 1.00 42.05  ? 4617 ASP A OD2   1 
ATOM   22700 N  N     . LEU A 1 4618 ? 183.276 168.340 144.471 1.00 17.52  ? 4618 LEU A N     1 
ATOM   22701 C  CA    . LEU A 1 4618 ? 184.023 168.283 143.223 1.00 13.70  ? 4618 LEU A CA    1 
ATOM   22702 C  C     . LEU A 1 4618 ? 184.770 169.597 143.035 1.00 17.91  ? 4618 LEU A C     1 
ATOM   22703 O  O     . LEU A 1 4618 ? 184.154 170.667 143.006 1.00 20.80  ? 4618 LEU A O     1 
ATOM   22704 C  CB    . LEU A 1 4618 ? 183.087 168.019 142.046 1.00 14.06  ? 4618 LEU A CB    1 
ATOM   22705 C  CG    . LEU A 1 4618 ? 183.663 168.240 140.649 1.00 18.61  ? 4618 LEU A CG    1 
ATOM   22706 C  CD1   . LEU A 1 4618 ? 184.573 167.095 140.279 1.00 15.30  ? 4618 LEU A CD1   1 
ATOM   22707 C  CD2   . LEU A 1 4618 ? 182.545 168.388 139.632 1.00 16.53  ? 4618 LEU A CD2   1 
ATOM   22708 N  N     . ILE A 1 4619 ? 186.094 169.513 142.905 1.00 16.85  ? 4619 ILE A N     1 
ATOM   22709 C  CA    . ILE A 1 4619 ? 186.902 170.717 142.746 1.00 14.30  ? 4619 ILE A CA    1 
ATOM   22710 C  C     . ILE A 1 4619 ? 186.965 171.131 141.283 1.00 14.30  ? 4619 ILE A C     1 
ATOM   22711 O  O     . ILE A 1 4619 ? 186.617 172.262 140.927 1.00 17.56  ? 4619 ILE A O     1 
ATOM   22712 C  CB    . ILE A 1 4619 ? 188.307 170.499 143.336 1.00 16.25  ? 4619 ILE A CB    1 
ATOM   22713 C  CG1   . ILE A 1 4619 ? 188.214 169.797 144.692 1.00 14.62  ? 4619 ILE A CG1   1 
ATOM   22714 C  CG2   . ILE A 1 4619 ? 189.035 171.825 143.483 1.00 19.00  ? 4619 ILE A CG2   1 
ATOM   22715 C  CD1   . ILE A 1 4619 ? 187.437 170.573 145.733 1.00 18.12  ? 4619 ILE A CD1   1 
ATOM   22716 N  N     . PHE A 1 4620 ? 187.399 170.224 140.414 1.00 12.09  ? 4620 PHE A N     1 
ATOM   22717 C  CA    . PHE A 1 4620 ? 187.454 170.483 138.980 1.00 13.73  ? 4620 PHE A CA    1 
ATOM   22718 C  C     . PHE A 1 4620 ? 187.537 169.144 138.254 1.00 15.43  ? 4620 PHE A C     1 
ATOM   22719 O  O     . PHE A 1 4620 ? 187.345 168.079 138.851 1.00 16.16  ? 4620 PHE A O     1 
ATOM   22720 C  CB    . PHE A 1 4620 ? 188.621 171.414 138.621 1.00 11.21  ? 4620 PHE A CB    1 
ATOM   22721 C  CG    . PHE A 1 4620 ? 189.976 170.901 139.034 1.00 11.75  ? 4620 PHE A CG    1 
ATOM   22722 C  CD1   . PHE A 1 4620 ? 190.368 170.911 140.362 1.00 15.40  ? 4620 PHE A CD1   1 
ATOM   22723 C  CD2   . PHE A 1 4620 ? 190.867 170.433 138.086 1.00 10.08  ? 4620 PHE A CD2   1 
ATOM   22724 C  CE1   . PHE A 1 4620 ? 191.613 170.447 140.737 1.00 11.80  ? 4620 PHE A CE1   1 
ATOM   22725 C  CE2   . PHE A 1 4620 ? 192.116 169.970 138.456 1.00 8.13   ? 4620 PHE A CE2   1 
ATOM   22726 C  CZ    . PHE A 1 4620 ? 192.488 169.976 139.782 1.00 8.97   ? 4620 PHE A CZ    1 
ATOM   22727 N  N     . THR A 1 4621 ? 187.804 169.201 136.952 1.00 16.77  ? 4621 THR A N     1 
ATOM   22728 C  CA    . THR A 1 4621 ? 187.912 168.016 136.115 1.00 13.45  ? 4621 THR A CA    1 
ATOM   22729 C  C     . THR A 1 4621 ? 189.221 168.064 135.344 1.00 13.97  ? 4621 THR A C     1 
ATOM   22730 O  O     . THR A 1 4621 ? 189.677 169.140 134.946 1.00 17.58  ? 4621 THR A O     1 
ATOM   22731 C  CB    . THR A 1 4621 ? 186.737 167.907 135.137 1.00 14.30  ? 4621 THR A CB    1 
ATOM   22732 O  OG1   . THR A 1 4621 ? 186.731 169.044 134.267 1.00 24.35  ? 4621 THR A OG1   1 
ATOM   22733 C  CG2   . THR A 1 4621 ? 185.415 167.842 135.889 1.00 10.24  ? 4621 THR A CG2   1 
ATOM   22734 N  N     . VAL A 1 4622 ? 189.822 166.897 135.137 1.00 14.06  ? 4622 VAL A N     1 
ATOM   22735 C  CA    . VAL A 1 4622 ? 191.089 166.778 134.428 1.00 14.53  ? 4622 VAL A CA    1 
ATOM   22736 C  C     . VAL A 1 4622 ? 190.881 165.910 133.196 1.00 15.53  ? 4622 VAL A C     1 
ATOM   22737 O  O     . VAL A 1 4622 ? 190.205 164.879 133.257 1.00 18.47  ? 4622 VAL A O     1 
ATOM   22738 C  CB    . VAL A 1 4622 ? 192.201 166.200 135.330 1.00 19.85  ? 4622 VAL A CB    1 
ATOM   22739 C  CG1   . VAL A 1 4622 ? 192.510 167.159 136.459 1.00 14.21  ? 4622 VAL A CG1   1 
ATOM   22740 C  CG2   . VAL A 1 4622 ? 191.800 164.842 135.889 1.00 20.16  ? 4622 VAL A CG2   1 
ATOM   22741 N  N     . ASP A 1 4623 ? 191.448 166.337 132.073 1.00 18.22  ? 4623 ASP A N     1 
ATOM   22742 C  CA    . ASP A 1 4623 ? 191.382 165.581 130.828 1.00 19.52  ? 4623 ASP A CA    1 
ATOM   22743 C  C     . ASP A 1 4623 ? 192.712 164.863 130.632 1.00 19.32  ? 4623 ASP A C     1 
ATOM   22744 O  O     . ASP A 1 4623 ? 193.736 165.498 130.364 1.00 22.76  ? 4623 ASP A O     1 
ATOM   22745 C  CB    . ASP A 1 4623 ? 191.065 166.498 129.649 1.00 22.29  ? 4623 ASP A CB    1 
ATOM   22746 C  CG    . ASP A 1 4623 ? 189.577 166.729 129.477 1.00 28.81  ? 4623 ASP A CG    1 
ATOM   22747 O  OD1   . ASP A 1 4623 ? 189.106 167.841 129.793 1.00 44.53  ? 4623 ASP A OD1   1 
ATOM   22748 O  OD2   . ASP A 1 4623 ? 188.876 165.800 129.026 1.00 26.48  ? 4623 ASP A OD2   1 
ATOM   22749 N  N     . PHE A 1 4624 ? 192.694 163.544 130.776 1.00 17.45  ? 4624 PHE A N     1 
ATOM   22750 C  CA    . PHE A 1 4624 ? 193.872 162.710 130.603 1.00 17.66  ? 4624 PHE A CA    1 
ATOM   22751 C  C     . PHE A 1 4624 ? 193.780 161.937 129.295 1.00 24.19  ? 4624 PHE A C     1 
ATOM   22752 O  O     . PHE A 1 4624 ? 192.712 161.811 128.696 1.00 30.01  ? 4624 PHE A O     1 
ATOM   22753 C  CB    . PHE A 1 4624 ? 194.022 161.737 131.774 1.00 19.46  ? 4624 PHE A CB    1 
ATOM   22754 C  CG    . PHE A 1 4624 ? 194.812 162.286 132.924 1.00 21.37  ? 4624 PHE A CG    1 
ATOM   22755 C  CD1   . PHE A 1 4624 ? 196.177 162.481 132.813 1.00 23.15  ? 4624 PHE A CD1   1 
ATOM   22756 C  CD2   . PHE A 1 4624 ? 194.188 162.610 134.116 1.00 21.47  ? 4624 PHE A CD2   1 
ATOM   22757 C  CE1   . PHE A 1 4624 ? 196.905 162.986 133.871 1.00 24.49  ? 4624 PHE A CE1   1 
ATOM   22758 C  CE2   . PHE A 1 4624 ? 194.911 163.115 135.177 1.00 19.00  ? 4624 PHE A CE2   1 
ATOM   22759 C  CZ    . PHE A 1 4624 ? 196.271 163.304 135.054 1.00 20.56  ? 4624 PHE A CZ    1 
ATOM   22760 N  N     . GLU A 1 4625 ? 194.918 161.412 128.859 1.00 28.74  ? 4625 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4625 ? 195.005 160.604 127.645 1.00 27.52  ? 4625 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4625 ? 195.402 159.191 128.054 1.00 32.46  ? 4625 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4625 ? 196.571 158.929 128.350 1.00 43.69  ? 4625 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4625 ? 196.006 161.204 126.663 1.00 32.42  ? 4625 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4625 ? 195.828 160.734 125.232 1.00 50.39  ? 4625 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4625 ? 196.986 161.134 124.341 1.00 56.74  ? 4625 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4625 ? 197.561 162.219 124.565 1.00 51.20  ? 4625 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4625 ? 197.322 160.362 123.418 1.00 62.44  ? 4625 GLU A OE2   1 
ATOM   22769 N  N     . ILE A 1 4626 ? 194.430 158.279 128.069 1.00 29.44  ? 4626 ILE A N     1 
ATOM   22770 C  CA    . ILE A 1 4626 ? 194.712 156.911 128.481 1.00 29.34  ? 4626 ILE A CA    1 
ATOM   22771 C  C     . ILE A 1 4626 ? 195.576 156.225 127.430 1.00 33.18  ? 4626 ILE A C     1 
ATOM   22772 O  O     . ILE A 1 4626 ? 195.551 156.571 126.242 1.00 39.76  ? 4626 ILE A O     1 
ATOM   22773 C  CB    . ILE A 1 4626 ? 193.411 156.124 128.722 1.00 31.66  ? 4626 ILE A CB    1 
ATOM   22774 C  CG1   . ILE A 1 4626 ? 192.611 156.005 127.428 1.00 29.65  ? 4626 ILE A CG1   1 
ATOM   22775 C  CG2   . ILE A 1 4626 ? 192.575 156.797 129.794 1.00 28.67  ? 4626 ILE A CG2   1 
ATOM   22776 C  CD1   . ILE A 1 4626 ? 191.456 155.057 127.529 1.00 30.24  ? 4626 ILE A CD1   1 
ATOM   22777 N  N     . ALA A 1 4627 ? 196.351 155.240 127.874 1.00 33.69  ? 4627 ALA A N     1 
ATOM   22778 C  CA    . ALA A 1 4627 ? 197.230 154.512 126.975 1.00 36.71  ? 4627 ALA A CA    1 
ATOM   22779 C  C     . ALA A 1 4627 ? 196.418 153.607 126.051 1.00 40.92  ? 4627 ALA A C     1 
ATOM   22780 O  O     . ALA A 1 4627 ? 195.219 153.387 126.240 1.00 42.94  ? 4627 ALA A O     1 
ATOM   22781 C  CB    . ALA A 1 4627 ? 198.246 153.693 127.768 1.00 33.31  ? 4627 ALA A CB    1 
ATOM   22782 N  N     . THR A 1 4628 ? 197.094 153.080 125.033 1.00 45.68  ? 4628 THR A N     1 
ATOM   22783 C  CA    . THR A 1 4628 ? 196.455 152.164 124.103 1.00 41.61  ? 4628 THR A CA    1 
ATOM   22784 C  C     . THR A 1 4628 ? 196.072 150.870 124.817 1.00 47.15  ? 4628 THR A C     1 
ATOM   22785 O  O     . THR A 1 4628 ? 196.541 150.571 125.920 1.00 45.77  ? 4628 THR A O     1 
ATOM   22786 C  CB    . THR A 1 4628 ? 197.376 151.868 122.922 1.00 47.18  ? 4628 THR A CB    1 
ATOM   22787 O  OG1   . THR A 1 4628 ? 198.523 151.139 123.378 1.00 50.89  ? 4628 THR A OG1   1 
ATOM   22788 C  CG2   . THR A 1 4628 ? 197.831 153.163 122.267 1.00 42.54  ? 4628 THR A CG2   1 
ATOM   22789 N  N     . LYS A 1 4629 ? 195.185 150.106 124.175 1.00 49.07  ? 4629 LYS A N     1 
ATOM   22790 C  CA    . LYS A 1 4629 ? 194.596 148.866 124.674 1.00 49.79  ? 4629 LYS A CA    1 
ATOM   22791 C  C     . LYS A 1 4629 ? 193.627 149.136 125.825 1.00 49.09  ? 4629 LYS A C     1 
ATOM   22792 O  O     . LYS A 1 4629 ? 192.865 148.239 126.210 1.00 52.60  ? 4629 LYS A O     1 
ATOM   22793 C  CB    . LYS A 1 4629 ? 195.684 147.851 125.083 1.00 50.46  ? 4629 LYS A CB    1 
ATOM   22794 C  CG    . LYS A 1 4629 ? 195.277 146.688 125.979 1.00 58.31  ? 4629 LYS A CG    1 
ATOM   22795 C  CD    . LYS A 1 4629 ? 196.175 145.481 125.762 1.00 64.55  ? 4629 LYS A CD    1 
ATOM   22796 C  CE    . LYS A 1 4629 ? 195.902 144.398 126.795 1.00 58.84  ? 4629 LYS A CE    1 
ATOM   22797 N  NZ    . LYS A 1 4629 ? 196.227 143.041 126.279 1.00 60.26  ? 4629 LYS A NZ    1 
ATOM   22798 N  N     . GLU A 1 4630 ? 193.560 150.366 126.321 1.00 47.64  ? 4630 GLU A N     1 
ATOM   22799 C  CA    . GLU A 1 4630 ? 192.672 150.728 127.413 1.00 39.81  ? 4630 GLU A CA    1 
ATOM   22800 C  C     . GLU A 1 4630 ? 191.360 151.275 126.867 1.00 40.59  ? 4630 GLU A C     1 
ATOM   22801 O  O     . GLU A 1 4630 ? 191.306 151.843 125.773 1.00 47.61  ? 4630 GLU A O     1 
ATOM   22802 C  CB    . GLU A 1 4630 ? 193.327 151.760 128.333 1.00 39.09  ? 4630 GLU A CB    1 
ATOM   22803 C  CG    . GLU A 1 4630 ? 194.512 151.222 129.116 1.00 38.67  ? 4630 GLU A CG    1 
ATOM   22804 C  CD    . GLU A 1 4630 ? 194.099 150.241 130.195 1.00 45.04  ? 4630 GLU A CD    1 
ATOM   22805 O  OE1   . GLU A 1 4630 ? 193.952 149.039 129.888 1.00 52.46  ? 4630 GLU A OE1   1 
ATOM   22806 O  OE2   . GLU A 1 4630 ? 193.919 150.671 131.353 1.00 41.46  ? 4630 GLU A OE2   1 
ATOM   22807 N  N     . ASP A 1 4631 ? 190.299 151.096 127.647 1.00 37.73  ? 4631 ASP A N     1 
ATOM   22808 C  CA    . ASP A 1 4631 ? 188.953 151.451 127.230 1.00 33.10  ? 4631 ASP A CA    1 
ATOM   22809 C  C     . ASP A 1 4631 ? 188.383 152.493 128.182 1.00 29.96  ? 4631 ASP A C     1 
ATOM   22810 O  O     . ASP A 1 4631 ? 188.159 152.181 129.361 1.00 33.27  ? 4631 ASP A O     1 
ATOM   22811 C  CB    . ASP A 1 4631 ? 188.078 150.200 127.202 1.00 34.46  ? 4631 ASP A CB    1 
ATOM   22812 C  CG    . ASP A 1 4631 ? 186.704 150.457 126.638 1.00 39.80  ? 4631 ASP A CG    1 
ATOM   22813 O  OD1   . ASP A 1 4631 ? 186.584 150.628 125.407 1.00 47.15  ? 4631 ASP A OD1   1 
ATOM   22814 O  OD2   . ASP A 1 4631 ? 185.739 150.454 127.424 1.00 37.89  ? 4631 ASP A OD2   1 
ATOM   22815 N  N     . PRO A 1 4632 ? 188.149 153.730 127.732 1.00 25.71  ? 4632 PRO A N     1 
ATOM   22816 C  CA    . PRO A 1 4632 ? 187.667 154.769 128.661 1.00 29.94  ? 4632 PRO A CA    1 
ATOM   22817 C  C     . PRO A 1 4632 ? 186.332 154.428 129.287 1.00 26.02  ? 4632 PRO A C     1 
ATOM   22818 O  O     . PRO A 1 4632 ? 186.029 154.878 130.402 1.00 23.31  ? 4632 PRO A O     1 
ATOM   22819 C  CB    . PRO A 1 4632 ? 187.564 156.016 127.770 1.00 26.54  ? 4632 PRO A CB    1 
ATOM   22820 C  CG    . PRO A 1 4632 ? 187.456 155.487 126.382 1.00 23.62  ? 4632 PRO A CG    1 
ATOM   22821 C  CD    . PRO A 1 4632 ? 188.247 154.220 126.348 1.00 28.49  ? 4632 PRO A CD    1 
ATOM   22822 N  N     . ARG A 1 4633 ? 185.520 153.642 128.586 1.00 28.12  ? 4633 ARG A N     1 
ATOM   22823 C  CA    . ARG A 1 4633 ? 184.237 153.218 129.122 1.00 23.90  ? 4633 ARG A CA    1 
ATOM   22824 C  C     . ARG A 1 4633 ? 184.451 152.395 130.391 1.00 21.64  ? 4633 ARG A C     1 
ATOM   22825 O  O     . ARG A 1 4633 ? 183.756 152.583 131.399 1.00 21.43  ? 4633 ARG A O     1 
ATOM   22826 C  CB    . ARG A 1 4633 ? 183.505 152.417 128.044 1.00 27.07  ? 4633 ARG A CB    1 
ATOM   22827 C  CG    . ARG A 1 4633 ? 182.157 151.886 128.407 1.00 30.13  ? 4633 ARG A CG    1 
ATOM   22828 C  CD    . ARG A 1 4633 ? 181.217 153.053 128.604 1.00 34.33  ? 4633 ARG A CD    1 
ATOM   22829 N  NE    . ARG A 1 4633 ? 180.976 153.803 127.378 1.00 37.65  ? 4633 ARG A NE    1 
ATOM   22830 C  CZ    . ARG A 1 4633 ? 180.385 154.989 127.334 1.00 38.23  ? 4633 ARG A CZ    1 
ATOM   22831 N  NH1   . ARG A 1 4633 ? 179.975 155.599 128.435 1.00 30.57  ? 4633 ARG A NH1   1 
ATOM   22832 N  NH2   . ARG A 1 4633 ? 180.197 155.577 126.157 1.00 44.73  ? 4633 ARG A NH2   1 
ATOM   22833 N  N     . SER A 1 4634 ? 185.450 151.507 130.366 1.00 25.52  ? 4634 SER A N     1 
ATOM   22834 C  CA    . SER A 1 4634 ? 185.844 150.766 131.559 1.00 21.15  ? 4634 SER A CA    1 
ATOM   22835 C  C     . SER A 1 4634 ? 186.393 151.685 132.643 1.00 17.58  ? 4634 SER A C     1 
ATOM   22836 O  O     . SER A 1 4634 ? 186.201 151.418 133.835 1.00 17.98  ? 4634 SER A O     1 
ATOM   22837 C  CB    . SER A 1 4634 ? 186.878 149.702 131.195 1.00 20.72  ? 4634 SER A CB    1 
ATOM   22838 O  OG    . SER A 1 4634 ? 188.186 150.241 131.219 1.00 20.83  ? 4634 SER A OG    1 
ATOM   22839 N  N     . PHE A 1 4635 ? 187.096 152.755 132.258 1.00 21.30  ? 4635 PHE A N     1 
ATOM   22840 C  CA    . PHE A 1 4635 ? 187.506 153.755 133.239 1.00 15.76  ? 4635 PHE A CA    1 
ATOM   22841 C  C     . PHE A 1 4635 ? 186.297 154.334 133.957 1.00 16.50  ? 4635 PHE A C     1 
ATOM   22842 O  O     . PHE A 1 4635 ? 186.334 154.560 135.173 1.00 12.44  ? 4635 PHE A O     1 
ATOM   22843 C  CB    . PHE A 1 4635 ? 188.304 154.873 132.568 1.00 15.55  ? 4635 PHE A CB    1 
ATOM   22844 C  CG    . PHE A 1 4635 ? 189.774 154.598 132.462 1.00 15.50  ? 4635 PHE A CG    1 
ATOM   22845 C  CD1   . PHE A 1 4635 ? 190.263 153.710 131.522 1.00 20.26  ? 4635 PHE A CD1   1 
ATOM   22846 C  CD2   . PHE A 1 4635 ? 190.670 155.242 133.297 1.00 13.95  ? 4635 PHE A CD2   1 
ATOM   22847 C  CE1   . PHE A 1 4635 ? 191.618 153.463 131.425 1.00 24.15  ? 4635 PHE A CE1   1 
ATOM   22848 C  CE2   . PHE A 1 4635 ? 192.024 154.998 133.204 1.00 18.35  ? 4635 PHE A CE2   1 
ATOM   22849 C  CZ    . PHE A 1 4635 ? 192.498 154.108 132.267 1.00 22.09  ? 4635 PHE A CZ    1 
ATOM   22850 N  N     . TYR A 1 4636 ? 185.217 154.588 133.217 1.00 19.30  ? 4636 TYR A N     1 
ATOM   22851 C  CA    . TYR A 1 4636 ? 183.981 155.032 133.851 1.00 12.00  ? 4636 TYR A CA    1 
ATOM   22852 C  C     . TYR A 1 4636 ? 183.423 153.964 134.785 1.00 15.55  ? 4636 TYR A C     1 
ATOM   22853 O  O     . TYR A 1 4636 ? 182.970 154.278 135.891 1.00 14.32  ? 4636 TYR A O     1 
ATOM   22854 C  CB    . TYR A 1 4636 ? 182.942 155.404 132.795 1.00 13.75  ? 4636 TYR A CB    1 
ATOM   22855 C  CG    . TYR A 1 4636 ? 183.398 156.451 131.807 1.00 16.08  ? 4636 TYR A CG    1 
ATOM   22856 C  CD1   . TYR A 1 4636 ? 184.364 157.387 132.149 1.00 12.41  ? 4636 TYR A CD1   1 
ATOM   22857 C  CD2   . TYR A 1 4636 ? 182.860 156.503 130.529 1.00 21.51  ? 4636 TYR A CD2   1 
ATOM   22858 C  CE1   . TYR A 1 4636 ? 184.780 158.340 131.246 1.00 13.77  ? 4636 TYR A CE1   1 
ATOM   22859 C  CE2   . TYR A 1 4636 ? 183.271 157.454 129.619 1.00 21.56  ? 4636 TYR A CE2   1 
ATOM   22860 C  CZ    . TYR A 1 4636 ? 184.231 158.370 129.983 1.00 19.18  ? 4636 TYR A CZ    1 
ATOM   22861 O  OH    . TYR A 1 4636 ? 184.643 159.320 129.079 1.00 27.03  ? 4636 TYR A OH    1 
ATOM   22862 N  N     . GLU A 1 4637 ? 183.446 152.695 134.358 1.00 20.66  ? 4637 GLU A N     1 
ATOM   22863 C  CA    . GLU A 1 4637 ? 182.859 151.640 135.185 1.00 13.84  ? 4637 GLU A CA    1 
ATOM   22864 C  C     . GLU A 1 4637 ? 183.616 151.428 136.491 1.00 9.25   ? 4637 GLU A C     1 
ATOM   22865 O  O     . GLU A 1 4637 ? 183.003 151.079 137.505 1.00 11.53  ? 4637 GLU A O     1 
ATOM   22866 C  CB    . GLU A 1 4637 ? 182.792 150.318 134.421 1.00 17.47  ? 4637 GLU A CB    1 
ATOM   22867 C  CG    . GLU A 1 4637 ? 182.225 150.413 133.027 1.00 29.21  ? 4637 GLU A CG    1 
ATOM   22868 C  CD    . GLU A 1 4637 ? 182.214 149.076 132.314 1.00 38.89  ? 4637 GLU A CD    1 
ATOM   22869 O  OE1   . GLU A 1 4637 ? 182.456 148.046 132.977 1.00 37.65  ? 4637 GLU A OE1   1 
ATOM   22870 O  OE2   . GLU A 1 4637 ? 181.961 149.054 131.092 1.00 34.22  ? 4637 GLU A OE2   1 
ATOM   22871 N  N     . ARG A 1 4638 ? 184.931 151.623 136.494 1.00 10.10  ? 4638 ARG A N     1 
ATOM   22872 C  CA    . ARG A 1 4638 ? 185.745 151.306 137.661 1.00 11.06  ? 4638 ARG A CA    1 
ATOM   22873 C  C     . ARG A 1 4638 ? 185.867 152.462 138.646 1.00 10.42  ? 4638 ARG A C     1 
ATOM   22874 O  O     . ARG A 1 4638 ? 186.571 152.324 139.651 1.00 9.61   ? 4638 ARG A O     1 
ATOM   22875 C  CB    . ARG A 1 4638 ? 187.139 150.847 137.223 1.00 8.70   ? 4638 ARG A CB    1 
ATOM   22876 C  CG    . ARG A 1 4638 ? 187.124 149.536 136.462 1.00 9.40   ? 4638 ARG A CG    1 
ATOM   22877 C  CD    . ARG A 1 4638 ? 188.507 149.111 136.026 1.00 14.52  ? 4638 ARG A CD    1 
ATOM   22878 N  NE    . ARG A 1 4638 ? 189.419 148.951 137.150 1.00 15.56  ? 4638 ARG A NE    1 
ATOM   22879 C  CZ    . ARG A 1 4638 ? 190.146 147.866 137.373 1.00 15.05  ? 4638 ARG A CZ    1 
ATOM   22880 N  NH1   . ARG A 1 4638 ? 190.075 146.812 136.577 1.00 13.50  ? 4638 ARG A NH1   1 
ATOM   22881 N  NH2   . ARG A 1 4638 ? 190.966 147.838 138.419 1.00 23.07  ? 4638 ARG A NH2   1 
ATOM   22882 N  N     . GLY A 1 4639 ? 185.202 153.584 138.392 1.00 10.84  ? 4639 GLY A N     1 
ATOM   22883 C  CA    . GLY A 1 4639 ? 185.220 154.699 139.323 1.00 7.46   ? 4639 GLY A CA    1 
ATOM   22884 C  C     . GLY A 1 4639 ? 186.569 155.359 139.501 1.00 7.39   ? 4639 GLY A C     1 
ATOM   22885 O  O     . GLY A 1 4639 ? 186.958 155.668 140.634 1.00 12.41  ? 4639 GLY A O     1 
ATOM   22886 N  N     . VAL A 1 4640 ? 187.294 155.584 138.412 1.00 7.14   ? 4640 VAL A N     1 
ATOM   22887 C  CA    . VAL A 1 4640 ? 188.599 156.231 138.478 1.00 7.30   ? 4640 VAL A CA    1 
ATOM   22888 C  C     . VAL A 1 4640 ? 188.401 157.728 138.673 1.00 7.94   ? 4640 VAL A C     1 
ATOM   22889 O  O     . VAL A 1 4640 ? 187.641 158.367 137.937 1.00 9.97   ? 4640 VAL A O     1 
ATOM   22890 C  CB    . VAL A 1 4640 ? 189.415 155.936 137.210 1.00 7.10   ? 4640 VAL A CB    1 
ATOM   22891 C  CG1   . VAL A 1 4640 ? 190.779 156.591 137.291 1.00 7.25   ? 4640 VAL A CG1   1 
ATOM   22892 C  CG2   . VAL A 1 4640 ? 189.551 154.437 137.010 1.00 8.21   ? 4640 VAL A CG2   1 
ATOM   22893 N  N     . ALA A 1 4641 ? 189.081 158.291 139.667 1.00 7.42   ? 4641 ALA A N     1 
ATOM   22894 C  CA    . ALA A 1 4641 ? 188.947 159.706 139.983 1.00 8.27   ? 4641 ALA A CA    1 
ATOM   22895 C  C     . ALA A 1 4641 ? 190.259 160.199 140.584 1.00 10.68  ? 4641 ALA A C     1 
ATOM   22896 O  O     . ALA A 1 4641 ? 191.249 159.465 140.651 1.00 12.57  ? 4641 ALA A O     1 
ATOM   22897 C  CB    . ALA A 1 4641 ? 187.757 159.939 140.923 1.00 6.89   ? 4641 ALA A CB    1 
ATOM   22898 N  N     . VAL A 1 4642 ? 190.265 161.458 141.015 1.00 11.29  ? 4642 VAL A N     1 
ATOM   22899 C  CA    . VAL A 1 4642 ? 191.420 162.077 141.652 1.00 8.89   ? 4642 VAL A CA    1 
ATOM   22900 C  C     . VAL A 1 4642 ? 190.977 162.668 142.982 1.00 9.12   ? 4642 VAL A C     1 
ATOM   22901 O  O     . VAL A 1 4642 ? 189.928 163.316 143.067 1.00 8.65   ? 4642 VAL A O     1 
ATOM   22902 C  CB    . VAL A 1 4642 ? 192.060 163.159 140.757 1.00 7.11   ? 4642 VAL A CB    1 
ATOM   22903 C  CG1   . VAL A 1 4642 ? 193.305 163.727 141.414 1.00 8.62   ? 4642 VAL A CG1   1 
ATOM   22904 C  CG2   . VAL A 1 4642 ? 192.394 162.590 139.389 1.00 8.78   ? 4642 VAL A CG2   1 
ATOM   22905 N  N     . LEU A 1 4643 ? 191.768 162.430 144.022 1.00 10.01  ? 4643 LEU A N     1 
ATOM   22906 C  CA    . LEU A 1 4643 ? 191.504 162.936 145.361 1.00 10.61  ? 4643 LEU A CA    1 
ATOM   22907 C  C     . LEU A 1 4643 ? 192.565 163.963 145.731 1.00 11.06  ? 4643 LEU A C     1 
ATOM   22908 O  O     . LEU A 1 4643 ? 193.761 163.726 145.532 1.00 11.64  ? 4643 LEU A O     1 
ATOM   22909 C  CB    . LEU A 1 4643 ? 191.492 161.801 146.387 1.00 14.02  ? 4643 LEU A CB    1 
ATOM   22910 C  CG    . LEU A 1 4643 ? 190.529 160.637 146.158 1.00 9.44   ? 4643 LEU A CG    1 
ATOM   22911 C  CD1   . LEU A 1 4643 ? 190.478 159.755 147.389 1.00 8.28   ? 4643 LEU A CD1   1 
ATOM   22912 C  CD2   . LEU A 1 4643 ? 189.143 161.143 145.803 1.00 11.46  ? 4643 LEU A CD2   1 
ATOM   22913 N  N     . CYS A 1 4644 ? 192.121 165.102 146.267 1.00 14.08  ? 4644 CYS A N     1 
ATOM   22914 C  CA    . CYS A 1 4644 ? 193.052 166.150 146.669 1.00 16.75  ? 4644 CYS A CA    1 
ATOM   22915 C  C     . CYS A 1 4644 ? 193.821 165.790 147.932 1.00 18.78  ? 4644 CYS A C     1 
ATOM   22916 O  O     . CYS A 1 4644 ? 194.910 166.329 148.153 1.00 24.92  ? 4644 CYS A O     1 
ATOM   22917 C  CB    . CYS A 1 4644 ? 192.303 167.467 146.873 1.00 12.24  ? 4644 CYS A CB    1 
ATOM   22918 S  SG    . CYS A 1 4644 ? 191.721 168.232 145.346 1.00 29.44  ? 4644 CYS A SG    1 
ATOM   22919 N  N     . THR A 1 4645 ? 193.285 164.901 148.761 1.00 16.48  ? 4645 THR A N     1 
ATOM   22920 C  CA    . THR A 1 4645 ? 193.966 164.475 149.976 1.00 19.53  ? 4645 THR A CA    1 
ATOM   22921 C  C     . THR A 1 4645 ? 193.510 163.081 150.388 1.00 14.88  ? 4645 THR A C     1 
ATOM   22922 O  O     . THR A 1 4645 ? 192.512 162.570 149.881 1.00 13.71  ? 4645 THR A O     1 
ATOM   22923 C  CB    . THR A 1 4645 ? 193.720 165.453 151.140 1.00 25.20  ? 4645 THR A CB    1 
ATOM   22924 O  OG1   . THR A 1 4645 ? 194.397 164.985 152.312 1.00 32.99  ? 4645 THR A OG1   1 
ATOM   22925 C  CG2   . THR A 1 4645 ? 192.234 165.568 151.435 1.00 17.88  ? 4645 THR A CG2   1 
HETATM 22926 P  PB    . ADP B 2 .    ? 163.222 176.153 142.196 1.00 2.49   ? 4701 ADP A PB    1 
HETATM 22927 O  O1B   . ADP B 2 .    ? 163.434 176.602 143.617 1.00 7.62   ? 4701 ADP A O1B   1 
HETATM 22928 O  O2B   . ADP B 2 .    ? 164.374 175.345 141.660 1.00 5.48   ? 4701 ADP A O2B   1 
HETATM 22929 O  O3B   . ADP B 2 .    ? 161.893 175.473 141.997 1.00 7.64   ? 4701 ADP A O3B   1 
HETATM 22930 P  PA    . ADP B 2 .    ? 161.917 178.257 140.642 1.00 9.53   ? 4701 ADP A PA    1 
HETATM 22931 O  O1A   . ADP B 2 .    ? 161.485 177.480 139.444 1.00 3.14   ? 4701 ADP A O1A   1 
HETATM 22932 O  O2A   . ADP B 2 .    ? 160.900 178.535 141.699 1.00 18.12  ? 4701 ADP A O2A   1 
HETATM 22933 O  O3A   . ADP B 2 .    ? 163.159 177.498 141.313 1.00 7.35   ? 4701 ADP A O3A   1 
HETATM 22934 O  "O5'" . ADP B 2 .    ? 162.586 179.637 140.180 1.00 9.22   ? 4701 ADP A "O5'" 1 
HETATM 22935 C  "C5'" . ADP B 2 .    ? 163.703 179.609 139.258 1.00 8.61   ? 4701 ADP A "C5'" 1 
HETATM 22936 C  "C4'" . ADP B 2 .    ? 164.020 181.017 138.822 1.00 8.99   ? 4701 ADP A "C4'" 1 
HETATM 22937 O  "O4'" . ADP B 2 .    ? 164.854 180.962 137.638 1.00 11.14  ? 4701 ADP A "O4'" 1 
HETATM 22938 C  "C3'" . ADP B 2 .    ? 162.824 181.860 138.377 1.00 9.82   ? 4701 ADP A "C3'" 1 
HETATM 22939 O  "O3'" . ADP B 2 .    ? 163.150 183.243 138.357 1.00 20.60  ? 4701 ADP A "O3'" 1 
HETATM 22940 C  "C2'" . ADP B 2 .    ? 162.623 181.316 136.963 1.00 9.04   ? 4701 ADP A "C2'" 1 
HETATM 22941 O  "O2'" . ADP B 2 .    ? 161.847 182.162 136.142 1.00 18.89  ? 4701 ADP A "O2'" 1 
HETATM 22942 C  "C1'" . ADP B 2 .    ? 164.070 181.203 136.489 1.00 7.94   ? 4701 ADP A "C1'" 1 
HETATM 22943 N  N9    . ADP B 2 .    ? 164.289 180.112 135.548 1.00 4.91   ? 4701 ADP A N9    1 
HETATM 22944 C  C8    . ADP B 2 .    ? 164.539 178.799 135.859 1.00 3.86   ? 4701 ADP A C8    1 
HETATM 22945 N  N7    . ADP B 2 .    ? 164.698 178.036 134.808 1.00 3.38   ? 4701 ADP A N7    1 
HETATM 22946 C  C5    . ADP B 2 .    ? 164.548 178.899 133.732 1.00 2.89   ? 4701 ADP A C5    1 
HETATM 22947 C  C6    . ADP B 2 .    ? 164.605 178.694 132.341 1.00 3.52   ? 4701 ADP A C6    1 
HETATM 22948 N  N6    . ADP B 2 .    ? 164.839 177.513 131.777 1.00 3.36   ? 4701 ADP A N6    1 
HETATM 22949 N  N1    . ADP B 2 .    ? 164.411 179.771 131.544 1.00 4.92   ? 4701 ADP A N1    1 
HETATM 22950 C  C2    . ADP B 2 .    ? 164.176 180.957 132.118 1.00 3.91   ? 4701 ADP A C2    1 
HETATM 22951 N  N3    . ADP B 2 .    ? 164.099 181.267 133.408 1.00 5.28   ? 4701 ADP A N3    1 
HETATM 22952 C  C4    . ADP B 2 .    ? 164.296 180.183 134.175 1.00 4.35   ? 4701 ADP A C4    1 
HETATM 22953 P  PG    . ATP C 3 .    ? 169.887 196.741 164.797 1.00 3.19   ? 4702 ATP A PG    1 
HETATM 22954 O  O1G   . ATP C 3 .    ? 170.714 195.706 164.080 1.00 4.96   ? 4702 ATP A O1G   1 
HETATM 22955 O  O2G   . ATP C 3 .    ? 168.430 196.686 164.421 1.00 5.55   ? 4702 ATP A O2G   1 
HETATM 22956 O  O3G   . ATP C 3 .    ? 170.103 196.725 166.288 1.00 3.79   ? 4702 ATP A O3G   1 
HETATM 22957 P  PB    . ATP C 3 .    ? 170.666 198.809 162.840 1.00 2.14   ? 4702 ATP A PB    1 
HETATM 22958 O  O1B   . ATP C 3 .    ? 171.862 198.161 162.230 1.00 3.23   ? 4702 ATP A O1B   1 
HETATM 22959 O  O2B   . ATP C 3 .    ? 169.372 198.817 162.100 1.00 3.48   ? 4702 ATP A O2B   1 
HETATM 22960 O  O3B   . ATP C 3 .    ? 170.423 198.174 164.289 1.00 2.54   ? 4702 ATP A O3B   1 
HETATM 22961 P  PA    . ATP C 3 .    ? 170.108 201.560 163.623 1.00 2.98   ? 4702 ATP A PA    1 
HETATM 22962 O  O1A   . ATP C 3 .    ? 168.880 201.046 164.295 1.00 7.55   ? 4702 ATP A O1A   1 
HETATM 22963 O  O2A   . ATP C 3 .    ? 169.949 202.430 162.421 1.00 2.65   ? 4702 ATP A O2A   1 
HETATM 22964 O  O3A   . ATP C 3 .    ? 171.037 200.312 163.238 1.00 2.03   ? 4702 ATP A O3A   1 
HETATM 22965 O  "O5'" . ATP C 3 .    ? 171.025 202.305 164.706 1.00 8.38   ? 4702 ATP A "O5'" 1 
HETATM 22966 C  "C5'" . ATP C 3 .    ? 172.230 202.979 164.268 1.00 6.00   ? 4702 ATP A "C5'" 1 
HETATM 22967 C  "C4'" . ATP C 3 .    ? 172.677 203.930 165.347 1.00 6.31   ? 4702 ATP A "C4'" 1 
HETATM 22968 O  "O4'" . ATP C 3 .    ? 173.435 205.007 164.743 1.00 11.01  ? 4702 ATP A "O4'" 1 
HETATM 22969 C  "C3'" . ATP C 3 .    ? 171.554 204.663 166.081 1.00 6.16   ? 4702 ATP A "C3'" 1 
HETATM 22970 O  "O3'" . ATP C 3 .    ? 172.029 205.259 167.280 1.00 27.38  ? 4702 ATP A "O3'" 1 
HETATM 22971 C  "C2'" . ATP C 3 .    ? 171.200 205.723 165.039 1.00 5.23   ? 4702 ATP A "C2'" 1 
HETATM 22972 O  "O2'" . ATP C 3 .    ? 170.494 206.820 165.578 1.00 7.83   ? 4702 ATP A "O2'" 1 
HETATM 22973 C  "C1'" . ATP C 3 .    ? 172.587 206.115 164.530 1.00 5.53   ? 4702 ATP A "C1'" 1 
HETATM 22974 N  N9    . ATP C 3 .    ? 172.610 206.434 163.109 1.00 5.84   ? 4702 ATP A N9    1 
HETATM 22975 C  C8    . ATP C 3 .    ? 172.076 205.701 162.081 1.00 5.63   ? 4702 ATP A C8    1 
HETATM 22976 N  N7    . ATP C 3 .    ? 172.252 206.270 160.910 1.00 5.05   ? 4702 ATP A N7    1 
HETATM 22977 C  C5    . ATP C 3 .    ? 172.928 207.451 161.192 1.00 5.01   ? 4702 ATP A C5    1 
HETATM 22978 C  C6    . ATP C 3 .    ? 173.401 208.496 160.377 1.00 4.96   ? 4702 ATP A C6    1 
HETATM 22979 N  N6    . ATP C 3 .    ? 173.260 208.524 159.056 1.00 5.58   ? 4702 ATP A N6    1 
HETATM 22980 N  N1    . ATP C 3 .    ? 174.035 209.523 160.990 1.00 5.83   ? 4702 ATP A N1    1 
HETATM 22981 C  C2    . ATP C 3 .    ? 174.172 209.490 162.322 1.00 5.80   ? 4702 ATP A C2    1 
HETATM 22982 N  N3    . ATP C 3 .    ? 173.770 208.563 163.187 1.00 7.00   ? 4702 ATP A N3    1 
HETATM 22983 C  C4    . ATP C 3 .    ? 173.147 207.560 162.548 1.00 7.45   ? 4702 ATP A C4    1 
HETATM 22984 P  PB    . ADP D 2 .    ? 171.044 188.740 193.823 1.00 5.89   ? 4703 ADP A PB    1 
HETATM 22985 O  O1B   . ADP D 2 .    ? 170.140 189.800 193.253 1.00 8.20   ? 4703 ADP A O1B   1 
HETATM 22986 O  O2B   . ADP D 2 .    ? 170.498 187.349 193.641 1.00 21.87  ? 4703 ADP A O2B   1 
HETATM 22987 O  O3B   . ADP D 2 .    ? 172.468 188.875 193.352 1.00 7.58   ? 4703 ADP A O3B   1 
HETATM 22988 P  PA    . ADP D 2 .    ? 169.942 189.297 196.497 1.00 11.09  ? 4703 ADP A PA    1 
HETATM 22989 O  O1A   . ADP D 2 .    ? 169.657 190.761 196.497 1.00 7.09   ? 4703 ADP A O1A   1 
HETATM 22990 O  O2A   . ADP D 2 .    ? 168.805 188.359 196.266 1.00 13.46  ? 4703 ADP A O2A   1 
HETATM 22991 O  O3A   . ADP D 2 .    ? 171.084 188.993 195.414 1.00 13.06  ? 4703 ADP A O3A   1 
HETATM 22992 O  "O5'" . ADP D 2 .    ? 170.694 188.895 197.854 1.00 10.71  ? 4703 ADP A "O5'" 1 
HETATM 22993 C  "C5'" . ADP D 2 .    ? 171.962 189.524 198.163 1.00 8.25   ? 4703 ADP A "C5'" 1 
HETATM 22994 C  "C4'" . ADP D 2 .    ? 172.461 189.007 199.489 1.00 8.83   ? 4703 ADP A "C4'" 1 
HETATM 22995 O  "O4'" . ADP D 2 .    ? 173.657 189.741 199.860 1.00 11.61  ? 4703 ADP A "O4'" 1 
HETATM 22996 C  "C3'" . ADP D 2 .    ? 171.502 189.173 200.675 1.00 8.44   ? 4703 ADP A "C3'" 1 
HETATM 22997 O  "O3'" . ADP D 2 .    ? 171.674 188.124 201.617 1.00 11.80  ? 4703 ADP A "O3'" 1 
HETATM 22998 C  "C2'" . ADP D 2 .    ? 171.963 190.509 201.256 1.00 6.93   ? 4703 ADP A "C2'" 1 
HETATM 22999 O  "O2'" . ADP D 2 .    ? 171.558 190.706 202.593 1.00 14.58  ? 4703 ADP A "O2'" 1 
HETATM 23000 C  "C1'" . ADP D 2 .    ? 173.472 190.351 201.116 1.00 8.50   ? 4703 ADP A "C1'" 1 
HETATM 23001 N  N9    . ADP D 2 .    ? 174.200 191.614 201.123 1.00 7.06   ? 4703 ADP A N9    1 
HETATM 23002 C  C8    . ADP D 2 .    ? 175.272 191.941 200.332 1.00 6.94   ? 4703 ADP A C8    1 
HETATM 23003 N  N7    . ADP D 2 .    ? 175.732 193.146 200.554 1.00 9.18   ? 4703 ADP A N7    1 
HETATM 23004 C  C5    . ADP D 2 .    ? 174.920 193.644 201.562 1.00 8.90   ? 4703 ADP A C5    1 
HETATM 23005 C  C6    . ADP D 2 .    ? 174.902 194.878 202.239 1.00 11.31  ? 4703 ADP A C6    1 
HETATM 23006 N  N6    . ADP D 2 .    ? 175.753 195.869 201.994 1.00 11.25  ? 4703 ADP A N6    1 
HETATM 23007 N  N1    . ADP D 2 .    ? 173.959 195.053 203.194 1.00 14.99  ? 4703 ADP A N1    1 
HETATM 23008 C  C2    . ADP D 2 .    ? 173.104 194.053 203.437 1.00 10.12  ? 4703 ADP A C2    1 
HETATM 23009 N  N3    . ADP D 2 .    ? 173.027 192.855 202.866 1.00 8.01   ? 4703 ADP A N3    1 
HETATM 23010 C  C4    . ADP D 2 .    ? 173.972 192.707 201.924 1.00 7.48   ? 4703 ADP A C4    1 
HETATM 23011 P  PB    . ADP E 2 .    ? 159.780 159.235 200.382 1.00 13.76  ? 4704 ADP A PB    1 
HETATM 23012 O  O1B   . ADP E 2 .    ? 161.022 159.450 201.209 1.00 18.32  ? 4704 ADP A O1B   1 
HETATM 23013 O  O2B   . ADP E 2 .    ? 158.862 160.430 200.389 1.00 12.96  ? 4704 ADP A O2B   1 
HETATM 23014 O  O3B   . ADP E 2 .    ? 160.082 158.740 198.992 1.00 15.20  ? 4704 ADP A O3B   1 
HETATM 23015 P  PA    . ADP E 2 .    ? 157.684 158.022 202.070 1.00 20.78  ? 4704 ADP A PA    1 
HETATM 23016 O  O1A   . ADP E 2 .    ? 157.931 158.900 203.250 1.00 9.45   ? 4704 ADP A O1A   1 
HETATM 23017 O  O2A   . ADP E 2 .    ? 156.465 158.276 201.247 1.00 23.05  ? 4704 ADP A O2A   1 
HETATM 23018 O  O3A   . ADP E 2 .    ? 158.966 158.049 201.108 1.00 26.51  ? 4704 ADP A O3A   1 
HETATM 23019 O  "O5'" . ADP E 2 .    ? 157.703 156.487 202.531 1.00 18.69  ? 4704 ADP A "O5'" 1 
HETATM 23020 C  "C5'" . ADP E 2 .    ? 156.666 156.021 203.428 1.00 23.50  ? 4704 ADP A "C5'" 1 
HETATM 23021 C  "C4'" . ADP E 2 .    ? 156.829 154.539 203.653 1.00 16.26  ? 4704 ADP A "C4'" 1 
HETATM 23022 O  "O4'" . ADP E 2 .    ? 158.148 154.290 204.202 1.00 16.93  ? 4704 ADP A "O4'" 1 
HETATM 23023 C  "C3'" . ADP E 2 .    ? 155.867 153.915 204.668 1.00 15.02  ? 4704 ADP A "C3'" 1 
HETATM 23024 O  "O3'" . ADP E 2 .    ? 155.729 152.518 204.449 1.00 24.13  ? 4704 ADP A "O3'" 1 
HETATM 23025 C  "C2'" . ADP E 2 .    ? 156.611 154.198 205.973 1.00 20.19  ? 4704 ADP A "C2'" 1 
HETATM 23026 O  "O2'" . ADP E 2 .    ? 156.179 153.398 207.053 1.00 31.92  ? 4704 ADP A "O2'" 1 
HETATM 23027 C  "C1'" . ADP E 2 .    ? 158.040 153.879 205.547 1.00 17.29  ? 4704 ADP A "C1'" 1 
HETATM 23028 N  N9    . ADP E 2 .    ? 159.055 154.576 206.326 1.00 15.28  ? 4704 ADP A N9    1 
HETATM 23029 C  C8    . ADP E 2 .    ? 159.621 155.791 206.033 1.00 16.62  ? 4704 ADP A C8    1 
HETATM 23030 N  N7    . ADP E 2 .    ? 160.504 156.179 206.918 1.00 18.05  ? 4704 ADP A N7    1 
HETATM 23031 C  C5    . ADP E 2 .    ? 160.516 155.162 207.861 1.00 14.73  ? 4704 ADP A C5    1 
HETATM 23032 C  C6    . ADP E 2 .    ? 161.246 154.984 209.051 1.00 16.81  ? 4704 ADP A C6    1 
HETATM 23033 N  N6    . ADP E 2 .    ? 162.137 155.858 209.510 1.00 20.32  ? 4704 ADP A N6    1 
HETATM 23034 N  N1    . ADP E 2 .    ? 161.019 153.853 209.760 1.00 16.32  ? 4704 ADP A N1    1 
HETATM 23035 C  C2    . ADP E 2 .    ? 160.122 152.977 209.292 1.00 16.38  ? 4704 ADP A C2    1 
HETATM 23036 N  N3    . ADP E 2 .    ? 159.380 153.038 208.191 1.00 14.56  ? 4704 ADP A N3    1 
HETATM 23037 C  C4    . ADP E 2 .    ? 159.624 154.168 207.509 1.00 13.56  ? 4704 ADP A C4    1 
HETATM 23038 MG MG    . MG  F 4 .    ? 160.160 176.381 144.062 1.00 5.93   ? 4705 MG  A MG    1 
HETATM 23039 MG MG    . MG  G 4 .    ? 167.169 198.208 163.597 1.00 2.69   ? 4706 MG  A MG    1 
HETATM 23040 O  O     . HOH H 5 .    ? 156.790 178.260 146.118 1.00 13.02  ? 4801 HOH A O     1 
HETATM 23041 O  O     . HOH H 5 .    ? 159.088 176.786 146.345 1.00 11.12  ? 4802 HOH A O     1 
HETATM 23042 O  O     . HOH H 5 .    ? 163.595 176.931 146.489 1.00 10.47  ? 4803 HOH A O     1 
HETATM 23043 O  O     . HOH H 5 .    ? 162.358 185.592 143.151 1.00 8.55   ? 4804 HOH A O     1 
HETATM 23044 O  O     . HOH H 5 .    ? 165.738 175.042 134.670 1.00 4.00   ? 4805 HOH A O     1 
HETATM 23045 O  O     . HOH H 5 .    ? 161.659 182.720 141.519 1.00 17.70  ? 4806 HOH A O     1 
HETATM 23046 O  O     . HOH H 5 .    ? 161.010 173.274 145.663 1.00 15.90  ? 4807 HOH A O     1 
# 
